PAK4_HUMAN - dbPTM
PAK4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PAK4_HUMAN
UniProt AC O96013
Protein Name Serine/threonine-protein kinase PAK 4
Gene Name PAK4
Organism Homo sapiens (Human).
Sequence Length 591
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 MFGKRKKRVEISAPSNFEHRVHTGFDQHEQKFTGLPRQWQSLIEESARRPKPLVDPACITSIQPGAPKTIVRGSKGAKDGALTLLLDEFENMSVTRSNSLRRDSPPPPARARQENGMPEEPATTARGGPGKAGSRGRFAGHSEAGGGSGDRRRAGPEKRPKSSREGSGGPQESSRDKRPLSGPDVGTPQPAGLASGAKLAAGRPFNTYPRADTDHPSRGAQGEPHDVAPNGPSAGGLAIPQSSSSSSRPPTRARGAPSPGVLGPHASEPQLAPPACTPAAPAVPGPPGPRSPQREPQRVSHEQFRAALQLVVDPGDPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPASIVPLMRQNRTR
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
23PhosphorylationNFEHRVHTGFDQHEQ
CCCHHCCCCCCHHHH		36.3728555341
31 (in isoform 4)Ubiquitination-41.7421890473
31 (in isoform 3)Ubiquitination-41.7421890473
31UbiquitinationGFDQHEQKFTGLPRQ
CCCHHHHHHHCCCHH		41.7421890473
31 (in isoform 1)Ubiquitination-41.7421890473
31 (in isoform 2)Ubiquitination-41.7421890473
33PhosphorylationDQHEQKFTGLPRQWQ
CHHHHHHHCCCHHHH		44.8624719451
41 (in isoform 3)Phosphorylation-28.49-
41PhosphorylationGLPRQWQSLIEESAR
CCCHHHHHHHHHHHC		28.4922617229
46PhosphorylationWQSLIEESARRPKPL
HHHHHHHHHCCCCCC		17.8123186163
60PhosphorylationLVDPACITSIQPGAP
CCCHHHCCCCCCCCC		21.4725850435
61PhosphorylationVDPACITSIQPGAPK
CCHHHCCCCCCCCCC		10.1824719451
69PhosphorylationIQPGAPKTIVRGSKG
CCCCCCCEEEECCCC		24.5227251275
74PhosphorylationPKTIVRGSKGAKDGA
CCEEEECCCCCCCCC		19.8324719451
78MethylationVRGSKGAKDGALTLL
EECCCCCCCCCEEHH		66.4224129315
93PhosphorylationLDEFENMSVTRSNSL
HHHHHCCCCCCCCCC		31.7324719451
97PhosphorylationENMSVTRSNSLRRDS
HCCCCCCCCCCCCCC		22.7726846344
99PhosphorylationMSVTRSNSLRRDSPP
CCCCCCCCCCCCCCC		25.2126846344
104PhosphorylationSNSLRRDSPPPPARA
CCCCCCCCCCCCHHH		37.1829255136
105 (in isoform 3)Phosphorylation-50.10-
114 (in isoform 3)Phosphorylation-50.64-
117SulfoxidationRARQENGMPEEPATT
HHHHHCCCCCCCCCC		5.9521406390
123PhosphorylationGMPEEPATTARGGPG
CCCCCCCCCCCCCCC		31.5329255136
124PhosphorylationMPEEPATTARGGPGK
CCCCCCCCCCCCCCC		19.2329255136
124 (in isoform 3)Phosphorylation-19.23-
126MethylationEEPATTARGGPGKAG
CCCCCCCCCCCCCCC		48.8182797081
138 (in isoform 3)Phosphorylation-12.14-
142PhosphorylationRGRFAGHSEAGGGSG
CCCCCCCCCCCCCCC		28.3721082442
148PhosphorylationHSEAGGGSGDRRRAG
CCCCCCCCCCCCCCC		40.5729255136
162PhosphorylationGPEKRPKSSREGSGG
CCCCCCCCCCCCCCC		36.9928102081
163PhosphorylationPEKRPKSSREGSGGP
CCCCCCCCCCCCCCC		40.2428102081
167PhosphorylationPKSSREGSGGPQESS
CCCCCCCCCCCCCCC		35.5029255136
173PhosphorylationGSGGPQESSRDKRPL
CCCCCCCCCCCCCCC		25.9828857561
174PhosphorylationSGGPQESSRDKRPLS
CCCCCCCCCCCCCCC		43.6928857561
181PhosphorylationSRDKRPLSGPDVGTP
CCCCCCCCCCCCCCC		51.4629255136
187PhosphorylationLSGPDVGTPQPAGLA
CCCCCCCCCCCCCHH		20.7129255136
189 (in isoform 3)Phosphorylation-40.07-
195PhosphorylationPQPAGLASGAKLAAG
CCCCCHHCCCCCCCC		44.3025159151
207PhosphorylationAAGRPFNTYPRADTD
CCCCCCCCCCCCCCC		34.9722322096
208PhosphorylationAGRPFNTYPRADTDH
CCCCCCCCCCCCCCC		7.5721945579
213PhosphorylationNTYPRADTDHPSRGA
CCCCCCCCCCCCCCC		34.9123403867
217PhosphorylationRADTDHPSRGAQGEP
CCCCCCCCCCCCCCC		39.6723186163
242PhosphorylationGGLAIPQSSSSSSRP
CCCCCCCCCCCCCCC		27.1718691976
243PhosphorylationGLAIPQSSSSSSRPP
CCCCCCCCCCCCCCC		29.0627251275
244PhosphorylationLAIPQSSSSSSRPPT
CCCCCCCCCCCCCCC		39.2127251275
245PhosphorylationAIPQSSSSSSRPPTR
CCCCCCCCCCCCCCC		33.9927251275
246PhosphorylationIPQSSSSSSRPPTRA
CCCCCCCCCCCCCCC		32.1127251275
247PhosphorylationPQSSSSSSRPPTRAR
CCCCCCCCCCCCCCC		51.2428348404
251PhosphorylationSSSSRPPTRARGAPS
CCCCCCCCCCCCCCC		39.3824719451
254MethylationSRPPTRARGAPSPGV
CCCCCCCCCCCCCCC		38.22115486383
258PhosphorylationTRARGAPSPGVLGPH
CCCCCCCCCCCCCCC		33.4829255136
267PhosphorylationGVLGPHASEPQLAPP
CCCCCCCCCCCCCCC		46.9429255136
277PhosphorylationQLAPPACTPAAPAVP
CCCCCCCCCCCCCCC		20.3322617229
291PhosphorylationPGPPGPRSPQREPQR
CCCCCCCCCCCCCCC		28.6323401153
321 (in isoform 3)Phosphorylation-4.59-
325 (in isoform 3)Phosphorylation-3.89-
327 (in isoform 3)Phosphorylation-5.33-
342PhosphorylationVCIATVRSSGKLVAV
EEEEEEECCCEEEEE		38.8220068231
343PhosphorylationCIATVRSSGKLVAVK
EEEEEECCCEEEEEE		29.4120068231
443PhosphorylationVIHRDIKSDSILLTH
CCCCCCCCCEEEEEE		36.6027251275
445PhosphorylationHRDIKSDSILLTHDG
CCCCCCCEEEEEECC		23.4020873877
455AcetylationLTHDGRVKLSDFGFC
EEECCCEEECCCCEE		40.6968397
467AcetylationGFCAQVSKEVPRRKS
CEEEEECCCCCCHHH		64.9768401
474PhosphorylationKEVPRRKSLVGTPYW
CCCCCHHHCCCCCCC		26.8622322096
478PhosphorylationRRKSLVGTPYWMAPE
CHHHCCCCCCCCCHH		13.0122322096
480PhosphorylationKSLVGTPYWMAPELI
HHCCCCCCCCCHHHH		13.9823927012
488PhosphorylationWMAPELISRLPYGPE
CCCHHHHHCCCCCCC		40.1523927012
540UbiquitinationPRLKNLHKVSPSLKG
HHHHHHHHCCHHHHH		47.80-
544PhosphorylationNLHKVSPSLKGFLDR
HHHHCCHHHHHHHHH		34.9024719451
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
99SPhosphorylationKinasePRKD1Q15139
PSP
99SPhosphorylationKinasePRKD2Q9BZL6
PSP
474SPhosphorylationKinasePRKD1Q15139
PSP
474SPhosphorylationKinasePAK4O96013
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PAK4_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDC42_HUMANCDC42physical
17353931
ODO2_HUMANDLSTphysical
16169070
LIMK1_HUMANLIMK1physical
11413130
RAC1_HUMANRAC1physical
11756552
CDC42_HUMANCDC42physical
11756552
ITB5_HUMANITGB5physical
12356872
RAN_HUMANRANphysical
20805321
A4_HUMANAPPphysical
21832049
SH3R2_HUMANSH3RF2physical
24130170
PAK6_HUMANPAK6physical
26186194
PAK5_HUMANPAK7physical
26186194
CARL1_HUMANLRRC16Aphysical
26186194
ARHGB_HUMANARHGEF11physical
26186194
SPT5H_HUMANSUPT5Hphysical
26186194
GGNB2_HUMANGGNBP2physical
26186194
KLH42_HUMANKLHL42physical
26186194
NAA20_HUMANNAA20physical
26344197
NAA25_HUMANNAA25physical
26344197
PPM1B_HUMANPPM1Bphysical
26344197
RHOU_HUMANRHOUphysical
26598620
PAK4_HUMANPAK4physical
26598620
PAXI_HUMANPXNphysical
26598620
VINC_HUMANVCLphysical
26598620
RHOV_HUMANRHOVphysical
26598620
CDC42_HUMANCDC42physical
26598620
H11_HUMANHIST1H1Aphysical
26598620
MMP2_HUMANMMP2physical
23254288
ITB3_HUMANITGB3physical
23254288
ITAV_HUMANITGAVphysical
23254288
MMP2_HUMANMMP2genetic
23254288
ARHGB_HUMANARHGEF11physical
28514442
CARL1_HUMANLRRC16Aphysical
28514442
PAK6_HUMANPAK6physical
28514442
GGNB2_HUMANGGNBP2physical
28514442
CDK6_HUMANCDK6physical
28514442
KLH42_HUMANKLHL42physical
28514442
KCTD3_HUMANKCTD3physical
27173435
KI13B_HUMANKIF13Bphysical
27173435
CBY1_HUMANCBY1physical
27173435
RAB3I_HUMANRAB3IPphysical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PAK4_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-474, ANDMASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-104; SER-142;SER-148; SER-167; SER-181; THR-187; SER-195; THR-207; SER-242;SER-258; SER-267; SER-291 AND SER-474, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-474, ANDMASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-104; SER-148;SER-167; SER-181; THR-187; THR-207; SER-258; SER-267; THR-277; SER-291AND SER-474, AND MASS SPECTROMETRY.
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry.";
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.;
Mol. Cell. Proteomics 6:537-547(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-104; SER-148;SER-167; SER-181; THR-207; SER-267; SER-291 AND SER-474, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474, AND MASSSPECTROMETRY.

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