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P25067

- CO8A2_HUMAN

UniProt

P25067 - CO8A2_HUMAN

Protein

Collagen alpha-2(VIII) chain

Gene

COL8A2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 2 (15 Mar 2004)
      Previous versions | rss
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    Functioni

    Macromolecular component of the subendothelium. Major component of the Descemet's membrane (basement membrane) of corneal endothelial cells. Also component of the endothelia of blood vessels. Necessary for migration and proliferation of vascular smooth muscle cells and thus, has a potential role in the maintenance of vessel wall integrity and structure, in particular in atherogenesis By similarity.By similarity

    GO - Molecular functioni

    1. extracellular matrix structural constituent Source: UniProtKB
    2. protein binding, bridging Source: UniProtKB

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. camera-type eye morphogenesis Source: Ensembl
    3. collagen catabolic process Source: Reactome
    4. epithelial cell proliferation Source: Ensembl
    5. extracellular matrix disassembly Source: Reactome
    6. extracellular matrix organization Source: UniProtKB
    7. single organismal cell-cell adhesion Source: UniProtKB

    Keywords - Biological processi

    Angiogenesis, 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.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Collagen alpha-2(VIII) chain
    Alternative name(s):
    Endothelial collagen
    Gene namesi
    Name:COL8A2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:2216. COL8A2.

    Subcellular locationi

    GO - Cellular componenti

    1. basement membrane Source: UniProtKB
    2. collagen trimer Source: UniProtKB-KW
    3. endoplasmic reticulum lumen Source: Reactome
    4. extracellular region Source: Reactome
    5. proteinaceous extracellular matrix Source: UniProtKB

    Keywords - Cellular componenti

    Basement membrane, Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Corneal dystrophy, Fuchs endothelial, 1 (FECD1) [MIM:136800]: A corneal disease caused by loss of endothelium of the central cornea. It is characterized by focal wart-like guttata that arise from Descemet membrane and develop in the central cornea, epithelial blisters, reduced vision and pain. Descemet membrane is thickened by abnormal collagenous deposition.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti155 – 1551R → Q in FECD1; identified as a polymorphism in the Japanese population. 2 Publications
    Corresponds to variant rs75864656 [ dbSNP | Ensembl ].
    VAR_017894
    Natural varianti304 – 3041R → Q in FECD1. 1 Publication
    VAR_017895
    Natural varianti357 – 3571G → R in FECD1; unknown pathological significance. 1 Publication
    VAR_017896
    Natural varianti434 – 4341R → H in FECD1. 1 Publication
    Corresponds to variant rs201235688 [ dbSNP | Ensembl ].
    VAR_017897
    Natural varianti455 – 4551Q → K in FECD1 and PPCD2. 1 Publication
    VAR_017898
    Natural varianti575 – 5751P → L in FECD1; unknown pathological significance. 1 Publication
    Corresponds to variant rs145553904 [ dbSNP | Ensembl ].
    VAR_017899
    Corneal dystrophy, posterior polymorphous, 2 (PPCD2) [MIM:609140]: A rare mild subtype of posterior corneal dystrophy characterized by alterations of Descemet membrane presenting as vesicles, opacities or band-like lesions on slit-lamp examination and specular microscopy. Affected patient typically are asymptomatic.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti455 – 4551Q → K in FECD1 and PPCD2. 1 Publication
    VAR_017898

    Keywords - Diseasei

    Corneal dystrophy, Disease mutation

    Organism-specific databases

    MIMi136800. phenotype.
    609140. phenotype.
    Orphaneti98974. Fuchs endothelial corneal dystrophy.
    98973. Posterior polymorphous corneal dystrophy.
    PharmGKBiPA26732.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2828Sequence AnalysisAdd
    BLAST
    Chaini29 – 703675Collagen alpha-2(VIII) chainPRO_0000005835Add
    BLAST

    Post-translational modificationi

    Proteolytically cleaved by neutrophil elastase, in vitro.1 Publication
    Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.

    Keywords - PTMi

    Hydroxylation

    Proteomic databases

    PaxDbiP25067.
    PRIDEiP25067.

    PTM databases

    PhosphoSiteiP25067.

    Expressioni

    Tissue specificityi

    Expressed primarily in the subendothelium of large blood vessels. Also expressed in arterioles and venules in muscle, heart, kidney, spleen, umbilical cord, liver and lung and is also found in connective tissue layers around hair follicles, around nerve bundles in muscle, in the dura of the optic nerve, in cornea and sclera, and in the perichondrium of cartilaginous tissues. In the kidney, expressed in mesangial cells, glomerular endothelial cells, and tubular epithelial cells. Also expressed in mast cells, and in astrocytes during the repair process. Expressed in Descemet's membrane.2 Publications

    Inductioni

    Some up-regulation in diabetic nephropathy.1 Publication

    Gene expression databases

    ArrayExpressiP25067.
    BgeeiP25067.
    CleanExiHS_COL8A2.
    GenevestigatoriP25067.

    Organism-specific databases

    HPAiHPA049788.

    Interactioni

    Subunit structurei

    Homotrimers, or heterotrimers in association with alpha 2(VIII) type collagens. Four homotrimers can form a tetrhedron stabilized by central interacting C-terminal NC1 trimers.1 Publication

    Protein-protein interaction databases

    BioGridi107693. 1 interaction.
    STRINGi9606.ENSP00000305913.

    Structurei

    3D structure databases

    ProteinModelPortaliP25067.
    SMRiP25067. Positions 575-702.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini570 – 703134C1qPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni29 – 7648Nonhelical region (NC2)Add
    BLAST
    Regioni77 – 536460Triple-helical regionAdd
    BLAST
    Regioni537 – 703167Nonhelical region (NC1)Add
    BLAST

    Sequence similaritiesi

    Contains 1 C1q domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Collagen, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG114228.
    HOGENOMiHOG000085653.
    HOVERGENiHBG108220.
    InParanoidiP25067.
    OMAiAGPPFRE.
    OrthoDBiEOG70ZZPW.
    PhylomeDBiP25067.
    TreeFamiTF334029.

    Family and domain databases

    Gene3Di2.60.120.40. 1 hit.
    InterProiIPR001073. C1q.
    IPR008160. Collagen.
    IPR008983. Tumour_necrosis_fac-like_dom.
    [Graphical view]
    PfamiPF00386. C1q. 1 hit.
    PF01391. Collagen. 3 hits.
    [Graphical view]
    PRINTSiPR00007. COMPLEMNTC1Q.
    SMARTiSM00110. C1Q. 1 hit.
    [Graphical view]
    SUPFAMiSSF49842. SSF49842. 1 hit.
    PROSITEiPS50871. C1Q. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P25067-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLGTLTPLSS LLLLLLVLVL GCGPRASSGG GAGGAAGYAP VKYIQPMQKG    50
    PVGPPFREGK GQYLEMPLPL LPMDLKGEPG PPGKPGPRGP PGPPGFPGKP 100
    GMGKPGLHGQ PGPAGPPGFS RMGKAGPPGL PGKVGPPGQP GLRGEPGIRG 150
    DQGLRGPPGP PGLPGPSGIT IPGKPGAQGV PGPPGFQGEP GPQGEPGPPG 200
    DRGLKGDNGV GQPGLPGAPG QGGAPGPPGL PGPAGLGKPG LDGLPGAPGD 250
    KGESGPPGVP GPRGEPGAVG PKGPPGVDGV GVPGAAGLPG PQGPSGAKGE 300
    PGTRGPPGLI GPTGYGMPGL PGPKGDRGPA GVPGLLGDRG EPGEDGEPGE 350
    QGPQGLGGPP GLPGSAGLPG RRGPPGPKGE AGPGGPPGVP GIRGDQGPSG 400
    LAGKPGVPGE RGLPGAHGPP GPTGPKGEPG FTGRPGGPGV AGALGQKGDL 450
    GLPGQPGLRG PSGIPGLQGP AGPIGPQGLP GLKGEPGLPG PPGEGRAGEP 500
    GTAGPTGPPG VPGSPGITGP PGPPGPPGPP GAPGAFDETG IAGLHLPNGG 550
    VEGAVLGKGG KPQFGLGELS AHATPAFTAV LTSPFPASGM PVKFDRTLYN 600
    GHSGYNPATG IFTCPVGGVY YFAYHVHVKG TNVWVALYKN NVPATYTYDE 650
    YKKGYLDQAS GGAVLQLRPN DQVWVQMPSD QANGLYSTEY IHSSFSGFLL 700
    CPT 703
    Length:703
    Mass (Da):67,244
    Last modified:March 15, 2004 - v2
    Checksum:i84BD7CBDBDECD466
    GO

    Sequence cautioni

    The sequence BAB84955.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti88 – 881R → W in AAA62822. (PubMed:2019595)Curated
    Sequence conflicti102 – 1021M → H in AAA62822. (PubMed:2019595)Curated
    Sequence conflicti133 – 1331K → N in AAA62822. (PubMed:2019595)Curated
    Sequence conflicti347 – 3471E → D in AAA62822. (PubMed:2019595)Curated
    Sequence conflicti377 – 3782PK → LR in AAA62822. (PubMed:2019595)Curated
    Sequence conflicti506 – 5061T → R in AAA62822. (PubMed:2019595)Curated
    Sequence conflicti523 – 5231P → L in AAA62822. (PubMed:2019595)Curated
    Sequence conflicti529 – 5313Missing in AAA62822. (PubMed:2019595)Curated
    Sequence conflicti585 – 5851F → L in AAA62822. (PubMed:2019595)Curated
    Sequence conflicti677 – 6771M → I in AAA62822. (PubMed:2019595)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti3 – 31G → R.1 Publication
    Corresponds to variant rs115156902 [ dbSNP | Ensembl ].
    VAR_017893
    Natural varianti155 – 1551R → Q in FECD1; identified as a polymorphism in the Japanese population. 2 Publications
    Corresponds to variant rs75864656 [ dbSNP | Ensembl ].
    VAR_017894
    Natural varianti304 – 3041R → Q in FECD1. 1 Publication
    VAR_017895
    Natural varianti357 – 3571G → R in FECD1; unknown pathological significance. 1 Publication
    VAR_017896
    Natural varianti434 – 4341R → H in FECD1. 1 Publication
    Corresponds to variant rs201235688 [ dbSNP | Ensembl ].
    VAR_017897
    Natural varianti455 – 4551Q → K in FECD1 and PPCD2. 1 Publication
    VAR_017898
    Natural varianti502 – 5021T → M.1 Publication
    Corresponds to variant rs117860804 [ dbSNP | Ensembl ].
    VAR_021387
    Natural varianti575 – 5751P → L in FECD1; unknown pathological significance. 1 Publication
    Corresponds to variant rs145553904 [ dbSNP | Ensembl ].
    VAR_017899
    Natural varianti645 – 6451T → I.1 Publication
    Corresponds to variant rs200767854 [ dbSNP | Ensembl ].
    VAR_017900

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK074129 mRNA. Translation: BAB84955.1. Different initiation.
    AL138787 Genomic DNA. Translation: CAI22267.1.
    CH471059 Genomic DNA. Translation: EAX07388.1.
    M60832 Genomic DNA. Translation: AAA62822.1.
    CCDSiCCDS403.1.
    PIRiA57131.
    RefSeqiNP_005193.1. NM_005202.2.
    XP_005270535.1. XM_005270478.2.
    UniGeneiHs.353001.

    Genome annotation databases

    EnsembliENST00000303143; ENSP00000305913; ENSG00000171812.
    ENST00000397799; ENSP00000380901; ENSG00000171812.
    GeneIDi1296.
    KEGGihsa:1296.
    UCSCiuc001bzv.2. human.

    Polymorphism databases

    DMDMi45644957.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK074129 mRNA. Translation: BAB84955.1 . Different initiation.
    AL138787 Genomic DNA. Translation: CAI22267.1 .
    CH471059 Genomic DNA. Translation: EAX07388.1 .
    M60832 Genomic DNA. Translation: AAA62822.1 .
    CCDSi CCDS403.1.
    PIRi A57131.
    RefSeqi NP_005193.1. NM_005202.2.
    XP_005270535.1. XM_005270478.2.
    UniGenei Hs.353001.

    3D structure databases

    ProteinModelPortali P25067.
    SMRi P25067. Positions 575-702.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107693. 1 interaction.
    STRINGi 9606.ENSP00000305913.

    PTM databases

    PhosphoSitei P25067.

    Polymorphism databases

    DMDMi 45644957.

    Proteomic databases

    PaxDbi P25067.
    PRIDEi P25067.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000303143 ; ENSP00000305913 ; ENSG00000171812 .
    ENST00000397799 ; ENSP00000380901 ; ENSG00000171812 .
    GeneIDi 1296.
    KEGGi hsa:1296.
    UCSCi uc001bzv.2. human.

    Organism-specific databases

    CTDi 1296.
    GeneCardsi GC01M036563.
    HGNCi HGNC:2216. COL8A2.
    HPAi HPA049788.
    MIMi 120252. gene.
    136800. phenotype.
    609140. phenotype.
    neXtProti NX_P25067.
    Orphaneti 98974. Fuchs endothelial corneal dystrophy.
    98973. Posterior polymorphous corneal dystrophy.
    PharmGKBi PA26732.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG114228.
    HOGENOMi HOG000085653.
    HOVERGENi HBG108220.
    InParanoidi P25067.
    OMAi AGPPFRE.
    OrthoDBi EOG70ZZPW.
    PhylomeDBi P25067.
    TreeFami TF334029.

    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.

    Miscellaneous databases

    GeneWikii COL8A2.
    GenomeRNAii 1296.
    NextBioi 5261.
    PROi P25067.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P25067.
    Bgeei P25067.
    CleanExi HS_COL8A2.
    Genevestigatori P25067.

    Family and domain databases

    Gene3Di 2.60.120.40. 1 hit.
    InterProi IPR001073. C1q.
    IPR008160. Collagen.
    IPR008983. Tumour_necrosis_fac-like_dom.
    [Graphical view ]
    Pfami PF00386. C1q. 1 hit.
    PF01391. Collagen. 3 hits.
    [Graphical view ]
    PRINTSi PR00007. COMPLEMNTC1Q.
    SMARTi SM00110. C1Q. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49842. SSF49842. 1 hit.
    PROSITEi PS50871. C1Q. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Spleen.
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The alpha 2(VIII) collagen gene. A novel member of the short chain collagen family located on the human chromosome 1."
      Muragaki Y., Jacenko O., Apte S., Mattei M.-G., Ninomiya Y., Olsen B.R.
      J. Biol. Chem. 266:7721-7727(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 66-703.
    5. Cited for: PROTEOLYTIC PROCESSING.
    6. "The alpha1(VIII) and alpha2(VIII) collagen chains form two distinct homotrimeric proteins in vivo."
      Greenhill N.S., Ruger B.M., Hasan Q., Davis P.F.
      Matrix Biol. 19:19-28(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    7. "Expression and supramolecular assembly of recombinant alpha1(viii) and alpha2(viii) collagen homotrimers."
      Stephan S., Sherratt M.J., Hodson N., Shuttleworth C.A., Kielty C.M.
      J. Biol. Chem. 279:21469-21477(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    8. Cited for: TISSUE SPECIFICITY, INDUCTION.
    9. "Missense mutations in COL8A2, the gene encoding the alpha-2 chain of type VIII collagen, cause two forms of corneal endothelial dystrophy."
      Biswas S., Munier F.L., Yardley J., Hart-Holden N., Perveen R., Cousin P., Sutphin J.E., Noble B., Batterbury M., Kielty C., Hackett A., Bonshek R., Ridgway A., McLeod D., Sheffield V.C., Stone E.M., Schorderet D.F., Black G.C.M.
      Hum. Mol. Genet. 10:2415-2423(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS FECD1 GLN-155; GLN-304; ARG-357; HIS-434; LYS-455 AND LEU-575, VARIANT PPCD2 LYS-455, VARIANTS ARG-3 AND ILE-645.
    10. "Analysis of COL8A2 gene mutation in Japanese patients with Fuchs' endothelial dystrophy and posterior polymorphous dystrophy."
      Kobayashi A., Fujiki K., Murakami A., Kato T., Chen L.-Z., Onoe H., Nakayasu K., Sakurai M., Takahashi M., Sugiyama K., Kanai A.
      Jpn. J. Ophthalmol. 48:195-198(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GLN-155 AND MET-502.

    Entry informationi

    Entry nameiCO8A2_HUMAN
    AccessioniPrimary (citable) accession number: P25067
    Secondary accession number(s): Q5JV31, Q8TEJ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: March 15, 2004
    Last modified: October 1, 2014
    This is version 139 of the entry and version 2 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, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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

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