位置:首页 > 蛋白库 > 3BP2_HUMAN
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}.
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; 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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024