PAK7

P21 protein (Cdc42/Rac)-activated kinase 7
PDB rendering based on 2f57.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2F57​
Identifiers
Symbols	PAK7 ; PAK5
External IDs	OMIM: 608038 MGI: 1920334 HomoloGene: 22211 IUPHAR: 2138 ChEMBL: 4524 GeneCards: PAK7 Gene
EC number	2.7.11.1
Gene ontology Molecular function • protein serine/threonine kinase activity • ATP binding • Rac GTPase binding Cellular component • nucleus • cytoplasm • mitochondrion Biological process • apoptotic process • cytoskeleton organization • signal transduction • Rho protein signal transduction • regulation of mitotic cell cycle • learning • memory • locomotory behavior • cell proliferation • cell growth • cell migration • signal transduction by protein phosphorylation • actin cytoskeleton organization • stress-activated protein kinase signaling cascade • activation of protein kinase activity • regulation of apoptotic process • regulation of MAPK cascade • negative regulation of extrinsic apoptotic signaling pathway Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	57144	241656
Ensembl	ENSG00000101349	ENSMUSG00000039913
UniProt	Q9P286	Q8C015
RefSeq (mRNA)	NM_020341	NM_172858
RefSeq (protein)	NP_065074	NP_766446
Location (UCSC)	Chr 20: 9.54 – 9.84 Mb	Chr 2: 136.08 – 136.39 Mb
PubMed search

Serine/threonine-protein kinase PAK 7 is an enzyme that in humans is encoded by the PAK7 gene.^[1][2][3]

Function

The protein encoded by this gene is a member of the PAK family of Ser/Thr protein kinases. PAK family members are known to be effectors of Rac/Cdc42 GTPases, which have been implicated in the regulation of cytoskeletal dynamics, proliferation, and cell survival signaling. This kinase contains a CDC42/Rac1 interactive binding (CRIB) motif, and has been shown to bind CDC42 in the presence of GTP. This kinase is predominantly expressed in brain. It is capable of promoting neurite outgrowth, and thus may play a role in neurite development. This kinase is associated with microtubule networks and induces microtubule stabilization. The subcellular localization of this kinase is tightly regulated during cell cycle progression. Alternatively spliced transcript variants encoding the same protein have been described.^[3]

Interactions

PAK7 has been shown to interact with CDC42.^[1][4]

References

1. Dan C, Nath N, Liberto M, Minden A (Jan 2002). "PAK5, a new brain-specific kinase, promotes neurite outgrowth in N1E-115 cells". Molecular and Cellular Biology 22 (2): 567–77. doi:10.1128/MCB.22.2.567-577.2002. PMC 139731. PMID 11756552.
2. Nagase T, Ishikawa K, Kikuno R, Hirosawa M, Nomura N, Ohara O (Oct 1999). "Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Research 6 (5): 337–45. doi:10.1093/dnares/6.5.337. PMID 10574462.
3. "Entrez Gene: PAK7 p21(CDKN1A)-activated kinase 7".
4. Pandey A, Dan I, Kristiansen TZ, Watanabe NM, Voldby J, Kajikawa E, Khosravi-Far R, Blagoev B, Mann M (May 2002). "Cloning and characterization of PAK5, a novel member of mammalian p21-activated kinase-II subfamily that is predominantly expressed in brain". Oncogene 21 (24): 3939–48. doi:10.1038/sj.onc.1205478. PMID 12032833.

Further reading

• Jaffer ZM, Chernoff J (Jul 2002). "p21-activated kinases: three more join the Pak". The International Journal of Biochemistry & Cell Biology 34 (7): 713–7. doi:10.1016/S1357-2725(01)00158-3. PMID 11950587.
• del Peso L, González-García M, Page C, Herrera R, Nuñez G (Oct 1997). "Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt". Science 278 (5338): 687–9. doi:10.1126/science.278.5338.687. PMID 9381178.
• Scheid MP, Schubert KM, Duronio V (Oct 1999). "Regulation of bad phosphorylation and association with Bcl-x(L) by the MAPK/Erk kinase". The Journal of Biological Chemistry 274 (43): 31108–13. doi:10.1074/jbc.274.43.31108. PMID 10521512.
• Tan Y, Demeter MR, Ruan H, Comb MJ (Aug 2000). "BAD Ser-155 phosphorylation regulates BAD/Bcl-XL interaction and cell survival". The Journal of Biological Chemistry 275 (33): 25865–9. doi:10.1074/jbc.M004199200. PMID 10837486.
• Lizcano JM, Morrice N, Cohen P (Jul 2000). "Regulation of BAD by cAMP-dependent protein kinase is mediated via phosphorylation of a novel site, Ser155". The Biochemical Journal 349 (Pt 2): 547–57. doi:10.1042/0264-6021:3490547. PMC 1221178. PMID 10880354.
• Cau J, Faure S, Comps M, Delsert C, Morin N (Dec 2001). "A novel p21-activated kinase binds the actin and microtubule networks and induces microtubule stabilization". The Journal of Cell Biology 155 (6): 1029–42. doi:10.1083/jcb.200104123. PMC 2150914. PMID 11733543.
• Pandey A, Dan I, Kristiansen TZ, Watanabe NM, Voldby J, Kajikawa E, Khosravi-Far R, Blagoev B, Mann M (May 2002). "Cloning and characterization of PAK5, a novel member of mammalian p21-activated kinase-II subfamily that is predominantly expressed in brain". Oncogene 21 (24): 3939–48. doi:10.1038/sj.onc.1205478. PMID 12032833.
• Cotteret S, Jaffer ZM, Beeser A, Chernoff J (Aug 2003). "p21-Activated kinase 5 (Pak5) localizes to mitochondria and inhibits apoptosis by phosphorylating BAD". Molecular and Cellular Biology 23 (16): 5526–39. doi:10.1128/MCB.23.16.5526-5539.2003. PMC 166342. PMID 12897128.
• Matenia D, Griesshaber B, Li XY, Thiessen A, Johne C, Jiao J, Mandelkow E, Mandelkow EM (Sep 2005). "PAK5 kinase is an inhibitor of MARK/Par-1, which leads to stable microtubules and dynamic actin". Molecular Biology of the Cell 16 (9): 4410–22. doi:10.1091/mbc.E05-01-0081. PMC 1196348. PMID 16014608.
• 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 (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Cotteret S, Chernoff J (Apr 2006). "Nucleocytoplasmic shuttling of Pak5 regulates its antiapoptotic properties". Molecular and Cellular Biology 26 (8): 3215–30. doi:10.1128/MCB.26.8.3215-3230.2006. PMC 1446938. PMID 16581795.
• Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.