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Cytoplasmic protein NCK2 (Growth factor receptor-bound protein 4) (NCK adaptor protein 2) (Nck-2) (SH2/SH3 adaptor protein NCK-beta)

 NCK2_HUMAN              Reviewed;         380 AA.
O43639; D3DVK1; Q9BWN9; Q9UIC3;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
10-MAY-2002, sequence version 2.
22-NOV-2017, entry version 180.
RecName: Full=Cytoplasmic protein NCK2;
AltName: Full=Growth factor receptor-bound protein 4;
AltName: Full=NCK adaptor protein 2;
Short=Nck-2;
AltName: Full=SH2/SH3 adaptor protein NCK-beta;
Name=NCK2; Synonyms=GRB4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9737977; DOI=10.1074/jbc.273.39.25171;
Chen M., She H., Davis E.M., Spicer C.M., Kim L., Ren R., LeBeau M.M.,
Li W.;
"Identification of Nck family genes, chromosomal localization,
expression, and signaling specificity.";
J. Biol. Chem. 273:25171-25178(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH LIMS1.
TISSUE=Lung;
PubMed=9843575; DOI=10.1091/mbc.9.12.3367;
Tu Y., Li F., Wu C.;
"Nck-2, a novel Src homology2/3-containing adaptor protein that
interacts with the LIM-only protein PINCH and components of growth
factor receptor kinase-signaling pathways.";
Mol. Biol. Cell 9:3367-3382(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, INTERACTION WITH EGFR; PAK1; PKN2 AND SOS1, AND
PHOSPHORYLATION.
PubMed=10026169; DOI=10.1074/jbc.274.9.5542;
Braverman L.E., Quilliam L.A.;
"Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-
containing adapter protein having similar binding and biological
properties to Nck.";
J. Biol. Chem. 274:5542-5549(1999).
[6]
INTERACTION WITH TGFB1I1.
PubMed=10330411; DOI=10.1083/jcb.145.4.851;
Turner C.E., Brown M.C., Perrotta J.A., Riedy M.C., Nikolopoulos S.N.,
McDonald A.R., Bagrodia S., Thomas S.M., Leventhal P.S.;
"Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin
repeat, ARF-GAP protein: a role in cytoskeletal remodeling.";
J. Cell Biol. 145:851-863(1999).
[7]
INTERACTION WITH DOCK1, AND MUTAGENESIS OF TRP-148 AND TRP-234.
PubMed=11240126; DOI=10.1016/S0014-5793(01)02195-0;
Tu Y., Kucik D.F., Wu C.;
"Identification and kinetic analysis of the interaction between Nck-2
and DOCK180.";
FEBS Lett. 491:193-199(2001).
[8]
INTERACTION WITH AXL.
PubMed=12470648; DOI=10.1016/S0006-291X(02)02718-3;
Hafizi S., Alindri F., Karlsson R., Dahlbaeck B.;
"Interaction of Axl receptor tyrosine kinase with C1-TEN, a novel C1
domain-containing protein with homology to tensin.";
Biochem. Biophys. Res. Commun. 299:793-800(2002).
[9]
INTERACTION WITH DDR1.
PubMed=16337946; DOI=10.1016/j.febslet.2005.11.035;
Koo D.H., McFadden C., Huang Y., Abdulhussein R., Friese-Hamim M.,
Vogel W.F.;
"Pinpointing phosphotyrosine-dependent interactions downstream of the
collagen receptor DDR1.";
FEBS Lett. 580:15-22(2006).
[10]
IDENTIFICATION IN COMPLEX WITH PP1 AND PPP1R15B, FUNCTION, AND
SUBCELLULAR LOCATION.
PubMed=16835242; DOI=10.1074/jbc.M513556200;
Latreille M., Larose L.;
"Nck in a complex containing the catalytic subunit of protein
phosphatase 1 regulates eukaryotic initiation factor 2alpha signaling
and cell survival to endoplasmic reticulum stress.";
J. Biol. Chem. 281:26633-26644(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-110, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[12]
INTERACTION WITH FASLG.
PubMed=19807924; DOI=10.1186/1471-2172-10-53;
Voss M., Lettau M., Janssen O.;
"Identification of SH3 domain interaction partners of human FasL
(CD178) by phage display screening.";
BMC Immunol. 10:53-53(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90 AND THR-92, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
STRUCTURE BY NMR OF 188-265.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the SH3 domain of the human cytoplasmic protein
NCK2.";
Submitted (JUL-2005) to the PDB data bank.
-!- FUNCTION: Adapter protein which associates with tyrosine-
phosphorylated growth factor receptors or their cellular
substrates. Maintains low levels of EIF2S1 phosphorylation by
promoting its dephosphorylation by PP1. Plays a role in ELK1-
dependent transcriptional activation in response to activated Ras
signaling. {ECO:0000269|PubMed:10026169,
ECO:0000269|PubMed:16835242}.
-!- SUBUNIT: Interacts with DOCK1, LIMS1 and TGFB1I1. Part of a
complex containing PPP1R15B, PP1 and NCK2. Interacts with FASLG
(By similarity). Interacts with AXL. Interacts with PAK1, PKN2 and
SOS1. Interacts (via SH2 domain) with EGFR. Interacts (via SH2
domain) with DDR1. {ECO:0000250, ECO:0000269|PubMed:10026169,
ECO:0000269|PubMed:10330411, ECO:0000269|PubMed:11240126,
ECO:0000269|PubMed:12470648, ECO:0000269|PubMed:16337946,
ECO:0000269|PubMed:16835242, ECO:0000269|PubMed:19807924,
ECO:0000269|PubMed:9843575}.
-!- INTERACTION:
Q9NYB9:ABI2; NbExp=4; IntAct=EBI-713635, EBI-743598;
Q9P2A4:ABI3; NbExp=5; IntAct=EBI-713635, EBI-742038;
A7KAX9:ARHGAP32; NbExp=3; IntAct=EBI-713635, EBI-308663;
Q9H165-2:BCL11A; NbExp=5; IntAct=EBI-713635, EBI-10183342;
Q53FE4:C4orf17; NbExp=4; IntAct=EBI-713635, EBI-715110;
Q13191:CBLB; NbExp=4; IntAct=EBI-713635, EBI-744027;
P15882:CHN1; NbExp=11; IntAct=EBI-713635, EBI-718947;
P52757:CHN2; NbExp=6; IntAct=EBI-713635, EBI-714925;
Q8N684:CPSF7; NbExp=4; IntAct=EBI-713635, EBI-746909;
Q08345:DDR1; NbExp=3; IntAct=EBI-713635, EBI-711879;
Q9Y2H0-1:DLGAP4; NbExp=4; IntAct=EBI-713635, EBI-12000556;
Q14919:DRAP1; NbExp=3; IntAct=EBI-713635, EBI-712941;
Q86TH3:DVL1; NbExp=3; IntAct=EBI-713635, EBI-10185025;
Q5JST6:EFHC2; NbExp=3; IntAct=EBI-713635, EBI-2349927;
P52799:EFNB2; NbExp=7; IntAct=EBI-713635, EBI-7532268;
Q6IB98:EIF3S3; NbExp=3; IntAct=EBI-713635, EBI-10184995;
P04626:ERBB2; NbExp=2; IntAct=EBI-713635, EBI-641062;
P21860:ERBB3; NbExp=2; IntAct=EBI-713635, EBI-720706;
Q9NYF3:FAM53C; NbExp=5; IntAct=EBI-713635, EBI-1644252;
P48023:FASLG; NbExp=3; IntAct=EBI-713635, EBI-495538;
Q96LA5:FCRL2; NbExp=3; IntAct=EBI-713635, EBI-10185081;
O15117:FYB; NbExp=3; IntAct=EBI-713635, EBI-1753267;
Q13480:GAB1; NbExp=5; IntAct=EBI-713635, EBI-517684;
Q8IX15-3:HOMEZ; NbExp=3; IntAct=EBI-713635, EBI-10172004;
P09017:HOXC4; NbExp=4; IntAct=EBI-713635, EBI-3923226;
Q86TF7:HOXC4; NbExp=3; IntAct=EBI-713635, EBI-10185009;
P10721:KIT; NbExp=2; IntAct=EBI-713635, EBI-1379503;
Q13094:LCP2; NbExp=6; IntAct=EBI-713635, EBI-346946;
P48059:LIMS1; NbExp=2; IntAct=EBI-713635, EBI-306928;
Q8TBB1:LNX1; NbExp=3; IntAct=EBI-713635, EBI-739832;
A6PVS8:LRRIQ3; NbExp=3; IntAct=EBI-713635, EBI-10184751;
Q9BRK4:LZTS2; NbExp=3; IntAct=EBI-713635, EBI-741037;
P43360:MAGEA6; NbExp=7; IntAct=EBI-713635, EBI-1045155;
P50222:MEOX2; NbExp=3; IntAct=EBI-713635, EBI-748397;
P08581:MET; NbExp=2; IntAct=EBI-713635, EBI-1039152;
Q99743:NPAS2; NbExp=4; IntAct=EBI-713635, EBI-3932727;
Q13285:NR5A1; NbExp=3; IntAct=EBI-713635, EBI-874629;
Q13153:PAK1; NbExp=6; IntAct=EBI-713635, EBI-1307;
P86479:PRR20C; NbExp=3; IntAct=EBI-713635, EBI-10172814;
Q02833:RASSF7; NbExp=3; IntAct=EBI-713635, EBI-929013;
Q5T8P6:RBM26; NbExp=3; IntAct=EBI-713635, EBI-3232077;
Q04864:REL; NbExp=3; IntAct=EBI-713635, EBI-307352;
Q7L0Q8:RHOU; NbExp=6; IntAct=EBI-713635, EBI-1638043;
Q96L33:RHOV; NbExp=4; IntAct=EBI-713635, EBI-8538631;
Q9NQC3:RTN4; NbExp=2; IntAct=EBI-713635, EBI-715945;
Q15427:SF3B4; NbExp=6; IntAct=EBI-713635, EBI-348469;
O14512:SOCS7; NbExp=4; IntAct=EBI-713635, EBI-1539606;
O94875:SORBS2; NbExp=3; IntAct=EBI-713635, EBI-311323;
O43597:SPRY2; NbExp=3; IntAct=EBI-713635, EBI-742487;
P15884:TCF4; NbExp=3; IntAct=EBI-713635, EBI-533224;
A1L306:TNR; NbExp=3; IntAct=EBI-713635, EBI-10182881;
P14373:TRIM27; NbExp=5; IntAct=EBI-713635, EBI-719493;
Q8WV44:TRIM41; NbExp=5; IntAct=EBI-713635, EBI-725997;
Q15654:TRIP6; NbExp=6; IntAct=EBI-713635, EBI-742327;
P0CG48:UBC; NbExp=2; IntAct=EBI-713635, EBI-3390054;
Q5ST30-4:VARS2; NbExp=3; IntAct=EBI-713635, EBI-10244997;
Q9H9H4:VPS37B; NbExp=5; IntAct=EBI-713635, EBI-4400866;
P42768:WAS; NbExp=3; IntAct=EBI-713635, EBI-346375;
O00401:WASL; NbExp=3; IntAct=EBI-713635, EBI-957615;
O15156:ZBTB7B; NbExp=3; IntAct=EBI-713635, EBI-740434;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16835242}.
Endoplasmic reticulum {ECO:0000269|PubMed:16835242}.
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- PTM: Phosphorylated. {ECO:0000269|PubMed:10026169}.
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EMBL; AF043119; AAC04831.1; -; mRNA.
EMBL; AF047487; AAC80284.1; -; mRNA.
EMBL; CH471127; EAX01753.1; -; Genomic_DNA.
EMBL; CH471127; EAX01754.1; -; Genomic_DNA.
EMBL; BC000103; AAH00103.1; -; mRNA.
EMBL; BC007195; AAH07195.1; -; mRNA.
CCDS; CCDS33266.1; -.
RefSeq; NP_001004720.1; NM_001004720.2.
RefSeq; NP_003572.2; NM_003581.4.
RefSeq; XP_006712860.1; XM_006712797.3.
RefSeq; XP_011510293.1; XM_011511991.2.
RefSeq; XP_016860592.1; XM_017005103.1.
RefSeq; XP_016860593.1; XM_017005104.1.
RefSeq; XP_016860594.1; XM_017005105.1.
UniGene; Hs.529244; -.
UniGene; Hs.735723; -.
PDB; 1U5S; NMR; -; A=192-262.
PDB; 1WX6; NMR; -; A=188-265.
PDB; 1Z3K; NMR; -; A=283-380.
PDB; 2B86; NMR; -; A=1-59.
PDB; 2CIA; X-ray; 1.45 A; A=284-380.
PDB; 2FRW; NMR; -; A=114-170.
PDB; 2FRY; NMR; -; A=198-256.
PDB; 2JXB; NMR; -; A=1-59.
PDB; 4E6R; X-ray; 2.20 A; A/B=114-170.
PDBsum; 1U5S; -.
PDBsum; 1WX6; -.
PDBsum; 1Z3K; -.
PDBsum; 2B86; -.
PDBsum; 2CIA; -.
PDBsum; 2FRW; -.
PDBsum; 2FRY; -.
PDBsum; 2JXB; -.
PDBsum; 4E6R; -.
ProteinModelPortal; O43639; -.
SMR; O43639; -.
BioGrid; 114020; 134.
IntAct; O43639; 131.
MINT; MINT-190960; -.
STRING; 9606.ENSP00000233154; -.
iPTMnet; O43639; -.
PhosphoSitePlus; O43639; -.
BioMuta; NCK2; -.
EPD; O43639; -.
MaxQB; O43639; -.
PaxDb; O43639; -.
PeptideAtlas; O43639; -.
PRIDE; O43639; -.
Ensembl; ENST00000233154; ENSP00000233154; ENSG00000071051.
Ensembl; ENST00000393349; ENSP00000377018; ENSG00000071051.
GeneID; 8440; -.
KEGG; hsa:8440; -.
UCSC; uc002tdg.4; human.
CTD; 8440; -.
DisGeNET; 8440; -.
EuPathDB; HostDB:ENSG00000071051.13; -.
GeneCards; NCK2; -.
HGNC; HGNC:7665; NCK2.
HPA; CAB016116; -.
HPA; HPA031004; -.
MIM; 604930; gene.
neXtProt; NX_O43639; -.
OpenTargets; ENSG00000071051; -.
PharmGKB; PA31467; -.
eggNOG; KOG4226; Eukaryota.
eggNOG; ENOG410XRPF; LUCA.
GeneTree; ENSGT00820000126999; -.
HOGENOM; HOG000290684; -.
HOVERGEN; HBG000719; -.
InParanoid; O43639; -.
KO; K19862; -.
OMA; QSMAGNM; -.
OrthoDB; EOG091G0AD0; -.
PhylomeDB; O43639; -.
TreeFam; TF351631; -.
Reactome; R-HSA-186763; Downstream signal transduction.
Reactome; R-HSA-373753; Nephrin family interactions.
Reactome; R-HSA-3928664; Ephrin signaling.
Reactome; R-HSA-428540; Activation of RAC1.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-8985801; Regulation of cortical dendrite branching.
SignaLink; O43639; -.
SIGNOR; O43639; -.
ChiTaRS; NCK2; human.
EvolutionaryTrace; O43639; -.
GeneWiki; NCK2; -.
GenomeRNAi; 8440; -.
PRO; PR:O43639; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000071051; -.
CleanEx; HS_NCK2; -.
ExpressionAtlas; O43639; baseline and differential.
Genevisible; O43639; HS.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
GO; GO:0012506; C:vesicle membrane; IEA:Ensembl.
GO; GO:0008093; F:cytoskeletal adaptor activity; NAS:UniProtKB.
GO; GO:0001784; F:phosphotyrosine residue binding; IPI:CAFA.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0030159; F:receptor signaling complex scaffold activity; NAS:UniProtKB.
GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
GO; GO:0005070; F:SH3/SH2 adaptor activity; NAS:ParkinsonsUK-UCL.
GO; GO:0007015; P:actin filament organization; IEA:Ensembl.
GO; GO:0016477; P:cell migration; IEA:Ensembl.
GO; GO:0060996; P:dendritic spine development; IEA:Ensembl.
GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:ProtInc.
GO; GO:0001771; P:immunological synapse formation; IEA:Ensembl.
GO; GO:0030032; P:lamellipodium assembly; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
GO; GO:1903912; P:negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:1903898; P:negative regulation of PERK-mediated unfolded protein response; IEA:Ensembl.
GO; GO:1990441; P:negative regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; IEA:Ensembl.
GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:UniProtKB.
GO; GO:1902237; P:positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0036493; P:positive regulation of translation in response to endoplasmic reticulum stress; IEA:Ensembl.
GO; GO:0007176; P:regulation of epidermal growth factor-activated receptor activity; TAS:ProtInc.
GO; GO:0007172; P:signal complex assembly; NAS:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0042110; P:T cell activation; NAS:UniProtKB.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
CDD; cd10409; SH2_Nck2; 1.
CDD; cd11899; SH3_Nck2_1; 1.
CDD; cd11902; SH3_Nck2_2; 1.
CDD; cd11903; SH3_Nck2_3; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR017304; NCK.
InterPro; IPR035883; Nck2_SH2.
InterPro; IPR035559; Nck2_SH3_1.
InterPro; IPR035560; Nck2_SH3_2.
InterPro; IPR035561; Nck2_SH3_3.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
Pfam; PF00017; SH2; 1.
Pfam; PF00018; SH3_1; 2.
Pfam; PF14604; SH3_9; 1.
PIRSF; PIRSF037874; Cytoplasmic_NCK; 1.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00452; SH3DOMAIN.
SMART; SM00252; SH2; 1.
SMART; SM00326; SH3; 3.
SUPFAM; SSF50044; SSF50044; 3.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS50001; SH2; 1.
PROSITE; PS50002; SH3; 3.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Endoplasmic reticulum; Phosphoprotein; Reference proteome; Repeat;
SH2 domain; SH3 domain; Translation regulation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 380 Cytoplasmic protein NCK2.
/FTId=PRO_0000096767.
DOMAIN 2 61 SH3 1. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 111 170 SH3 2. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 195 257 SH3 3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 285 380 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
MOD_RES 2 2 N-acetylthreonine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 90 90 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 92 92 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 94 94 Phosphoserine.
{ECO:0000250|UniProtKB:O55033}.
MOD_RES 110 110 Phosphotyrosine.
{ECO:0000244|PubMed:18088087}.
MUTAGEN 148 148 W->K: Abolishes interaction with DOCK1.
{ECO:0000269|PubMed:11240126}.
MUTAGEN 234 234 W->K: Abolishes interaction with DOCK1.
{ECO:0000269|PubMed:11240126}.
CONFLICT 25 25 K -> KV (in Ref. 1; AAC04831).
{ECO:0000305}.
CONFLICT 100 100 P -> A (in Ref. 2; AAC80284).
{ECO:0000305}.
CONFLICT 296 296 E -> Q (in Ref. 1; AAC04831).
{ECO:0000305}.
STRAND 5 11 {ECO:0000244|PDB:2B86}.
STRAND 17 20 {ECO:0000244|PDB:2JXB}.
STRAND 28 33 {ECO:0000244|PDB:2B86}.
STRAND 35 38 {ECO:0000244|PDB:2B86}.
STRAND 40 42 {ECO:0000244|PDB:2B86}.
STRAND 48 50 {ECO:0000244|PDB:2B86}.
STRAND 55 58 {ECO:0000244|PDB:2B86}.
STRAND 115 118 {ECO:0000244|PDB:4E6R}.
STRAND 137 142 {ECO:0000244|PDB:4E6R}.
STRAND 147 153 {ECO:0000244|PDB:4E6R}.
STRAND 156 161 {ECO:0000244|PDB:4E6R}.
HELIX 162 164 {ECO:0000244|PDB:4E6R}.
STRAND 165 167 {ECO:0000244|PDB:4E6R}.
STRAND 196 204 {ECO:0000244|PDB:1U5S}.
STRAND 210 213 {ECO:0000244|PDB:1U5S}.
STRAND 222 226 {ECO:0000244|PDB:1U5S}.
TURN 230 232 {ECO:0000244|PDB:1U5S}.
STRAND 234 239 {ECO:0000244|PDB:1U5S}.
TURN 240 242 {ECO:0000244|PDB:1U5S}.
STRAND 243 248 {ECO:0000244|PDB:1U5S}.
STRAND 251 254 {ECO:0000244|PDB:1U5S}.
HELIX 292 302 {ECO:0000244|PDB:2CIA}.
STRAND 307 312 {ECO:0000244|PDB:2CIA}.
STRAND 314 316 {ECO:0000244|PDB:2CIA}.
STRAND 320 324 {ECO:0000244|PDB:2CIA}.
STRAND 327 329 {ECO:0000244|PDB:2CIA}.
STRAND 331 338 {ECO:0000244|PDB:2CIA}.
STRAND 341 344 {ECO:0000244|PDB:2CIA}.
STRAND 347 351 {ECO:0000244|PDB:2CIA}.
HELIX 352 361 {ECO:0000244|PDB:2CIA}.
STRAND 364 366 {ECO:0000244|PDB:2CIA}.
TURN 368 370 {ECO:0000244|PDB:1Z3K}.
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


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