Harmonizome 3.0

integrin, alpha 8

Integrins are heterodimeric transmembrane receptor proteins that mediate numerous cellular processes including cell adhesion, cytoskeletal rearrangement, and activation of cell signaling pathways. Integrins are composed of alpha and beta subunits. This gene encodes the alpha 8 subunit of the heterodimeric integrin alpha8beta1 protein. The encoded protein is a single-pass type 1 membrane protein that contains multiple FG-GAP repeats. This repeat is predicted to fold into a beta propeller structure. This gene regulates the recruitment of mesenchymal cells into epithelial structures, mediates cell-cell interactions, and regulates neurite outgrowth of sensory and motor neurons. The integrin alpha8beta1 protein thus plays an important role in wound-healing and organogenesis. Mutations in this gene have been associated with renal hypodysplasia/aplasia-1 (RHDA1) and with several animal models of chronic kidney disease. Alternate splicing results in multiple transcript variants encoding distinct isoforms. [provided by RefSeq, Apr 2014]

integrin, alpha 9

This gene encodes an alpha integrin. Integrins are heterodimeric integral membrane glycoproteins composed of an alpha chain and a beta chain that mediate cell-cell and cell-matrix adhesion. The protein encoded by this gene, when bound to the beta 1 chain, forms an integrin that is a receptor for VCAM1, cytotactin and osteopontin. Expression of this gene has been found to be upregulated in small cell lung cancers. [provided by RefSeq, Jul 2008]

integrin, alpha 1

This gene encodes the alpha 1 subunit of integrin receptors. This protein heterodimerizes with the beta 1 subunit to form a cell-surface receptor for collagen and laminin. The heterodimeric receptor is involved in cell-cell adhesion and may play a role in inflammation and fibrosis. The alpha 1 subunit contains an inserted (I) von Willebrand factor type I domain which is thought to be involved in collagen binding. [provided by RefSeq, Jul 2008]

integrin, alpha 2 (CD49B, alpha 2 subunit of VLA-2 receptor)

This gene encodes the alpha subunit of a transmembrane receptor for collagens and related proteins. The encoded protein forms a heterodimer with a beta subunit and mediates the adhesion of platelets and other cell types to the extracellular matrix. Loss of the encoded protein is associated with bleeding disorder platelet-type 9. Antibodies against this protein are found in several immune disorders, including neonatal alloimmune thrombocytopenia. This gene is located adjacent to a related alpha subunit gene. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Aug 2012]

integrin, alpha 3 (antigen CD49C, alpha 3 subunit of VLA-3 receptor)

The gene encodes a member of the integrin alpha chain family of proteins. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain that function as cell surface adhesion molecules. The encoded preproprotein is proteolytically processed to generate light and heavy chains that comprise the alpha 3 subunit. This subunit joins with a beta 1 subunit to form an integrin that interacts with extracellular matrix proteins including members of the laminin family. Expression of this gene may be correlated with breast cancer metastasis. [provided by RefSeq, Oct 2015]

integrin, alpha 4 (antigen CD49D, alpha 4 subunit of VLA-4 receptor)

The gene encodes a member of the integrin alpha chain family of proteins. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain that function in cell surface adhesion and signaling. The encoded preproprotein is proteolytically processed to generate light and heavy chains that comprise the alpha 4 subunit. This subunit associates with a beta 1 or beta 7 subunit to form an integrin that may play a role in cell motility and migration. This integrin is a therapeutic target for the treatment of multiple sclerosis, Crohn's disease and inflammatory bowel disease. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Oct 2015]

integrin, alpha 5 (fibronectin receptor, alpha polypeptide)

The product of this gene belongs to the integrin alpha chain family. Integrins are heterodimeric integral membrane proteins composed of an alpha subunit and a beta subunit that function in cell surface adhesion and signaling. The encoded preproprotein is proteolytically processed to generate light and heavy chains that comprise the alpha 5 subunit. This subunit associates with the beta 1 subunit to form a fibronectin receptor. This integrin may promote tumor invasion, and higher expression of this gene may be correlated with shorter survival time in lung cancer patients. Note that the integrin alpha 5 and integrin alpha V subunits are encoded by distinct genes. [provided by RefSeq, Oct 2015]

integrin, alpha 6

The gene encodes a member of the integrin alpha chain family of proteins. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain that function in cell surface adhesion and signaling. The encoded preproprotein is proteolytically processed to generate light and heavy chains that comprise the alpha 6 subunit. This subunit may associate with a beta 1 or beta 4 subunit to form an integrin that interacts with extracellular matrix proteins including members of the laminin family. The alpha 6 beta 4 integrin may promote tumorigenesis, while the alpha 6 beta 1 integrin may negatively regulate erbB2/HER2 signaling. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Oct 2015]

integrin, alpha 7

The protein encoded by this gene belongs to the integrin alpha chain family. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. They mediate a wide spectrum of cell-cell and cell-matrix interactions, and thus play a role in cell migration, morphologic development, differentiation, and metastasis. This protein functions as a receptor for the basement membrane protein laminin-1. It is mainly expressed in skeletal and cardiac muscles and may be involved in differentiation and migration processes during myogenesis. Defects in this gene are associated with congenital myopathy. Alternatively spliced transcript variants encoding different isoforms have been noted for this gene. [provided by RefSeq, Feb 2009]

integrin, alpha X (complement component 3 receptor 4 subunit)

This gene encodes the integrin alpha X chain protein. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. This protein combines with the beta 2 chain (ITGB2) to form a leukocyte-specific integrin referred to as inactivated-C3b (iC3b) receptor 4 (CR4). The alpha X beta 2 complex seems to overlap the properties of the alpha M beta 2 integrin in the adherence of neutrophils and monocytes to stimulated endothelium cells, and in the phagocytosis of complement coated particles. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Nov 2013]

integrin, alpha V

The product of this gene belongs to the integrin alpha chain family. Integrins are heterodimeric integral membrane proteins composed of an alpha subunit and a beta subunit that function in cell surface adhesion and signaling. The encoded preproprotein is proteolytically processed to generate light and heavy chains that comprise the alpha V subunit. This subunit associates with beta 1, beta 3, beta 5, beta 6 and beta 8 subunits. The heterodimer consisting of alpha V and beta 3 subunits is also known as the vitronectin receptor. This integrin may regulate angiogenesis and cancer progression. Alternative splicing results in multiple transcript variants. Note that the integrin alpha 5 and integrin alpha V subunits are encoded by distinct genes. [provided by RefSeq, Oct 2015]

integrin, alpha L (antigen CD11A (p180), lymphocyte function-associated antigen 1; alpha polypeptide)

ITGAL encodes the integrin alpha L chain. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. This I-domain containing alpha integrin combines with the beta 2 chain (ITGB2) to form the integrin lymphocyte function-associated antigen-1 (LFA-1), which is expressed on all leukocytes. LFA-1 plays a central role in leukocyte intercellular adhesion through interactions with its ligands, ICAMs 1-3 (intercellular adhesion molecules 1 through 3), and also functions in lymphocyte costimulatory signaling. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]

integrin, alpha M (complement component 3 receptor 3 subunit)

This gene encodes the integrin alpha M chain. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. This I-domain containing alpha integrin combines with the beta 2 chain (ITGB2) to form a leukocyte-specific integrin referred to as macrophage receptor 1 ('Mac-1'), or inactivated-C3b (iC3b) receptor 3 ('CR3'). The alpha M beta 2 integrin is important in the adherence of neutrophils and monocytes to stimulated endothelium, and also in the phagocytosis of complement coated particles. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Mar 2009]

integrin, alpha D

This gene belongs to the beta-2 integrin family of membrane glycoproteins, which are are composed of non-covalently linked alpha and beta subunits to form a heterodimer. It encodes the alpha subunit of the cell surface heterodimers and is involved in the activation and adhesion functions of leukocytes. The gene is located about 11kb downstream of the integrin subunit alpha X gene, another member of the integrin family. It is expressed in the tissue and circulating myeloid leukocytes. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Dec 2015]

integrin, alpha E (antigen CD103, human mucosal lymphocyte antigen 1; alpha polypeptide)

Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. This gene encodes an I-domain-containing alpha integrin that undergoes post-translational cleavage in the extracellular domain, yielding disulfide-linked heavy and light chains. In combination with the beta 7 integrin, this protein forms the E-cadherin binding integrin known as the human mucosal lymphocyte-1 antigen. This protein is preferentially expressed in human intestinal intraepithelial lymphocytes (IEL), and in addition to a role in adhesion, it may serve as an accessory molecule for IEL activation. [provided by RefSeq, Jul 2008]

integrin-binding sialoprotein

The protein encoded by this gene is a major structural protein of the bone matrix. It constitutes approximately 12% of the noncollagenous proteins in human bone and is synthesized by skeletal-associated cell types, including hypertrophic chondrocytes, osteoblasts, osteocytes, and osteoclasts. The only extraskeletal site of its synthesis is the trophoblast. This protein binds to calcium and hydroxyapatite via its acidic amino acid clusters, and mediates cell attachment through an RGD sequence that recognizes the vitronectin receptor. [provided by RefSeq, Jul 2008]

integrin, alpha X (complement component 3 receptor 4 subunit) pseudogene

integrin, beta 1 (fibronectin receptor, beta polypeptide, antigen CD29 includes MDF2, MSK12)

Integrins are heterodimeric proteins made up of alpha and beta subunits. At least 18 alpha and 8 beta subunits have been described in mammals. Integrin family members are membrane receptors involved in cell adhesion and recognition in a variety of processes including embryogenesis, hemostasis, tissue repair, immune response and metastatic diffusion of tumor cells. This gene encodes a beta subunit. Multiple alternatively spliced transcript variants which encode different protein isoforms have been found for this gene. [provided by RefSeq, Jul 2008]

integrin, beta 2 (complement component 3 receptor 3 and 4 subunit)

This gene encodes an integrin beta chain, which combines with multiple different alpha chains to form different integrin heterodimers. Integrins are integral cell-surface proteins that participate in cell adhesion as well as cell-surface mediated signalling. The encoded protein plays an important role in immune response and defects in this gene cause leukocyte adhesion deficiency. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Dec 2014]

integrin, beta 5

This gene encodes a beta subunit of integrin, which can combine with different alpha chains to form a variety of integrin heterodimers. Integrins are integral cell-surface receptors that participate in cell adhesion as well as cell-surface mediated signaling. The alphav beta5 integrin is involved in adhesion to vitronectin. [provided by RefSeq, Aug 2017]

integrin, beta 4

Integrins are heterodimers comprised of alpha and beta subunits, that are noncovalently associated transmembrane glycoprotein receptors. Different combinations of alpha and beta polypeptides form complexes that vary in their ligand-binding specificities. Integrins mediate cell-matrix or cell-cell adhesion, and transduced signals that regulate gene expression and cell growth. This gene encodes the integrin beta 4 subunit, a receptor for the laminins. This subunit tends to associate with alpha 6 subunit and is likely to play a pivotal role in the biology of invasive carcinoma. Mutations in this gene are associated with epidermolysis bullosa with pyloric atresia. Multiple alternatively spliced transcript variants encoding distinct isoforms have been found for this gene. [provided by RefSeq, Jul 2008]

integrin, beta 7

This gene encodes a protein that is a member of the integrin superfamily. Members of this family are adhesion receptors that function in signaling from the extracellular matrix to the cell. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. The encoded protein forms dimers with an alpha4 chain or an alphaE chain and plays a role in leukocyte adhesion. Dimerization with alpha4 forms a homing receptor for migration of lymphocytes to the intestinal mucosa and Peyer's patches. Dimerization with alphaE permits binding to the ligand epithelial cadherin, a calcium-dependent adhesion molecule. Alternate splicing results in multiple transcript variants. Additional alternatively spliced transcript variants of this gene have been described, but their full-length nature is not known. [provided by RefSeq, Sep 2013]

integrin, beta 6

This gene encodes a protein that is a member of the integrin superfamily. Members of this family are adhesion receptors that function in signaling from the extracellular matrix to the cell. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. The encoded protein forms a dimer with an alpha v chain and this heterodimer can bind to ligands like fibronectin and transforming growth factor beta 1. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Sep 2013]

integrin, beta 8

This gene is a member of the integrin beta chain family and encodes a single-pass type I membrane protein with a VWFA domain and four cysteine-rich repeats. This protein noncovalently binds to an alpha subunit to form a heterodimeric integrin complex. In general, integrin complexes mediate cell-cell and cell-extracellular matrix interactions and this complex plays a role in human airway epithelial proliferation. Alternatively spliced variants which encode different protein isoforms have been described; however, not all variants have been fully characterized. [provided by RefSeq, Jul 2008]

integrin, alpha 10

Integrins are integral transmembrane glycoproteins composed of noncovalently linked alpha and beta chains. They participate in cell adhesion as well as cell-surface mediated signalling. This gene encodes an integrin alpha chain and is expressed at high levels in chondrocytes, where it is transcriptionally regulated by AP-2epsilon and Ets-1. The protein encoded by this gene binds to collagen. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Dec 2014]

integrin, alpha 11

This gene encodes an alpha integrin. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. This protein contains an I domain, is expressed in muscle tissue, dimerizes with beta 1 integrin in vitro, and appears to bind collagen in this form. Therefore, the protein may be involved in attaching muscle tissue to the extracellular matrix. Alternative transcriptional splice variants have been found for this gene, but their biological validity is not determined. [provided by RefSeq, Jul 2008]

integrin, beta-like 1 (with EGF-like repeat domains)

This gene encodes a beta integrin-related protein that is a member of the EGF-like protein family. The encoded protein contains integrin-like cysteine-rich repeats. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Nov 2012]

integrin beta 1 pseudogene 1

calcium and integrin binding family member 2

The protein encoded by this gene is similar to that of KIP/CIB, calcineurin B, and calmodulin. The encoded protein is a calcium-binding regulatory protein that interacts with DNA-dependent protein kinase catalytic subunits (DNA-PKcs), and it is involved in photoreceptor cell maintenance. Mutations in this gene cause deafness, autosomal recessive, 48 (DFNB48), and also Usher syndrome 1J (USH1J). Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2014]

calcium and integrin binding family member 3

This gene product shares a high degree of sequence similarity with DNA-dependent protein kinase catalytic subunit-interacting protein 2 in human and mouse, and like them may bind the catalytic subunit of DNA-dependent protein kinases. The exact function of this gene is not known. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2014]

calcium and integrin binding 1 (calmyrin)

This gene encodes a member of the EF-hand domain-containing calcium-binding superfamily. The encoded protein interacts with many other proteins, including the platelet integrin alpha-IIb-beta-3, DNA-dependent protein kinase, presenilin-2, focal adhesion kinase, p21 activated kinase, and protein kinase D. The encoded protein may be involved in cell survival and proliferation, and is associated with several disease states including cancer and Alzheimer's disease. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Apr 2013]

calcium and integrin binding family member 4

Enables calcium ion binding activity and magnesium ion binding activity. [provided by Alliance of Genome Resources, Mar 2025]

integrin alpha FG-GAP repeat containing 2 pseudogene

integrin beta 1 binding protein 1

The cytoplasmic domains of integrins are essential for cell adhesion. The protein encoded by this gene binds to the beta1 integrin cytoplasmic domain. The interaction between this protein and beta1 integrin is highly specific. Two isoforms of this protein are derived from alternatively spliced transcripts. The shorter form of this protein does not interact with the beta1 integrin cytoplasmic domain. The longer form is a phosphoprotein and the extent of its phosphorylation is regulated by the cell-matrix interaction, suggesting an important role of this protein during integrin-dependent cell adhesion. Several transcript variants, some protein-coding and some non-protein coding, have been found for this gene. [provided by RefSeq, Jan 2016]

integrin beta 1 binding protein (melusin) 2

This gene encodes a protein with two cysteine and histidine-rich (CHORD) domains, PXXP motifs, YXXI/P motifs, putative SH2 and SH3 domain binding motifs, and an acidic region at the C-terminus that can bind calcium. Two hybrid analysis showed that this protein interacts with the cytoplasmic domain of the beta 1 integrin subunit and is thought to act as a chaperone protein. Studies in the mouse ortholog of this gene indicate that absence of this gene in mouse results in failed cardiac hypertrophy in response to mechanical stress. Alternative splicing results in multiple transcript variants encoding different isoforms, including an isoform that lacks several domains, including one of the CHORD domains. [provided by RefSeq, May 2017]

integrin-linked kinase-associated serine/threonine phosphatase

The protein encoded by this gene is a protein serine/threonine phosphatase of the PP2C family. This protein can interact with integrin-linked kinase (ILK/ILK1), a regulator of integrin mediated signaling, and regulate the kinase activity of ILK. Through the interaction with ILK, this protein may selectively affect the signaling process of ILK-mediated glycogen synthase kinase 3 beta (GSK3beta), and thus participate in Wnt signaling pathway. [provided by RefSeq, Jul 2008]

integrin beta 1 binding protein 1 pseudogene

integrin alpha FG-GAP repeat containing 3

Located in cell surface. [provided by Alliance of Genome Resources, Mar 2025]

integrin alpha FG-GAP repeat containing 2

Involved in cellular response to amino acid starvation; cellular response to glucose starvation; and negative regulation of TORC1 signaling. Located in Golgi apparatus and lysosomal membrane. Part of KICSTOR complex. [provided by Alliance of Genome Resources, Mar 2025]

integrin alpha FG-GAP repeat containing 1

Located in extracellular exosome. [provided by Alliance of Genome Resources, Mar 2025]

integrin-linked kinase

This gene encodes a protein with a kinase-like domain and four ankyrin-like repeats. The encoded protein associates at the cell membrane with the cytoplasmic domain of beta integrins, where it regulates integrin-mediated signal transduction. Activity of this protein is important in the epithelial to mesenchymal transition, and over-expression of this gene is implicated in tumor growth and metastasis. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jun 2013]

dystroglycan 1 (dystrophin-associated glycoprotein 1)

This gene encodes dystroglycan, a central component of dystrophin-glycoprotein complex that links the extracellular matrix and the cytoskeleton in the skeletal muscle. The encoded preproprotein undergoes O- and N-glycosylation, and proteolytic processing to generate alpha and beta subunits. Certain mutations in this gene are known to cause distinct forms of muscular dystrophy. Alternative splicing results in multiple transcript variants, all encoding the same protein. [provided by RefSeq, Nov 2015]

POM121 membrane glycoprotein (rat) pseudogene

glycoprotein M6B pseudogene 3

glycoprotein hormone alpha 2

GPHA2 is a cystine knot-forming polypeptide and a subunit of the dimeric glycoprotein hormone family (Hsu et al., 2002 [PubMed 12089349]).[supplied by OMIM, Mar 2008]

myelin oligodendrocyte glycoprotein

The product of this gene is a membrane protein expressed on the oligodendrocyte cell surface and the outermost surface of myelin sheaths. Due to this localization, it is a primary target antigen involved in immune-mediated demyelination. This protein may be involved in completion and maintenance of the myelin sheath and in cell-cell communication. Alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq, Jul 2008]

ice-structuring glycoprotein-like

pregnancy specific beta-1-glycoprotein 8

The human pregnancy-specific glycoproteins (PSGs) are a group of molecules that are mainly produced by the placental syncytiotrophoblasts during pregnancy. PSGs comprise a subgroup of the carcinoembryonic antigen (CEA) family, which belongs to the immunoglobulin superfamily. For additional general information about the PSG gene family, see PSG1 (MIM 176390).[supplied by OMIM, Oct 2009]

pregnancy specific beta-1-glycoprotein 9

The protein encoded by this gene is a member of the pregnancy-specific glycoprotein (PSG) family. This protein family and the closely related carcinoembryonic antigen cell adhesion molecule (CEACAM) gene family are both members of the immunoglobulin superfamily, and are organized as a large gene cluster. This protein is thought to inhibit platelet-fibrinogen interactions. Several studies suggest that reduced serum concentrations of PSGs are associated with fetal growth restrictions, while up-regulation of this gene has been observed in colorectal cancers. Several pseudogenes of this gene are found on chromosome 19. Alternative splicing results in multiple transcript variants that encode multiple protein isoforms. [provided by RefSeq, Sep 2014]

pregnancy specific beta-1-glycoprotein 6

This gene is a member of the pregnancy-specific glycoprotein (PSG) gene family. The PSG genes are a subgroup of the carcinoembryonic antigen (CEA) family of immunoglobulin-like genes, and are found in a gene cluster at 19q13.1-q13.2 telomeric to another cluster of CEA-related genes. The PSG genes are expressed by placental trophoblasts and released into the maternal circulation during pregnancy, and are thought to be essential for maintenance of normal pregnancy. The protein encoded by this gene contains the Arg-Gly-Asp tripeptide associated with cellular adhesion and recognition. Alternative splicing results in multiple transcript variants and protein isoforms. [provided by RefSeq, Jul 2012]

pregnancy specific beta-1-glycoprotein 7 (gene/pseudogene)

This gene is a member of the pregnancy-specific glycoprotein (PSG) gene family. The PSG genes are a subgroup of the carcinoembryonic antigen (CEA) family of immunoglobulin-like genes, and are found in a gene cluster at 19q13.1-q13.2 telomeric to another cluster of CEA-related genes. The PSG genes are expressed by placental trophoblasts and released into the maternal circulation during pregnancy, and are thought to be essential for maintenance of normal pregnancy. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Feb 2014]

pregnancy specific beta-1-glycoprotein 4

The protein encoded by this gene is a pregnancy-specific glycoprotein (PSG), one of several encoded by a cluster of similar genes on chromosome 19. This gene is a member of the carcinoembryonic antigen (CEA) gene family and may play a role in regulation of the innate immune system. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Oct 2015]

pregnancy specific beta-1-glycoprotein 5

The human pregnancy-specific glycoproteins (PSGs) are a group of molecules that are mainly produced by the placental syncytiotrophoblasts during pregnancy. PSGs comprise a subgroup of the carcinoembryonic antigen (CEA) family, which belongs to the immunoglobulin superfamily. For additional general information about the PSG gene family, see PSG1 (MIM 176390).[supplied by OMIM, Oct 2009]

pregnancy specific beta-1-glycoprotein 2

The human pregnancy-specific glycoproteins (PSGs) are a family of proteins that are synthesized in large amounts by placental trophoblasts and released into the maternal circulation during pregnancy. Molecular cloning and analysis of several PSG genes has indicated that the PSGs form a subgroup of the carcinoembryonic antigen (CEA) gene family, which belongs to the immunoglobulin superfamily of genes. Members of the CEA family consist of a single N domain, with structural similarity to the immunoglobulin variable domains, followed by a variable number of immunoglobulin constant-like A and/or B domains. Most PSGs have an arg-gly-asp (RGD) motif, which has been shown to function as an adhesion recognition signal for several integrins, in the N-terminal domain (summary by Teglund et al., 1994 [PubMed 7851896]). For additional general information about the PSG gene family, see PSG1 (MIM 176390).[supplied by OMIM, Oct 2009]

pregnancy specific beta-1-glycoprotein 3

The human pregnancy-specific glycoproteins (PSGs) are a family of proteins that are synthesized in large amounts by placental trophoblasts and released into the maternal circulation during pregnancy. Molecular cloning and analysis of several PSG genes has indicated that the PSGs form a subgroup of the carcinoembryonic antigen (CEA) gene family, which belongs to the immunoglobulin superfamily of genes. Members of the CEA family consist of a single N domain, with structural similarity to the immunoglobulin variable domains, followed by a variable number of immunoglobulin constant-like A and/or B domains. Most PSGs have an arg-gly-asp (RGD) motif, which has been shown to function as an adhesion recognition signal for several integrins, in the N-terminal domain (summary by Teglund et al., 1994 [PubMed 7851896]). For additional general information about the PSG gene family, see PSG1 (MIM 176390).[supplied by OMIM, Oct 2009]

pregnancy specific beta-1-glycoprotein 1

The human placenta is a multihormonal endocrine organ that produces hormones, enzymes, and other molecules that support fetal survival and development. Pregnancy-specific beta-1-glycoprotein (PSBG, PSG) is a major product of the syncytiotrophoblast, reaching concentrations of 100 to 290 mg/l at term in the serum of pregnant women (Horne et al., 1976 [PubMed 971765]). PSG is a member of the immunoglobulin (Ig) superfamily (Watanabe and Chou, 1988 [PubMed 3257488]; Streydio et al., 1988 [PubMed 3260773]).[supplied by OMIM, Oct 2009]

zona pellucida glycoprotein 3 (sperm receptor) pseudogene

nuclear pore membrane glycoprotein 210-like

carcinoembryonic antigen-related cell adhesion molecule 1 (biliary glycoprotein) pseudogene

POM121 membrane glycoprotein (rat) pseudogene

POM121 membrane glycoprotein (rat) pseudogene

trehalase (brush-border membrane glycoprotein) pseudogene

chitinase 3-like 1 (cartilage glycoprotein-39)

Chitinases catalyze the hydrolysis of chitin, which is an abundant glycopolymer found in insect exoskeletons and fungal cell walls. The glycoside hydrolase 18 family of chitinases includes eight human family members. This gene encodes a glycoprotein member of the glycosyl hydrolase 18 family. The protein lacks chitinase activity and is secreted by activated macrophages, chondrocytes, neutrophils and synovial cells. The protein is thought to play a role in the process of inflammation and tissue remodeling. [provided by RefSeq, Sep 2009]

golgi glycoprotein 1

Predicted to enable fibroblast growth factor binding activity. Predicted to act upstream of or within several processes, including negative regulation of protein processing; negative regulation of transforming growth factor beta receptor signaling pathway; and regulation of chondrocyte differentiation. Located in Golgi apparatus. [provided by Alliance of Genome Resources, Mar 2025]

trehalase (brush-border membrane glycoprotein)

This gene encodes an enzyme that hydrolyses trehalose, a disaccharide formed from two glucose molecules found mainly in fungi, plants, and insects. A partial duplication of this gene is located adjacent to this locus on chromosome 11. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2014]

synaptic vesicle glycoprotein 2A

The protein encoded by this gene is one of three related synaptic vesicle proteins. The encoded protein may interact with synaptotagmin to enhance low frequency neurotransmission in quiescent neurons. [provided by RefSeq, Jun 2016]

synaptic vesicle glycoprotein 2C

Predicted to enable transmembrane transporter activity. Predicted to be involved in several processes, including chemical synaptic transmission; neurotransmitter transport; and regulation of synaptic vesicle exocytosis. Predicted to be located in plasma membrane and synaptic vesicle. Predicted to be active in dopaminergic synapse and synaptic vesicle membrane. [provided by Alliance of Genome Resources, Mar 2025]

synaptic vesicle glycoprotein 2B

This gene encodes a member of the synaptic vesicle proteins 2 (SV2) family and major facilitator superfamily of proteins. This protein and other members of the family are localized to synaptic vesicles and may function in the regulation of vesicle trafficking and exocytosis. Studies in mice suggest that the encoded protein may act as a protein receptor for botulinum neurotoxin E in neurons, and that this protein may be important for the integrity of the glomerular filtration barrier. This gene shows reduced expression in areas of synaptic loss in the hippocampus of human temporal lobe epilepsy patients. [provided by RefSeq, Sep 2016]

POM121 membrane glycoprotein (rat) pseudogene

glycoprotein 2 (zymogen granule membrane)

This gene encodes an integral membrane protein that is secreted from intracellular zymogen granules and associates with the plasma membrane via glycosylphosphatidylinositol (GPI) linkage. The encoded protein binds pathogens such as enterobacteria, thereby playing an important role in the innate immune response. The C-terminus of this protein is related to the C-terminus of the protein encoded by the neighboring gene, uromodulin (UMOD). Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2015]

alpha-2-glycoprotein 1, zinc-binding pseudogene 1

apolipoprotein H (beta-2-glycoprotein I)

Apolipoprotein H, also known as beta-2-glycoprotein I, is a component of circulating plasma lipoproteins. It has been implicated in a variety of physiologic pathways including lipoprotein metabolism, coagulation, hemostasis, and the production of antiphospholipid autoantibodies. APOH may be a required cofactor for anionic phospholipid binding by the antiphospholipid autoantibodies found in sera of many patients with lupus and primary antiphospholipid syndrome (APS). The anti-beta (2) glycoprotein I antibodies from APS patients, mediate inhibition of activated protein C which has anticoagulant properties. Because beta-2-GPI is the main autoantigen in patients with APS, the disruption of this pathway by autoantibodies may be an important mechanism for thrombosis in patients with APS.[provided by RefSeq, Dec 2019]

integral membrane glycoprotein-like

ice-structuring glycoprotein-like

zona pellucida glycoprotein 1 (sperm receptor)

The zona pellucida is an extracellular matrix that surrounds the oocyte and early embryo. It is composed primarily of three or four glycoproteins with various functions during fertilization and preimplantation development. The protein encoded by this gene ensures the structural integrity of the zona pellucida. Mutations in this gene are a cause of oocyte maturation defect and infertility. [provided by RefSeq, May 2014]

zona pellucida glycoprotein 3 (sperm receptor)

The zona pellucida is an extracellular matrix that surrounds the oocyte and early embryo. It is composed primarily of three or four glycoproteins with various functions during fertilization and preimplantation development. The protein encoded by this gene is a structural component of the zona pellucida and functions in primary binding and induction of the sperm acrosome reaction. The nascent protein contains a N-terminal signal peptide sequence, a conserved ZP domain, a C-terminal consensus furin cleavage site, and a transmembrane domain. It is hypothesized that furin cleavage results in release of the mature protein from the plasma membrane for subsequent incorporation into the zona pellucida matrix. However, the requirement for furin cleavage in this process remains controversial based on mouse studies. A variation in the last exon of this gene has previously served as the basis for an additional ZP3 locus; however, sequence and literature review reveals that there is only one full-length ZP3 locus in the human genome. Another locus encoding a bipartite transcript designated POMZP3 contains a duplication of the last four exons of ZP3, including the above described variation, and maps closely to this gene. [provided by RefSeq, Jul 2008]

zona pellucida glycoprotein 2 (sperm receptor)

The zona pellucida is an extracellular matrix that surrounds the oocyte and early embryo. It is composed of three glycoproteins with various functions during fertilization and preimplantation development. The glycosylated mature peptide is one of the structural components of the zona pellucida and functions in secondary binding and penetration of acrosome-reacted spermatozoa. Female mice lacking this gene do not form a stable zona matrix and are sterile. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Feb 2014]

zona pellucida glycoprotein 4

The zona pellucida is an extracellular matrix that surrounds the oocyte and early embryo. It is composed primarily of three or four glycoproteins with various functions during fertilization and preimplantation development. The nascent protein contains a N-terminal signal peptide sequence, a conserved ZP domain, a consensus furin cleavage site, and a C-terminal transmembrane domain. It is hypothesized that furin cleavage results in release of the mature protein from the plasma membrane for subsequent incorporation into the zona pellucida matrix. However, the requirement for furin cleavage in this process remains controversial based on mouse studies. Previously, this gene has been referred to as ZP1 or ZPB and thought to have similar functions as mouse Zp1. However, a human gene with higher similarity and chromosomal synteny to mouse Zp1 has been assigned the symbol ZP1 and this gene has been assigned the symbol ZP4. [provided by RefSeq, Jul 2008]

oligodendrocyte myelin glycoprotein

Predicted to enable identical protein binding activity. Predicted to be involved in neuron projection regeneration. Predicted to act upstream of or within regulation of collateral sprouting of intact axon in response to injury. Predicted to be located in plasma membrane. [provided by Alliance of Genome Resources, Mar 2025]

Rh family, B glycoprotein (gene/pseudogene)

This gene encodes one of two non-erythroid members of the Rhesus (Rh) protein family. Non-erythroid Rh protein family members are mainly expressed in the kidney and belong to the methylammonium-ammonium permease/ammonia transporters superfamily. All Rh family proteins are predicted to be transmembrane proteins with 12 membrane spanning domains and intracytoplasmic N- and C-termini. Alternative splicing of this gene results in multiple transcript variants. [provided by RefSeq, Jan 2012]

mannosyl (alpha-1,6-)-glycoprotein beta-1,6-N-acetyl-glucosaminyltransferase, isozyme B

Enables alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase activity and manganese ion binding activity. Involved in protein O-linked glycosylation via serine. Predicted to be located in Golgi membrane. Predicted to be active in Golgi apparatus. [provided by Alliance of Genome Resources, Mar 2025]

zona pellucida glycoprotein 3 (sperm receptor) pseudogene

mannosyl (alpha-1,3-)-glycoprotein beta-1,2-N-acetylglucosaminyltransferase

There are believed to be over 100 different glycosyltransferases involved in the synthesis of protein-bound and lipid-bound oligosaccharides. UDP-N-acetylglucosamine:alpha-3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I is a medial-Golgi enzyme essential for the synthesis of hybrid and complex N-glycans. The protein, encoded by a single exon, shows typical features of a type II transmembrane protein. The protein is believed to be essential for normal embryogenesis. Several variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008]

mannosyl (alpha-1,6-)-glycoprotein beta-1,2-N-acetylglucosaminyltransferase

The product of this gene is a Golgi enzyme catalyzing an essential step in the conversion of oligomannose to complex N-glycans. The enzyme has the typical glycosyltransferase domains: a short N-terminal cytoplasmic domain, a hydrophobic non-cleavable signal-anchor domain, and a C-terminal catalytic domain. Mutations in this gene may lead to carbohydrate-deficient glycoprotein syndrome, type II. The coding region of this gene is intronless. Transcript variants with a spliced 5' UTR may exist, but their biological validity has not been determined. [provided by RefSeq, Jul 2008]

mannosyl (beta-1,4-)-glycoprotein beta-1,4-N-acetylglucosaminyltransferase

There are believed to be over 100 different glycosyltransferases involved in the synthesis of protein-bound and lipid-bound oligosaccharides. The enzyme encoded by this gene transfers a GlcNAc residue to the beta-linked mannose of the trimannosyl core of N-linked oligosaccharides and produces a bisecting GlcNAc. Multiple alternatively spliced variants, encoding the same protein, have been identified. [provided by RefSeq, Jul 2008]

mannosyl (alpha-1,6-)-glycoprotein beta-1,6-N-acetyl-glucosaminyltransferase

The protein encoded by this gene belongs to the glycosyltransferase family. It catalyzes the addition of beta-1,6-N-acetylglucosamine to the alpha-linked mannose of biantennary N-linked oligosaccharides present on the newly synthesized glycoproteins. It is one of the most important enzymes involved in the regulation of the biosynthesis of glycoprotein oligosaccharides. Alterations of the oligosaccharides on cell surface glycoproteins cause significant changes in the adhesive or migratory behavior of a cell. Increase in the activity of this enzyme has been correlated with the progression of invasive malignancies. [provided by RefSeq, Oct 2011]

POM121 membrane glycoprotein (rat) pseudogene

follistatin-like 3 (secreted glycoprotein)

Follistatin-like 3 is a secreted glycoprotein of the follistatin-module-protein family. It may have a role in leukemogenesis. [provided by RefSeq, Jul 2008]

small cell adhesion glycoprotein

Located in cell junction; nucleoplasm; and plasma membrane. [provided by Alliance of Genome Resources, Mar 2025]

Rh-associated glycoprotein

The protein encoded by this gene is erythrocyte-specific and is thought to be part of a membrane channel that transports ammonium and carbon dioxide across the blood cell membrane. The encoded protein appears to interact with Rh blood group antigens and Rh30 polypeptides. Defects in this gene are a cause of regulator type Rh-null hemolytic anemia (RHN), or Rh-deficiency syndrome.[provided by RefSeq, Mar 2009]

POM121 membrane glycoprotein (rat) pseudogene

pregnancy specific beta-1-glycoprotein 9 pseudogene

glycoprotein hormones, alpha polypeptide

The four human glycoprotein hormones chorionic gonadotropin (CG), luteinizing hormone (LH), follicle stimulating hormone (FSH), and thyroid stimulating hormone (TSH) are dimers consisting of alpha and beta subunits that are associated noncovalently. The alpha subunits of these hormones are identical, however, their beta chains are unique and confer biological specificity. The protein encoded by this gene is the alpha subunit and belongs to the glycoprotein hormones alpha chain family. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Nov 2011]

glycoprotein (transmembrane) nmb

The protein encoded by this gene is a type I transmembrane glycoprotein which shows homology to the pMEL17 precursor, a melanocyte-specific protein. GPNMB shows expression in the lowly metastatic human melanoma cell lines and xenografts but does not show expression in the highly metastatic cell lines. GPNMB may be involved in growth delay and reduction of metastatic potential. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]

glycoprotein Xg-like

pregnancy specific beta-1-glycoprotein 11

The human pregnancy-specific glycoproteins (PSGs) are a group of molecules that are mainly produced by the placental syncytiotrophoblasts during pregnancy. PSGs comprise a subgroup of the carcinoembryonic antigen (CEA) family, which belongs to the immunoglobulin superfamily. For additional general information about the PSG gene family, see PSG1 (MIM 176390).[supplied by OMIM, Oct 2009]

pancreatic beta cell glycoprotein 1

alpha-2-HS-glycoprotein

The protein encoded by this gene is a negatively-charged serum glycoprotein that is synthesized by hepatocytes. The encoded protein consists of two polypeptide chains, which are both cleaved from a proprotein encoded from a single mRNA. It is involved in several processes, including endocytosis, brain development, and the formation of bone tissue. Defects in this gene are a cause of susceptibility to leanness. [provided by RefSeq, Aug 2017]

histidine-rich glycoprotein

This histidine-rich glycoprotein contains two cystatin-like domains and is located in plasma and platelets. The physiological function has not been determined but it is known that the protein binds heme, dyes and divalent metal ions. The encoded protein also has a peptide that displays antimicrobial activity against C. albicans, E. coli, S. aureus, P. aeruginosa, and E. faecalis. It can inhibit rosette formation and interacts with heparin, thrombospondin and plasminogen. Two of the protein's effects, the inhibition of fibrinolysis and the reduction of inhibition of coagulation, indicate a potential prothrombotic effect. Mutations in this gene lead to thrombophilia due to abnormal histidine-rich glycoprotein levels. [provided by RefSeq, Nov 2014]

histidine-rich glycoprotein pseudogene

sarcoglycan, gamma (35kDa dystrophin-associated glycoprotein)

This gene encodes gamma-sarcoglycan, one of several sarcolemmal transmembrane glycoproteins that interact with dystrophin. The dystrophin-glycoprotein complex (DGC) spans the sarcolemma and is comprised of dystrophin, syntrophin, alpha- and beta-dystroglycans and sarcoglycans. The DGC provides a structural link between the subsarcolemmal cytoskeleton and the extracellular matrix of muscle cells. Defects in the encoded protein can lead to early onset autosomal recessive muscular dystrophy, in particular limb-girdle muscular dystrophy, type 2C (LGMD2C). [provided by RefSeq, Oct 2008]

sarcoglycan, delta (35kDa dystrophin-associated glycoprotein)

The protein encoded by this gene is one of the four known components of the sarcoglycan complex, which is a subcomplex of the dystrophin-glycoprotein complex (DGC). DGC forms a link between the F-actin cytoskeleton and the extracellular matrix. This protein is expressed most abundantly in skeletal and cardiac muscle. Mutations in this gene have been associated with autosomal recessive limb-girdle muscular dystrophy and dilated cardiomyopathy. Alternatively spliced transcript variants encoding distinct isoforms have been observed for this gene. [provided by RefSeq, Jul 2008]

sarcoglycan, beta (43kDa dystrophin-associated glycoprotein)

This gene encodes a member of the sarcoglycan family. Sarcoglycans are transmembrane components in the dystrophin-glycoprotein complex which help stabilize the muscle fiber membranes and link the muscle cytoskeleton to the extracellular matrix. Mutations in this gene have been associated with limb-girdle muscular dystrophy.[provided by RefSeq, Oct 2008]

sarcoglycan, alpha (50kDa dystrophin-associated glycoprotein)

This gene encodes a component of the dystrophin-glycoprotein complex (DGC), which is critical to the stability of muscle fiber membranes and to the linking of the actin cytoskeleton to the extracellular matrix. Its expression is thought to be restricted to striated muscle. Mutations in this gene result in type 2D autosomal recessive limb-girdle muscular dystrophy. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Oct 2008]

UDP-glucose glycoprotein glucosyltransferase 2

UDP-glucose:glycoprotein glucosyltransferase (UGT) is a soluble protein of the endoplasmic reticulum (ER) that selectively reglucosylates unfolded glycoproteins, thus providing quality control for protein transport out of the ER.[supplied by OMIM, Oct 2009]

UDP-glucose glycoprotein glucosyltransferase 1

UDP-glucose:glycoprotein glucosyltransferase (UGT) is a soluble protein of the endoplasmic reticulum (ER) that selectively reglucosylates unfolded glycoproteins, thus providing quality control for protein transport out of the ER.[supplied by OMIM, Oct 2009]

glycoprotein A33 (transmembrane)

The glycoprotein encoded by this gene is a cell surface antigen that is expressed in greater than 95% of human colon cancers. The open reading frame encodes a 319-amino acid polypeptide having a putative secretory signal sequence and 3 potential glycosylation sites. The predicted mature protein has a 213-amino acid extracellular region, a single transmembrane domain, and a 62-amino acid intracellular tail. The sequence of the extracellular region contains 2 domains characteristic of the CD2 subgroup of the immunoglobulin (Ig) superfamily. [provided by RefSeq, Jul 2008]

alpha-2-glycoprotein 1, zinc-binding pseudogene 2

POM121 membrane glycoprotein (rat) pseudogene

glycoprotein integral membrane 1

Predicted to be located in membrane. [provided by Alliance of Genome Resources, Mar 2025]

alpha-1-B glycoprotein

The protein encoded by this gene is a plasma glycoprotein of unknown function. The protein shows sequence similarity to the variable regions of some immunoglobulin supergene family member proteins. [provided by RefSeq, Jul 2008]

POM121 membrane glycoprotein (rat) pseudogene

alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase-like protein LOC641515 homolog

glycoprotein hormone beta 5

GPHB5 is a cystine knot-forming polypeptide and a subunit of the dimeric glycoprotein hormone family (Hsu et al., 2002 [PubMed 12089349]).[supplied by OMIM, Mar 2008]

ore 1 synthase, glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1 pseudogene 2

leucine-rich alpha-2-glycoprotein 1

The leucine-rich repeat (LRR) family of proteins, including LRG1, have been shown to be involved in protein-protein interaction, signal transduction, and cell adhesion and development. LRG1 is expressed during granulocyte differentiation (O'Donnell et al., 2002 [PubMed 12223515]).[supplied by OMIM, Mar 2008]

POM121 membrane glycoprotein pseudogene

alpha-2-glycoprotein 1, zinc-binding

Predicted to enable RNA nuclease activity and protein transmembrane transporter activity. Involved in cell adhesion and detection of chemical stimulus involved in sensory perception of bitter taste. Located in extracellular space. Implicated in prostate carcinoma. Biomarker of several diseases, including gastrointestinal system cancer (multiple); kidney failure (multiple); liver cirrhosis; lung adenocarcinoma; and obesity. [provided by Alliance of Genome Resources, Mar 2025]

trophoblast glycoprotein

This gene encodes a leucine-rich transmembrane glycoprotein that may be involved in cell adhesion. The encoded protein is an oncofetal antigen that is specific to trophoblast cells. In adults this protein is highly expressed in many tumor cells and is associated with poor clinical outcome in numerous cancers. Alternate splicing in the 5' UTR results in multiple transcript variants that encode the same protein. [provided by RefSeq, Oct 2009]

core 1 synthase, glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1 pseudogene 1

papilin, proteoglycan-like sulfated glycoprotein

Predicted to enable serine-type endopeptidase inhibitor activity. Predicted to be involved in extracellular matrix organization. Predicted to be located in basement membrane. [provided by Alliance of Genome Resources, Mar 2025]

trophoblast glycoprotein-like

Predicted to be involved in negative regulation of canonical Wnt signaling pathway. Predicted to be located in membrane. Predicted to be active in plasma membrane. [provided by Alliance of Genome Resources, Mar 2025]

oviductal glycoprotein 1, 120kDa

This gene encodes a large, carbohydrate-rich, epithelial glycoprotein with numerous O-glycosylation sites located within threonine, serine, and proline-rich tandem repeats. The gene is similar to members of the mucin and the glycosyl hydrolase 18 gene families. Regulation of expression may be estrogen-dependent. Gene expression and protein secretion occur during late follicular development through early cleavage-stage embryonic development. The protein is secreted from non-ciliated oviductal epithelial cells and associates with ovulated oocytes, blastomeres, and spermatozoan acrosomal regions. [provided by RefSeq, Jul 2008]

pregnancy specific beta-1-glycoprotein 10, pseudogene

The human pregnancy-specific glycoproteins (PSGs) are a group of molecules that are mainly produced by the placental syncytiotrophoblasts during pregnancy. PSGs comprise a subgroup of the carcinoembryonic antigen (CEA) family, which belongs to the immunoglobulin superfamily. For additional general information about the PSG gene family, see PSG1 (MIM 176390).[supplied by OMIM, Oct 2009]

myelin associated glycoprotein

The protein encoded by this gene is a type I membrane protein and member of the immunoglobulin superfamily. It is thought to be involved in the process of myelination. It is a lectin that binds to sialylated glycoconjugates and mediates certain myelin-neuron cell-cell interactions. Three alternatively spliced transcripts encoding different isoforms have been described for this gene. [provided by RefSeq, Nov 2010]

glycoprotein, alpha-galactosyltransferase 2, pseudogene

POM121 membrane glycoprotein (rat) pseudogene

zona pellucida glycoprotein AX, pseudogene

glycoprotein M6A

Predicted to enable calcium channel activity. Involved in neuron migration and stem cell differentiation. Located in extracellular exosome. [provided by Alliance of Genome Resources, Mar 2025]

glycoprotein M6B

This gene encodes a membrane glycoprotein that belongs to the proteolipid protein family. Proteolipid protein family members are expressed in most brain regions and are thought to be involved in cellular housekeeping functions such as membrane trafficking and cell-to-cell communication. This protein may also be involved in osteoblast differentiation. Alternate splicing results in multiple transcript variants. Pseudogenes of this gene are located on chromosomes Y and 22. [provided by RefSeq, Jan 2016]

P-selectin glycoprotein ligand 1-like

protein Z, vitamin K-dependent plasma glycoprotein

This gene encodes a liver vitamin K-dependent glycoprotein that is synthesized in the liver and secreted into the plasma. The encoded protein plays a role in regulating blood coagulation by complexing with protein Z-dependent protease inhibitor to directly inhibit activated factor X at the phospholipid surface. Deficiencies in this protein are associated with an increased risk of ischemic arterial diseases and fetal loss. Mutations in this gene are the cause of protein Z deficiency. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Jan 2012]

glycoprotein, alpha-galactosyltransferase 1 pseudogene

Alpha-1,3-galactosyltransferase (GGTA1) is an enzyme present in most mammals except man, apes, and Old World monkeys. This gene is thought to encode a truncated, non-enzymatic form of the GGTA1 protein that lacks the C-terminal catalytic domain. Aberrant expression of the GGTA1 protein in man can lead to autoimmune diseases and sometimes germ cell tumors. [provided by RefSeq, May 2020]

POM121 membrane glycoprotein (rat) pseudogene

uncharacterized threonine-rich GPI-anchored glycoprotein PJ4664.02-like

carcinoembryonic antigen-related cell adhesion molecule 1 (biliary glycoprotein)

This gene encodes a member of the carcinoembryonic antigen (CEA) gene family, which belongs to the immunoglobulin superfamily. Two subgroups of the CEA family, the CEA cell adhesion molecules and the pregnancy-specific glycoproteins, are located within a 1.2 Mb cluster on the long arm of chromosome 19. Eleven pseudogenes of the CEA cell adhesion molecule subgroup are also found in the cluster. The encoded protein was originally described in bile ducts of liver as biliary glycoprotein. Subsequently, it was found to be a cell-cell adhesion molecule detected on leukocytes, epithelia, and endothelia. The encoded protein mediates cell adhesion via homophilic as well as heterophilic binding to other proteins of the subgroup. Multiple cellular activities have been attributed to the encoded protein, including roles in the differentiation and arrangement of tissue three-dimensional structure, angiogenesis, apoptosis, tumor suppression, metastasis, and the modulation of innate and adaptive immune responses. Multiple transcript variants encoding different isoforms have been reported, but the full-length nature of all variants has not been defined. [provided by RefSeq, May 2010]

Rh family, C glycoprotein

Enables several functions, including ammonium channel activity; ankyrin binding activity; and carbon dioxide transmembrane transporter activity. Involved in ammonium transmembrane transport; intracellular monoatomic ion homeostasis; and transepithelial ammonium transport. Located in apical plasma membrane and basolateral plasma membrane. [provided by Alliance of Genome Resources, Mar 2025]

mannosyl (alpha-1,3-)-glycoprotein beta-1,4-N-acetylglucosaminyltransferase, isozyme A

This gene encodes a key glycosyltransferase that regulates the formation of tri- and multiantennary branching structures in the Golgi apparatus. The encoded protein, in addition to the related isoenzyme B, catalyzes the transfer of N-acetylglucosamine (GlcNAc) from UDP-GlcNAc in a beta-1,4 linkage to the Man-alpha-1,3-Man-beta-1,4-GlcNAc arm of R-Man-alpha-1,6(GlcNAc-beta-1,2-Man-alpha-1,3)Man-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1-Asn. The encoded protein may play a role in regulating the availability of serum glycoproteins, oncogenesis, and differentiation. [provided by RefSeq, Jul 2008]

mannosyl (alpha-1,3-)-glycoprotein beta-1,4-N-acetylglucosaminyltransferase, isozyme B

This gene encodes a key glycosyltransferase that regulates the formation of tri- and multiantennary branching structures in the Golgi apparatus. The encoded protein, in addition to the related isoenzyme A, catalyzes the transfer of N-acetylglucosamine (GlcNAc) from UDP-GlcNAc in a beta-1,4 linkage to the Man-alpha-1,3-Man-beta-1,4-GlcNAc arm of R-Man-alpha-1,6(GlcNAc-beta-1,2-Man-alpha-1,3)Man-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1-Asn. The encoded protein may play a role in regulating the availability of serum glycoproteins, oncogenesis, and differentiation. [provided by RefSeq, Jul 2008]

integral membrane glycoprotein-like

core 1 synthase, glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1

The protein encoded by this gene generates the common core 1 O-glycan structure, Gal-beta-1-3GalNAc-R, by the transfer of Gal from UDP-Gal to GalNAc-alpha-1-R. Core 1 is a precursor for many extended mucin-type O-glycans on cell surface and secreted glycoproteins. Studies in mice suggest that this gene plays a key role in thrombopoiesis and kidney homeostasis.[provided by RefSeq, Sep 2010]

glycoprotein alpha-galactosyltransferase 1 (inactive)

Alpha-1,3-galactosyltransferase (GGTA1) is an enzyme present in most mammals except man, apes, and Old World monkeys. This gene is thought to encode a truncated, non-enzymatic form of the GGTA1 protein that lacks the C-terminal catalytic domain. Aberrant expression of the GGTA1 protein in man can lead to autoimmune diseases and sometimes germ cell tumors. [provided by RefSeq, May 2020]

From GeneRIF Biological Term Annotations

genes co-occuring with the biological term alphaiib in literature-supported statements describing functions of genes from the GeneRIF Biological Term Annotations dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the dystrophin-associated glycoprotein complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the dystrophin-associated glycoprotein complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From GO Cellular Component Annotations 2015

proteins localized to the dystrophin-associated glycoprotein complex cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the dystrophin-associated glycoprotein complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Glycoprotein Ib-IX-V complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the dystrophin-associated glycoprotein complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Glycoprotein Ib-IX-V complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the integrin alpha11-beta1 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the alpha9-beta1 integrin-adam8 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the integrin alpha4-beta7 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the integrin alpha8-beta1 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the integrin alpha2-beta1 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the integrin alpha6-beta4 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the integrin complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the integrin alphal-beta2 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the alpha9-beta1 integrin-vascular cell adhesion molecule-1 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the integrin alpha7-beta1 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the integrin alphav-beta5 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the integrin alpha9-beta1 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the integrin alpha1-beta1 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the integrin alphav-beta8 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the integrin alpha3-beta1 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the integrin alpha10-beta1 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the integrin alpha11-beta1 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the alpha3-beta1 integrin-cd151 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the integrin alphav-beta1 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the integrin alpha4-beta7 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the integrin alpha4-beta1 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the integrin alpha8-beta1 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the integrin alpha9-beta1 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the integrin alpha6-beta1 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the integrin alpha2-beta1 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the integrin alpha6-beta4 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the integrin alphad-beta2 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the integrin complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the integrin alpha5-beta1 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the integrin alphal-beta2 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the integrin alphav-beta6 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the integrin alpha7-beta1 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the integrin alphav-beta5 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the integrin alpha1-beta1 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the integrin alphae-beta7 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the integrin alphax-beta2 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the integrin alphav-beta8 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the integrin alpham-beta2 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the integrin alpha3-beta1 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the integrin alpha10-beta1 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From CORUM Protein Complexes

proteins in the FAK-beta5 integrin complex, VEGF induced protein complex from the CORUM Protein Complexes dataset.

From GO Cellular Component Annotations 2015

proteins localized to the integrin alpha11-beta1 complex cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the alpha9-beta1 integrin-adam8 complex cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the integrin alpha4-beta7 complex cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the integrin alpha8-beta1 complex cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the integrin alpha2-beta1 complex cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the integrin alpha6-beta4 complex cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the integrin complex cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the integrin alphal-beta2 complex cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the alpha9-beta1 integrin-vascular cell adhesion molecule-1 complex cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the integrin alpha7-beta1 complex cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the integrin alphav-beta5 complex cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the integrin alpha9-beta1 complex cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the integrin alpha1-beta1 complex cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the integrin alphav-beta8 complex cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the integrin alpha3-beta1 complex cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the integrin alpha10-beta1 complex cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the integrin alpha10-beta1 complex cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the integrin alphaL-beta2 complex cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the integrin alphaM-beta2 complex cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the integrin alphaX-beta2 complex cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the integrin alpha5-beta1 complex cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the integrin alpha1-beta1 complex cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the integrin alpha2-beta1 complex cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the integrin alpha3-beta1 complex cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the integrin alpha4-beta1 complex cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the integrin alpha8-beta1 complex cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the integrin alpha11-beta1 complex cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the integrin alphav-beta8 complex cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the integrin alphav-beta5 complex cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the integrin alphav-beta6 complex cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the integrin alpha4-beta7 complex cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the alpha9-beta1 integrin-vascular cell adhesion molecule-1 complex cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the alpha9-beta1 integrin-ADAM8 complex cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the integrin alpha10-beta1 complex cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the integrin alphaL-beta2 complex cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the integrin alphaM-beta2 complex cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the integrin alphaX-beta2 complex cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the integrin alpha1-beta1 complex cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the integrin alpha2-beta1 complex cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the integrin alpha3-beta1 complex cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the integrin alpha4-beta1 complex cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the integrin alpha5-beta1 complex cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the integrin alpha6-beta1 complex cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the integrin alpha8-beta1 complex cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the integrin alpha9-beta1 complex cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the integrin alpha11-beta1 complex cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the integrin alphav-beta1 complex cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the integrin alphav-beta5 complex cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the integrin alphav-beta6 complex cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the integrin alphav-beta8 complex cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the integrin alpha4-beta7 complex cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the alpha9-beta1 integrin-vascular cell adhesion molecule-1 complex cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the alpha9-beta1 integrin-ADAM8 complex cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Integrin alpha3-beta1 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Integrin alpha2-beta1 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Integrin alphav-beta5 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Integrin alpha4-beta7 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Integrin alphaL-beta2 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Integrin alpha5-beta1 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Integrin alphav-beta6 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Integrin alphav-beta8 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Integrin alpha10-beta1 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Integrin alpha1-beta1 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Integrin alpha11-beta1 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Integrin complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the alpha9-beta1 integrin-vascular cell adhesion molecule-1 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Integrin alpha8-beta1 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Integrin alpha6-beta1 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Integrin alphaX-beta2 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Integrin alphaM-beta2 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Integrin alpha9-beta1 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Integrin alpha4-beta1 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Integrin alphav-beta1 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the alpha9-beta1 integrin-ADAM8 complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Integrin alpha4-beta7 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Integrin alpha4-beta1 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Integrin complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Integrin alpha5-beta1 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Integrin alpha2-beta1 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Integrin alpha8-beta1 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Integrin alpha1-beta1 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Integrin alpha6-beta4 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Integrin alphav-beta6 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Integrin alpha3-beta1 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Integrin alpha9-beta1 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Integrin alpha11-beta1 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Integrin alphav-beta8 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Integrin alphaE-beta7 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Integrin alpha10-beta1 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Integrin alpha6-beta1 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Integrin alphaM-beta2 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Integrin alpha7-beta1 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Integrin alphaL-beta2 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Integrin alphaD-beta2 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Integrin alphav-beta5 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Integrin alphaX-beta2 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Integrin alphav-beta1 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the alpha3-beta1 integrin-basigin complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the alphaE-beta7 integrin-E-cadherin complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the alpha9-beta1 integrin-ADAM12 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the alpha5-beta1 integrin-endostatin complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the alpha4-beta1 integrin-JAM2 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the alpha6-beta1 integrin-CD151 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the alpha5-beta1 integrin-fibronectin-tissue transglutaminase complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the alpha3-beta1 integrin-CD151 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the alpha6-beta4 integrin-laminin 5 complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the alphav-beta1 integrin-osteopontin complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the alphav-beta5 integrin-vitronectin complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the alpha3-beta1 integrin-thrombospondin complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Thrombophilia, histidine-rich glycoprotein-related phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Carbohydrate-deficient glycoprotein syndrome type I phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the glycoprotein network cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From CTD Gene-Disease Associations

genes/proteins associated with the disease Thrombophilia Due To Elevated Histidine-Rich Glycoprotein from the curated CTD Gene-Disease Associations dataset.

From GAD Gene-Disease Associations

genes associated with the disease reduced gene expression and lower plasma levels of beta2-glycoprotein i in GWAS and other genetic association datasets from the GAD Gene-Disease Associations dataset.

From GAD Gene-Disease Associations

genes associated with the disease altered efflux of the p-glycoprotein substrate rhodamine in GWAS and other genetic association datasets from the GAD Gene-Disease Associations dataset.

From GAD Gene-Disease Associations

genes associated with the disease p-glycoprotein in GWAS and other genetic association datasets from the GAD Gene-Disease Associations dataset.

From GAD Gene-Disease Associations

genes associated with the disease p-glycoprotein expression, placental in GWAS and other genetic association datasets from the GAD Gene-Disease Associations dataset.

From GeneRIF Biological Term Annotations

genes co-occuring with the biological term glycoprotein in literature-supported statements describing functions of genes from the GeneRIF Biological Term Annotations dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation of glycoprotein metabolic process biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation by host of viral glycoprotein metabolic process biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the glycoprotein transport biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the modulation by host of viral glycoprotein metabolic process biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the glycoprotein metabolic process biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the positive regulation of glycoprotein biosynthetic process biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of glycoprotein biosynthetic process biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation of glycoprotein biosynthetic process biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the glycoprotein biosynthetic process biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of glycoprotein metabolic process biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the glycoprotein catabolic process biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the positive regulation of glycoprotein biosynthetic process involved in immunological synapse formation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the positive regulation of glycoprotein metabolic process biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the n-acetyl-beta-glucosaminyl-glycoprotein 4-beta-n-acetylgalactosaminyltransferase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the glycoprotein-fucosylgalactoside alpha-n-acetylgalactosaminyltransferase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the glycoprotein-n-acetylgalactosamine 3-beta-galactosyltransferase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the mannosyl-glycoprotein endo-beta-n-acetylglucosaminidase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the beta-1,3-galactosyl-o-glycosyl-glycoprotein beta-1,6-n-acetylglucosaminyltransferase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the udp-glucose:glycoprotein glucosyltransferase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the glycoprotein transporter activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the glycoprotein binding molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the acetylgalactosaminyl-o-glycosyl-glycoprotein beta-1,6-n-acetylglucosaminyltransferase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the glycoprotein endo-alpha-1,2-mannosidase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the beta-1,3-galactosyl-o-glycosyl-glycoprotein beta-1,3-n-acetylglucosaminyltransferase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the glycoprotein 6-alpha-l-fucosyltransferase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GWAS Catalog SNP-Phenotype Associations

genes associated with the β2-Glycoprotein I (β2-GPI) plasma levels phenotype in GWAS datasets from the GWAS Catalog SNP-Phenotype Associations dataset.

From GWASdb SNP-Phenotype Associations

genes associated with the abnormality of glycoprotein metabolism phenotype in GWAS datasets from the GWASdb SNP-Phenotype Associations dataset.

From HPO Gene-Disease Associations

genes associated with the abnormality of glycoprotein metabolism phenotype by mapping known disease genes to disease phenotypes from the HPO Gene-Disease Associations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Lipid-binding serum glycoprotein, conserved site protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the T-cell surface glycoprotein CD3 zeta/eta subunit/High affinity IgE receptor gamma subunit protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Amyloidogenic glycoprotein, E2 domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Neurogenesis glycoprotein protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Amyloidogenic glycoprotein, extracellular domain conserved site protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Glycoprotein phospholipase D protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Lysosome-associated membrane glycoprotein protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Myelin-oligodendrocyte glycoprotein protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Lipid-binding serum glycoprotein, C-terminal protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Lipid-binding serum glycoprotein, N-terminal protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the UDP-glucose:Glycoprotein Glucosyltransferase protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Lysosome-associated membrane glycoprotein, conserved site protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Amyloidogenic glycoprotein protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Mitochondrial glycoprotein protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Amyloidogenic glycoprotein, heparin-binding protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Beta-2-glycoprotein-1 fifth domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Glycoprotein hormone subunit beta, cystine knot protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Amyloidogenic glycoprotein, extracellular protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Amyloidogenic glycoprotein, copper-binding protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the T-cell surface glycoprotein CD3 zeta/eta subunit protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Glycoprotein hormone alpha chain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Glycoprotein hormone receptor family protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the T-cell surface glycoprotein CD5 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Amyloidogenic glycoprotein, amyloid-beta peptide protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Kell blood group glycoprotein protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Alpha-1B-glycoprotein/leukocyte immunoglobulin-like receptor protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the CD59 glycoprotein protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the P-selectin glycoprotein ligand 1 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Amyloidogenic glycoprotein, intracellular domain, conserved site protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Microfibril-associated glycoprotein protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Alpha-1-acid glycoprotein protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From OMIM Gene-Disease Associations

genes associated with the ?glycoprotein ia deficiency phenotype from the curated OMIM Gene-Disease Associations dataset.

From Reactome Pathways 2014

proteins participating in the Glycoprotein hormones pathway from the Reactome Pathways dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Carbohydrate Deficient Glycoprotein Syndrome Type 1O in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Glycoprotein Vi Deficiency in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Glycoprotein Ia Deficiency in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Glycoprotein Storage Disease in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Carbohydrate Deficient Glycoprotein Syndrome Type 2K in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From GO Biological Process Annotations 2023

genes participating in the glycoprotein catabolic process biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the positive regulation of glycoprotein biosynthetic process biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the glycoprotein metabolic process biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the glycoprotein biosynthetic process biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the negative regulation by host of viral glycoprotein metabolic process biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the negative regulation of glycoprotein metabolic process biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the regulation of glycoprotein biosynthetic process biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the cellular response to glycoprotein biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the positive regulation of glycoprotein biosynthetic process involved in immunological synapse formation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the mannose trimming involved in glycoprotein ERAD pathway biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the glycoprotein transport biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the positive regulation of glycoprotein metabolic process biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the ubiquitin-dependent glycoprotein ERAD pathway biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the negative regulation of glycoprotein biosynthetic process biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the modulation by host of viral glycoprotein metabolic process biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the regulation of glycoprotein metabolic process biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the response to glycoprotein biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the protein deglycosylation involved in glycoprotein catabolic process biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the cell wall glycoprotein biosynthetic process biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the glycoprotein endo-alpha-1,2-mannosidase activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the glycoprotein 6-alpha-L-fucosyltransferase activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the UDP-glucose:glycoprotein glucosyltransferase activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From Reactome Pathways 2024

proteins participating in the Glycoprotein hormones pathway from the Reactome Pathways 2024 dataset.

From GO Biological Process Annotations 2025

genes participating in the glycoprotein catabolic process biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the positive regulation of glycoprotein biosynthetic process biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the glycoprotein metabolic process biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the glycoprotein biosynthetic process biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the negative regulation by host of viral glycoprotein metabolic process biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the negative regulation of glycoprotein metabolic process biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the regulation of glycoprotein biosynthetic process biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the cellular response to glycoprotein biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the positive regulation of glycoprotein biosynthetic process involved in immunological synapse formation biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the mannose trimming involved in glycoprotein ERAD pathway biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the glycoprotein transport biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the positive regulation of glycoprotein metabolic process biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the ubiquitin-dependent glycoprotein ERAD pathway biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the negative regulation of glycoprotein biosynthetic process biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the modulation by host of viral glycoprotein metabolic process biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the regulation of glycoprotein metabolic process biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the response to glycoprotein biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the protein deglycosylation involved in glycoprotein catabolic process biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the glycoprotein endo-alpha-1,2-mannosidase activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the glycoprotein 6-alpha-L-fucosyltransferase activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the UDP-glucose:glycoprotein glucosyltransferase activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Glycoprotein network cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Glycoprotein storage disease phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From GWAS Catalog SNP-Phenotype Associations 2025

genes associated with the β2-Glycoprotein I (β2-GPI) plasma levels phenotype in GWAS datasets from the GWAS Catalog SNP-Phenotype Associations 2025 dataset.

From DGIdb Drug Targets 2026

interacting proteins for the KLEBSIELLA PNEUMONIAE GLYCOPROTEIN drug from theDGIdb Drug Targets 2026 dataset.

From DGIdb Drug Targets 2026

interacting proteins for the VARICELLA ZOSTER VIRUS ENVELOPE GLYCOPROTEIN E drug from theDGIdb Drug Targets 2026 dataset.

From DGIdb Drug Targets 2026

interacting proteins for the VACCINIA VIRUS, MODIFIED ENCODING EBOLA VIRUS GLYCOPROTEIN AND NUCLEOPROTEIN drug from theDGIdb Drug Targets 2026 dataset.

From DGIdb Drug Targets 2026

interacting proteins for the ADENOVIRUS TYPE 26 ENCODING EBOLA VIRUS GLYCOPROTEIN drug from theDGIdb Drug Targets 2026 dataset.

From DGIdb Drug Targets 2026

interacting proteins for the VESICULAR STOMATITIS VIRUS ENCODING EBOLA VIRUS GLYCOPROTEIN drug from theDGIdb Drug Targets 2026 dataset.

From Biocarta Pathways

proteins participating in the integrin signaling pathway pathway from the Biocarta Pathways dataset.

From CTD Gene-Disease Associations

genes/proteins associated with the disease Muscular Dystrophy, Congenital, Due To Integrin Alpha-7 Deficiency from the curated CTD Gene-Disease Associations dataset.

From GeneRIF Biological Term Annotations

genes co-occuring with the biological term integrin in literature-supported statements describing functions of genes from the GeneRIF Biological Term Annotations dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of integrin-mediated signaling pathway biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the integrin activation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the cell adhesion mediated by integrin biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the positive regulation of integrin biosynthetic process biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of integrin activation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of cell-cell adhesion mediated by integrin biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the integrin biosynthetic process biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the cell-cell adhesion mediated by integrin biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the positive regulation of cell-cell adhesion mediated by integrin biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation of integrin biosynthetic process biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the positive regulation of integrin activation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the positive regulation of cell adhesion mediated by integrin biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the integrin-mediated signaling pathway biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the positive regulation of integrin-mediated signaling pathway biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of integrin biosynthetic process biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation of cell adhesion mediated by integrin biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of cell adhesion mediated by integrin biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation of integrin activation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation of integrin-mediated signaling pathway biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the integrin binding molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the integrin binding involved in cell-matrix adhesion molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Integrin beta subunit protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Integrin beta subunit, cytoplasmic domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Integrin beta-like protein 1 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Integrin alpha-2 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Integrin beta-1 subunit protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Integrin beta-2 subunit protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Integrin alpha chain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Integrin beta-7 subunit protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Integrin beta-8 subunit protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Integrin binding protein, ICAP-1 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Integrin-linked protein kinase protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Integrin beta-6 subunit protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Integrin beta subunit, N-terminal protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Na-Ca exchanger/integrin-beta4 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Integrin beta-4 subunit protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Integrin beta subunit, tail protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Integrin beta-5 subunit protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Integrin beta-3 subunit protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Integrin alpha beta-propellor protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Integrin alpha chain, C-terminal cytoplasmic region, conserved site protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From PANTHER Pathways

proteins participating in the Integrin signalling pathway pathway from the PANTHER Pathways dataset.

From Phosphosite Textmining Biological Term Annotations

proteins co-occuring with the biological term integrin in abstracts of publications describing phosphosites from the Phosphosite Textmining Biological Term Annotations dataset.

From PID Pathways

proteins participating in the Beta5 beta6 beta7 and beta8 integrin cell surface interactions pathway from the PID Pathways dataset.

From PID Pathways

proteins participating in the Integrin family cell surface interactions pathway from the PID Pathways dataset.

From PID Pathways

proteins participating in the a4b7 Integrin signaling pathway from the PID Pathways dataset.

From PID Pathways

proteins participating in the Beta2 integrin cell surface interactions pathway from the PID Pathways dataset.

From PID Pathways

proteins participating in the Integrin-linked kinase signaling pathway from the PID Pathways dataset.

From PID Pathways

proteins participating in the a6b1 and a6b4 Integrin signaling pathway from the PID Pathways dataset.

From PID Pathways

proteins participating in the Alpha6 beta4 integrin-ligand interactions pathway from the PID Pathways dataset.

From PID Pathways

proteins participating in the Alpha4 beta1 integrin signaling events pathway from the PID Pathways dataset.

From PID Pathways

proteins participating in the amb2 Integrin signaling pathway from the PID Pathways dataset.

From PID Pathways

proteins participating in the Beta1 integrin cell surface interactions pathway from the PID Pathways dataset.

From PID Pathways

proteins participating in the Alpha9 beta1 integrin signaling events pathway from the PID Pathways dataset.

From PID Pathways

proteins participating in the AlphaE beta7 integrin cell surface interactions pathway from the PID Pathways dataset.

From Reactome Pathways 2014

proteins participating in the Non-integrin membrane-ECM interactions pathway from the Reactome Pathways dataset.

From Reactome Pathways 2014

proteins participating in the Integrin cell surface interactions pathway from the Reactome Pathways dataset.

From Reactome Pathways 2014

proteins participating in the SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion pathway from the Reactome Pathways dataset.

From WikiPathways Pathways 2014

proteins participating in the Integrin-mediated Cell Adhesion(Homo sapiens) pathway from the WikiPathways Pathways 2014 dataset.

From WikiPathways Pathways 2014

proteins participating in the Integrin-mediated Cell Adhesion(Mus musculus) pathway from the WikiPathways Pathways 2014 dataset.

From WikiPathways Pathways 2014

proteins participating in the Alpha6-Beta4 Integrin Signaling Pathway(Mus musculus) pathway from the WikiPathways Pathways 2014 dataset.

From GO Biological Process Annotations 2023

genes participating in the integrin activation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the positive regulation of cell adhesion mediated by integrin biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the positive regulation of cell-cell adhesion mediated by integrin biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the integrin-mediated signaling pathway biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the cell-cell adhesion mediated by integrin biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the regulation of cell adhesion mediated by integrin biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the regulation of integrin-mediated signaling pathway biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the negative regulation of cell adhesion mediated by integrin biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the positive regulation of integrin activation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the regulation of integrin activation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the negative regulation of integrin-mediated signaling pathway biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the regulation of cell-cell adhesion mediated by integrin biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the positive regulation of integrin-mediated signaling pathway biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the negative regulation of integrin biosynthetic process biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the positive regulation of integrin biosynthetic process biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the integrin biosynthetic process biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the negative regulation of integrin activation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the positive regulation of integrin activation by cell surface receptor linked signal transduction biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the negative regulation of cell-cell adhesion mediated by integrin biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the regulation of integrin biosynthetic process biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the integrin binding involved in cell-matrix adhesion molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From WikiPathways Pathways 2024

proteins participating in the Integrin mediated cell adhesion pathway from the WikiPathways Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Integrin cell surface interactions pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Integrin signaling pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Non-integrin membrane-ECM interactions pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion pathway from the Reactome Pathways 2024 dataset.

From GO Biological Process Annotations 2025

genes participating in the integrin activation biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the positive regulation of cell adhesion mediated by integrin biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the positive regulation of cell-cell adhesion mediated by integrin biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the integrin-mediated signaling pathway biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the cell-cell adhesion mediated by integrin biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the regulation of cell adhesion mediated by integrin biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the regulation of integrin-mediated signaling pathway biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the negative regulation of cell adhesion mediated by integrin biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the positive regulation of integrin activation biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the regulation of integrin activation biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the negative regulation of integrin-mediated signaling pathway biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the regulation of cell-cell adhesion mediated by integrin biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the positive regulation of integrin-mediated signaling pathway biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the negative regulation of integrin biosynthetic process biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the positive regulation of integrin biosynthetic process biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the integrin biosynthetic process biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the negative regulation of integrin activation biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the positive regulation of integrin activation by cell surface receptor linked signal transduction biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the negative regulation of cell-cell adhesion mediated by integrin biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the regulation of integrin biosynthetic process biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the integrin binding involved in cell-matrix adhesion molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From DISEASES Text-mining Gene-Disease Association Evidence Scores 2025

genes co-occuring with the disease Congenital muscular dystrophy due to integrin alpha-7 deficiency in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Congenital muscular dystrophy due to integrin alpha-7 deficiency phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From KEGG Pathways 2026

proteins participating in the Integrin signaling pathway from the KEGG Pathways 2026 dataset.

From DGIdb Drug Targets 2026

interacting proteins for the INTEGRIN RECEPTOR ANTAGONIST GLPG0187 drug from theDGIdb Drug Targets 2026 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the proteasome core complex, alpha-subunit complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the tho complex part of transcription export complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the light-harvesting complex, core complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the light-harvesting complex, peripheral complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From CORUM Protein Complexes

proteins in the ORC 2-5 complex (origin recognition 2-5 complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the ORC 1-5 complex (origin recognition 1-5 complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the MRN complex (MRE11-RAD50-NBS1 complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the Exon junction complex (EIF4A3-MLN51-MAGOH-Y14), RNA-protein complex protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the PHAX-CBC complex (cap binding complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the RFC complex (activator A 1 complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the NRD complex (Nucleosome remodeling and deacetylation complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the TFTC complex (TATA-binding protein-free TAF-II-containing complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the hs4 enhancer complex (slow migrating complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the CF IIAm complex (Cleavage factor IIAm complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the NELF complex (Negative elongation factor complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the NUMAC complex (nucleosomal methylation activator complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the PBAF complex (Polybromo- and BAF containing complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the Exon junction complex, EIF4A3-MLN51-MAGOH-Y14 (RNA-protein complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the FA core complex (Fanconi anemia core complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the STAGA core complex (SPT3-TAF9-GCN5 acetyltransferase complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the RNA polymerase II complex, incomplete (CDK8 complex), chromatin structure modifying protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the RC complex (Replication competent complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the R/M complex (RAD50-MRE11 complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the hs4 enhancer complex (faster migrating complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the MRN complex (MRE11-RAD50-NBN complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the CRM1-RAN-PHAX-CBC complex (cap binding complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the DJ-1-SNCA complex, high molecular weight complex protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the ORC complex (origin recognition complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the BASC (Ab 80) complex (BRCA1-associated genome surveillance complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the DNA ligase IV-XRCC4 complex (LX complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the Cdk5/p35 complex (Cdk5-Cdk5r1 complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the Nucleolar remodeling complex (NoRC complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the SAP complex (Sin3-associated protein complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the FA core complex 1 (Fanconi anemia core complex 1) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the STAGA complex (SPT3-TAF9-GCN5 acetyltransferase complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the DSIF complex (DRB sensitivity-inducing factor complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the TLE1 corepressor complex (MASH1 promoter-corepressor complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the CCT complex (chaperonin containing TCP1 complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the MRN-TRRAP complex (MRE11A-RAD50-NBN-TRRAP complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the LARC complex (LCR-associated remodeling complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the CERF complex (CECR2-containing remodeling factor complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the FA complex (Fanconi anemia complex), cytoplasmic protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the CCT complex (chaperonin containing TCP1 complex), testis specific protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the FA complex (Fanconi anemia complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the BASC (Ab C-20) complex (BRCA1-associated genome surveillance complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the CAK complex (Cdk-activating kinase complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the Chromatin assembly complex (CAF-1 complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the CAK core complex (Cdk-activating kinase core complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the CBC complex (cap binding complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the BASC (Ab 81) complex (BRCA1-associated genome surveillance complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the ORC 2-4 complex (origin recognition 2-4 complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the BASC complex (BRCA1-associated genome surveillance complex) protein complex from the CORUM Protein Complexes dataset.

From CTD Gene-Disease Associations

genes/proteins associated with the disease MITOCHONDRIAL COMPLEX V (ATP SYNTHASE) DEFICIENCY, NUCLEAR TYPE 1;MC5DN1 MITOCHONDRIAL COMPLEX V (ATP SYNTHASE) DEFICIENCY, ATPAF2 TYPE from the curated CTD Gene-Disease Associations dataset.

From GAD Gene-Disease Associations

genes associated with the disease aids dementia complex; aids related dementia complex in GWAS and other genetic association datasets from the GAD Gene-Disease Associations dataset.

From GAD Gene-Disease Associations

genes associated with the disease acquired immunodeficiency syndrome; aids dementia complex; aids related dementia complex; disease progression in GWAS and other genetic association datasets from the GAD Gene-Disease Associations dataset.

From GO Cellular Component Annotations 2015

proteins localized to the proteasome core complex, alpha-subunit complex cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the tho complex part of transcription export complex cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the electron transporter, transferring electrons from coqh2-cytochrome c reductase complex and cytochrome c oxidase complex activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the ATPase, F1 complex beta subunit/V1 complex, C-terminal protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From Reactome Pathways 2014

proteins participating in the Formation of the ternary complex, and subsequently, the 43S complex pathway from the Reactome Pathways dataset.

From GO Cellular Component Annotations 2023

proteins localized to the mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone) cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the THO complex part of transcription export complex cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the core TFIIH complex portion of holo TFIIH complex cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From Reactome Pathways 2024

proteins participating in the Formation of the ternary complex, and subsequently, the 43S complex pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the TRAF6-mediated induction of TAK1 complex within TLR4 complex pathway from the Reactome Pathways 2024 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the THO complex part of transcription export complex cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the core TFIIH complex portion of holo TFIIH complex cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the THO complex part of transcription export complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Core TFIIH complex portion of holo TFIIH complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Proteasome core complex, alpha-subunit complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Proteasome core complex, beta-subunit complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone) cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the light-harvesting complex, peripheral complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the light-harvesting complex, core complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Proteasome core complex, beta-subunit complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the THO complex part of transcription export complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Proteasome core complex, alpha-subunit complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles

genes with high or low expression in oculomotor nuclear complex, left relative to other tissues from the Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles

genes with high or low expression in medial geniculate complex, left relative to other tissues from the Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles

genes with high or low expression in superior olivary complex, right relative to other tissues from the Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles

genes with high or low expression in inferior olivary complex, left relative to other tissues from the Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles

genes with high or low expression in superior olivary complex, left relative to other tissues from the Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles

genes with high or low expression in inferior olivary complex, right relative to other tissues from the Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles

genes with high or low expression in medial geniculate complex, right relative to other tissues from the Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles

genes with high or low expression in oculomotor nuclear complex, right relative to other tissues from the Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles

genes with high or low expression in Ventral posterior complex of the thalamus relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles

genes with high or low expression in Superior olivary complex, medial part relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles

genes with high or low expression in Ventral part of the lateral geniculate complex relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles

genes with high or low expression in Lateral septal complex relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles

genes with high or low expression in Medial geniculate complex, medial part relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles

genes with high or low expression in zona incerta complex relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles

genes with high or low expression in Superior olivary complex relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles

genes with high or low expression in reticular complex relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles

genes with high or low expression in Ventral anterior-lateral complex of the thalamus relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles

genes with high or low expression in pallidum (globus pallidus complex) relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles

genes with high or low expression in r6 (gustatory) part of solitary complex relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles

genes with high or low expression in Medial septal complex relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles

genes with high or low expression in r5 (gustatory) part of solitary complex relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles

genes with high or low expression in Posterior complex of the thalamus relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles

genes with high or low expression in r8 (gustatory) part of solitary complex relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles

genes with high or low expression in Inferior olivary complex relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles

genes with high or low expression in Superior olivary complex, periolivary region relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles

genes with high or low expression in Medial geniculate complex, dorsal part relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles

genes with high or low expression in r7 (gustatory) part of solitary complex relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles

genes with high or low expression in Superior olivary complex, lateral part relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles

genes with high or low expression in r10 part of solitary complex relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles

genes with high or low expression in Intergeniculate leaflet of the lateral geniculate complex relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles

genes with high or low expression in Medial geniculate complex, ventral part relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles

genes with high or low expression in r9 (gustatory) part of solitary complex relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles

genes with high or low expression in parabrachial complex relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles

genes with high or low expression in Medial geniculate complex relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles

genes with high or low expression in Dorsal part of the lateral geniculate complex relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles

genes with high or low expression in pretectal nuclear complex relative to other tissues from the Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles

genes with high or low expression in midline nuclear complex relative to other tissues from the Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles dataset.

From Biocarta Pathways

proteins participating in the the prc2 complex sets long-term gene silencing through modification of histone tails pathway from the Biocarta Pathways dataset.

From Biocarta Pathways

proteins participating in the proteasome complex pathway from the Biocarta Pathways dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Fibular hypoplasia and complex brachydactyly phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Mitochondrial complex I deficiency phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Nuclearly-encoded mitochondrial complex V (ATP synthase) deficiency 1 phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Nuclearly-encoded mitochondrial complex V (ATP synthase) deficiency 2 phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Mitochondrial complex III deficiency phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Mitochondrial complex III deficiency, nuclear type 5 phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Mitochondrial complex III deficiency, nuclear type 2 phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Leigh syndrome due to mitochondrial complex I deficiency phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the MITOCHONDRIAL COMPLEX III DEFICIENCY, NUCLEAR TYPE 7 phenotype from the curated ClinVar Gene-Phenotype Associations dataset.