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
