NCK2_HUMAN
ID NCK2_HUMAN Reviewed; 380 AA.
AC O43639; D3DVK1; Q9BWN9; Q9UIC3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Cytoplasmic protein NCK2;
DE AltName: Full=Growth factor receptor-bound protein 4;
DE AltName: Full=NCK adaptor protein 2;
DE Short=Nck-2;
DE AltName: Full=SH2/SH3 adaptor protein NCK-beta;
GN Name=NCK2; Synonyms=GRB4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9737977; DOI=10.1074/jbc.273.39.25171;
RA Chen M., She H., Davis E.M., Spicer C.M., Kim L., Ren R., LeBeau M.M.,
RA Li W.;
RT "Identification of Nck family genes, chromosomal localization, expression,
RT and signaling specificity.";
RL J. Biol. Chem. 273:25171-25178(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH LIMS1.
RC TISSUE=Lung;
RX PubMed=9843575; DOI=10.1091/mbc.9.12.3367;
RA Tu Y., Li F., Wu C.;
RT "Nck-2, a novel Src homology2/3-containing adaptor protein that interacts
RT with the LIM-only protein PINCH and components of growth factor receptor
RT kinase-signaling pathways.";
RL Mol. Biol. Cell 9:3367-3382(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, INTERACTION WITH EGFR; PAK1; PKN2 AND SOS1, AND PHOSPHORYLATION.
RX PubMed=10026169; DOI=10.1074/jbc.274.9.5542;
RA Braverman L.E., Quilliam L.A.;
RT "Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing
RT adapter protein having similar binding and biological properties to Nck.";
RL J. Biol. Chem. 274:5542-5549(1999).
RN [6]
RP INTERACTION WITH TGFB1I1.
RX PubMed=10330411; DOI=10.1083/jcb.145.4.851;
RA Turner C.E., Brown M.C., Perrotta J.A., Riedy M.C., Nikolopoulos S.N.,
RA McDonald A.R., Bagrodia S., Thomas S.M., Leventhal P.S.;
RT "Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat,
RT ARF-GAP protein: a role in cytoskeletal remodeling.";
RL J. Cell Biol. 145:851-863(1999).
RN [7]
RP INTERACTION WITH DOCK1, AND MUTAGENESIS OF TRP-148 AND TRP-234.
RX PubMed=11240126; DOI=10.1016/s0014-5793(01)02195-0;
RA Tu Y., Kucik D.F., Wu C.;
RT "Identification and kinetic analysis of the interaction between Nck-2 and
RT DOCK180.";
RL FEBS Lett. 491:193-199(2001).
RN [8]
RP INTERACTION WITH AXL.
RX PubMed=12470648; DOI=10.1016/s0006-291x(02)02718-3;
RA Hafizi S., Alindri F., Karlsson R., Dahlbaeck B.;
RT "Interaction of Axl receptor tyrosine kinase with C1-TEN, a novel C1
RT domain-containing protein with homology to tensin.";
RL Biochem. Biophys. Res. Commun. 299:793-800(2002).
RN [9]
RP INTERACTION WITH DDR1.
RX PubMed=16337946; DOI=10.1016/j.febslet.2005.11.035;
RA Koo D.H., McFadden C., Huang Y., Abdulhussein R., Friese-Hamim M.,
RA Vogel W.F.;
RT "Pinpointing phosphotyrosine-dependent interactions downstream of the
RT collagen receptor DDR1.";
RL FEBS Lett. 580:15-22(2006).
RN [10]
RP IDENTIFICATION IN COMPLEX WITH PP1 AND PPP1R15B, FUNCTION, AND SUBCELLULAR
RP 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 phosphatase 1
RT regulates eukaryotic initiation factor 2alpha signaling and cell survival
RT to endoplasmic reticulum stress.";
RL J. Biol. Chem. 281:26633-26644(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-110, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [12]
RP INTERACTION WITH FASLG.
RX PubMed=19807924; DOI=10.1186/1471-2172-10-53;
RA Voss M., Lettau M., Janssen O.;
RT "Identification of SH3 domain interaction partners of human FasL (CD178) by
RT phage display screening.";
RL BMC Immunol. 10:53-53(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90 AND THR-92, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP STRUCTURE BY NMR OF 188-265.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the SH3 domain of the human cytoplasmic protein
RT NCK2.";
RL Submitted (JUL-2005) to the PDB data bank.
CC -!- FUNCTION: Adapter protein which associates with tyrosine-phosphorylated
CC growth factor receptors or their cellular substrates. Maintains low
CC levels of EIF2S1 phosphorylation by promoting its dephosphorylation by
CC PP1. Plays a role in ELK1-dependent transcriptional activation in
CC response to activated Ras signaling. {ECO:0000269|PubMed:10026169,
CC ECO:0000269|PubMed:16835242}.
CC -!- SUBUNIT: Interacts with DOCK1, LIMS1 and TGFB1I1. Part of a complex
CC containing PPP1R15B, PP1 and NCK2. Interacts with FASLG (By
CC similarity). Interacts with AXL. Interacts with PAK1, PKN2 and SOS1.
CC Interacts (via SH2 domain) with EGFR. Interacts (via SH2 domain) with
CC DDR1. {ECO:0000250, ECO:0000269|PubMed:10026169,
CC ECO:0000269|PubMed:10330411, ECO:0000269|PubMed:11240126,
CC ECO:0000269|PubMed:12470648, ECO:0000269|PubMed:16337946,
CC ECO:0000269|PubMed:16835242, ECO:0000269|PubMed:19807924,
CC ECO:0000269|PubMed:9843575}.
CC -!- INTERACTION:
CC O43639; Q9NYB9: ABI2; NbExp=6; IntAct=EBI-713635, EBI-743598;
CC O43639; Q9NYB9-2: ABI2; NbExp=10; IntAct=EBI-713635, EBI-11096309;
CC O43639; Q9P2A4: ABI3; NbExp=6; IntAct=EBI-713635, EBI-742038;
CC O43639; Q3KP44: ANKRD55; NbExp=3; IntAct=EBI-713635, EBI-14493093;
CC O43639; Q7Z6G8-3: ANKS1B; NbExp=3; IntAct=EBI-713635, EBI-17714371;
CC O43639; A7KAX9: ARHGAP32; NbExp=3; IntAct=EBI-713635, EBI-308663;
CC O43639; P56945: BCAR1; NbExp=3; IntAct=EBI-713635, EBI-702093;
CC O43639; Q9H165-2: BCL11A; NbExp=6; IntAct=EBI-713635, EBI-10183342;
CC O43639; P62324: BTG1; NbExp=3; IntAct=EBI-713635, EBI-742279;
CC O43639; Q53FE4: C4orf17; NbExp=3; IntAct=EBI-713635, EBI-715110;
CC O43639; Q8N350-4: CBARP; NbExp=3; IntAct=EBI-713635, EBI-19051169;
CC O43639; Q13191: CBLB; NbExp=8; IntAct=EBI-713635, EBI-744027;
CC O43639; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-713635, EBI-744556;
CC O43639; P07766: CD3E; NbExp=4; IntAct=EBI-713635, EBI-1211297;
CC O43639; P15882: CHN1; NbExp=16; IntAct=EBI-713635, EBI-718947;
CC O43639; P52757: CHN2; NbExp=6; IntAct=EBI-713635, EBI-714925;
CC O43639; Q99828: CIB1; NbExp=3; IntAct=EBI-713635, EBI-372594;
CC O43639; Q9C0C6: CIPC; NbExp=3; IntAct=EBI-713635, EBI-5654244;
CC O43639; Q6ZS10: CLEC17A; NbExp=3; IntAct=EBI-713635, EBI-11977093;
CC O43639; Q16630-2: CPSF6; NbExp=3; IntAct=EBI-713635, EBI-11088043;
CC O43639; Q8N684: CPSF7; NbExp=4; IntAct=EBI-713635, EBI-746909;
CC O43639; Q8N684-3: CPSF7; NbExp=3; IntAct=EBI-713635, EBI-11523759;
CC O43639; Q9NWM3: CUEDC1; NbExp=3; IntAct=EBI-713635, EBI-5838167;
CC O43639; Q08345: DDR1; NbExp=3; IntAct=EBI-713635, EBI-711879;
CC O43639; Q8NES8: DEFB124; NbExp=3; IntAct=EBI-713635, EBI-12843376;
CC O43639; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-713635, EBI-11988027;
CC O43639; Q9Y2H0-1: DLGAP4; NbExp=6; IntAct=EBI-713635, EBI-12000556;
CC O43639; Q14919: DRAP1; NbExp=3; IntAct=EBI-713635, EBI-712941;
CC O43639; Q8N9I9: DTX3; NbExp=5; IntAct=EBI-713635, EBI-2340258;
CC O43639; Q86TH3: DVL1; NbExp=3; IntAct=EBI-713635, EBI-10185025;
CC O43639; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-713635, EBI-2349927;
CC O43639; P52799: EFNB2; NbExp=7; IntAct=EBI-713635, EBI-7532268;
CC O43639; O15372: EIF3H; NbExp=6; IntAct=EBI-713635, EBI-709735;
CC O43639; Q6IB98: EIF3S3; NbExp=3; IntAct=EBI-713635, EBI-10184995;
CC O43639; P04626: ERBB2; NbExp=2; IntAct=EBI-713635, EBI-641062;
CC O43639; P21860: ERBB3; NbExp=2; IntAct=EBI-713635, EBI-720706;
CC O43639; Q86V42: FAM124A; NbExp=3; IntAct=EBI-713635, EBI-744506;
CC O43639; B7ZLH0: FAM22F; NbExp=3; IntAct=EBI-713635, EBI-10220102;
CC O43639; A0A0C4DGW7: FAM47A; NbExp=3; IntAct=EBI-713635, EBI-12011070;
CC O43639; Q9NYF3: FAM53C; NbExp=8; IntAct=EBI-713635, EBI-1644252;
CC O43639; Q86UY5: FAM83A; NbExp=3; IntAct=EBI-713635, EBI-1384254;
CC O43639; P48023: FASLG; NbExp=4; IntAct=EBI-713635, EBI-495538;
CC O43639; Q6PCT2-2: FBXL19; NbExp=3; IntAct=EBI-713635, EBI-11959077;
CC O43639; Q96LA5: FCRL2; NbExp=3; IntAct=EBI-713635, EBI-10185081;
CC O43639; P53539: FOSB; NbExp=3; IntAct=EBI-713635, EBI-2806743;
CC O43639; O15117: FYB1; NbExp=3; IntAct=EBI-713635, EBI-1753267;
CC O43639; Q13480: GAB1; NbExp=5; IntAct=EBI-713635, EBI-517684;
CC O43639; Q9H706: GAREM1; NbExp=3; IntAct=EBI-713635, EBI-3440103;
CC O43639; Q86UU5: GGN; NbExp=3; IntAct=EBI-713635, EBI-10259069;
CC O43639; Q8IX15-3: HOMEZ; NbExp=3; IntAct=EBI-713635, EBI-10172004;
CC O43639; P49639: HOXA1; NbExp=3; IntAct=EBI-713635, EBI-740785;
CC O43639; P09017: HOXC4; NbExp=3; IntAct=EBI-713635, EBI-3923226;
CC O43639; Q86TF7: HOXC4; NbExp=3; IntAct=EBI-713635, EBI-10185009;
CC O43639; P13378: HOXD8; NbExp=3; IntAct=EBI-713635, EBI-7098661;
CC O43639; O75031: HSF2BP; NbExp=3; IntAct=EBI-713635, EBI-7116203;
CC O43639; Q0VD86: INCA1; NbExp=3; IntAct=EBI-713635, EBI-6509505;
CC O43639; Q9H0H0: INTS2; NbExp=3; IntAct=EBI-713635, EBI-8471507;
CC O43639; Q8N5Z5: KCTD17; NbExp=3; IntAct=EBI-713635, EBI-743960;
CC O43639; Q6ZU52: KIAA0408; NbExp=7; IntAct=EBI-713635, EBI-739493;
CC O43639; P10721: KIT; NbExp=2; IntAct=EBI-713635, EBI-1379503;
CC O43639; Q6TFL4: KLHL24; NbExp=3; IntAct=EBI-713635, EBI-2510117;
CC O43639; Q6PF15: KLHL35; NbExp=3; IntAct=EBI-713635, EBI-9477654;
CC O43639; Q5T749: KPRP; NbExp=3; IntAct=EBI-713635, EBI-10981970;
CC O43639; Q13094: LCP2; NbExp=10; IntAct=EBI-713635, EBI-346946;
CC O43639; P48059: LIMS1; NbExp=2; IntAct=EBI-713635, EBI-306928;
CC O43639; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-713635, EBI-739832;
CC O43639; A6PVS8: LRRIQ3; NbExp=6; IntAct=EBI-713635, EBI-10184751;
CC O43639; Q9BRK4: LZTS2; NbExp=6; IntAct=EBI-713635, EBI-741037;
CC O43639; P43360: MAGEA6; NbExp=6; IntAct=EBI-713635, EBI-1045155;
CC O43639; Q96DN6: MBD6; NbExp=3; IntAct=EBI-713635, EBI-719591;
CC O43639; P50222: MEOX2; NbExp=3; IntAct=EBI-713635, EBI-748397;
CC O43639; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-713635, EBI-16439278;
CC O43639; P08581: MET; NbExp=2; IntAct=EBI-713635, EBI-1039152;
CC O43639; Q5JRA6: MIA3; NbExp=3; IntAct=EBI-713635, EBI-2291868;
CC O43639; Q99583: MNT; NbExp=3; IntAct=EBI-713635, EBI-7959025;
CC O43639; Q86VE0: MYPOP; NbExp=3; IntAct=EBI-713635, EBI-2858213;
CC O43639; Q9NZQ3-3: NCKIPSD; NbExp=3; IntAct=EBI-713635, EBI-10963850;
CC O43639; Q9H3P2: NELFA; NbExp=3; IntAct=EBI-713635, EBI-5461341;
CC O43639; Q7Z628: NET1; NbExp=3; IntAct=EBI-713635, EBI-2511306;
CC O43639; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-713635, EBI-10271199;
CC O43639; Q5HYW2: NHSL2; NbExp=6; IntAct=EBI-713635, EBI-2859639;
CC O43639; Q99743: NPAS2; NbExp=6; IntAct=EBI-713635, EBI-3932727;
CC O43639; Q13285: NR5A1; NbExp=3; IntAct=EBI-713635, EBI-874629;
CC O43639; O60422: ONECUT3; NbExp=3; IntAct=EBI-713635, EBI-17431136;
CC O43639; Q13153: PAK1; NbExp=10; IntAct=EBI-713635, EBI-1307;
CC O43639; Q13177: PAK2; NbExp=8; IntAct=EBI-713635, EBI-1045887;
CC O43639; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-713635, EBI-10302990;
CC O43639; Q8N4B1-4: PHETA1; NbExp=3; IntAct=EBI-713635, EBI-14131832;
CC O43639; Q6ZUJ8-3: PIK3AP1; NbExp=7; IntAct=EBI-713635, EBI-11981743;
CC O43639; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-713635, EBI-11320284;
CC O43639; Q569H4: PRR16; NbExp=3; IntAct=EBI-713635, EBI-5564642;
CC O43639; P86479: PRR20C; NbExp=3; IntAct=EBI-713635, EBI-10172814;
CC O43639; P86480: PRR20D; NbExp=3; IntAct=EBI-713635, EBI-12754095;
CC O43639; O75832: PSMD10; NbExp=2; IntAct=EBI-713635, EBI-752185;
CC O43639; Q02833: RASSF7; NbExp=5; IntAct=EBI-713635, EBI-929013;
CC O43639; Q8NC74: RBBP8NL; NbExp=3; IntAct=EBI-713635, EBI-11322432;
CC O43639; Q5T8P6: RBM26; NbExp=3; IntAct=EBI-713635, EBI-3232077;
CC O43639; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-713635, EBI-7545592;
CC O43639; Q04864: REL; NbExp=3; IntAct=EBI-713635, EBI-307352;
CC O43639; Q04864-2: REL; NbExp=3; IntAct=EBI-713635, EBI-10829018;
CC O43639; Q7L0Q8: RHOU; NbExp=6; IntAct=EBI-713635, EBI-1638043;
CC O43639; Q96L33: RHOV; NbExp=4; IntAct=EBI-713635, EBI-8538631;
CC O43639; Q9NQC3: RTN4; NbExp=2; IntAct=EBI-713635, EBI-715945;
CC O43639; Q9UQR0: SCML2; NbExp=3; IntAct=EBI-713635, EBI-2513111;
CC O43639; Q7RTU7: SCX; NbExp=3; IntAct=EBI-713635, EBI-17492262;
CC O43639; Q15637-4: SF1; NbExp=3; IntAct=EBI-713635, EBI-12223157;
CC O43639; Q15428: SF3A2; NbExp=3; IntAct=EBI-713635, EBI-2462271;
CC O43639; Q15427: SF3B4; NbExp=7; IntAct=EBI-713635, EBI-348469;
CC O43639; Q96IW2: SHD; NbExp=3; IntAct=EBI-713635, EBI-4402781;
CC O43639; Q13573: SNW1; NbExp=3; IntAct=EBI-713635, EBI-632715;
CC O43639; O14512: SOCS7; NbExp=3; IntAct=EBI-713635, EBI-1539606;
CC O43639; O94875: SORBS2; NbExp=3; IntAct=EBI-713635, EBI-311323;
CC O43639; Q8IUW3: SPATA2L; NbExp=3; IntAct=EBI-713635, EBI-2510414;
CC O43639; Q9H0A9-2: SPATC1L; NbExp=5; IntAct=EBI-713635, EBI-11995806;
CC O43639; O43597: SPRY2; NbExp=3; IntAct=EBI-713635, EBI-742487;
CC O43639; Q9H3Y6: SRMS; NbExp=3; IntAct=EBI-713635, EBI-8541270;
CC O43639; Q8TE77: SSH3; NbExp=3; IntAct=EBI-713635, EBI-8743776;
CC O43639; Q96PV0: SYNGAP1; NbExp=3; IntAct=EBI-713635, EBI-2682386;
CC O43639; P15884: TCF4; NbExp=3; IntAct=EBI-713635, EBI-533224;
CC O43639; Q8TDR4: TCP10L; NbExp=3; IntAct=EBI-713635, EBI-3923210;
CC O43639; Q9BTD3: TMEM121; NbExp=3; IntAct=EBI-713635, EBI-12155101;
CC O43639; A1L306: TNR; NbExp=3; IntAct=EBI-713635, EBI-10182881;
CC O43639; P14373: TRIM27; NbExp=6; IntAct=EBI-713635, EBI-719493;
CC O43639; Q8WV44: TRIM41; NbExp=8; IntAct=EBI-713635, EBI-725997;
CC O43639; Q15654: TRIP6; NbExp=8; IntAct=EBI-713635, EBI-742327;
CC O43639; P42681: TXK; NbExp=3; IntAct=EBI-713635, EBI-7877438;
CC O43639; P0CG48: UBC; NbExp=2; IntAct=EBI-713635, EBI-3390054;
CC O43639; Q8NFA0-2: USP32; NbExp=5; IntAct=EBI-713635, EBI-12220239;
CC O43639; Q5ST30: VARS2; NbExp=3; IntAct=EBI-713635, EBI-2116622;
CC O43639; Q5ST30-4: VARS2; NbExp=3; IntAct=EBI-713635, EBI-10244997;
CC O43639; Q9H9H4: VPS37B; NbExp=6; IntAct=EBI-713635, EBI-4400866;
CC O43639; P42768: WAS; NbExp=3; IntAct=EBI-713635, EBI-346375;
CC O43639; Q92558: WASF1; NbExp=4; IntAct=EBI-713635, EBI-1548747;
CC O43639; O00401: WASL; NbExp=7; IntAct=EBI-713635, EBI-957615;
CC O43639; O43516-4: WIPF1; NbExp=3; IntAct=EBI-713635, EBI-12052927;
CC O43639; Q9Y330: ZBTB12; NbExp=3; IntAct=EBI-713635, EBI-12377219;
CC O43639; B2RXF5: ZBTB42; NbExp=3; IntAct=EBI-713635, EBI-12287587;
CC O43639; O15156: ZBTB7B; NbExp=3; IntAct=EBI-713635, EBI-740434;
CC O43639; O15156-2: ZBTB7B; NbExp=3; IntAct=EBI-713635, EBI-11522250;
CC O43639; Q96GY0: ZC2HC1A; NbExp=3; IntAct=EBI-713635, EBI-5458880;
CC O43639; Q5TFG8: ZC2HC1B; NbExp=3; IntAct=EBI-713635, EBI-12275374;
CC O43639; Q9BYN7: ZNF341; NbExp=3; IntAct=EBI-713635, EBI-9089622;
CC O43639; Q8TF50: ZNF526; NbExp=3; IntAct=EBI-713635, EBI-11035148;
CC O43639; P0C7X2: ZNF688; NbExp=3; IntAct=EBI-713635, EBI-4395732;
CC O43639; Q7VLE8: lspA1; Xeno; NbExp=2; IntAct=EBI-713635, EBI-26445163;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16835242}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:16835242}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:10026169}.
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DR EMBL; AF043119; AAC04831.1; -; mRNA.
DR EMBL; AF047487; AAC80284.1; -; mRNA.
DR EMBL; CH471127; EAX01753.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01754.1; -; Genomic_DNA.
DR EMBL; BC000103; AAH00103.1; -; mRNA.
DR EMBL; BC007195; AAH07195.1; -; mRNA.
DR CCDS; CCDS33266.1; -.
DR RefSeq; NP_001004720.1; NM_001004720.2.
DR RefSeq; NP_003572.2; NM_003581.4.
DR RefSeq; XP_006712860.1; XM_006712797.3.
DR RefSeq; XP_011510293.1; XM_011511991.2.
DR RefSeq; XP_016860592.1; XM_017005103.1.
DR RefSeq; XP_016860593.1; XM_017005104.1.
DR RefSeq; XP_016860594.1; XM_017005105.1.
DR PDB; 1U5S; NMR; -; A=192-262.
DR PDB; 1WX6; NMR; -; A=188-265.
DR PDB; 1Z3K; NMR; -; A=283-380.
DR PDB; 2B86; NMR; -; A=1-59.
DR PDB; 2CIA; X-ray; 1.45 A; A=284-380.
DR PDB; 2FRW; NMR; -; A=114-170.
DR PDB; 2FRY; NMR; -; A=198-256.
DR PDB; 2JXB; NMR; -; A=1-59.
DR PDB; 4E6R; X-ray; 2.20 A; A/B=114-170.
DR PDBsum; 1U5S; -.
DR PDBsum; 1WX6; -.
DR PDBsum; 1Z3K; -.
DR PDBsum; 2B86; -.
DR PDBsum; 2CIA; -.
DR PDBsum; 2FRW; -.
DR PDBsum; 2FRY; -.
DR PDBsum; 2JXB; -.
DR PDBsum; 4E6R; -.
DR AlphaFoldDB; O43639; -.
DR BMRB; O43639; -.
DR SMR; O43639; -.
DR BioGRID; 114020; 246.
DR IntAct; O43639; 204.
DR MINT; O43639; -.
DR STRING; 9606.ENSP00000233154; -.
DR MoonDB; O43639; Predicted.
DR iPTMnet; O43639; -.
DR PhosphoSitePlus; O43639; -.
DR BioMuta; NCK2; -.
DR EPD; O43639; -.
DR jPOST; O43639; -.
DR MassIVE; O43639; -.
DR MaxQB; O43639; -.
DR PaxDb; O43639; -.
DR PeptideAtlas; O43639; -.
DR PRIDE; O43639; -.
DR ProteomicsDB; 49088; -.
DR ABCD; O43639; 1 sequenced antibody.
DR Antibodypedia; 4240; 358 antibodies from 37 providers.
DR DNASU; 8440; -.
DR Ensembl; ENST00000233154.9; ENSP00000233154.4; ENSG00000071051.14.
DR Ensembl; ENST00000393349.2; ENSP00000377018.2; ENSG00000071051.14.
DR GeneID; 8440; -.
DR KEGG; hsa:8440; -.
DR MANE-Select; ENST00000233154.9; ENSP00000233154.4; NM_003581.5; NP_003572.2.
DR UCSC; uc002tdg.4; human.
DR CTD; 8440; -.
DR DisGeNET; 8440; -.
DR GeneCards; NCK2; -.
DR HGNC; HGNC:7665; NCK2.
DR HPA; ENSG00000071051; Low tissue specificity.
DR MIM; 604930; gene.
DR neXtProt; NX_O43639; -.
DR OpenTargets; ENSG00000071051; -.
DR PharmGKB; PA31467; -.
DR VEuPathDB; HostDB:ENSG00000071051; -.
DR eggNOG; KOG4226; Eukaryota.
DR GeneTree; ENSGT00940000157728; -.
DR HOGENOM; CLU_025160_0_1_1; -.
DR InParanoid; O43639; -.
DR OMA; ASMTNGQ; -.
DR OrthoDB; 1097449at2759; -.
DR PhylomeDB; O43639; -.
DR TreeFam; TF351631; -.
DR PathwayCommons; O43639; -.
DR Reactome; R-HSA-186763; Downstream signal transduction.
DR Reactome; R-HSA-373753; Nephrin family interactions.
DR Reactome; R-HSA-3928664; Ephrin signaling.
DR Reactome; R-HSA-428540; Activation of RAC1.
DR Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-HSA-8985801; Regulation of cortical dendrite branching.
DR Reactome; R-HSA-9013420; RHOU GTPase cycle.
DR Reactome; R-HSA-9013424; RHOV GTPase cycle.
DR SignaLink; O43639; -.
DR SIGNOR; O43639; -.
DR BioGRID-ORCS; 8440; 10 hits in 1079 CRISPR screens.
DR ChiTaRS; NCK2; human.
DR EvolutionaryTrace; O43639; -.
DR GeneWiki; NCK2; -.
DR GenomeRNAi; 8440; -.
DR Pharos; O43639; Tbio.
DR PRO; PR:O43639; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O43639; protein.
DR Bgee; ENSG00000071051; Expressed in cortical plate and 194 other tissues.
DR ExpressionAtlas; O43639; baseline and differential.
DR Genevisible; O43639; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0012506; C:vesicle membrane; IEA:Ensembl.
DR GO; GO:0008093; F:cytoskeletal anchor activity; NAS:UniProtKB.
DR GO; GO:0001784; F:phosphotyrosine residue binding; IPI:CAFA.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IBA:GO_Central.
DR GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
DR GO; GO:0035591; F:signaling adaptor activity; IBA:GO_Central.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; NAS:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0060996; P:dendritic spine development; IEA:Ensembl.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0001771; P:immunological synapse formation; IEA:Ensembl.
DR GO; GO:0030032; P:lamellipodium assembly; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:1903912; P:negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IDA:ParkinsonsUK-UCL.
DR GO; GO:1903898; P:negative regulation of PERK-mediated unfolded protein response; IBA:GO_Central.
DR GO; GO:1990441; P:negative regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; IEA:Ensembl.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:UniProtKB.
DR GO; GO:1902237; P:positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IBA:GO_Central.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0036493; P:positive regulation of translation in response to endoplasmic reticulum stress; IBA:GO_Central.
DR GO; GO:0007176; P:regulation of epidermal growth factor-activated receptor activity; TAS:ProtInc.
DR GO; GO:0007172; P:signal complex assembly; NAS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0042110; P:T cell activation; NAS:UniProtKB.
DR CDD; cd10409; SH2_Nck2; 1.
DR CDD; cd11899; SH3_Nck2_1; 1.
DR CDD; cd11902; SH3_Nck2_2; 1.
DR CDD; cd11903; SH3_Nck2_3; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR017304; NCK.
DR InterPro; IPR028524; NCK2.
DR InterPro; IPR035883; Nck2_SH2.
DR InterPro; IPR035559; Nck2_SH3_1.
DR InterPro; IPR035560; Nck2_SH3_2.
DR InterPro; IPR035561; Nck2_SH3_3.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR19969:SF12; PTHR19969:SF12; 2.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF00018; SH3_1; 2.
DR Pfam; PF14604; SH3_9; 1.
DR PIRSF; PIRSF037874; Cytoplasmic_NCK; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00326; SH3; 3.
DR SUPFAM; SSF50044; SSF50044; 3.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50002; SH3; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Endoplasmic reticulum;
KW Phosphoprotein; Reference proteome; Repeat; SH2 domain; SH3 domain;
KW Translation regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..380
FT /note="Cytoplasmic protein NCK2"
FT /id="PRO_0000096767"
FT DOMAIN 2..61
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 111..170
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 195..257
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 285..380
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 79..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 92
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55033"
FT MOD_RES 110
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18088087"
FT MUTAGEN 148
FT /note="W->K: Abolishes interaction with DOCK1."
FT /evidence="ECO:0000269|PubMed:11240126"
FT MUTAGEN 234
FT /note="W->K: Abolishes interaction with DOCK1."
FT /evidence="ECO:0000269|PubMed:11240126"
FT CONFLICT 25
FT /note="K -> KV (in Ref. 1; AAC04831)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="P -> A (in Ref. 2; AAC80284)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="E -> Q (in Ref. 1; AAC04831)"
FT /evidence="ECO:0000305"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:2B86"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:2JXB"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:2B86"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:2B86"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:2B86"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:2B86"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:2B86"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:4E6R"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:4E6R"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:4E6R"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:4E6R"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:4E6R"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:4E6R"
FT STRAND 196..204
FT /evidence="ECO:0007829|PDB:1U5S"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:1U5S"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:1U5S"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:1U5S"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:1U5S"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:1U5S"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:1U5S"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:1U5S"
FT HELIX 292..302
FT /evidence="ECO:0007829|PDB:2CIA"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:2CIA"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:2CIA"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:2CIA"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:2CIA"
FT STRAND 331..338
FT /evidence="ECO:0007829|PDB:2CIA"
FT STRAND 341..344
FT /evidence="ECO:0007829|PDB:2CIA"
FT STRAND 347..351
FT /evidence="ECO:0007829|PDB:2CIA"
FT HELIX 352..361
FT /evidence="ECO:0007829|PDB:2CIA"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:2CIA"
FT TURN 368..370
FT /evidence="ECO:0007829|PDB:1Z3K"
SQ SEQUENCE 380 AA; 42915 MW; 3A211085E46F4452 CRC64;
MTEEVIVIAK WDYTAQQDQE LDIKKNERLW LLDDSKTWWR VRNAANRTGY VPSNYVERKN
SLKKGSLVKN LKDTLGLGKT RRKTSARDAS PTPSTDAEYP ANGSGADRIY DLNIPAFVKF
AYVAEREDEL SLVKGSRVTV MEKCSDGWWR GSYNGQIGWF PSNYVLEEVD EAAAESPSFL
SLRKGASLSN GQGSRVLHVV QTLYPFSSVT EEELNFEKGE TMEVIEKPEN DPEWWKCKNA
RGQVGLVPKN YVVVLSDGPA LHPAHAPQIS YTGPSSSGRF AGREWYYGNV TRHQAECALN
ERGVEGDFLI RDSESSPSDF SVSLKASGKN KHFKVQLVDN VYCIGQRRFH TMDELVEHYK
KAPIFTSEHG EKLYLVRALQ
