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P20023 (CR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified August 10, 2010. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
Customize displayNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Names and origin

Protein namesRecommended name:
Complement receptor type 2

Short name=Cr2
Alternative name(s):
Complement C3d receptor
Epstein-Barr virus receptor
Short name=EBV receptor
CD_antigen=CD21
Gene names
Name:CR2
Synonyms:C3DR
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1033 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Receptor for complement C3Dd, for the Epstein-Barr virus on human B-cells and T-cells and for HNRPU. Participates in B lymphocytes activation. Ref.9

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Mature B-lymphocytes, T-lymphocytes, pharyngeal epithelial cells, astrocytes and follicular dendritic cells of the spleen.

Involvement in disease

Genetic variations in CR2 are associated with susceptibility to systemic lupus erythematosus type 9 (SLEB9) [MIM:610927]. Systemic lupus erythematosus (SLE) is a chronic autoimmune disease with a complex genetic basis. SLE is an inflammatory, and often febrile multisystemic disorder of connective tissue characterized principally by involvement of the skin, joints, kidneys, and serosal membranes. It is thought to represent a failure of the regulatory mechanisms of the autoimmune system. Ref.14

Sequence similarities

Belongs to the receptors of complement activation (RCA) family.

Contains 15 Sushi (CCP/SCR) domains.

Sequence caution

The sequence AAA35784.1 differs from that shown. Reason: Frameshift at positions 758, 769 and 776.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: P20023-1)

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.
Isoform B (identifier: P20023-2)

The sequence of this isoform differs from the canonical sequence as follows:
     499-524: Missing.
     525-556: ITCPPPPVIYNGAHTGSSLEDFPYGTTVTYTC → NHLPTTPCYLQWGTHREFLRRFSIWNHGHLHM
Isoform C (identifier: P20023-3)

The sequence of this isoform differs from the canonical sequence as follows:
     659-659: K → KGCQPPPGLHHGRHTGGNTVFFVSGMTVDYTCDPGYLLVGNKSIHCMPSGNWSPSAPRCE
Isoform D (identifier: P20023-4)

The sequence of this isoform differs from the canonical sequence as follows:
     659-659: K → KGCQPPPGLHHGRHTGGNTVFFVSGMTVDYTCDPGYLLVGNKSIHCMPSGNWSPSAPRCE
     716-723: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020
Chain21 – 10331013Complement receptor type 2
PRO_0000006010

Regions

Topological domain21 – 971951Extracellular Potential
Transmembrane972 – 99928Helical; Potential
Topological domain1000 – 103334Cytoplasmic Potential
Domain21 – 8464Sushi 1
Domain89 – 14860Sushi 2
Domain152 – 21261Sushi 3
Domain213 – 27361Sushi 4
Domain274 – 34471Sushi 5
Domain349 – 40860Sushi 6
Domain409 – 46860Sushi 7
Domain469 – 52456Sushi 8
Domain525 – 59571Sushi 9
Domain600 – 65960Sushi 10
Domain660 – 71657Sushi 11
Domain717 – 78165Sushi 12
Domain786 – 84560Sushi 13
Domain849 – 90961Sushi 14
Domain910 – 97061Sushi 15

Amino acid modifications

Modified residue10291Phosphotyrosine Ref.10
Glycosylation1211N-linked (GlcNAc...) Ref.13
Glycosylation1271N-linked (GlcNAc...) Ref.13
Glycosylation2941N-linked (GlcNAc...) Potential
Glycosylation3721N-linked (GlcNAc...) Potential
Glycosylation4921N-linked (GlcNAc...) Potential
Glycosylation6231N-linked (GlcNAc...) Ref.11
Glycosylation6821N-linked (GlcNAc...) Potential
Glycosylation8001N-linked (GlcNAc...) Potential
Glycosylation8231N-linked (GlcNAc...) Potential
Glycosylation8611N-linked (GlcNAc...) Potential
Glycosylation9111N-linked (GlcNAc...) Potential
Disulfide bond23 ↔ 65 Ref.13 Ref.12
Disulfide bond51 ↔ 82 Ref.13 Ref.12
Disulfide bond91 ↔ 132 Ref.13 Ref.12
Disulfide bond118 ↔ 146 Ref.13 Ref.12
Disulfide bond154 ↔ 197 By similarity
Disulfide bond183 ↔ 210 By similarity
Disulfide bond215 ↔ 256 By similarity
Disulfide bond242 ↔ 271 By similarity
Disulfide bond276 ↔ 325 By similarity
Disulfide bond305 ↔ 342 By similarity
Disulfide bond351 ↔ 393 By similarity
Disulfide bond379 ↔ 406 By similarity
Disulfide bond410 ↔ 453 By similarity
Disulfide bond439 ↔ 466 By similarity
Disulfide bond471 ↔ 509 By similarity
Disulfide bond495 ↔ 522 By similarity
Disulfide bond527 ↔ 576 By similarity
Disulfide bond556 ↔ 593 By similarity
Disulfide bond602 ↔ 644 By similarity
Disulfide bond630 ↔ 657 By similarity
Disulfide bond662 ↔ 699 By similarity
Disulfide bond685 ↔ 714 By similarity
Disulfide bond719 ↔ 762 By similarity
Disulfide bond748 ↔ 779 By similarity
Disulfide bond788 ↔ 830 By similarity
Disulfide bond816 ↔ 843 By similarity
Disulfide bond851 ↔ 894 By similarity
Disulfide bond880 ↔ 907 By similarity
Disulfide bond912 ↔ 955 By similarity
Disulfide bond941 ↔ 968 By similarity

Natural variations

Alternative sequence499 – 52426Missing in isoform B.
VSP_001208
Alternative sequence525 – 55632ITCPP…VTYTC → NHLPTTPCYLQWGTHREFLR RFSIWNHGHLHM in isoform B.
VSP_001209
Alternative sequence6591K → KGCQPPPGLHHGRHTGGNTV FFVSGMTVDYTCDPGYLLVG NKSIHCMPSGNWSPSAPRCE in isoform C and isoform D.
VSP_001210
Alternative sequence716 – 7238Missing in isoform D.
VSP_001211
Natural variant6391S → N. [dbSNP:rs17615] Ref.14 Ref.6
VAR_016164
Natural variant9931I → V. [dbSNP:rs17258982] Ref.2
VAR_016165
Natural variant10031A → E. [dbSNP:rs6540433] Ref.1 Ref.3
VAR_016166

Experimental info

Sequence conflict4571Missing in CAA68674. Ref.2
Sequence conflict6461A → R in AAA35784. Ref.3
Sequence conflict6671Q → D AA sequence Ref.7
Sequence conflict7741G → E in AAA35784. Ref.3
Sequence conflict783 – 7875PPVTR → L in AAA35784. Ref.3
Sequence conflict8441I → M in AAA35786. Ref.1
Sequence conflict8441I → M in AAB04638. Ref.1
Sequence conflict8861L → V in AAA35784. Ref.3
Sequence conflict8901A → P in AAA35784. Ref.3
Sequence conflict9021Q → G AA sequence Ref.7
Sequence conflict9061H → L AA sequence Ref.7

Secondary structure

........................... 1033
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: 7D89DB4A07847E9A

FASTA1,033112,916
        10         20         30         40         50         60 
MGAAGLLGVF LALVAPGVLG ISCGSPPPIL NGRISYYSTP IAVGTVIRYS CSGTFRLIGE 

        70         80         90        100        110        120 
KSLLCITKDK VDGTWDKPAP KCEYFNKYSS CPEPIVPGGY KIRGSTPYRH GDSVTFACKT 

       130        140        150        160        170        180 
NFSMNGNKSV WCQANNMWGP TRLPTCVSVF PLECPALPMI HNGHHTSENV GSIAPGLSVT 

       190        200        210        220        230        240 
YSCESGYLLV GEKIINCLSS GKWSAVPPTC EEARCKSLGR FPNGKVKEPP ILRVGVTANF 

       250        260        270        280        290        300 
FCDEGYRLQG PPSSRCVIAG QGVAWTKMPV CEEIFCPSPP PILNGRHIGN SLANVSYGSI 

       310        320        330        340        350        360 
VTYTCDPDPE EGVNFILIGE STLRCTVDSQ KTGTWSGPAP RCELSTSAVQ CPHPQILRGR 

       370        380        390        400        410        420 
MVSGQKDRYT YNDTVIFACM FGFTLKGSKQ IRCNAQGTWE PSAPVCEKEC QAPPNILNGQ 

       430        440        450        460        470        480 
KEDRHMVRFD PGTSIKYSCN PGYVLVGEES IQCTSEGVWT PPVPQCKVAA CEATGRQLLT 

       490        500        510        520        530        540 
KPQHQFVRPD VNSSCGEGYK LSGSVYQECQ GTIPWFMEIR LCKEITCPPP PVIYNGAHTG 

       550        560        570        580        590        600 
SSLEDFPYGT TVTYTCNPGP ERGVEFSLIG ESTIRCTSND QERGTWSGPA PLCKLSLLAV 

       610        620        630        640        650        660 
QCSHVHIANG YKISGKEAPY FYNDTVTFKC YSGFTLKGSS QIRCKADNTW DPEIPVCEKE 

       670        680        690        700        710        720 
TCQHVRQSLQ ELPAGSRVEL VNTSCQDGYQ LTGHAYQMCQ DAENGIWFKK IPLCKVIHCH 

       730        740        750        760        770        780 
PPPVIVNGKH TGMMAENFLY GNEVSYECDQ GFYLLGEKKL QCRSDSKGHG SWSGPSPQCL 

       790        800        810        820        830        840 
RSPPVTRCPN PEVKHGYKLN KTHSAYSHND IVYVDCNPGF IMNGSRVIRC HTDNTWVPGV 

       850        860        870        880        890        900 
PTCIKKAFIG CPPPPKTPNG NHTGGNIARF SPGMSILYSC DQGYLLVGEA LLLCTHEGTW 

       910        920        930        940        950        960 
SQPAPHCKEV NCSSPADMDG IQKGLEPRKM YQYGAVVTLE CEDGYMLEGS PQSQCQSDHQ 

       970        980        990       1000       1010       1020 
WNPPLAVCRS RSLAPVLCGI AAGLILLTFL IVITLYVISK HRARNYYTDT SQKEAFHLEA 

      1030 
REVYSVDPYN PAS 

« Hide

Isoform B.

Checksum: BA75D3B0A8EB5511
Show »

FASTA1,007110,408
Isoform C.

Checksum: 24C5A3C4344CCBD6
Show »

FASTA1,092119,170
Isoform D.

Checksum: EEC08419A7EA1484
Show »

FASTA1,084118,289

References

« Hide 'large scale' references
[1]"Genomic organization and polymorphisms of the human C3d/Epstein-Barr virus receptor."
Fujisaku A., Harley J.B., Frank M.B., Gruner B.A., Frazier B., Holers V.M.
J. Biol. Chem. 264:2118-2125(1989) [PubMed: 2563370] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANT GLU-1003.
[2]"Structure of the human B lymphocyte receptor for C3d and the Epstein-Barr virus and relatedness to other members of the family of C3/C4 binding proteins."
Weis J.J., Toothaker L.E., Smith J.A., Weis J.H., Fearon D.T.
J. Exp. Med. 167:1047-1066(1988) [PubMed: 2832506] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-993.
Tissue: B-cell.
[3]"Molecular cloning of the cDNA encoding the Epstein-Barr virus.C3d receptor (complement receptor type 2) of human b lymphocytes."
Moore M., Cooper N., Tack B., Nemerow G.
Proc. Natl. Acad. Sci. U.S.A. 84:9194-9198(1987) [PubMed: 2827171] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), VARIANT GLU-1003.
[4]"Evidence for a new transcript of the Epstein-Barr virus/C3d receptor (CR2, CD21) which is due to alternative exon usage."
Barel M., Balbo M., Frade R.
Mol. Immunol. 35:1025-1031(1998) [PubMed: 10068037] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; C AND D).
[5]"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. expand/collapse author list , 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: 16710414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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 A), VARIANT ASN-639.
Tissue: Lymph.
[7]"Identification of a partial cDNA clone for the C3d/Epstein-Barr virus receptor of human B lymphocytes: homology with the receptor for fragments C3b and C4b of the third and fourth components of complement."
Weis J.J., Fearon D.T., Klickstein L.B., Wong W.W., Richards S.A., de Bruyn Kops A., Smith J.A., Weis J.H.
Proc. Natl. Acad. Sci. U.S.A. 83:5639-5643(1986) [PubMed: 3016712] [Abstract]
Cited for: PROTEIN SEQUENCE OF 226-233; 256-267; 332-341; 667-677 AND 898-908.
[8]"Characterization of the EBV/C3d receptor on the human Jurkat T cell line: evidence for a novel transcript."
Sinha S.K., Todd S.C., Hedrick J.A., Speiser C.L., Lambris J.D., Tsoukas C.D.
J. Immunol. 150:5311-5320(1993) [PubMed: 8390533] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 492-556 (ISOFORM B).
[9]"Binding sites of the Epstein-Barr virus and C3d receptor (CR2, CD21) for its three intracellular ligands, the p53 anti-oncoprotein, the p68 calcium binding protein and the nuclear p120 ribonucleoprotein."
Barel M., Balbo M., Gauffre A., Frade R.
Mol. Immunol. 32:389-397(1995) [PubMed: 7753047] [Abstract]
Cited for: FUNCTION AS A RECEPTOR FOR HNRPU.
[10]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1029, MASS SPECTROMETRY.
Tissue: Lung carcinoma.
[11]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed: 19349973] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-623, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[12]"Structure of complement receptor 2 in complex with its C3d ligand."
Szakonyi G., Guthridge J.M., Li D., Young K., Holers V.M., Chen X.S.
Science 292:1725-1728(2001) [PubMed: 11387479] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF 21-153 IN COMPLEX WITH C3D, DISULFIDE BONDS.
[13]"The crystal structure of human CD21: Implications for Epstein-Barr virus and C3d binding."
Prota A.E., Sage D.R., Stehle T., Fingeroth J.D.
Proc. Natl. Acad. Sci. U.S.A. 99:10641-10646(2002) [PubMed: 12122212] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-148, DISULFIDE BONDS, GLYCOSYLATION AT ASN-121 AND ASN-127.
[14]"Association of a common complement receptor 2 haplotype with increased risk of systemic lupus erythematosus."
Wu H., Boackle S.A., Hanvivadhanakul P., Ulgiati D., Grossman J.M., Lee Y., Shen N., Abraham L.J., Mercer T.R., Park E., Hebert L.A., Rovin B.H., Birmingham D.J., Chang D.-M., Chen C.J., McCurdy D., Badsha H.M., Thong B.Y.H. expand/collapse author list , Chng H.H., Arnett F.C., Wallace D.J., Yu C.Y., Hahn B.H., Cantor R.M., Tsao B.P.
Proc. Natl. Acad. Sci. U.S.A. 104:3961-3966(2007) [PubMed: 17360460] [Abstract]
Cited for: VARIANT ASN-639, INVOLVEMENT IN SLEB9.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M26004 mRNA. Translation: AAA35786.1.
M26016 expand/collapse EMBL AC list , M24007, M24008, M24009, M24010, M24011, M26009, M26010, M26011, M26012, M26013, M26014, M26015 Genomic DNA. Translation: AAB04638.1.
Y00649 mRNA. Translation: CAA68674.1.
J03565 mRNA. Translation: AAA35784.1. Frameshift.
AL391597, AL691452 Genomic DNA. Translation: CAH72949.1.
AL691452, AL391597 Genomic DNA. Translation: CAI16730.1.
BC090937 mRNA. Translation: AAH90937.1.
S62696 mRNA. Translation: AAB27186.1.
IPIIPI00216985.
IPI00216986.
IPI00216987.
IPI00292859.
PIRPL0009. JL0028.
RefSeqNP_001006659.1.
NP_001868.2.
UniGeneHs.445757.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GHQX-ray2.04B/C21-153[»]
1LY2X-ray1.80A22-148[»]
1W2RX-ray-A21-153[»]
1W2SX-ray-B21-153[»]
2GSXX-ray-A21-971[»]
ProteinModelPortalP20023.
SMRP20023. Positions 178-213, 276-407, 349-473, 805-914, 849-916.
ModBaseSearch...

Protein-protein interaction databases

STRINGP20023.

PTM databases

PhosphoSiteP20023.

Proteomic databases

PRIDEP20023.

Genome annotation databases

EnsemblENST00000367058; ENSP00000356025; ENSG00000117322; Homo sapiens. [Genome view]
GeneID1380.
KEGGhsa:1380.

Organism-specific databases

CTD1380.
GeneCardsGC01P207627.
HGNCHGNC:2336. CR2.
HPACAB002659.
MIM120650. gene.
610927. phenotype.
Orphanet101994. Complement regulatory proteins anomaly.
PharmGKBPA24743.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG08926.
HOVERGENHBG005399.

Gene expression databases

ArrayExpressP20023.
BgeeP20023.
CleanExHS_CR2.
GenevestigatorP20023.
GermOnlineENSG00000117322. Homo sapiens.

Family and domain databases

InterProIPR016060. Complement_control_module.
IPR000436. Sushi_SCR_CCP.
[Graphical view]
Gene3DG3DSA:2.10.70.10. Complement_control_module. 11 hits.
PfamPF00084. Sushi. 14 hits.
[Graphical view]
SMARTSM00032. CCP. 14 hits.
[Graphical view]
SUPFAMSSF57535. Complement_control_module. 14 hits.
PROSITEPS50923. SUSHI. 15 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio5605.
SOURCESearch...

Entry information

Entry nameCR2_HUMAN
AccessionPrimary (citable) accession number: P20023
Secondary accession number(s): Q13866 expand/collapse secondary AC list , Q14212, Q5BKT9, Q5SR48
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: November 25, 2008
Last modified: August 10, 2010
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Relevant documents

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries

Human chromosome 1

Human chromosome 1: 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