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Protein

Collagen alpha-6(VI) chain

Gene

COL6A6

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

Functioni

Collagen VI acts as a cell-binding protein.By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiR-HSA-1442490. Collagen degradation.
R-HSA-1650814. Collagen biosynthesis and modifying enzymes.
R-HSA-186797. Signaling by PDGF.
R-HSA-2022090. Assembly of collagen fibrils and other multimeric structures.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-3000178. ECM proteoglycans.
R-HSA-419037. NCAM1 interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-6(VI) chain
Gene namesi
Name:COL6A6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:27023. COL6A6.

Subcellular locationi

GO - Cellular componenti

  • collagen trimer Source: UniProtKB-KW
  • extracellular region Source: Reactome
  • proteinaceous extracellular matrix Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165697087.

Chemistry

ChEMBLiCHEMBL2364188.

Polymorphism and mutation databases

BioMutaiCOL6A6.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 22632244Collagen alpha-6(VI) chainPRO_5000266306Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi198 – 1981N-linked (GlcNAc...)1 Publication
Glycosylationi275 – 2751N-linked (GlcNAc...)1 Publication
Glycosylationi288 – 2881N-linked (GlcNAc...)1 Publication
Glycosylationi298 – 2981N-linked (GlcNAc...)1 Publication
Glycosylationi347 – 3471N-linked (GlcNAc...)Sequence analysis
Glycosylationi520 – 5201N-linked (GlcNAc...)Sequence analysis
Glycosylationi930 – 9301N-linked (GlcNAc...)1 Publication
Glycosylationi988 – 9881N-linked (GlcNAc...)1 Publication
Glycosylationi1290 – 12901N-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.By similarity

Keywords - PTMi

Glycoprotein, Hydroxylation

Proteomic databases

MaxQBiA6NMZ7.
PaxDbiA6NMZ7.
PRIDEiA6NMZ7.

PTM databases

iPTMnetiA6NMZ7.
PhosphoSiteiA6NMZ7.

Expressioni

Gene expression databases

BgeeiA6NMZ7.
ExpressionAtlasiA6NMZ7. baseline and differential.
GenevisibleiA6NMZ7. HS.

Organism-specific databases

HPAiHPA045239.

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).Curated

Protein-protein interaction databases

STRINGi9606.ENSP00000351310.

Structurei

3D structure databases

ProteinModelPortaliA6NMZ7.
SMRiA6NMZ7. Positions 26-1325, 1424-1452, 1672-1701.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 206180VWFA 1PROSITE-ProRule annotationAdd
BLAST
Domaini229 – 411183VWFA 2PROSITE-ProRule annotationAdd
BLAST
Domaini436 – 606171VWFA 3PROSITE-ProRule annotationAdd
BLAST
Domaini622 – 791170VWFA 4PROSITE-ProRule annotationAdd
BLAST
Domaini809 – 982174VWFA 5PROSITE-ProRule annotationAdd
BLAST
Domaini1000 – 1171172VWFA 6PROSITE-ProRule annotationAdd
BLAST
Domaini1187 – 1371185VWFA 7PROSITE-ProRule annotationAdd
BLAST
Domaini1757 – 1937181VWFA 8PROSITE-ProRule annotationAdd
BLAST
Domaini1965 – 2166202VWFA 9PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni20 – 13911372Nonhelical regionAdd
BLAST
Regioni1392 – 1725334Triple-helical regionAdd
BLAST
Regioni1726 – 2263538Nonhelical regionAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1508 – 15103Cell attachment siteSequence analysis

Sequence similaritiesi

Belongs to the type VI collagen family.Curated
Contains 9 VWFA domains.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG410Y0KT. LUCA.
GeneTreeiENSGT00760000119000.
HOGENOMiHOG000111864.
HOVERGENiHBG107743.
InParanoidiA6NMZ7.
KOiK06238.
OMAiFQVTNAM.
OrthoDBiEOG7C2R09.
PhylomeDBiA6NMZ7.
TreeFamiTF318242.

Family and domain databases

Gene3Di3.40.50.410. 8 hits.
InterProiIPR008160. Collagen.
IPR002035. VWF_A.
[Graphical view]
PfamiPF01391. Collagen. 1 hit.
PF00092. VWA. 8 hits.
[Graphical view]
SMARTiSM00327. VWA. 9 hits.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 9 hits.
PROSITEiPS50234. VWFA. 9 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: A6NMZ7-1) [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

        10         20         30         40         50
MMLLILFLVI ICSHISVNQD SGPEYADVVF LVDSSDRLGS KSFPFVKMFI
60 70 80 90 100
TKMISSLPIE ADKYRVALAQ YSDKLHSEFH LSTFKGRSPM LNHLRKNFGF
110 120 130 140 150
IGGSLQIGKA LQEAHRTYFS APANGRDKKQ FPPILVVLAS SESEDNVEEA
160 170 180 190 200
SKALRKDGVK IISVGVQKAS EENLKAMATS QFHFNLRTVR DLSMFSQNMT
210 220 230 240 250
HIIKDVIKYK EGAVDDIFVE ACQGPSMADV VFLLDMSING SEENFDYLKG
260 270 280 290 300
FLEESVSALD IKENCMRVGL VAYSNETKVI NSLSMGINKS EVLQHIQNLS
310 320 330 340 350
PRTGKAYTGA AIKKLRKEVF SARNGSRKNQ GVPQIAVLVT HRDSEDNVTK
360 370 380 390 400
AAVNLRREGV TIFTLGIEGA SDTQLEKIAS HPAEQYVSKL KTFADLAAHN
410 420 430 440 450
QTFLKKLRNQ ITHTVSVFSE RTETLKSGCV DTEEADIYLL IDGSGSTQAT
460 470 480 490 500
DFHEMKTFLS EVVGMFNIAP HKVRVGAVQY ADSWDLEFEI NKYSNKQDLG
510 520 530 540 550
KAIENIRQMG GNTNTGAALN FTLSLLQKAK KQRGNKVPCH LVVLTNGMSK
560 570 580 590 600
DSILEPANRL REEHIRVYAI GIKEANQTQL REIAGEEKRV YYVHDFDALK
610 620 630 640 650
DIRNQVVQEI CTEEACKEMK ADIMFLVDSS GSIGPENFSK MKTFMKNLVS
660 670 680 690 700
KSQIGPDRVQ IGVVQFSDIN KEEFQLNRFM SQSDISNAID QMAHIGQTTL
710 720 730 740 750
TGSALSFVSQ YFSPTKGARP NIRKFLILIT DGEAQDIVKE PAVVLRQEGV
760 770 780 790 800
IIYSVGVFGS NVTQLEEISG RPEMVFYVEN FDILQRIEDD LVFGICSPRE
810 820 830 840 850
ECKRIEVLDV VFVIDSSGSI DYDEYNIMKD FMIGLVKKAD VGKNQVRFGA
860 870 880 890 900
LKYADDPEVL FYLDDFGTKL EVISVLQNDQ AMGGSTYTAE ALGFSDHMFT
910 920 930 940 950
EARGSRLNKG VPQVLIVITD GESHDADKLN ATAKALRDKG ILVLAVGIDG
960 970 980 990 1000
ANPVELLAMA GSSDKYFFVE TFGGLKGIFS DVTASVCNSS KVDCEIDKVD
1010 1020 1030 1040 1050
LVFLMDGSTS IQPNDFKKMK EFLASVVQDF DVSLNRVRIG AAQFSDTYHP
1060 1070 1080 1090 1100
EFPLGTFIGE KEISFQIENI KQIFGNTHIG AALREVEHYF RPDMGSRINT
1110 1120 1130 1140 1150
GTPQVLLVLT DGQSQDEVAQ AAEALRHRGI DIYSVGIGDV DDQQLIQITG
1160 1170 1180 1190 1200
TAEKKLTVHN FDELKKVNKR IVRNICTTAG ESNCFVDVVV GFDVSTQEKG
1210 1220 1230 1240 1250
QTLLEGQPWM ETYLQDILRA ISSLNGVSCE VGTETQVSVA FQVTNAMEKY
1260 1270 1280 1290 1300
SPKFEIYSEN ILNSLKDITV KGPSLLNANL LDSLWDTFQN KSAARGKVVL
1310 1320 1330 1340 1350
LFSDGLDDDV EKLEQKSDEL RKEGLNALIT VALDGPADSS DLADLPYIEF
1360 1370 1380 1390 1400
GKGFEYRTQL SIGMRELGSR LSKQLVNVAE RTCCCLFCKC IGGDGTMGDP
1410 1420 1430 1440 1450
GPPGKRGPPG FKGSEGYLGE EGIAGERGAP GPVGEQGTKG CYGTKGPKGN
1460 1470 1480 1490 1500
RGLNGQEGEV GENGIDGLNG EQGDNGLPGR KGEKGDEGSQ GSPGKRGTPG
1510 1520 1530 1540 1550
DRGAKGLRGD PGAPGVDSSI EGPTGLKGER GRQGRRGWPG PPGTPGSRRK
1560 1570 1580 1590 1600
TAAHGRRGHT GPQGTAGIPG PDGLEGSLGL KGPQGPRGEA GVKGEKGGVG
1610 1620 1630 1640 1650
SKGPQGPPGP GGEAGNQGRL GSQGNKGEPG DLGEKGAVGF PGPRGLQGND
1660 1670 1680 1690 1700
GSPGYGSVGR KGAKGQEGFP GESGPKGEIG DPGGPGETGL KGARGKMISA
1710 1720 1730 1740 1750
GLPGEMGSPG EPGPPGRKGV KGAKGLASFS TCELIQYVRD RSPGRHGKPE
1760 1770 1780 1790 1800
CPVHPTELVF ALDHSRDVTE QEFERMKEMM AFLVRDIKVR ENSCPVGAHI
1810 1820 1830 1840 1850
AILSYNSHAR HLVRFSDAYK KSQLLREIET IPYERSSASR EIGRAMRFIS
1860 1870 1880 1890 1900
RNVFKRTLPG AHTRKIATFF SSGQSADAHS ITTAAMEFGA LEIIPVVITF
1910 1920 1930 1940 1950
SNVPSVRRAF AIDDTGTFQV IVVPSGADYI PALERLQRCT FCYDVCKPDA
1960 1970 1980 1990 2000
SCDQARPPPV QSYMDAAFLL DASRNMGSAE FEDIRAFLGA LLDHFEITPE
2010 2020 2030 2040 2050
PETSVTGDRV ALLSHAPPDF LPNTQKSPVR AEFNLTTYRS KRLMKRHVHE
2060 2070 2080 2090 2100
SVKQLNGDAF IGHALQWTLD NVFLSTPNLR RNKVIFVISA GETSHLDGEI
2110 2120 2130 2140 2150
LKKESLRAKC QGYALFVFSL GPIWDDKELE DLASHPLDHH LVQLGRIHKP
2160 2170 2180 2190 2200
DHSYGVKFVK SFINSIRRAI NKYPPINLKI KCNRLNSIDP KQPPRPFRSF
2210 2220 2230 2240 2250
VPGPLKATLK EDVLQKAKFF QDKKYLSRVA RSGRDDAIQN FMRSTSHTFK
2260
NGRMIESAPK QHD
Length:2,263
Mass (Da):247,173
Last modified:May 20, 2008 - v2
Checksum:iEED4F30ABAED7F30
GO
Isoform 2 (identifier: A6NMZ7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1512-1520: GAPGVDSSI → VSARAANWS
     1521-2263: Missing.

Note: No experimental confirmation available.
Show »
Length:1,520
Mass (Da):166,865
Checksum:i227C6A3808F5FA5F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1429 – 14291A → V in CAH10639 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti345 – 3451E → K.
Corresponds to variant rs4613427 [ dbSNP | Ensembl ].
VAR_043609
Natural varianti370 – 3701A → T.
Corresponds to variant rs9830253 [ dbSNP | Ensembl ].
VAR_043610
Natural varianti461 – 4611E → A.
Corresponds to variant rs11921769 [ dbSNP | Ensembl ].
VAR_043611
Natural varianti556 – 5561P → S.
Corresponds to variant rs59021909 [ dbSNP | Ensembl ].
VAR_061120
Natural varianti1739 – 17391R → Q.
Corresponds to variant rs16830494 [ dbSNP | Ensembl ].
VAR_043612
Natural varianti1799 – 17991H → R.
Corresponds to variant rs7614116 [ dbSNP | Ensembl ].
VAR_043613

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1512 – 15209GAPGVDSSI → VSARAANWS in isoform 2. 1 PublicationVSP_033914
Alternative sequencei1521 – 2263743Missing in isoform 2. 1 PublicationVSP_033915Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM774225 mRNA. Translation: CAO81741.1.
AM774226 mRNA. Translation: CAO81739.1.
AM774227 mRNA. Translation: CAO81740.1.
AC093006 Genomic DNA. No translation available.
AC128683 Genomic DNA. No translation available.
AL713792 mRNA. Translation: CAH10639.2.
CCDSiCCDS46911.1. [A6NMZ7-1]
RefSeqiNP_001096078.1. NM_001102608.1. [A6NMZ7-1]
XP_005247178.1. XM_005247121.3. [A6NMZ7-1]
XP_011510727.1. XM_011512425.1. [A6NMZ7-1]
XP_011510728.1. XM_011512426.1. [A6NMZ7-1]
XP_011510729.1. XM_011512427.1. [A6NMZ7-1]
XP_011510730.1. XM_011512428.1. [A6NMZ7-1]
UniGeneiHs.591282.
Hs.596805.

Genome annotation databases

EnsembliENST00000358511; ENSP00000351310; ENSG00000206384. [A6NMZ7-1]
GeneIDi131873.
KEGGihsa:131873.
UCSCiuc010htl.4. human. [A6NMZ7-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM774225 mRNA. Translation: CAO81741.1.
AM774226 mRNA. Translation: CAO81739.1.
AM774227 mRNA. Translation: CAO81740.1.
AC093006 Genomic DNA. No translation available.
AC128683 Genomic DNA. No translation available.
AL713792 mRNA. Translation: CAH10639.2.
CCDSiCCDS46911.1. [A6NMZ7-1]
RefSeqiNP_001096078.1. NM_001102608.1. [A6NMZ7-1]
XP_005247178.1. XM_005247121.3. [A6NMZ7-1]
XP_011510727.1. XM_011512425.1. [A6NMZ7-1]
XP_011510728.1. XM_011512426.1. [A6NMZ7-1]
XP_011510729.1. XM_011512427.1. [A6NMZ7-1]
XP_011510730.1. XM_011512428.1. [A6NMZ7-1]
UniGeneiHs.591282.
Hs.596805.

3D structure databases

ProteinModelPortaliA6NMZ7.
SMRiA6NMZ7. Positions 26-1325, 1424-1452, 1672-1701.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000351310.

Chemistry

ChEMBLiCHEMBL2364188.

PTM databases

iPTMnetiA6NMZ7.
PhosphoSiteiA6NMZ7.

Polymorphism and mutation databases

BioMutaiCOL6A6.

Proteomic databases

MaxQBiA6NMZ7.
PaxDbiA6NMZ7.
PRIDEiA6NMZ7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000358511; ENSP00000351310; ENSG00000206384. [A6NMZ7-1]
GeneIDi131873.
KEGGihsa:131873.
UCSCiuc010htl.4. human. [A6NMZ7-1]

Organism-specific databases

CTDi131873.
GeneCardsiCOL6A6.
H-InvDBHIX0003677.
HGNCiHGNC:27023. COL6A6.
HPAiHPA045239.
MIMi616613. gene.
neXtProtiNX_A6NMZ7.
PharmGKBiPA165697087.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG410Y0KT. LUCA.
GeneTreeiENSGT00760000119000.
HOGENOMiHOG000111864.
HOVERGENiHBG107743.
InParanoidiA6NMZ7.
KOiK06238.
OMAiFQVTNAM.
OrthoDBiEOG7C2R09.
PhylomeDBiA6NMZ7.
TreeFamiTF318242.

Enzyme and pathway databases

ReactomeiR-HSA-1442490. Collagen degradation.
R-HSA-1650814. Collagen biosynthesis and modifying enzymes.
R-HSA-186797. Signaling by PDGF.
R-HSA-2022090. Assembly of collagen fibrils and other multimeric structures.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-3000178. ECM proteoglycans.
R-HSA-419037. NCAM1 interactions.

Miscellaneous databases

ChiTaRSiCOL6A6. human.
GenomeRNAii131873.
PROiA6NMZ7.
SOURCEiSearch...

Gene expression databases

BgeeiA6NMZ7.
ExpressionAtlasiA6NMZ7. baseline and differential.
GenevisibleiA6NMZ7. HS.

Family and domain databases

Gene3Di3.40.50.410. 8 hits.
InterProiIPR008160. Collagen.
IPR002035. VWF_A.
[Graphical view]
PfamiPF01391. Collagen. 1 hit.
PF00092. VWA. 8 hits.
[Graphical view]
SMARTiSM00327. VWA. 9 hits.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 9 hits.
PROSITEiPS50234. VWFA. 9 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Three novel collagen VI chains with high homology to the alpha 3 chain."
    Gara S.K., Grumati P., Urciuolo A., Bonaldo P., Kobbe B., Koch M., Paulsson M., Wagener R.
    J. Biol. Chem. 283:10658-10670(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1364-2263 (ISOFORM 2).
    Tissue: Lymph node.
  4. "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-198; ASN-275; ASN-288; ASN-298; ASN-930; ASN-988 AND ASN-1290.
    Tissue: Liver.
  5. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiCO6A6_HUMAN
AccessioniPrimary (citable) accession number: A6NMZ7
Secondary accession number(s): A7DZQ0
, A7DZQ1, A7DZQ2, Q69YT0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: June 8, 2016
This is version 81 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 3
    Human chromosome 3: 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

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 one 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.