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P20023 (CR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 157. Feed History...

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

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) [Reference 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.12

Subunit structure

Interacts (via Sushi domain 1 and 2) with C3dg. Ref.18

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

Systemic lupus erythematosus 9 (SLEB9) [MIM:610927]: A chronic, relapsing, inflammatory, and often febrile multisystemic disorder of connective tissue, characterized principally by involvement of the skin, joints, kidneys and serosal membranes. It is of unknown etiology, but is thought to represent a failure of the regulatory mechanisms of the autoimmune system. The disease is marked by a wide range of system dysfunctions, an elevated erythrocyte sedimentation rate, and the formation of LE cells in the blood or bone marrow.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.19

Immunodeficiency, common variable, 7 (CVID7) [MIM:614699]: A primary immunodeficiency characterized by antibody deficiency, hypogammaglobulinemia, recurrent bacterial infections and an inability to mount an antibody response to antigen. The defect results from a failure of B-cell differentiation and impaired secretion of immunoglobulins; the numbers of circulating B-cells is usually in the normal range, but can be low.
Note: The disease is caused by mutations affecting the gene represented in this entry. 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.

Ontologies

Keywords
   Biological processComplement pathway
Immunity
Innate immunity
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseSystemic lupus erythematosus
   DomainRepeat
Signal
Sushi
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processB cell differentiation

Inferred from direct assay PubMed 2995485. Source: UniProt

B cell proliferation

Inferred from direct assay PubMed 2995485. Source: UniProt

complement activation, classical pathway

Inferred from electronic annotation. Source: UniProtKB-KW

immune response

Non-traceable author statement Ref.3. Source: UniProtKB

innate immune response

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentexternal side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

integral component of membrane

Non-traceable author statement Ref.3. Source: UniProtKB

plasma membrane

Non-traceable author statement Ref.1. Source: ProtInc

receptor complex

Inferred from direct assay PubMed 23382219. Source: MGI

   Molecular_functionDNA binding

Inferred from direct assay PubMed 22885687. Source: UniProt

complement binding

Inferred from direct assay PubMed 11034390. Source: UniProt

complement receptor activity

Non-traceable author statement Ref.3. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay PubMed 11728339. Source: MGI

transmembrane signaling receptor activity

Non-traceable author statement Ref.3. Source: UniProtKB

Complete GO annotation...

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 → KGCQSPPGLHHGRHTGGNTVFFVSGMTVDYTCDPGYLLVGNKSIHCMPSGNWSPSAPRCE
Isoform D (identifier: P20023-4)

The sequence of this isoform differs from the canonical sequence as follows:
     659-659: K → KGCQSPPGLHHGRHTGGNTVFFVSGMTVDYTCDPGYLLVGNKSIHCMPSGNWSPSAPRCE
     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

Glycosylation1211N-linked (GlcNAc...) Ref.16
Glycosylation1271N-linked (GlcNAc...) Ref.16
Glycosylation2941N-linked (GlcNAc...) Potential
Glycosylation3721N-linked (GlcNAc...) Potential
Glycosylation4921N-linked (GlcNAc...) Potential
Glycosylation6231N-linked (GlcNAc...) Ref.13
Glycosylation6821N-linked (GlcNAc...) Potential
Glycosylation8001N-linked (GlcNAc...) Potential
Glycosylation8231N-linked (GlcNAc...) Potential
Glycosylation8611N-linked (GlcNAc...) Potential
Glycosylation9111N-linked (GlcNAc...) Potential
Disulfide bond23 ↔ 65 Ref.15 Ref.16 Ref.18
Disulfide bond51 ↔ 82 Ref.15 Ref.16 Ref.18
Disulfide bond91 ↔ 132 Ref.15 Ref.16 Ref.18
Disulfide bond118 ↔ 146 Ref.15 Ref.16 Ref.18
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 → KGCQSPPGLHHGRHTGGNTV FFVSGMTVDYTCDPGYLLVG NKSIHCMPSGNWSPSAPRCE in isoform C and isoform D.
VSP_001210
Alternative sequence716 – 7238Missing in isoform D.
VSP_001211
Natural variant6391S → N. Ref.9 Ref.19
Corresponds to variant rs17615 [ dbSNP | Ensembl ].
VAR_016164
Natural variant9931I → V. Ref.2
Corresponds to variant rs17258982 [ dbSNP | Ensembl ].
VAR_016165
Natural variant10031A → E. Ref.1 Ref.3
Corresponds to variant rs6540433 [ dbSNP | Ensembl ].
VAR_016166

Experimental info

Mutagenesis1031R → A: No effect on affinity for C3. Ref.18
Mutagenesis1121D → A: Reduced affinity for C3. Ref.18
Mutagenesis1281K → A: Strongly reduced affinity for C3. Ref.18
Sequence conflict4571Missing in CAA68674. Ref.2
Sequence conflict6461A → R in AAA35784. Ref.3
Sequence conflict6671Q → D AA sequence Ref.10
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.10
Sequence conflict9061H → L AA sequence Ref.10
Isoform C:
Sequence conflict6631S → P in AAA35784. Ref.3

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 [UniParc].

Checksum: BA75D3B0A8EB5511
Show »

FASTA1,007110,408
Isoform C [UniParc].

Checksum: A52592EB53DE7374
Show »

FASTA1,092119,160
Isoform D [UniParc].

Checksum: 9C232F47D384E59B
Show »

FASTA1,084118,279

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; C AND D).
[5]"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. expand/collapse author list , 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] (ISOFORM C).
Tissue: Synovium.
[6]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
Tissue: Spleen.
[7]Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B., Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O., Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I., Nickerson D.A.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND C), VARIANT ASN-639.
Tissue: Lymph.
[10]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 226-233; 256-267; 332-341; 667-677 AND 898-908.
[11]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 492-556 (ISOFORM B).
[12]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A RECEPTOR FOR HNRPU.
[13]"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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-623.
Tissue: Leukemic T-cell.
[14]"Genetic CD21 deficiency is associated with hypogammaglobulinemia."
Thiel J., Kimmig L., Salzer U., Grudzien M., Lebrecht D., Hagena T., Draeger R., Volxen N., Bergbreiter A., Jennings S., Gutenberger S., Aichem A., Illges H., Hannan J.P., Kienzler A.K., Rizzi M., Eibel H., Peter H.H. expand/collapse author list , Warnatz K., Grimbacher B., Rump J.A., Schlesier M.
J. Allergy Clin. Immunol. 129:801-810(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CVID7.
[15]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF 21-153 IN COMPLEX WITH C3D, DISULFIDE BONDS.
[16]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-148, DISULFIDE BONDS, GLYCOSYLATION AT ASN-121 AND ASN-127.
[17]"The 15 SCR flexible extracellular domains of human complement receptor type 2 can mediate multiple ligand and antigen interactions."
Gilbert H.E., Asokan R., Holers V.M., Perkins S.J.
J. Mol. Biol. 362:1132-1147(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY SCATTERING SOLUTION STRUCTURE OF 21-971.
[18]"A crystal structure of the complex between human complement receptor 2 and its ligand C3d."
van den Elsen J.M., Isenman D.E.
Science 332:608-611(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.16 ANGSTROMS) OF 996-1303 IN COMPLEX WITH C3, INTERACTION WITH CR2, DISULFIDE BONDS, MUTAGENESIS OF ARG-103; ASP-112 AND LYS-128.
[19]"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] [Europe PMC] [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.
AK223627 mRNA. Translation: BAD97347.1.
AK301496 mRNA. Translation: BAG63007.1.
EF064746 Genomic DNA. Translation: ABK41929.1.
AL391597, AL691452 Genomic DNA. Translation: CAH72949.1.
AL391597, AL691452 Genomic DNA. Translation: CAH72950.1.
AL691452, AL391597 Genomic DNA. Translation: CAI16729.1.
AL691452, AL391597 Genomic DNA. Translation: CAI16730.1.
BC090937 mRNA. Translation: AAH90937.1.
BC136394 mRNA. Translation: AAI36395.1.
S62696 mRNA. Translation: AAB27186.1.
CCDSCCDS1478.1. [P20023-1]
CCDS31007.1. [P20023-3]
PIRPL0009. JL0028.
RefSeqNP_001006659.1. NM_001006658.2. [P20023-3]
NP_001868.2. NM_001877.4. [P20023-1]
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[»]
3OEDX-ray3.16C/D20-153[»]
ProteinModelPortalP20023.
SMRP20023. Positions 20-969.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107771. 7 interactions.
IntActP20023. 1 interaction.
MINTMINT-1508214.
STRING9606.ENSP00000356024.

PTM databases

PhosphoSiteP20023.

Polymorphism databases

DMDM215273962.

Proteomic databases

PaxDbP20023.
PRIDEP20023.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367057; ENSP00000356024; ENSG00000117322. [P20023-3]
ENST00000367058; ENSP00000356025; ENSG00000117322. [P20023-1]
GeneID1380.
KEGGhsa:1380.
UCSCuc001hfv.3. human. [P20023-3]
uc001hfw.3. human. [P20023-1]

Organism-specific databases

CTD1380.
GeneCardsGC01P207627.
GeneReviewsCR2.
HGNCHGNC:2336. CR2.
HPACAB002659.
MIM120650. gene.
610927. phenotype.
614699. phenotype.
neXtProtNX_P20023.
Orphanet1572. Common variable immunodeficiency.
536. Systemic lupus erythematosus.
PharmGKBPA26857.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG005399.
KOK04012.
OMAQIRCKAD.
OrthoDBEOG7D59MJ.
PhylomeDBP20023.
TreeFamTF316872.

Gene expression databases

ArrayExpressP20023.
BgeeP20023.
CleanExHS_CR2.
GenevestigatorP20023.

Family and domain databases

InterProIPR000436. Sushi_SCR_CCP.
[Graphical view]
PfamPF00084. Sushi. 14 hits.
[Graphical view]
SMARTSM00032. CCP. 14 hits.
[Graphical view]
SUPFAMSSF57535. SSF57535. 15 hits.
PROSITEPS50923. SUSHI. 15 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP20023.
GeneWikiComplement_receptor_2.
GenomeRNAi1380.
NextBio5605.
PROP20023.
SOURCESearch...

Entry information

Entry nameCR2_HUMAN
AccessionPrimary (citable) accession number: P20023
Secondary accession number(s): C9JHD2 expand/collapse secondary AC list , Q13866, Q14212, Q53EL2, Q5BKT9, Q5SR46, Q5SR48
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human cell differentiation molecules

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