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BIN2_MOUSE
ID   BIN2_MOUSE              Reviewed;         489 AA.
AC   D3Z6Q9;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Bridging integrator 2;
GN   Name=Bin2;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND IDENTIFICATION BY
RP   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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380; SER-420; SER-422;
RP   SER-424; SER-430; SER-435; SER-439 AND SER-443, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Liver, Lung, Spleen, and Testis;
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).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=23285027; DOI=10.1371/journal.pone.0052401;
RA   Sanchez-Barrena M.J., Vallis Y., Clatworthy M.R., Doherty G.J.,
RA   Veprintsev D.B., Evans P.R., McMahon H.T.;
RT   "Bin2 is a membrane sculpting N-BAR protein that influences leucocyte
RT   podosomes, motility and phagocytosis.";
RL   PLoS ONE 7:E52401-E52401(2012).
CC   -!- FUNCTION: Promotes cell motility and migration, probably via its
CC       interaction with the cell membrane and with podosome proteins that
CC       mediate interaction with the cytoskeleton. Modulates membrane curvature
CC       and mediates membrane tubulation. Inhibits phagocytosis (By
CC       similarity). Plays a role in podosome formation. {ECO:0000250,
CC       ECO:0000269|PubMed:23285027}.
CC   -!- SUBUNIT: Homodimer. Interacts with BIN1. Interacts with ARHGEF6 (via
CC       SH3 domain), ARHGEF7 (via SH3 domain), SH3GL1, SH3GL2 and SH3GL3.
CC       Identified in a complex with ARHGEF6 and GIT2 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UBW5}. Cell
CC       projection, podosome membrane {ECO:0000269|PubMed:23285027}; Peripheral
CC       membrane protein {ECO:0000269|PubMed:23285027}; Cytoplasmic side
CC       {ECO:0000269|PubMed:23285027}. Cytoplasm, cell cortex
CC       {ECO:0000250|UniProtKB:Q9UBW5}. Cell projection, phagocytic cup
CC       {ECO:0000250|UniProtKB:Q9UBW5}. Note=Associates with membranes enriched
CC       in phosphoinositides. Detected in the actin-rich cell cortex at the
CC       leading edge of migrating cells. Detected at podosomes, at an actin-
CC       rich ring-like structure. {ECO:0000250|UniProtKB:Q9UBW5}.
CC   -!- DOMAIN: The BAR domain mediates dimerization and interaction with
CC       membranes enriched in phosphatidylinositides. {ECO:0000250}.
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DR   EMBL; AC123724; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; D3Z6Q9; -.
DR   SMR; D3Z6Q9; -.
DR   IntAct; D3Z6Q9; 1.
DR   STRING; 10090.ENSMUSP00000138523; -.
DR   iPTMnet; D3Z6Q9; -.
DR   PhosphoSitePlus; D3Z6Q9; -.
DR   SwissPalm; D3Z6Q9; -.
DR   EPD; D3Z6Q9; -.
DR   jPOST; D3Z6Q9; -.
DR   MaxQB; D3Z6Q9; -.
DR   PeptideAtlas; D3Z6Q9; -.
DR   PRIDE; D3Z6Q9; -.
DR   ProteomicsDB; 273674; -.
DR   MGI; MGI:3611448; Bin2.
DR   eggNOG; KOG3771; Eukaryota.
DR   InParanoid; D3Z6Q9; -.
DR   PhylomeDB; D3Z6Q9; -.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   PRO; PR:D3Z6Q9; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; D3Z6Q9; protein.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR   GO; GO:0001891; C:phagocytic cup; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0002102; C:podosome; ISS:UniProtKB.
DR   GO; GO:0005543; F:phospholipid binding; ISS:UniProtKB.
DR   GO; GO:0060326; P:cell chemotaxis; ISS:UniProtKB.
DR   GO; GO:0006911; P:phagocytosis, engulfment; ISO:MGI.
DR   GO; GO:0097320; P:plasma membrane tubulation; ISS:UniProtKB.
DR   GO; GO:0071800; P:podosome assembly; ISS:UniProtKB.
DR   Gene3D; 1.20.1270.60; -; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR003005; Amphiphysin.
DR   InterPro; IPR004148; BAR_dom.
DR   InterPro; IPR028827; BIN2.
DR   PANTHER; PTHR46514:SF1; PTHR46514:SF1; 1.
DR   Pfam; PF03114; BAR; 1.
DR   PRINTS; PR01251; AMPHIPHYSIN.
DR   SMART; SM00721; BAR; 1.
DR   SUPFAM; SSF103657; SSF103657; 1.
DR   PROSITE; PS51021; BAR; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Cell projection; Cytoplasm; Membrane;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..489
FT                   /note="Bridging integrator 2"
FT                   /id="PRO_0000416099"
FT   DOMAIN          28..244
FT                   /note="BAR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT   REGION          267..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..305
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..375
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        423..450
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         273
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBW5"
FT   MOD_RES         357
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBW5"
FT   MOD_RES         380
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         392
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBW5"
FT   MOD_RES         420
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         422
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         424
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         430
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         435
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         439
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         443
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   489 AA;  52554 MW;  8E207C53B1D31A99 CRC64;
     MAEGKAGGAA GLFAKQMQKK FSRAQEKVLQ KLGKTVETKD ERFEQSASNF YQQQAEGHKL
     YKDLKNFLSA VKVMHESSKR VSETLQEVYS SDWDGHEDLK AIVGNNDLLW EDYEEKLADQ
     ALRTMENYVS QFSEIKERIA KRGRKLVDYD SARHHLEAVQ NAKKKDDAKM AKAEEDFSKA
     QIVFEDLNQE LLEELPILYN SRIGCYVTVF QNISNLRDVF YREMSKLNHN LYEVMSKLEK
     QHSNKVFVVK GLSSSSRRSL VISPPVQSCA ASSPVSPVSP VSPVTSPTSP SATSEPESVS
     ATGEELTSEA GGEDSCESQE SLKDEEADEA QSETSSSLPA CNGPTPAPAS PAAEVGSQEE
     ALSSSAQSPG RGQTGKDTPS PGDVVLRARA SSEGAEQSKR AASIQRTSAP PSRPPPPRAS
     GSGSCNAPGS PEGSSQLCSP RASPDASSNP EPAETREKEG AGSSGPEEPR AVSTKSATQA
     SGGLVGLFL
 
 
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