ID NCK1_HUMAN Reviewed; 377 AA. AC P16333; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1990, sequence version 1. DT 22-SEP-2009, entry version 109. DE RecName: Full=Cytoplasmic protein NCK1; DE AltName: Full=NCK adaptor protein 1; DE Short=Nck-1; DE AltName: Full=SH2/SH3 adaptor protein NCK-alpha; GN Name=NCK1; Synonyms=NCK; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=90192089; PubMed=2107526; DOI=10.1093/nar/18.4.1048; RA Lehmann J.M., Riethmueller G., Johnson J.P.; RT "Nck, a melanoma cDNA encoding a cytoplasmic protein consisting of the RT src homology units SH2 and SH3."; RL Nucleic Acids Res. 18:1048-1048(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Uterus; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PHOSPHORYLATION, AND PARTIAL PROTEIN SEQUENCE. RX MEDLINE=93078783; PubMed=1333046; RA Park D., Rhee S.G.; RT "Phosphorylation of Nck in response to a variety of receptors, phorbol RT myristate acetate, and cyclic AMP."; RL Mol. Cell. Biol. 12:5816-5823(1992). RN [4] RP PHOSPHORYLATION. RX MEDLINE=93078786; PubMed=1448108; RA Meisenhelder J., Hunter T.; RT "The SH2/SH3 domain-containing protein Nck is recognized by certain RT anti-phospholipase C-gamma 1 monoclonal antibodies, and its RT phosphorylation on tyrosine is stimulated by platelet-derived growth RT factor and epidermal growth factor treatment."; RL Mol. Cell. Biol. 12:5843-5856(1992). RN [5] RP INTERACTION WITH SOCS7. RX MEDLINE=98008866; PubMed=9344857; DOI=10.1006/bbrc.1997.7492; RA Matuoka K., Miki H., Takahashi K., Takenawa T.; RT "A novel ligand for an SH3 domain of the adaptor protein Nck bears an RT SH2 domain and nuclear signaling motifs."; RL Biochem. Biophys. Res. Commun. 239:488-492(1997). RN [6] RP INTERACTION WITH BLNK; GRB2; PLCG1 AND VAV. RX MEDLINE=98361304; PubMed=9697839; DOI=10.1016/S1074-7613(00)80591-9; RA Fu C., Turck C.W., Kurosaki T., Chan A.C.; RT "BLNK: a central linker protein in B cell activation."; RL Immunity 9:93-103(1998). RN [7] RP INTERACTION WITH RALGPS1. RX MEDLINE=20250892; PubMed=10747847; DOI=10.1074/jbc.C000085200; RA Rebhun J.F., Chen H., Quilliam L.A.; RT "Identification and characterization of a new family of guanine RT nucleotide exchange factors for the ras-related GTPase Ral."; RL J. Biol. Chem. 275:13406-13410(2000). RN [8] RP INTERACTION WITH CAV2. RX MEDLINE=22206546; PubMed=12091389; DOI=10.1074/jbc.M204367200; RA Lee H., Park D.S., Wang X.B., Scherer P.E., Schwartz P.E., RA Lisanti M.P.; RT "Src-induced phosphorylation of caveolin-2 on tyrosine 19. Phospho- RT caveolin-2 (Tyr(P)19) is localized near focal adhesions, remains RT associated with lipid rafts/caveolae, but no longer forms a high RT molecular mass hetero-oligomer with caveolin-1."; RL J. Biol. Chem. 277:34556-34567(2002). RN [9] RP INTERACTION WITH CAV2. RX PubMed=15504032; RA Wang X.B., Lee H., Capozza F., Marmon S., Sotgia F., Brooks J.W., RA Campos-Gonzalez R., Lisanti M.P.; RT "Tyrosine phosphorylation of caveolin-2 at residue 27: differences in RT the spatial and temporal behavior of phospho-Cav-2 (pY19 and pY27)."; RL Biochemistry 43:13694-13706(2004). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-105, AND MASS RP SPECTROMETRY. RC TISSUE=Epithelium; RX PubMed=15951569; DOI=10.1074/mcp.M500089-MCP200; RA Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., RA Lauffenburger D.A., White F.M.; RT "Time-resolved mass spectrometry of tyrosine phosphorylation sites in RT the epidermal growth factor receptor signaling network reveals dynamic RT modules."; RL Mol. Cell. Proteomics 4:1240-1250(2005). RN [11] RP IDENTIFICATION IN COMPLEX WITH PP1 AND PPP1R15B, FUNCTION, AND RP SUBCELLULAR LOCATION. RX PubMed=16835242; DOI=10.1074/jbc.M513556200; RA Latreille M., Larose L.; RT "Nck in a complex containing the catalytic subunit of protein RT phosphatase 1 regulates eukaryotic initiation factor 2alpha signaling RT and cell survival to endoplasmic reticulum stress."; RL J. Biol. Chem. 281:26633-26644(2006). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-96 AND TYR-105, RP AND MASS SPECTROMETRY. RX PubMed=17287340; DOI=10.1073/pnas.0611217104; RA Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; RT "Global proteomic profiling of phosphopeptides using electron transfer RT dissociation tandem mass spectrometry."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-105, AND MASS RP SPECTROMETRY. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-91 AND SER-96, RP AND MASS SPECTROMETRY. RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [15] RP IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. RN [16] RP STRUCTURE BY NMR OF 99-174. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the SH3 domain of the human cytoplasmic protein RT NCK1."; RL Submitted (NOV-2005) to the PDB data bank. CC -!- FUNCTION: Adapter protein which associates with tyrosine- CC phosphorylated growth factor receptors or their cellular CC substrates. Maintains low levels of EIF2S1 phosphorylation by CC promoting its dephosphorylation by PP1. CC -!- SUBUNIT: Associates with BLNK, PLCG1, VAV1 and NCK1 in a B-cell CC antigen receptor-dependent fashion. Interacts with SOCS7. Part of CC a complex containing PPP1R15B, PP1 and NCK1. Interacts with CC RALGPS1. Interacts with CAV2 (tyrosine phosphorylated form). CC -!- INTERACTION: CC Q9H222:ABCG5; NbExp=1; IntAct=EBI-389883, EBI-1761423; CC Q8IZP0:ABI1; NbExp=1; IntAct=EBI-389883, EBI-375446; CC P00519:ABL1; NbExp=1; IntAct=EBI-389883, EBI-375543; CC P42684:ABL2; NbExp=1; IntAct=EBI-389883, EBI-1102694; CC Q15027:ACAP1; NbExp=1; IntAct=EBI-389883, EBI-751746; CC P51816:AFF2; NbExp=1; IntAct=EBI-389883, EBI-1754468; CC Q15109:AGER; NbExp=1; IntAct=EBI-389883, EBI-1646426; CC O43918:AIRE; NbExp=1; IntAct=EBI-389883, EBI-1753081; CC Q9Y2D5:AKAP2; NbExp=1; IntAct=EBI-389883, EBI-1754555; CC Q13023:AKAP6; NbExp=1; IntAct=EBI-389883, EBI-1056102; CC Q01484:ANK2; NbExp=1; IntAct=EBI-389883, EBI-941975; CC Q9BWW9:APOL5; NbExp=1; IntAct=EBI-389883, EBI-1753592; CC O15085:ARHGEF11; NbExp=1; IntAct=EBI-389883, EBI-311099; CC Q9ULH1:ASAP1; NbExp=1; IntAct=EBI-389883, EBI-346622; CC O43150:ASAP2; NbExp=1; IntAct=EBI-389883, EBI-310968; CC Q96NS5:ASB16; NbExp=1; IntAct=EBI-389883, EBI-1751918; CC Q8IXJ9:ASXL1; NbExp=1; IntAct=EBI-389883, EBI-1646500; CC Q93084:ATP2A3; NbExp=1; IntAct=EBI-389883, EBI-1046185; CC Q9UIF9:BAZ2A; NbExp=1; IntAct=EBI-389883, EBI-934890; CC P38398:BRCA1; NbExp=1; IntAct=EBI-389883, EBI-349905; CC O60885:BRD4; NbExp=1; IntAct=EBI-389883, EBI-723869; CC Q9ULD4:BRPF3; NbExp=1; IntAct=EBI-389883, EBI-1753470; CC P13671:C6; NbExp=1; IntAct=EBI-389883, EBI-1753221; CC P20810:CAST; NbExp=1; IntAct=EBI-389883, EBI-1268770; CC P32239:CCKBR; NbExp=1; IntAct=EBI-389883, EBI-1753137; CC P46092:CCR10; NbExp=1; IntAct=EBI-389883, EBI-348022; CC P30260:CDC27; NbExp=1; IntAct=EBI-389883, EBI-994813; CC Q9HCU4:CELSR2; NbExp=1; IntAct=EBI-389883, EBI-724117; CC Q9NYQ7:CELSR3; NbExp=1; IntAct=EBI-389883, EBI-308417; CC Q13111:CHAF1A; NbExp=1; IntAct=EBI-389883, EBI-1020839; CC Q9H2X0:CHRD; NbExp=1; IntAct=EBI-389883, EBI-947551; CC Q14008:CKAP5; NbExp=1; IntAct=EBI-389883, EBI-310585; CC P26992:CNTFR; NbExp=1; IntAct=EBI-389883, EBI-743758; CC P78357:CNTNAP1; NbExp=1; IntAct=EBI-389883, EBI-1751903; CC Q8WX92:COBRA1; NbExp=1; IntAct=EBI-389883, EBI-347721; CC O75534:CSDE1; NbExp=1; IntAct=EBI-389883, EBI-719186; CC Q7Z408:CSMD2; NbExp=1; IntAct=EBI-389883, EBI-1957312; CC P78329:CYP4F2; NbExp=1; IntAct=EBI-389883, EBI-1752413; CC P98082:DAB2; NbExp=1; IntAct=EBI-389883, EBI-1171238; CC Q14118:DAG1; NbExp=1; IntAct=EBI-389883, EBI-1755945; CC O14490:DLGAP1; NbExp=1; IntAct=EBI-389883, EBI-1753207; CC Q9P1A6:DLGAP2; NbExp=1; IntAct=EBI-389883, EBI-1753397; CC O95886:DLGAP3; NbExp=1; IntAct=EBI-389883, EBI-1752541; CC Q9Y2H0:DLGAP4; NbExp=1; IntAct=EBI-389883, EBI-722139; CC Q92988:DLX4; NbExp=1; IntAct=EBI-389883, EBI-1752755; CC Q05193:DNM1; NbExp=2; IntAct=EBI-389883, EBI-713135; CC P21575:Dnm1 (xeno); NbExp=1; IntAct=EBI-389883, EBI-80070; CC Q14185:DOCK1; NbExp=1; IntAct=EBI-389883, EBI-446740; CC Q8IZD9:DOCK3; NbExp=1; IntAct=EBI-389883, EBI-1752361; CC Q96EV8:DTNBP1; NbExp=1; IntAct=EBI-389883, EBI-465804; CC Q9H1R2:DUSP15; NbExp=1; IntAct=EBI-389883, EBI-1752795; CC Q9H8V3:ECT2; NbExp=1; IntAct=EBI-389883, EBI-1054039; CC O43281:EFS; NbExp=1; IntAct=EBI-389883, EBI-718488; CC Q96KQ7:EHMT2; NbExp=1; IntAct=EBI-389883, EBI-744366; CC P41970:ELK3; NbExp=1; IntAct=EBI-389883, EBI-1758534; CC P42566:EPS15; NbExp=1; IntAct=EBI-389883, EBI-396684; CC P11678:EPX; NbExp=1; IntAct=EBI-389883, EBI-1761505; CC O00254:F2RL2; NbExp=1; IntAct=EBI-389883, EBI-1751853; CC Q9BQ89:FAM110A; NbExp=1; IntAct=EBI-389883, EBI-1752811; CC O15360:FANCA; NbExp=1; IntAct=EBI-389883, EBI-81570; CC P31994:FCGR2B; NbExp=1; IntAct=EBI-389883, EBI-724784; CC P31995:FCGR2C; NbExp=1; IntAct=EBI-389883, EBI-1396036; CC O75369:FLNB; NbExp=1; IntAct=EBI-389883, EBI-352089; CC Q14315:FLNC; NbExp=1; IntAct=EBI-389883, EBI-489954; CC O75593:FOXH1; NbExp=1; IntAct=EBI-389883, EBI-1759806; CC O15117:FYB; NbExp=1; IntAct=EBI-389883, EBI-1753267; CC Q9UBS5:GABBR1; NbExp=1; IntAct=EBI-389883, EBI-724156; CC Q99259:GAD1; NbExp=1; IntAct=EBI-389883, EBI-743184; CC P10912:GHR; NbExp=1; IntAct=EBI-389883, EBI-286316; CC Q9NZM4:GLTSCR1; NbExp=1; IntAct=EBI-389883, EBI-1754943; CC P15586:GNS; NbExp=1; IntAct=EBI-389883, EBI-1752200; CC Q9Y5Y3:GPR45; NbExp=1; IntAct=EBI-389883, EBI-1751869; CC O43708:GSTZ1; NbExp=1; IntAct=EBI-389883, EBI-748043; CC P10412:HIST1H1E; NbExp=1; IntAct=EBI-389883, EBI-358163; CC O43390:HNRNPR; NbExp=1; IntAct=EBI-389883, EBI-713419; CC P31273:HOXC8; NbExp=1; IntAct=EBI-389883, EBI-1752118; CC P47928:ID4; NbExp=1; IntAct=EBI-389883, EBI-1754719; CC P26951:IL3RA; NbExp=1; IntAct=EBI-389883, EBI-1757512; CC Q9H9L3:ISG20L2; NbExp=1; IntAct=EBI-389883, EBI-751335; CC O60674:JAK2; NbExp=1; IntAct=EBI-389883, EBI-518647; CC Q9H1H9:KIF13A; NbExp=1; IntAct=EBI-389883, EBI-1759129; CC Q96AC6:KIFC2; NbExp=1; IntAct=EBI-389883, EBI-724040; CC Q9BY71:LRRC3; NbExp=1; IntAct=EBI-389883, EBI-1761329; CC P27816:MAP4; NbExp=1; IntAct=EBI-389883, EBI-715255; CC Q92918:MAP4K1; NbExp=1; IntAct=EBI-389883, EBI-881; CC Q8IVH8:MAP4K3; NbExp=1; IntAct=EBI-389883, EBI-1758170; CC Q9Y4K4:MAP4K5; NbExp=1; IntAct=EBI-389883, EBI-1279; CC O60244:MED14; NbExp=1; IntAct=EBI-389883, EBI-394489; CC Q9NQ76:MEPE; NbExp=1; IntAct=EBI-389883, EBI-1753293; CC Q15746:MYLK; NbExp=1; IntAct=EBI-389883, EBI-968482; CC Q8NFW9:MYRIP; NbExp=1; IntAct=EBI-389883, EBI-1759414; CC O14513:NAP5; NbExp=1; IntAct=EBI-389883, EBI-1752508; CC Q86SG6:NEK8; NbExp=1; IntAct=EBI-389883, EBI-1752987; CC O94856:NFASC; NbExp=1; IntAct=EBI-389883, EBI-1751948; CC P43699:NKX2-1; NbExp=1; IntAct=EBI-389883, EBI-1391923; CC Q9UM47:NOTCH3; NbExp=1; IntAct=EBI-389883, EBI-1236377; CC O60500:NPHS1; NbExp=2; IntAct=EBI-389883, EBI-996920; CC Q9HCQ7:NPVF; NbExp=1; IntAct=EBI-389883, EBI-1753111; CC Q13285:NR5A1; NbExp=1; IntAct=EBI-389883, EBI-874629; CC O95157:NXPH3; NbExp=1; IntAct=EBI-389883, EBI-1752913; CC P01178:OXT; NbExp=1; IntAct=EBI-389883, EBI-1762651; CC Q99572:P2RX7; NbExp=1; IntAct=EBI-389883, EBI-1753251; CC P23760:PAX3; NbExp=1; IntAct=EBI-389883, EBI-1167564; CC P23759:PAX7; NbExp=1; IntAct=EBI-389883, EBI-1042757; CC Q13087:PDIA2; NbExp=1; IntAct=EBI-389883, EBI-1752525; CC O75167:PHACTR2; NbExp=1; IntAct=EBI-389883, EBI-1754409; CC O00750:PIK3C2B; NbExp=1; IntAct=EBI-389883, EBI-641107; CC O00329:PIK3CD; NbExp=1; IntAct=EBI-389883, EBI-718309; CC Q9UL42:PNMA2; NbExp=1; IntAct=EBI-389883, EBI-302355; CC Q9H9Y6:POLR1B; NbExp=1; IntAct=EBI-389883, EBI-355441; CC O43900:PRICKLE3; NbExp=1; IntAct=EBI-389883, EBI-1751761; CC Q9BXM0:PRX; NbExp=1; IntAct=EBI-389883, EBI-1753064; CC P29074:PTPN4; NbExp=1; IntAct=EBI-389883, EBI-710431; CC P15918:RAG1; NbExp=1; IntAct=EBI-389883, EBI-1755109; CC Q13905:RAPGEF1; NbExp=1; IntAct=EBI-389883, EBI-976876; CC Q86UR5:RIMS1; NbExp=1; IntAct=EBI-389883, EBI-1043236; CC Q9UQ26:RIMS2; NbExp=1; IntAct=EBI-389883, EBI-1756749; CC Q8TB24:RIN3; NbExp=1; IntAct=EBI-389883, EBI-1570523; CC Q9NRR4:RNASEN; NbExp=1; IntAct=EBI-389883, EBI-528367; CC Q8IWN7:RP1L1; NbExp=1; IntAct=EBI-389883, EBI-1757848; CC P26373:RPL13; NbExp=1; IntAct=EBI-389883, EBI-356849; CC P78345:RPP38; NbExp=1; IntAct=EBI-389883, EBI-366493; CC P10301:RRAS; NbExp=1; IntAct=EBI-389883, EBI-968703; CC P21817:RYR1; NbExp=1; IntAct=EBI-389883, EBI-1221290; CC O94885:SASH1; NbExp=1; IntAct=EBI-389883, EBI-1761310; CC Q96GP6:SCARF2; NbExp=1; IntAct=EBI-389883, EBI-1752088; CC O75326:SEMA7A; NbExp=1; IntAct=EBI-389883, EBI-1753538; CC Q9NZV5:SEPN1; NbExp=1; IntAct=EBI-389883, EBI-1751965; CC Q15427:SF3B4; NbExp=1; IntAct=EBI-389883, EBI-348469; CC Q9UPX8:SHANK2; NbExp=1; IntAct=EBI-389883, EBI-1570571; CC Q9BYB0:SHANK3; NbExp=1; IntAct=EBI-389883, EBI-1752330; CC Q13796:SHROOM2; NbExp=1; IntAct=EBI-389883, EBI-1644065; CC O75751:SLC22A3; NbExp=1; IntAct=EBI-389883, EBI-1752674; CC Q9UHI7:SLC23A1; NbExp=1; IntAct=EBI-389883, EBI-1759386; CC O60721:SLC24A1; NbExp=1; IntAct=EBI-389883, EBI-1753504; CC Q9UMY4:SNX12; NbExp=1; IntAct=EBI-389883, EBI-1752602; CC Q15036:SNX17; NbExp=1; IntAct=EBI-389883, EBI-1752620; CC O60493:SNX3; NbExp=1; IntAct=EBI-389883, EBI-727209; CC Q9UNH6:SNX7; NbExp=1; IntAct=EBI-389883, EBI-751422; CC Q9Y5X2:SNX8; NbExp=1; IntAct=EBI-389883, EBI-1752557; CC Q07889:SOS1; NbExp=2; IntAct=EBI-389883, EBI-297487; CC Q497A5:Sos1 (xeno); NbExp=1; IntAct=EBI-389883, EBI-922895; CC Q07890:SOS2; NbExp=1; IntAct=EBI-389883, EBI-298181; CC P08047:SP1; NbExp=1; IntAct=EBI-389883, EBI-298336; CC Q96T58:SPEN; NbExp=1; IntAct=EBI-389883, EBI-765739; CC Q9H5I1:SUV39H2; NbExp=1; IntAct=EBI-389883, EBI-723127; CC O15056:SYNJ2; NbExp=1; IntAct=EBI-389883, EBI-310513; CC O95455:TGDS; NbExp=1; IntAct=EBI-389883, EBI-1761487; CC O43493:TGOLN2; NbExp=1; IntAct=EBI-389883, EBI-1752146; CC Q9NR96:TLR9; NbExp=1; IntAct=EBI-389883, EBI-1762509; CC P42167:TMPO; NbExp=1; IntAct=EBI-389883, EBI-455283; CC Q9UKE5:TNIK; NbExp=1; IntAct=EBI-389883, EBI-1051794; CC P15157:TPSAB1; NbExp=1; IntAct=EBI-389883, EBI-1762849; CC Q15661:TPSAB1; NbExp=1; IntAct=EBI-389883, EBI-1761369; CC P20231:TPSB2; NbExp=1; IntAct=EBI-389883, EBI-1761383; CC Q9ULW0:TPX2; NbExp=1; IntAct=EBI-389883, EBI-1037322; CC Q9BWF2:TRAIP; NbExp=1; IntAct=EBI-389883, EBI-1756205; CC Q9HCM9:TRIM39; NbExp=1; IntAct=EBI-389883, EBI-739510; CC O00294:TULP1; NbExp=1; IntAct=EBI-389883, EBI-1756778; CC O60287:URB1; NbExp=1; IntAct=EBI-389883, EBI-1762349; CC Q96RL7:VPS13A; NbExp=1; IntAct=EBI-389883, EBI-1752583; CC O00401:WASL; NbExp=1; IntAct=EBI-389883, EBI-957615; CC Q9UMN6:WBP7; NbExp=1; IntAct=EBI-389883, EBI-765774; CC O43516:WIPF1; NbExp=2; IntAct=EBI-389883, EBI-346356; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum. CC -!- PTM: Phosphorylated on Ser and Tyr residues. CC -!- SIMILARITY: Contains 1 SH2 domain. CC -!- SIMILARITY: Contains 3 SH3 domains. 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; X17576; CAA35599.1; -; mRNA. DR EMBL; BC006403; AAH06403.1; -; mRNA. DR IPI; IPI00028065; -. DR PIR; S08636; S08636. DR RefSeq; NP_006144.1; -. DR UniGene; Hs.477693; -. DR PDB; 2CI8; X-ray; 1.80 A; A=281-377. DR PDB; 2CI9; X-ray; 1.50 A; A/B=281-377. DR PDB; 2CUB; NMR; -; A=99-173. DR PDB; 2JS0; NMR; -; A=107-165. DR PDB; 2JS2; NMR; -; A=1-61. DR PDB; 2JW4; NMR; -; A=1-63. DR PDBsum; 2CI8; -. DR PDBsum; 2CI9; -. DR PDBsum; 2CUB; -. DR PDBsum; 2JS0; -. DR PDBsum; 2JS2; -. DR PDBsum; 2JW4; -. DR SMR; P16333; 190-254. DR DIP; DIP:639N; -. DR IntAct; P16333; 164. DR STRING; P16333; -. DR PhosphoSite; P16333; -. DR PeptideAtlas; P16333; -. DR PRIDE; P16333; -. DR Ensembl; ENST00000288986; ENSP00000288986; ENSG00000158092; Homo sapiens. DR GeneID; 4690; -. DR KEGG; hsa:4690; -. DR UCSC; uc003erh.1; human. DR CTD; 4690; -. DR GeneCards; GC03P138063; -. DR H-InvDB; HIX0003707; -. DR HGNC; HGNC:7664; NCK1. DR HPA; CAB005063; -. DR MIM; 600508; gene. DR PharmGKB; PA31466; -. DR HOGENOM; P16333; -. DR HOVERGEN; P16333; -. DR OMA; P16333; RFAGKEW. DR Pathway_Interaction_DB; angiopoietinreceptor_pathway; Angiopoietin receptor Tie2-mediated signaling. DR Pathway_Interaction_DB; ephbfwdpathway; EPHB forward signaling. DR Pathway_Interaction_DB; insulin_pathway; Insulin Pathway. DR Pathway_Interaction_DB; pdgfrbpathway; PDGFR-beta signaling pathway. DR Pathway_Interaction_DB; met_pathway; Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met). DR Pathway_Interaction_DB; vegfr1_2_pathway; Signaling events mediated by VEGFR1 and VEGFR2. DR Pathway_Interaction_DB; ret_pathway; Signaling events regulated by Ret tyrosine kinase. DR Pathway_Interaction_DB; tcrpathway; TCR signaling in naive CD4+ T cells. DR Pathway_Interaction_DB; vegfr1_pathway; VEGFR1 specific signals. DR Reactome; REACT_16888; Signaling by PDGF. DR NextBio; 18086; -. DR PMAP-CutDB; P16333; -. DR ArrayExpress; P16333; -. DR Bgee; P16333; -. DR CleanEx; HS_NCK1; -. DR GermOnline; ENSG00000158092; Homo sapiens. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0008093; F:cytoskeletal adaptor activity; NAS:UniProtKB. DR GO; GO:0005102; F:receptor binding; IPI:UniProtKB. DR GO; GO:0030159; F:receptor signaling complex scaffold activity; NAS:UniProtKB. DR GO; GO:0030838; P:positive regulation of actin filament polym...; IMP:UniProtKB. DR GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:UniProtKB. DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW. DR GO; GO:0007172; P:signal complex assembly; NAS:UniProtKB. DR GO; GO:0042110; P:T cell activation; IMP:UniProtKB. DR InterPro; IPR017304; Cytoplasmic_NCK. DR InterPro; IPR000980; SH2. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR020473; SH3_region. DR Gene3D; G3DSA:3.30.505.10; SH2; 1. DR Pfam; PF00017; SH2; 1. DR Pfam; PF00018; SH3_1; 3. DR PIRSF; PIRSF037874; Cytoplasmic_NCK; 1. DR PRINTS; PR00401; SH2DOMAIN. DR PRINTS; PR00452; SH3DOMAIN. DR ProDom; PD000093; SH2; 1. DR ProDom; PD000066; SH3; 3. DR SMART; SM00252; SH2; 1. DR SMART; SM00326; SH3; 3. DR PROSITE; PS50001; SH2; 1. DR PROSITE; PS50002; SH3; 3. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; KW Endoplasmic reticulum; Phosphoprotein; Polymorphism; Repeat; KW SH2 domain; SH3 domain; Translation regulation. FT CHAIN 1 377 Cytoplasmic protein NCK1. FT /FTId=PRO_0000096766. FT DOMAIN 2 61 SH3 1. FT DOMAIN 115 165 SH3 2. FT DOMAIN 190 252 SH3 3. FT DOMAIN 282 376 SH2. FT MOD_RES 85 85 Phosphoserine. FT MOD_RES 91 91 Phosphoserine. FT MOD_RES 96 96 Phosphoserine. FT MOD_RES 105 105 Phosphotyrosine. FT VARIANT 180 180 A -> V (in dbSNP:rs13320485). FT /FTId=VAR_051228. FT STRAND 5 11 FT STRAND 28 33 FT STRAND 35 42 FT STRAND 48 51 FT TURN 53 55 FT STRAND 56 58 FT STRAND 99 101 FT STRAND 109 115 FT STRAND 131 138 FT STRAND 142 148 FT STRAND 151 156 FT HELIX 157 159 FT STRAND 160 162 FT STRAND 168 170 FT HELIX 289 299 FT STRAND 305 309 FT STRAND 311 313 FT STRAND 316 323 FT STRAND 326 332 FT STRAND 339 341 FT STRAND 344 348 FT HELIX 349 358 FT STRAND 361 363 SQ SEQUENCE 377 AA; 42864 MW; 554E9B1A936AEF30 CRC64; MAEEVVVVAK FDYVAQQEQE LDIKKNERLW LLDDSKSWWR VRNSMNKTGF VPSNYVERKN SARKASIVKN LKDTLGIGKV KRKPSVPDSA SPADDSFVDP GERLYDLNMP AYVKFNYMAE REDELSLIKG TKVIVMEKCS DGWWRGSYNG QVGWFPSNYV TEEGDSPLGD HVGSLSEKLA AVVNNLNTGQ VLHVVQALYP FSSSNDEELN FEKGDVMDVI EKPENDPEWW KCRKINGMVG LVPKNYVTVM QNNPLTSGLE PSPPQCDYIR PSLTGKFAGN PWYYGKVTRH QAEMALNERG HEGDFLIRDS ESSPNDFSVS LKAQGKNKHF KVQLKETVYC IGQRKFSTME ELVEHYKKAP IFTSEQGEKL YLVKHLS //