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 24-JAN-2024, entry version 201. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 26. DR MINT; P78314; -. DR STRING; 9606.ENSP00000424846; -. 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; 9606-ENSP00000422168; -. DR PeptideAtlas; P78314; -. DR ProteomicsDB; 12870; -. DR ProteomicsDB; 57557; -. [P78314-1] DR ProteomicsDB; 57558; -. [P78314-2] DR ProteomicsDB; 57559; -. [P78314-3] DR Pumba; P78314; -. DR Antibodypedia; 8898; 238 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 AGR; HGNC:10825; -. 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; 5473346at2759; -. DR PhylomeDB; P78314; -. DR TreeFam; TF333342; -. DR PathwayCommons; P78314; -. DR SignaLink; P78314; -. DR SIGNOR; P78314; -. DR BioGRID-ORCS; 6452; 19 hits in 1153 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 137 other cell types or tissues. DR ExpressionAtlas; P78314; baseline and differential. 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; cd13308; PH_3BP2; 1. DR CDD; cd10359; SH2_SH3BP2; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR Gene3D; 3.30.505.10; SH2 domain; 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:SF4; SH3 DOMAIN-BINDING PROTEIN 2; 1. DR PANTHER; PTHR15126; SH3-BINDING; 1. DR Pfam; PF00169; PH; 1. DR Pfam; PF00017; SH2; 1. DR SMART; SM00233; PH; 1. DR SMART; SM00252; SH2; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR SUPFAM; SSF55550; SH2 domain; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. DR PROSITE; PS50001; SH2; 1. DR Genevisible; P78314; HS. 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 //