HUMAN:CO3A1

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	COL3A1
Protein Name(s)	Collagen alpha-1(III) chain
External Links
UniProt	P02461
EMBL	X14420 AY054301 AY016295 KC567894 GU143397 AC066694 CH471058 CH471058 BC028178 M26939 X07240 X15332 S62925 S79877 M59312 M59227 M55603 X06700 X01655 X01742 M13146 M11134 M10795 M10615 M10793 M10794 M10800 M10801
CCDS	CCDS2297.1
PIR	S05272
RefSeq	NP_000081.1
UniGene	Hs.443625
PDB	2V53 3DMW 4AE2 4AEJ 4AK3 4GYX
PDBsum	2V53 3DMW 4AE2 4AEJ 4AK3 4GYX
ProteinModelPortal	P02461
SMR	P02461
BioGrid	107678
DIP	DIP-57177N
IntAct	P02461
MINT	MINT-7299332
ChEMBL	CHEMBL2364188
DrugBank	DB00048
PhosphoSite	P02461
DMDM	124056490
PaxDb	P02461
PRIDE	P02461
Ensembl	ENST00000304636 ENST00000317840
GeneID	1281
KEGG	hsa:1281
UCSC	uc002uqj.1
CTD	1281
GeneCards	GC02P189803
GeneReviews	COL3A1
HGNC	HGNC:2201
HPA	CAB016766 HPA007583
MIM	100070 120180 130020 130050
neXtProt	NX_P02461
Orphanet	2500 286 86 231160
PharmGKB	PA26716
eggNOG	NOG12793
GeneTree	ENSGT00770000120467
HOVERGEN	HBG004933
InParanoid	P02461
KO	K06236
OMA	PGPSGHQ
OrthoDB	EOG7TJ3HH
PhylomeDB	P02461
TreeFam	TF344135
Reactome	REACT_118779 REACT_121139 REACT_13552 REACT_150180 REACT_150401 REACT_163699 REACT_163874 REACT_163906 REACT_163942 REACT_16888 REACT_18312
ChiTaRS	COL3A1
EvolutionaryTrace	P02461
GeneWiki	Collagen,_type_III,_alpha_1
GenomeRNAi	1281
NextBio	35489581
PRO	PR:P02461
Proteomes	UP000005640
Bgee	P02461
ExpressionAtlas	P02461
Genevestigator	P02461
GO	GO:0005586 GO:0005788 GO:0031012 GO:0005576 GO:0005615 GO:0005201 GO:0005178 GO:0046872 GO:0048407 GO:0007568 GO:0007411 GO:0001568 GO:0007160 GO:0071230 GO:0021987 GO:0030574 GO:0030199 GO:0048565 GO:0043206 GO:0022617 GO:0030198 GO:0007507 GO:0007229 GO:0050777 GO:2001223 GO:0018149 GO:0030168 GO:0035025 GO:0034097 GO:0009612 GO:0009314 GO:0001501 GO:0043588 GO:0007179 GO:0042060
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:0032966	negative regulation of collagen biosynthetic process	PMID:24288677^[1]	ECO:0000314			P		Figure 5 depicts through immunofluorescence, nAG protein expression in human fibroblast cells has an inhibitory effect on the expression of collagen I and III.	complete CACAO 9313
Contributes to	GO:0032966	negative regulation of collagen biosynthetic process	PMID:24288677^[1]	ECO:0000314			P		Figure 4 displays a western blot assay showing collagen III expression in untreated control fibroblasts and control fibroblasts treated with TGF-β1. With TGF-β1 treatment, there was also decreased collagen III expression in transfected fibroblasts. This shows that the inhibitory effect of nAG is dominant over the TGF-β1 effect.	complete CACAO 9322
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
enables	GO:0030020	extracellular matrix structural constituent conferring tensile strength	PMID:25037231^[6]	ECO:0007666	automatically integrated combinatorial computational and experimental evidence used in manual assertion		F	occurs_in:(UBERON:0001155)	Seeded From UniProt	complete
part_of	GO:0062023	collagen-containing extracellular matrix	PMID:25037231^[6]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0002107)	Seeded From UniProt	complete
part_of	GO:0062023	collagen-containing extracellular matrix	PMID:25037231^[6]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001155)	Seeded From UniProt	complete
enables	GO:0030020	extracellular matrix structural constituent conferring tensile strength	PMID:25037231^[6]	ECO:0007666	automatically integrated combinatorial computational and experimental evidence used in manual assertion		F	occurs_in:(UBERON:0002107)	Seeded From UniProt	complete
enables	GO:0002020	protease binding	PMID:19932771^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P39900	F		Seeded From UniProt	complete
part_of	GO:0005586	collagen type III trimer	PMID:19932771^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		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
involved_in	GO:2001223	negative regulation of neuron migration	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P08121	P		Seeded From UniProt	complete
involved_in	GO:0050777	negative regulation of immune response	PMID:16754721^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043588	skin development	PMID:9036918^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0097435	supramolecular fiber organization	PMID:14970208^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042060	wound healing	PMID:1466622^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042060	wound healing	PMID:14736764^[13]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0035025	positive regulation of Rho protein signal transduction	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P08121	P		Seeded From UniProt	complete
involved_in	GO:0034097	response to cytokine	PMID:9076960^[14]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034097	response to cytokine	PMID:16360482^[15]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0062023	collagen-containing extracellular matrix	PMID:14970208^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0062023	collagen-containing extracellular matrix	PMID:7487954^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0030199	collagen fibril organization	PMID:7546986^[17]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030199	collagen fibril organization	PMID:9036918^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030199	collagen fibril organization	PMID:1672129^[18]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030168	platelet activation	PMID:9573018^[19]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0021987	cerebral cortex development	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P08121	P		Seeded From UniProt	complete
involved_in	GO:0018149	peptide cross-linking	PMID:16754721^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0009314	response to radiation	PMID:14736764^[13]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007507	heart development	PMID:7546986^[17]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007229	integrin-mediated signaling pathway	PMID:14970208^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007179	transforming growth factor beta receptor signaling pathway	PMID:16360482^[15]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007160	cell-matrix adhesion	PMID:16912226^[20]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:7487954^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:9036918^[10]	ECO:0000303	author statement without traceable support used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005586	collagen type III trimer	PMID:17576241^[21]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005586	collagen type III trimer	PMID:7487954^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005586	collagen type III trimer	PMID:1672129^[18]	ECO:0000303	author statement without traceable support used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005201	extracellular matrix structural constituent	PMID:7487954^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0005201	extracellular matrix structural constituent	PMID:9036918^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0005178	integrin binding	PMID:9573018^[19]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0005178	integrin binding	PMID:14970208^[11]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0031012	extracellular matrix	PMID:21873635^[22]	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:0030198	extracellular matrix organization	PMID:21873635^[22]	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^[22]	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:0005586	collagen type III trimer	PMID:21873635^[22]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:88453 PANTHER:PTN002770836 UniProtKB:P02461	C		Seeded From UniProt	complete
enables	GO:0005201	extracellular matrix structural constituent	PMID:21873635^[22]	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
enables	GO:0048407	platelet-derived growth factor binding	PMID:8900172^[23]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:2001223	negative regulation of neuron migration	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P08121 ensembl:ENSMUSP00000085192	P		Seeded From UniProt	complete
involved_in	GO:0071230	cellular response to amino acid stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P08121 ensembl:ENSMUSP00000085192	P		Seeded From UniProt	complete
involved_in	GO:0060414	aorta smooth muscle tissue morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P08121 ensembl:ENSMUSP00000085192	P		Seeded From UniProt	complete
involved_in	GO:0048565	digestive tract development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P08121 ensembl:ENSMUSP00000085192	P		Seeded From UniProt	complete
enables	GO:0046332	SMAD binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P08121 ensembl:ENSMUSP00000085192	F		Seeded From UniProt	complete
involved_in	GO:0035025	positive regulation of Rho protein signal transduction	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P08121 ensembl:ENSMUSP00000085192	P		Seeded From UniProt	complete
part_of	GO:0031012	extracellular matrix	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P08121 ensembl:ENSMUSP00000085192	C		Seeded From UniProt	complete
involved_in	GO:0030199	collagen fibril organization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P08121 ensembl:ENSMUSP00000085192	P		Seeded From UniProt	complete
involved_in	GO:0021987	cerebral cortex development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P08121 ensembl:ENSMUSP00000085192	P		Seeded From UniProt	complete
part_of	GO:0005586	collagen type III trimer	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P08121 ensembl:ENSMUSP00000085192	C		Seeded From UniProt	complete
part_of	GO:0005581	collagen trimer	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P08121 ensembl:ENSMUSP00000085192	C		Seeded From UniProt	complete
involved_in	GO:0001568	blood vessel development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P08121 ensembl:ENSMUSP00000085192	P		Seeded From UniProt	complete
part_of	GO:0062023	collagen-containing extracellular matrix	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P13941 ensembl:ENSRNOP00000004956	C		Seeded From UniProt	complete
involved_in	GO:0009612	response to mechanical stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P13941 ensembl:ENSRNOP00000004956	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:P13941 ensembl:ENSRNOP00000004956	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
colocalizes_with	GO:0062023	collagen-containing extracellular matrix	PMID:22261194^[24]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	part_of:(UBERON:0002084)	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-8944240 Reactome:R-HSA-2089971 Reactome:R-HSA-2022073 Reactome:R-HSA-2002460 Reactome:R-HSA-1650808	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-5696357 Reactome:R-HSA-5696356 Reactome:R-HSA-382054 Reactome:R-HSA-375151 Reactome:R-HSA-2473584 Reactome:R-HSA-2465890 Reactome:R-HSA-2396370 Reactome:R-HSA-2327909 Reactome:R-HSA-2327738 Reactome:R-HSA-2327733 Reactome:R-HSA-2327695 Reactome:R-HSA-2213201 Reactome:R-HSA-2089971 Reactome:R-HSA-2002440 Reactome:R-HSA-2002428 Reactome:R-HSA-1474266 Reactome:R-HSA-1474213 Reactome:R-HSA-1474210 Reactome:R-HSA-1454757	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		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
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: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
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Notes

References

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

↑ ^1.0 ^1.1 Al-Qattan, MM et al. (2013) Salamander-derived, human-optimized nAG protein suppresses collagen synthesis and increases collagen degradation in primary human fibroblasts. Biomed Res Int 2013 384091 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
↑ ^6.0 ^6.1 ^6.2 ^6.3 Naba, A et al. (2014) Extracellular matrix signatures of human primary metastatic colon cancers and their metastases to liver. BMC Cancer 14 518 PubMed GONUTS page
↑ ^7.0 ^7.1 Taddese, S et al. (2010) MMP-12 catalytic domain recognizes and cleaves at multiple sites in human skin collagen type I and type III. Biochim. Biophys. Acta 1804 731-9 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
↑ ^9.0 ^9.1 Lebbink, RJ et al. (2006) Collagens are functional, high affinity ligands for the inhibitory immune receptor LAIR-1. J. Exp. Med. 203 1419-25 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 Smith, LT et al. (1997) Mutations in the COL3A1 gene result in the Ehlers-Danlos syndrome type IV and alterations in the size and distribution of the major collagen fibrils of the dermis. J. Invest. Dermatol. 108 241-7 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 ^11.3 Zoppi, N et al. (2004) Human fibroblasts with mutations in COL5A1 and COL3A1 genes do not organize collagens and fibronectin in the extracellular matrix, down-regulate alpha2beta1 integrin, and recruit alphavbeta3 Instead of alpha5beta1 integrin. J. Biol. Chem. 279 18157-68 PubMed GONUTS page
↑ Rasmussen, LH et al. (1992) Collagen types I and III propeptides as markers of healing in chronic leg ulcers. A noninvasive method for the determination of procollagen propeptides in wound fluid--influence of growth hormone. Ann. Surg. 216 684-91 PubMed GONUTS page
↑ ^13.0 ^13.1 Constable, PH et al. (2004) The effects of single doses of beta radiation on the wound healing behaviour of human Tenon's capsule fibroblasts. Br J Ophthalmol 88 169-73 PubMed GONUTS page
↑ Diaz, A & Jiménez, SA (1997) Interferon-gamma regulates collagen and fibronectin gene expression by transcriptional and post-transcriptional mechanisms. Int. J. Biochem. Cell Biol. 29 251-60 PubMed GONUTS page
↑ ^15.0 ^15.1 Howard, PS et al. (2005) Transforming growth factor-beta1-induced hypertrophy and matrix expression in human bladder smooth muscle cells. Urology 66 1349-53 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 ^16.3 Chiodo, AA et al. (1995) Abnormal type III collagen produced by an exon-17-skipping mutation of the COL3A1 gene in Ehlers-Danlos syndrome type IV is not incorporated into the extracellular matrix. Biochem. J. 311 ( Pt 3) 939-43 PubMed GONUTS page
↑ ^17.0 ^17.1 Adès, LC et al. (1995) Myocardial infarction resulting from coronary artery dissection in an adolescent with Ehlers-Danlos syndrome type IV due to a type III collagen mutation. Br Heart J 74 112-6 PubMed GONUTS page
↑ ^18.0 ^18.1 Lee, B et al. (1991) G to T transversion at position +5 of a splice donor site causes skipping of the preceding exon in the type III procollagen transcripts of a patient with Ehlers-Danlos syndrome type IV. J. Biol. Chem. 266 5256-9 PubMed GONUTS page
↑ ^19.0 ^19.1 Verkleij, MW et al. (1998) Simple collagen-like peptides support platelet adhesion under static but not under flow conditions: interaction via alpha2 beta1 and von Willebrand factor with specific sequences in native collagen is a requirement to resist shear forces. Blood 91 3808-16 PubMed GONUTS page
↑ Lisman, T et al. (2006) A single high-affinity binding site for von Willebrand factor in collagen III, identified using synthetic triple-helical peptides. Blood 108 3753-6 PubMed GONUTS page
↑ Wang, Q et al. (2007) RNAi-mediated inhibition of COL1A1 and COL3A1 in human skin fibroblasts. Exp. Dermatol. 16 611-7 PubMed GONUTS page
↑ ^22.0 ^22.1 ^22.2 ^22.3 ^22.4 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
↑ Barallobre-Barreiro, J et al. (2012) Proteomics analysis of cardiac extracellular matrix remodeling in a porcine model of ischemia/reperfusion injury. Circulation 125 789-802 PubMed GONUTS page

[PMID:24288677-1] 1.0 ^1.1 Al-Qattan, MM et al. (2013) Salamander-derived, human-optimized nAG protein suppresses collagen synthesis and increases collagen degradation in primary human fibroblasts. Biomed Res Int 2013 384091 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

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[PMID:19932771-7] 7.0 ^7.1 Taddese, S et al. (2010) MMP-12 catalytic domain recognizes and cleaves at multiple sites in human skin collagen type I and type III. Biochim. Biophys. Acta 1804 731-9 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

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[PMID:9036918-10] 10.0 ^10.1 ^10.2 ^10.3 Smith, LT et al. (1997) Mutations in the COL3A1 gene result in the Ehlers-Danlos syndrome type IV and alterations in the size and distribution of the major collagen fibrils of the dermis. J. Invest. Dermatol. 108 241-7 PubMed GONUTS page

[PMID:14970208-11] 11.0 ^11.1 ^11.2 ^11.3 Zoppi, N et al. (2004) Human fibroblasts with mutations in COL5A1 and COL3A1 genes do not organize collagens and fibronectin in the extracellular matrix, down-regulate alpha2beta1 integrin, and recruit alphavbeta3 Instead of alpha5beta1 integrin. J. Biol. Chem. 279 18157-68 PubMed GONUTS page

[PMID:1466622-12] Rasmussen, LH et al. (1992) Collagen types I and III propeptides as markers of healing in chronic leg ulcers. A noninvasive method for the determination of procollagen propeptides in wound fluid--influence of growth hormone. Ann. Surg. 216 684-91 PubMed GONUTS page

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[PMID:9076960-14] Diaz, A & Jiménez, SA (1997) Interferon-gamma regulates collagen and fibronectin gene expression by transcriptional and post-transcriptional mechanisms. Int. J. Biochem. Cell Biol. 29 251-60 PubMed GONUTS page

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[PMID:9573018-19] 19.0 ^19.1 Verkleij, MW et al. (1998) Simple collagen-like peptides support platelet adhesion under static but not under flow conditions: interaction via alpha2 beta1 and von Willebrand factor with specific sequences in native collagen is a requirement to resist shear forces. Blood 91 3808-16 PubMed GONUTS page

[PMID:16912226-20] Lisman, T et al. (2006) A single high-affinity binding site for von Willebrand factor in collagen III, identified using synthetic triple-helical peptides. Blood 108 3753-6 PubMed GONUTS page

[PMID:17576241-21] Wang, Q et al. (2007) RNAi-mediated inhibition of COL1A1 and COL3A1 in human skin fibroblasts. Exp. Dermatol. 16 611-7 PubMed GONUTS page

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HUMAN:CO3A1

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