3BP2_MOUSE
ID 3BP2_MOUSE Reviewed; 559 AA.
AC Q06649;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=SH3 domain-binding protein 2;
DE Short=3BP-2;
GN Name=Sh3bp2; Synonyms=3bp2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8438166; DOI=10.1126/science.8438166;
RA Ren R., Mayer B.J., Cicchetti P., Baltimore D.;
RT "Identification of a ten-amino acid proline-rich SH3 binding site.";
RL Science 259:1157-1161(1993).
RN [2]
RP PHOSPHORYLATION AT TYR-174; TYR-183 AND TYR-446.
RX PubMed=12709437; DOI=10.1074/jbc.m301201200;
RA Maeno K., Sada K., Kyo S., Miah S.M., Kawauchi-Kamata K., Qu X., Shi Y.,
RA Yamamura H.;
RT "Adaptor protein 3BP2 is a potential ligand of Src homology 2 and 3 domains
RT of Lyn protein-tyrosine kinase.";
RL J. Biol. Chem. 278:24912-24920(2003).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q06649; Q9H2K2: TNKS2; Xeno; NbExp=6; IntAct=EBI-5323518, EBI-4398527;
CC -!- PTM: Phosphorylated. Phosphorylation at Tyr-446 may stimulate the
CC activity of the LYN kinase. {ECO:0000269|PubMed:12709437}.
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DR EMBL; L14543; AAA37121.1; -; mRNA.
DR CCDS; CCDS19215.1; -.
DR PIR; I49444; I49444.
DR AlphaFoldDB; Q06649; -.
DR SMR; Q06649; -.
DR IntAct; Q06649; 8.
DR MINT; Q06649; -.
DR STRING; 10090.ENSMUSP00000112554; -.
DR iPTMnet; Q06649; -.
DR PhosphoSitePlus; Q06649; -.
DR EPD; Q06649; -.
DR MaxQB; Q06649; -.
DR PaxDb; Q06649; -.
DR PRIDE; Q06649; -.
DR ProteomicsDB; 285892; -.
DR MGI; MGI:1346349; Sh3bp2.
DR eggNOG; ENOG502RF2Z; Eukaryota.
DR InParanoid; Q06649; -.
DR PhylomeDB; Q06649; -.
DR ChiTaRS; Sh3bp2; mouse.
DR PRO; PR:Q06649; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q06649; protein.
DR GO; GO:0001784; F:phosphotyrosine residue binding; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; IPI:MGI.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
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 Phosphoprotein; Reference proteome; SH2 domain; SH3-binding.
FT CHAIN 1..559
FT /note="SH3 domain-binding protein 2"
FT /id="PRO_0000064366"
FT DOMAIN 26..130
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 455..553
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 164..449
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 231..245
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..390
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 174
FT /note="Phosphotyrosine; by SYK"
FT /evidence="ECO:0000269|PubMed:12709437"
FT MOD_RES 183
FT /note="Phosphotyrosine; by SYK"
FT /evidence="ECO:0000269|PubMed:12709437"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78314"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78314"
FT MOD_RES 446
FT /note="Phosphotyrosine; by SYK"
FT /evidence="ECO:0000269|PubMed:12709437"
SQ SEQUENCE 559 AA; 62208 MW; EDFE1F11B259646E CRC64;
MAAEEMQWPV PMKAIGAQNL LTMPGGVAKA GYLHKKGGTQ LQLLKWPLRF VIIHKRCIYY
FKSSTSASPQ GAFSLSGYNR VMRAAEETTS NNVFPFKIIH ISKKHRTWFF SASSEDERKS
WMAFVRREIG HFHEKKELPL DTSDSSSDTD SFYGAVERPI DISLSSYPMD NEDYEHEDED
DSYLEPDSPG PMKLEDALTY PPAYPPPPVP VPRKPAFSDL PRAHSFTSKS PSPLLPPPPP
KRGLPDTGSA PEDAKDALGL RRVEPGLRVP ATPRRMSDPP MSNVPTVPNL RKHPCFRDSV
NPGLEPWTPG HGTSSVSSST TMAVATSRNC DKLKSFHLSS RGPPTSEPPP VPANKPKFLK
IAEEPSPREA AKFAPVPPVA PRPPVQKMPM PEATVRPAVL PRPENTPLPH LQRSPPDGQS
FRGFSFEKAR QPSQADTGEE DSDEDYEKVP LPNSVFVNTT ESCEVERLFK ATDPRGEPQD
GLYCIRNSST KSGKVLVVWD ESSNKVRNYR IFEKDSKFYL EGEVLFASVG SMVEHYHTHV
LPSHQSLLLR HPYGYAGPR
