SH3K1_MOUSE
ID SH3K1_MOUSE Reviewed; 709 AA.
AC Q8R550; B1AZ86; B1AZ87; Q8CAL8; Q8CEF6; Q8R545; Q8R546; Q8R547; Q8R548;
AC Q8R549; Q8R551; Q9CTQ9; Q9DC14; Q9JKC3;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=SH3 domain-containing kinase-binding protein 1;
DE AltName: Full=Regulator of ubiquitous kinase;
DE Short=Ruk;
DE AltName: Full=SH3-containing, expressed in tumorigenic astrocytes;
GN Name=Sh3kbp1; Synonyms=Ruk, Seta;
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 [GENOMIC DNA] (ISOFORMS 1; 2; 3; 4; 5; 6 AND 7).
RC STRAIN=129/Ola;
RX PubMed=12242006; DOI=10.1016/s0378-1119(02)00821-1;
RA Buchman V.L., Luke C., Borthwick E.B., Gout I., Ninkina N.;
RT "Organization of the mouse Ruk locus and expression of isoforms in mouse
RT tissues.";
RL Gene 295:13-17(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J;
RC TISSUE=Embryonic stem cell, Hypothalamus, Lung, 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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 247-286.
RC STRAIN=129/SvJ;
RX PubMed=10965144; DOI=10.1159/000015634;
RA Hyatt M.A., Sykes V.W., Boyer A.D., Arden K.C., Boegler O.;
RT "Assignment of SETA to distal mouse X chromosome by radiation hybrid
RT mapping.";
RL Cytogenet. Cell Genet. 89:278-278(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 250-709 (ISOFORM 8).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RA Marra M., Hillier L., Kucaba T., Martin J., Beck C., Wylie T.,
RA Underwood K., Steptoe M., Theising B., Allen M., Bowers Y., Person B.,
RA Swaller T., Gibbons M., Pape D., Harvey N., Schurk R., Ritter E., Kohn S.,
RA Shin T., Jackson Y., Cardenas M., McCann R., Waterston R., Wilson R.;
RT "The WashU-NCI mouse EST project 1999.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH SHKBP1.
RX PubMed=11152963; DOI=10.1016/s0898-6568(00)00129-7;
RA Borinstein S.C., Hyatt M.A., Sykes V.W., Straub R.E., Lipkowitz S.,
RA Boulter J., Boegler O.;
RT "SETA is a multifunctional adapter protein with three SH3 domains that
RT binds Grb2, Cbl, and the novel SB1 proteins.";
RL Cell. Signal. 12:769-779(2000).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274, 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 [8]
RP INTERACTION WITH ATX2.
RX PubMed=18602463; DOI=10.1016/j.cellsig.2008.05.018;
RA Nonis D., Schmidt M.H., van de Loo S., Eich F., Dikic I., Nowock J.,
RA Auburger G.;
RT "Ataxin-2 associates with the endocytosis complex and affects EGF receptor
RT trafficking.";
RL Cell. Signal. 20:1725-1739(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156; SER-159; SER-274;
RP SER-480; SER-553; SER-555 AND SER-565, AND IDENTIFICATION BY MASS
RP 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).
RN [11]
RP INTERACTION WITH CBL AND SHKBP1, AND SUBCELLULAR LOCATION.
RX PubMed=21830225; DOI=10.1002/cbf.1792;
RA Feng L., Wang J.T., Jin H., Qian K., Geng J.G.;
RT "SH3KBP1-binding protein 1 prevents epidermal growth factor receptor
RT degradation by the interruption of c-Cbl-CIN85 complex.";
RL Cell Biochem. Funct. 29:589-596(2011).
RN [12]
RP STRUCTURE BY NMR OF 101-159 AND 314-370.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the SH3 domains of SH3-domain kinase binding protein
RT 1.";
RL Submitted (JUN-2006) to the PDB data bank.
CC -!- FUNCTION: Adapter protein involved in regulating diverse signal
CC transduction pathways. Involved in the regulation of endocytosis and
CC lysosomal degradation of ligand-induced receptor tyrosine kinases,
CC including EGFR and MET/hepatocyte growth factor receptor, through an
CC association with CBL and endophilins. The association with CBL, and
CC thus the receptor internalization, may be inhibited by an interaction
CC with PDCD6IP and/or SPRY2. Involved in regulation of ligand-dependent
CC endocytosis of the IgE receptor. Attenuates phosphatidylinositol 3-
CC kinase activity by interaction with its regulatory subunit (By
CC similarity). May be involved in regulation of cell adhesion; promotes
CC the interaction between TTK2B and PDCD6IP. May be involved in the
CC regulation of cellular stress response via the MAPK pathways through
CC its interaction with MAP3K4. Is involved in modulation of tumor
CC necrosis factor mediated apoptosis. Plays a role in the regulation of
CC cell morphology and cytoskeletal organization. Required in the control
CC of cell shape and migration (By similarity). Has an essential role in
CC the stimulation of B cell activation (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q96B97}.
CC -!- SUBUNIT: Can self-associate and form homotetramers. Interacts with CD2,
CC F-actin capping protein, PIK3R3, GRB2, EGFR, MET, BLNK, MAP3K4,
CC PDCD6IP, SPRY2, ARHGAP17, ARHGAP27, CRK, BCAR1, SOS1, ASAP1, ARAP3,
CC HIP1R, SYNJ2, INPP5D and STAP1 (By similarity). Interacts with CBL
CC (PubMed:21830225). Interacts with CBLB, but does not interact with
CC CBLC. Two molecules of SH3KBP1 seem to bind through their respective
CC SH3 1 domain to one molecule of CBLB. The interaction with CBL or CBLB
CC and EGFR is increased upon EGF stimulation. The interaction with CBL is
CC attenuated by PDCD6IP. Interacts through its proline-rich region with
CC the SH3 domain of endophilins SH3GL1, SH3GL2 and SH3GL3. The SH3KBP1-
CC endophilin complex seems to associate with a complex containing the
CC phosphorylated receptor (EGFR or MET) and phosphorylated CBL. Probably
CC associates with ASAP1 and phosphorylated EGFR. Probably part of a
CC complex consisting of at least SH3KBP1, ASAP1 and ARAP3. Interacts with
CC focal adhesion kinases PTK2/FAK1 AND PTK2B/PYK2, probably as a dimer.
CC Interacts with DAB2 and probably associates with chathrin through its
CC interaction with DAB2. Part of a complex consisting of SH3KBP1, DAB2,
CC and clathrin heavy chain. DAB2 and clathrin dissociate from SH3KBP1
CC following growth factor treatment, enabling interaction with CBL.
CC Interacts with DDN and probably associates with MAGI2 through its
CC interaction with DDN. Interacts with the SH3 domains of SRC tyrosine-
CC protein kinases SRC, LCK, LYN, FGR, FYN and HCK. Interacts with TRADD,
CC BIRC2, TRAF1, TRAF2 and TNFR1, and the association with a TNFR1-
CC associated complex upon stimulation with TNF-alpha seems to be mediated
CC by SRC. Probably part of a complex consisting of at least SH3KBP1,
CC ASAP1 and ARAP3 (By similarity). Interacts (via SH3 domains) with
CC SHKBP1 (via PXXXPR motifs) (PubMed:11152963, PubMed:21830225).
CC Interacts with ATX2 (PubMed:18602463). Interaction with CBL is
CC abolished in the presence of SHKBP1 (PubMed:21830225). Interacts (via
CC SH3 domains) with ZFP36 (via extreme C-terminal region). Interacts with
CC MAP3K4; this interaction enhances the association with ZFP36 (By
CC similarity). {ECO:0000250|UniProtKB:Q96B97,
CC ECO:0000269|PubMed:11152963, ECO:0000269|PubMed:18602463,
CC ECO:0000269|PubMed:21830225}.
CC -!- INTERACTION:
CC Q8R550; Q62108: Dlg4; NbExp=3; IntAct=EBI-642709, EBI-300895;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96B97}.
CC Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasmic vesicle membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Synapse,
CC synaptosome {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}.
CC Note=Localized in endocytic vesicles containing clustered receptors.
CC Colocalizes with ASAP1 in vesicular structures. Colocalized with actin
CC microfilaments and focal adhesions (By similarity). Colocalized with
CC MAGI2 in synaptosomes (By similarity). Translocation to EGFR containing
CC vesicles upon EGF stimulation is inhibited in the presence of SH3KBP1
CC (PubMed:21830225). Colocalizes with ZFP36 in the cytoplasm (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q96B97,
CC ECO:0000269|PubMed:21830225}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1; Synonyms=Ruk-xl;
CC IsoId=Q8R550-1; Sequence=Displayed;
CC Name=2; Synonyms=Ruk-l;
CC IsoId=Q8R550-2; Sequence=VSP_007510;
CC Name=3; Synonyms=Ruk-deltaA;
CC IsoId=Q8R550-3; Sequence=VSP_007505, VSP_007510;
CC Name=4; Synonyms=Ruk-m1;
CC IsoId=Q8R550-4; Sequence=VSP_007507;
CC Name=5; Synonyms=Ruk-m3;
CC IsoId=Q8R550-5; Sequence=VSP_007506;
CC Name=6; Synonyms=Ruk-t;
CC IsoId=Q8R550-6; Sequence=VSP_007508;
CC Name=7; Synonyms=Ruk-h;
CC IsoId=Q8R550-7; Sequence=VSP_007509;
CC Name=8; Synonyms=Ruk-deltaCP;
CC IsoId=Q8R550-8; Sequence=VSP_007510, VSP_007511;
CC -!- PTM: Monoubiquitinated by CBL and CBLB after EGF stimulation; probably
CC on its C-terminus. {ECO:0000250}.
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DR EMBL; AF472327; AAL82456.1; -; Genomic_DNA.
DR EMBL; AF472306; AAL82456.1; JOINED; Genomic_DNA.
DR EMBL; AF472307; AAL82456.1; JOINED; Genomic_DNA.
DR EMBL; AF472308; AAL82456.1; JOINED; Genomic_DNA.
DR EMBL; AF472309; AAL82456.1; JOINED; Genomic_DNA.
DR EMBL; AF472312; AAL82456.1; JOINED; Genomic_DNA.
DR EMBL; AF472315; AAL82456.1; JOINED; Genomic_DNA.
DR EMBL; AF472316; AAL82456.1; JOINED; Genomic_DNA.
DR EMBL; AF472317; AAL82456.1; JOINED; Genomic_DNA.
DR EMBL; AF472318; AAL82456.1; JOINED; Genomic_DNA.
DR EMBL; AF472319; AAL82456.1; JOINED; Genomic_DNA.
DR EMBL; AF472320; AAL82456.1; JOINED; Genomic_DNA.
DR EMBL; AF472322; AAL82456.1; JOINED; Genomic_DNA.
DR EMBL; AF472323; AAL82456.1; JOINED; Genomic_DNA.
DR EMBL; AF472324; AAL82456.1; JOINED; Genomic_DNA.
DR EMBL; AF472325; AAL82456.1; JOINED; Genomic_DNA.
DR EMBL; AF472326; AAL82456.1; JOINED; Genomic_DNA.
DR EMBL; AF472327; AAL82457.1; -; Genomic_DNA.
DR EMBL; AF472325; AAL82457.1; JOINED; Genomic_DNA.
DR EMBL; AF472326; AAL82457.1; JOINED; Genomic_DNA.
DR EMBL; AF472327; AAL82458.1; -; Genomic_DNA.
DR EMBL; AF472304; AAL82458.1; JOINED; Genomic_DNA.
DR EMBL; AF472305; AAL82458.1; JOINED; Genomic_DNA.
DR EMBL; AF472307; AAL82458.1; JOINED; Genomic_DNA.
DR EMBL; AF472308; AAL82458.1; JOINED; Genomic_DNA.
DR EMBL; AF472309; AAL82458.1; JOINED; Genomic_DNA.
DR EMBL; AF472312; AAL82458.1; JOINED; Genomic_DNA.
DR EMBL; AF472315; AAL82458.1; JOINED; Genomic_DNA.
DR EMBL; AF472316; AAL82458.1; JOINED; Genomic_DNA.
DR EMBL; AF472317; AAL82458.1; JOINED; Genomic_DNA.
DR EMBL; AF472318; AAL82458.1; JOINED; Genomic_DNA.
DR EMBL; AF472319; AAL82458.1; JOINED; Genomic_DNA.
DR EMBL; AF472320; AAL82458.1; JOINED; Genomic_DNA.
DR EMBL; AF472322; AAL82458.1; JOINED; Genomic_DNA.
DR EMBL; AF472323; AAL82458.1; JOINED; Genomic_DNA.
DR EMBL; AF472324; AAL82458.1; JOINED; Genomic_DNA.
DR EMBL; AF472325; AAL82458.1; JOINED; Genomic_DNA.
DR EMBL; AF472326; AAL82458.1; JOINED; Genomic_DNA.
DR EMBL; AF472327; AAL82459.1; -; Genomic_DNA.
DR EMBL; AF472313; AAL82459.1; JOINED; Genomic_DNA.
DR EMBL; AF472314; AAL82459.1; JOINED; Genomic_DNA.
DR EMBL; AF472315; AAL82459.1; JOINED; Genomic_DNA.
DR EMBL; AF472316; AAL82459.1; JOINED; Genomic_DNA.
DR EMBL; AF472317; AAL82459.1; JOINED; Genomic_DNA.
DR EMBL; AF472318; AAL82459.1; JOINED; Genomic_DNA.
DR EMBL; AF472319; AAL82459.1; JOINED; Genomic_DNA.
DR EMBL; AF472320; AAL82459.1; JOINED; Genomic_DNA.
DR EMBL; AF472322; AAL82459.1; JOINED; Genomic_DNA.
DR EMBL; AF472323; AAL82459.1; JOINED; Genomic_DNA.
DR EMBL; AF472324; AAL82459.1; JOINED; Genomic_DNA.
DR EMBL; AF472325; AAL82459.1; JOINED; Genomic_DNA.
DR EMBL; AF472326; AAL82459.1; JOINED; Genomic_DNA.
DR EMBL; AF472327; AAL82460.1; -; Genomic_DNA.
DR EMBL; AF472313; AAL82460.1; JOINED; Genomic_DNA.
DR EMBL; AF472315; AAL82460.1; JOINED; Genomic_DNA.
DR EMBL; AF472316; AAL82460.1; JOINED; Genomic_DNA.
DR EMBL; AF472317; AAL82460.1; JOINED; Genomic_DNA.
DR EMBL; AF472318; AAL82460.1; JOINED; Genomic_DNA.
DR EMBL; AF472319; AAL82460.1; JOINED; Genomic_DNA.
DR EMBL; AF472320; AAL82460.1; JOINED; Genomic_DNA.
DR EMBL; AF472322; AAL82460.1; JOINED; Genomic_DNA.
DR EMBL; AF472323; AAL82460.1; JOINED; Genomic_DNA.
DR EMBL; AF472324; AAL82460.1; JOINED; Genomic_DNA.
DR EMBL; AF472325; AAL82460.1; JOINED; Genomic_DNA.
DR EMBL; AF472326; AAL82460.1; JOINED; Genomic_DNA.
DR EMBL; AF472327; AAL82461.1; -; Genomic_DNA.
DR EMBL; AF472321; AAL82461.1; JOINED; Genomic_DNA.
DR EMBL; AF472322; AAL82461.1; JOINED; Genomic_DNA.
DR EMBL; AF472323; AAL82461.1; JOINED; Genomic_DNA.
DR EMBL; AF472324; AAL82461.1; JOINED; Genomic_DNA.
DR EMBL; AF472325; AAL82461.1; JOINED; Genomic_DNA.
DR EMBL; AF472326; AAL82461.1; JOINED; Genomic_DNA.
DR EMBL; AF472327; AAL82462.1; -; Genomic_DNA.
DR EMBL; AF472304; AAL82462.1; JOINED; Genomic_DNA.
DR EMBL; AF472305; AAL82462.1; JOINED; Genomic_DNA.
DR EMBL; AF472307; AAL82462.1; JOINED; Genomic_DNA.
DR EMBL; AF472308; AAL82462.1; JOINED; Genomic_DNA.
DR EMBL; AF472309; AAL82462.1; JOINED; Genomic_DNA.
DR EMBL; AF472310; AAL82462.1; JOINED; Genomic_DNA.
DR EMBL; AF472311; AAL82462.1; JOINED; Genomic_DNA.
DR EMBL; AF472312; AAL82462.1; JOINED; Genomic_DNA.
DR EMBL; AF472315; AAL82462.1; JOINED; Genomic_DNA.
DR EMBL; AF472316; AAL82462.1; JOINED; Genomic_DNA.
DR EMBL; AF472317; AAL82462.1; JOINED; Genomic_DNA.
DR EMBL; AF472318; AAL82462.1; JOINED; Genomic_DNA.
DR EMBL; AF472319; AAL82462.1; JOINED; Genomic_DNA.
DR EMBL; AF472320; AAL82462.1; JOINED; Genomic_DNA.
DR EMBL; AF472322; AAL82462.1; JOINED; Genomic_DNA.
DR EMBL; AF472323; AAL82462.1; JOINED; Genomic_DNA.
DR EMBL; AF472324; AAL82462.1; JOINED; Genomic_DNA.
DR EMBL; AF472325; AAL82462.1; JOINED; Genomic_DNA.
DR EMBL; AF472326; AAL82462.1; JOINED; Genomic_DNA.
DR EMBL; AK004636; BAB23427.2; -; mRNA.
DR EMBL; AK020782; BAB32209.2; -; mRNA.
DR EMBL; AK038540; BAC30033.1; -; mRNA.
DR EMBL; AK049182; BAC33592.1; -; mRNA.
DR EMBL; AL929452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF243508; AAF68439.1; -; Genomic_DNA.
DR EMBL; AI428677; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS41194.1; -. [Q8R550-3]
DR CCDS; CCDS53234.1; -. [Q8R550-2]
DR CCDS; CCDS53235.1; -. [Q8R550-5]
DR RefSeq; NP_001129199.1; NM_001135727.2. [Q8R550-2]
DR RefSeq; NP_001129200.1; NM_001135728.2. [Q8R550-5]
DR RefSeq; NP_001277590.1; NM_001290661.1. [Q8R550-7]
DR RefSeq; NP_001277593.1; NM_001290664.1. [Q8R550-7]
DR RefSeq; NP_067364.2; NM_021389.6. [Q8R550-3]
DR RefSeq; XP_006528987.1; XM_006528924.3. [Q8R550-1]
DR RefSeq; XP_011246151.1; XM_011247849.2.
DR RefSeq; XP_011246153.1; XM_011247851.2. [Q8R550-6]
DR PDB; 1WI7; NMR; -; A=101-155.
DR PDB; 2DA9; NMR; -; A=314-370.
DR PDB; 5XHZ; X-ray; 1.32 A; A/B=98-157.
DR PDBsum; 1WI7; -.
DR PDBsum; 2DA9; -.
DR PDBsum; 5XHZ; -.
DR AlphaFoldDB; Q8R550; -.
DR SMR; Q8R550; -.
DR BioGRID; 208383; 38.
DR CORUM; Q8R550; -.
DR IntAct; Q8R550; 13.
DR MINT; Q8R550; -.
DR STRING; 10090.ENSMUSP00000108075; -.
DR iPTMnet; Q8R550; -.
DR PhosphoSitePlus; Q8R550; -.
DR EPD; Q8R550; -.
DR jPOST; Q8R550; -.
DR MaxQB; Q8R550; -.
DR PeptideAtlas; Q8R550; -.
DR PRIDE; Q8R550; -.
DR ProteomicsDB; 261024; -. [Q8R550-1]
DR ProteomicsDB; 261025; -. [Q8R550-2]
DR ProteomicsDB; 261026; -. [Q8R550-3]
DR ProteomicsDB; 261027; -. [Q8R550-4]
DR ProteomicsDB; 261028; -. [Q8R550-5]
DR ProteomicsDB; 261029; -. [Q8R550-6]
DR ProteomicsDB; 261030; -. [Q8R550-7]
DR ProteomicsDB; 261031; -. [Q8R550-8]
DR Antibodypedia; 521; 216 antibodies from 32 providers.
DR DNASU; 58194; -.
DR Ensembl; ENSMUST00000073094; ENSMUSP00000072840; ENSMUSG00000040990. [Q8R550-1]
DR Ensembl; ENSMUST00000080394; ENSMUSP00000079257; ENSMUSG00000040990. [Q8R550-3]
DR Ensembl; ENSMUST00000112451; ENSMUSP00000108070; ENSMUSG00000040990. [Q8R550-5]
DR Ensembl; ENSMUST00000112453; ENSMUSP00000108072; ENSMUSG00000040990. [Q8R550-4]
DR Ensembl; ENSMUST00000112456; ENSMUSP00000108075; ENSMUSG00000040990. [Q8R550-2]
DR GeneID; 58194; -.
DR KEGG; mmu:58194; -.
DR UCSC; uc009uss.3; mouse. [Q8R550-1]
DR UCSC; uc009usv.3; mouse. [Q8R550-3]
DR UCSC; uc009usx.3; mouse. [Q8R550-5]
DR CTD; 30011; -.
DR MGI; MGI:1889583; Sh3kbp1.
DR VEuPathDB; HostDB:ENSMUSG00000040990; -.
DR eggNOG; KOG4348; Eukaryota.
DR GeneTree; ENSGT00940000155886; -.
DR HOGENOM; CLU_024255_1_0_1; -.
DR InParanoid; Q8R550; -.
DR OMA; PNSCHRS; -.
DR OrthoDB; 1577081at2759; -.
DR PhylomeDB; Q8R550; -.
DR TreeFam; TF350191; -.
DR Reactome; R-MMU-182971; EGFR downregulation.
DR Reactome; R-MMU-6807004; Negative regulation of MET activity.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-MMU-8866376; Reelin signalling pathway.
DR Reactome; R-MMU-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR BioGRID-ORCS; 58194; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Sh3kbp1; mouse.
DR EvolutionaryTrace; Q8R550; -.
DR PRO; PR:Q8R550; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q8R550; protein.
DR Bgee; ENSMUSG00000040990; Expressed in thymus and 248 other tissues.
DR ExpressionAtlas; Q8R550; baseline and differential.
DR Genevisible; Q8R550; MM.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030139; C:endocytic vesicle; IDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0050871; P:positive regulation of B cell activation; ISO:MGI.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR CDD; cd12052; SH3_CIN85_1; 1.
DR CDD; cd12055; SH3_CIN85_2; 1.
DR CDD; cd12057; SH3_CIN85_3; 1.
DR InterPro; IPR035770; CIN85_SH3_1.
DR InterPro; IPR035771; CIN85_SH3_2.
DR InterPro; IPR035772; CIN85_SH3_3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR028506; Sorbin_SH3.
DR PANTHER; PTHR14167:SF6; PTHR14167:SF6; 2.
DR Pfam; PF14604; SH3_9; 3.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 3.
DR SUPFAM; SSF50044; SSF50044; 3.
DR PROSITE; PS50002; SH3; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Cell junction; Coiled coil;
KW Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Endocytosis; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; SH3 domain; SH3-binding;
KW Synapse; Synaptosome; Ubl conjugation.
FT CHAIN 1..709
FT /note="SH3 domain-containing kinase-binding protein 1"
FT /id="PRO_0000097729"
FT DOMAIN 1..58
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 98..157
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 311..372
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 221..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 646..708
FT /evidence="ECO:0000255"
FT COMPBIAS 222..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96B97"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 298
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96B97"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 553
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96B97"
FT VAR_SEQ 1..599
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_007509"
FT VAR_SEQ 1..477
FT /note="MVEAIVEFDYQAQHDDELTISVGEVITNIRKEDGGWWEGQINGRRGLFPDNF
FT VREIKKDMKKDLLSNKAPEKPMHDVSSGNALLSSETILRTNKRGERRRRRCQVAFSYLP
FT QNDDELELKVGDIIEVVGEVEEGWWEGVLNGKTGMFPSNFIKELSGESDELGISQDEQL
FT SKSRPEGFLPASLLPFPAHGAKGKTTFEGTILYRAAPGKTEGHRRYYSLRETTGSESDG
FT GDSSSTKSEGANGTMATAAIQPKKVKGVGFGDIFKDKPIKLRPRSIEVENDFLPVEKTI
FT GKKLPPATSTPDPSKTEMDSRTKTKDYCKVIFPYEAQNDDELTIKEGDIVTLINKDCID
FT VGWWEGELNGRRGVFPDNFVKLLPSDFDKEGNRPKKPPPPSAPVVKQGAGTTERKHEIK
FT KIPPERPETLPNRTEEKERPEREPKLDLQKPSVPAIPPKKPRPPKTNSLNRPGALPPRR
FT PERPVGPLTHTR -> MFPFRKGARPPSMNLFRQTCW (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_007508"
FT VAR_SEQ 1..286
FT /note="MVEAIVEFDYQAQHDDELTISVGEVITNIRKEDGGWWEGQINGRRGLFPDNF
FT VREIKKDMKKDLLSNKAPEKPMHDVSSGNALLSSETILRTNKRGERRRRRCQVAFSYLP
FT QNDDELELKVGDIIEVVGEVEEGWWEGVLNGKTGMFPSNFIKELSGESDELGISQDEQL
FT SKSRPEGFLPASLLPFPAHGAKGKTTFEGTILYRAAPGKTEGHRRYYSLRETTGSESDG
FT GDSSSTKSEGANGTMATAAIQPKKVKGVGFGDIFKDKPIKLRPRSIEVENDFLPVEK
FT -> MGEEVSLGEKNISPEQASCGALHPRGWGSQTFGVFLVNEET (in isoform
FT 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_007507"
FT VAR_SEQ 1..286
FT /note="MVEAIVEFDYQAQHDDELTISVGEVITNIRKEDGGWWEGQINGRRGLFPDNF
FT VREIKKDMKKDLLSNKAPEKPMHDVSSGNALLSSETILRTNKRGERRRRRCQVAFSYLP
FT QNDDELELKVGDIIEVVGEVEEGWWEGVLNGKTGMFPSNFIKELSGESDELGISQDEQL
FT SKSRPEGFLPASLLPFPAHGAKGKTTFEGTILYRAAPGKTEGHRRYYSLRETTGSESDG
FT GDSSSTKSEGANGTMATAAIQPKKVKGVGFGDIFKDKPIKLRPRSIEVENDFLPVEK
FT -> MGEE (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_007506"
FT VAR_SEQ 1..54
FT /note="MVEAIVEFDYQAQHDDELTISVGEVITNIRKEDGGWWEGQINGRRGLFPDNF
FT VR -> MELSAAKAPSPTDLPES (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007505"
FT VAR_SEQ 174..217
FT /note="Missing (in isoform 2, isoform 3 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.5"
FT /id="VSP_007510"
FT VAR_SEQ 320..630
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_007511"
FT CONFLICT 251..259
FT /note="PKKVKGVGF -> NDDELTIKE (in Ref. 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 478..528
FT /note="GDSPKIDLAGSALSGILDKDLSDRSNDIDLEGFDSVISSTEKLSHPTTSRP
FT -> YCHVLTKAGGHGMIMKIGEGMRTKLCLKIPATFFSSEKVVARCWGATWCRL (in
FT Ref. 2; BAC30033)"
FT /evidence="ECO:0000305"
FT CONFLICT 529..709
FT /note="Missing (in Ref. 2; BAC30033)"
FT /evidence="ECO:0000305"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:5XHZ"
FT STRAND 124..132
FT /evidence="ECO:0007829|PDB:5XHZ"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:5XHZ"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:5XHZ"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:5XHZ"
FT STRAND 314..318
FT /evidence="ECO:0007829|PDB:2DA9"
FT STRAND 336..342
FT /evidence="ECO:0007829|PDB:2DA9"
FT STRAND 350..354
FT /evidence="ECO:0007829|PDB:2DA9"
FT STRAND 359..363
FT /evidence="ECO:0007829|PDB:2DA9"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:2DA9"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:2DA9"
SQ SEQUENCE 709 AA; 78170 MW; AC2DDFB3248A458B CRC64;
MVEAIVEFDY QAQHDDELTI SVGEVITNIR KEDGGWWEGQ INGRRGLFPD NFVREIKKDM
KKDLLSNKAP EKPMHDVSSG NALLSSETIL RTNKRGERRR RRCQVAFSYL PQNDDELELK
VGDIIEVVGE VEEGWWEGVL NGKTGMFPSN FIKELSGESD ELGISQDEQL SKSRPEGFLP
ASLLPFPAHG AKGKTTFEGT ILYRAAPGKT EGHRRYYSLR ETTGSESDGG DSSSTKSEGA
NGTMATAAIQ PKKVKGVGFG DIFKDKPIKL RPRSIEVEND FLPVEKTIGK KLPPATSTPD
PSKTEMDSRT KTKDYCKVIF PYEAQNDDEL TIKEGDIVTL INKDCIDVGW WEGELNGRRG
VFPDNFVKLL PSDFDKEGNR PKKPPPPSAP VVKQGAGTTE RKHEIKKIPP ERPETLPNRT
EEKERPEREP KLDLQKPSVP AIPPKKPRPP KTNSLNRPGA LPPRRPERPV GPLTHTRGDS
PKIDLAGSAL SGILDKDLSD RSNDIDLEGF DSVISSTEKL SHPTTSRPKA TGRRPPSQSL
TSSSLSSPDI FDSPSPEEDK EEHISLAHRG IDVSKKTSKT VTISQVSDNK TSLPPKPGTM
AAASSGPASL SSVASSPMSS SLGTAGQRAS SPSLFSTEGK PKMEPAVSSQ AAIEELKMQV
RELRTIIETM KDQQKREIKQ LLSELDEEKK IRLRLQMEVN DIKKALQSK
