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P20023

- CR2_HUMAN

UniProt

P20023 - CR2_HUMAN

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Protein

Complement receptor type 2

Gene

CR2

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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiP20023.
CleanExiHS_CR2.
ExpressionAtlasiP20023. baseline and differential.
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.
GeneTreeiENSGT00760000118803.
HOVERGENiHBG005399.
InParanoidiP20023.
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

        10         20         30         40         50
MGAAGLLGVF LALVAPGVLG ISCGSPPPIL NGRISYYSTP IAVGTVIRYS
60 70 80 90 100
CSGTFRLIGE KSLLCITKDK VDGTWDKPAP KCEYFNKYSS CPEPIVPGGY
110 120 130 140 150
KIRGSTPYRH GDSVTFACKT NFSMNGNKSV WCQANNMWGP TRLPTCVSVF
160 170 180 190 200
PLECPALPMI HNGHHTSENV GSIAPGLSVT YSCESGYLLV GEKIINCLSS
210 220 230 240 250
GKWSAVPPTC EEARCKSLGR FPNGKVKEPP ILRVGVTANF FCDEGYRLQG
260 270 280 290 300
PPSSRCVIAG QGVAWTKMPV CEEIFCPSPP PILNGRHIGN SLANVSYGSI
310 320 330 340 350
VTYTCDPDPE EGVNFILIGE STLRCTVDSQ KTGTWSGPAP RCELSTSAVQ
360 370 380 390 400
CPHPQILRGR MVSGQKDRYT YNDTVIFACM FGFTLKGSKQ IRCNAQGTWE
410 420 430 440 450
PSAPVCEKEC QAPPNILNGQ KEDRHMVRFD PGTSIKYSCN PGYVLVGEES
460 470 480 490 500
IQCTSEGVWT PPVPQCKVAA CEATGRQLLT KPQHQFVRPD VNSSCGEGYK
510 520 530 540 550
LSGSVYQECQ GTIPWFMEIR LCKEITCPPP PVIYNGAHTG SSLEDFPYGT
560 570 580 590 600
TVTYTCNPGP ERGVEFSLIG ESTIRCTSND QERGTWSGPA PLCKLSLLAV
610 620 630 640 650
QCSHVHIANG YKISGKEAPY FYNDTVTFKC YSGFTLKGSS QIRCKADNTW
660 670 680 690 700
DPEIPVCEKE TCQHVRQSLQ ELPAGSRVEL VNTSCQDGYQ LTGHAYQMCQ
710 720 730 740 750
DAENGIWFKK IPLCKVIHCH PPPVIVNGKH TGMMAENFLY GNEVSYECDQ
760 770 780 790 800
GFYLLGEKKL QCRSDSKGHG SWSGPSPQCL RSPPVTRCPN PEVKHGYKLN
810 820 830 840 850
KTHSAYSHND IVYVDCNPGF IMNGSRVIRC HTDNTWVPGV PTCIKKAFIG
860 870 880 890 900
CPPPPKTPNG NHTGGNIARF SPGMSILYSC DQGYLLVGEA LLLCTHEGTW
910 920 930 940 950
SQPAPHCKEV NCSSPADMDG IQKGLEPRKM YQYGAVVTLE CEDGYMLEGS
960 970 980 990 1000
PQSQCQSDHQ WNPPLAVCRS RSLAPVLCGI AAGLILLTFL IVITLYVISK
1010 1020 1030
HRARNYYTDT SQKEAFHLEA REVYSVDPYN PAS
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.
GeneTreei ENSGT00760000118803.
HOVERGENi HBG005399.
InParanoidi P20023.
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

Bgeei P20023.
CleanExi HS_CR2.
ExpressionAtlasi P20023. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 159 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