HUMAN:CO2A1

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	COL2A1
Protein Name(s)	Collagen alpha-1(II) chain Alpha-1 type II collagen Collagen alpha-1(II) chain Chondrocalcin
External Links
UniProt	P02458
EMBL	X16468 L10347 BT007205 AC004801 BC007252 BC116449 X16711 M25730 M32168 M25655 M25656 M64345 M60299 M25698 X58709 X57010 U15195 X13783 M25728 X02371 X02372 X02373 X02374 X02375 X02376 X02377 X02378 X16158 X16158 X16158 X16158 X16158 X16158 X16158 J00116 L00977 M63281 M27468 X06268 X00339 M12048
CCDS	CCDS41778.1 CCDS8759.1
PIR	A38513
RefSeq	NP_001835.3 NP_149162.2
UniGene	Hs.408182
PDB	1U5M 2FSE 2SEB
PDBsum	1U5M 2FSE 2SEB
DisProt	DP00274
ProteinModelPortal	P02458
SMR	P02458
BioGrid	107677
IntAct	P02458
MINT	MINT-6796075
ChEMBL	CHEMBL2364188
DrugBank	DB00048
PhosphoSite	P02458
DMDM	124056489
MaxQB	P02458
PaxDb	P02458
PRIDE	P02458
DNASU	1280
Ensembl	ENST00000337299 ENST00000380518
GeneID	1280
KEGG	hsa:1280
UCSC	uc001rqt.3 uc001rqu.3 uc001rqv.3
CTD	1280
GeneCards	GC12M048366
GeneReviews	COL2A1
HGNC	HGNC:2200
HPA	CAB002214 HPA045939
MIM	108300 120140 132450 150600 151210 156550 183900 184250 200610 271700 604864 608805 609162 609508
neXtProt	NX_P02458
Orphanet	93296 209867 137678 85198 86820 93297 485 2380 93279 166011 1427 85166 93346 94068 93315 93316 1856 90653
PharmGKB	PA26715
eggNOG	NOG12793
GeneTree	ENSGT00770000120467
HOVERGEN	HBG004933
InParanoid	P02458
KO	K06236
OMA	LQDGCTK
OrthoDB	EOG7TJ3HH
PhylomeDB	P02458
TreeFam	TF344135
Reactome	REACT_118779 REACT_121139 REACT_13552 REACT_150180 REACT_150401 REACT_163874 REACT_163906 REACT_16888 REACT_18312
ChiTaRS	COL2A1
EvolutionaryTrace	P02458
GeneWiki	Collagen,_type_II,_alpha_1
GenomeRNAi	1280
NextBio	5171
PMAP-CutDB	P02458
PRO	PR:P02458
Proteomes	UP000005640
Bgee	P02458
Genevestigator	P02458
GO	GO:0005604 GO:0005585 GO:0005788 GO:0031012 GO:0005576 GO:0005615 GO:0030020 GO:0042802 GO:0046872 GO:0048407 GO:0007411 GO:0001502 GO:0051216 GO:0060351 GO:0071773 GO:0007417 GO:0002062 GO:0030574 GO:0030199 GO:0060272 GO:0001958 GO:0022617 GO:0030198 GO:0003007 GO:0042472 GO:0060174 GO:2001240 GO:0030903 GO:0071599 GO:0060021 GO:0006029 GO:0010468 GO:0007605 GO:0001501 GO:0001894 GO:0007601
InterPro	IPR008160 IPR000885 IPR001007
Pfam	PF01410 PF01391 PF00093
ProDom	PD002078
SMART	SM00038 SM00214
PROSITE	PS51461 PS01208 PS50184

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
Contributes to	GO:0005202	collagen	PMID:25653215^[1]	ECO:0000314			F		Load bearing replacement that mimics bone	complete CACAO 10559
enables	GO:0030020	extracellular matrix structural constituent conferring tensile strength	PMID:28327460^[2]	ECO:0007666	automatically integrated combinatorial computational and experimental evidence used in manual assertion		F	occurs_in:(CL:0002540)\|occurs_in:(CL:0002570)\|occurs_in:(CL:0002551)	Seeded From UniProt	complete
part_of	GO:0062023	collagen-containing extracellular matrix	PMID:28327460^[2]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0002540)\|part_of:(CL:0002570)\|part_of:(CL:0002551)	Seeded From UniProt	complete
part_of	GO:0062023	collagen-containing extracellular matrix	PMID:28344315^[3]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0002371)	Seeded From UniProt	complete
enables	GO:0030020	extracellular matrix structural constituent conferring tensile strength	PMID:28344315^[3]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F	occurs_in:(UBERON:0002371)	Seeded From UniProt	complete
enables	GO:0030020	extracellular matrix structural constituent conferring tensile strength	PMID:27559042^[4]	ECO:0007666	automatically integrated combinatorial computational and experimental evidence used in manual assertion		F	occurs_in:(UBERON:0006618) occurs_in:(UBERON:0002302)	Seeded From UniProt	complete
part_of	GO:0062023	collagen-containing extracellular matrix	PMID:28675934^[5]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0003688)\|part_of:(UBERON:0001911)	Seeded From UniProt	complete
enables	GO:0030020	extracellular matrix structural constituent conferring tensile strength	PMID:28675934^[5]	ECO:0007666	automatically integrated combinatorial computational and experimental evidence used in manual assertion		F	occurs_in:(UBERON:0003688)\|occurs_in:(UBERON:0001911)	Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:20603131^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0042289	MHC class II protein binding	PMID:9354468^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P01903,UniProtKB:P13760	F		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	PMID:27068509^[8]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0007318)	Seeded From UniProt	complete
part_of	GO:0062023	collagen-containing extracellular matrix	PMID:27559042^[4]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0006618) part_of:(UBERON:0002302)	Seeded From UniProt	complete
part_of	GO:0062023	collagen-containing extracellular matrix	PMID:23658023^[9]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0002322)	Seeded From UniProt	complete
involved_in	GO:0060272	embryonic skeletal joint morphogenesis	PMID:16752401^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:2587267^[11]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0030199	collagen fibril organization	PMID:1429602^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0030020	extracellular matrix structural constituent conferring tensile strength	PMID:8660302^[13]	ECO:0000305	curator inference used in manual assertion	GO:0005585	F		Seeded From UniProt	complete
involved_in	GO:0007605	sensory perception of sound	PMID:16752401^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007601	visual perception	PMID:16752401^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005585	collagen type II trimer	PMID:8660302^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0001501	skeletal system development	PMID:1429602^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007601	visual perception	PMID:10486316^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0031012	extracellular matrix	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:88445 MGI:MGI:88446 MGI:MGI:88452 MGI:MGI:88453 MGI:MGI:88457 MGI:MGI:88467 PANTHER:PTN002513067	C		Seeded From UniProt	complete
involved_in	GO:0030903	notochord development	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:88452 PANTHER:PTN002771202	P		Seeded From UniProt	complete
involved_in	GO:0030199	collagen fibril organization	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:88452 MGI:MGI:88458 PANTHER:PTN002771202 UniProtKB:P02458 UniProtKB:P05997	P		Seeded From UniProt	complete
involved_in	GO:0030198	extracellular matrix organization	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1095415 MGI:MGI:2152695 MGI:MGI:2672118 MGI:MGI:88451 PANTHER:PTN002513067 WB:WBGene00001263 ZFIN:ZDB-GENE-030131-2281	P		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:88452 MGI:MGI:88468 PANTHER:PTN002513067 RGD:61817 RGD:70936 RGD:727898 UniProtKB:P02452 UniProtKB:P02458 UniProtKB:P02461 UniProtKB:P08123 UniProtKB:Q9BXS0	C		Seeded From UniProt	complete
part_of	GO:0005585	collagen type II trimer	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:88452 PANTHER:PTN001166557 UniProtKB:P02458	C		Seeded From UniProt	complete
part_of	GO:0005581	collagen trimer	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:88452 MGI:MGI:88458 PANTHER:PTN002771202	C		Seeded From UniProt	complete
enables	GO:0005201	extracellular matrix structural constituent	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:104687 MGI:MGI:2672118 MGI:MGI:88457 MGI:MGI:88467 PANTHER:PTN002513067 UniProtKB:P02461 UniProtKB:P02462 UniProtKB:P53420	F		Seeded From UniProt	complete
involved_in	GO:0001501	skeletal system development	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:88458 PANTHER:PTN002771202 UniProtKB:P02458	P		Seeded From UniProt	complete
enables	GO:0048407	platelet-derived growth factor binding	PMID:8900172^[16]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0043394	proteoglycan binding	PMID:29030641^[17]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:2001240	negative regulation of extrinsic apoptotic signaling pathway in absence of ligand	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28481 ensembl:ENSMUSP00000023123	P		Seeded From UniProt	complete
involved_in	GO:0097065	anterior head development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28481 ensembl:ENSMUSP00000023123	P		Seeded From UniProt	complete
involved_in	GO:0071773	cellular response to BMP stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28481 ensembl:ENSMUSP00000023123	P		Seeded From UniProt	complete
involved_in	GO:0071599	otic vesicle development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28481 ensembl:ENSMUSP00000023123	P		Seeded From UniProt	complete
involved_in	GO:0060351	cartilage development involved in endochondral bone morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28481 ensembl:ENSMUSP00000023123	P		Seeded From UniProt	complete
involved_in	GO:0060348	bone development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28481 ensembl:ENSMUSP00000023123	P		Seeded From UniProt	complete
involved_in	GO:0060174	limb bud formation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28481 ensembl:ENSMUSP00000023123	P		Seeded From UniProt	complete
involved_in	GO:0060021	roof of mouth development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28481 ensembl:ENSMUSP00000023123	P		Seeded From UniProt	complete
involved_in	GO:0051216	cartilage development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28481 ensembl:ENSMUSP00000023123	P		Seeded From UniProt	complete
involved_in	GO:0048839	inner ear development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28481 ensembl:ENSMUSP00000023123	P		Seeded From UniProt	complete
involved_in	GO:0048705	skeletal system morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28481 ensembl:ENSMUSP00000023123	P		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28481 ensembl:ENSMUSP00000023123	F		Seeded From UniProt	complete
involved_in	GO:0042472	inner ear morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28481 ensembl:ENSMUSP00000023123	P		Seeded From UniProt	complete
involved_in	GO:0035108	limb morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28481 ensembl:ENSMUSP00000023123	P		Seeded From UniProt	complete
part_of	GO:0031012	extracellular matrix	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28481 ensembl:ENSMUSP00000023123	C		Seeded From UniProt	complete
involved_in	GO:0030903	notochord development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28481 ensembl:ENSMUSP00000023123	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:P28481 ensembl:ENSMUSP00000023123	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:P28481 ensembl:ENSMUSP00000023123	P		Seeded From UniProt	complete
involved_in	GO:0007417	central nervous system development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28481 ensembl:ENSMUSP00000023123	P		Seeded From UniProt	complete
involved_in	GO:0006029	proteoglycan metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28481 ensembl:ENSMUSP00000023123	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28481 ensembl:ENSMUSP00000023123	C		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28481 ensembl:ENSMUSP00000023123	C		Seeded From UniProt	complete
part_of	GO:0005604	basement membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28481 ensembl:ENSMUSP00000023123	C		Seeded From UniProt	complete
part_of	GO:0005585	collagen type II trimer	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28481 ensembl:ENSMUSP00000023123	C		Seeded From UniProt	complete
part_of	GO:0005581	collagen trimer	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28481 ensembl:ENSMUSP00000023123	C		Seeded From UniProt	complete
involved_in	GO:0003007	heart morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28481 ensembl:ENSMUSP00000023123	P		Seeded From UniProt	complete
involved_in	GO:0002062	chondrocyte differentiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28481 ensembl:ENSMUSP00000023123	P		Seeded From UniProt	complete
involved_in	GO:0001958	endochondral ossification	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28481 ensembl:ENSMUSP00000023123	P		Seeded From UniProt	complete
involved_in	GO:0001894	tissue homeostasis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28481 ensembl:ENSMUSP00000023123	P		Seeded From UniProt	complete
involved_in	GO:0001503	ossification	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28481 ensembl:ENSMUSP00000023123	P		Seeded From UniProt	complete
involved_in	GO:0001502	cartilage condensation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28481 ensembl:ENSMUSP00000023123	P		Seeded From UniProt	complete
enables	GO:0005201	extracellular matrix structural constituent	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000885	F		Seeded From UniProt	complete
involved_in	GO:0051216	cartilage development	PMID:7550321^[18]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0050776	regulation of immune response	Reactome:R-HSA-198933	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:0005788	endoplasmic reticulum lumen	Reactome:R-HSA-8944266 Reactome:R-HSA-8944263 Reactome:R-HSA-2089971 Reactome:R-HSA-2022073	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	Reactome:R-HSA-5696356 Reactome:R-HSA-382054 Reactome:R-HSA-375151 Reactome:R-HSA-2473594 Reactome:R-HSA-2465890 Reactome:R-HSA-2424252 Reactome:R-HSA-2396370 Reactome:R-HSA-2327909 Reactome:R-HSA-2327738 Reactome:R-HSA-2327733 Reactome:R-HSA-2299620 Reactome:R-HSA-2213210 Reactome:R-HSA-2213208 Reactome:R-HSA-2213205 Reactome:R-HSA-2213201 Reactome:R-HSA-216043 Reactome:R-HSA-2089971 Reactome:R-HSA-2002440 Reactome:R-HSA-2002428 Reactome:R-HSA-1474266 Reactome:R-HSA-1474197 Reactome:R-HSA-1454757	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005581	collagen trimer	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0176	C		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		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.

↑ Banglmaier, RF et al. (2015) Induction and quantification of collagen fiber alignment in a three-dimensional hydroxyapatite-collagen composite scaffold. Acta Biomater 17 26-35 PubMed GONUTS page
↑ ^2.0 ^2.1 Ragelle, H et al. (2017) Comprehensive proteomic characterization of stem cell-derived extracellular matrices. Biomaterials 128 147-159 PubMed GONUTS page
↑ ^3.0 ^3.1 Glavey, SV et al. (2017) Proteomic characterization of human multiple myeloma bone marrow extracellular matrix. Leukemia 31 2426-2434 PubMed GONUTS page
↑ ^4.0 ^4.1 Barallobre-Barreiro, J et al. (2016) Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin Activity in Human Atrial Fibrillation. Circulation 134 817-32 PubMed GONUTS page
↑ ^5.0 ^5.1 Naba, A et al. (2017) Characterization of the Extracellular Matrix of Normal and Diseased Tissues Using Proteomics. J. Proteome Res. 16 3083-3091 PubMed GONUTS page
↑ Cai, L et al. (2010) Nonmuscle myosin-dependent synthesis of type I collagen. J. Mol. Biol. 401 564-78 PubMed GONUTS page
↑ Dessen, A et al. (1997) X-ray crystal structure of HLA-DR4 (DRA*0101, DRB1*0401) complexed with a peptide from human collagen II. Immunity 7 473-81 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
↑ Soteriou, D et al. (2013) Comparative proteomic analysis of supportive and unsupportive extracellular matrix substrates for human embryonic stem cell maintenance. J. Biol. Chem. 288 18716-31 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 Richards, AJ et al. (2006) High efficiency of mutation detection in type 1 stickler syndrome using a two-stage approach: vitreoretinal assessment coupled with exon sequencing for screening COL2A1. Hum. Mutat. 27 696-704 PubMed GONUTS page
↑ Su, MW et al. (1989) Nucleotide sequence of the full length cDNA encoding for human type II procollagen. Nucleic Acids Res. 17 9473 PubMed GONUTS page
↑ ^12.0 ^12.1 Bogaert, R et al. (1992) An amino acid substitution (Gly853-->Glu) in the collagen alpha 1(II) chain produces hypochondrogenesis. J. Biol. Chem. 267 22522-6 PubMed GONUTS page
↑ ^13.0 ^13.1 Diab, M et al. (1996) Collagen type IX from human cartilage: a structural profile of intermolecular cross-linking sites. Biochem. J. 314 ( Pt 1) 327-32 PubMed GONUTS page
↑ Annunen, S et al. (1999) Splicing mutations of 54-bp exons in the COL11A1 gene cause Marshall syndrome, but other mutations cause overlapping Marshall/Stickler phenotypes. Am. J. Hum. Genet. 65 974-83 PubMed GONUTS page
↑ ^15.0 ^15.1 ^15.2 ^15.3 ^15.4 ^15.5 ^15.6 ^15.7 ^15.8 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Somasundaram, R & Schuppan, D (1996) Type I, II, III, IV, V, and VI collagens serve as extracellular ligands for the isoforms of platelet-derived growth factor (AA, BB, and AB). J. Biol. Chem. 271 26884-91 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
↑ Tiller, GE et al. (1995) Dominant mutations in the type II collagen gene, COL2A1, produce spondyloepimetaphyseal dysplasia, Strudwick type. Nat. Genet. 11 87-9 PubMed GONUTS page

[PMID:25653215-1] Banglmaier, RF et al. (2015) Induction and quantification of collagen fiber alignment in a three-dimensional hydroxyapatite-collagen composite scaffold. Acta Biomater 17 26-35 PubMed GONUTS page

[PMID:28327460-2] 2.0 ^2.1 Ragelle, H et al. (2017) Comprehensive proteomic characterization of stem cell-derived extracellular matrices. Biomaterials 128 147-159 PubMed GONUTS page

[PMID:28344315-3] 3.0 ^3.1 Glavey, SV et al. (2017) Proteomic characterization of human multiple myeloma bone marrow extracellular matrix. Leukemia 31 2426-2434 PubMed GONUTS page

[PMID:27559042-4] 4.0 ^4.1 Barallobre-Barreiro, J et al. (2016) Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin Activity in Human Atrial Fibrillation. Circulation 134 817-32 PubMed GONUTS page

[PMID:28675934-5] 5.0 ^5.1 Naba, A et al. (2017) Characterization of the Extracellular Matrix of Normal and Diseased Tissues Using Proteomics. J. Proteome Res. 16 3083-3091 PubMed GONUTS page

[PMID:20603131-6] Cai, L et al. (2010) Nonmuscle myosin-dependent synthesis of type I collagen. J. Mol. Biol. 401 564-78 PubMed GONUTS page

[PMID:9354468-7] Dessen, A et al. (1997) X-ray crystal structure of HLA-DR4 (DRA*0101, DRB1*0401) complexed with a peptide from human collagen II. Immunity 7 473-81 PubMed GONUTS page

[PMID:27068509-8] 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:23658023-9] Soteriou, D et al. (2013) Comparative proteomic analysis of supportive and unsupportive extracellular matrix substrates for human embryonic stem cell maintenance. J. Biol. Chem. 288 18716-31 PubMed GONUTS page

[PMID:16752401-10] 10.0 ^10.1 ^10.2 Richards, AJ et al. (2006) High efficiency of mutation detection in type 1 stickler syndrome using a two-stage approach: vitreoretinal assessment coupled with exon sequencing for screening COL2A1. Hum. Mutat. 27 696-704 PubMed GONUTS page

[PMID:2587267-11] Su, MW et al. (1989) Nucleotide sequence of the full length cDNA encoding for human type II procollagen. Nucleic Acids Res. 17 9473 PubMed GONUTS page

[PMID:1429602-12] 12.0 ^12.1 Bogaert, R et al. (1992) An amino acid substitution (Gly853-->Glu) in the collagen alpha 1(II) chain produces hypochondrogenesis. J. Biol. Chem. 267 22522-6 PubMed GONUTS page

[PMID:8660302-13] 13.0 ^13.1 Diab, M et al. (1996) Collagen type IX from human cartilage: a structural profile of intermolecular cross-linking sites. Biochem. J. 314 ( Pt 1) 327-32 PubMed GONUTS page

[PMID:10486316-14] Annunen, S et al. (1999) Splicing mutations of 54-bp exons in the COL11A1 gene cause Marshall syndrome, but other mutations cause overlapping Marshall/Stickler phenotypes. Am. J. Hum. Genet. 65 974-83 PubMed GONUTS page

[PMID:21873635-15] 15.0 ^15.1 ^15.2 ^15.3 ^15.4 ^15.5 ^15.6 ^15.7 ^15.8 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:8900172-16] Somasundaram, R & Schuppan, D (1996) Type I, II, III, IV, V, and VI collagens serve as extracellular ligands for the isoforms of platelet-derived growth factor (AA, BB, and AB). J. Biol. Chem. 271 26884-91 PubMed GONUTS page

[PMID:29030641-17] 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:7550321-18] Tiller, GE et al. (1995) Dominant mutations in the type II collagen gene, COL2A1, produce spondyloepimetaphyseal dysplasia, Strudwick type. Nat. Genet. 11 87-9 PubMed GONUTS page

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