NCK1

From Wikipedia, the free encyclopedia
NCK adaptor protein 1

PDB rendering based on 2ci8.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsNCK1; NCK; NCKalpha; nck-1
External IDsOMIM: 600508 MGI: 109601 HomoloGene: 38148 ChEMBL: 4846 GeneCards: NCK1 Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez469017973
EnsemblENSG00000158092ENSMUSG00000032475
UniProtP16333Q99M51
RefSeq (mRNA)NM_001190796NM_010878
RefSeq (protein)NP_001177725NP_035008
Location (UCSC)Chr 3:
136.58 – 136.67 Mb		Chr 9:
100.49 – 100.55 Mb
PubMed search
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Cytoplasmic protein NCK1 is a protein that in humans is encoded by the NCK1 gene.[1][2]

Gene

The Nck (non-catalytic region of tyrosine kinase adaptor protein 1) belongs to the adaptor family of proteins. The nck gene was initially isolated from a human melanoma cDNA library using a monoclonal antibody produced against the human melanoma-associated antigen. The Nck family has two known members in human cells (Nck-1/Nckalpha and NcK2/NcKbeta), two in mouse cells (mNckalpha and mNckbeta/Grb4) and one in drosophila (Dock means dreadlocks-ortholog).

The two murine gene products exhibit 68% amino acid identity to one another, with most of the sequence variation being located to the linker regions between the SH3 and SH2 domains, and are 96% identical to their human counterparts. While human nck-1 gene has been localised to the 3q21 locus of chromosome 3, the nck-2 gene can be found on chromosome 2 at the 2q12 locus.

Function

The protein encoded by this gene is one of the signaling and transforming proteins containing Src homology 2 and 3 (SH2 and SH3) domains. It is located in the cytoplasm and is an adaptor protein involved in transducing signals from receptor tyrosine kinases to downstream signal recipients such as RAS.[3]

Interactions

NCK1 has been shown to interact with:

See also

References

  1. ↑ Huebner K, Kastury K, Druck T, Salcini AE, Lanfrancone L, Pelicci G, Lowenstein E, Li W, Park SH (January 1995). "Chromosome locations of genes encoding human signal transduction adapter proteins, Nck (NCK), Shc (SHC1), and Grb2 (GRB2)". Genomics 22 (2): 281–7. doi:10.1006/geno.1994.1385. PMID 7806213. 
  2. ↑ Chen M, She H, Davis EM, Spicer CM, Kim L, Ren R, Le Beau MM, Li W (October 1998). "Identification of Nck family genes, chromosomal localization, expression, and signaling specificity". J Biol Chem 273 (39): 25171–8. doi:10.1074/jbc.273.39.25171. PMID 9737977. 
  3. ↑ "Entrez Gene: NCK1 NCK adaptor protein 1". 
  4. ↑ 4.0 4.1 Miyoshi-Akiyama T, Aleman LM, Smith JM, Adler CE, Mayer BJ (July 2001). "Regulation of Cbl phosphorylation by the Abl tyrosine kinase and the Nck SH2/SH3 adaptor". Oncogene 20 (30): 4058–69. doi:10.1038/sj.onc.1204528. PMID 11494134. 
  5. ↑ Ren R, Ye ZS, Baltimore D (April 1994). "Abl protein-tyrosine kinase selects the Crk adapter as a substrate using SH3-binding sites". Genes Dev. 8 (7): 783–95. doi:10.1101/gad.8.7.783. PMID 7926767. 
  6. ↑ Erdreich-Epstein A, Liu M, Kant AM, Izadi KD, Nolta JA, Durden DL (April 1999). "Cbl functions downstream of Src kinases in Fc gamma RI signaling in primary human macrophages". J. Leukoc. Biol. 65 (4): 523–34. PMID 10204582. 
  7. ↑ 7.0 7.1 Wunderlich L, Faragó A, Buday L (January 1999). "Characterization of interactions of Nck with Sos and dynamin". Cell. Signal. 11 (1): 25–9. doi:10.1016/S0898-6568(98)00027-8. PMID 10206341. 
  8. ↑ Sotgia F, Lee H, Bedford MT, Petrucci T, Sudol M, Lisanti MP (December 2001). "Tyrosine phosphorylation of beta-dystroglycan at its WW domain binding motif, PPxY, recruits SH2 domain containing proteins". Biochemistry 40 (48): 14585–92. doi:10.1021/bi011247r. PMID 11724572. 
  9. ↑ Kebache S, Zuo D, Chevet E, Larose L (April 2002). "Modulation of protein translation by Nck-1". Proc. Natl. Acad. Sci. U.S.A. 99 (8): 5406–11. doi:10.1073/pnas.082483399. PMC 122782. PMID 11959995. 
  10. ↑ 10.0 10.1 Matuoka K, Miki H, Takahashi K, Takenawa T (October 1997). "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 (2): 488–92. doi:10.1006/bbrc.1997.7492. PMID 9344857. 
  11. ↑ 11.0 11.1 Tang J, Feng GS, Li W (October 1997). "Induced direct binding of the adapter protein Nck to the GTPase-activating protein-associated protein p62 by epidermal growth factor". Oncogene 15 (15): 1823–32. doi:10.1038/sj.onc.1201351. PMID 9362449. 
  12. ↑ 12.0 12.1 12.2 Li, W; Hu P, Skolnik E Y, Ullrich A, Schlessinger J (December 1992). "The SH2 and SH3 domain-containing Nck protein is oncogenic and a common target for phosphorylation by different surface receptors". Mol. Cell. Biol. (UNITED STATES) 12 (12): 5824–33. doi:10.1128/MCB.12.12.5824. ISSN 0270-7306. PMC 360522. PMID 1333047. 
  13. ↑ Lawe DC, Hahn C, Wong AJ (January 1997). "The Nck SH2/SH3 adaptor protein is present in the nucleus and associates with the nuclear protein SAM68". Oncogene 14 (2): 223–31. doi:10.1038/sj.onc.1200821. PMID 9010224. 
  14. ↑ Shim EK, Moon CS, Lee GY, Ha YJ, Chae SK, Lee JR (September 2004). "Association of the Src homology 2 domain-containing leukocyte phosphoprotein of 76 kD (SLP-76) with the p85 subunit of phosphoinositide 3-kinase". FEBS Lett. 575 (1–3): 35–40. doi:10.1016/j.febslet.2004.07.090. PMID 15388330. 
  15. ↑ Wunderlich L, Faragó A, Downward J, Buday L (April 1999). "Association of Nck with tyrosine-phosphorylated SLP-76 in activated T lymphocytes". Eur. J. Immunol. 29 (4): 1068–75. doi:10.1002/(SICI)1521-4141(199904)29:04<1068::AID-IMMU1068>3.0.CO;2-P. PMID 10229072. 
  16. ↑ Ling P, Yao Z, Meyer CF, Wang XS, Oehrl W, Feller SM, Tan TH (February 1999). "Interaction of hematopoietic progenitor kinase 1 with adapter proteins Crk and CrkL leads to synergistic activation of c-Jun N-terminal kinase". Mol. Cell. Biol. 19 (2): 1359–68. PMC 116064. PMID 9891069. 
  17. ↑ Ling P, Meyer CF, Redmond LP, Shui JW, Davis B, Rich RR, Hu MC, Wange RL, Tan TH (June 2001). "Involvement of hematopoietic progenitor kinase 1 in T cell receptor signaling". J. Biol. Chem. 276 (22): 18908–14. doi:10.1074/jbc.M101485200. PMID 11279207. 
  18. ↑ Su YC, Han J, Xu S, Cobb M, Skolnik EY (March 1997). "NIK is a new Ste20-related kinase that binds NCK and MEKK1 and activates the SAPK/JNK cascade via a conserved regulatory domain". EMBO J. 16 (6): 1279–90. doi:10.1093/emboj/16.6.1279. PMC 1169726. PMID 9135144. 
  19. ↑ Hu Y, Leo C, Yu S, Huang BC, Wang H, Shen M, Luo Y, Daniel-Issakani S, Payan DG, Xu X (December 2004). "Identification and functional characterization of a novel human misshapen/Nck interacting kinase-related kinase, hMINK beta". J. Biol. Chem. 279 (52): 54387–97. doi:10.1074/jbc.M404497200. PMID 15469942. 
  20. ↑ Lim CS, Park ES, Kim DJ, Song YH, Eom SH, Chun JS, Kim JH, Kim JK, Park D, Song WK (April 2001). "SPIN90 (SH3 protein interacting with Nck, 90 kDa), an adaptor protein that is developmentally regulated during cardiac myocyte differentiation". J. Biol. Chem. 276 (16): 12871–8. doi:10.1074/jbc.M009411200. PMID 11278500. 
  21. ↑ 21.0 21.1 Minegishi M, Tachibana K, Sato T, Iwata S, Nojima Y, Morimoto C (October 1996). "Structure and function of Cas-L, a 105-kD Crk-associated substrate-related protein that is involved in beta 1 integrin-mediated signaling in lymphocytes". J. Exp. Med. 184 (4): 1365–75. doi:10.1084/jem.184.4.1365. PMC 2192828. PMID 8879209. 
  22. ↑ 22.0 22.1 22.2 22.3 22.4 Braverman LE, Quilliam LA (February 1999). "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 (9): 5542–9. doi:10.1074/jbc.274.9.5542. PMID 10026169. 
  23. ↑ Ku GM, Yablonski D, Manser E, Lim L, Weiss A (February 2001). "A PAK1-PIX-PKL complex is activated by the T-cell receptor independent of Nck, Slp-76 and LAT". EMBO J. 20 (3): 457–65. doi:10.1093/emboj/20.3.457. PMC 133476. PMID 11157752. 
  24. ↑ Bokoch GM, Wang Y, Bohl BP, Sells MA, Quilliam LA, Knaus UG (October 1996). "Interaction of the Nck adapter protein with p21-activated kinase (PAK1)". J. Biol. Chem. 271 (42): 25746–9. doi:10.1074/jbc.271.42.25746. PMID 8824201. 
  25. ↑ Quilliam LA, Lambert QT, Mickelson-Young LA, Westwick JK, Sparks AB, Kay BK, Jenkins NA, Gilbert DJ, Copeland NG, Der CJ (November 1996). "Isolation of a NCK-associated kinase, PRK2, an SH3-binding protein and potential effector of Rho protein signaling". J. Biol. Chem. 271 (46): 28772–6. doi:10.1074/jbc.271.46.28772. PMID 8910519. 
  26. ↑ Goicoechea SM, Tu Y, Hua Y, Chen K, Shen TL, Guan JL, Wu C (July 2002). "Nck-2 interacts with focal adhesion kinase and modulates cell motility". Int. J. Biochem. Cell Biol. 34 (7): 791–805. doi:10.1016/S1357-2725(02)00002-X. PMID 11950595. 
  27. ↑ Ger M, Zitkus Z, Valius M (October 2011). "Adaptor protein Nck1 interacts with p120 Ras GTPase-activating protein and regulates its activity". Cell. Signal. 23 (10): 1651–8. doi:10.1016/j.cellsig.2011.05.019. PMID 21664272. 
  28. ↑ Zhao C, Ma H, Bossy-Wetzel E, Lipton SA, Zhang Z, Feng GS (September 2003). "GC-GAP, a Rho family GTPase-activating protein that interacts with signaling adapters Gab1 and Gab2". J. Biol. Chem. 278 (36): 34641–53. doi:10.1074/jbc.M304594200. PMID 12819203. 
  29. ↑ Wang B, Zou JX, Ek-Rylander B, Ruoslahti E (February 2000). "R-Ras contains a proline-rich site that binds to SH3 domains and is required for integrin activation by R-Ras". J. Biol. Chem. 275 (7): 5222–7. doi:10.1074/jbc.275.7.5222. PMID 10671570. 
  30. ↑ Hu Q, Milfay D, Williams LT (March 1995). "Binding of NCK to SOS and activation of ras-dependent gene expression". Mol. Cell. Biol. 15 (3): 1169–74. PMC 230339. PMID 7862111. 
  31. ↑ Okada S, Pessin JE (October 1996). "Interactions between Src homology (SH) 2/SH3 adapter proteins and the guanylnucleotide exchange factor SOS are differentially regulated by insulin and epidermal growth factor". J. Biol. Chem. 271 (41): 25533–8. doi:10.1074/jbc.271.41.25533. PMID 8810325. 
  32. ↑ Chou MM, Hanafusa H (March 1995). "A novel ligand for SH3 domains. The Nck adaptor protein binds to a serine/threonine kinase via an SH3 domain". J. Biol. Chem. 270 (13): 7359–64. doi:10.1074/jbc.270.13.7359. PMID 7706279. 
  33. ↑ Rohatgi R, Nollau P, Ho HY, Kirschner MW, Mayer BJ (July 2001). "Nck and phosphatidylinositol 4,5-bisphosphate synergistically activate actin polymerization through the N-WASP-Arp2/3 pathway". J. Biol. Chem. 276 (28): 26448–52. doi:10.1074/jbc.M103856200. PMID 11340081. 
  34. ↑ Antón IM, Lu W, Mayer BJ, Ramesh N, Geha RS (August 1998). "The Wiskott-Aldrich syndrome protein-interacting protein (WIP) binds to the adaptor protein Nck". J. Biol. Chem. 273 (33): 20992–5. doi:10.1074/jbc.273.33.20992. PMID 9694849. 
  35. ↑ Krause M, Sechi AS, Konradt M, Monner D, Gertler FB, Wehland J (April 2000). "Fyn-binding protein (Fyb)/SLP-76-associated protein (SLAP), Ena/vasodilator-stimulated phosphoprotein (VASP) proteins and the Arp2/3 complex link T cell receptor (TCR) signaling to the actin cytoskeleton". J. Cell Biol. 149 (1): 181–94. doi:10.1083/jcb.149.1.181. PMC 2175102. PMID 10747096. 
  36. ↑ Okabe S, Fukuda S, Broxmeyer HE (July 2002). "Activation of Wiskott-Aldrich syndrome protein and its association with other proteins by stromal cell-derived factor-1alpha is associated with cell migration in a T-lymphocyte line". Exp. Hematol. 30 (7): 761–6. doi:10.1016/S0301-472X(02)00823-8. PMID 12135674. 
  37. ↑ Rivero-Lezcano OM, Marcilla A, Sameshima JH, Robbins KC (October 1995). "Wiskott-Aldrich syndrome protein physically associates with Nck through Src homology 3 domains". Mol. Cell. Biol. 15 (10): 5725–31. PMC 230823. PMID 7565724. 

Further reading

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