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Reviewed, UniProtKB/Swiss-Prot P39060 (COIA1_HUMAN)

Last modified June 16, 2009. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Collagen alpha-1(XVIII) chain
Cleaved into the following chain:
    1- Recommended name:
            Endostatin
Gene names
Name: COL18A1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length1754 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

COLA18A probably plays a major role in determining the retinal structure as well as in the closure of the neural tube.

Endostatin potently inhibits endothelial cell proliferation and angiogenesis. May inhibit angiogenesis by binding to the heparan sulfate proteoglycans involved in growth factor signaling.

Subcellular location

Secreted › extracellular space › extracellular matrix By similarity.

Tissue specificity

Present in multiple organs with highest levels in liver, lung and kidney.

Post-translational modification

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

Polymorphism

There is an association between a polymorphism in position 1675 and prostate cancer. Heterozygous Asn-1675 individuals have a 2.5 times increased chance of developing prostate cancer as compared with homozygous Asp-1675 individuals.

Involvement in disease

Defects in COL18A1 are a cause of Knobloch syndrome (KNO) [MIM:267750]. KNO is an autosomal recessive disorder defined by the occurrence of high myopia, vitreoretinal degeneration with retinal detachment, macular abnormalities and occipital encephalocele. Ref.10

Sequence similarities

Belongs to the multiplexin collagen family.

Contains 1 FZ (frizzled) domain.

Contains 1 TSP N-terminal (TSPN) domain.

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Alternative products

This entry describes 3 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]
Isoform 1 (identifier: P39060-3)

Also known as: NC1-728;

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.
Note: Produced by alternative promoter usage.
Isoform 2 (identifier: P39060-1)

Also known as: Long; NC-493;

The sequence of this isoform differs from the canonical sequence as follows:
     216-450: Missing.
Note: Produced by alternative splicing of isoform 1.
Isoform 3 (identifier: P39060-2)

Also known as: Short; NC1-303;

The sequence of this isoform differs from the canonical sequence as follows:
     1-415: Missing.
     416-450: QDACWSRLGGGRLPVACASLPTQEDGYCVLIGPAA → MAPRCPWPWPRRRRLLDVLAPLVLLLGVRAASAEP
Note: Produced by alternative promoter usage.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 17541731Collagen alpha-1(XVIII) chain
PRO_0000005793
Chain1572 – 1754183Endostatin
PRO_0000005794

Regions

Domain329 – 446118FZ
Domain456 – 644189TSP N-terminal
Region645 – 751107Nonhelical region 1 (NC1)
Region752 – 78534Triple-helical region 1 (COL1)
Region786 – 79510Nonhelical region 2 (NC2)
Region796 – 87580Triple-helical region 2 (COL2)
Region876 – 89924Nonhelical region 3 (NC3)
Region900 – 1021122Triple-helical region 3 (COL3)
Region1022 – 104423Nonhelical region 4 (NC4)
Region1045 – 112783Triple-helical region 4 (COL4)
Region1128 – 114114Nonhelical region 5 (NC5)
Region1142 – 118342Triple-helical region 5 (COL5)
Region1184 – 119613Nonhelical region 6 (NC6)
Region1197 – 126973Triple-helical region 6 (COL6)
Region1270 – 127910Nonhelical region 7 (NC7)
Region1280 – 131233Triple-helical region 7 (COL7)
Region1313 – 132412Nonhelical region 8 (NC8)
Region1325 – 134622Triple-helical region 8 (COL8)
Region1347 – 13537Nonhelical region 9 (NC9)
Region1354 – 141158Triple-helical region 9 (COL9)
Region1412 – 142413Nonhelical region 10 (NC10)
Region1425 – 144218Triple-helical region 10 (COL10)
Region1443 – 1754312Nonhelical region 11 (NC11)
Motif1330 – 13323Cell attachment site Potential

Sites

Metal binding15721Zinc
Metal binding15741Zinc
Metal binding15821Zinc
Metal binding16471Zinc

Amino acid modifications

Glycosylation681N-linked (GlcNAc...) Potential
Glycosylation1291N-linked (GlcNAc...) Potential
Glycosylation1641N-linked (GlcNAc...) Potential
Glycosylation9261N-linked (GlcNAc...) Potential
Glycosylation15671O-linked (GalNAc...)
CAR_000150
Disulfide bond334 ↔ 397 By similarity
Disulfide bond344 ↔ 390 By similarity
Disulfide bond381 ↔ 419 By similarity
Disulfide bond408 ↔ 443 By similarity
Disulfide bond412 ↔ 432 By similarity
Disulfide bond1604 ↔ 1744 By similarity
Disulfide bond1706 ↔ 1736 By similarity

Natural variations

Alternative sequence1 – 415415Missing in isoform 3.
VSP_023130
Alternative sequence216 – 450235Missing in isoform 2.
VSP_023131
Alternative sequence416 – 45035QDACW…IGPAA → MAPRCPWPWPRRRRLLDVLA PLVLLLGVRAASAEP in isoform 3.
VSP_023132
Natural variant491Q → L Ref.12
VAR_018053
Natural variant1111G → R Ref.12
VAR_018054
Natural variant10761V → I Ref.12 Ref.1 Ref.2 Ref.4 Ref.11
VAR_018055
Natural variant11211P → R Ref.12 Ref.5 Ref.13
VAR_018056
Natural variant16751D → N Decreased activity for binding laminin; increased risk of developing prostate cancer; in compound heterozygotes may cause Knobloch syndrome when in combination with a frameshift/truncating mutation. Ref.12 Ref.2 Ref.11 Ref.7
VAR_012709

Experimental info

Sequence conflict2991R → K in AAR83296. Ref.2
Sequence conflict6631S → F in AAC39658. Ref.1
Sequence conflict6631S → F in AAC39659. Ref.1
Sequence conflict11121V → L in AAA51864. Ref.5
Sequence conflict11471P → R in AAA51864. Ref.5
Sequence conflict11681R → L in AAA51864. Ref.5
Sequence conflict12101P → L in AAA51864. Ref.5
Sequence conflict12991A → P in AAA51864. Ref.5
Sequence conflict13191L → K in AAA51864. Ref.5
Sequence conflict13551P → A in AAA51864. Ref.5
Sequence conflict13581P → A in AAA51864. Ref.5
Sequence conflict1362 – 13643Missing in AAC39658. Ref.1
Sequence conflict1362 – 13643Missing in AAC39659. Ref.1
Sequence conflict1362 – 13643Missing in AAR83296. Ref.2
Sequence conflict1362 – 13643Missing in AAR83297. Ref.2
Sequence conflict1362 – 13643Missing in AAR83298. Ref.2
Sequence conflict1362 – 13643Missing in AAH33715. Ref.4
Sequence conflict1362 – 13643Missing in AAH63833. Ref.4
Sequence conflict1362 – 13643Missing in AAA51864. Ref.5
Sequence conflict14441G → GQ in AAA51864. Ref.5
Sequence conflict15421R → G in AAA51864. Ref.5
Sequence conflict15521A → G in AAA51864. Ref.5
Sequence conflict1561 – 15622LR → CG in AAA51864. Ref.5
Sequence conflict16811R → T in AAF01310. Ref.7
Sequence conflict16851W → R in AAK50626. Ref.8
Sequence conflict17211S → Y in AAF01310. Ref.7
Sequence conflict17361C → S in AAK50626. Ref.8

Secondary structure

1 .............................. 1754
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (NC1-728) [UniParc].

Last modified November 25, 2008. Version 5.
Checksum: 23A327DCBD3B328D

FASTA1,754178,188
        10         20         30         40         50         60 
MAPYPCGCHI LLLLFCCLAA ARANLLNLNW LWFNNEDTSH AATTIPEPQG PLPVQPTADT 

        70         80         90        100        110        120 
TTHVTPRNGS TEPATAPGSP EPPSELLEDG QDTPTSAESP DAPEENIAGV GAEILNVAKG 

       130        140        150        160        170        180 
IRSFVQLWND TVPTESLARA ETLVLETPVG PLALAGPSST PQENGTTLWP SRGIPSSPGA 

       190        200        210        220        230        240 
HTTEAGTLPA PTPSPPSLGR PWAPLTGPSV PPPSSGRASL SSLLGGAPPW GSLQDPDSQG 

       250        260        270        280        290        300 
LSPAAAAPSQ QLQRPDVRLR TPLLHPLVMG SLGKHAAPSA FSSGLPGALS QVAVTTLTRD 

       310        320        330        340        350        360 
SGAWVSHVAN SVGPGLANNS ALLGADPEAP AGRCLPLPPS LPVCGHLGIS RFWLPNHLHH 

       370        380        390        400        410        420 
ESGEQVRAGA RAWGGLLQTH CHPFLAWFFC LLLVPPCGSV PPPAPPPCCQ FCEALQDACW 

       430        440        450        460        470        480 
SRLGGGRLPV ACASLPTQED GYCVLIGPAA ERISEEVGLL QLLGDPPPQQ VTQTDDPDVG 

       490        500        510        520        530        540 
LAYVFGPDAN SGQVARYHFP SLFFRDFSLL FHIRPATEGP GVLFAITDSA QAMVLLGVKL 

       550        560        570        580        590        600 
SGVQDGHQDI SLLYTEPGAG QTHTAASFRL PAFVGQWTHL ALSVAGGFVA LYVDCEEFQR 

       610        620        630        640        650        660 
MPLARSSRGL ELEPGAGLFV AQAGGADPDK FQGVIAELKV RRDPQVSPMH CLDEEGDDSD 

       670        680        690        700        710        720 
GASGDSGSGL GDARELLREE TGAALKPRLP APPPVTTPPL AGGSSTEDSR SEEVEEQTTV 

       730        740        750        760        770        780 
ASLGAQTLPG SDSVSTWDGS VRTPGGRVKE GGLKGQKGEP GVPGPPGRAG PPGSPCLPGP 

       790        800        810        820        830        840 
PGLPCPVSPL GPAGPALQTV PGPQGPPGPP GRDGTPGRDG EPGDPGEDGK PGDTGPQGFP 

       850        860        870        880        890        900 
GTPGDVGPKG DKGDPGVGER GPPGPQGPPG PPGPSFRHDK LTFIDMEGSG FGGDLEALRG 

       910        920        930        940        950        960 
PRGFPGPPGP PGVPGLPGEP GRFGVNSSDV PGPAGLPGVP GREGPPGFPG LPGPPGPPGR 

       970        980        990       1000       1010       1020 
EGPPGRTGQK GSLGEAGAPG HKGSKGAPGP AGARGESGLA GAPGPAGPPG PPGPPGPPGP 

      1030       1040       1050       1060       1070       1080 
GLPAGFDDME GSGGPFWSTA RSADGPQGPP GLPGLKGDPG VPGLPGAKGE VGADGVPGFP 

      1090       1100       1110       1120       1130       1140 
GLPGREGIAG PQGPKGDRGS RGEKGDPGKD GVGQPGLPGP PGPPGPVVYV SEQDGSVLSV 

      1150       1160       1170       1180       1190       1200 
PGPEGRPGFA GFPGPAGPKG NLGSKGERGS PGPKGEKGEP GSIFSPDGGA LGPAQKGAKG 

      1210       1220       1230       1240       1250       1260 
EPGFRGPPGP YGRPGYKGEI GFPGRPGRPG MNGLKGEKGE PGDASLGFGM RGMPGPPGPP 

      1270       1280       1290       1300       1310       1320 
GPPGPPGTPV YDSNVFAESS RPGPPGLPGN QGPPGPKGAK GEVGPPGPPG QFPFDFLQLE 

      1330       1340       1350       1360       1370       1380 
AEMKGEKGDR GDAGQKGERG EPGGGGFFGS SLPGPPGPPG PPGPRGYPGI PGPKGESIRG 

      1390       1400       1410       1420       1430       1440 
QPGPPGPQGP PGIGYEGRQG PPGPPGPPGP PSFPGPHRQT ISVPGPPGPP GPPGPPGTMG 

      1450       1460       1470       1480       1490       1500 
ASSGVRLWAT RQAMLGQVHE VPEGWLIFVA EQEELYVRVQ NGFRKVQLEA RTPLPRGTDN 

      1510       1520       1530       1540       1550       1560 
EVAALQPPVV QLHDSNPYPR REHPHPTARP WRADDILASP PRLPEPQPYP GAPHHSSYVH 

      1570       1580       1590       1600       1610       1620 
LRPARPTSPP AHSHRDFQPV LHLVALNSPL SGGMRGIRGA DFQCFQQARA VGLAGTFRAF 

      1630       1640       1650       1660       1670       1680 
LSSRLQDLYS IVRRADRAAV PIVNLKDELL FPSWEALFSG SEGPLKPGAR IFSFDGKDVL 

      1690       1700       1710       1720       1730       1740 
RHPTWPQKSV WHGSDPNGRR LTESYCETWR TEAPSATGQA SSLLGGRLLG QSAASCHHAY 

      1750 
IVLCIENSFM TASK

« Hide

Isoform 2 (Long) (NC-493).

Checksum: 7456050495512DE2
Show »

FASTA1,519154,018
Isoform 3 (Short) (NC1-303).

Checksum: A8171B3EC21CBBF0
Show »

FASTA1,339135,761

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References

« Hide 'large scale' references
[1]"Complete primary structure of two variant forms of human type XVIII collagen and tissue-specific differences in the expression of the corresponding transcripts."
Saarela J., Ylikarppa R., Rehn M., Purmonen S., Pihlajaniemi T.
Matrix Biol. 16:319-328(1998) [PubMed: 9503365] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), VARIANT ILE-1076.
[2]"Characterization of the human type XVIII collagen gene and proteolytic processing and tissue location of the variant containing a frizzled motif."
Elamaa H., Snellman A., Rehn M., Autio-Harmainen H., Pihlajaniemi T.
Matrix Biol. 22:427-442(2003) [PubMed: 14614989] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3), VARIANTS ILE-1076 AND ASN-1675.
[3]"The DNA sequence of human chromosome 21."
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A. expand/collapse author list , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
Nature 405:311-319(2000) [PubMed: 10830953] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT ILE-1076.
Tissue: Kidney and PNS.
[5]"Cloning of cDNA and genomic DNA encoding human type XVIII collagen and localization of the alpha 1(XVIII) collagen gene to mouse chromosome 10 and human chromosome 21."
Oh S.P., Warman M.L., Seldin M.F., Cheng S., Knoll J.H., Timmons S., Olsen B.R.
Genomics 19:494-499(1994) [PubMed: 8188291] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1069-1754, VARIANT ARG-1121.
[6]"Inhibition effect in vitro of purified endostatin expressed in Pichia pastoris."
Feng Y., Cui L.B., Liu C.X., Ma Q.J.
Sheng Wu Gong Cheng Xue Bao 17:278-282(2001) [PubMed: 11517600] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1568-1754.
[7]"Cloning and expression of human endostatin gene in Escherichia coli."
Zhi-Yong H., Biao L., Wei-Jie Z., Xiang-Fu W.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1572-1754, VARIANT ASN-1675.
Tissue: Placenta.
[8]"Endostatin promotes delayed secondary damage following traumatic brain injury."
Deininger M.H., Trautmann K., Schluesener H.J.
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1642-1743.
[9]"Zinc-dependent dimers observed in crystals of human endostatin."
Ding Y.-H., Javaherian K., Lo K.-M., Chopra R., Boehm T., Lanciotti J., Harris B.A., Li Y., Shapiro R., Hohenester E., Timpl R., Folkman J., Wiley D.C.
Proc. Natl. Acad. Sci. U.S.A. 95:10443-10448(1998) [PubMed: 9724722] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1572-1749, ZINC-BINDING SITE.
[10]"Collagen XVIII, containing an endogenous inhibitor of angiogenesis and tumor growth, plays a critical role in the maintenance of retinal structure and in neural tube closure."
Sertie A.L., Sossi V., Camargo A.A., Zatz M., Brahe C., Passos-Bueno M.R.
Hum. Mol. Genet. 9:2051-2058(2000) [PubMed: 10942434] [Abstract]
Cited for: INVOLVEMENT IN KNOBLOCH SYNDROME.
[11]"A polymorphism in endostatin, an angiogenesis inhibitor, predisposes for the development of prostatic adenocarcinoma."
Iughetti P., Suzuki O., Godoi P.H., Alves V.A., Sertie A.L., Zorick T., Soares F., Camargo A.A., Moreira E.S., di Loreto C., Moreira-Filho C.A., Simpson A., Oliva G., Passos-Bueno M.R.
Cancer Res. 61:7375-7378(2001) [PubMed: 11606364] [Abstract]
Cited for: VARIANTS ILE-1076 AND ASN-1675.
[12]"Knobloch syndrome: novel mutations in COL18A1, evidence for genetic heterogeneity, and a functionally impaired polymorphism in endostatin."
Menzel O., Bekkeheien R.C.J., Reymond A., Fukai N., Boye E., Kosztolanyi G., Aftimos S., Deutsch S., Scott H.S., Olsen B.R., Antonarakis S.E., Guipponi M.
Hum. Mutat. 23:77-84(2004) [PubMed: 14695535] [Abstract]
Cited for: VARIANTS LEU-49; ARG-111; ILE-1076 AND ARG-1121, CHARACTERIZATION OF VARIANT ASN-1675.
[13]"DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome."
Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K., Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L., Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A., Abbott S. expand/collapse author list , Locke D., Hillier L.W., Miner T., Fulton L., Magrini V., Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R., Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E., Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A., DiPersio J.F., Wilson R.K.
Nature 456:66-72(2008) [PubMed: 18987736] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-1121.
+Additional computationally mapped references.

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Web resources

GeneReviews

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Cross-references

Sequence databases

AF018081 mRNA. Translation: AAC39658.1.
AF018082 mRNA. Translation: AAC39659.1.
AY484971 expand/collapse EMBL AC list , AY484968, AY484969, AY484970 Genomic DNA. Translation: AAR83296.1.
AY484971 expand/collapse EMBL AC list , AY484968, AY484969, AY484970 Genomic DNA. Translation: AAR83297.1.
AY484971 expand/collapse EMBL AC list , AY484967, AY484969, AY484970 Genomic DNA. Translation: AAR83298.1.
AL163302 Genomic DNA. Translation: CAB90482.1.
BX322561 Genomic DNA. No translation available.
BC033715 mRNA. Translation: AAH33715.1.
BC063833 mRNA. Translation: AAH63833.1.
L22548 mRNA. Translation: AAA51864.1.
AF416592 mRNA. Translation: AAL37720.1.
AF184060 mRNA. Translation: AAF01310.1. Different initiation.
AF333247 mRNA. Translation: AAK50626.1.
IPIIPI00022822.
IPI00414694.
IPI00783931.
RefSeqNP_085059.2.
NP_569711.2.
NP_569712.2.
UniGeneHs.517356

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1BNLX-ray2.90A/B/C/D1572-1749[»]
SMRP39060. Positions 1572-1749.
ModBaseSearch...

PTM databases

GlycoSuiteDBP39060.

Genome annotation databases

EnsemblENSG00000182871. Homo sapiens. [Contig view]
GeneID80781.
KEGGhsa:80781.

Organism-specific databases

GeneCardsGC21P045649.
HGNCHGNC:2195. COL18A1.
HPACAB001961.
HPA011025.
MIM120328. gene.
267750. phenotype.
Orphanet1571. Knobloch syndrome.
PharmGKBPA26711.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP39060.

Enzyme and pathway databases

Pathway_Interaction_DBhnf3apathway. FOXA1 transcription factor network.

Gene expression databases

ArrayExpressP39060.
BgeeP39060.
GermOnlineENSG00000182871. Homo sapiens.

Family and domain databases

InterProIPR008160. Collagen.
IPR010363. DUF959_COL18_N.
IPR010515. Endostatin.
[Graphical view]
PfamPF01391. Collagen. 8 hits.
PF06121. DUF959. 1 hit.
PF06482. Endostatin. 1 hit.
[Graphical view]
ProDomPD000007. Clg_helix. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS50038. FZ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio71187.
SOURCESearch...

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Entry information

Entry nameCOIA1_HUMAN
AccessionPrimary (citable) accession number: P39060
Secondary accession number(s): Q58EX6 expand/collapse secondary AC list , Q6RZ39, Q6RZ40, Q6RZ41, Q8N4S4, Q8WXI5, Q96T70, Q9UK38, Q9Y6Q7, Q9Y6Q8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 25, 2008
Last modified: June 16, 2009
This is version 102 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 21

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents