Harmonizome 3.0

matrix extracellular phosphoglycoprotein

This gene encodes a secreted calcium-binding phosphoprotein that belongs to the small integrin-binding ligand, N-linked glycoprotein (SIBLING) family of proteins. Members of this family are components of the extracellular matrix of bone and dentin and regulate bone mineralization. Deficiency of a similar protein in mouse results in increased bone mass. Mice lacking this gene are resistant to aging-related trabecular bone loss. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Mar 2014]

extracellular matrix protein 2-like

extracellular matrix protein 2-like

superoxide dismutase 3, extracellular

This gene encodes a member of the superoxide dismutase (SOD) protein family. SODs are antioxidant enzymes that catalyze the conversion of superoxide radicals into hydrogen peroxide and oxygen, which may protect the brain, lungs, and other tissues from oxidative stress. Proteolytic processing of the encoded protein results in the formation of two distinct homotetramers that differ in their ability to interact with the extracellular matrix (ECM). Homotetramers consisting of the intact protein, or type C subunit, exhibit high affinity for heparin and are anchored to the ECM. Homotetramers consisting of a proteolytically cleaved form of the protein, or type A subunit, exhibit low affinity for heparin and do not interact with the ECM. A mutation in this gene may be associated with increased heart disease risk. [provided by RefSeq, Oct 2015]

extracellular matrix protein 1 pseudogene 1

extracellular matrix protein 2, female organ and adipocyte specific

ECM2 encodes extracellular matrix protein 2, so named because it shares extensive similarity with known extracelluar matrix proteins. Three transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Oct 2010]

extracellular matrix protein 1

This gene encodes a soluble protein that is involved in endochondral bone formation, angiogenesis, and tumor biology. It also interacts with a variety of extracellular and structural proteins, contributing to the maintenance of skin integrity and homeostasis. Mutations in this gene are associated with lipoid proteinosis disorder (also known as hyalinosis cutis et mucosae or Urbach-Wiethe disease) that is characterized by generalized thickening of skin, mucosae and certain viscera. Alternatively spliced transcript variants encoding distinct isoforms have been described for this gene. [provided by RefSeq, Feb 2011]

spondin 2, extracellular matrix protein

Predicted to enable antigen binding activity; lipopolysaccharide binding activity; and metal ion binding activity. Predicted to be involved in cell adhesion. Predicted to act upstream of or within several processes, including defense response to other organism; opsonization; and positive regulation of cytokine production. Located in extracellular exosome. Biomarker of meningioma. [provided by Alliance of Genome Resources, Mar 2025]

spondin 1, extracellular matrix protein

Predicted to enable LBD domain binding activity and metal ion binding activity. Predicted to be an extracellular matrix structural constituent. Predicted to be involved in cell adhesion. Predicted to act upstream of or within negative regulation of amyloid-beta formation; positive regulation of amyloid precursor protein catabolic process; and positive regulation of protein processing. Located in collagen-containing extracellular matrix and extracellular space. [provided by Alliance of Genome Resources, Mar 2025]

FRAS1 related extracellular matrix 3

This gene encodes an integral membrane protein containing numerous CSPG (chondroitin sulfate proteoglycan element) repeats and Calx-beta domains. The protein belongs to the family of FRAS1/FREM extracellular matrix proteins and may play a role cell adhesion. [provided by RefSeq, Feb 2017]

FRAS1 related extracellular matrix protein 2

This gene encodes an integral membrane protein containing numerous CSPG (chondroitin sulfate proteoglycan element) repeats and Calx-beta domains. The encoded protein localizes to the basement membrane, forming a ternary complex that plays a role in epidermal-dermal interactions. This protein is important for the integrity of skin and renal epithelia. Mutations in this gene are associated with Fraser syndrome. [provided by RefSeq, Apr 2014]

FRAS1 related extracellular matrix 1

This gene encodes a basement membrane protein that may play a role in craniofacial and renal development. Mutations in this gene have been associated with bifid nose with or without anorectal and renal anomalies. Alternatively spliced transcript variants encoding different isoforms have been described. PubMed ID 19940113 describes one such variant that initiates transcription within a distinct, internal exon; the resulting shorter isoform (named Toll-like/interleukin-1 receptor regulator, TILRR) is suggested to be a co-receptor of the interleukin 1 receptor family and may regulate receptor function and Toll-like receptor/interleukin 1 receptor signal transduction, contributing to the control of inflammatory response activation. [provided by RefSeq, Apr 2011]

Fraser extracellular matrix complex subunit 1

This gene encodes an extracellular matrix protein that appears to function in the regulation of epidermal-basement membrane adhesion and organogenesis during development. Mutations in this gene cause Fraser syndrome, a multisystem malformation that can include craniofacial, urogenital and respiratory system abnormalities. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Oct 2009]

glycine rich extracellular protein 1

collagen alpha-1(III) chain-like

collagen alpha-2(I) chain-like

collagen, type XIV, alpha 1

This gene encodes the alpha chain of type XIV collagen, a member of the FACIT (fibril-associated collagens with interrupted triple helices) collagen family. Type XIV collagen interacts with the fibril surface and is involved in the regulation of fibrillogenesis. [provided by RefSeq, Jan 2013]

collagen alpha-1(I) chain-like

collagen alpha-2(I) chain-like

collagen, type XXVII, alpha 1

This gene encodes a member of the fibrillar collagen family, and plays a role during the calcification of cartilage and the transition of cartilage to bone. The encoded protein product is a preproprotein. It includes an N-terminal signal peptide, which is followed by an N-terminal propetide, mature peptide and a C-terminal propeptide. The N-terminal propeptide contains thrombospondin N-terminal-like and laminin G-like domains. The mature peptide is a major triple-helical region. The C-terminal propeptide, also known as COLFI domain, plays crucial roles in tissue growth and repair. Mutations in this gene cause Steel syndrome. Alternatively spliced transcript variants have been found, but the full-length nature of some variants has not been determined. [provided by RefSeq, Sep 2014]

collagen alpha-1(I) chain-like

collagen, type IX, alpha 2

This gene encodes one of the three alpha chains of type IX collagen, the major collagen component of hyaline cartilage. Type IX collagen, a heterotrimeric molecule, is usually found in tissues containing type II collagen, a fibrillar collagen. This chain is unusual in that, unlike the other two type IX alpha chains, it contains a covalently attached glycosaminoglycan side chain. Mutations in this gene are associated with multiple epiphyseal dysplasia. [provided by RefSeq, Jul 2008]

collagen, type IX, alpha 3

This gene encodes one of the three alpha chains of type IX collagen, the major collagen component of hyaline cartilage. Type IX collagen, a heterotrimeric molecule, is usually found in tissues containing type II collagen, a fibrillar collagen. Mutations in this gene are associated with multiple epiphyseal dysplasia type 3. [provided by RefSeq, Jan 2010]

collagen, type IX, alpha 1

This gene encodes one of the three alpha chains of type IX collagen, which is a minor (5-20%) collagen component of hyaline cartilage. Type IX collagen is usually found in tissues containing type II collagen, a fibrillar collagen. Studies in knockout mice have shown that synthesis of the alpha 1 chain is essential for assembly of type IX collagen molecules, a heterotrimeric molecule, and that lack of type IX collagen is associated with early onset osteoarthritis. Mutations in this gene are associated with osteoarthritis in humans, with multiple epiphyseal dysplasia, 6, a form of chondrodysplasia, and with Stickler syndrome, a disease characterized by ophthalmic, orofacial, articular, and auditory defects. Two transcript variants that encode different isoforms have been identified for this gene. [provided by RefSeq, Jul 2008]

collagen, type XXII, alpha 1 pseudogene

collagen alpha-3(IX) chain-like

collagen, type I, alpha, receptor

collagen, type I, alpha 2

This gene encodes the pro-alpha2 chain of type I collagen whose triple helix comprises two alpha1 chains and one alpha2 chain. Type I is a fibril-forming collagen found in most connective tissues and is abundant in bone, cornea, dermis and tendon. Mutations in this gene are associated with osteogenesis imperfecta types I-IV, Ehlers-Danlos syndrome type VIIB, recessive Ehlers-Danlos syndrome Classical type, idiopathic osteoporosis, and atypical Marfan syndrome. Symptoms associated with mutations in this gene, however, tend to be less severe than mutations in the gene for the alpha1 chain of type I collagen (COL1A1) reflecting the different role of alpha2 chains in matrix integrity. Three transcripts, resulting from the use of alternate polyadenylation signals, have been identified for this gene. [provided by R. Dalgleish, Feb 2008]

collagen alpha-1(XXVII) chain-like

collagen, type VI, alpha 1

The collagens are a superfamily of proteins that play a role in maintaining the integrity of various tissues. Collagens are extracellular matrix proteins and have a triple-helical domain as their common structural element. Collagen VI is a major structural component of microfibrils. The basic structural unit of collagen VI is a heterotrimer of the alpha1(VI), alpha2(VI), and alpha3(VI) chains. The alpha2(VI) and alpha3(VI) chains are encoded by the COL6A2 and COL6A3 genes, respectively. The protein encoded by this gene is the alpha 1 subunit of type VI collagen (alpha1(VI) chain). Mutations in the genes that code for the collagen VI subunits result in the autosomal dominant disorder, Bethlem myopathy. [provided by RefSeq, Jul 2008]

collagen, type VI, alpha 2

This gene encodes one of the three alpha chains of type VI collagen, a beaded filament collagen found in most connective tissues. The product of this gene contains several domains similar to von Willebrand Factor type A domains. These domains have been shown to bind extracellular matrix proteins, an interaction that explains the importance of this collagen in organizing matrix components. Mutations in this gene are associated with Bethlem myopathy and Ullrich scleroatonic muscular dystrophy. Three transcript variants have been identified for this gene. [provided by RefSeq, Jul 2008]

collagen, type VI, alpha 5

This gene encodes a member of the collagen superfamily of proteins. The encoded protein contains multiple von Willebrand factor A-like domains and may interact with the alpha 1 and alpha 2 chains of collagen VI to form the complete collagen VI trimer. Polymorphisms in this gene may be linked to dermal phenotypes, such as eczema. Alternative splicing results in multiple transcript variants. [provided by RefSeq, May 2013]

collagen alpha-2(I) chain-like

fibril-forming collagen alpha chain-like

collagen, type XVII, alpha 1

This gene encodes the alpha chain of type XVII collagen. Unlike most collagens, collagen XVII is a transmembrane protein. Collagen XVII is a structural component of hemidesmosomes, multiprotein complexes at the dermal-epidermal basement membrane zone that mediate adhesion of keratinocytes to the underlying membrane. Mutations in this gene are associated with both generalized atrophic benign and junctional epidermolysis bullosa. Two homotrimeric forms of type XVII collagen exist. The full length form is the transmembrane protein. A soluble form, referred to as either ectodomain or LAD-1, is generated by proteolytic processing of the full length form. [provided by RefSeq, Jul 2008]

collagen alpha-1(XI) chain-like

collagen alpha-1(III) chain-like

collagen alpha-4(IV) chain-like

collagen alpha-2(VIII) chain-like

collagen alpha-2(I) chain-like

cuticle collagen 7-like

collagen alpha-1(X) chain

collagen alpha-1(I) chain-like

collagen, type XXI, alpha 1

This gene encodes the alpha chain of type XXI collagen, a member of the FACIT (fibril-associated collagens with interrupted helices) collagen family. Type XXI collagen is localized to tissues containing type I collagen and maintains the integrity of the extracellular matrix. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2016]

collagen, type XVIII, alpha 1

This gene encodes the alpha chain of type XVIII collagen. This collagen is one of the multiplexins, extracellular matrix proteins that contain multiple triple-helix domains (collagenous domains) interrupted by non-collagenous domains. A long isoform of the protein has an N-terminal domain that is homologous to the extracellular part of frizzled receptors. Proteolytic processing at several endogenous cleavage sites in the C-terminal domain results in production of endostatin, a potent antiangiogenic protein that is able to inhibit angiogenesis and tumor growth. Mutations in this gene are associated with Knobloch syndrome. The main features of this syndrome involve retinal abnormalities, so type XVIII collagen may play an important role in retinal structure and in neural tube closure. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Dec 2014]

collagen, type XXVIII, alpha 1

COL28A1 belongs to a class of collagens containing von Willebrand factor (VWF; MIM 613160) type A (VWFA) domains (Veit et al., 2006 [PubMed 16330543]).[supplied by OMIM, Nov 2010]

collagen, type XI, alpha 1

This gene encodes one of the two alpha chains of type XI collagen, a minor fibrillar collagen. Type XI collagen is a heterotrimer but the third alpha chain is a post-translationally modified alpha 1 type II chain. Mutations in this gene are associated with type II Stickler syndrome and with Marshall syndrome. A single-nucleotide polymorphism in this gene is also associated with susceptibility to lumbar disc herniation. Multiple transcript variants have been identified for this gene. [provided by RefSeq, Nov 2009]

collagen, type XI, alpha 2

This gene encodes one of the two alpha chains of type XI collagen, a minor fibrillar collagen. It is located on chromosome 6 very close to but separate from the gene for retinoid X receptor beta. Type XI collagen is a heterotrimer but the third alpha chain is a post-translationally modified alpha 1 type II chain. Proteolytic processing of this type XI chain produces PARP, a proline/arginine-rich protein that is an amino terminal domain. Mutations in this gene are associated with type III Stickler syndrome, otospondylomegaepiphyseal dysplasia (OSMED syndrome), Weissenbacher-Zweymuller syndrome, autosomal dominant non-syndromic sensorineural type 13 deafness (DFNA13), and autosomal recessive non-syndromic sensorineural type 53 deafness (DFNB53). Alternative splicing results in multiple transcript variants. A related pseudogene is located nearby on chromosome 6. [provided by RefSeq, Jul 2009]

collagen alpha-2(I) chain-like

collagen alpha-4(IV) chain-like

collagen alpha-1(III) chain-like

collagen, type XXII, alpha 1

This gene encodes member of the collagen family which is thought to contribute to the stabilization of myotendinous junctions and strengthen skeletal muscle attachments during contractile activity. It belongs to the fibril-associated collagens with interrupted triple helix (FACIT) subset of the collagen superfamily, which associate with collagen fibers through their C-terminal collagenous domains and mediate protein-protein interactions through their N-terminal noncollagenous domains. The encoded protein is deposited in the basement membrane zone of the myotendinous junction which is present only at the tissue junctions of muscles, tendons, the heart, articular cartilage, and skin. A knockdown of the orthologous zebrafish gene induces a muscular dystrophy by disruption of the myotendinous junction. [provided by RefSeq, May 2017]

collagen, type V, alpha 2

This gene encodes an alpha chain for one of the low abundance fibrillar collagens. Fibrillar collagen molecules are trimers that can be composed of one or more types of alpha chains. Type V collagen is found in tissues containing type I collagen and appears to regulate the assembly of heterotypic fibers composed of both type I and type V collagen. This gene product is closely related to type XI collagen and it is possible that the collagen chains of types V and XI constitute a single collagen type with tissue-specific chain combinations. Mutations in this gene are associated with Ehlers-Danlos syndrome, types I and II. [provided by RefSeq, Jul 2008]

collagen, type V, alpha 3

This gene encodes an alpha chain for one of the low abundance fibrillar collagens. Fibrillar collagen molecules are trimers that can be composed of one or more types of alpha chains. Type V collagen is found in tissues containing type I collagen and appears to regulate the assembly of heterotypic fibers composed of both type I and type V collagen. This gene product is closely related to type XI collagen and it is possible that the collagen chains of types V and XI constitute a single collagen type with tissue-specific chain combinations. Mutations in this gene are thought to be responsible for the symptoms of a subset of patients with Ehlers-Danlos syndrome type III. Messages of several sizes can be detected in northern blots but sequence information cannot confirm the identity of the shorter messages. [provided by RefSeq, Jul 2008]

collagen, type V, alpha 1

This gene encodes an alpha chain for one of the low abundance fibrillar collagens. Fibrillar collagen molecules are trimers that can be composed of one or more types of alpha chains. Type V collagen is found in tissues containing type I collagen and appears to regulate the assembly of heterotypic fibers composed of both type I and type V collagen. This gene product is closely related to type XI collagen and it is possible that the collagen chains of types V and XI constitute a single collagen type with tissue-specific chain combinations. The encoded procollagen protein occurs commonly as the heterotrimer pro-alpha1(V)-pro-alpha1(V)-pro-alpha2(V). Mutations in this gene are associated with Ehlers-Danlos syndrome, types I and II. Alternative splicing of this gene results in multiple transcript variants. [provided by RefSeq, May 2013]

fibril-forming collagen alpha chain

collagen alpha-1(I) chain-like

collagen, type XII, alpha 1

This gene encodes the alpha chain of type XII collagen, a member of the FACIT (fibril-associated collagens with interrupted triple helices) collagen family. Type XII collagen is a homotrimer found in association with type I collagen, an association that is thought to modify the interactions between collagen I fibrils and the surrounding matrix. Alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq, Jul 2008]

collagen, type VI, alpha 4 pseudogene 1

This transcribed pseudogene represents the 5' end of a presumed ortholog to a mouse gene which encodes a collagen VI alpha 4 chain protein (GeneID 68553). No complete ORF of comparable size to the mouse protein is found in this gene. The predicted protein lacks a signal peptide; however, this truncated collagen polypeptide may have achieved a different function as suggested by PubMed ID: 18622395. Evidence of in vivo translation is incomplete. A large chromosome break separates this pseudogene from the 3' end of the presumed ortholog (COL6A4P2, GeneID 646300) which is located downstream at chromosome 3q21.3. [provided by RefSeq, Jun 2009]

collagen alpha-1(I) chain-like

collagen, type VI, alpha 4 pseudogene 2

This transcribed pseudogene represents the 3' end of a presumed ortholog to a mouse gene which encodes a collagen VI alpha 4 chain protein (GeneID 68553). The predicted ORF contains multiple premature stop codons. A large chromosome break separates this pseudogene from the 5' end of the presumed ortholog (DVWA, GeneID 344875) which is located upstream at chromosome 3p24.3. [provided by RefSeq, Jun 2009]

collagen, type XXV, alpha 1

This gene encodes a brain-specific membrane associated collagen. A product of proteolytic processing of the encoded protein, CLAC (collagenous Alzheimer amyloid plaque component), binds to amyloid beta-peptides found in Alzheimer amyloid plaques but CLAC inhibits rather than facilitates amyloid fibril elongation (PMID: 16300410). A study of over-expression of this collagen in mice, however, found changes in pathology and behavior suggesting that the encoded protein may promote amyloid plaque formation (PMID: 19548013). Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Dec 2011]

collagen, type II, alpha 1

This gene encodes the alpha-1 chain of type II collagen, a fibrillar collagen found in cartilage and the vitreous humor of the eye. Mutations in this gene are associated with achondrogenesis, chondrodysplasia, early onset familial osteoarthritis, SED congenita, Langer-Saldino achondrogenesis, Kniest dysplasia, Stickler syndrome type I, and spondyloepimetaphyseal dysplasia Strudwick type. In addition, defects in processing chondrocalcin, a calcium binding protein that is the C-propeptide of this collagen molecule, are also associated with chondrodysplasia. There are two transcripts identified for this gene. [provided by RefSeq, Jul 2008]

collagen-like tail subunit (single strand of homotrimer) of asymmetric acetylcholinesterase

This gene encodes the subunit of a collagen-like molecule associated with acetylcholinesterase in skeletal muscle. Each molecule is composed of three identical subunits. Each subunit contains a proline-rich attachment domain (PRAD) that binds an acetylcholinesterase tetramer to anchor the catalytic subunit of the enzyme to the basal lamina. Mutations in this gene are associated with endplate acetylcholinesterase deficiency. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]

collagen alpha-1(I) chain-like

collagen, type XV, alpha 1

This gene encodes the alpha chain of type XV collagen, a member of the FACIT collagen family (fibril-associated collagens with interrupted helices). Type XV collagen has a wide tissue distribution but the strongest expression is localized to basement membrane zones so it may function to adhere basement membranes to underlying connective tissue stroma. The proteolytically produced C-terminal fragment of type XV collagen is restin, a potentially antiangiogenic protein that is closely related to endostatin. Mouse studies have shown that collagen XV deficiency is associated with muscle and microvessel deterioration. [provided by RefSeq, May 2013]

collagen alpha-2(I) chain-like

collagen alpha-1(III) chain-like

collagen alpha-1(II) chain-like

collagen alpha-2(IV) chain-like

collagen, type XXVI, alpha 1

This gene encodes a protein containing an emilin domain and two collagen stretches. This gene may be associated with aspirin-intolerant asthma. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Aug 2013]

collagen alpha-3(IX) chain-like

collagen, type VIII, alpha 2

This gene encodes the alpha 2 chain of type VIII collagen. This protein is a major component of the basement membrane of the corneal endothelium and forms homo- or heterotrimers with alpha 1 (VIII) type collagens. Defects in this gene are associated with Fuchs endothelial corneal dystrophy and posterior polymorphous corneal dystrophy type 2. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jun 2014]

collagen, type VIII, alpha 1

This gene encodes one of the two alpha chains of type VIII collagen. The gene product is a short chain collagen and a major component of the basement membrane of the corneal endothelium. The type VIII collagen fibril can be either a homo- or a heterotrimer. Alternatively spliced transcript variants encoding the same protein have been observed. [provided by RefSeq, Dec 2011]

collagen, type XVI, alpha 1

This gene encodes the alpha chain of type XVI collagen, a member of the FACIT collagen family (fibril-associated collagens with interrupted helices). Members of this collagen family are found in association with fibril-forming collagens such as type I and II, and serve to maintain the integrity of the extracellular matrix. High levels of type XVI collagen have been found in fibroblasts and keratinocytes, and in smooth muscle and amnion. [provided by RefSeq, Jul 2008]

collagen alpha-1(III) chain-like

collagen and calcium binding EGF domains 1

This gene is thought to function in extracellular matrix remodeling and migration. It is predominantly expressed in the ovary, but down regulated in ovarian cancer cell lines and primary carcinomas, suggesting its role as a tumour suppressor. Mutations in this gene have been associated with Hennekam lymphangiectasia-lymphedema syndrome, a generalized lymphatic dysplasia in humans. [provided by RefSeq, Mar 2010]

collagen beta(1-O)galactosyltransferase 2

Predicted to enable procollagen galactosyltransferase activity. Predicted to be involved in collagen fibril organization. Predicted to be located in endoplasmic reticulum lumen. [provided by Alliance of Genome Resources, Mar 2025]

collagen beta(1-O)galactosyltransferase 1

The protein encoded by this gene is one of two enzymes that transfers galactose moieties to hydroxylysine residues of collagen and mannose binding lectin. This gene is constitutively expressed and encodes a soluble protein that localizes to the endoplasmic reticulum. [provided by RefSeq, Dec 2015]

collagen alpha-1(I) chain-like

collagen alpha-1(III) chain-like

collagen alpha-1(II) chain-like

collagen alpha-1(III) chain-like

collagen alpha-1(I) chain-like

collagen, type XX, alpha 1

Predicted to be located in endoplasmic reticulum lumen and extracellular region. Predicted to be part of collagen trimer. Predicted to be active in collagen-containing extracellular matrix. [provided by Alliance of Genome Resources, Mar 2025]

serpin peptidase inhibitor, clade H (heat shock protein 47), member 1, (collagen binding protein 1)

This gene encodes a member of the serpin superfamily of serine proteinase inhibitors. The encoded protein is localized to the endoplasmic reticulum and plays a role in collagen biosynthesis as a collagen-specific molecular chaperone. Autoantibodies to the encoded protein have been found in patients with rheumatoid arthritis. Expression of this gene may be a marker for cancer, and nucleotide polymorphisms in this gene may be associated with preterm birth caused by preterm premature rupture of membranes. Alternatively spliced transcript variants have been observed for this gene, and a pseudogene of this gene is located on the short arm of chromosome 9. [provided by RefSeq, May 2011]

collagen, type VII, alpha 1

This gene encodes the alpha chain of type VII collagen. The type VII collagen fibril, composed of three identical alpha collagen chains, is restricted to the basement zone beneath stratified squamous epithelia. It functions as an anchoring fibril between the external epithelia and the underlying stroma. Mutations in this gene are associated with all forms of dystrophic epidermolysis bullosa. In the absence of mutations, however, an acquired form of this disease can result from an autoimmune response made to type VII collagen. [provided by RefSeq, Jul 2008]

collagen, type IV, alpha 6

This gene encodes one of the six subunits of type IV collagen, the major structural component of basement membranes. Like the other members of the type IV collagen gene family, this gene is organized in a head-to-head conformation with another type IV collagen gene, alpha 5 type IV collagen, so that the gene pair shares a common promoter. Deletions in the alpha 5 gene that extend into the alpha 6 gene result in diffuse leiomyomatosis accompanying the X-linked Alport syndrome caused by the deletion in the alpha 5 gene. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Dec 2013]

collagen, type IV, alpha 5

This gene encodes one of the six subunits of type IV collagen, the major structural component of basement membranes. Mutations in this gene are associated with X-linked Alport syndrome, also known as hereditary nephritis. Like the other members of the type IV collagen gene family, this gene is organized in a head-to-head conformation with another type IV collagen gene so that each gene pair shares a common promoter. Alternatively spliced transcript variants have been identified for this gene. [provided by RefSeq, Aug 2010]

collagen, type IV, alpha 4

This gene encodes one of the six subunits of type IV collagen, the major structural component of basement membranes. This particular collagen IV subunit, however, is only found in a subset of basement membranes. Like the other members of the type IV collagen gene family, this gene is organized in a head-to-head conformation with another type IV collagen gene so that each gene pair shares a common promoter. Mutations in this gene are associated with type II autosomal recessive Alport syndrome (hereditary glomerulonephropathy) and with familial benign hematuria (thin basement membrane disease). Two transcripts, differing only in their transcription start sites, have been identified for this gene and, as is common for collagen genes, multiple polyadenylation sites are found in the 3' UTR. [provided by RefSeq, Jul 2008]

collagen, type IV, alpha 3 (Goodpasture antigen)

Type IV collagen, the major structural component of basement membranes, is a multimeric protein composed of 3 alpha subunits. These subunits are encoded by 6 different genes, alpha 1 through alpha 6, each of which can form a triple helix structure with 2 other subunits to form type IV collagen. This gene encodes alpha 3. In the Goodpasture syndrome, autoantibodies bind to the collagen molecules in the basement membranes of alveoli and glomeruli. The epitopes that elicit these autoantibodies are localized largely to the non-collagenous C-terminal domain of the protein. A specific kinase phosphorylates amino acids in this same C-terminal region and the expression of this kinase is upregulated during pathogenesis. This gene is also linked to an autosomal recessive form of Alport syndrome. The mutations contributing to this syndrome are also located within the exons that encode this C-terminal region. Like the other members of the type IV collagen gene family, this gene is organized in a head-to-head conformation with another type IV collagen gene so that each gene pair shares a common promoter. [provided by RefSeq, Jun 2010]

collagen, type IV, alpha 2

This gene encodes one of the six subunits of type IV collagen, the major structural component of basement membranes. The C-terminal portion of the protein, known as canstatin, is an inhibitor of angiogenesis and tumor growth. Like the other members of the type IV collagen gene family, this gene is organized in a head-to-head conformation with another type IV collagen gene so that each gene pair shares a common promoter. [provided by RefSeq, Jul 2008]

collagen, type IV, alpha 1

This gene encodes a type IV collagen alpha protein. Type IV collagen proteins are integral components of basement membranes. This gene shares a bidirectional promoter with a paralogous gene on the opposite strand. The protein consists of an amino-terminal 7S domain, a triple-helix forming collagenous domain, and a carboxy-terminal non-collagenous domain. It functions as part of a heterotrimer and interacts with other extracellular matrix components such as perlecans, proteoglycans, and laminins. In addition, proteolytic cleavage of the non-collagenous carboxy-terminal domain results in a biologically active fragment known as arresten, which has anti-angiogenic and tumor suppressor properties. Mutations in this gene cause porencephaly, cerebrovascular disease, and renal and muscular defects. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Dec 2014]

collagen alpha-1(III) chain-like

collagen, type XIX, alpha 1

This gene encodes the alpha chain of type XIX collagen, a member of the FACIT collagen family (fibril-associated collagens with interrupted helices). Although the function of this collagen is not known, other members of this collagen family are found in association with fibril-forming collagens such as type I and II, and serve to maintain the integrity of the extracellular matrix. The transcript produced from this gene has an unusually large 3' UTR which has not been completely sequenced. [provided by RefSeq, Jul 2008]

collagen, type X, alpha 1

This gene encodes the alpha chain of type X collagen, a short chain collagen expressed by hypertrophic chondrocytes during endochondral ossification. Unlike type VIII collagen, the other short chain collagen, type X collagen is a homotrimer. Mutations in this gene are associated with Schmid type metaphyseal chondrodysplasia (SMCD) and Japanese type spondylometaphyseal dysplasia (SMD). [provided by RefSeq, Jul 2008]

collagen, type XI, alpha 2 pseudogene 1

collagen, type I, alpha 1

This gene encodes the pro-alpha1 chains of type I collagen whose triple helix comprises two alpha1 chains and one alpha2 chain. Type I is a fibril-forming collagen found in most connective tissues and is abundant in bone, cornea, dermis and tendon. Mutations in this gene are associated with osteogenesis imperfecta types I-IV, Ehlers-Danlos syndrome type VIIA, Ehlers-Danlos syndrome Classical type, Caffey Disease and idiopathic osteoporosis. Reciprocal translocations between chromosomes 17 and 22, where this gene and the gene for platelet-derived growth factor beta are located, are associated with a particular type of skin tumor called dermatofibrosarcoma protuberans, resulting from unregulated expression of the growth factor. Two transcripts, resulting from the use of alternate polyadenylation signals, have been identified for this gene. [provided by R. Dalgleish, Feb 2008]

collagen, type VI, alpha 3

This gene encodes the alpha-3 chain, one of the three alpha chains of type VI collagen, a beaded filament collagen found in most connective tissues. The alpha-3 chain of type VI collagen is much larger than the alpha-1 and -2 chains. This difference in size is largely due to an increase in the number of subdomains, similar to von Willebrand Factor type A domains, that are found in the amino terminal globular domain of all the alpha chains. These domains have been shown to bind extracellular matrix proteins, an interaction that explains the importance of this collagen in organizing matrix components. Mutations in the type VI collagen genes are associated with Bethlem myopathy, a rare autosomal dominant proximal myopathy with early childhood onset. Mutations in this gene are also a cause of Ullrich congenital muscular dystrophy, also referred to as Ullrich scleroatonic muscular dystrophy, an autosomal recessive congenital myopathy that is more severe than Bethlem myopathy. Multiple transcript variants have been identified, but the full-length nature of only some of these variants has been described. [provided by RefSeq, Jun 2009]

collagen, type VI, alpha 6

This gene encodes a large protein that contains multiple von Willebrand factor domains and forms a component of the basal lamina of epithelial cells. This protein may regulate epithelial cell-fibronectin interactions. Variation in this gene may be implicated in skin diseases. [provided by RefSeq, May 2017]

collagen, type IV, alpha 3 (Goodpasture antigen) binding protein

This gene encodes a kinase that specifically phosphorylates the N-terminal region of the non-collagenous domain of the alpha 3 chain of type IV collagen, known as the Goodpasture antigen. Goodpasture disease is the result of an autoimmune response directed at this antigen. One isoform of this protein is also involved in ceramide intracellular transport. Three transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]

collagen, type XXIII, alpha 1

COL23A1 is a member of the transmembrane collagens, a subfamily of the nonfibrillar collagens that contain a single pass hydrophobic transmembrane domain (Banyard et al., 2003 [PubMed 12644459]).[supplied by OMIM, Mar 2008]

collagen alpha-1(I) chain-like

collagen alpha-2(V) chain-like

collagen alpha-2(IV) chain-like

collagen alpha-2(IV) chain-like

collagen alpha-1(X) chain-like

collagen, type XIII, alpha 1

This gene encodes the alpha chain of one of the nonfibrillar collagens. The function of this gene product is not known, however, it has been detected at low levels in all connective tissue-producing cells so it may serve a general function in connective tissues. Unlike most of the collagens, which are secreted into the extracellular matrix, collagen XIII contains a transmembrane domain and the protein has been localized to the plasma membrane. The transcripts for this gene undergo complex and extensive splicing involving at least eight exons. Like other collagens, collagen XIII is a trimer; it is not known whether this trimer is composed of one or more than one alpha chain isomer. A number of alternatively spliced transcript variants have been described, but the full length nature of some of them has not been determined. [provided by RefSeq, Jul 2008]

collagen alpha-1(II) chain-like

collagen alpha-1(XIII) chain

collagen alpha-2(IV) chain-like

collagen alpha-1(III) chain-like

collagen alpha-1(I) chain-like

collagen, type III, alpha 1

This gene encodes the pro-alpha1 chains of type III collagen, a fibrillar collagen that is found in extensible connective tissues such as skin, lung, uterus, intestine and the vascular system, frequently in association with type I collagen. Mutations in this gene are associated with Ehlers-Danlos syndrome type IV, and with aortic and arterial aneurysms. [provided by R. Dalgleish, Feb 2008]

collagen, type XXIV, alpha 1

This gene is a member of the collagen gene family and is thought to regulate type I collagen fibrillogenesis during fetal development. [provided by RefSeq, Mar 2017]

collagen alpha-1(III) chain-like

collagen alpha-1(I) chain-like

collagen alpha-5(IV) chain-like

collagen alpha-1(III) chain-like

From GO Cellular Component Annotations 2023

proteins localized to the collagen-containing extracellular matrix cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the collagen-containing extracellular matrix cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the collagen-containing extracellular matrix 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 collagen-containing extracellular matrix 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

proteins co-occuring with the cortical layer of collagen and cuticulin-based cuticle extracellular matrix 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 collagen and cuticulin-based cuticle extracellular matrix 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 collagen and cuticulin-based cuticle extracellular matrix part 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 2025

proteins co-occuring with the Cortical layer of collagen and cuticulin-based cuticle extracellular matrix 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 Collagen and cuticulin-based cuticle extracellular matrix 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 Medial layer of collagen and cuticulin-based cuticle extracellular matrix cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From CM4AI U2OS Cell Map Protein Localization Assemblies

proteins comprising Collagen biosynthesis and extracellular matrix organization assembly using integrated AP-MS and IF data from the CM4AI U2OS Cell Map Protein Localization Assemblies dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the proteinaceous extracellular matrix cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the extracellular matrix cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the extracellular matrix part cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the proteinaceous extracellular matrix 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 extracellular matrix 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 extracellular matrix part 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 annuli extracellular matrix cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of extracellular matrix assembly biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the sequestering of tgfbeta in extracellular matrix biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the extracellular matrix disassembly biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the extracellular matrix-cell signaling biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the positive regulation of extracellular matrix disassembly biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the sequestering of bmp in extracellular matrix biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of branching involved in salivary gland morphogenesis by extracellular matrix-epithelial cell signaling biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the positive regulation of extracellular matrix assembly biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the positive regulation of extracellular matrix organization biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the extracellular matrix organization biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of extracellular matrix organization biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the positive regulation of extracellular matrix constituent secretion biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of extracellular matrix constituent secretion biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation of extracellular matrix disassembly biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of extracellular matrix disassembly biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the extracellular matrix constituent secretion biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation of extracellular matrix organization biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the extracellular matrix assembly biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the proteinaceous extracellular matrix cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the extracellular matrix cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the extracellular matrix part cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the extracellular matrix structural constituent conferring tensile strength molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the extracellular matrix structural constituent conferring compression resistance molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the extracellular matrix constituent, lubricant activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

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

From GO Molecular Function Annotations 2015

genes performing the extracellular matrix structural constituent molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the extracellular matrix protein binding molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the extracellular matrix constituent conferring elasticity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Extracellular matrix 1 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From MPO Gene-Phenotype Associations

gene mutations causing the abnormal extracellular matrix morphology phenotype in transgenic mice from the MPO Gene-Phenotype Associations dataset.

From Reactome Pathways 2014

proteins participating in the Extracellular matrix organization pathway from the Reactome Pathways dataset.

From Reactome Pathways 2014

proteins participating in the Cell-extracellular matrix interactions pathway from the Reactome Pathways dataset.

From Reactome Pathways 2014

proteins participating in the Degradation of the extracellular matrix pathway from the Reactome Pathways dataset.

From GO Biological Process Annotations 2023

genes participating in the extracellular matrix disassembly biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the extracellular matrix assembly biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the extracellular matrix organization biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the regulation of extracellular matrix organization biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the positive regulation of extracellular matrix disassembly biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the sequestering of BMP in extracellular matrix biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the regulation of extracellular matrix assembly biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the negative regulation of extracellular matrix disassembly biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the positive regulation of extracellular matrix assembly biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the positive regulation of extracellular matrix organization biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the positive regulation of extracellular matrix constituent secretion biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the negative regulation of extracellular matrix constituent secretion biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the regulation of extracellular matrix disassembly biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the sequestering of TGFbeta in extracellular matrix biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the negative regulation of extracellular matrix organization biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the regulation of extracellular matrix constituent secretion biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the extracellular matrix constituent secretion biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the perisynaptic extracellular matrix cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the synapse-associated extracellular matrix cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From MGI Mouse Phenotype Associations 2023

gene mutations causing the abnormal extracellular matrix morphology phenotype in transgenic mice from the MGI Mouse Phenotype Associations 2023 dataset.

From SynGO Synaptic Gene Annotations

genes associated with the synaptic term perisynaptic extracellular matrix from the SynGO Synaptic Gene Annotations dataset.

From SynGO Synaptic Gene Annotations

genes associated with the synaptic term extracellular matrix of synaptic cleft from the SynGO Synaptic Gene Annotations dataset.

From SynGO Synaptic Gene Annotations

genes associated with the synaptic term structural constituent of synapse-associated extracellular matrix from the SynGO Synaptic Gene Annotations dataset.

From CellMarker Gene-Cell Type Associations

genes associated with the Extracellular matrix (ECM)-producing cell_Kidney_Mouse cell type from the CellMarker Gene-Cell Type Associations dataset.

From Reactome Pathways 2024

proteins participating in the Cell-extracellular matrix interactions pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Degradation of the extracellular matrix pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Extracellular matrix organization pathway from the Reactome Pathways 2024 dataset.

From GO Biological Process Annotations 2025

genes participating in the extracellular matrix disassembly biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the extracellular matrix assembly biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the extracellular matrix organization biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the regulation of extracellular matrix organization biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the positive regulation of extracellular matrix disassembly biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the sequestering of BMP in extracellular matrix biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the positive regulation of extracellular matrix assembly biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the regulation of extracellular matrix assembly biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the negative regulation of extracellular matrix disassembly biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the positive regulation of extracellular matrix organization biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the positive regulation of extracellular matrix constituent secretion biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the negative regulation of extracellular matrix constituent secretion biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the regulation of extracellular matrix disassembly biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the sequestering of TGFbeta in extracellular matrix biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the negative regulation of extracellular matrix assembly biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the negative regulation of extracellular matrix organization biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the regulation of extracellular matrix constituent secretion biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the extracellular matrix constituent secretion biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the perisynaptic extracellular matrix cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the specialized extracellular matrix cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the synapse-associated extracellular matrix cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

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

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the synapse-associated extracellular matrix cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Perisynaptic extracellular matrix 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 Extracellular matrix 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 Perisynaptic extracellular matrix 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 synapse-associated extracellular matrix 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 Annuli extracellular matrix 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 Extracellular matrix of synaptic cleft 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 chitin-based extracellular matrix 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 Adhesive extracellular matrix cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From CM4AI U2OS Cell Map Protein Localization Assemblies

proteins comprising Extracellular matrix organization and signaling modulation assembly using integrated AP-MS and IF data from the CM4AI U2OS Cell Map Protein Localization Assemblies dataset.

From CM4AI U2OS Cell Map Protein Localization Assemblies

proteins comprising Extracellular matrix organization subcomplex assembly using integrated AP-MS and IF data from the CM4AI U2OS Cell Map Protein Localization Assemblies dataset.

From GO Molecular Function Annotations 2015

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

From GO Molecular Function Annotations 2023

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

From GO Molecular Function Annotations 2025

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

From Biocarta Pathways

proteins participating in the transcription factor creb and its extracellular signals pathway from the Biocarta Pathways dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Superoxide dismutase, elevated extracellular phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the extracellular membrane-bounded organelle cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the extracellular vesicular exosome cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the extracellular region part cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the extracellular region cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the extracellular space cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the extracellular vesicle cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the extracellular organelle cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the extracellular membrane-bounded organelle 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 extracellular space of host 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 extracellular vesicular exosome 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 extracellular non-membrane-bounded organelle 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 extracellular region part 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 extracellular region 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 extracellular space 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 extracellular ferritin 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 extracellular vesicle 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 extracellular organelle cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From GAD Gene-Disease Associations

genes associated with the disease extracellular magnesium concentration 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 extracellular 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 cellular response to extracellular stimulus biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation of response to extracellular stimulus biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the response to extracellular stimulus biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

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

From GO Biological Process Annotations 2015

genes participating in the positive regulation of extracellular vesicular exosome assembly biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the sequestering of extracellular ligand from receptor biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of response to extracellular stimulus biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the extracellular vesicular exosome assembly biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

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

From GO Biological Process Annotations 2015

genes participating in the extracellular negative regulation of signal transduction biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the extracellular fibril organization biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the extracellular structure organization biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of extracellular vesicular exosome assembly biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of cell growth by extracellular stimulus biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the extracellular polysaccharide 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 response to extracellular stimulus biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the extracellular regulation of signal transduction biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the maintenance of protein location in extracellular region biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

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

From GO Biological Process Annotations 2015

genes participating in the calcium-mediated signaling using extracellular calcium source biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the extracellular membrane-bounded organelle cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the extracellular vesicular exosome cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the extracellular region part cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the extracellular region cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the extracellular space cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the extracellular vesicle cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the extracellular organelle cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the inhibitory extracellular ligand-gated ion channel activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the extracellular-glycine-gated chloride channel activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the extracellular ligand-gated ion channel activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the extracellular-glycine-gated ion channel activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the excitatory extracellular ligand-gated ion channel activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the extracellular-glutamate-gated ion channel activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the extracellular atp-gated cation channel activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Peptidase M41, FtsH extracellular protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the GPCR, family 2, extracellular hormone receptor domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the EGF-like domain, extracellular 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 P2X purinoreceptor extracellular domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the TGF-beta family type I/II receptor, extracellular C-terminal domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Extracellular Endonuclease, subunit A protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Superoxide dismutase (Cu/Zn), extracellular protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the CD81 antigen, large extracellular loop domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Extracellular ligand-binding receptor 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 Extracellular sulfatase, C-terminal protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Extracellular sulfatase protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

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

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Anthrax toxin receptor, extracellular protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the CD4, extracellular protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From LOCATE Curated Protein Localization Annotations

proteins localized to the extracellular region cellular component in low- or high-throughput protein localization assays from the LOCATE Curated Protein Localization Annotations dataset.

From OMIM Gene-Disease Associations

genes associated with the [superoxide dismutase, elevated extracellular] phenotype from the curated OMIM Gene-Disease Associations dataset.

From Phosphosite Textmining Biological Term Annotations

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

From WikiPathways Pathways 2014

proteins participating in the Extracellular vesicle-mediated signaling in recipient cells(Homo sapiens) pathway from the WikiPathways Pathways 2014 dataset.

From LOCATE Predicted Protein Localization Annotations

proteins predicted to localize to the extracellular region cellular component from the LOCATE Predicted Protein Localization Annotations dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Neutrophil Extracellular Trap Formation in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From DisGeNET Gene-Phenotype Associations

genes associated with the phenotype Superoxide Dismutase, Elevated Extracellular in GWAS and other genetic association datasets from the DisGeNET Gene-Phenotype Associations dataset.

From GO Biological Process Annotations 2023

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

From GO Biological Process Annotations 2023

genes participating in the extracellular 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 extracellular exosome assembly biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the epithelial cilium movement involved in extracellular fluid movement biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the cell-cell adhesion in response to extracellular stimulus biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the sequestering of extracellular ligand from receptor biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the extracellular exosome assembly biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the extracellular negative regulation of signal transduction biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the extracellular structure organization biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the protein transport within extracellular region biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the calcium-mediated signaling using extracellular calcium source biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the extracellular vesicle biogenesis biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the regulation of extracellular exosome assembly biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the regulation of cell growth by extracellular stimulus biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the extracellular exosome biogenesis biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

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

From GO Biological Process Annotations 2023

genes participating in the establishment of protein localization to extracellular region biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the maintenance of protein location in extracellular region biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the extracellular regulation of signal transduction biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the extracellular vesicle cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the extracellular membrane-bounded organelle cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the extracellular ligand-gated monoatomic ion channel activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the excitatory extracellular ligand-gated monoatomic ion channel activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the inhibitory extracellular ligand-gated monoatomic ion channel activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From WikiPathways Pathways 2024

proteins participating in the Extracellular vesicle mediated signaling in recipient cells pathway from the WikiPathways Pathways 2024 dataset.

From WikiPathways Pathways 2024

proteins participating in the Extracellular vesicles in the crosstalk of cardiac cells pathway from the WikiPathways Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Signaling by PDGFRA extracellular domain mutants pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Signaling by extracellular domain mutants of KIT pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Signaling by phosphorylated juxtamembrane, extracellular and kinase domain KIT mutants pathway from the Reactome Pathways 2024 dataset.

From GO Biological Process Annotations 2025

genes participating in the extracellular 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 extracellular exosome assembly biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the epithelial cilium movement involved in extracellular fluid movement biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the sequestering of extracellular ligand from receptor biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the extracellular exosome assembly biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the extracellular negative regulation of signal transduction biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the extracellular structure organization biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the protein transport within extracellular region biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the establishment of protein localization to extracellular region biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the extracellular vesicle biogenesis biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the extracellular exosome biogenesis biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the regulation of extracellular exosome assembly biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the maintenance of protein location in extracellular region biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the extracellular regulation of signal transduction biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the protein localization to extracellular region biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the extracellular vesicle cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the extracellular membrane-bounded organelle cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the extracellular ligand-gated monoatomic ion channel activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the excitatory extracellular ligand-gated monoatomic ion channel activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the inhibitory extracellular ligand-gated monoatomic ion channel activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

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

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

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

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

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

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

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

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Extracellular membrane-bounded organelle cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Extracellular exosome 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 Extracellular space 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 Extracellular region 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 Extracellular exosome 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 Extracellular membrane-bounded organelle 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 Extracellular vesicle 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 Extracellular ferritin 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 Extracellular organelle 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 Neutrophil extracellular trap 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 Extracellular non-membrane-bounded organelle 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 Host extracellular space 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 Extracellular isoamylase 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 Extracellular core region of desmosome 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 Bacterial extracellular vesicle cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From KEGG Pathways 2026

proteins participating in the Neutrophil extracellular trap formation pathway from the KEGG Pathways 2026 dataset.

From Biocarta Pathways

proteins participating in the erk and pi-3 kinase are necessary for collagen binding in corneal epithelia pathway from the Biocarta Pathways dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the transmembrane collagen trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the collagen type iv trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the fibrillar collagen trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the collagen type xvi trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the collagen type viii trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

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

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the collagen type xiii trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the basement membrane collagen trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the sheet-forming collagen trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the network-forming collagen trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the collagen type xi trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the short-chain collagen trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the collagen type v trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the collagen type iii trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the collagen type ii trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the collagen type ix trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the collagen type vii trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the collagen trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the collagen type vi trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the facit collagen trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the collagen type xv trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the collagen type xii trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the collagen type xiv trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the collagen type i trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the transmembrane collagen trimer 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 collagen type iv trimer 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 collagen type xviii trimer 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 network-forming collagen trimer 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 fibrillar collagen trimer 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 collagen type xvi trimer 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 collagen type viii trimer 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 collagen type x trimer 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 collagen type xvii trimer 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 basement membrane collagen trimer 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 sheet-forming collagen trimer 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 anchoring collagen 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 collagen type xi trimer 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 short-chain collagen trimer 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 collagen type v trimer 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 collagen type iii trimer 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 collagen type ii trimer 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 collagen type xii trimer 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 collagen type ix trimer 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 collagen type vii trimer 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 collagen trimer 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 collagen type vi trimer 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 collagen type xiii trimer 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 facit collagen trimer 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 collagen type xv trimer 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 collagen type xiv trimer 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 collagen type i trimer cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From DISEASES Curated Gene-Disease Association Evidence Scores

genes involed in the disease collagen disease from the DISEASES Curated Gene-Disease Assocation Evidence Scores dataset.

From DISEASES Experimental Gene-Disease Association Evidence Scores

genes associated with the disease collagen disease in GWAS datasets from the DISEASES Experimental Gene-Disease Assocation Evidence Scores dataset.

From DISEASES Text-mining Gene-Disease Association Evidence Scores

genes co-occuring with the disease collagen disease in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores dataset.

From GeneRIF Biological Term Annotations

genes co-occuring with the biological term collagen 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 collagen-activated tyrosine kinase receptor 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 collagen binding biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

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

From GO Biological Process Annotations 2015

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

From GO Biological Process Annotations 2015

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

From GO Biological Process Annotations 2015

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

From GO Biological Process Annotations 2015

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

From GO Biological Process Annotations 2015

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

From GO Biological Process Annotations 2015

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

From GO Biological Process Annotations 2015

genes participating in the collagen fibril organization biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

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

From GO Cellular Component Annotations 2015

proteins localized to the transmembrane collagen trimer cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the collagen type iv trimer cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the collagen type viii trimer cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the network-forming collagen trimer cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the fibrillar collagen trimer cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the collagen type xvi trimer cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the collagen type xiii trimer cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the basement membrane collagen trimer cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the sheet-forming collagen trimer cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

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

From GO Cellular Component Annotations 2015

proteins localized to the collagen type xi trimer cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the short-chain collagen trimer cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the collagen type v trimer cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the collagen type iii trimer cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the collagen type ii trimer cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the collagen type xv trimer cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the collagen type xii trimer cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the collagen type ix trimer cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the collagen type vii trimer cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the collagen trimer cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the collagen type vi trimer cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the facit collagen trimer cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the collagen type xiv trimer cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the collagen type i trimer cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the collagen receptor activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

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

From GO Molecular Function Annotations 2015

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

From GO Molecular Function Annotations 2015

genes performing the protein tyrosine kinase collagen receptor activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GWASdb SNP-Disease Associations

genes associated with the disease collagen disease in GWAS and other genetic association datasets from the GWASdb SNP-Disease Associations dataset.

From HPO Gene-Disease Associations

genes associated with the impaired collagen-induced platelet aggregation phenotype by mapping known disease genes to disease phenotypes from the HPO Gene-Disease Associations dataset.

From HPO Gene-Disease Associations

genes associated with the type 1 collagen overmodification phenotype by mapping known disease genes to disease phenotypes from the HPO Gene-Disease Associations dataset.

From HPO Gene-Disease Associations

genes associated with the abnormal bone collagen fibril morphology phenotype by mapping known disease genes to disease phenotypes from the HPO Gene-Disease Associations dataset.

From HPO Gene-Disease Associations

genes associated with the abnormal cartilage collagen 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 Fibrillar collagen, C-terminal protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Fibronectin, type II, collagen-binding protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Collagen alpha-1(XVIII) chain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Collagen triple helix repeat protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Collagen IV, non-collagenous protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Collagen alpha-1(XXV) chain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Domain of unknown function DUF959, collagen XVIII, N-terminal protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From MPO Gene-Phenotype Associations

gene mutations causing the increased collagen deposition in the muscles phenotype in transgenic mice from the MPO Gene-Phenotype Associations dataset.

From MPO Gene-Phenotype Associations

gene mutations causing the abnormal pulmonary collagen fibril morphology phenotype in transgenic mice from the MPO Gene-Phenotype Associations dataset.

From MPO Gene-Phenotype Associations

gene mutations causing the abnormal tendon collagen fibril morphology phenotype in transgenic mice from the MPO Gene-Phenotype Associations dataset.

From MPO Gene-Phenotype Associations

gene mutations causing the abnormal collagen level phenotype in transgenic mice from the MPO Gene-Phenotype Associations dataset.

From MPO Gene-Phenotype Associations

gene mutations causing the decreased collagen level phenotype in transgenic mice from the MPO Gene-Phenotype Associations dataset.

From MPO Gene-Phenotype Associations

gene mutations causing the abnormal aorta collagen fibril morphology phenotype in transgenic mice from the MPO Gene-Phenotype Associations dataset.

From MPO Gene-Phenotype Associations

gene mutations causing the abnormal bone collagen fibril morphology phenotype in transgenic mice from the MPO Gene-Phenotype Associations dataset.

From MPO Gene-Phenotype Associations

gene mutations causing the abnormal dermis reticular layer collagen network phenotype in transgenic mice from the MPO Gene-Phenotype Associations dataset.

From MPO Gene-Phenotype Associations

gene mutations causing the abnormal cutaneous collagen fibril morphology phenotype in transgenic mice from the MPO Gene-Phenotype Associations dataset.

From Phosphosite Textmining Biological Term Annotations

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

From Reactome Pathways 2014

proteins participating in the Platelet Adhesion to exposed collagen pathway from the Reactome Pathways dataset.

From Reactome Pathways 2014

proteins participating in the Crosslinking of collagen fibrils pathway from the Reactome Pathways dataset.

From Reactome Pathways 2014

proteins participating in the Assembly of collagen fibrils and other multimeric structures pathway from the Reactome Pathways dataset.

From Reactome Pathways 2014

proteins participating in the Collagen formation pathway from the Reactome Pathways dataset.

From Reactome Pathways 2014

proteins participating in the Collagen degradation pathway from the Reactome Pathways dataset.

From Reactome Pathways 2014

proteins participating in the Collagen biosynthesis and modifying enzymes pathway from the Reactome Pathways dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Collagen Nevus Of Skin in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Collagen-Vascular 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 Abnormal Cartilage Collagen in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Abnormal Type Ii Collagen in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Low Grade Fibromyxoid Sarcoma With Giant Collagen Rosettes in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From DisGeNET Gene-Disease Associations

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

From DisGeNET Gene-Phenotype Associations

genes associated with the phenotype Impaired Collagen-Induced Platelet Aggregation in GWAS and other genetic association datasets from the DisGeNET Gene-Phenotype Associations dataset.

From DisGeNET Gene-Phenotype Associations

genes associated with the phenotype Reduced Muscle Collagen in GWAS and other genetic association datasets from the DisGeNET Gene-Phenotype Associations dataset.

From DisGeNET Gene-Phenotype Associations

genes associated with the phenotype Collagen Overmodification in GWAS and other genetic association datasets from the DisGeNET Gene-Phenotype Associations dataset.

From GO Biological Process Annotations 2023

genes participating in the collagen fibril organization biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the collagen-activated 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 collagen fibril organization biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the positive regulation of collagen fibril organization biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

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

From GO Biological Process Annotations 2023

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

From GO Biological Process Annotations 2023

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

From GO Biological Process Annotations 2023

genes participating in the collagen-activated tyrosine kinase receptor 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 collagen fibril organization biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

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

From GO Biological Process Annotations 2023

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

From GO Cellular Component Annotations 2023

proteins localized to the collagen type I trimer cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the collagen type XI trimer cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the collagen type II trimer cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the collagen type III trimer cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the collagen type IV trimer cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the collagen type V trimer cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the collagen type IX trimer cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the collagen type VIII trimer cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the collagen type XV trimer cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the collagen type VII trimer cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the collagen type X trimer cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the collagen type XIV trimer cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the collagen type XVI trimer cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the collagen type XIII trimer cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the collagen type XII trimer cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the sheet-forming collagen trimer cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the collagen type VII anchoring fibril cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the collagen V binding molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the collagen receptor activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the protein tyrosine kinase collagen receptor activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From MGI Mouse Phenotype Associations 2023

gene mutations causing the abnormal cutaneous collagen fibril morphology phenotype in transgenic mice from the MGI Mouse Phenotype Associations 2023 dataset.

From MGI Mouse Phenotype Associations 2023

gene mutations causing the increased collagen deposition in the muscles phenotype in transgenic mice from the MGI Mouse Phenotype Associations 2023 dataset.

From MGI Mouse Phenotype Associations 2023

gene mutations causing the abnormal tendon collagen fibril morphology phenotype in transgenic mice from the MGI Mouse Phenotype Associations 2023 dataset.

From MGI Mouse Phenotype Associations 2023

gene mutations causing the increased circulating type I collagen C-terminal telopeptide level phenotype in transgenic mice from the MGI Mouse Phenotype Associations 2023 dataset.

From MGI Mouse Phenotype Associations 2023

gene mutations causing the decreased circulating type I collagen C-terminal telopeptide level phenotype in transgenic mice from the MGI Mouse Phenotype Associations 2023 dataset.

From MGI Mouse Phenotype Associations 2023

gene mutations causing the abnormal bone collagen fibril morphology phenotype in transgenic mice from the MGI Mouse Phenotype Associations 2023 dataset.

From MGI Mouse Phenotype Associations 2023

gene mutations causing the abnormal dermis reticular layer collagen network phenotype in transgenic mice from the MGI Mouse Phenotype Associations 2023 dataset.

From MGI Mouse Phenotype Associations 2023

gene mutations causing the decreased collagen level phenotype in transgenic mice from the MGI Mouse Phenotype Associations 2023 dataset.

From MGI Mouse Phenotype Associations 2023

gene mutations causing the abnormal corneal stroma collagen fibril morphology phenotype in transgenic mice from the MGI Mouse Phenotype Associations 2023 dataset.

From MGI Mouse Phenotype Associations 2023

gene mutations causing the abnormal pulmonary collagen fibril morphology phenotype in transgenic mice from the MGI Mouse Phenotype Associations 2023 dataset.

From MGI Mouse Phenotype Associations 2023

gene mutations causing the abnormal aorta collagen fibril morphology phenotype in transgenic mice from the MGI Mouse Phenotype Associations 2023 dataset.

From MGI Mouse Phenotype Associations 2023

gene mutations causing the increased collagen level phenotype in transgenic mice from the MGI Mouse Phenotype Associations 2023 dataset.

From MGI Mouse Phenotype Associations 2023

gene mutations causing the abnormal collagen level phenotype in transgenic mice from the MGI Mouse Phenotype Associations 2023 dataset.

From WikiPathways Pathways 2024

proteins participating in the Type I collagen synthesis in the context of osteogenesis imperfecta pathway from the WikiPathways Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Assembly of collagen fibrils and other multimeric structures pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Collagen biosynthesis and modifying enzymes pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Collagen chain trimerization pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Collagen degradation pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Collagen formation pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Crosslinking of collagen fibrils pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Defective VWF binding to collagen type I pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Defects of platelet adhesion to exposed collagen pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Enhanced binding of GP1BA variant to VWF multimer:collagen pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Platelet Adhesion to exposed collagen pathway from the Reactome Pathways 2024 dataset.

From GO Biological Process Annotations 2025

genes participating in the collagen fibril organization biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

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

From GO Biological Process Annotations 2025

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

From GO Biological Process Annotations 2025

genes participating in the collagen-activated 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 collagen fibril organization biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the positive regulation of collagen fibril organization biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

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

From GO Biological Process Annotations 2025

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

From GO Biological Process Annotations 2025

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

From GO Biological Process Annotations 2025

genes participating in the collagen-activated tyrosine kinase receptor 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 collagen fibril organization biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

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

From GO Biological Process Annotations 2025

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

From GO Cellular Component Annotations 2025

proteins localized to the collagen type I trimer cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the collagen type II trimer cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the collagen type XI trimer cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the collagen type III trimer cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the collagen type IV trimer cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the collagen type V trimer cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the collagen type IX trimer cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the collagen type VIII trimer cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the collagen type X trimer cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the collagen type XIV trimer cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the collagen type XVI trimer cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the collagen type XIII trimer cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the collagen type XII trimer cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the interstitial hexagonal collagen network cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the collagen V binding molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the collagen receptor activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the protein tyrosine kinase collagen receptor activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From DISEASES Curated Gene-Disease Association Evidence Scores 2025

genes involed in the disease Collagen disease from the DISEASES Curated Gene-Disease Association Evidence Scores 2025 dataset.

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

genes co-occuring with the disease Collagen disease in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.

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

genes co-occuring with the disease Multiple epiphyseal dysplasia due to collagen 9 anomaly in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.

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

genes co-occuring with the disease Disseminated eosinophilic collagen disease in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Collagen type VI trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

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

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Collagen beaded filament cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Collagen type XIII trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Transmembrane collagen trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Collagen type I trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Fibrillar collagen trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Banded collagen fibril cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Complex of collagen trimers cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Collagen type XI trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Basement membrane collagen trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Collagen type XV trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Collagen type V trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the FACIT collagen trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Collagen type XIV trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Anchoring collagen 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 Collagen type IV trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

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

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the network-forming collagen trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Collagen type III trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Collagen type XII trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Collagen type XXVI trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Collagen type IX trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Collagen type VII anchoring fibril cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Collagen anchoring fibril cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Collagen type VII trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

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

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the sheet-forming collagen trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the short-chain collagen trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Collagen type VIII trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Collagen type II trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Collagen type XVI trimer cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Collagen type X trimer 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 Collagen network 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 Complex of collagen trimers 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 Collagen beaded filament 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 Anchoring collagen 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 Collagen trimer 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 Transmembrane collagen trimer 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 Banded collagen fibril 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 Fibrillar collagen trimer 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 Collagen type XI trimer 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 Collagen sheet 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 network-forming collagen trimer 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 Collagen type IV trimer 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 Basement membrane collagen trimer 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 Collagen type VI trimer 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 Collagen type V trimer 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 short-chain collagen trimer 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 Collagen anchoring fibril 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 Collagen type I trimer 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 sheet-forming collagen trimer 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 Collagen type VII anchoring fibril 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 Collagen type IX trimer 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 Collagen type II trimer 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 Collagen type III trimer 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 FACIT collagen trimer 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 Collagen type XIII trimer 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 Collagen 6-related myopathy phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the COLLAGEN POLYMORPH phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Qualitative or quantitative defects of collagen phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From CM4AI U2OS Cell Map Protein Localization Assemblies

proteins comprising Collagen biosynthesis assembly using integrated AP-MS and IF data from the CM4AI U2OS Cell Map Protein Localization Assemblies dataset.

From GWAS Catalog SNP-Phenotype Associations 2025

genes associated with the Liver fibrosis (total hepatic collagen content) phenotype in GWAS datasets from the GWAS Catalog SNP-Phenotype Associations 2025 dataset.

From GWAS Catalog SNP-Phenotype Associations 2025

genes associated with the Serum type 1 collagen metabolite levels phenotype in GWAS datasets from the GWAS Catalog SNP-Phenotype Associations 2025 dataset.

From GWAS Catalog SNP-Phenotype Associations 2025

genes associated with the Platelet reactivity measurement (collagen-ADP) phenotype in GWAS datasets from the GWAS Catalog SNP-Phenotype Associations 2025 dataset.

From GWAS Catalog SNP-Phenotype Associations 2025

genes associated with the Platelet reactivity measurement (collagen-epinephrine) phenotype in GWAS datasets from the GWAS Catalog SNP-Phenotype Associations 2025 dataset.

From Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles

genes with high or low expression in ventricular (matrix) zone of pons 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 ventricular (matrix) zone of cerebellum relative to other tissues from the Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles dataset.

From Biocarta Pathways

proteins participating in the inhibition of matrix metalloproteinases pathway from the Biocarta Pathways dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the presynaptic cytoskeletal matrix assembled at active zones cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the peroxisomal matrix cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the interphotoreceptor matrix cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the interstitial matrix cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the nuclear matrix cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the acrosomal matrix cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the mitochondrial matrix cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the extrahaustorial matrix 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 peroxisomal matrix 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 pectic matrix 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 interphotoreceptor matrix 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 spindle matrix 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 interstitial matrix 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 protein complex involved in cell-matrix adhesion 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 presynaptic cytoskeletal matrix assembled at active zones 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 biofilm matrix 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 acrosomal matrix 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 nuclear matrix 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 mitochondrial matrix cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From dbGAP Gene-Trait Associations

genes associated with the trait Matrix Metalloproteinases in GWAS and other genetic association datasets from the dbGAP Gene-Trait Associations dataset.

From GAD Gene-Disease Associations

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

From GAD Gene-Disease Associations

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

From GAD Gene-Disease Associations

genes associated with the disease matrix metalloproteinase 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 matrix 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 calcium-independent cell-matrix adhesion biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the cellular response to cell-matrix adhesion biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the nuclear matrix organization biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the protein import into mitochondrial matrix biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

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

From GO Biological Process Annotations 2015

genes participating in the protein import into peroxisome matrix, docking biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation of smooth muscle cell-matrix adhesion biological process from the curated GO Biological Process Annotations 2015 dataset.