ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P16333

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name NCK1_HUMAN
Primary accession number P16333
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1990
Sequence was last modified on August 1, 1990 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 105)
Name and origin of the protein
Protein name Cytoplasmic protein NCK1
Synonyms NCK adaptor protein 1
Nck-1
SH2/SH3 adaptor protein NCK-alpha
Gene name
Name: NCK1
Synonyms: NCK
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1093/nar/18.4.1048; PubMed=2107526 [NCBI, ExPASy, EBI, Israel, Japan]
Lehmann J.M., Riethmueller G., Johnson J.P.;
"Nck, a melanoma cDNA encoding a cytoplasmic protein consisting of the src homology units SH2 and SH3.";
Nucleic Acids Res. 18:1048-1048(1990).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[3]
 PHOSPHORYLATION, AND PARTIAL PROTEIN SEQUENCE.
PubMed=1333046 [NCBI, ExPASy, EBI, Israel, Japan]
Park D., Rhee S.G.;
"Phosphorylation of Nck in response to a variety of receptors, phorbol myristate acetate, and cyclic AMP.";
Mol. Cell. Biol. 12:5816-5823(1992).
[4]
 PHOSPHORYLATION.
PubMed=1448108 [NCBI, ExPASy, EBI, Israel, Japan]
Meisenhelder J., Hunter T.;
"The SH2/SH3 domain-containing protein Nck is recognized by certain anti-phospholipase C-gamma 1 monoclonal antibodies, and its phosphorylation on tyrosine is stimulated by platelet-derived growth factor and epidermal growth factor treatment.";
Mol. Cell. Biol. 12:5843-5856(1992).
[5]
 INTERACTION WITH SOCS7.
DOI=10.1006/bbrc.1997.7492; PubMed=9344857 [NCBI, ExPASy, EBI, Israel, Japan]
Matuoka K., Miki H., Takahashi K., Takenawa T.;
"A novel ligand for an SH3 domain of the adaptor protein Nck bears an SH2 domain and nuclear signaling motifs.";
Biochem. Biophys. Res. Commun. 239:488-492(1997).
[6]
 INTERACTION WITH BLNK; GRB2; PLCG1 AND VAV.
DOI=10.1016/S1074-7613(00)80591-9; PubMed=9697839 [NCBI, ExPASy, EBI, Israel, Japan]
Fu C., Turck C.W., Kurosaki T., Chan A.C.;
"BLNK: a central linker protein in B cell activation.";
Immunity 9:93-103(1998).
[7]
 INTERACTION WITH RALGPS1.
DOI=10.1074/jbc.C000085200; PubMed=10747847 [NCBI, ExPASy, EBI, Israel, Japan]
Rebhun J.F., Chen H., Quilliam L.A.;
"Identification and characterization of a new family of guanine nucleotide exchange factors for the ras-related GTPase Ral.";
J. Biol. Chem. 275:13406-13410(2000).
[8]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-105, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1074/mcp.M500089-MCP200; PubMed=15951569 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M.;
"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules.";
Mol. Cell. Proteomics 4:1240-1250(2005).
[9]
 IDENTIFICATION IN COMPLEX WITH PP1 AND PPP1R15B, FUNCTION, AND SUBCELLULAR LOCATION.
DOI=10.1074/jbc.M513556200; PubMed=16835242 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[10]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-96 AND TYR-105, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[11]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-105, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan]
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]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-91 AND SER-96, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
 IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[14]
 STRUCTURE BY NMR OF 99-174.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the SH3 domain of the human cytoplasmic protein NCK1.";
Submitted (NOV-2005) to the PDB data bank.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X17576; CAA35599.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC006403; AAH06403.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00028065; -.
PIR S08636; S08636.
RefSeq NP_006144.1; -.
UniGene Hs.477693
3D structure databases
PDB
2CI8; X-ray; 1.80 A; A=281-377.[ExPASy / RCSB / EBI]
2CI9; X-ray; 1.50 A; A/B=281-377.[ExPASy / RCSB / EBI]
2CUB; NMR; -; A=99-173.[ExPASy / RCSB / EBI]
2JS0; NMR; -; A=107-165.[ExPASy / RCSB / EBI]
2JS2; NMR; -; A=1-61.[ExPASy / RCSB / EBI]
2JW4; NMR; -; A=1-63.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2CI8; -.
2CI9; -.
2CUB; -.
2JS0; -.
2JS2; -.
2JW4; -.
SMR P16333; 190-254.
ModBase P16333.
Protein-protein interaction databases
DIP DIP:639N; -.
IntAct P16333; 164.
PTM databases
PhosphoSite P16333; -.
Enzyme and pathway databases
Pathway_Interaction_DB angiopoietinreceptor_pathway; Angiopoietin receptor Tie2-mediated signaling.
ephbfwdpathway; EPHB forward signaling.
insulin_pathway; Insulin Pathway.
pdgfrbpathway; PDGFR-beta signaling pathway.
met_pathway; Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).
vegfr1_2_pathway; Signaling events mediated by VEGFR1 and VEGFR2.
ret_pathway; Signaling events regulated by Ret tyrosine kinase.
tcrpathway; TCR signaling in naive CD4+ T cells.
vegfr1_pathway; VEGFR1 specific signals.
Organism-specific databases
GeneCards GC03P138063; -.
H-InvDB HIX0003707; -.
HGNC HGNC:7664; NCK1.
GenAtlas NCK1.
HPA CAB005063; -.
MIM 600508; gene. [NCBI / EBI]
PharmGKB PA31466; -.
Gene expression databases
ArrayExpress P16333; -.
Bgee P16333; -.
CleanEx HS_NCK1; -.
GermOnline ENSG00000158092; Homo sapiens.
Ontologies
GO
GO:0005783; Cellular component: endoplasmic reticulum (inferred from electronic annotation from UniProtKB-SubCell).
GO:0008093; Molecular function: cytoskeletal adaptor activity (non-traceable author statement from UniProtKB).
GO:0005102; Molecular function: receptor binding (inferred from physical interaction from UniProtKB).
GO:0030159; Molecular function: receptor signaling complex scaffold activity (non-traceable author statement from UniProtKB).
GO:0030838; Biological process: positive regulation of actin filament polymerization (inferred from mutant phenotype from UniProtKB).
GO:0042102; Biological process: positive regulation of T cell proliferation (inferred from mutant phenotype from UniProtKB).
GO:0006417; Biological process: regulation of translation (inferred from electronic annotation from UniProtKB-KW).
GO:0007172; Biological process: signal complex assembly (non-traceable author statement from UniProtKB).
GO:0042110; Biological process: T cell activation (inferred from mutant phenotype from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR017304; Cytoplasmic_NCK.
IPR000980; SH2.
IPR001452; SH3_domain.
Graphical view of domain structure.
Gene3D G3DSA:3.30.505.10; SH2; 1.
Pfam PF00017; SH2; 1.
PF00018; SH3_1; 3.
Pfam graphical view of domain structure.
PIRSF PIRSF037874; Cytoplasmic_NCK; 1.
PRINTS PR00401; SH2DOMAIN.
ProDom PD000093; SH2; 1.
PD000066; SH3; 3.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00252; SH2; 1.
SM00326; SH3; 3.
SMART graphical view of domain structure.
PROSITE PS50001; SH2; 1.
PS50002; SH3; 3.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas P16333; -.
PRIDE P16333; -.
Genome annotation databases
Ensembl ENSG00000158092; Homo sapiens. [Contig view]
GeneID 4690; -.
KEGG hsa:4690; -.
Phylogenomic databases
HOGENOM P16333; -.
HOVERGEN P16333; -.
OMA P16333; RFAGKEW.
Other
NextBio 18086; -.
PMAP-CutDB P16333; -.
SOURCE NCK1; Homo sapiens.
ProtoNet P16333.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; Direct protein sequencing; Endoplasmic reticulum; Phosphoprotein; Polymorphism; Repeat; SH2 domain; SH3 domain; Translation regulation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   377  377     Cytoplasmic protein NCK1. PRO_0000096766
DOMAIN   2    61  60     SH3 1. 
DOMAIN   115   165  51     SH3 2. 
DOMAIN   190   252  63     SH3 3. 
DOMAIN   282   376  95     SH2. 
MOD_RES   85    85        Phosphoserine. 
MOD_RES   91    91        Phosphoserine. 
MOD_RES   96    96        Phosphoserine. 
MOD_RES   105   105        Phosphotyrosine. 
VARIANT   180   180  1     A -> V (in dbSNP:rs13320485 [NCBI]). VAR_051228 
STRAND   5    11  7      
STRAND   28    33  6      
STRAND   35    42  8      
STRAND   48    51  4      
TURN   53    55  3      
STRAND   56    58  3      
STRAND   99   101  3      
STRAND   109   115  7      
STRAND   131   138  8      
STRAND   142   148  7      
STRAND   151   156  6      
HELIX   157   159  3      
STRAND   160   162  3      
STRAND   168   170  3      
HELIX   289   299  11      
STRAND   305   309  5      
STRAND   311   313  3      
STRAND   316   323  8      
STRAND   326   332  7      
STRAND   339   341  3      
STRAND   344   348  5      
HELIX   349   358  10      
STRAND   361   363  3      
Sequence information
Length: 377 AA [This is the length of the unprocessed precursor] Molecular weight: 42864 Da [This is the MW of the unprocessed precursor] CRC64: 554E9B1A936AEF30 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MAEEVVVVAK FDYVAQQEQE LDIKKNERLW LLDDSKSWWR VRNSMNKTGF VPSNYVERKN 

        70         80         90        100        110        120 
SARKASIVKN LKDTLGIGKV KRKPSVPDSA SPADDSFVDP GERLYDLNMP AYVKFNYMAE 

       130        140        150        160        170        180 
REDELSLIKG TKVIVMEKCS DGWWRGSYNG QVGWFPSNYV TEEGDSPLGD HVGSLSEKLA 

       190        200        210        220        230        240 
AVVNNLNTGQ VLHVVQALYP FSSSNDEELN FEKGDVMDVI EKPENDPEWW KCRKINGMVG 

       250        260        270        280        290        300 
LVPKNYVTVM QNNPLTSGLE PSPPQCDYIR PSLTGKFAGN PWYYGKVTRH QAEMALNERG 

       310        320        330        340        350        360 
HEGDFLIRDS ESSPNDFSVS LKAQGKNKHF KVQLKETVYC IGQRKFSTME ELVEHYKKAP 

       370 
IFTSEQGEKL YLVKHLS
P16333 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ch flag SIB Switzerland Mirror sites: Australia Brazil Canada China Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!