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PRKCI

From Wikipedia, the free encyclopedia
Protein-coding gene in the species Homo sapiens
PRKCI
Available structures
PDBOrtholog search:PDBeRCSB
List of PDB id codes

1VD2,1WMH,1ZRZ,3A8W,3A8X,3ZH8

Identifiers
AliasesPRKCI, DXS1179E, PKCI, nPKC-iota, protein kinase C iota
External IDsOMIM:600539;MGI:99260;HomoloGene:37667;GeneCards:PRKCI;OMA:PRKCI - orthologs
Gene location (Human)
Chromosome 3 (human)
Chr.Chromosome 3 (human)[1]
Chromosome 3 (human)
Genomic location for PRKCI
Genomic location for PRKCI
Band3q26.2Start170,222,424bp[1]
End170,305,977bp[1]
Gene location (Mouse)
Chromosome 3 (mouse)
Chr.Chromosome 3 (mouse)[2]
Chromosome 3 (mouse)
Genomic location for PRKCI
Genomic location for PRKCI
Band3 A3|3 14.65 cMStart31,049,896bp[2]
End31,107,108bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • buccal mucosa cell

  • pylorus

  • lower lobe of lung

  • corpus epididymis

  • cardia

  • oral cavity

  • renal medulla

  • mucosa of pharynx

  • nipple

  • palpebral conjunctiva
Top expressed in
  • molar

  • ciliary body

  • urothelium

  • hair follicle

  • iris

  • conjunctival fornix

  • transitional epithelium of urinary bladder

  • epithelium of lens

  • primitive streak

  • ureter
More reference expression data
BioGPS




More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo /QuickGO
Orthologs
SpeciesHumanMouse
Entrez

5584

18759

Ensembl

ENSG00000163558

ENSMUSG00000037643

UniProt

P41743

Q62074

RefSeq (mRNA)

NM_002740

NM_008857

RefSeq (protein)

NP_002731

NP_032883

Location (UCSC)Chr 3: 170.22 – 170.31 MbChr 3: 31.05 – 31.11 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Protein kinase C iota type is anenzyme that in humans is encoded by thePRKCIgene.[5][6][7]

Function

[edit]

This gene encodes a member of the protein kinase C (PKC) family of serine/threonine protein kinases. The PKC family comprises at least eight members, which are differentially expressed and are involved in a wide variety of cellular processes. This protein kinase is calcium-independent and phospholipid-dependent. It is not activated byphorbol esters or diacylglycerol. This kinase can be recruited to vesicle tubular clusters (VTCs) by direct interaction with the small GTPase RAB2, where this kinase phosphorylates glyceraldehyde-3-phosphate dehydrogenase (GAPD/GAPDH) and plays a role in microtubule dynamics in the early secretory pathway. This kinase is found to be necessary for BCL-ABL-mediated resistance to drug-induced apoptosis and therefore protects leukemia cells against drug-induced apoptosis. There is a single exon pseudogene mapped on chromosome X.[7]

Interactions

[edit]

PRKCI has been shown tointeract with:

[17]

References

[edit]
  1. ^abcGRCh38: Ensembl release 89: ENSG00000163558Ensembl, May 2017
  2. ^abcGRCm38: Ensembl release 89: ENSMUSG00000037643Ensembl, May 2017
  3. ^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^Mazzarella R, Ciccodicola A, Esposito T, Arcucci A, Migliaccio C, Jones C, Schlessinger D, D'Urso M, D'Esposito M (Apr 1995). "Human protein kinase C Iota gene (PRKCI) is closely linked to the BTK gene in Xq21.3".Genomics.26 (3):629–31.doi:10.1016/0888-7543(95)80190-W.PMID 7607695.
  6. ^De Donato M, Gallagher DS, Davis SK, Stelly DM, Taylor JF (April 2002). "The assignment of PRKCI to bovine chromosome 1q34-->q36 by FISH suggests a new assignment to human chromosome 3".Cytogenetics and Cell Genetics.95 (1–2):79–81.doi:10.1159/000057021.PMID 11978974.S2CID 40052490.
  7. ^ab"Entrez Gene: PRKCI protein kinase C, iota".
  8. ^Zemlickova E, Dubois T, Kerai P, Clokie S, Cronshaw AD, Wakefield RI, Johannes FJ, Aitken A (Aug 2003). "Centaurin-alpha(1) associates with and is phosphorylated by isoforms of protein kinase C".Biochemical and Biophysical Research Communications.307 (3):459–65.doi:10.1016/s0006-291x(03)01187-2.PMID 12893243.
  9. ^Lim YP, Low BC, Lim J, Wong ES, Guy GR (Jul 1999)."Association of atypical protein kinase C isotypes with the docker protein FRS2 in fibroblast growth factor signaling".The Journal of Biological Chemistry.274 (27):19025–34.doi:10.1074/jbc.274.27.19025.PMID 10383403.
  10. ^Tisdale EJ (Feb 2002)."Glyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein kinase Ciota /lambda and plays a role in microtubule dynamics in the early secretory pathway".The Journal of Biological Chemistry.277 (5):3334–41.doi:10.1074/jbc.M109744200.PMID 11724794.
  11. ^Sanchez P, De Carcer G, Sandoval IV, Moscat J, Diaz-Meco MT (May 1998)."Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62".Molecular and Cellular Biology.18 (5):3069–80.doi:10.1128/mcb.18.5.3069.PMC 110686.PMID 9566925.
  12. ^Kohjima M, Noda Y, Takeya R, Saito N, Takeuchi K, Sumimoto H (Dec 2002). "PAR3beta, a novel homologue of the cell polarity protein PAR3, localizes to tight junctions".Biochemical and Biophysical Research Communications.299 (4):641–6.doi:10.1016/s0006-291x(02)02698-0.PMID 12459187.
  13. ^Balendran A, Biondi RM, Cheung PC, Casamayor A, Deak M, Alessi DR (Jul 2000)."A 3-phosphoinositide-dependent protein kinase-1 (PDK1) docking site is required for the phosphorylation of protein kinase Czeta (PKCzeta ) and PKC-related kinase 2 by PDK1".The Journal of Biological Chemistry.275 (27):20806–13.doi:10.1074/jbc.M000421200.PMID 10764742.
  14. ^Diaz-Meco MT, Municio MM, Sanchez P, Lozano J, Moscat J (Jan 1996)."Lambda-interacting protein, a novel protein that specifically interacts with the zinc finger domain of the atypical protein kinase C isotype lambda/iota and stimulates its kinase activity in vitro and in vivo".Molecular and Cellular Biology.16 (1):105–14.doi:10.1128/mcb.16.1.105.PMC 230983.PMID 8524286.
  15. ^Guo W, Wu S, Liu J, Fang B (Sep 2008)."Identification of a small molecule with synthetic lethality for K-ras and protein kinase C iota".Cancer Research.68 (18):7403–8.doi:10.1158/0008-5472.CAN-08-1449.PMC 2678915.PMID 18794128.
  16. ^Ratnayake WS, Apostolatos AH, Ostrov DA, Acevedo-Duncan M (2017)."Two novel atypical PKC inhibitors; ACPD and DNDA effectively mitigate cell proliferation and epithelial to mesenchymal transition of metastatic melanoma while inducing apoptosis".Int. J. Oncol.51 (5):1370–1382.doi:10.3892/ijo.2017.4131.PMC 5642393.PMID 29048609.
  17. ^Ratnayake WS, Apostolatos CA, Apostolatos AH, Schutte RJ, Huynh MA, Ostrov DA, Acevedo-Duncan M (2018)."Oncogenic PKC-ι activates Vimentin during epithelial-mesenchymal transition in melanoma; a study based on PKC-ι and PKC-ζ specific inhibitors".Cell Adhes. Migr.12 (5):1–17.doi:10.1080/19336918.2018.1471323.PMC 6363030.PMID 29781749.

Further reading

[edit]
PDB gallery
  • 1vd2: Solution Structure of the PB1 domain of PKCiota
    1vd2: Solution Structure of the PB1 domain of PKCiota
  • 1wmh: Crystal structure of a PB1 domain complex of Protein kinase c iota and Par6 alpha
    1wmh: Crystal structure of a PB1 domain complex of Protein kinase c iota and Par6 alpha
  • 1zrz: Crystal Structure of the Catalytic Domain of Atypical Protein Kinase C-iota
    1zrz: Crystal Structure of the Catalytic Domain of Atypical Protein Kinase C-iota
Non-specific serine/threonine protein kinases (EC 2.7.11.1)
Pyruvate dehydrogenase kinase (EC 2.7.11.2)
Dephospho-(reductase kinase) kinase (EC 2.7.11.3)
3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)
(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)
(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)
Myosin-heavy-chain kinase (EC 2.7.11.7)
Fas-activated serine/threonine kinase (EC 2.7.11.8)
Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)
  • -
IκB kinase (EC 2.7.11.10)
cAMP-dependent protein kinase (EC 2.7.11.11)
cGMP-dependent protein kinase (EC 2.7.11.12)
Protein kinase C (EC 2.7.11.13)
Rhodopsin kinase (EC 2.7.11.14)
Beta adrenergic receptor kinase (EC 2.7.11.15)
G-protein coupled receptor kinases (EC 2.7.11.16)
Ca2+/calmodulin-dependent (EC 2.7.11.17)
Myosin light-chain kinase (EC 2.7.11.18)
Phosphorylase kinase (EC 2.7.11.19)
Elongation factor 2 kinase (EC 2.7.11.20)
Polo kinase (EC 2.7.11.21)
Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)
Polo kinase (EC 2.7.11.21)
Cyclin-dependent kinase (EC 2.7.11.22)
(RNA-polymerase)-subunit kinase (EC 2.7.11.23)
Mitogen-activated protein kinase (EC 2.7.11.24)
MAP3K (EC 2.7.11.25)
Tau-protein kinase (EC 2.7.11.26)
(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)
  • -
Tropomyosin kinase (EC 2.7.11.28)
  • -
Low-density-lipoprotein receptor kinase (EC 2.7.11.29)
  • -
Receptor protein serine/threonine kinase (EC 2.7.11.30)
MAP2K
Activity
Regulation
Classification
Kinetics
Types
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