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P16333 (NCK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

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

General annotation (Comments)

Function

Adapter protein which associates with tyrosine-phosphorylated growth factor receptors, such as KDR and PDGFRB, 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. Plays a role in ELK1-dependent transcriptional activation in response to activated Ras signaling. Modulates the activation of EIF2AK2/PKR by dsRNA. May play a role in cell adhesion and migration through interaction with ephrin receptors. Ref.12 Ref.13 Ref.19 Ref.21 Ref.22 Ref.33

Subunit structure

Interacts (via SH2 domain and SH3 domain 2) with EGFR. Interacts with PAK1 and SOS1. Interacts (via SH3 domains) with PKN2. 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). Interacts with ADAM15. Interacts with FASLG. Directly interacts with RASA1. Interacts with isoform 4of MINK1. Interacts with FLT1 (tyrosine phosphorylated). Interacts with KDR (tyrosine phosphorylated). Interacts (via SH2 domain) with EPHB1; activates the JUN cascade to regulate cell adhesion. Interacts with EPHA2. Interacts (via SH2 domain) with PDGFRB (tyrosine phosphorylated). Interacts with the inactive form of EIF2AK2/PKR. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.22 Ref.24 Ref.26 Ref.30 Ref.33 Ref.35

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.19 Ref.21

Domain

Only the first and third SH3 domains seem to be involved in RASA1-binding; the second SH3 domain and the SH2 domains do not seeem to be involved.

Post-translational modification

Phosphorylated on Ser and Tyr residues. Phosphorylated in response to activation of EGFR and FcERI. Phosphorylated by activated PDGFRB. Ref.6 Ref.7 Ref.8 Ref.13 Ref.22

Sequence similarities

Contains 1 SH2 domain.

Contains 3 SH3 domains.

Ontologies

Keywords
   Biological processTranslation regulation
   Cellular componentCytoplasm
Endoplasmic reticulum
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
SH2 domain
SH3 domain
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processFc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

T cell activation

Inferred from mutant phenotype PubMed 12110186. Source: UniProtKB

T cell receptor signaling pathway

Traceable author statement. Source: Reactome

actin filament organization

Inferred from electronic annotation. Source: Ensembl

axon guidance

Traceable author statement. Source: Reactome

cell migration

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

lamellipodium assembly

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell death

Inferred from direct assay Ref.22. Source: UniProtKB

negative regulation of protein kinase activity

Inferred from direct assay Ref.22. Source: GOC

positive regulation of T cell proliferation

Inferred from mutant phenotype PubMed 12110186. Source: UniProtKB

positive regulation of actin filament polymerization

Inferred from mutant phenotype PubMed 12110186. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.13. Source: UniProtKB

regulation of translation

Inferred from electronic annotation. Source: UniProtKB-KW

response to other organism

Inferred from electronic annotation. Source: Ensembl

signal complex assembly

Non-traceable author statement PubMed 12110186. Source: UniProtKB

   Cellular_componentcytoplasm

Non-traceable author statement PubMed 12110186. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

endoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Traceable author statement. Source: Reactome

vesicle membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncytoskeletal adaptor activity

Non-traceable author statement PubMed 12110186. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.13PubMed 10521462Ref.17Ref.22. Source: UniProtKB

protein kinase inhibitor activity

Inferred from direct assay Ref.22. Source: UniProtKB

receptor binding

Inferred from physical interaction PubMed 12110186. Source: UniProtKB

receptor signaling complex scaffold activity

Non-traceable author statement PubMed 12110186. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ABCG5Q9H2222EBI-389883,EBI-1761423
ABL1P005192EBI-389883,EBI-375543
ABL2P426843EBI-389883,EBI-1102694
AGERQ151092EBI-389883,EBI-1646426
AIREO439182EBI-389883,EBI-1753081
ARHGEF11O150853EBI-389883,EBI-311099
ASAP1Q9ULH16EBI-389883,EBI-346622
ASB16Q96NS52EBI-389883,EBI-1751918
BAZ2AQ9UIF92EBI-389883,EBI-934890
BRD4O608852EBI-389883,EBI-723869
BRPF3Q9ULD43EBI-389883,EBI-1753470
C6P136712EBI-389883,EBI-1753221
CASTP208102EBI-389883,EBI-1268770
CD247P209632EBI-389883,EBI-1165705
CD3EP077666EBI-389883,EBI-1211297
CDC27P302603EBI-389883,EBI-994813
CELSR3Q9NYQ72EBI-389883,EBI-308417
CHAF1AQ131112EBI-389883,EBI-1020839
CKAP5Q140083EBI-389883,EBI-310585
CNTNAP1P783572EBI-389883,EBI-1751903
CYP4F2P783292EBI-389883,EBI-1752413
DAB2P980822EBI-389883,EBI-1171238
DAG1Q141182EBI-389883,EBI-1755945
DLGAP1O144904EBI-389883,EBI-1753207
DLGAP2Q9P1A64EBI-389883,EBI-1753397
DLGAP3O958862EBI-389883,EBI-1752541
DLGAP4Q9Y2H05EBI-389883,EBI-722139
DLX4Q929883EBI-389883,EBI-1752755
DNM1Q051932EBI-389883,EBI-713135
DOCK3Q8IZD93EBI-389883,EBI-1752361
DUSP15Q9H1R22EBI-389883,EBI-1752795
ECT2Q9H8V33EBI-389883,EBI-1054039
ELK3P419703EBI-389883,EBI-1758534
EPS15P425662EBI-389883,EBI-396684
F2RL2O002542EBI-389883,EBI-1751853
FAM110AQ9BQ892EBI-389883,EBI-1752811
FCGR2BP319942EBI-389883,EBI-724784
FCGR2CP319952EBI-389883,EBI-1396036
FLNBO753693EBI-389883,EBI-352089
FOXH1O755932EBI-389883,EBI-1759806
FYBO151173EBI-389883,EBI-1753267
GAB1Q134803EBI-389883,EBI-517684
GABBR1Q9UBS53EBI-389883,EBI-724156
GAD1Q992592EBI-389883,EBI-743184
GHRP109122EBI-389883,EBI-286316
GLTSCR1Q9NZM43EBI-389883,EBI-1754943
GNSP155862EBI-389883,EBI-1752200
GSTZ1O437082EBI-389883,EBI-748043
HIST1H1EP104122EBI-389883,EBI-358163
HNRNPRO433902EBI-389883,EBI-713419
ID4P479283EBI-389883,EBI-1754719
ISG20L2Q9H9L32EBI-389883,EBI-751335
JAK2O606742EBI-389883,EBI-518647
KDRP359683EBI-389883,EBI-1005487
KITP107213EBI-389883,EBI-1379503
KMT2BQ9UMN62EBI-389883,EBI-765774
LCP2Q1309414EBI-389883,EBI-346946
LRRC3Q9BY712EBI-389883,EBI-1761329
MAP4P278162EBI-389883,EBI-715255
MAP4K1Q929184EBI-389883,EBI-881
MAP4K5Q9Y4K42EBI-389883,EBI-1279
MEPEQ9NQ763EBI-389883,EBI-1753293
METP085812EBI-389883,EBI-1039152
MYLKQ157462EBI-389883,EBI-968482
NELFBQ8WX926EBI-389883,EBI-347721
NKX2-1P436992EBI-389883,EBI-1391923
NPHS1O605003EBI-389883,EBI-996920
PAK2Q131772EBI-389883,EBI-1045887
PDIA2Q130873EBI-389883,EBI-1752525
PHACTR2O751672EBI-389883,EBI-1754409
PIK3C2BO007503EBI-389883,EBI-641107
PNMA2Q9UL422EBI-389883,EBI-302355
PRXQ9BXM02EBI-389883,EBI-1753064
PTPN4P290743EBI-389883,EBI-710431
RAG1P159182EBI-389883,EBI-1755109
RAPGEF1Q139052EBI-389883,EBI-976876
RASA1P209366EBI-389883,EBI-1026476
RIMS2Q9UQ262EBI-389883,EBI-1756749
RIN3Q8TB242EBI-389883,EBI-1570523
RPL13P263732EBI-389883,EBI-356849
RPP38P783452EBI-389883,EBI-366493
RRASP103013EBI-389883,EBI-968703
SCARF2Q96GP62EBI-389883,EBI-1752088
SEMA7AO753262EBI-389883,EBI-1753538
SEPN1Q9NZV52EBI-389883,EBI-1751965
SHANK2Q9UPX86EBI-389883,EBI-1570571
SHANK3Q9BYB04EBI-389883,EBI-1752330
SHROOM2Q137962EBI-389883,EBI-1644065
SLC23A1Q9UHI72EBI-389883,EBI-1759386
SLC24A1O607213EBI-389883,EBI-1753504
SNX12Q9UMY43EBI-389883,EBI-1752602
SNX17Q150363EBI-389883,EBI-1752620
SNX8Q9Y5X22EBI-389883,EBI-1752557
SOS1Q078895EBI-389883,EBI-297487
SOS2Q078903EBI-389883,EBI-298181
SP1P080472EBI-389883,EBI-298336
SPENQ96T583EBI-389883,EBI-765739
SUV39H2Q9H5I12EBI-389883,EBI-723127
SYNJ2O150563EBI-389883,EBI-310513
TGOLN2O434933EBI-389883,EBI-1752146
TMPOP421672EBI-389883,EBI-455283
TPSAB1Q156612EBI-389883,EBI-1761369
TPX2Q9ULW04EBI-389883,EBI-1037322
TRAIPQ9BWF23EBI-389883,EBI-1756205
TRIM39Q9HCM92EBI-389883,EBI-739510
TULP1O002942EBI-389883,EBI-1756778
VPS13AQ96RL73EBI-389883,EBI-1752583
WIPF1O435162EBI-389883,EBI-346356

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P16333-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P16333-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-76: MAEEVVVVAK...IVKNLKDTLG → MDWLNVFKDFFS
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.31
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.31 Ref.32
Modified residue851Phosphoserine Ref.25 Ref.27
Modified residue911Phosphoserine Ref.25
Modified residue961Phosphoserine Ref.25
Modified residue1051Phosphotyrosine Ref.23 Ref.27 Ref.28

Natural variations

Alternative sequence1 – 7676MAEEV…KDTLG → MDWLNVFKDFFS in isoform 2.
VSP_043122
Natural variant1801A → V.
Corresponds to variant rs13320485 [ dbSNP | Ensembl ].
VAR_051228

Experimental info

Mutagenesis381W → K: Small decrease in RASA1-binding. Almost complete loss of RASA1-binding; when associated with K-143 and K-229. Ref.30
Mutagenesis1431W → K: No effect on RASA1-binding. Almost complete loss of RASA1-binding; when associated with K-38 and K-229. Ref.30
Mutagenesis2291W → K: Small decrease in RASA1-binding. Almost complete loss of RASA1-binding; when associated with K-38 and K-229. Ref.30
Mutagenesis3081R → K: No effect on RASA1-binding. Ref.30

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 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

Isoform 2 [UniParc].

Checksum: D10F0F2DEF1D72F7
Show »

FASTA31335,511

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Synovium.
[3]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Uterus.
[6]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, PARTIAL PROTEIN SEQUENCE.
[7]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[8]"Two signaling molecules share a phosphotyrosine-containing binding site in the platelet-derived growth factor receptor."
Nishimura R., Li W., Kashishian A., Mondino A., Zhou M., Cooper J., Schlessinger J.
Mol. Cell. Biol. 13:6889-6896(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDGFRB, PHOSPHORYLATION.
[9]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SOCS7.
[10]"Tyrosine 1213 of Flt-1 is a major binding site of Nck and SHP-2."
Igarashi K., Isohara T., Kato T., Shigeta K., Yamano T., Uno I.
Biochem. Biophys. Res. Commun. 246:95-99(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FLT1.
[11]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BLNK; GRB2; PLCG1 AND VAV.
[12]"Nck recruitment to Eph receptor, EphB1/ELK, couples ligand activation to c-Jun kinase."
Stein E., Huynh-Do U., Lane A.A., Cerretti D.P., Daniel T.O.
J. Biol. Chem. 273:1303-1308(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL ADHESION, INTERACTION WITH EPHB1.
Tissue: Kidney.
[13]"Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing adapter protein having similar binding and biological properties to Nck."
Braverman L.E., Quilliam L.A.
J. Biol. Chem. 274:5542-5549(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EGFR; PAK1; PKN2 AND SOS1, PHOSPHORYLATION.
[14]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RALGPS1.
[15]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CAV2.
[16]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CAV2.
[17]"Identification and functional characterization of a novel human misshapen/Nck interacting kinase-related kinase, hMINK beta."
Hu Y., Leo C., Yu S., Huang B.C., Wang H., Shen M., Luo Y., Daniel-Issakani S., Payan D.G., Xu X.
J. Biol. Chem. 279:54387-54397(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MINK1.
[18]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN COMPLEX WITH PP1 AND PPP1R15B, FUNCTION, SUBCELLULAR LOCATION.
[20]"Phosphorylation of Tyr1214 within VEGFR-2 triggers the recruitment of Nck and activation of Fyn leading to SAPK2/p38 activation and endothelial cell migration in response to VEGF."
Lamalice L., Houle F., Huot J.
J. Biol. Chem. 281:34009-34020(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KDR.
[21]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SOCS7.
[22]"Nck-1 interacts with PKR and modulates its activation by dsRNA."
Cardin E., Larose L.
Biochem. Biophys. Res. Commun. 377:231-235(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EIF2AK2, PHOSPHORYLATION.
[23]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[24]"Distinct functions of natural ADAM-15 cytoplasmic domain variants in human mammary carcinoma."
Zhong J.L., Poghosyan Z., Pennington C.J., Scott X., Handsley M.M., Warn A., Gavrilovic J., Honert K., Kruger A., Span P.N., Sweep F.C., Edwards D.R.
Mol. Cancer Res. 6:383-394(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ADAM15.
[25]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-91 AND SER-96, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[26]"Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
Voss M., Lettau M., Janssen O.
BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FASLG.
[27]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85 AND TYR-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[28]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[29]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"Adaptor protein Nck1 interacts with p120 Ras GTPase-activating protein and regulates its activity."
Ger M., Zitkus Z., Valius M.
Cell. Signal. 23:1651-1658(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RASA1, MUTAGENESIS OF TRP-38; TRP-143; TRP-229 AND ARG-308.
[31]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[32]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[33]"Receptor protein tyrosine phosphatase-receptor tyrosine kinase substrate screen identifies EphA2 as a target for LAR in cell migration."
Lee H., Bennett A.M.
Mol. Cell. Biol. 33:1430-1441(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL MIGRATION, INTERACTION WITH EPHA2.
[34]"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.
[35]"Specificity determinants of a novel Nck interaction with the juxtamembrane domain of the epidermal growth factor receptor."
Hake M.J., Choowongkomon K., Kostenko O., Carlin C.R., Sonnichsen F.D.
Biochemistry 47:3096-3108(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-61 AND 107-165, INTERACTION WITH EGFR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X17576 mRNA. Translation: CAA35599.1.
AK301460 mRNA. Translation: BAH13487.1.
AC011597 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79105.1.
CH471052 Genomic DNA. Translation: EAW79108.1.
CH471052 Genomic DNA. Translation: EAW79109.1.
BC006403 mRNA. Translation: AAH06403.1.
CCDSCCDS3092.1. [P16333-1]
CCDS54644.1. [P16333-2]
PIRS08636.
RefSeqNP_001177725.1. NM_001190796.2. [P16333-2]
NP_006144.1. NM_006153.5. [P16333-1]
XP_006713713.1. XM_006713650.1. [P16333-1]
XP_006713714.1. XM_006713651.1. [P16333-1]
XP_006713715.1. XM_006713652.1. [P16333-1]
UniGeneHs.126889.
Hs.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[»]
ProteinModelPortalP16333.
SMRP16333. Positions 1-61, 99-174, 193-250, 279-377.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110770. 68 interactions.
DIPDIP-639N.
IntActP16333. 193 interactions.
MINTMINT-92747.
STRING9606.ENSP00000288986.

Chemistry

BindingDBP16333.
ChEMBLCHEMBL4846.

PTM databases

PhosphoSiteP16333.

Polymorphism databases

DMDM127962.

Proteomic databases

MaxQBP16333.
PaxDbP16333.
PeptideAtlasP16333.
PRIDEP16333.

Protocols and materials databases

DNASU4690.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000288986; ENSP00000288986; ENSG00000158092. [P16333-1]
ENST00000469404; ENSP00000419631; ENSG00000158092. [P16333-2]
ENST00000481752; ENSP00000417273; ENSG00000158092. [P16333-1]
GeneID4690.
KEGGhsa:4690.
UCSCuc003erh.3. human. [P16333-1]
uc011bme.2. human. [P16333-2]

Organism-specific databases

CTD4690.
GeneCardsGC03P136581.
HGNCHGNC:7664. NCK1.
HPACAB005063.
MIM600508. gene.
neXtProtNX_P16333.
PharmGKBPA31466.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG261435.
HOGENOMHOG000290684.
HOVERGENHBG000719.
InParanoidP16333.
KOK07365.
OMATIMQNNP.
OrthoDBEOG7SV0VJ.
PhylomeDBP16333.
TreeFamTF351631.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_111155. Cell-Cell communication.
REACT_6900. Immune System.
SignaLinkP16333.

Gene expression databases

ArrayExpressP16333.
BgeeP16333.
CleanExHS_NCK1.
GenevestigatorP16333.

Family and domain databases

Gene3D3.30.505.10. 1 hit.
InterProIPR017304. NCK.
IPR028526. NCK1.
IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]
PANTHERPTHR22820:SF11. PTHR22820:SF11. 1 hit.
PfamPF00017. SH2. 1 hit.
PF00018. SH3_1. 2 hits.
PF14604. SH3_9. 1 hit.
[Graphical view]
PIRSFPIRSF037874. Cytoplasmic_NCK. 1 hit.
PRINTSPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
SMARTSM00252. SH2. 1 hit.
SM00326. SH3. 3 hits.
[Graphical view]
SUPFAMSSF50044. SSF50044. 3 hits.
SSF55550. SSF55550. 1 hit.
PROSITEPS50001. SH2. 1 hit.
PS50002. SH3. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP16333.
GeneWikiNCK1.
GenomeRNAi4690.
NextBio18086.
PMAP-CutDBP16333.
PROP16333.
SOURCESearch...

Entry information

Entry nameNCK1_HUMAN
AccessionPrimary (citable) accession number: P16333
Secondary accession number(s): B7Z751, D3DNE3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: July 9, 2014
This is version 162 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

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