3BP2_HUMAN
ID 3BP2_HUMAN Reviewed; 561 AA.
AC P78314; A6NNC2; B2R5R6; B4DT04; D3DVR0; D6R919; O00500; O15373; P78315;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=SH3 domain-binding protein 2;
DE Short=3BP-2;
GN Name=SH3BP2; Synonyms=3BP2; ORFNames=RES4-23;
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).
RC TISSUE=Tonsil;
RA Gokemeijer J., Deligiannidis K.E., Ligris K., Ernst T.J.;
RT "3BP2 binds to phosphatidylinositols; linking the hemopoietic tyrosine
RT kinase c-FES to the cytoplasmic membrane in a phosphorylation dependent
RT mechanism.";
RL Blood 88:473A-473A(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9299232; DOI=10.1006/geno.1997.4849;
RA Bell S.M., Shaw M., Jou Y.-S., Myers R.M., Knowles M.A.;
RT "Identification and characterization of the human homologue of SH3BP2, an
RT SH3 binding domain protein within a common region of deletion at 4p16.3
RT involved in bladder cancer.";
RL Genomics 44:163-170(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9734812; DOI=10.1093/dnares/5.3.177;
RA Hadano S., Ishida Y., Ikeda J.-E.;
RT "The primary structure and genomic organization of five novel transcripts
RT located close to the Huntington's disease gene on human chromosome
RT 4p16.3.";
RL DNA Res. 5:177-186(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Cerebellum;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix;
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 [8]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278 AND SER-427, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278 AND SER-416, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP STRUCTURE BY NMR OF 444-558.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the SH2 domain of human SH3BP2 protein.";
RL Submitted (NOV-2005) to the PDB data bank.
RN [13]
RP VARIANTS CRBM GLN-415; PRO-415; ARG-418; HIS-418; LEU-418; ARG-420 AND
RP GLU-420.
RX PubMed=11381256; DOI=10.1038/88832;
RA Ueki Y., Tiziani V., Santanna C., Fukai N., Maulik C., Garfinkle J.,
RA Ninomiya C., doAmaral C., Peters H., Habal M., Rhee-Morris L., Doss J.B.,
RA Kreiborg S., Olsen B.R., Reichenberger E.;
RT "Mutations in the gene encoding c-Abl-binding protein SH3BP2 cause
RT cherubism.";
RL Nat. Genet. 28:125-126(2001).
RN [14]
RP VARIANT CRBM ARG-420.
RX PubMed=12900899; DOI=10.1002/ajmg.a.20226;
RA Lo B., Faiyaz-Ul-Haque M., Kennedy S., Aviv R., Tsui L.-C., Teebi A.S.;
RT "Novel mutation in the gene encoding c-Abl-binding protein SH3BP2 causes
RT cherubism.";
RL Am. J. Med. Genet. A 121:37-40(2003).
RN [15]
RP VARIANT CRBM ARG-418.
RX PubMed=14577811; DOI=10.1597/1545-1569_2003_040_0632_ammits_2.0.co_2;
RA Imai Y., Kanno K., Moriya T., Kayano S., Seino H., Matsubara Y., Yamada A.;
RT "A missense mutation in the SH3BP2 gene on chromosome 4p16.3 found in a
RT case of nonfamilial cherubism.";
RL Cleft Palate Craniofac. J. 40:632-638(2003).
CC -!- FUNCTION: Binds differentially to the SH3 domains of certain proteins
CC of signal transduction pathways. Binds to phosphatidylinositols;
CC linking the hemopoietic tyrosine kinase fes to the cytoplasmic membrane
CC in a phosphorylation dependent mechanism.
CC -!- INTERACTION:
CC P78314; Q9UJU6: DBNL; NbExp=7; IntAct=EBI-727062, EBI-751783;
CC P78314; P10721: KIT; NbExp=3; IntAct=EBI-727062, EBI-1379503;
CC P78314; Q96B97: SH3KBP1; NbExp=8; IntAct=EBI-727062, EBI-346595;
CC P78314; Q9H2K2: TNKS2; NbExp=5; IntAct=EBI-727062, EBI-4398527;
CC P78314; P15498: VAV1; NbExp=8; IntAct=EBI-727062, EBI-625518;
CC P78314; P52735: VAV2; NbExp=4; IntAct=EBI-727062, EBI-297549;
CC P78314-3; Q14247-3: CTTN; NbExp=3; IntAct=EBI-12304031, EBI-12748199;
CC P78314-3; Q9UJU6-2: DBNL; NbExp=3; IntAct=EBI-12304031, EBI-12192777;
CC P78314-3; P14317: HCLS1; NbExp=3; IntAct=EBI-12304031, EBI-750369;
CC P78314-3; O00160: MYO1F; NbExp=3; IntAct=EBI-12304031, EBI-741792;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Long;
CC IsoId=P78314-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=P78314-2; Sequence=VSP_004085, VSP_004086;
CC Name=3;
CC IsoId=P78314-3; Sequence=VSP_043636;
CC Name=4;
CC IsoId=P78314-4; Sequence=VSP_055046;
CC -!- TISSUE SPECIFICITY: Expressed in a variety of tissues including lung,
CC liver, skeletal muscle, kidney and pancreas.
CC {ECO:0000269|PubMed:9734812}.
CC -!- PTM: Phosphorylated. Phosphorylation at Tyr-448 may stimulate the
CC activity of the LYN kinase (By similarity). {ECO:0000250}.
CC -!- DISEASE: Cherubism (CRBM) [MIM:118400]: An autosomal dominant syndrome
CC characterized by excessive bone degradation of the upper and lower
CC jaws, which often begins around three years of age. It is followed by
CC development of fibrous tissue masses, which causes a characteristic
CC facial swelling. {ECO:0000269|PubMed:11381256,
CC ECO:0000269|PubMed:12900899, ECO:0000269|PubMed:14577811}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
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DR EMBL; AF000936; AAB59973.1; -; mRNA.
DR EMBL; U56386; AAB72034.1; -; mRNA.
DR EMBL; AB000462; BAA19119.1; -; mRNA.
DR EMBL; AB000463; BAA19120.1; -; mRNA.
DR EMBL; AK299996; BAG61816.1; -; mRNA.
DR EMBL; AK312286; BAG35213.1; -; mRNA.
DR EMBL; AL121750; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471131; EAW82509.1; -; Genomic_DNA.
DR EMBL; CH471131; EAW82510.1; -; Genomic_DNA.
DR EMBL; CH471131; EAW82511.1; -; Genomic_DNA.
DR EMBL; CH471131; EAW82512.1; -; Genomic_DNA.
DR EMBL; BC022996; AAH22996.1; -; mRNA.
DR CCDS; CCDS33944.1; -. [P78314-1]
DR CCDS; CCDS54715.1; -. [P78314-3]
DR CCDS; CCDS54716.1; -. [P78314-4]
DR RefSeq; NP_001116153.1; NM_001122681.1. [P78314-1]
DR RefSeq; NP_001139327.1; NM_001145855.1. [P78314-3]
DR RefSeq; NP_001139328.1; NM_001145856.1. [P78314-4]
DR RefSeq; NP_003014.3; NM_003023.4. [P78314-1]
DR PDB; 2CR4; NMR; -; A=446-558.
DR PDB; 3TWR; X-ray; 1.55 A; E/F/G/H=410-425.
DR PDBsum; 2CR4; -.
DR PDBsum; 3TWR; -.
DR AlphaFoldDB; P78314; -.
DR SMR; P78314; -.
DR BioGRID; 112350; 37.
DR IntAct; P78314; 27.
DR MINT; P78314; -.
DR STRING; 9606.ENSP00000422168; -.
DR GlyGen; P78314; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P78314; -.
DR PhosphoSitePlus; P78314; -.
DR BioMuta; SH3BP2; -.
DR DMDM; 3023207; -.
DR EPD; P78314; -.
DR jPOST; P78314; -.
DR MassIVE; P78314; -.
DR MaxQB; P78314; -.
DR PaxDb; P78314; -.
DR PeptideAtlas; P78314; -.
DR PRIDE; P78314; -.
DR ProteomicsDB; 12870; -.
DR ProteomicsDB; 57557; -. [P78314-1]
DR ProteomicsDB; 57558; -. [P78314-2]
DR ProteomicsDB; 57559; -. [P78314-3]
DR Antibodypedia; 8898; 207 antibodies from 29 providers.
DR DNASU; 6452; -.
DR Ensembl; ENST00000356331.9; ENSP00000348685.5; ENSG00000087266.17. [P78314-1]
DR Ensembl; ENST00000435136.8; ENSP00000403231.3; ENSG00000087266.17. [P78314-3]
DR Ensembl; ENST00000503393.8; ENSP00000422168.3; ENSG00000087266.17. [P78314-1]
DR Ensembl; ENST00000511747.6; ENSP00000424846.2; ENSG00000087266.17. [P78314-4]
DR Ensembl; ENST00000513020.5; ENSP00000424072.1; ENSG00000087266.17. [P78314-2]
DR Ensembl; ENST00000515737.5; ENSP00000422605.1; ENSG00000087266.17. [P78314-2]
DR GeneID; 6452; -.
DR KEGG; hsa:6452; -.
DR MANE-Select; ENST00000503393.8; ENSP00000422168.3; NM_001122681.2; NP_001116153.1.
DR UCSC; uc003gfi.5; human. [P78314-1]
DR CTD; 6452; -.
DR DisGeNET; 6452; -.
DR GeneCards; SH3BP2; -.
DR GeneReviews; SH3BP2; -.
DR HGNC; HGNC:10825; SH3BP2.
DR HPA; ENSG00000087266; Low tissue specificity.
DR MalaCards; SH3BP2; -.
DR MIM; 118400; phenotype.
DR MIM; 602104; gene.
DR neXtProt; NX_P78314; -.
DR OpenTargets; ENSG00000087266; -.
DR Orphanet; 184; Cherubism.
DR PharmGKB; PA35733; -.
DR VEuPathDB; HostDB:ENSG00000087266; -.
DR eggNOG; ENOG502RF2Z; Eukaryota.
DR GeneTree; ENSGT00390000002216; -.
DR HOGENOM; CLU_040124_0_0_1; -.
DR InParanoid; P78314; -.
DR OrthoDB; 1189650at2759; -.
DR PhylomeDB; P78314; -.
DR TreeFam; TF333342; -.
DR PathwayCommons; P78314; -.
DR SignaLink; P78314; -.
DR SIGNOR; P78314; -.
DR BioGRID-ORCS; 6452; 19 hits in 1075 CRISPR screens.
DR ChiTaRS; SH3BP2; human.
DR EvolutionaryTrace; P78314; -.
DR GenomeRNAi; 6452; -.
DR Pharos; P78314; Tbio.
DR PRO; PR:P78314; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P78314; protein.
DR Bgee; ENSG00000087266; Expressed in granulocyte and 135 other tissues.
DR ExpressionAtlas; P78314; baseline and differential.
DR Genevisible; P78314; HS.
DR GO; GO:0001784; F:phosphotyrosine residue binding; IPI:CAFA.
DR GO; GO:0017124; F:SH3 domain binding; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR CDD; cd10359; SH2_SH3BP2; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR035848; SH3BP2.
DR InterPro; IPR035847; SH3BP2_SH2.
DR PANTHER; PTHR15126; PTHR15126; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00017; SH2; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50001; SH2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disease variant; Phosphoprotein;
KW Reference proteome; SH2 domain; SH3-binding.
FT CHAIN 1..561
FT /note="SH3 domain-binding protein 2"
FT /id="PRO_0000064365"
FT DOMAIN 26..130
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 457..555
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 160..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 201..210
FT /note="SH3-binding"
FT COMPBIAS 200..215
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..392
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 174
FT /note="Phosphotyrosine; by SYK"
FT /evidence="ECO:0000250|UniProtKB:Q06649"
FT MOD_RES 183
FT /note="Phosphotyrosine; by SYK"
FT /evidence="ECO:0000250|UniProtKB:Q06649"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 448
FT /note="Phosphotyrosine; by SYK"
FT /evidence="ECO:0000250|UniProtKB:Q06649"
FT VAR_SEQ 1
FT /note="M -> MASLGPRTPAPSRSRGRRAMCWVSTISFM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043636"
FT VAR_SEQ 1
FT /note="M -> MAGSGPRPRSWGRREAGARDEAAAAGGRGPGPCRCSQGRRAWIAPGK
FT PAMPAAWTPFM (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_055046"
FT VAR_SEQ 81..97
FT /note="VMRAAEETTSNNVFPFK -> QPRPQPAQALSQTEAGP (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:9734812"
FT /id="VSP_004085"
FT VAR_SEQ 98..561
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:9734812"
FT /id="VSP_004086"
FT VARIANT 415
FT /note="R -> P (in CRBM; dbSNP:rs121909149)"
FT /evidence="ECO:0000269|PubMed:11381256"
FT /id="VAR_013257"
FT VARIANT 415
FT /note="R -> Q (in CRBM; dbSNP:rs121909149)"
FT /evidence="ECO:0000269|PubMed:11381256"
FT /id="VAR_013258"
FT VARIANT 418
FT /note="P -> H (in CRBM; dbSNP:rs121909146)"
FT /evidence="ECO:0000269|PubMed:11381256"
FT /id="VAR_013259"
FT VARIANT 418
FT /note="P -> L (in CRBM; dbSNP:rs121909146)"
FT /evidence="ECO:0000269|PubMed:11381256"
FT /id="VAR_013260"
FT VARIANT 418
FT /note="P -> R (in CRBM; dbSNP:rs121909146)"
FT /evidence="ECO:0000269|PubMed:11381256,
FT ECO:0000269|PubMed:14577811"
FT /id="VAR_013261"
FT VARIANT 420
FT /note="G -> E (in CRBM; dbSNP:rs28938171)"
FT /evidence="ECO:0000269|PubMed:11381256"
FT /id="VAR_013262"
FT VARIANT 420
FT /note="G -> R (in CRBM; dbSNP:rs28938170)"
FT /evidence="ECO:0000269|PubMed:11381256,
FT ECO:0000269|PubMed:12900899"
FT /id="VAR_013263"
FT CONFLICT 27
FT /note="V -> L (in Ref. 3; AAB59973)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="H -> N (in Ref. 3; AAB59973)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="L -> R (in Ref. 3; AAB59973)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="A -> P (in Ref. 3; AAB59973)"
FT /evidence="ECO:0000305"
FT TURN 455..457
FT /evidence="ECO:0007829|PDB:2CR4"
FT HELIX 464..474
FT /evidence="ECO:0007829|PDB:2CR4"
FT STRAND 485..489
FT /evidence="ECO:0007829|PDB:2CR4"
FT STRAND 496..501
FT /evidence="ECO:0007829|PDB:2CR4"
FT TURN 503..505
FT /evidence="ECO:0007829|PDB:2CR4"
FT STRAND 506..508
FT /evidence="ECO:0007829|PDB:2CR4"
FT STRAND 514..516
FT /evidence="ECO:0007829|PDB:2CR4"
FT STRAND 519..525
FT /evidence="ECO:0007829|PDB:2CR4"
FT STRAND 527..530
FT /evidence="ECO:0007829|PDB:2CR4"
FT HELIX 531..538
FT /evidence="ECO:0007829|PDB:2CR4"
FT STRAND 544..548
FT /evidence="ECO:0007829|PDB:2CR4"
FT STRAND 553..556
FT /evidence="ECO:0007829|PDB:2CR4"
SQ SEQUENCE 561 AA; 62244 MW; 69E6846A4F6D8F15 CRC64;
MAAEEMHWPV PMKAIGAQNL LTMPGGVAKA GYLHKKGGTQ LQLLKWPLRF VIIHKRCVYY
FKSSTSASPQ GAFSLSGYNR VMRAAEETTS NNVFPFKIIH ISKKHRTWFF SASSEEERKS
WMALLRREIG HFHEKKDLPL DTSDSSSDTD SFYGAVERPV DISLSPYPTD NEDYEHDDED
DSYLEPDSPE PGRLEDALMH PPAYPPPPVP TPRKPAFSDM PRAHSFTSKG PGPLLPPPPP
KHGLPDVGLA AEDSKRDPLC PRRAEPCPRV PATPRRMSDP PLSTMPTAPG LRKPPCFRES
ASPSPEPWTP GHGACSTSSA AIMATATSRN CDKLKSFHLS PRGPPTSEPP PVPANKPKFL
KIAEEDPPRE AAMPGLFVPP VAPRPPALKL PVPEAMARPA VLPRPEKPQL PHLQRSPPDG
QSFRSFSFEK PRQPSQADTG GDDSDEDYEK VPLPNSVFVN TTESCEVERL FKATSPRGEP
QDGLYCIRNS STKSGKVLVV WDETSNKVRN YRIFEKDSKF YLEGEVLFVS VGSMVEHYHT
HVLPSHQSLL LRHPYGYTGP R
