HUMAN:B4DKJ3

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	COMP
Protein Name(s)	Cartilage oligomeric matrix protein cDNA FLJ59562, highly similar to Cartilage oligomeric matrix protein
External Links
UniProt	B4DKJ3
EMBL	AC003107 AK296586
UniGene	Hs.1584
ProteinModelPortal	B4DKJ3
SMR	B4DKJ3
Ensembl	ENST00000425807
KEGG	hsa:1311
UCSC	uc010xqj.2
HGNC	HGNC:2227
HOGENOM	HOG000007542
HOVERGEN	HBG000636
ChiTaRS	COMP
GenomeRNAi	1311
NextBio	35472801
GO	GO:0005576 GO:0005509 GO:0007155
Gene3D	2.60.120.200 4.10.1080.10
InterPro	IPR028492 IPR008985 IPR013320 IPR000742 IPR001881 IPR013032 IPR018097 IPR024665 IPR003367 IPR017897 IPR008859 IPR028974
PANTHER	PTHR10199:SF81
Pfam	PF11598 PF07645 PF02412 PF05735
SMART	SM00181 SM00179
SUPFAM	SSF103647 SSF49899
PROSITE	PS01186 PS50026 PS01187 PS51234 PS51236

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
enables	GO:0005201	extracellular matrix structural constituent	PMID:20551380^[1]	ECO:0007666	automatically integrated combinatorial computational and experimental evidence used in manual assertion		F	occurs_in:(UBERON:0001496)	Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	PMID:27068509^[2]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0007318)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:23533145^[3]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0002020	protease binding	PMID:18485748^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P58397	F		Seeded From UniProt	complete
enables	GO:0002020	protease binding	PMID:18485748^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9UKP4	F		Seeded From UniProt	complete
colocalizes_with	GO:0062023	collagen-containing extracellular matrix	PMID:20551380^[1]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001496)	Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:20551380^[1]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001496)	Seeded From UniProt	complete
involved_in	GO:0060173	limb development	PMID:16542502^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0043395	heparan sulfate proteoglycan binding	PMID:17588949^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	PMID:17993464^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008201	heparin binding	PMID:17588949^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0005518	collagen binding	PMID:11084047^[8]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0005509	calcium ion binding	PMID:11084047^[8]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0005509	calcium ion binding	PMID:10852928^[9]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:1902732	positive regulation of chondrocyte proliferation	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:88469 PANTHER:PTN001610300	P		Seeded From UniProt	complete
part_of	GO:0062023	collagen-containing extracellular matrix	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0031850 MGI:MGI:1101779 MGI:MGI:98738 PANTHER:PTN002565423 RGD:2378 UniProtKB:P35443	C		Seeded From UniProt	complete
enables	GO:0043394	proteoglycan binding	PMID:29030641^[11]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:1902732	positive regulation of chondrocyte proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	P		Seeded From UniProt	complete
involved_in	GO:1900047	negative regulation of hemostasis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	P		Seeded From UniProt	complete
involved_in	GO:0098868	bone growth	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	P		Seeded From UniProt	complete
involved_in	GO:0097084	vascular smooth muscle cell development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	P		Seeded From UniProt	complete
involved_in	GO:0070527	platelet aggregation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	P		Seeded From UniProt	complete
involved_in	GO:0060349	bone morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	P		Seeded From UniProt	complete
involved_in	GO:0060173	limb development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	P		Seeded From UniProt	complete
involved_in	GO:0051216	cartilage development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	P		Seeded From UniProt	complete
involved_in	GO:0050905	neuromuscular process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	P		Seeded From UniProt	complete
involved_in	GO:0050881	musculoskeletal movement	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	P		Seeded From UniProt	complete
involved_in	GO:0048844	artery morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	P		Seeded From UniProt	complete
involved_in	GO:0048747	muscle fiber development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	P		Seeded From UniProt	complete
involved_in	GO:0043588	skin development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	P		Seeded From UniProt	complete
enables	GO:0036122	BMP binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	F		Seeded From UniProt	complete
involved_in	GO:0035989	tendon development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	P		Seeded From UniProt	complete
involved_in	GO:0035988	chondrocyte proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	P		Seeded From UniProt	complete
involved_in	GO:0035264	multicellular organism growth	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	P		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	C		Seeded From UniProt	complete
involved_in	GO:0030509	BMP signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	P		Seeded From UniProt	complete
involved_in	GO:0030500	regulation of bone mineralization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	P		Seeded From UniProt	complete
involved_in	GO:0030282	bone mineralization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	P		Seeded From UniProt	complete
involved_in	GO:0030199	collagen fibril organization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	P		Seeded From UniProt	complete
involved_in	GO:0016485	protein processing	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	P		Seeded From UniProt	complete
involved_in	GO:0014829	vascular smooth muscle contraction	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	P		Seeded From UniProt	complete
involved_in	GO:0010468	regulation of gene expression	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	P		Seeded From UniProt	complete
involved_in	GO:0010260	animal organ senescence	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	P		Seeded From UniProt	complete
involved_in	GO:0010259	multicellular organism aging	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	P		Seeded From UniProt	complete
involved_in	GO:0009306	protein secretion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	P		Seeded From UniProt	complete
involved_in	GO:0007596	blood coagulation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	P		Seeded From UniProt	complete
involved_in	GO:0006986	response to unfolded protein	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	P		Seeded From UniProt	complete
involved_in	GO:0006915	apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	P		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	C		Seeded From UniProt	complete
enables	GO:0005178	integrin binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	F		Seeded From UniProt	complete
involved_in	GO:0003417	growth plate cartilage development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	P		Seeded From UniProt	complete
involved_in	GO:0003416	endochondral bone growth	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	P		Seeded From UniProt	complete
involved_in	GO:0002063	chondrocyte development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	P		Seeded From UniProt	complete
enables	GO:0002020	protease binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	F		Seeded From UniProt	complete
involved_in	GO:0001503	ossification	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	P		Seeded From UniProt	complete
involved_in	GO:0001501	skeletal system development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R0G6 ensembl:ENSMUSP00000003659	P		Seeded From UniProt	complete
enables	GO:0005509	calcium ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001881 InterPro:IPR003367 InterPro:IPR008859 InterPro:IPR018097 InterPro:IPR028974	F		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR008859	C		Seeded From UniProt	complete
involved_in	GO:0007155	cell adhesion	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003367 InterPro:IPR008859	P		Seeded From UniProt	complete
involved_in	GO:0009887	animal organ morphogenesis	PMID:7713493^[12]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0031012	extracellular matrix	PMID:7713493^[12]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005509	calcium ion binding	PMID:7670472^[13]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0005201	extracellular matrix structural constituent	PMID:7713493^[12]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0001501	skeletal system development	PMID:7670472^[13]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030198	extracellular matrix organization	Reactome:R-HSA-1474244	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	Reactome:R-HSA-2426259 Reactome:R-HSA-2424252	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006915	apoptotic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0053	P		Seeded From UniProt	complete
enables	GO:0008201	heparin binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0358	F		Seeded From UniProt	complete
involved_in	GO:0007155	cell adhesion	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0130	P		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0964	C		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 Didangelos, A et al. (2010) Proteomics characterization of extracellular space components in the human aorta. Mol. Cell Proteomics 9 2048-62 PubMed GONUTS page
↑ Barallobre-Barreiro, J et al. (2016) Extracellular matrix remodelling in response to venous hypertension: proteomics of human varicose veins. Cardiovasc. Res. 110 419-30 PubMed GONUTS page
↑ Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
↑ ^4.0 ^4.1 Luan, Y et al. (2008) Inhibition of ADAMTS-7 and ADAMTS-12 degradation of cartilage oligomeric matrix protein by alpha-2-macroglobulin. Osteoarthr. Cartil. 16 1413-20 PubMed GONUTS page
↑ Koelling, S et al. (2006) Cartilage oligomeric matrix protein is involved in human limb development and in the pathogenesis of osteoarthritis. Arthritis Res. Ther. 8 R56 PubMed GONUTS page
↑ ^6.0 ^6.1 Chen, FH et al. (2007) Interaction of cartilage oligomeric matrix protein/thrombospondin 5 with aggrecan. J. Biol. Chem. 282 24591-8 PubMed GONUTS page
↑ Gagarina, V et al. (2008) Cartilage oligomeric matrix protein protects cells against death by elevating members of the IAP family of survival proteins. J. Biol. Chem. 283 648-59 PubMed GONUTS page
↑ ^8.0 ^8.1 Thur, J et al. (2001) Mutations in cartilage oligomeric matrix protein causing pseudoachondroplasia and multiple epiphyseal dysplasia affect binding of calcium and collagen I, II, and IX. J. Biol. Chem. 276 6083-92 PubMed GONUTS page
↑ Chen, H et al. (2000) Cartilage oligomeric matrix protein is a calcium-binding protein, and a mutation in its type 3 repeats causes conformational changes. J. Biol. Chem. 275 26538-44 PubMed GONUTS page
↑ ^10.0 ^10.1 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Flowers, SA et al. (2017) Lubricin binds cartilage proteins, cartilage oligomeric matrix protein, fibronectin and collagen II at the cartilage surface. Sci Rep 7 13149 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 Newton, G et al. (1994) Characterization of human and mouse cartilage oligomeric matrix protein. Genomics 24 435-9 PubMed GONUTS page
↑ ^13.0 ^13.1 Briggs, MD et al. (1995) Pseudoachondroplasia and multiple epiphyseal dysplasia due to mutations in the cartilage oligomeric matrix protein gene. Nat. Genet. 10 330-6 PubMed GONUTS page

[PMID:20551380-1] 1.0 ^1.1 ^1.2 Didangelos, A et al. (2010) Proteomics characterization of extracellular space components in the human aorta. Mol. Cell Proteomics 9 2048-62 PubMed GONUTS page

[PMID:27068509-2] Barallobre-Barreiro, J et al. (2016) Extracellular matrix remodelling in response to venous hypertension: proteomics of human varicose veins. Cardiovasc. Res. 110 419-30 PubMed GONUTS page

[PMID:23533145-3] Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page

[PMID:18485748-4] 4.0 ^4.1 Luan, Y et al. (2008) Inhibition of ADAMTS-7 and ADAMTS-12 degradation of cartilage oligomeric matrix protein by alpha-2-macroglobulin. Osteoarthr. Cartil. 16 1413-20 PubMed GONUTS page

[PMID:16542502-5] Koelling, S et al. (2006) Cartilage oligomeric matrix protein is involved in human limb development and in the pathogenesis of osteoarthritis. Arthritis Res. Ther. 8 R56 PubMed GONUTS page

[PMID:17588949-6] 6.0 ^6.1 Chen, FH et al. (2007) Interaction of cartilage oligomeric matrix protein/thrombospondin 5 with aggrecan. J. Biol. Chem. 282 24591-8 PubMed GONUTS page

[PMID:17993464-7] Gagarina, V et al. (2008) Cartilage oligomeric matrix protein protects cells against death by elevating members of the IAP family of survival proteins. J. Biol. Chem. 283 648-59 PubMed GONUTS page

[PMID:11084047-8] 8.0 ^8.1 Thur, J et al. (2001) Mutations in cartilage oligomeric matrix protein causing pseudoachondroplasia and multiple epiphyseal dysplasia affect binding of calcium and collagen I, II, and IX. J. Biol. Chem. 276 6083-92 PubMed GONUTS page

[PMID:10852928-9] Chen, H et al. (2000) Cartilage oligomeric matrix protein is a calcium-binding protein, and a mutation in its type 3 repeats causes conformational changes. J. Biol. Chem. 275 26538-44 PubMed GONUTS page

[PMID:21873635-10] 10.0 ^10.1 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:29030641-11] Flowers, SA et al. (2017) Lubricin binds cartilage proteins, cartilage oligomeric matrix protein, fibronectin and collagen II at the cartilage surface. Sci Rep 7 13149 PubMed GONUTS page

[PMID:7713493-12] 12.0 ^12.1 ^12.2 Newton, G et al. (1994) Characterization of human and mouse cartilage oligomeric matrix protein. Genomics 24 435-9 PubMed GONUTS page

[PMID:7670472-13] 13.0 ^13.1 Briggs, MD et al. (1995) Pseudoachondroplasia and multiple epiphyseal dysplasia due to mutations in the cartilage oligomeric matrix protein gene. Nat. Genet. 10 330-6 PubMed GONUTS page

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HUMAN:B4DKJ3

Contents

Annotations

Notes

References

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