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Protein

Collagen alpha-2(VIII) chain

Gene

COL8A2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

  • extracellular matrix structural constituent Source: UniProtKB
  • protein binding, bridging Source: UniProtKB

GO - Biological processi

Complete GO annotation...

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 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:2216. COL8A2.

Subcellular locationi

GO - Cellular componenti

  • basement membrane Source: UniProtKB
  • collagen trimer Source: UniProtKB-KW
  • endoplasmic reticulum lumen Source: Reactome
  • extracellular region Source: Reactome
  • proteinaceous extracellular matrix Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Corneal dystrophy, Fuchs endothelial, 1 (FECD1)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:136800
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)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:609140
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.

Polymorphism and mutation databases

BioMutaiCOL8A2.
DMDMi45644957.

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

BgeeiP25067.
CleanExiHS_COL8A2.
ExpressionAtlasiP25067. baseline and differential.
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. 16 interactions.
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.
GeneTreeiENSGT00760000118830.
HOGENOMiHOG000085653.
HOVERGENiHBG108220.
InParanoidiP25067.
OMAiASMAPAF.
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

        10         20         30         40         50
MLGTLTPLSS LLLLLLVLVL GCGPRASSGG GAGGAAGYAP VKYIQPMQKG
60 70 80 90 100
PVGPPFREGK GQYLEMPLPL LPMDLKGEPG PPGKPGPRGP PGPPGFPGKP
110 120 130 140 150
GMGKPGLHGQ PGPAGPPGFS RMGKAGPPGL PGKVGPPGQP GLRGEPGIRG
160 170 180 190 200
DQGLRGPPGP PGLPGPSGIT IPGKPGAQGV PGPPGFQGEP GPQGEPGPPG
210 220 230 240 250
DRGLKGDNGV GQPGLPGAPG QGGAPGPPGL PGPAGLGKPG LDGLPGAPGD
260 270 280 290 300
KGESGPPGVP GPRGEPGAVG PKGPPGVDGV GVPGAAGLPG PQGPSGAKGE
310 320 330 340 350
PGTRGPPGLI GPTGYGMPGL PGPKGDRGPA GVPGLLGDRG EPGEDGEPGE
360 370 380 390 400
QGPQGLGGPP GLPGSAGLPG RRGPPGPKGE AGPGGPPGVP GIRGDQGPSG
410 420 430 440 450
LAGKPGVPGE RGLPGAHGPP GPTGPKGEPG FTGRPGGPGV AGALGQKGDL
460 470 480 490 500
GLPGQPGLRG PSGIPGLQGP AGPIGPQGLP GLKGEPGLPG PPGEGRAGEP
510 520 530 540 550
GTAGPTGPPG VPGSPGITGP PGPPGPPGPP GAPGAFDETG IAGLHLPNGG
560 570 580 590 600
VEGAVLGKGG KPQFGLGELS AHATPAFTAV LTSPFPASGM PVKFDRTLYN
610 620 630 640 650
GHSGYNPATG IFTCPVGGVY YFAYHVHVKG TNVWVALYKN NVPATYTYDE
660 670 680 690 700
YKKGYLDQAS GGAVLQLRPN DQVWVQMPSD QANGLYSTEY IHSSFSGFLL

CPT
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. Curated

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:
EMBLi
GenBanki
DDBJi
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_001281276.1. NM_001294347.1.
NP_005193.1. NM_005202.3.
UniGeneiHs.353001.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001281276.1. NM_001294347.1.
NP_005193.1. NM_005202.3.
UniGeneiHs.353001.

3D structure databases

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

Protein-protein interaction databases

BioGridi107693. 16 interactions.
STRINGi9606.ENSP00000305913.

PTM databases

PhosphoSiteiP25067.

Polymorphism and mutation databases

BioMutaiCOL8A2.
DMDMi45644957.

Proteomic databases

PaxDbiP25067.
PRIDEiP25067.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1296.
GeneCardsiGC01M036563.
HGNCiHGNC:2216. COL8A2.
HPAiHPA049788.
MIMi120252. gene.
136800. phenotype.
609140. phenotype.
neXtProtiNX_P25067.
Orphaneti98974. Fuchs endothelial corneal dystrophy.
98973. Posterior polymorphous corneal dystrophy.
PharmGKBiPA26732.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG114228.
GeneTreeiENSGT00760000118830.
HOGENOMiHOG000085653.
HOVERGENiHBG108220.
InParanoidiP25067.
OMAiASMAPAF.
OrthoDBiEOG70ZZPW.
PhylomeDBiP25067.
TreeFamiTF334029.

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.

Miscellaneous databases

ChiTaRSiCOL8A2. human.
GeneWikiiCOL8A2.
GenomeRNAii1296.
NextBioi5261.
PROiP25067.
SOURCEiSearch...

Gene expression databases

BgeeiP25067.
CleanExiHS_COL8A2.
ExpressionAtlasiP25067. baseline and differential.
GenevestigatoriP25067.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 29, 2015
This is version 144 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

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.