CD20_HUMAN
ID CD20_HUMAN Reviewed; 297 AA.
AC P11836; A6NMS4; B4DT24; P08984; Q13963;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=B-lymphocyte antigen CD20;
DE AltName: Full=B-lymphocyte surface antigen B1;
DE AltName: Full=Bp35;
DE AltName: Full=Leukocyte surface antigen Leu-16;
DE AltName: Full=Membrane-spanning 4-domains subfamily A member 1;
DE AltName: CD_antigen=CD20;
GN Name=MS4A1; Synonyms=CD20;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3260267; DOI=10.1084/jem.167.6.1975;
RA Stamenkovic I., Seed B.;
RT "Analysis of two cDNA clones encoding the B lymphocyte antigen CD20 (B1,
RT Bp35), a type III integral membrane protein.";
RL J. Exp. Med. 167:1975-1980(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2448768; DOI=10.1073/pnas.85.1.208;
RA Tedder T.F., Streuli M., Schlossman S.F., Saito H.;
RT "Isolation and structure of a cDNA encoding the B1 (CD20) cell-surface
RT antigen of human B lymphocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:208-212(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2456210; DOI=10.1002/j.1460-2075.1988.tb02867.x;
RA Einfeld D.A., Brown J.P., Valentine M.A., Clark E.A., Ledbetter J.A.;
RT "Molecular cloning of the human B cell CD20 receptor predicts a hydrophobic
RT protein with multiple transmembrane domains.";
RL EMBO J. 7:711-717(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2466899;
RA Tedder T.F., Klejman G., Schlossman S.F., Saito H.;
RT "Structure of the gene encoding the human B lymphocyte differentiation
RT antigen CD20 (B1).";
RL J. Immunol. 142:2560-2568(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP FUNCTION.
RX PubMed=3925015;
RA Tedder T.F., Boyd A.W., Freedman A.S., Nadler L.M., Schlossman S.F.;
RT "The B cell surface molecule B1 is functionally linked with B cell
RT activation and differentiation.";
RL J. Immunol. 135:973-979(1985).
RN [10]
RP PHOSPHORYLATION BY PKC.
RX PubMed=2472394; DOI=10.1016/s0021-9258(18)60461-2;
RA Valentine M.A., Meier K.E., Rossie S., Clark E.A.;
RT "Phosphorylation of the CD20 phosphoprotein in resting B lymphocytes.
RT Regulation by protein kinase C.";
RL J. Biol. Chem. 264:11282-11287(1989).
RN [11]
RP FUNCTION, SUBUNIT, AND PHOSPHORYLATION.
RX PubMed=7684739; DOI=10.1083/jcb.121.5.1121;
RA Bubien J.K., Zhou L.J., Bell P.D., Frizzell R.A., Tedder T.F.;
RT "Transfection of the CD20 cell surface molecule into ectopic cell types
RT generates a Ca2+ conductance found constitutively in B lymphocytes.";
RL J. Cell Biol. 121:1121-1132(1993).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12920111; DOI=10.1074/jbc.m308802200;
RA Li H., Ayer L.M., Lytton J., Deans J.P.;
RT "Store-operated cation entry mediated by CD20 in membrane rafts.";
RL J. Biol. Chem. 278:42427-42434(2003).
RN [13]
RP EPITOPE MAPPING, AND MUTAGENESIS OF THR-159; ASN-163; ASN-166; ALA-170 AND
RP PRO-172.
RX PubMed=16785532; DOI=10.4049/jimmunol.177.1.362;
RA Teeling J.L., Mackus W.J.M., Wiegman L.J.J.M., van den Brakel J.H.N.,
RA Beers S.A., French R.R., van Meerten T., Ebeling S., Vink T.,
RA Slootstra J.W., Parren P.W.H.I., Glennie M.J., van de Winkel J.G.J.;
RT "The biological activity of human CD20 monoclonal antibodies is linked to
RT unique epitopes on CD20.";
RL J. Immunol. 177:362-371(2006).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [15]
RP FUNCTION, SUBUNIT, AND IMMUNOGLOBULIN-BINDING.
RX PubMed=18474602; DOI=10.1074/jbc.m800784200;
RA Polyak M.J., Li H., Shariat N., Deans J.P.;
RT "CD20 homo-oligomers physically associate with the B cell antigen receptor.
RT Dissociation upon receptor engagement and recruitment of phosphoproteins
RT and calmodulin-binding proteins.";
RL J. Biol. Chem. 283:18545-18552(2008).
RN [16]
RP INVOLVEMENT IN CVID5.
RX PubMed=20038800; DOI=10.1172/jci40231;
RA Kuijpers T.W., Bende R.J., Baars P.A., Grummels A., Derks I.A.M.,
RA Dolman K.M., Beaumont T., Tedder T.F., van Noesel C.J.M., Eldering E.,
RA van Lier R.A.W.;
RT "CD20 deficiency in humans results in impaired T cell-independent antibody
RT responses.";
RL J. Clin. Invest. 120:214-222(2010).
RN [17]
RP PALMITOYLATION AT CYS-111 AND CYS-220, TOPOLOGY, AND SUBCELLULAR LOCATION.
RC TISSUE=B-cell;
RX PubMed=22615937; DOI=10.1371/journal.pone.0037187;
RA Ivaldi C., Martin B.R., Kieffer-Jaquinod S., Chapel A., Levade T.,
RA Garin J., Journet A.;
RT "Proteomic analysis of S-acylated proteins in human B cells reveals
RT palmitoylation of the immune regulators CD20 and CD23.";
RL PLoS ONE 7:E37187-E37187(2012).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 163-187, AND DISULFIDE BOND.
RX PubMed=17395584; DOI=10.1074/jbc.m701654200;
RA Du J., Wang H., Zhong C., Peng B., Zhang M., Li B., Huo S., Guo Y.,
RA Ding J.;
RT "Structural basis for recognition of CD20 by therapeutic antibody
RT Rituximab.";
RL J. Biol. Chem. 282:15073-15080(2007).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 163-187, AND DISULFIDE BOND.
RX PubMed=18346788; DOI=10.1016/j.molimm.2008.01.034;
RA Du J., Wang H., Zhong C., Peng B., Zhang M., Li B., Hou S., Guo Y.,
RA Ding J.;
RT "Crystal structure of chimeric antibody C2H7 Fab in complex with a CD20
RT peptide.";
RL Mol. Immunol. 45:2861-2868(2008).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 163-187 IN COMPLEX WITH ANTIBODY,
RP AND DISULFIDE BOND.
RX PubMed=21444918; DOI=10.1182/blood-2010-09-305847;
RA Niederfellner G., Lammens A., Mundigl O., Georges G.J., Schaefer W.,
RA Schwaiger M., Franke A., Wiechmann K., Jenewein S., Slootstra J.W.,
RA Timmerman P., Brannstrom A., Lindstrom F., Mossner E., Umana P.,
RA Hopfner K.P., Klein C.;
RT "Epitope characterization and crystal structure of GA101 provide insights
RT into the molecular basis for type I/II distinction of CD20 antibodies.";
RL Blood 118:358-367(2011).
CC -!- FUNCTION: B-lymphocyte-specific membrane protein that plays a role in
CC the regulation of cellular calcium influx necessary for the
CC development, differentiation, and activation of B-lymphocytes
CC (PubMed:3925015, PubMed:7684739, PubMed:12920111). Functions as a
CC store-operated calcium (SOC) channel component promoting calcium influx
CC after activation by the B-cell receptor/BCR (PubMed:7684739,
CC PubMed:12920111, PubMed:18474602). {ECO:0000269|PubMed:12920111,
CC ECO:0000269|PubMed:18474602, ECO:0000269|PubMed:3925015,
CC ECO:0000269|PubMed:7684739}.
CC -!- SUBUNIT: Forms homotetramers (PubMed:7684739, PubMed:18474602).
CC Interacts with the heavy and light chains of cell surface IgM, the
CC antigen-binding components of the BCR (PubMed:18474602).
CC {ECO:0000269|PubMed:18474602, ECO:0000269|PubMed:7684739}.
CC -!- INTERACTION:
CC P11836; O00590: ACKR2; NbExp=3; IntAct=EBI-2808234, EBI-13379418;
CC P11836; Q13520: AQP6; NbExp=3; IntAct=EBI-2808234, EBI-13059134;
CC P11836; Q9HA82: CERS4; NbExp=3; IntAct=EBI-2808234, EBI-2622997;
CC P11836; Q86T13: CLEC14A; NbExp=3; IntAct=EBI-2808234, EBI-17710733;
CC P11836; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-2808234, EBI-6942903;
CC P11836; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-2808234, EBI-18304435;
CC P11836; Q96P31-6: FCRL3; NbExp=3; IntAct=EBI-2808234, EBI-17443171;
CC P11836; Q5T7V8: GORAB; NbExp=3; IntAct=EBI-2808234, EBI-3917143;
CC P11836; O15529: GPR42; NbExp=3; IntAct=EBI-2808234, EBI-18076404;
CC P11836; Q8NBQ5: HSD17B11; NbExp=3; IntAct=EBI-2808234, EBI-1052304;
CC P11836; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-2808234, EBI-18053395;
CC P11836; P16871: IL7R; NbExp=3; IntAct=EBI-2808234, EBI-80490;
CC P11836; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-2808234, EBI-749265;
CC P11836; A8MZ59: LEUTX; NbExp=3; IntAct=EBI-2808234, EBI-17490413;
CC P11836; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-2808234, EBI-373355;
CC P11836; Q15546: MMD; NbExp=3; IntAct=EBI-2808234, EBI-17873222;
CC P11836; P11836: MS4A1; NbExp=2; IntAct=EBI-2808234, EBI-2808234;
CC P11836; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-2808234, EBI-3923617;
CC P11836; Q9BRK0: REEP2; NbExp=3; IntAct=EBI-2808234, EBI-11337973;
CC P11836; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-2808234, EBI-7545592;
CC P11836; Q6ZMZ0: RNF19B; NbExp=3; IntAct=EBI-2808234, EBI-2466594;
CC P11836; Q99942: RNF5; NbExp=3; IntAct=EBI-2808234, EBI-348482;
CC P11836; Q14973: SLC10A1; NbExp=3; IntAct=EBI-2808234, EBI-3923031;
CC P11836; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-2808234, EBI-18159983;
CC P11836; P54219-3: SLC18A1; NbExp=3; IntAct=EBI-2808234, EBI-17595455;
CC P11836; Q9NQQ7-3: SLC35C2; NbExp=3; IntAct=EBI-2808234, EBI-17295964;
CC P11836; Q8WY91: THAP4; NbExp=3; IntAct=EBI-2808234, EBI-726691;
CC P11836; A0PK05: TMEM72; NbExp=3; IntAct=EBI-2808234, EBI-12878352;
CC P11836; Q6ZT21: TMPPE; NbExp=3; IntAct=EBI-2808234, EBI-11724433;
CC P11836; Q9Y320: TMX2; NbExp=3; IntAct=EBI-2808234, EBI-6447886;
CC P11836; Q5TGU0: TSPO2; NbExp=3; IntAct=EBI-2808234, EBI-12195249;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12920111,
CC ECO:0000269|PubMed:22615937}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:22615937}. Cell membrane
CC {ECO:0000269|PubMed:22615937}; Lipid-anchor
CC {ECO:0000269|PubMed:22615937}. Note=Constitutively associated with
CC membrane rafts. {ECO:0000269|PubMed:12920111}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P11836-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P11836-2; Sequence=VSP_057058;
CC -!- TISSUE SPECIFICITY: Expressed on B-cells.
CC -!- PTM: Phosphorylated on serines and threonines in resting B-cells.
CC Protein kinase C/PKC can use CD20 as substrate.
CC {ECO:0000269|PubMed:2472394}.
CC -!- DISEASE: Immunodeficiency, common variable, 5 (CVID5) [MIM:613495]: A
CC primary immunodeficiency characterized by antibody deficiency,
CC hypogammaglobulinemia, recurrent bacterial infections and an inability
CC to mount an antibody response to antigen. The defect results from a
CC failure of B-cell differentiation and impaired secretion of
CC immunoglobulins; the numbers of circulating B-cells is usually in the
CC normal range, but can be low. {ECO:0000269|PubMed:20038800}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- PHARMACEUTICAL: Monoclonal antibodies (mAb) against CD20 are used to
CC treat B-cell non-Hodgkin lymphoma (NHL). These antibodies include
CC Rituximab (Mabthera), Britumomab (Zevalin) and Tositumomab (Bexxar).
CC CD20 engaged by mAb can generate transmembrane signals capable of
CC directly controlling cell growth and triggering cell death in certain
CC tumors. Alternatively, mAb can mediate complement-dependent
CC cytotoxicity.
CC -!- SIMILARITY: Belongs to the MS4A family. {ECO:0000305}.
CC -!- CAUTION: Epitope 1, mapped in PubMed:16785532, is predicted to be
CC buried in the membrane. Its accessibility to the extracellular space,
CC and thus to antibody recognition, is not explained. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=CD20 entry;
CC URL="https://en.wikipedia.org/wiki/CD20";
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DR EMBL; X12530; CAA31046.1; -; mRNA.
DR EMBL; M27394; AAA35581.1; -; Genomic_DNA.
DR EMBL; X07203; CAA30179.1; -; mRNA.
DR EMBL; X07204; CAA30180.1; -; mRNA.
DR EMBL; L23419; AAA88911.1; -; Genomic_DNA.
DR EMBL; L23415; AAA88911.1; JOINED; Genomic_DNA.
DR EMBL; L23416; AAA88911.1; JOINED; Genomic_DNA.
DR EMBL; L23417; AAA88911.1; JOINED; Genomic_DNA.
DR EMBL; M27395; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001034; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK300025; BAG61836.1; -; mRNA.
DR EMBL; AP003127; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW73889.1; -; Genomic_DNA.
DR EMBL; BC002807; AAH02807.1; -; mRNA.
DR CCDS; CCDS31570.1; -. [P11836-1]
DR PIR; A30586; A30586.
DR RefSeq; NP_068769.2; NM_021950.3. [P11836-1]
DR RefSeq; NP_690605.1; NM_152866.2. [P11836-1]
DR PDB; 2OSL; X-ray; 2.60 A; P/Q=163-187.
DR PDB; 3BKY; X-ray; 2.61 A; P=163-187.
DR PDB; 3PP4; X-ray; 1.60 A; P=163-187.
DR PDB; 6VJA; EM; 3.30 A; C/D=41-297.
DR PDB; 6Y90; EM; 3.69 A; A/B=45-216.
DR PDB; 6Y92; EM; 4.73 A; A/B=41-218.
DR PDB; 6Y97; EM; 4.33 A; A/B=45-213.
DR PDB; 6Y9A; EM; 4.20 A; A/B=45-213.
DR PDBsum; 2OSL; -.
DR PDBsum; 3BKY; -.
DR PDBsum; 3PP4; -.
DR PDBsum; 6VJA; -.
DR PDBsum; 6Y90; -.
DR PDBsum; 6Y92; -.
DR PDBsum; 6Y97; -.
DR PDBsum; 6Y9A; -.
DR AlphaFoldDB; P11836; -.
DR SMR; P11836; -.
DR BioGRID; 107369; 47.
DR CORUM; P11836; -.
DR IntAct; P11836; 35.
DR MINT; P11836; -.
DR STRING; 9606.ENSP00000433277; -.
DR ChEMBL; CHEMBL2058; -.
DR DrugBank; DB00078; Ibritumomab tiuxetan.
DR DrugBank; DB08935; Obinutuzumab.
DR DrugBank; DB11988; Ocrelizumab.
DR DrugBank; DB06650; Ofatumumab.
DR DrugBank; DB00073; Rituximab.
DR DrugBank; DB09336; Technetium Tc-99m nofetumomab merpentan.
DR DrugBank; DB00081; Tositumomab.
DR DrugCentral; P11836; -.
DR GuidetoPHARMACOLOGY; 2628; -.
DR TCDB; 1.A.37.1.1; the cd20 ca(2+) channel (cd20) family.
DR GlyGen; P11836; 1 site.
DR iPTMnet; P11836; -.
DR PhosphoSitePlus; P11836; -.
DR SwissPalm; P11836; -.
DR BioMuta; MS4A1; -.
DR DMDM; 115968; -.
DR jPOST; P11836; -.
DR MassIVE; P11836; -.
DR MaxQB; P11836; -.
DR PaxDb; P11836; -.
DR PeptideAtlas; P11836; -.
DR PRIDE; P11836; -.
DR ProteomicsDB; 5066; -.
DR ProteomicsDB; 52807; -. [P11836-1]
DR ABCD; P11836; 81 sequenced antibodies.
DR Antibodypedia; 3497; 4004 antibodies from 61 providers.
DR CPTC; P11836; 1 antibody.
DR DNASU; 931; -.
DR Ensembl; ENST00000345732.9; ENSP00000314620.7; ENSG00000156738.18. [P11836-1]
DR Ensembl; ENST00000389939.2; ENSP00000374589.2; ENSG00000156738.18. [P11836-1]
DR Ensembl; ENST00000528313.1; ENSP00000432270.1; ENSG00000156738.18. [P11836-2]
DR Ensembl; ENST00000534668.6; ENSP00000433277.1; ENSG00000156738.18. [P11836-1]
DR Ensembl; ENST00000674194.1; ENSP00000501369.1; ENSG00000156738.18. [P11836-1]
DR GeneID; 931; -.
DR KEGG; hsa:931; -.
DR MANE-Select; ENST00000345732.9; ENSP00000314620.7; NM_152866.3; NP_690605.1.
DR UCSC; uc001npq.3; human. [P11836-1]
DR CTD; 931; -.
DR DisGeNET; 931; -.
DR GeneCards; MS4A1; -.
DR HGNC; HGNC:7315; MS4A1.
DR HPA; ENSG00000156738; Tissue enriched (lymphoid).
DR MalaCards; MS4A1; -.
DR MIM; 112210; gene.
DR MIM; 613495; phenotype.
DR neXtProt; NX_P11836; -.
DR OpenTargets; ENSG00000156738; -.
DR Orphanet; 1572; Common variable immunodeficiency.
DR PharmGKB; PA31111; -.
DR VEuPathDB; HostDB:ENSG00000156738; -.
DR eggNOG; ENOG502S6Z3; Eukaryota.
DR GeneTree; ENSGT00510000048781; -.
DR HOGENOM; CLU_082137_0_0_1; -.
DR InParanoid; P11836; -.
DR OMA; HFLKMER; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; P11836; -.
DR TreeFam; TF335157; -.
DR PathwayCommons; P11836; -.
DR SignaLink; P11836; -.
DR SIGNOR; P11836; -.
DR BioGRID-ORCS; 931; 10 hits in 1069 CRISPR screens.
DR ChiTaRS; MS4A1; human.
DR EvolutionaryTrace; P11836; -.
DR GeneWiki; CD20; -.
DR GenomeRNAi; 931; -.
DR Pharos; P11836; Tclin.
DR PRO; PR:P11836; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P11836; protein.
DR Bgee; ENSG00000156738; Expressed in epithelium of nasopharynx and 139 other tissues.
DR ExpressionAtlas; P11836; baseline and differential.
DR Genevisible; P11836; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0044853; C:plasma membrane raft; IDA:UniProtKB.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019865; F:immunoglobulin binding; IDA:UniProtKB.
DR GO; GO:0023026; F:MHC class II protein complex binding; HDA:UniProtKB.
DR GO; GO:0042113; P:B cell activation; IDA:UniProtKB.
DR GO; GO:0030183; P:B cell differentiation; IDA:UniProtKB.
DR GO; GO:0042100; P:B cell proliferation; NAS:UniProtKB.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:1902656; P:calcium ion import into cytosol; IDA:UniProtKB.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006959; P:humoral immune response; NAS:UniProtKB.
DR GO; GO:1905665; P:positive regulation of calcium ion import across plasma membrane; IEA:Ensembl.
DR GO; GO:0051262; P:protein tetramerization; IDA:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR GO; GO:0002115; P:store-operated calcium entry; IMP:UniProtKB.
DR InterPro; IPR007237; CD20-like.
DR InterPro; IPR030417; MS4A.
DR InterPro; IPR030418; MS4A1.
DR PANTHER; PTHR23320; PTHR23320; 1.
DR PANTHER; PTHR23320:SF79; PTHR23320:SF79; 1.
DR Pfam; PF04103; CD20; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; B-cell activation; Cell membrane;
KW Disulfide bond; Lipoprotein; Membrane; Palmitate; Pharmaceutical;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..297
FT /note="B-lymphocyte antigen CD20"
FT /id="PRO_0000158627"
FT TOPO_DOM 1..56
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..84
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 106..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..188
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 74..80
FT /note="Epitope 1"
FT REGION 146..160
FT /note="Epitope 2"
FT REGION 168..175
FT /note="Epitope 3 (recognized by antibodies, including
FT Rituximab)"
FT REGION 247..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..280
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19437"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19437"
FT MOD_RES 239
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19437"
FT LIPID 111
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:22615937"
FT LIPID 220
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:22615937"
FT DISULFID 167..183
FT /evidence="ECO:0000269|PubMed:17395584,
FT ECO:0000269|PubMed:18346788, ECO:0000269|PubMed:21444918"
FT VAR_SEQ 38..204
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057058"
FT MUTAGEN 159
FT /note="T->K: Abrogates recognition by some antibodies; when
FT associated with D-163 and D-166. Slight decrease of
FT rituximab binding; when associated with D-163 and D-166."
FT /evidence="ECO:0000269|PubMed:16785532"
FT MUTAGEN 163
FT /note="N->D: Decreased binding of some antibodies. No
FT effect on rituximab binding."
FT /evidence="ECO:0000269|PubMed:16785532"
FT MUTAGEN 166
FT /note="N->D: Decreased binding of some antibodies. No
FT effect on rituximab binding."
FT /evidence="ECO:0000269|PubMed:16785532"
FT MUTAGEN 170
FT /note="A->S: Abrogates recognition by therapeutic
FT antibodies, including rituximab; when associated with S-
FT 172."
FT /evidence="ECO:0000269|PubMed:16785532"
FT MUTAGEN 172
FT /note="P->S: Marked reduction in rituximab binding.
FT Abrogates recognition by antibodies, including rituximab;
FT when associated with S-170."
FT /evidence="ECO:0000269|PubMed:16785532"
FT CONFLICT 13
FT /note="P -> L (in Ref. 3; CAA30179/CAA30180)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="M -> I (in Ref. 4; AAA88911)"
FT /evidence="ECO:0000305"
FT HELIX 48..70
FT /evidence="ECO:0007829|PDB:6VJA"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:6VJA"
FT HELIX 86..96
FT /evidence="ECO:0007829|PDB:6VJA"
FT HELIX 97..101
FT /evidence="ECO:0007829|PDB:6VJA"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:6VJA"
FT HELIX 115..142
FT /evidence="ECO:0007829|PDB:6VJA"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:6VJA"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:3PP4"
FT HELIX 178..185
FT /evidence="ECO:0007829|PDB:3PP4"
FT TURN 206..209
FT /evidence="ECO:0007829|PDB:6VJA"
SQ SEQUENCE 297 AA; 33077 MW; AC5420F8B626BDD1 CRC64;
MTTPRNSVNG TFPAEPMKGP IAMQSGPKPL FRRMSSLVGP TQSFFMRESK TLGAVQIMNG
LFHIALGGLL MIPAGIYAPI CVTVWYPLWG GIMYIISGSL LAATEKNSRK CLVKGKMIMN
SLSLFAAISG MILSIMDILN IKISHFLKME SLNFIRAHTP YINIYNCEPA NPSEKNSPST
QYCYSIQSLF LGILSVMLIF AFFQELVIAG IVENEWKRTC SRPKSNIVLL SAEEKKEQTI
EIKEEVVGLT ETSSQPKNEE DIEIIPIQEE EEEETETNFP EPPQDQESSP IENDSSP
