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 27-MAR-2024, entry version 181. 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, RC 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 [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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 40. 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 PaxDb; 10090-ENSMUSP00000108075; -. DR PeptideAtlas; 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 Pumba; Q8R550; -. DR Antibodypedia; 521; 236 antibodies from 32 providers. DR DNASU; 58194; -. DR Ensembl; ENSMUST00000073094.10; ENSMUSP00000072840.4; ENSMUSG00000040990.18. [Q8R550-1] DR Ensembl; ENSMUST00000080394.13; ENSMUSP00000079257.7; ENSMUSG00000040990.18. [Q8R550-3] DR Ensembl; ENSMUST00000112451.8; ENSMUSP00000108070.2; ENSMUSG00000040990.18. [Q8R550-5] DR Ensembl; ENSMUST00000112453.9; ENSMUSP00000108072.3; ENSMUSG00000040990.18. [Q8R550-4] DR Ensembl; ENSMUST00000112456.9; ENSMUSP00000108075.3; ENSMUSG00000040990.18. [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 AGR; MGI:1889583; -. 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; QHITKNR; -. DR OrthoDB; 2972088at2759; -. 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 80 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 251 other cell types or tissues. DR ExpressionAtlas; Q8R550; baseline and differential. 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:0060090; F:molecular adaptor activity; ISO:MGI. 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:0050871; P:positive regulation of B cell activation; ISO:MGI. DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB. DR GO; GO:0070086; P:ubiquitin-dependent endocytosis; ISO:MGI. DR CDD; cd12052; SH3_CIN85_1; 1. DR CDD; cd12055; SH3_CIN85_2; 1. DR CDD; cd12057; SH3_CIN85_3; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 3. 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 PANTHER; PTHR14167; SH3 DOMAIN-CONTAINING; 1. DR PANTHER; PTHR14167:SF6; SH3 DOMAIN-CONTAINING KINASE-BINDING PROTEIN 1; 1. DR Pfam; PF14604; SH3_9; 3. DR PRINTS; PR00499; P67PHOX. DR PRINTS; PR00452; SH3DOMAIN. DR SMART; SM00326; SH3; 3. DR SUPFAM; SSF50044; SH3-domain; 3. DR PROSITE; PS50002; SH3; 3. DR Genevisible; Q8R550; MM. 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 //