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P20023

- CR2_HUMAN

UniProt

P20023 - CR2_HUMAN

Protein

Complement receptor type 2

Gene

CR2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 2 (25 Nov 2008)
      Previous versions | rss
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    Functioni

    Receptor for complement C3Dd, for the Epstein-Barr virus on human B-cells and T-cells and for HNRPU. Participates in B lymphocytes activation.1 Publication

    GO - Molecular functioni

    1. complement binding Source: UniProt
    2. complement receptor activity Source: UniProtKB
    3. DNA binding Source: UniProt
    4. protein homodimerization activity Source: MGI
    5. transmembrane signaling receptor activity Source: UniProtKB

    GO - Biological processi

    1. B cell differentiation Source: UniProt
    2. B cell proliferation Source: UniProt
    3. complement activation, classical pathway Source: UniProtKB-KW
    4. immune response Source: UniProtKB
    5. innate immune response Source: UniProtKB-KW

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Complement pathway, Immunity, Innate immunity

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:CR2
    Synonyms:C3DR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:2336. CR2.

    Subcellular locationi

    GO - Cellular componenti

    1. external side of plasma membrane Source: Ensembl
    2. extracellular vesicular exosome Source: UniProt
    3. integral component of membrane Source: UniProtKB
    4. plasma membrane Source: ProtInc
    5. receptor complex Source: MGI

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi103 – 1031R → A: No effect on affinity for C3. 1 Publication
    Mutagenesisi112 – 1121D → A: Reduced affinity for C3. 1 Publication
    Mutagenesisi128 – 1281K → A: Strongly reduced affinity for C3. 1 Publication

    Keywords - Diseasei

    Systemic lupus erythematosus

    Organism-specific databases

    MIMi610927. phenotype.
    614699. phenotype.
    Orphaneti1572. Common variable immunodeficiency.
    536. Systemic lupus erythematosus.
    PharmGKBiPA26857.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Add
    BLAST
    Chaini21 – 10331013Complement receptor type 2PRO_0000006010Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi23 ↔ 65
    Disulfide bondi51 ↔ 82
    Disulfide bondi91 ↔ 132
    Disulfide bondi118 ↔ 146
    Glycosylationi121 – 1211N-linked (GlcNAc...)1 Publication
    Glycosylationi127 – 1271N-linked (GlcNAc...)1 Publication
    Disulfide bondi154 ↔ 197PROSITE-ProRule annotation
    Disulfide bondi183 ↔ 210PROSITE-ProRule annotation
    Disulfide bondi215 ↔ 256PROSITE-ProRule annotation
    Disulfide bondi242 ↔ 271PROSITE-ProRule annotation
    Disulfide bondi276 ↔ 325PROSITE-ProRule annotation
    Glycosylationi294 – 2941N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi305 ↔ 342PROSITE-ProRule annotation
    Disulfide bondi351 ↔ 393PROSITE-ProRule annotation
    Glycosylationi372 – 3721N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi379 ↔ 406PROSITE-ProRule annotation
    Disulfide bondi410 ↔ 453PROSITE-ProRule annotation
    Disulfide bondi439 ↔ 466PROSITE-ProRule annotation
    Disulfide bondi471 ↔ 509PROSITE-ProRule annotation
    Glycosylationi492 – 4921N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi495 ↔ 522PROSITE-ProRule annotation
    Disulfide bondi527 ↔ 576PROSITE-ProRule annotation
    Disulfide bondi556 ↔ 593PROSITE-ProRule annotation
    Disulfide bondi602 ↔ 644PROSITE-ProRule annotation
    Glycosylationi623 – 6231N-linked (GlcNAc...)1 Publication
    Disulfide bondi630 ↔ 657PROSITE-ProRule annotation
    Disulfide bondi662 ↔ 699PROSITE-ProRule annotation
    Glycosylationi682 – 6821N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi685 ↔ 714PROSITE-ProRule annotation
    Disulfide bondi719 ↔ 762PROSITE-ProRule annotation
    Disulfide bondi748 ↔ 779PROSITE-ProRule annotation
    Disulfide bondi788 ↔ 830PROSITE-ProRule annotation
    Glycosylationi800 – 8001N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi816 ↔ 843PROSITE-ProRule annotation
    Glycosylationi823 – 8231N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi851 ↔ 894PROSITE-ProRule annotation
    Glycosylationi861 – 8611N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi880 ↔ 907PROSITE-ProRule annotation
    Glycosylationi911 – 9111N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi912 ↔ 955PROSITE-ProRule annotation
    Disulfide bondi941 ↔ 968PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP20023.
    PRIDEiP20023.

    PTM databases

    PhosphoSiteiP20023.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiP20023.
    BgeeiP20023.
    CleanExiHS_CR2.
    GenevestigatoriP20023.

    Organism-specific databases

    HPAiCAB002659.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi107771. 7 interactions.
    IntActiP20023. 1 interaction.
    MINTiMINT-1508214.
    STRINGi9606.ENSP00000356024.

    Structurei

    Secondary structure

    1
    1033
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi32 – 343
    Beta strandi39 – 424
    Beta strandi46 – 516
    Beta strandi55 – 595
    Beta strandi61 – 666
    Beta strandi68 – 725
    Beta strandi74 – 774
    Beta strandi81 – 844
    Beta strandi99 – 1035
    Beta strandi106 – 1094
    Beta strandi113 – 1186
    Beta strandi122 – 1265
    Beta strandi128 – 1325
    Beta strandi136 – 1416
    Beta strandi145 – 1484

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP20023.
    SMRiP20023. Positions 20-969.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP20023.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini21 – 971951ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1000 – 103334CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei972 – 99928HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini21 – 8464Sushi 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini89 – 14860Sushi 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini152 – 21261Sushi 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini213 – 27361Sushi 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini274 – 34471Sushi 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini349 – 40860Sushi 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini409 – 46860Sushi 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini469 – 52456Sushi 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini525 – 59571Sushi 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini600 – 65960Sushi 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini660 – 71657Sushi 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini717 – 78165Sushi 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini786 – 84560Sushi 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini849 – 90961Sushi 14PROSITE-ProRule annotationAdd
    BLAST
    Domaini910 – 97061Sushi 15PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 15 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Sushi, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG12793.
    HOVERGENiHBG005399.
    KOiK04012.
    OMAiQIRCKAD.
    OrthoDBiEOG7D59MJ.
    PhylomeDBiP20023.
    TreeFamiTF316872.

    Family and domain databases

    InterProiIPR000436. Sushi_SCR_CCP.
    [Graphical view]
    PfamiPF00084. Sushi. 14 hits.
    [Graphical view]
    SMARTiSM00032. CCP. 14 hits.
    [Graphical view]
    SUPFAMiSSF57535. SSF57535. 15 hits.
    PROSITEiPS50923. SUSHI. 15 hits.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform A (identifier: P20023-1) [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

    MGAAGLLGVF LALVAPGVLG ISCGSPPPIL NGRISYYSTP IAVGTVIRYS     50
    CSGTFRLIGE KSLLCITKDK VDGTWDKPAP KCEYFNKYSS CPEPIVPGGY 100
    KIRGSTPYRH GDSVTFACKT NFSMNGNKSV WCQANNMWGP TRLPTCVSVF 150
    PLECPALPMI HNGHHTSENV GSIAPGLSVT YSCESGYLLV GEKIINCLSS 200
    GKWSAVPPTC EEARCKSLGR FPNGKVKEPP ILRVGVTANF FCDEGYRLQG 250
    PPSSRCVIAG QGVAWTKMPV CEEIFCPSPP PILNGRHIGN SLANVSYGSI 300
    VTYTCDPDPE EGVNFILIGE STLRCTVDSQ KTGTWSGPAP RCELSTSAVQ 350
    CPHPQILRGR MVSGQKDRYT YNDTVIFACM FGFTLKGSKQ IRCNAQGTWE 400
    PSAPVCEKEC QAPPNILNGQ KEDRHMVRFD PGTSIKYSCN PGYVLVGEES 450
    IQCTSEGVWT PPVPQCKVAA CEATGRQLLT KPQHQFVRPD VNSSCGEGYK 500
    LSGSVYQECQ GTIPWFMEIR LCKEITCPPP PVIYNGAHTG SSLEDFPYGT 550
    TVTYTCNPGP ERGVEFSLIG ESTIRCTSND QERGTWSGPA PLCKLSLLAV 600
    QCSHVHIANG YKISGKEAPY FYNDTVTFKC YSGFTLKGSS QIRCKADNTW 650
    DPEIPVCEKE TCQHVRQSLQ ELPAGSRVEL VNTSCQDGYQ LTGHAYQMCQ 700
    DAENGIWFKK IPLCKVIHCH PPPVIVNGKH TGMMAENFLY GNEVSYECDQ 750
    GFYLLGEKKL QCRSDSKGHG SWSGPSPQCL RSPPVTRCPN PEVKHGYKLN 800
    KTHSAYSHND IVYVDCNPGF IMNGSRVIRC HTDNTWVPGV PTCIKKAFIG 850
    CPPPPKTPNG NHTGGNIARF SPGMSILYSC DQGYLLVGEA LLLCTHEGTW 900
    SQPAPHCKEV NCSSPADMDG IQKGLEPRKM YQYGAVVTLE CEDGYMLEGS 950
    PQSQCQSDHQ WNPPLAVCRS RSLAPVLCGI AAGLILLTFL IVITLYVISK 1000
    HRARNYYTDT SQKEAFHLEA REVYSVDPYN PAS 1033
    Length:1,033
    Mass (Da):112,916
    Last modified:November 25, 2008 - v2
    Checksum:i7D89DB4A07847E9A
    GO
    Isoform B (identifier: P20023-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         499-524: Missing.
         525-556: ITCPPPPVIYNGAHTGSSLEDFPYGTTVTYTC → NHLPTTPCYLQWGTHREFLRRFSIWNHGHLHM

    Show »
    Length:1,007
    Mass (Da):110,408
    Checksum:iBA75D3B0A8EB5511
    GO
    Isoform C (identifier: P20023-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:1,092
    Mass (Da):119,160
    Checksum:iA52592EB53DE7374
    GO
    Isoform D (identifier: P20023-4) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:1,084
    Mass (Da):118,279
    Checksum:i9C232F47D384E59B
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti457 – 4571Missing in CAA68674. (PubMed:2832506)Curated
    Sequence conflicti646 – 6461A → R in AAA35784. (PubMed:2827171)Curated
    Sequence conflicti667 – 6671Q → D AA sequence (PubMed:3016712)Curated
    Sequence conflicti774 – 7741G → E in AAA35784. (PubMed:2827171)Curated
    Sequence conflicti783 – 7875PPVTR → L in AAA35784. (PubMed:2827171)Curated
    Sequence conflicti844 – 8441I → M in AAA35786. (PubMed:2563370)Curated
    Sequence conflicti844 – 8441I → M in AAB04638. (PubMed:2563370)Curated
    Sequence conflicti886 – 8861L → V in AAA35784. (PubMed:2827171)Curated
    Sequence conflicti890 – 8901A → P in AAA35784. (PubMed:2827171)Curated
    Sequence conflicti902 – 9021Q → G AA sequence (PubMed:3016712)Curated
    Sequence conflicti906 – 9061H → L AA sequence (PubMed:3016712)Curated
    Isoform C (identifier: P20023-3)
    Sequence conflicti663 – 6631S → P in AAA35784. (PubMed:2827171)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti639 – 6391S → N.2 Publications
    Corresponds to variant rs17615 [ dbSNP | Ensembl ].
    VAR_016164
    Natural varianti993 – 9931I → V.1 Publication
    Corresponds to variant rs17258982 [ dbSNP | Ensembl ].
    VAR_016165
    Natural varianti1003 – 10031A → E.2 Publications
    Corresponds to variant rs6540433 [ dbSNP | Ensembl ].
    VAR_016166

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei499 – 52426Missing in isoform B. 1 PublicationVSP_001208Add
    BLAST
    Alternative sequencei525 – 55632ITCPP…VTYTC → NHLPTTPCYLQWGTHREFLR RFSIWNHGHLHM in isoform B. 1 PublicationVSP_001209Add
    BLAST
    Alternative sequencei659 – 6591K → KGCQSPPGLHHGRHTGGNTV FFVSGMTVDYTCDPGYLLVG NKSIHCMPSGNWSPSAPRCE in isoform C and isoform D. 5 PublicationsVSP_001210
    Alternative sequencei716 – 7238Missing in isoform D. 1 PublicationVSP_001211

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26004 mRNA. Translation: AAA35786.1.
    M26016
    , 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.
    CCDSiCCDS1478.1. [P20023-1]
    CCDS31007.1. [P20023-3]
    PIRiJL0028. PL0009.
    RefSeqiNP_001006659.1. NM_001006658.2. [P20023-3]
    NP_001868.2. NM_001877.4. [P20023-1]
    UniGeneiHs.445757.

    Genome annotation databases

    EnsembliENST00000367057; ENSP00000356024; ENSG00000117322. [P20023-3]
    ENST00000367058; ENSP00000356025; ENSG00000117322. [P20023-1]
    GeneIDi1380.
    KEGGihsa:1380.
    UCSCiuc001hfv.3. human. [P20023-3]
    uc001hfw.3. human. [P20023-1]

    Polymorphism databases

    DMDMi215273962.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26004 mRNA. Translation: AAA35786.1 .
    M26016
    , 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 .
    CCDSi CCDS1478.1. [P20023-1 ]
    CCDS31007.1. [P20023-3 ]
    PIRi JL0028. PL0009.
    RefSeqi NP_001006659.1. NM_001006658.2. [P20023-3 ]
    NP_001868.2. NM_001877.4. [P20023-1 ]
    UniGenei Hs.445757.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GHQ X-ray 2.04 B/C 21-153 [» ]
    1LY2 X-ray 1.80 A 22-148 [» ]
    1W2R X-ray - A 21-153 [» ]
    1W2S X-ray - B 21-153 [» ]
    2GSX X-ray - A 21-971 [» ]
    3OED X-ray 3.16 C/D 20-153 [» ]
    ProteinModelPortali P20023.
    SMRi P20023. Positions 20-969.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107771. 7 interactions.
    IntActi P20023. 1 interaction.
    MINTi MINT-1508214.
    STRINGi 9606.ENSP00000356024.

    PTM databases

    PhosphoSitei P20023.

    Polymorphism databases

    DMDMi 215273962.

    Proteomic databases

    PaxDbi P20023.
    PRIDEi P20023.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367057 ; ENSP00000356024 ; ENSG00000117322 . [P20023-3 ]
    ENST00000367058 ; ENSP00000356025 ; ENSG00000117322 . [P20023-1 ]
    GeneIDi 1380.
    KEGGi hsa:1380.
    UCSCi uc001hfv.3. human. [P20023-3 ]
    uc001hfw.3. human. [P20023-1 ]

    Organism-specific databases

    CTDi 1380.
    GeneCardsi GC01P207627.
    GeneReviewsi CR2.
    HGNCi HGNC:2336. CR2.
    HPAi CAB002659.
    MIMi 120650. gene.
    610927. phenotype.
    614699. phenotype.
    neXtProti NX_P20023.
    Orphaneti 1572. Common variable immunodeficiency.
    536. Systemic lupus erythematosus.
    PharmGKBi PA26857.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOVERGENi HBG005399.
    KOi K04012.
    OMAi QIRCKAD.
    OrthoDBi EOG7D59MJ.
    PhylomeDBi P20023.
    TreeFami TF316872.

    Miscellaneous databases

    EvolutionaryTracei P20023.
    GeneWikii Complement_receptor_2.
    GenomeRNAii 1380.
    NextBioi 5605.
    PROi P20023.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P20023.
    Bgeei P20023.
    CleanExi HS_CR2.
    Genevestigatori P20023.

    Family and domain databases

    InterProi IPR000436. Sushi_SCR_CCP.
    [Graphical view ]
    Pfami PF00084. Sushi. 14 hits.
    [Graphical view ]
    SMARTi SM00032. CCP. 14 hits.
    [Graphical view ]
    SUPFAMi SSF57535. SSF57535. 15 hits.
    PROSITEi PS50923. SUSHI. 15 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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.
      , 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. 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. Cited for: VARIANT ASN-639, INVOLVEMENT IN SLEB9.

    Entry informationi

    Entry nameiCR2_HUMAN
    AccessioniPrimary (citable) accession number: P20023
    Secondary accession number(s): C9JHD2
    , Q13866, Q14212, Q53EL2, Q5BKT9, Q5SR46, Q5SR48
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 158 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3