dbPTM

PAK4_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PAK4_MOUSE
UniProt AC	Q8BTW9
Protein Name	Serine/threonine-protein kinase PAK 4
Gene Name	Pak4
Organism	Mus musculus (Mouse).
Sequence Length	593
Subcellular Localization	Cytoplasm . Seems to shuttle between cytoplasmic compartments depending on the activating effector. For example, can be found on the cell periphery after activation of growth-factor or integrin-mediated signaling pathways.
Protein Description	Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, growth, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates and inactivates the protein phosphatase SSH1, leading to increased inhibitory phosphorylation of the actin binding/depolymerizing factor cofilin. Decreased cofilin activity may lead to stabilization of actin filaments. Phosphorylates LIMK1, a kinase that also inhibits the activity of cofilin. Phosphorylates integrin beta5/ITGB5 and thus regulates cell motility. Phosphorylates ARHGEF2 and activates the downstream target RHOA that plays a role in the regulation of assembly of focal adhesions and actin stress fibers. Stimulates cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Alternatively, inhibits apoptosis by preventing caspase-8 binding to death domain receptors in a kinase independent manner. Plays a role in cell-cycle progression by controlling levels of the cell-cycle regulatory protein CDKN1A and by phosphorylating RAN..
Protein Sequence	MFGKKKKRVEISAPSNFEHRVHTGFDQHEQKFTGLPRQWQSLIEESARRPKPLIDPACITSIQPGAPKTIVRGSKGAKDGALTLLLDEFENMSVTRSNSLRRESPPPPARAHQENGMLEERAAPARMAPDKAGSRARATGHSEAGSGSGDRRRVGPEKRPKSSRDGPGGPQEASRDKRPLSGPDVSTPQPGSLTSGTKLAAGRPFNTYPRADTDHPPRGAQGEPHTMAPNGPSATGLAAPQSSSSSRPPTRARGAPSPGVLGPHASEPQLAPPARALAAPAVPPAPGPPGPRSPQREPQRVSHEQFRAALQLVVDPGDPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYRHENVVEMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALAVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGVMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKASPSLKGFLDRLLVRDPAQRATAAELLKHPFLTKAGPPASIVPLMRQHRTR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
33	Phosphorylation	DQHEQKFTGLPRQWQ CHHHHHHHCCCHHHH	44.86	-
41	Phosphorylation	GLPRQWQSLIEESAR CCCHHHHHHHHHHHC	28.49	-
51	Ubiquitination	EESARRPKPLIDPAC HHHHCCCCCCCCHHH	51.12	22790023
74	Phosphorylation	PKTIVRGSKGAKDGA CCEEEECCCCCCCCC	19.83	-
78	Methylation	VRGSKGAKDGALTLL EECCCCCCCCCEEHH	66.42	-
93	Phosphorylation	LDEFENMSVTRSNSL HHHHHHCCCCCCCCC	31.73	29899451
97	Phosphorylation	ENMSVTRSNSLRRES HHCCCCCCCCCCCCC	22.77	26239621
99	Phosphorylation	MSVTRSNSLRRESPP CCCCCCCCCCCCCCC	25.21	27087446
104	Phosphorylation	SNSLRRESPPPPARA CCCCCCCCCCCCCHH	40.68	25521595
142	Phosphorylation	RARATGHSEAGSGSG CCCCCCCCCCCCCCC	30.41	27717184
146	Phosphorylation	TGHSEAGSGSGDRRR CCCCCCCCCCCCCCC	36.51	27717184
148	Phosphorylation	HSEAGSGSGDRRRVG CCCCCCCCCCCCCCC	38.94	27717184
181	Phosphorylation	SRDKRPLSGPDVSTP CCCCCCCCCCCCCCC	51.46	27087446
186	Phosphorylation	PLSGPDVSTPQPGSL CCCCCCCCCCCCCCC	41.57	25619855
187	Phosphorylation	LSGPDVSTPQPGSLT CCCCCCCCCCCCCCC	26.28	25619855
192	Phosphorylation	VSTPQPGSLTSGTKL CCCCCCCCCCCCCEE	34.85	25619855
194	Phosphorylation	TPQPGSLTSGTKLAA CCCCCCCCCCCEECC	27.14	25619855
195	Phosphorylation	PQPGSLTSGTKLAAG CCCCCCCCCCEECCC	50.16	25619855
197	Phosphorylation	PGSLTSGTKLAAGRP CCCCCCCCEECCCCC	23.74	25619855
207	Phosphorylation	AAGRPFNTYPRADTD CCCCCCCCCCCCCCC	34.97	22322096
208	Phosphorylation	AGRPFNTYPRADTDH CCCCCCCCCCCCCCC	7.57	24899341
257	Phosphorylation	TRARGAPSPGVLGPH CCCCCCCCCCCCCCC	33.48	26824392
266	Phosphorylation	GVLGPHASEPQLAPP CCCCCCCCCCCCCCC	46.94	27087446
293	Phosphorylation	PGPPGPRSPQREPQR CCCCCCCCCCCCCCC	28.63	26824392
476	Phosphorylation	KEVPRRKSLVGTPYW CCCCCHHHCCCCCCC	26.86	25521595
480	Phosphorylation	RRKSLVGTPYWMAPE CHHHCCCCCCCCCHH	13.01	22322096
482	Phosphorylation	KSLVGTPYWMAPELI HHCCCCCCCCCHHHH	13.98	26239621
484	Oxidation	LVGTPYWMAPELISR CCCCCCCCCHHHHHC	3.53	17242355
490	Phosphorylation	WMAPELISRLPYGPE CCCHHHHHCCCCCCC	40.15	25777480
548	Ubiquitination	HKASPSLKGFLDRLL HHCCHHHHHHHHHHH	52.53	22790023

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
476	S	Phosphorylation	Kinase	PAK4	Q8BTW9	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PAK4_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of PAK4_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of PAK4_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PAK4_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND MASSSPECTROMETRY.	19367708 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476, AND MASSSPECTROMETRY.	17242355 [Abstract]
"Phosphoproteomic analysis of the developing mouse brain."; Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; Mol. Cell. Proteomics 3:1093-1101(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476, AND MASSSPECTROMETRY.	15345747 [Abstract]
"p21-activated protein kinase 4 (PAK4) interacts with the keratinocytegrowth factor receptor and participates in keratinocyte growth factor-mediated inhibition of oxidant-induced cell death."; Lu Y., Pan Z.-Z., Devaux Y., Ray P.; J. Biol. Chem. 278:10374-10380(2003). Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH FGFR2 AND GRB2, ANDPHOSPHORYLATION AT TYROSINE RESIDUES.	12529371 [Abstract]