Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P16333 (NCK1_HUMAN)

Last modified February 9, 2010. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Cytoplasmic protein NCK1
Alternative name(s):
    NCK adaptor protein 1
      Short name=Nck-1
    SH2/SH3 adaptor protein NCK-alpha
Gene names
Name: NCK1
Synonyms: NCK
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Protein attributes

Sequence length377 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

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 the DNA damage response, not in the detection of the damage by ATM/ATR, but for efficient activation of downstream effectors, such as that of CHEK2. Ref.11 Ref.12

Subunit structure

Associates with BLNK, PLCG1, VAV1 and NCK1 in a B-cell antigen receptor-dependent fashion. Interacts with SOCS7. This interaction is required for nuclear import. Part of a complex containing PPP1R15B, PP1 and NCK1. Interacts with RALGPS1. Interacts with CAV2 (tyrosine phosphorylated form). Ref.12 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9

Subcellular location

Cytoplasm. Endoplasmic reticulum. Nucleus. Note: Mostly cytoplasmic, but shuttles between the cytoplasm and the nucleus. Import into the nucleus requires the interaction with SOCS7. Predominantly nuclear following genotoxic stresses, such as UV irradiation, hydroxyurea or mitomycin C treatments. Ref.11 Ref.12

Post-translational modification

Phosphorylated on Ser and Tyr residues. Ref.3 Ref.4 Ref.10 Ref.13 Ref.14 Ref.15 Ref.18 Ref.19

Sequence similarities

Contains 1 SH2 domain.

Contains 3 SH3 domains.

Hide | Top

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ABCG5Q9H2221EBI-389883,EBI-1761423
ABI1Q8IZP01EBI-389883,EBI-375446
ABL1P005191EBI-389883,EBI-375543
ABL2P426841EBI-389883,EBI-1102694
ACAP1Q150271EBI-389883,EBI-751746
AFF2P518161EBI-389883,EBI-1754468
AGERQ151091EBI-389883,EBI-1646426
AIREO439181EBI-389883,EBI-1753081
AKAP2Q9Y2D51EBI-389883,EBI-1754555
AKAP6Q130231EBI-389883,EBI-1056102
ANK2Q014841EBI-389883,EBI-941975
APOL5Q9BWW91EBI-389883,EBI-1753592
ARHGEF11O150851EBI-389883,EBI-311099
ASAP1Q9ULH11EBI-389883,EBI-346622
ASAP2O431501EBI-389883,EBI-310968
ASB16Q96NS51EBI-389883,EBI-1751918
ASXL1Q8IXJ91EBI-389883,EBI-1646500
ATP2A3Q930841EBI-389883,EBI-1046185
BAZ2AQ9UIF91EBI-389883,EBI-934890
BRCA1P383981EBI-389883,EBI-349905
BRD4O608851EBI-389883,EBI-723869
BRPF3Q9ULD41EBI-389883,EBI-1753470
C6P136711EBI-389883,EBI-1753221
CASTP208101EBI-389883,EBI-1268770
CCKBRP322391EBI-389883,EBI-1753137
CCR10P460921EBI-389883,EBI-348022
CDC27P302601EBI-389883,EBI-994813
CELSR2Q9HCU41EBI-389883,EBI-724117
CELSR3Q9NYQ71EBI-389883,EBI-308417
CHAF1AQ131111EBI-389883,EBI-1020839
CHRDQ9H2X01EBI-389883,EBI-947551
CKAP5Q140081EBI-389883,EBI-310585
CNTFRP269921EBI-389883,EBI-743758
CNTNAP1P783571EBI-389883,EBI-1751903
COBRA1Q8WX921EBI-389883,EBI-347721
CSDE1O755341EBI-389883,EBI-719186
CSMD2Q7Z4081EBI-389883,EBI-1957312
CYP4F2P783291EBI-389883,EBI-1752413
DAB2P980821EBI-389883,EBI-1171238
DAG1Q141181EBI-389883,EBI-1755945
DLGAP1O144901EBI-389883,EBI-1753207
DLGAP2Q9P1A61EBI-389883,EBI-1753397
DLGAP3O958861EBI-389883,EBI-1752541
DLGAP4Q9Y2H01EBI-389883,EBI-722139
DLX4Q929881EBI-389883,EBI-1752755
DNM1Q051932EBI-389883,EBI-713135
Dnm1P215751EBI-389883,EBI-80070From a different organism.
DOCK1Q141851EBI-389883,EBI-446740
DOCK3Q8IZD91EBI-389883,EBI-1752361
DTNBP1Q96EV81EBI-389883,EBI-465804
DUSP15Q9H1R21EBI-389883,EBI-1752795
ECT2Q9H8V31EBI-389883,EBI-1054039
EFSO432811EBI-389883,EBI-718488
EHMT2Q96KQ71EBI-389883,EBI-744366
ELK3P419701EBI-389883,EBI-1758534
EPS15P425661EBI-389883,EBI-396684
EPXP116781EBI-389883,EBI-1761505
F2RL2O002541EBI-389883,EBI-1751853
FAM110AQ9BQ891EBI-389883,EBI-1752811
FANCAO153601EBI-389883,EBI-81570
FASLGP480231EBI-389883,EBI-495538
FCGR2BP319941EBI-389883,EBI-724784
FCGR2CP319951EBI-389883,EBI-1396036
FLNBO753691EBI-389883,EBI-352089
FLNCQ143151EBI-389883,EBI-489954
FOXH1O755931EBI-389883,EBI-1759806
FYBO151171EBI-389883,EBI-1753267
GABBR1Q9UBS51EBI-389883,EBI-724156
GAD1Q992591EBI-389883,EBI-743184
GHRP109121EBI-389883,EBI-286316
GLTSCR1Q9NZM41EBI-389883,EBI-1754943
GNSP155861EBI-389883,EBI-1752200
GPR45Q9Y5Y31EBI-389883,EBI-1751869
GSTZ1O437081EBI-389883,EBI-748043
HIST1H1EP104121EBI-389883,EBI-358163
HNRNPRO433901EBI-389883,EBI-713419
HOXC8P312731EBI-389883,EBI-1752118
ID4P479281EBI-389883,EBI-1754719
IL3RAP269511EBI-389883,EBI-1757512
ISG20L2Q9H9L31EBI-389883,EBI-751335
JAK2O606741EBI-389883,EBI-518647
KIF13AQ9H1H91EBI-389883,EBI-1759129
KIFC2Q96AC61EBI-389883,EBI-724040
LRRC3Q9BY711EBI-389883,EBI-1761329
MAP4P278161EBI-389883,EBI-715255
MAP4K1Q929181EBI-389883,EBI-881
MAP4K3Q8IVH81EBI-389883,EBI-1758170
MAP4K5Q9Y4K41EBI-389883,EBI-1279
MED14O602441EBI-389883,EBI-394489
MEPEQ9NQ761EBI-389883,EBI-1753293
MYLKQ157461EBI-389883,EBI-968482
MYRIPQ8NFW91EBI-389883,EBI-1759414
NCKAP5O145131EBI-389883,EBI-1752508
NEK8Q86SG61EBI-389883,EBI-1752987
NFASCO948561EBI-389883,EBI-1751948
NKX2-1P436991EBI-389883,EBI-1391923
NOTCH3Q9UM471EBI-389883,EBI-1236377
NPHS1O605002EBI-389883,EBI-996920
NPVFQ9HCQ71EBI-389883,EBI-1753111
NR5A1Q132851EBI-389883,EBI-874629
NXPH3O951571EBI-389883,EBI-1752913
OXTP011781EBI-389883,EBI-1762651
P2RX7Q995721EBI-389883,EBI-1753251
PAX3P237601EBI-389883,EBI-1167564
PAX7P237591EBI-389883,EBI-1042757
PDIA2Q130871EBI-389883,EBI-1752525
PHACTR2O751671EBI-389883,EBI-1754409
PIK3C2BO007501EBI-389883,EBI-641107
PIK3CDO003291EBI-389883,EBI-718309
PNMA2Q9UL421EBI-389883,EBI-302355
POLR1BQ9H9Y61EBI-389883,EBI-355441
PRICKLE3O439001EBI-389883,EBI-1751761
PRXQ9BXM01EBI-389883,EBI-1753064
PTPN4P290741EBI-389883,EBI-710431
RAG1P159181EBI-389883,EBI-1755109
RAPGEF1Q139051EBI-389883,EBI-976876
RIMS1Q86UR51EBI-389883,EBI-1043236
RIMS2Q9UQ261EBI-389883,EBI-1756749
RIN3Q8TB241EBI-389883,EBI-1570523
RNASENQ9NRR41EBI-389883,EBI-528367
RP1L1Q8IWN71EBI-389883,EBI-1757848
RPL13P263731EBI-389883,EBI-356849
RPP38P783451EBI-389883,EBI-366493
RRASP103011EBI-389883,EBI-968703
RYR1P218171EBI-389883,EBI-1221290
SASH1O948851EBI-389883,EBI-1761310
SCARF2Q96GP61EBI-389883,EBI-1752088
SEMA7AO753261EBI-389883,EBI-1753538
SEPN1Q9NZV51EBI-389883,EBI-1751965
SF3B4Q154271EBI-389883,EBI-348469
SHANK2Q9UPX81EBI-389883,EBI-1570571
SHANK3Q9BYB01EBI-389883,EBI-1752330
SHROOM2Q137961EBI-389883,EBI-1644065
SLC22A3O757511EBI-389883,EBI-1752674
SLC23A1Q9UHI71EBI-389883,EBI-1759386
SLC24A1O607211EBI-389883,EBI-1753504
SNX12Q9UMY41EBI-389883,EBI-1752602
SNX17Q150361EBI-389883,EBI-1752620
SNX3O604931EBI-389883,EBI-727209
SNX7Q9UNH61EBI-389883,EBI-751422
SNX8Q9Y5X21EBI-389883,EBI-1752557
SOS1Q078892EBI-389883,EBI-297487
Sos1Q497A51EBI-389883,EBI-922895From a different organism.
SOS2Q078901EBI-389883,EBI-298181
SP1P080471EBI-389883,EBI-298336
SPENQ96T581EBI-389883,EBI-765739
SUV39H2Q9H5I11EBI-389883,EBI-723127
SYNJ2O150561EBI-389883,EBI-310513
TGDSO954551EBI-389883,EBI-1761487
TGOLN2O434931EBI-389883,EBI-1752146
TLR9Q9NR961EBI-389883,EBI-1762509
TMPOP421671EBI-389883,EBI-455283
TNIKQ9UKE51EBI-389883,EBI-1051794
TPSAB1P151571EBI-389883,EBI-1762849
TPSAB1Q156611EBI-389883,EBI-1761369
TPSB2P202311EBI-389883,EBI-1761383
TPX2Q9ULW01EBI-389883,EBI-1037322
TRAIPQ9BWF21EBI-389883,EBI-1756205
TRIM39Q9HCM91EBI-389883,EBI-739510
TULP1O002941EBI-389883,EBI-1756778
URB1O602871EBI-389883,EBI-1762349
VPS13AQ96RL71EBI-389883,EBI-1752583
WASLO004011EBI-389883,EBI-957615
WBP7Q9UMN61EBI-389883,EBI-765774
WIPF1O435162EBI-389883,EBI-346356

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 377376Cytoplasmic protein NCK1
PRO_0000096766

Regions

Domain2 – 6160SH3 1
Domain115 – 16551SH3 2
Domain190 – 25263SH3 3
Domain282 – 37695SH2

Amino acid modifications

Modified residue21N-acetylalanine Ref.17
Modified residue851Phosphoserine Ref.13 Ref.15 Ref.19
Modified residue911Phosphoserine Ref.15
Modified residue961Phosphoserine Ref.13 Ref.15 Ref.19
Modified residue1051Phosphotyrosine Ref.10 Ref.13 Ref.14 Ref.18 Ref.19

Natural variations

Natural variant1801A → V: dbSNP rs13320485.
VAR_051228

Secondary structure

1 ........................................... 377
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P16333-1 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 554E9B1A936AEF30

FASTA37742,864
        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

« Hide

Hide | Top

References

« Hide 'large scale' references
[1]"Nck, a melanoma cDNA encoding a cytoplasmic protein consisting of the src homology units SH2 and SH3."
Lehmann J.M., Riethmueller G., Johnson J.P.
Nucleic Acids Res. 18:1048-1048(1990) [PubMed: 2107526] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Uterus.
[3]"Phosphorylation of Nck in response to a variety of receptors, phorbol myristate acetate, and cyclic AMP."
Park D., Rhee S.G.
Mol. Cell. Biol. 12:5816-5823(1992) [PubMed: 1333046] [Abstract]
Cited for: PHOSPHORYLATION, PARTIAL PROTEIN SEQUENCE.
[4]"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."
Meisenhelder J., Hunter T.
Mol. Cell. Biol. 12:5843-5856(1992) [PubMed: 1448108] [Abstract]
Cited for: PHOSPHORYLATION.
[5]"A novel ligand for an SH3 domain of the adaptor protein Nck bears an SH2 domain and nuclear signaling motifs."
Matuoka K., Miki H., Takahashi K., Takenawa T.
Biochem. Biophys. Res. Commun. 239:488-492(1997) [PubMed: 9344857] [Abstract]
Cited for: INTERACTION WITH SOCS7.
[6]"BLNK: a central linker protein in B cell activation."
Fu C., Turck C.W., Kurosaki T., Chan A.C.
Immunity 9:93-103(1998) [PubMed: 9697839] [Abstract]
Cited for: INTERACTION WITH BLNK; GRB2; PLCG1 AND VAV.
[7]"Identification and characterization of a new family of guanine nucleotide exchange factors for the ras-related GTPase Ral."
Rebhun J.F., Chen H., Quilliam L.A.
J. Biol. Chem. 275:13406-13410(2000) [PubMed: 10747847] [Abstract]
Cited for: INTERACTION WITH RALGPS1.
[8]"Src-induced phosphorylation of caveolin-2 on tyrosine 19. Phospho-caveolin-2 (Tyr(P)19) is localized near focal adhesions, remains associated with lipid rafts/caveolae, but no longer forms a high molecular mass hetero-oligomer with caveolin-1."
Lee H., Park D.S., Wang X.B., Scherer P.E., Schwartz P.E., Lisanti M.P.
J. Biol. Chem. 277:34556-34567(2002) [PubMed: 12091389] [Abstract]
Cited for: INTERACTION WITH CAV2.
[9]"Tyrosine phosphorylation of caveolin-2 at residue 27: differences in the spatial and temporal behavior of phospho-Cav-2 (pY19 and pY27)."
Wang X.B., Lee H., Capozza F., Marmon S., Sotgia F., Brooks J.W., Campos-Gonzalez R., Lisanti M.P.
Biochemistry 43:13694-13706(2004) [PubMed: 15504032] [Abstract]
Cited for: INTERACTION WITH CAV2.
[10]"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules."
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M.
Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed: 15951569] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-105, MASS SPECTROMETRY.
Tissue: Epithelium.
[11]"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."
Latreille M., Larose L.
J. Biol. Chem. 281:26633-26644(2006) [PubMed: 16835242] [Abstract]
Cited for: IDENTIFICATION IN COMPLEX WITH PP1 AND PPP1R15B, FUNCTION, SUBCELLULAR LOCATION.
[12]"Septins regulate actin organization and cell-cycle arrest through nuclear accumulation of NCK mediated by SOCS7."
Kremer B.E., Adang L.A., Macara I.G.
Cell 130:837-850(2007) [PubMed: 17803907] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SOCS7.
[13]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-96 AND TYR-105, MASS SPECTROMETRY.
[14]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-105, MASS SPECTROMETRY.
Tissue: Platelet.
[15]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-91 AND SER-96, MASS SPECTROMETRY.
[16]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[17]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY.
[18]"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells."
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J.
J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-105, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[19]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-96 AND TYR-105, MASS SPECTROMETRY.
Tissue: T-cell.
[20]"Solution structure of the SH3 domain of the human cytoplasmic protein NCK1."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 99-174.
+Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X17576 mRNA. Translation: CAA35599.1.
BC006403 mRNA. Translation: AAH06403.1.
IPIIPI00028065.
PIRS08636.
RefSeqNP_006144.1.
UniGeneHs.477693

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CI8X-ray1.80A281-377[»]
2CI9X-ray1.50A/B281-377[»]
2CUBNMR-A99-173[»]
2JS0NMR-A107-165[»]
2JS2NMR-A1-61[»]
2JW4NMR-A1-63[»]
SMRP16333. Positions 7-165, 112-251, 190-254, 194-360.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-639N.
IntActP16333. 165 interactions.
STRINGP16333.

PTM databases

PhosphoSiteP16333.

Proteomic databases

PeptideAtlasP16333.
PRIDEP16333.

Genome annotation databases

EnsemblENST00000288986; ENSP00000288986; ENSG00000158092; Homo sapiens. [Genome view]
ENST00000481752; ENSP00000417273; ENSG00000158092; Homo sapiens. [Genome view]
GeneID4690.
KEGGhsa:4690.
UCSCuc003erh.1. human.

Organism-specific databases

CTD4690.
GeneCardsGC03P138063.
H-InvDBHIX0003707.
HGNCHGNC:7664. NCK1.
HPACAB005063.
MIM600508. gene.
PharmGKBPA31466.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG16125.
HOGENOMHBG387920.
HOVERGENP16333.
InParanoidP16333.
OMANERGNEG.
OrthoDBEOG980MFS.
PhylomeDBP16333.

Enzyme and pathway databases

Pathway_Interaction_DBangiopoietinreceptor_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.
ReactomeREACT_16888. Signaling by PDGF.
REACT_18266. Axon guidance.
REACT_6900. Signaling in Immune system.

Gene expression databases

ArrayExpressP16333.
BgeeP16333.
CleanExHS_NCK1.
GenevestigatorP16333.
GermOnlineENSG00000158092. Homo sapiens.

Family and domain databases

InterProIPR017304. Cytoplasmic_NCK.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR020473. SH3_region.
[Graphical view]
Gene3DG3DSA:3.30.505.10. SH2. 1 hit.
PfamPF00017. SH2. 1 hit.
PF00018. SH3_1. 3 hits.
[Graphical view]
PIRSFPIRSF037874. Cytoplasmic_NCK. 1 hit.
PRINTSPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
SMARTSM00252. SH2. 1 hit.
SM00326. SH3. 3 hits.
[Graphical view]
PROSITEPS50001. SH2. 1 hit.
PS50002. SH3. 3 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio18086.
PMAP-CutDBP16333.
SOURCESearch...

Hide | Top

Entry information

Entry nameNCK1_HUMAN
AccessionPrimary (citable) accession number: P16333
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: February 9, 2010
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Hide | Top

Relevant documents

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Forthcoming format changes

Announcement of forthcoming format changes

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents