Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P12110 (CO6A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 166. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-2(VI) chain
Gene names
Name:COL6A2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1019 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Collagen VI acts as a cell-binding protein.

Subunit structure

Trimers composed of three different chains: alpha-1(VI), alpha-2(VI), and alpha-3(VI) or alpha-5(VI) or alpha-6(VI). Interacts with CSPG4. Ref.14

Subcellular location

Secretedextracellular spaceextracellular matrix. Membrane; Peripheral membrane protein. Note: Recruited on membranes by CSPG4. Ref.13

Post-translational modification

Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.

Involvement in disease

Bethlem myopathy (BM) [MIM:158810]: A benign autosomal dominant proximal myopathy characterized by early childhood onset and joint contractures most frequently affecting the elbows and ankles.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17 Ref.18 Ref.20 Ref.21

Ullrich congenital muscular dystrophy (UCMD) [MIM:254090]: UCMD is a congenital myopathy characterized by muscle weakness and multiple joint contractures, generally noted at birth or early infancy. The clinical course is more severe than in Bethlem myopathy.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.19 Ref.20

Myosclerosis autosomal recessive (MYOSAR) [MIM:255600]: A condition characterized by chronic inflammation of skeletal muscle with hyperplasia of the interstitial connective tissue. The clinical picture includes slender muscles with firm 'woody' consistency and restriction of movement of many joints because of muscle contractures.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Sequence similarities

Belongs to the type VI collagen family.

Contains 3 VWFA domains.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DISC1Q9NRI53EBI-928749,EBI-529989

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2C2 (identifier: P12110-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2C2A (identifier: P12110-2)

The sequence of this isoform differs from the canonical sequence as follows:
     821-991: ELSVAQCTQR...MDVLTTLSLG → DAPWPGGEPP...GDPETALALC
     992-1019: Missing.
Isoform 2C2A' (identifier: P12110-3)

The sequence of this isoform differs from the canonical sequence as follows:
     821-828: ELSVAQCT → GLDGAVLC
     829-1019: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 1019999Collagen alpha-2(VI) chain
PRO_0000005832

Regions

Domain46 – 234189VWFA 1
Domain615 – 805191VWFA 2
Domain833 – 1014182VWFA 3
Region21 – 256236Nonhelical region
Region257 – 590334Triple-helical region
Region591 – 1019429Nonhelical region
Motif366 – 3683Cell attachment site Potential
Motif426 – 4283Cell attachment site Potential
Motif489 – 4913Cell attachment site Potential
Motif498 – 5003Cell attachment site Potential
Motif539 – 5413Cell attachment site Potential

Amino acid modifications

Modified residue7011Phosphothreonine Ref.16
Modified residue7031Phosphothreonine Ref.16
Modified residue7051Phosphoserine Ref.16
Glycosylation1401N-linked (GlcNAc...) Ref.15
Glycosylation3271N-linked (GlcNAc...) Potential
Glycosylation6301N-linked (GlcNAc...) Potential
Glycosylation7851N-linked (GlcNAc...) Ref.15
Glycosylation8971N-linked (GlcNAc...) Ref.15
Glycosylation9541N-linked (GlcNAc...) Ref.15

Natural variations

Alternative sequence821 – 991171ELSVA…TLSLG → DAPWPGGEPPVTFLRTEEGP DATFPRTIPLIQQLLNATEL TQDPAAYSQLVAVLVYTAER AKFATGVERQDWMELFIDTF KLVHRDIVGDPETALALC in isoform 2C2A.
VSP_001163
Alternative sequence821 – 8288ELSVAQCT → GLDGAVLC in isoform 2C2A'.
VSP_001161
Alternative sequence829 – 1019191Missing in isoform 2C2A'.
VSP_001162
Alternative sequence992 – 101928Missing in isoform 2C2A.
VSP_001164
Natural variant1061E → K in BM. Ref.20
Corresponds to variant rs141703710 [ dbSNP | Ensembl ].
VAR_058225
Natural variant2271D → N. Ref.1 Ref.19 Ref.20 Ref.21
Corresponds to variant rs35881321 [ dbSNP | Ensembl ].
VAR_048801
Natural variant2711G → S in BM. Ref.17
VAR_013589
Natural variant2831G → R in UCMD. Ref.20
VAR_058226
Natural variant3991S → N. Ref.1 Ref.2 Ref.7 Ref.19 Ref.20 Ref.21
Corresponds to variant rs2839110 [ dbSNP | Ensembl ].
VAR_030315
Natural variant4891R → Q. Ref.20
Corresponds to variant rs61735828 [ dbSNP | Ensembl ].
VAR_058227
Natural variant4981R → H in UCMD. Ref.20
VAR_058228
Natural variant5181P → S. Ref.20
Corresponds to variant rs141166141 [ dbSNP | Ensembl ].
VAR_058229
Natural variant5311G → R in UCMD. Ref.20
VAR_058230
Natural variant6211D → N in BM. Ref.18
VAR_013590
Natural variant6801R → H. Ref.1 Ref.11 Ref.19 Ref.20 Ref.21
Corresponds to variant rs1042917 [ dbSNP | Ensembl ].
VAR_030316
Natural variant7001G → S in BM. Ref.20
VAR_058231
Natural variant7241R → C. Ref.20
VAR_058232
Natural variant7771C → R in BM. Ref.20
VAR_058233
Natural variant7841R → H in UCMD. Ref.20
Corresponds to variant rs75120695 [ dbSNP | Ensembl ].
VAR_058234
Natural variant8041V → G. Ref.20
VAR_058235
Natural variant8371L → P in UCMD; prevents collagen VI assembly. Ref.19
VAR_058236
Natural variant8531R → Q in BM. Ref.20
Corresponds to variant rs144830948 [ dbSNP | Ensembl ].
VAR_058237
Natural variant8761R → S in UCMD. Ref.20
VAR_058238
Natural variant8951S → R. Ref.21
Corresponds to variant rs141233891 [ dbSNP | Ensembl ].
VAR_058239
Natural variant8971Missing in UCMD; results in severe collagen VI matrix deficiencies. Ref.19
VAR_058240
Natural variant9321P → L in BM; results in reduced intracellular collagen VI assembly and secretion. Ref.21
VAR_058241
Natural variant9351G → R. Ref.20
Corresponds to variant rs35548026 [ dbSNP | Ensembl ].
VAR_048802
Natural variant10151I → L.
Corresponds to variant rs11910483 [ dbSNP | Ensembl ].
VAR_048803

Experimental info

Sequence conflict5071K → S in AAB20836. Ref.7
Sequence conflict966 – 9672KQ → NE in AAA52056. Ref.1
Sequence conflict966 – 9672KQ → NE in AAA35620. Ref.11

Sequences

Sequence LengthMass (Da)Tools
Isoform 2C2 [UniParc].

Last modified February 6, 2007. Version 4.
Checksum: 6C513ADE46C1D111

FASTA1,019108,579
        10         20         30         40         50         60 
MLQGTCSVLL LWGILGAIQA QQQEVISPDT TERNNNCPEK TDCPIHVYFV LDTSESVTMQ 

        70         80         90        100        110        120 
SPTDILLFHM KQFVPQFISQ LQNEFYLDQV ALSWRYGGLH FSDQVEVFSP PGSDRASFIK 

       130        140        150        160        170        180 
NLQGISSFRR GTFTDCALAN MTEQIRQDRS KGTVHFAVVI TDGHVTGSPC GGIKLQAERA 

       190        200        210        220        230        240 
REEGIRLFAV APNQNLKEQG LRDIASTPHE LYRNDYATML PDSTEIDQDT INRIIKVMKH 

       250        260        270        280        290        300 
EAYGECYKVS CLEIPGPSGP KGYRGQKGAK GNMGEPGEPG QKGRQGDPGI EGPIGFPGPK 

       310        320        330        340        350        360 
GVPGFKGEKG EFGADGRKGA PGLAGKNGTD GQKGKLGRIG PPGCKGDPGN RGPDGYPGEA 

       370        380        390        400        410        420 
GSPGERGDQG GKGDPGRPGR RGPPGEIGAK GSKGYQGNSG APGSPGVKGA KGGPGPRGPK 

       430        440        450        460        470        480 
GEPGRRGDPG TKGSPGSDGP KGEKGDPGPE GPRGLAGEVG NKGAKGDRGL PGPRGPQGAL 

       490        500        510        520        530        540 
GEPGKQGSRG DPGDAGPRGD SGQPGPKGDP GRPGFSYPGP RGAPGEKGEP GPRGPEGGRG 

       550        560        570        580        590        600 
DFGLKGEPGR KGEKGEPADP GPPGEPGPRG PRGVPGPEGE PGPPGDPGLT ECDVMTYVRE 

       610        620        630        640        650        660 
TCGCCDCEKR CGALDVVFVI DSSESIGYTN FTLEKNFVIN VVNRLGAIAK DPKSETGTRV 

       670        680        690        700        710        720 
GVVQYSHEGT FEAIQLDDER IDSLSSFKEA VKNLEWIAGG TWTPSALKFA YDRLIKESRR 

       730        740        750        760        770        780 
QKTRVFAVVI TDGRHDPRDD DLNLRALCDR DVTVTAIGIG DMFHEKHESE NLYSIACDKP 

       790        800        810        820        830        840 
QQVRNMTLFS DLVAEKFIDD MEDVLCPDPQ IVCPDLPCQT ELSVAQCTQR PVDIVFLLDG 

       850        860        870        880        890        900 
SERLGEQNFH KARRFVEQVA RRLTLARRDD DPLNARVALL QFGGPGEQQV AFPLSHNLTA 

       910        920        930        940        950        960 
IHEALETTQY LNSFSHVGAG VVHAINAIVR SPRGGARRHA ELSFVFLTDG VTGNDSLHES 

       970        980        990       1000       1010 
AHSMRKQNVV PTVLALGSDV DMDVLTTLSL GDRAAVFHEK DYDSLAQPGF FDRFIRWIC 

« Hide

Isoform 2C2A [UniParc].

Checksum: 336CB9B6FC8394D8
Show »

FASTA91897,419
Isoform 2C2A' [UniParc].

Checksum: 9690A499C8E8827F
Show »

FASTA82887,280

References

« Hide 'large scale' references
[1]Chu M.-L.
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2C2), SEQUENCE REVISION, VARIANTS ASN-227; ASN-399 AND HIS-680.
Tissue: Fibroblast and Placenta.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2C2), VARIANT ASN-399.
Tissue: Ovary.
[3]"Human alpha 2(VI) collagen gene. Heterogeneity at the 5'-untranslated region generated by an alternate exon."
Saitta B., Timpl R., Chu M.-L.
J. Biol. Chem. 267:6188-6196(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-266, ALTERNATIVE SPLICING.
[4]"Sequence analysis of alpha 1(VI) and alpha 2(VI) chains of human type VI collagen reveals internal triplication of globular domains similar to the A domains of von Willebrand factor and two alpha 2(VI) chain variants that differ in the carboxy terminus."
Chu M.-L., Pan T.-C., Conway D., Kuo H.J., Glanville R.W., Timpl R., Mann K., Deutzmann R.
EMBO J. 8:1939-1946(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-255 AND 591-1019, NUCLEOTIDE SEQUENCE [MRNA] OF 821-1019 (ISOFORM 2C2A).
Tissue: Fibroblast and Placenta.
[5]"Recombinant expression and structural and binding properties of alpha 1(VI) and alpha 2(VI) chains of human collagen type VI."
Tillet E., Wiedemann H., Golbik R., Pan T.-C., Zhang R.Z., Mann K., Chu M.-L., Timpl R.
Eur. J. Biochem. 221:177-185(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 179-185 AND 581-594.
[6]"Characterization of three constituent chains of collagen type VI by peptide sequences and cDNA clones."
Chu M.-L., Mann K., Deutzmann R., Pribula-Conway D., Hsu-Chen C.-C., Bernard M.P., Timpl R.
Eur. J. Biochem. 168:309-317(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 238-299.
[7]"The exon organization of the triple-helical coding regions of the human alpha 1(VI) and alpha 2(VI) collagen genes is highly similar."
Saitta B., Wang Y.-M., Renkart L., Zhang R.-Z., Pan T.-C., Timpl R., Chu M.-L.
Genomics 11:145-153(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 246-590, VARIANT ASN-399.
[8]"Further characterization of the three polypeptide chains of bovine and human short-chain collagen (intima collagen)."
Jander R., Rauterberg J., Glanville R.W.
Eur. J. Biochem. 133:39-46(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 251-264.
[9]"Amino acid sequence of the triple-helical domain of human collagen type VI."
Chu M.-L., Conway D., Pan T.-C., Baldwin C., Mann K., Deutzmann R., Timpl R.
J. Biol. Chem. 263:18601-18606(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 256-590.
[10]"Cloning and chromosomal localization of human genes encoding the three chains of type VI collagen."
Weil D., Mattei M.-G., Passage E., N'Guyen V.C., Pribula-Conway D., Mann K., Deutzmann R., Timpl R., Chu M.-L.
Am. J. Hum. Genet. 42:435-445(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 316-359.
Tissue: Placenta.
[11]"Alternative splicing of the human alpha 2(VI) collagen gene generates multiple mRNA transcripts which predict three protein variants with distinct carboxyl termini."
Saitta B., Stokes D.G., Vissing H., Timpl R., Chu M.-L.
J. Biol. Chem. 265:6473-6480(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 591-1019, ALTERNATIVE SPLICING, VARIANT HIS-680.
[12]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 820-1019 (ISOFORM 2C2).
Tissue: Uterus.
[13]"Expression of NG2 proteoglycan causes retention of type VI collagen on the cell surface."
Nishiyama A., Stallcup W.B.
Mol. Biol. Cell 4:1097-1108(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[14]"The membrane-spanning proteoglycan NG2 binds to collagens V and VI through the central nonglobular domain of its core protein."
Tillet E., Ruggiero F., Nishiyama A., Stallcup W.B.
J. Biol. Chem. 272:10769-10776(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CSPG4.
[15]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-140; ASN-785; ASN-897 AND ASN-954.
Tissue: Liver.
[16]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-701; THR-703 AND SER-705, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"Type VI collagen mutations in Bethlem myopathy, an autosomal dominant myopathy with contractures."
Joebsis G.J., Keizers H., Vreijling J.P., de Visser M., Speer M.C., Wolterman R.A., Baas F., Bohlhuis P.A.
Nat. Genet. 14:113-115(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BM SER-271.
[18]"Novel mutations in collagen VI genes: expansion of the Bethlem myopathy phenotype."
Scacheri P.C., Gillanders E.M., Subramony S.H., Vedanarayanan V., Crowe C.A., Thakore N., Bingler M., Hoffman E.P.
Neurology 58:593-602(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BM ASN-621.
[19]"Dominant collagen VI mutations are a common cause of Ullrich congenital muscular dystrophy."
Baker N.L., Moergelin M., Peat R., Goemans N., North K.N., Bateman J.F., Lamande S.R.
Hum. Mol. Genet. 14:279-293(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS UCMD PRO-837 AND ASN-897 DEL, CHARACTERIZATION OF VARIANTS UCMD PRO-837 AND ASN-897 DEL, VARIANTS ASN-227; ASN-399 AND HIS-680.
[20]"Automated genomic sequence analysis of the three collagen VI genes: applications to Ullrich congenital muscular dystrophy and Bethlem myopathy."
Lampe A.K., Dunn D.M., von Niederhausern A.C., Hamil C., Aoyagi A., Laval S.H., Marie S.K., Chu M.-L., Swoboda K., Muntoni F., Bonnemann C.G., Flanigan K.M., Bushby K.M.D., Weiss R.B.
J. Med. Genet. 42:108-120(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BM LYS-106; SER-700; ARG-777 AND GLN-853, VARIANTS UCMD ARG-283; HIS-498; ARG-531; ARG-777; HIS-784 AND SER-876, VARIANTS ASN-227; ASN-399; GLN-489; SER-518; HIS-680; CYS-724; GLY-804 AND ARG-935.
[21]"Molecular consequences of dominant Bethlem myopathy collagen VI mutations."
Baker N.L., Moergelin M., Pace R.A., Peat R.A., Adams N.E., Gardner R.J., Rowland L.P., Miller G., De Jonghe P., Ceulemans B., Hannibal M.C., Edwards M., Thompson E.M., Jacobson R., Quinlivan R.C.M., Aftimos S., Kornberg A.J., North K.N., Bateman J.F., Lamande S.R.
Ann. Neurol. 62:390-405(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BM LEU-932, VARIANTS ASN-227; ASN-399; HIS-680 AND ARG-895.
[22]"Autosomal recessive myosclerosis myopathy is a collagen VI disorder."
Merlini L., Martoni E., Grumati P., Sabatelli P., Squarzoni S., Urciuolo A., Ferlini A., Gualandi F., Bonaldo P.
Neurology 71:1245-1253(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MYOSCLEROSIS.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY029208 mRNA. Translation: AAA52056.2.
BC065509 mRNA. Translation: AAH65509.1.
M81835 Genomic DNA. No translation available.
X15977 mRNA. Translation: CAA34099.1.
X06195 mRNA. Translation: CAA29556.1.
S75462 expand/collapse EMBL AC list , S75425, S75428, S75430, S75432, S75434, S75436, S75438, S75440, S75442, S75444, S75446, S75448, S75450, S75452, S75454, S75456, S75458, S75460 Genomic DNA. Translation: AAB20836.1.
M34572, M34571 mRNA. Translation: AAA35618.1.
M34572, M34571 mRNA. Translation: AAA35619.1.
M34573, M34571 mRNA. Translation: AAA35620.1.
M34570 mRNA. Translation: AAA35621.1.
AL096746 mRNA. Translation: CAB46421.2.
PIRCGHU2A. S05378.
S09646.
T12549.
RefSeqNP_001840.3. NM_001849.3.
NP_478054.2. NM_058174.2.
NP_478055.2. NM_058175.2.
UniGeneHs.420269.

3D structure databases

ProteinModelPortalP12110.
SMRP12110. Positions 44-211, 615-782, 830-1019.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107689. 3 interactions.
IntActP12110. 3 interactions.

Chemistry

ChEMBLCHEMBL2364188.

PTM databases

PhosphoSiteP12110.

Polymorphism databases

DMDM125987812.

2D gel databases

REPRODUCTION-2DPAGEP12110.

Proteomic databases

PaxDbP12110.
PRIDEP12110.

Protocols and materials databases

DNASU1292.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000300527; ENSP00000300527; ENSG00000142173. [P12110-1]
ENST00000310645; ENSP00000312529; ENSG00000142173. [P12110-3]
ENST00000357838; ENSP00000350497; ENSG00000142173. [P12110-2]
ENST00000397763; ENSP00000380870; ENSG00000142173. [P12110-2]
ENST00000409416; ENSP00000387115; ENSG00000142173. [P12110-3]
GeneID1292.
KEGGhsa:1292.
UCSCuc002zhy.1. human. [P12110-3]
uc002zhz.1. human. [P12110-2]
uc002zia.1. human. [P12110-1]

Organism-specific databases

CTD1292.
GeneCardsGC21P047518.
H-InvDBHIX0016186.
HGNCHGNC:2212. COL6A2.
HPAHPA007029.
MIM120240. gene.
158810. phenotype.
254090. phenotype.
255600. phenotype.
neXtProtNX_P12110.
Orphanet610. Bethlem myopathy.
75840. Congenital muscular dystrophy, Ullrich type.
289380. Myosclerosis.
PharmGKBPA26728.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG256042.
HOVERGENHBG051051.
InParanoidP12110.
KOK06238.
OMAELSFVFI.
OrthoDBEOG72G16P.
PhylomeDBP12110.
TreeFamTF331207.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressP12110.
BgeeP12110.
GenevestigatorP12110.

Family and domain databases

Gene3D3.40.50.410. 3 hits.
InterProIPR008160. Collagen.
IPR002035. VWF_A.
[Graphical view]
PfamPF01391. Collagen. 5 hits.
PF00092. VWA. 3 hits.
[Graphical view]
SMARTSM00327. VWA. 3 hits.
[Graphical view]
SUPFAMSSF53300. SSF53300. 3 hits.
PROSITEPS50234. VWFA. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCOL6A2. human.
GeneWikiCOL6A2.
GenomeRNAi1292.
NextBio5231.
PMAP-CutDBP12110.
PROP12110.
SOURCESearch...

Entry information

Entry nameCO6A2_HUMAN
AccessionPrimary (citable) accession number: P12110
Secondary accession number(s): Q13909 expand/collapse secondary AC list , Q13910, Q13911, Q14048, Q14049, Q16259, Q16597, Q6P0Q1, Q9UML3, Q9Y4S8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: February 6, 2007
Last modified: April 16, 2014
This is version 166 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 21

Human chromosome 21: entries, gene names and cross-references to MIM