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3BP5_MOUSE
ID   3BP5_MOUSE              Reviewed;         463 AA.
AC   Q9Z131; Q3TTD6; Q8C903; Q8VCZ0;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=SH3 domain-binding protein 5;
DE            Short=SH3BP-5;
DE   AltName: Full=SH3 domain-binding protein that preferentially associates with BTK;
GN   Name=Sh3bp5; Synonyms=Sab {ECO:0000303|PubMed:10339589};
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 MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Embryo, and Mammary gland;
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   [3]
RP   PROTEIN SEQUENCE OF 16-22, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 33-458 (ISOFORM 2), AND FUNCTION.
RC   STRAIN=C57BL/6J; TISSUE=Spleen;
RX   PubMed=10339589; DOI=10.1073/pnas.96.11.6341;
RA   Yamadori T., Baba Y., Mastushita M., Hashimoto S., Kurosaki M.,
RA   Kurosaki T., Kishimoto T., Tsukada S.;
RT   "Bruton's tyrosine kinase activity is negatively regulated by Sab, the Btk-
RT   SH3 domain-binding protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:6341-6346(1999).
RN   [5]
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378; SER-379 AND SER-424, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Liver, Lung, 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).
RN   [7]
RP   INTERACTION WITH RAB11A.
RX   PubMed=26506309; DOI=10.1016/j.devcel.2015.09.013;
RA   Sakaguchi A., Sato M., Sato K., Gengyo-Ando K., Yorimitsu T., Nakai J.,
RA   Hara T., Sato K., Sato K.;
RT   "REI-1 is a guanine nucleotide exchange factor regulating RAB-11
RT   localization and function in C. elegans embryos.";
RL   Dev. Cell 35:211-221(2015).
CC   -!- FUNCTION: Functions as guanine nucleotide exchange factor (GEF) with
CC       specificity for RAB11A and RAB25 (By similarity). Inhibits the
CC       auto- and transphosphorylation activity of BTK. Plays a negative
CC       regulatory role in BTK-related cytoplasmic signaling in B-cells. May be
CC       involved in BCR-induced apoptotic cell death.
CC       {ECO:0000250|UniProtKB:O60239, ECO:0000269|PubMed:10339589}.
CC   -!- SUBUNIT: Interacts with BTK (By similarity). Interacts with all
CC       isoforms of MAPK8, MAPK9, MAPK10 and MAPK12 (By similarity). Interacts
CC       with GDP-bound and nucleotide-free forms of RAB11A (PubMed:26506309).
CC       {ECO:0000250|UniProtKB:O60239, ECO:0000269|PubMed:26506309}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC       {ECO:0000250|UniProtKB:O60239}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:O60239}. Mitochondrion
CC       {ECO:0000250|UniProtKB:O60239}. Note=Colocalizes with RAB11A on
CC       cytoplasmic vesicle membranes. {ECO:0000250|UniProtKB:O60239}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9Z131-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Z131-2; Sequence=VSP_010882;
CC       Name=3;
CC         IsoId=Q9Z131-3; Sequence=VSP_022572, VSP_010882;
CC   -!- DOMAIN: The N-terminal half of the protein mediates interaction with
CC       RAB11A and functions as guanine nucleotide exchange factor. Four long
CC       alpha-helices (interrupted by a central kink) assemble into coiled
CC       coils, giving rise to a 'V' shape. {ECO:0000250|UniProtKB:O60239}.
CC   -!- SIMILARITY: Belongs to the SH3BP5 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC31530.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK043375; BAC31530.1; ALT_INIT; mRNA.
DR   EMBL; AK161427; BAE36389.1; -; mRNA.
DR   EMBL; BC018237; AAH18237.2; -; mRNA.
DR   EMBL; BC053741; AAH53741.2; -; mRNA.
DR   EMBL; AB016835; BAA75641.1; -; mRNA.
DR   CCDS; CCDS36855.1; -. [Q9Z131-2]
DR   CCDS; CCDS84108.1; -. [Q9Z131-3]
DR   RefSeq; NP_001334514.1; NM_001347585.1. [Q9Z131-3]
DR   RefSeq; NP_036024.2; NM_011894.3. [Q9Z131-2]
DR   AlphaFoldDB; Q9Z131; -.
DR   SMR; Q9Z131; -.
DR   BioGRID; 204869; 1.
DR   IntAct; Q9Z131; 1.
DR   STRING; 10090.ENSMUSP00000089517; -.
DR   iPTMnet; Q9Z131; -.
DR   PhosphoSitePlus; Q9Z131; -.
DR   EPD; Q9Z131; -.
DR   MaxQB; Q9Z131; -.
DR   PaxDb; Q9Z131; -.
DR   PeptideAtlas; Q9Z131; -.
DR   PRIDE; Q9Z131; -.
DR   ProteomicsDB; 285813; -. [Q9Z131-1]
DR   ProteomicsDB; 285814; -. [Q9Z131-2]
DR   ProteomicsDB; 285815; -. [Q9Z131-3]
DR   Antibodypedia; 26718; 168 antibodies from 27 providers.
DR   Ensembl; ENSMUST00000091903; ENSMUSP00000089517; ENSMUSG00000021892. [Q9Z131-2]
DR   Ensembl; ENSMUST00000100730; ENSMUSP00000098296; ENSMUSG00000021892. [Q9Z131-3]
DR   Ensembl; ENSMUST00000140002; ENSMUSP00000117152; ENSMUSG00000021892. [Q9Z131-1]
DR   GeneID; 24056; -.
DR   KEGG; mmu:24056; -.
DR   UCSC; uc007sxp.1; mouse. [Q9Z131-2]
DR   CTD; 9467; -.
DR   MGI; MGI:1344391; Sh3bp5.
DR   VEuPathDB; HostDB:ENSMUSG00000021892; -.
DR   eggNOG; KOG2008; Eukaryota.
DR   GeneTree; ENSGT00390000018500; -.
DR   HOGENOM; CLU_048895_1_0_1; -.
DR   InParanoid; Q9Z131; -.
DR   OMA; QFPPATR; -.
DR   OrthoDB; 566222at2759; -.
DR   PhylomeDB; Q9Z131; -.
DR   TreeFam; TF105573; -.
DR   BioGRID-ORCS; 24056; 2 hits in 74 CRISPR screens.
DR   ChiTaRS; Sh3bp5; mouse.
DR   PRO; PR:Q9Z131; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; Q9Z131; protein.
DR   Bgee; ENSMUSG00000021892; Expressed in stroma of bone marrow and 244 other tissues.
DR   Genevisible; Q9Z131; MM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR   GO; GO:0016604; C:nuclear body; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR   GO; GO:0004860; F:protein kinase inhibitor activity; ISO:MGI.
DR   GO; GO:0017124; F:SH3 domain binding; TAS:UniProtKB.
DR   GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
DR   GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:UniProtKB.
DR   GO; GO:0061099; P:negative regulation of protein tyrosine kinase activity; IBA:GO_Central.
DR   InterPro; IPR007940; SH3BP5.
DR   PANTHER; PTHR19423; PTHR19423; 2.
DR   Pfam; PF05276; SH3BP5; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasmic vesicle;
KW   Direct protein sequencing; Guanine-nucleotide releasing factor; Membrane;
KW   Mitochondrion; Phosphoprotein; Reference proteome; SH3-binding.
FT   CHAIN           1..463
FT                   /note="SH3 domain-binding protein 5"
FT                   /id="PRO_0000064369"
FT   REGION          1..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          33..268
FT                   /note="Sufficient for interaction with RAB11A and for
FT                   guanine nucleotide exchange activity"
FT                   /evidence="ECO:0000250|UniProtKB:O60239"
FT   REGION          309..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          372..429
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          47..93
FT                   /evidence="ECO:0000250|UniProtKB:O60239"
FT   COILED          100..148
FT                   /evidence="ECO:0000250|UniProtKB:O60239"
FT   COILED          157..203
FT                   /evidence="ECO:0000250|UniProtKB:O60239"
FT   COILED          214..258
FT                   /evidence="ECO:0000250|UniProtKB:O60239"
FT   COMPBIAS        1..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..46
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        309..336
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..398
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        399..429
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         354
FT                   /note="Phosphoserine; by MAPK12 and MAPK9"
FT                   /evidence="ECO:0000250|UniProtKB:Q91Y80"
FT   MOD_RES         378
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         379
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         421
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91Y80"
FT   MOD_RES         424
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         1..70
FT                   /note="MDTALKRSRSDEPAELPPPAREVEEKEEEEERMEQGLEEEEEEVDPRIQGEL
FT                   EKLNQSTDDINRRETELE -> MDWARTVMASTGLAPASAAPHTGSRAQPCLFLAPVPP
FT                   HFAWFIFLDPALPCSTLAQSVSFKPCCGVVK (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_022572"
FT   VAR_SEQ         455..463
FT                   /note="IFIFYTFLQ -> VQIG (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:10339589,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT                   /id="VSP_010882"
FT   CONFLICT        299
FT                   /note="S -> SS (in Ref. 1; BAC31530)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   463 AA;  51807 MW;  A4274A91DDD91670 CRC64;
     MDTALKRSRS DEPAELPPPA REVEEKEEEE ERMEQGLEEE EEEVDPRIQG ELEKLNQSTD
     DINRRETELE DARQKFRSVL VEATVKLDEL AKKIGKAVED SKPYWEARRV ARQAQLEAQK
     ATQDFQRATE VLRAAKETIS LAEQRLLEDD KRQFDSAWQE MLNHATQRVM EAEQTKTRSE
     LVHKETAARY NAAMGRMRQL EKKLKRAINK SKPYFELKAK YYVQLEQLKK TVDDLQAKLA
     LAKGEYKAAL KSLERISDEI HERRRSNAMG PRGCGVGAEG SIASVENLPV SKPEPDAISV
     ASEAFEDDNC SNLVSEDDSE TQSVSSFSSG PTSPSEMPDQ FPAVARPGSL DLPSPVSLSE
     FGMMFPILGP RSECSGASSP ECEVERGDRA EGAENKMSDK ANNNRVLGST NGGSGRSRSQ
     SSTSLESQAL ETRMKQLSLQ CSKGRDGIIA DIKMIFIFYT FLQ
 
 
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