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P12110

- CO6A2_HUMAN

UniProt

P12110 - CO6A2_HUMAN

Protein

Collagen alpha-2(VI) chain

Gene

COL6A2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 171 (01 Oct 2014)
      Sequence version 4 (06 Feb 2007)
      Previous versions | rss
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    Functioni

    Collagen VI acts as a cell-binding protein.

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. cell adhesion Source: UniProtKB-KW
    3. collagen catabolic process Source: Reactome
    4. extracellular matrix disassembly Source: Reactome
    5. extracellular matrix organization Source: Reactome
    6. protein heterotrimerization Source: MGI
    7. response to glucose Source: Ensembl

    Keywords - Biological processi

    Cell adhesion

    Enzyme and pathway databases

    ReactomeiREACT_121139. Collagen biosynthesis and modifying enzymes.
    REACT_13552. Integrin cell surface interactions.
    REACT_150180. Assembly of collagen fibrils and other multimeric structures.
    REACT_150401. Collagen degradation.
    REACT_163906. ECM proteoglycans.
    REACT_16888. Signaling by PDGF.
    REACT_18312. NCAM1 interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Collagen alpha-2(VI) chain
    Gene namesi
    Name:COL6A2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 21

    Organism-specific databases

    HGNCiHGNC:2212. COL6A2.

    Subcellular locationi

    Secretedextracellular spaceextracellular matrix 1 Publication. Membrane 1 Publication; Peripheral membrane protein 1 Publication
    Note: Recruited on membranes by CSPG4.

    GO - Cellular componenti

    1. collagen trimer Source: UniProtKB-KW
    2. endoplasmic reticulum lumen Source: Reactome
    3. extracellular region Source: MGI
    4. extracellular space Source: BHF-UCL
    5. extracellular vesicular exosome Source: UniProt
    6. proteinaceous extracellular matrix Source: UniProtKB-SubCell
    7. protein complex Source: MGI
    8. sarcolemma Source: Ensembl

    Keywords - Cellular componenti

    Extracellular matrix, Membrane, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    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.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti106 – 1061E → K in BM. 1 Publication
    Corresponds to variant rs141703710 [ dbSNP | Ensembl ].
    VAR_058225
    Natural varianti271 – 2711G → S in BM. 1 Publication
    VAR_013589
    Natural varianti621 – 6211D → N in BM. 1 Publication
    VAR_013590
    Natural varianti700 – 7001G → S in BM. 1 Publication
    VAR_058231
    Natural varianti777 – 7771C → R in BM. 1 Publication
    VAR_058233
    Natural varianti853 – 8531R → Q in BM. 1 Publication
    Corresponds to variant rs144830948 [ dbSNP | Ensembl ].
    VAR_058237
    Natural varianti932 – 9321P → L in BM; results in reduced intracellular collagen VI assembly and secretion. 1 Publication
    VAR_058241
    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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti283 – 2831G → R in UCMD. 1 Publication
    VAR_058226
    Natural varianti498 – 4981R → H in UCMD. 1 Publication
    VAR_058228
    Natural varianti531 – 5311G → R in UCMD. 1 Publication
    VAR_058230
    Natural varianti784 – 7841R → H in UCMD. 1 Publication
    Corresponds to variant rs75120695 [ dbSNP | Ensembl ].
    VAR_058234
    Natural varianti837 – 8371L → P in UCMD; prevents collagen VI assembly. 1 Publication
    VAR_058236
    Natural varianti876 – 8761R → S in UCMD. 1 Publication
    VAR_058238
    Natural varianti897 – 8971Missing in UCMD; results in severe collagen VI matrix deficiencies. 1 Publication
    VAR_058240
    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.

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi158810. phenotype.
    254090. phenotype.
    255600. phenotype.
    Orphaneti610. Bethlem myopathy.
    75840. Congenital muscular dystrophy, Ullrich type.
    289380. Myosclerosis.
    PharmGKBiPA26728.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 1019999Collagen alpha-2(VI) chainPRO_0000005832Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi140 – 1401N-linked (GlcNAc...)1 Publication
    Glycosylationi327 – 3271N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi630 – 6301N-linked (GlcNAc...)Sequence Analysis
    Modified residuei701 – 7011Phosphothreonine1 Publication
    Modified residuei703 – 7031Phosphothreonine1 Publication
    Modified residuei705 – 7051Phosphoserine1 Publication
    Glycosylationi785 – 7851N-linked (GlcNAc...)1 Publication
    Glycosylationi897 – 8971N-linked (GlcNAc...)1 Publication
    Glycosylationi954 – 9541N-linked (GlcNAc...)1 Publication

    Post-translational modificationi

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

    Keywords - PTMi

    Glycoprotein, Hydroxylation, Phosphoprotein

    Proteomic databases

    MaxQBiP12110.
    PaxDbiP12110.
    PRIDEiP12110.

    2D gel databases

    REPRODUCTION-2DPAGEP12110.

    PTM databases

    PhosphoSiteiP12110.

    Miscellaneous databases

    PMAP-CutDBP12110.

    Expressioni

    Gene expression databases

    ArrayExpressiP12110.
    BgeeiP12110.
    GenevestigatoriP12110.

    Organism-specific databases

    HPAiHPA007029.

    Interactioni

    Subunit structurei

    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 CSPG4.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DISC1Q9NRI53EBI-928749,EBI-529989

    Protein-protein interaction databases

    BioGridi107689. 3 interactions.
    IntActiP12110. 3 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP12110.
    SMRiP12110. Positions 614-808.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini46 – 234189VWFA 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini615 – 805191VWFA 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini833 – 1014182VWFA 3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni21 – 256236Nonhelical regionAdd
    BLAST
    Regioni257 – 590334Triple-helical regionAdd
    BLAST
    Regioni591 – 1019429Nonhelical regionAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi366 – 3683Cell attachment siteSequence Analysis
    Motifi426 – 4283Cell attachment siteSequence Analysis
    Motifi489 – 4913Cell attachment siteSequence Analysis
    Motifi498 – 5003Cell attachment siteSequence Analysis
    Motifi539 – 5413Cell attachment siteSequence Analysis

    Sequence similaritiesi

    Belongs to the type VI collagen family.Curated
    Contains 3 VWFA domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Collagen, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG256042.
    HOVERGENiHBG051051.
    InParanoidiP12110.
    KOiK06238.
    OMAiDIAWIGF.
    OrthoDBiEOG72G16P.
    PhylomeDBiP12110.
    TreeFamiTF331207.

    Family and domain databases

    Gene3Di3.40.50.410. 3 hits.
    InterProiIPR008160. Collagen.
    IPR002035. VWF_A.
    [Graphical view]
    PfamiPF01391. Collagen. 5 hits.
    PF00092. VWA. 3 hits.
    [Graphical view]
    SMARTiSM00327. VWA. 3 hits.
    [Graphical view]
    SUPFAMiSSF53300. SSF53300. 3 hits.
    PROSITEiPS50234. VWFA. 3 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 2C2 (identifier: P12110-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MLQGTCSVLL LWGILGAIQA QQQEVISPDT TERNNNCPEK TDCPIHVYFV     50
    LDTSESVTMQ SPTDILLFHM KQFVPQFISQ LQNEFYLDQV ALSWRYGGLH 100
    FSDQVEVFSP PGSDRASFIK NLQGISSFRR GTFTDCALAN MTEQIRQDRS 150
    KGTVHFAVVI TDGHVTGSPC GGIKLQAERA REEGIRLFAV APNQNLKEQG 200
    LRDIASTPHE LYRNDYATML PDSTEIDQDT INRIIKVMKH EAYGECYKVS 250
    CLEIPGPSGP KGYRGQKGAK GNMGEPGEPG QKGRQGDPGI EGPIGFPGPK 300
    GVPGFKGEKG EFGADGRKGA PGLAGKNGTD GQKGKLGRIG PPGCKGDPGN 350
    RGPDGYPGEA GSPGERGDQG GKGDPGRPGR RGPPGEIGAK GSKGYQGNSG 400
    APGSPGVKGA KGGPGPRGPK GEPGRRGDPG TKGSPGSDGP KGEKGDPGPE 450
    GPRGLAGEVG NKGAKGDRGL PGPRGPQGAL GEPGKQGSRG DPGDAGPRGD 500
    SGQPGPKGDP GRPGFSYPGP RGAPGEKGEP GPRGPEGGRG DFGLKGEPGR 550
    KGEKGEPADP GPPGEPGPRG PRGVPGPEGE PGPPGDPGLT ECDVMTYVRE 600
    TCGCCDCEKR CGALDVVFVI DSSESIGYTN FTLEKNFVIN VVNRLGAIAK 650
    DPKSETGTRV GVVQYSHEGT FEAIQLDDER IDSLSSFKEA VKNLEWIAGG 700
    TWTPSALKFA YDRLIKESRR QKTRVFAVVI TDGRHDPRDD DLNLRALCDR 750
    DVTVTAIGIG DMFHEKHESE NLYSIACDKP QQVRNMTLFS DLVAEKFIDD 800
    MEDVLCPDPQ IVCPDLPCQT ELSVAQCTQR PVDIVFLLDG SERLGEQNFH 850
    KARRFVEQVA RRLTLARRDD DPLNARVALL QFGGPGEQQV AFPLSHNLTA 900
    IHEALETTQY LNSFSHVGAG VVHAINAIVR SPRGGARRHA ELSFVFLTDG 950
    VTGNDSLHES AHSMRKQNVV PTVLALGSDV DMDVLTTLSL GDRAAVFHEK 1000
    DYDSLAQPGF FDRFIRWIC 1019
    Length:1,019
    Mass (Da):108,579
    Last modified:February 6, 2007 - v4
    Checksum:i6C513ADE46C1D111
    GO
    Isoform 2C2A (identifier: P12110-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         821-991: ELSVAQCTQR...MDVLTTLSLG → DAPWPGGEPP...GDPETALALC
         992-1019: Missing.

    Show »
    Length:918
    Mass (Da):97,419
    Checksum:i336CB9B6FC8394D8
    GO
    Isoform 2C2A' (identifier: P12110-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:828
    Mass (Da):87,280
    Checksum:i9690A499C8E8827F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti507 – 5071K → S in AAB20836. (PubMed:1765372)Curated
    Sequence conflicti966 – 9672KQ → NE in AAA52056. 1 PublicationCurated
    Sequence conflicti966 – 9672KQ → NE in AAA35620. (PubMed:1690728)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti106 – 1061E → K in BM. 1 Publication
    Corresponds to variant rs141703710 [ dbSNP | Ensembl ].
    VAR_058225
    Natural varianti227 – 2271D → N.4 Publications
    Corresponds to variant rs35881321 [ dbSNP | Ensembl ].
    VAR_048801
    Natural varianti271 – 2711G → S in BM. 1 Publication
    VAR_013589
    Natural varianti283 – 2831G → R in UCMD. 1 Publication
    VAR_058226
    Natural varianti399 – 3991S → N.6 Publications
    Corresponds to variant rs2839110 [ dbSNP | Ensembl ].
    VAR_030315
    Natural varianti489 – 4891R → Q.1 Publication
    Corresponds to variant rs61735828 [ dbSNP | Ensembl ].
    VAR_058227
    Natural varianti498 – 4981R → H in UCMD. 1 Publication
    VAR_058228
    Natural varianti518 – 5181P → S.1 Publication
    Corresponds to variant rs141166141 [ dbSNP | Ensembl ].
    VAR_058229
    Natural varianti531 – 5311G → R in UCMD. 1 Publication
    VAR_058230
    Natural varianti621 – 6211D → N in BM. 1 Publication
    VAR_013590
    Natural varianti680 – 6801R → H.5 Publications
    Corresponds to variant rs1042917 [ dbSNP | Ensembl ].
    VAR_030316
    Natural varianti700 – 7001G → S in BM. 1 Publication
    VAR_058231
    Natural varianti724 – 7241R → C.1 Publication
    VAR_058232
    Natural varianti777 – 7771C → R in BM. 1 Publication
    VAR_058233
    Natural varianti784 – 7841R → H in UCMD. 1 Publication
    Corresponds to variant rs75120695 [ dbSNP | Ensembl ].
    VAR_058234
    Natural varianti804 – 8041V → G.1 Publication
    VAR_058235
    Natural varianti837 – 8371L → P in UCMD; prevents collagen VI assembly. 1 Publication
    VAR_058236
    Natural varianti853 – 8531R → Q in BM. 1 Publication
    Corresponds to variant rs144830948 [ dbSNP | Ensembl ].
    VAR_058237
    Natural varianti876 – 8761R → S in UCMD. 1 Publication
    VAR_058238
    Natural varianti895 – 8951S → R.1 Publication
    Corresponds to variant rs141233891 [ dbSNP | Ensembl ].
    VAR_058239
    Natural varianti897 – 8971Missing in UCMD; results in severe collagen VI matrix deficiencies. 1 Publication
    VAR_058240
    Natural varianti932 – 9321P → L in BM; results in reduced intracellular collagen VI assembly and secretion. 1 Publication
    VAR_058241
    Natural varianti935 – 9351G → R.1 Publication
    Corresponds to variant rs35548026 [ dbSNP | Ensembl ].
    VAR_048802
    Natural varianti1015 – 10151I → L.
    Corresponds to variant rs11910483 [ dbSNP | Ensembl ].
    VAR_048803

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei821 – 991171ELSVA…TLSLG → DAPWPGGEPPVTFLRTEEGP DATFPRTIPLIQQLLNATEL TQDPAAYSQLVAVLVYTAER AKFATGVERQDWMELFIDTF KLVHRDIVGDPETALALC in isoform 2C2A. 1 PublicationVSP_001163Add
    BLAST
    Alternative sequencei821 – 8288ELSVAQCT → GLDGAVLC in isoform 2C2A'. CuratedVSP_001161
    Alternative sequencei829 – 1019191Missing in isoform 2C2A'. CuratedVSP_001162Add
    BLAST
    Alternative sequencei992 – 101928Missing in isoform 2C2A. 1 PublicationVSP_001164Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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
    , 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.
    CCDSiCCDS13728.1. [P12110-1]
    CCDS13729.1. [P12110-2]
    CCDS13730.1. [P12110-3]
    PIRiS05378. CGHU2A.
    S09646.
    T12549.
    RefSeqiNP_001840.3. NM_001849.3. [P12110-1]
    NP_478054.2. NM_058174.2. [P12110-2]
    NP_478055.2. NM_058175.2. [P12110-3]
    UniGeneiHs.420269.

    Genome annotation databases

    EnsembliENST00000300527; ENSP00000300527; ENSG00000142173. [P12110-1]
    ENST00000310645; ENSP00000312529; ENSG00000142173. [P12110-3]
    ENST00000397763; ENSP00000380870; ENSG00000142173. [P12110-2]
    ENST00000409416; ENSP00000387115; ENSG00000142173. [P12110-3]
    GeneIDi1292.
    KEGGihsa:1292.
    UCSCiuc002zhy.1. human. [P12110-3]
    uc002zhz.1. human. [P12110-2]
    uc002zia.1. human. [P12110-1]

    Polymorphism databases

    DMDMi125987812.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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
    , 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 .
    CCDSi CCDS13728.1. [P12110-1 ]
    CCDS13729.1. [P12110-2 ]
    CCDS13730.1. [P12110-3 ]
    PIRi S05378. CGHU2A.
    S09646.
    T12549.
    RefSeqi NP_001840.3. NM_001849.3. [P12110-1 ]
    NP_478054.2. NM_058174.2. [P12110-2 ]
    NP_478055.2. NM_058175.2. [P12110-3 ]
    UniGenei Hs.420269.

    3D structure databases

    ProteinModelPortali P12110.
    SMRi P12110. Positions 614-808.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107689. 3 interactions.
    IntActi P12110. 3 interactions.

    Chemistry

    ChEMBLi CHEMBL2364188.

    PTM databases

    PhosphoSitei P12110.

    Polymorphism databases

    DMDMi 125987812.

    2D gel databases

    REPRODUCTION-2DPAGE P12110.

    Proteomic databases

    MaxQBi P12110.
    PaxDbi P12110.
    PRIDEi P12110.

    Protocols and materials databases

    DNASUi 1292.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000300527 ; ENSP00000300527 ; ENSG00000142173 . [P12110-1 ]
    ENST00000310645 ; ENSP00000312529 ; ENSG00000142173 . [P12110-3 ]
    ENST00000397763 ; ENSP00000380870 ; ENSG00000142173 . [P12110-2 ]
    ENST00000409416 ; ENSP00000387115 ; ENSG00000142173 . [P12110-3 ]
    GeneIDi 1292.
    KEGGi hsa:1292.
    UCSCi uc002zhy.1. human. [P12110-3 ]
    uc002zhz.1. human. [P12110-2 ]
    uc002zia.1. human. [P12110-1 ]

    Organism-specific databases

    CTDi 1292.
    GeneCardsi GC21P047518.
    GeneReviewsi COL6A2.
    H-InvDB HIX0016186.
    HGNCi HGNC:2212. COL6A2.
    HPAi HPA007029.
    MIMi 120240. gene.
    158810. phenotype.
    254090. phenotype.
    255600. phenotype.
    neXtProti NX_P12110.
    Orphaneti 610. Bethlem myopathy.
    75840. Congenital muscular dystrophy, Ullrich type.
    289380. Myosclerosis.
    PharmGKBi PA26728.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG256042.
    HOVERGENi HBG051051.
    InParanoidi P12110.
    KOi K06238.
    OMAi DIAWIGF.
    OrthoDBi EOG72G16P.
    PhylomeDBi P12110.
    TreeFami TF331207.

    Enzyme and pathway databases

    Reactomei REACT_121139. Collagen biosynthesis and modifying enzymes.
    REACT_13552. Integrin cell surface interactions.
    REACT_150180. Assembly of collagen fibrils and other multimeric structures.
    REACT_150401. Collagen degradation.
    REACT_163906. ECM proteoglycans.
    REACT_16888. Signaling by PDGF.
    REACT_18312. NCAM1 interactions.

    Miscellaneous databases

    ChiTaRSi COL6A2. human.
    GeneWikii COL6A2.
    GenomeRNAii 1292.
    NextBioi 5231.
    PMAP-CutDB P12110.
    PROi P12110.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P12110.
    Bgeei P12110.
    Genevestigatori P12110.

    Family and domain databases

    Gene3Di 3.40.50.410. 3 hits.
    InterProi IPR008160. Collagen.
    IPR002035. VWF_A.
    [Graphical view ]
    Pfami PF01391. Collagen. 5 hits.
    PF00092. VWA. 3 hits.
    [Graphical view ]
    SMARTi SM00327. VWA. 3 hits.
    [Graphical view ]
    SUPFAMi SSF53300. SSF53300. 3 hits.
    PROSITEi PS50234. VWFA. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. Cited for: VARIANT BM LEU-932, VARIANTS ASN-227; ASN-399; HIS-680 AND ARG-895.
    22. Cited for: INVOLVEMENT IN MYOSCLEROSIS.

    Entry informationi

    Entry nameiCO6A2_HUMAN
    AccessioniPrimary (citable) accession number: P12110
    Secondary accession number(s): Q13909
    , Q13910, Q13911, Q14048, Q14049, Q16259, Q16597, Q6P0Q1, Q9UML3, Q9Y4S8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: February 6, 2007
    Last modified: October 1, 2014
    This is version 171 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 21
      Human chromosome 21: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3