NCKIPSD

Protein-coding gene in the species Homo sapiens

NCKIPSD
Identifiers
AliasesNCKIPSD, AF3P21, DIP, DIP1, ORF1, SPIN90, VIP54, WASLBP, WISH, NCK interacting protein with SH3 domain
External IDsOMIM: 606671; MGI: 1931834; HomoloGene: 9514; GeneCards: NCKIPSD; OMA:NCKIPSD - orthologs
Gene location (Human)
Chromosome 3 (human)
Chr.Chromosome 3 (human)[1]
Chromosome 3 (human)
Genomic location for NCKIPSD
Genomic location for NCKIPSD
Band3p21.31Start48,673,844 bp[1]
End48,686,364 bp[1]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right frontal lobe

  • prefrontal cortex

  • middle temporal gyrus

  • primary visual cortex

  • Brodmann area 9

  • right hemisphere of cerebellum

  • Brodmann area 23

  • right auricle

  • anterior cingulate cortex

  • superior frontal gyrus
    n/a
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • SH3 domain binding
  • cytoskeletal protein binding
  • protein binding
Cellular component
  • COP9 signalosome
  • cytosol
  • intermediate filament
  • nucleus
Biological process
  • cytoskeleton organization
  • Fc-gamma receptor signaling pathway involved in phagocytosis
  • signal transduction
  • NLS-bearing protein import into nucleus
  • positive regulation of neuron projection development
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

51517

80987

Ensembl

ENSG00000213672

ENSMUSG00000032598

UniProt

Q9NZQ3

Q9ESJ4

RefSeq (mRNA)

NM_184231
NM_016453

NM_030729

RefSeq (protein)

NP_057537
NP_909119

NP_109654

Location (UCSC)Chr 3: 48.67 – 48.69 Mbn/a
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

NCK-interacting protein with SH3 domain is a protein that in humans is encoded by the NCKIPSD gene.[4][5][6]

The protein encoded by this gene is localized exclusively in the cell nucleus. It plays a role in signal transduction, and may function in the maintenance of sarcomeres and in the assembly of myofibrils into sarcomeres. It also plays an important role in stress fiber formation. The gene is involved in therapy-related leukemia by a chromosomal translocation t(3;11)(p21;q23) that involves this gene and the myeloid/lymphoid leukemia gene. Alternative splicing occurs in this locus and two transcript variants encoding distinct isoforms have been identified.[6]

Interactions

NCKIPSD has been shown to interact with Grb2[7][8] and NCK1.[9]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000213672 – Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ Sano K, Hayakawa A, Piao JH, Kosaka Y, Nakamura H (February 2000). "Novel SH3 protein encoded by the AF3p21 gene is fused to the mixed lineage leukemia protein in a therapy-related leukemia with t(3;11) (p21;q23)". Blood. 95 (3): 1066–8. doi:10.1182/blood.V95.3.1066.003k11_1066_1068. PMID 10648423.
  5. ^ de Bernard M, Moschioni M, Napolitani G, Rappuoli R, Montecucco C (January 2000). "The VacA toxin of Helicobacter pylori identifies a new intermediate filament-interacting protein". The EMBO Journal. 19 (1): 48–56. doi:10.1093/emboj/19.1.48. PMC 1171776. PMID 10619843.
  6. ^ a b "Entrez Gene: NCKIPSD NCK interacting protein with SH3 domain".
  7. ^ Satoh S, Tominaga T (October 2001). "mDia-interacting protein acts downstream of Rho-mDia and modifies Src activation and stress fiber formation". The Journal of Biological Chemistry. 276 (42): 39290–4. doi:10.1074/jbc.M107026200. PMID 11509578.
  8. ^ Fukuoka M, Suetsugu S, Miki H, Fukami K, Endo T, Takenawa T (February 2001). "A novel neural Wiskott-Aldrich syndrome protein (N-WASP) binding protein, WISH, induces Arp2/3 complex activation independent of Cdc42". The Journal of Cell Biology. 152 (3): 471–82. doi:10.1083/jcb.152.3.471. PMC 2196001. PMID 11157975.
  9. ^ 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". The Journal of Biological Chemistry. 276 (16): 12871–8. doi:10.1074/jbc.M009411200. PMID 11278500.

Further reading

  • Fukuoka M, Suetsugu S, Miki H, Fukami K, Endo T, Takenawa T (February 2001). "A novel neural Wiskott-Aldrich syndrome protein (N-WASP) binding protein, WISH, induces Arp2/3 complex activation independent of Cdc42". The Journal of Cell Biology. 152 (3): 471–82. doi:10.1083/jcb.152.3.471. PMC 2196001. PMID 11157975.
  • Hayakawa A, Matsuda Y, Daibata M, Nakamura H, Sano K (April 2001). "Genomic organization, tissue expression, and cellular localization of AF3p21, a fusion partner of MLL in therapy-related leukemia". Genes, Chromosomes & Cancer. 30 (4): 364–74. doi:10.1002/gcc.1102. PMID 11241789. S2CID 25952711.
  • 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". The Journal of Biological Chemistry. 276 (16): 12871–8. doi:10.1074/jbc.M009411200. PMID 11278500.
  • Satoh S, Tominaga T (October 2001). "mDia-interacting protein acts downstream of Rho-mDia and modifies Src activation and stress fiber formation". The Journal of Biological Chemistry. 276 (42): 39290–4. doi:10.1074/jbc.M107026200. PMID 11509578.
  • Lim CS, Kim SH, Jung JG, Kim JK, Song WK (December 2003). "Regulation of SPIN90 phosphorylation and interaction with Nck by ERK and cell adhesion". The Journal of Biological Chemistry. 278 (52): 52116–23. doi:10.1074/jbc.M310974200. PMID 14559906.
  • Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, Kulkarni S, Metalnikov P, O'Donnell P, Taylor P, Taylor L, Zougman A, Woodgett JR, Langeberg LK, Scott JD, Pawson T (August 2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Current Biology. 14 (16): 1436–50. Bibcode:2004CBio...14.1436J. doi:10.1016/j.cub.2004.07.051. PMID 15324660. S2CID 2371325.
  • Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  • Kim DJ, Kim SH, Lim CS, Choi KY, Park CS, Sung BH, Yeo MG, Chang S, Kim JK, Song WK (January 2006). "Interaction of SPIN90 with the Arp2/3 complex mediates lamellipodia and actin comet tail formation". The Journal of Biological Chemistry. 281 (1): 617–25. doi:10.1074/jbc.M504450200. PMID 16253999.
  • Eisenmann KM, Harris ES, Kitchen SM, Holman HA, Higgs HN, Alberts AS (April 2007). "Dia-interacting protein modulates formin-mediated actin assembly at the cell cortex". Current Biology. 17 (7): 579–91. Bibcode:2007CBio...17..579E. doi:10.1016/j.cub.2007.03.024. PMID 17398099. S2CID 11733142.
  • Rönty M, Taivainen A, Heiska L, Otey C, Ehler E, Song WK, Carpen O (July 2007). "Palladin interacts with SH3 domains of SPIN90 and Src and is required for Src-induced cytoskeletal remodeling". Experimental Cell Research. 313 (12): 2575–85. doi:10.1016/j.yexcr.2007.04.030. PMC 2000818. PMID 17537434.
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