SH3B4_MOUSE
ID SH3B4_MOUSE Reviewed; 962 AA.
AC Q921I6; Q8BXV5; Q8BY95; Q8C007;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=SH3 domain-binding protein 4;
GN Name=Sh3bp4;
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].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Skin, and Thymus;
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].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245; SER-250 AND SER-295, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC 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).
CC -!- FUNCTION: May function in transferrin receptor internalization at the
CC plasma membrane through a cargo-specific control of clathrin-mediated
CC endocytosis. Alternatively, may act as a negative regulator of the
CC amino acid-induced TOR signaling by inhibiting the formation of active
CC Rag GTPase complexes. Preferentially binds inactive Rag GTPase
CC complexes and prevents their interaction with the mTORC1 complex
CC inhibiting its relocalization to lysosomes and its activation. Thereby,
CC may indirectly regulate cell growth, proliferation and autophagy (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer or homooligomer. Interacts with DNM2, EPS15,
CC clathrin, the adapter protein complex 2/AP-2 and TFRC. Interacts with
CC the Rag GTPases RRAGA, RRAGB, RRAGC and RRAGD; the interaction is most
CC probably direct, preferentially occurs with their inactive GDP-bound
CC form and is negatively regulated by amino acids (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit {ECO:0000250}.
CC Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250}. Nucleus
CC {ECO:0000250}. Note=Specifically associated with transferrin receptor-
CC containing clathrin-coated pits and clathrin-coated vesicles. May also
CC localize to the nucleus (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The SH3 domain mediates localization to the clathrin-coated
CC pits and vesicles. The SH3 domain mediates interaction with DNM2 and
CC the cytoplasmic part of TFRC with a lower affinity. The SH3 domain also
CC mediates interaction with RRAGB, RRAGC and is required for the negative
CC regulation of mTORC1 (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated upon EGF stimulation. Phosphorylation prevents
CC interaction with DNM2 (By similarity). {ECO:0000250}.
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DR EMBL; AK028826; BAC26140.1; -; mRNA.
DR EMBL; AK032634; BAC27961.1; -; mRNA.
DR EMBL; AK041504; BAC30966.1; -; mRNA.
DR EMBL; AK043259; BAC31506.1; -; mRNA.
DR EMBL; BC012284; AAH12284.1; -; mRNA.
DR EMBL; BC034733; AAH34733.1; -; mRNA.
DR CCDS; CCDS15147.1; -.
DR RefSeq; NP_598577.1; NM_133816.2.
DR RefSeq; XP_006530038.1; XM_006529975.3.
DR AlphaFoldDB; Q921I6; -.
DR SMR; Q921I6; -.
DR BioGRID; 221051; 6.
DR STRING; 10090.ENSMUSP00000067581; -.
DR iPTMnet; Q921I6; -.
DR PhosphoSitePlus; Q921I6; -.
DR jPOST; Q921I6; -.
DR MaxQB; Q921I6; -.
DR PaxDb; Q921I6; -.
DR PeptideAtlas; Q921I6; -.
DR PRIDE; Q921I6; -.
DR ProteomicsDB; 261344; -.
DR Antibodypedia; 34462; 185 antibodies from 31 providers.
DR DNASU; 98402; -.
DR Ensembl; ENSMUST00000066279; ENSMUSP00000067581; ENSMUSG00000036206.
DR GeneID; 98402; -.
DR KEGG; mmu:98402; -.
DR UCSC; uc007byv.1; mouse.
DR CTD; 23677; -.
DR MGI; MGI:2138297; Sh3bp4.
DR VEuPathDB; HostDB:ENSMUSG00000036206; -.
DR eggNOG; ENOG502QTUW; Eukaryota.
DR GeneTree; ENSGT00390000013151; -.
DR HOGENOM; CLU_013080_2_0_1; -.
DR InParanoid; Q921I6; -.
DR OMA; PQDLHVC; -.
DR OrthoDB; 140316at2759; -.
DR PhylomeDB; Q921I6; -.
DR TreeFam; TF105572; -.
DR Reactome; R-MMU-9639288; Amino acids regulate mTORC1.
DR BioGRID-ORCS; 98402; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Sh3bp4; mouse.
DR PRO; PR:Q921I6; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q921I6; protein.
DR Bgee; ENSMUSG00000036206; Expressed in lacrimal gland and 210 other tissues.
DR Genevisible; Q921I6; MM.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0034260; P:negative regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0032007; P:negative regulation of TOR signaling; ISS:UniProtKB.
DR GO; GO:0010508; P:positive regulation of autophagy; ISS:UniProtKB.
DR GO; GO:0061462; P:protein localization to lysosome; ISS:UniProtKB.
DR GO; GO:0050790; P:regulation of catalytic activity; ISS:UniProtKB.
DR CDD; cd11757; SH3_SH3BP4; 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR035455; SH3BP4.
DR InterPro; IPR035456; SH3BP4_SH3.
DR InterPro; IPR000906; ZU5_dom.
DR PANTHER; PTHR15603:SF3; PTHR15603:SF3; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF07653; SH3_2; 1.
DR Pfam; PF00791; ZU5; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 2.
DR PROSITE; PS51145; ZU5; 1.
PE 1: Evidence at protein level;
KW Coated pit; Cytoplasmic vesicle; Endocytosis; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..962
FT /note="SH3 domain-binding protein 4"
FT /id="PRO_0000274575"
FT DOMAIN 55..114
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 316..453
FT /note="ZU5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00485"
FT DOMAIN 653..723
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0V3"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0V3"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0V3"
FT CONFLICT 312
FT /note="Q -> K (in Ref. 1; BAC30966)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="V -> E (in Ref. 1; BAC27961)"
FT /evidence="ECO:0000305"
FT CONFLICT 534
FT /note="Q -> K (in Ref. 1; BAC27961)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 962 AA; 107584 MW; 11154849455F4063 CRC64;
MAAQRIRAAN ASGLPRCKSE GTLIDLSEGF SETSFNDVKV PSPSALLVDN PTPFGNAKEV
IAIKDYCPNN FTTLKFSKGD HLYVLDTSGG EWWYAHNTTE MGYIPSSYVQ PLNYRNSTLS
DSGMIDNLPD SPEEVAKELD LLGGGWTDDQ KESGRPYSNN PFWNGVRTNP FLNGNAQPST
DELNPKSTVD LLLFDTGTSS FTESSSATTN STGNIFDELP ATNGLQVEQP VKRDNPFFRS
KRSYSLSELS VLQAKSDAPP TSSFFTGLKS PVPEQFQSRE DFRTAWLNHR KLARSCHDLD
LLGQSPGWGQ TQAVETNIVC KLDSSGGSVQ LPDTNISIHV PEGHVAPGET QQISMKALLD
PPLDLNSDRS TSVSPVVEVK LSNLEVSTFI ILEMKVSAEV KGDIFSKSTV VLQCLRSDSK
EGPYVPIPLA YSYGDTIQVQ LDNLEPCMYL AIVAQGPNIL YPSTVWDFIN KRVTVGLYGP
KHIHPSFKTV VTIFGHDCAP KTLLVSEVTR QAPSPAPVAL QLWGKHQFIL SRPQDLRVCM
FSNMTNYEVK ANEQARVVRG FQMKLGKVSR LIFSVISQNP NELSDFTLRV QVKDDQDTIL
TQFCVQTPQP PPKSAIKPSG QRRFLKKNEV GKIILSPFVV TTKYPTFQDR PVSSLKFGKL
LKTVVRQNKS HYLLEYKKGD VVALLSEERI RLKGQLWTKE WYIGYYQGKV GLVHTKNVLV
VGKARPSLFS GPELSTSVLL EQILRPCKFL TYIYASVRTL LMENISSWRA FADALGYGNL
PLTFFCRAEL DSEPERVASV LEKLKEDCNN PDNKDRKSFQ KELVMALLKM DCQGLVVRLI
QDFVLLTTAV EVAQRWRELA EKLAKVSKQQ MDAYESPHRD RNGVVDSEAM WKPAYDFLLT
WSHQIGDSYR DVIQELHIGL DKMKNPITRR WKHLTGTLIL VNSLDILRAA AFSPADHDDF
VI
