PAK3_HUMAN - dbPTM
PAK3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PAK3_HUMAN
UniProt AC O75914
Protein Name Serine/threonine-protein kinase PAK 3
Gene Name PAK3
Organism Homo sapiens (Human).
Sequence Length 559
Subcellular Localization Cytoplasm.
Protein Description Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, or cell cycle regulation. Plays a role in dendrite spine morphogenesis as well as synapse formation and plasticity. Acts as downstream effector of the small GTPases CDC42 and RAC1. Activation by the binding of active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration. Additionally, phosphorylates TNNI3/troponin I to modulate calcium sensitivity and relaxation kinetics of thin myofilaments. May also be involved in early neuronal development..
Protein Sequence MSDGLDNEEKPPAPPLRMNSNNRDSSALNHSSKPLPMAPEEKNKKARLRSIFPGGGDKTNKKKEKERPEISLPSDFEHTIHVGFDAVTGEFTPDLYGSQMCPGKLPEGIPEQWARLLQTSNITKLEQKKNPQAVLDVLKFYDSKETVNNQKYMSFTSGDKSAHGYIAAHPSSTKTASEPPLAPPVSEEEDEEEEEEEDENEPPPVIAPRPEHTKSIYTRSVVESIASPAVPNKEVTPPSAENANSSTLYRNTDRQRKKSKMTDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPERLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLKLAKPLSSLTPLIIAAKEAIKNSSR
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
2Phosphorylation------MSDGLDNEE
------CCCCCCCCC		40.1522617229
32PhosphorylationSSALNHSSKPLPMAP
CCCCCCCCCCCCCCC		30.6424719451
50PhosphorylationNKKARLRSIFPGGGD
CHHHHHHHHCCCCCC		32.9220068231
58UbiquitinationIFPGGGDKTNKKKEK
HCCCCCCCCCCCCCC		58.22-
59PhosphorylationFPGGGDKTNKKKEKE
CCCCCCCCCCCCCCC		57.9420068231
62UbiquitinationGGDKTNKKKEKERPE
CCCCCCCCCCCCCCC		69.13-
71PhosphorylationEKERPEISLPSDFEH
CCCCCCCCCCCCCCC		32.3427732954
74PhosphorylationRPEISLPSDFEHTIH
CCCCCCCCCCCCEEE		61.2927732954
79PhosphorylationLPSDFEHTIHVGFDA
CCCCCCCEEEECCEE		12.9414707132
109 (in isoform 2)Ubiquitination-3.0221890473
119PhosphorylationQWARLLQTSNITKLE
HHHHHHHHCCCHHHH		24.5820068231
120PhosphorylationWARLLQTSNITKLEQ
HHHHHHHCCCHHHHH		17.1828857561
123PhosphorylationLLQTSNITKLEQKKN
HHHHCCCHHHHHCCC		33.5528122231
124UbiquitinationLQTSNITKLEQKKNP
HHHCCCHHHHHCCCH		46.35-
124 (in isoform 1)Ubiquitination-46.3521890473
124UbiquitinationLQTSNITKLEQKKNP
HHHCCCHHHHHCCCH		46.3521890473
124AcetylationLQTSNITKLEQKKNP
HHHCCCHHHHHCCCH		46.3525953088
130UbiquitinationTKLEQKKNPQAVLDV
HHHHHCCCHHHHHHH		40.7421890473
139 (in isoform 2)Phosphorylation-41.5511278486
145UbiquitinationLKFYDSKETVNNQKY
HHHHCCCCCCCCEEE		63.0421890473
146PhosphorylationKFYDSKETVNNQKYM
HHHCCCCCCCCEEEE		32.0730576142
150 (in isoform 3)Ubiquitination-32.81-
154PhosphorylationVNNQKYMSFTSGDKS
CCCEEEEEEECCCCC		23.4517077177
156PhosphorylationNQKYMSFTSGDKSAH
CEEEEEEECCCCCCC		25.2130576142
171PhosphorylationGYIAAHPSSTKTASE
EEEEECCCCCCCCCC		40.5530576142
186PhosphorylationPPLAPPVSEEEDEEE
CCCCCCCCHHHCHHH		45.0925921289
217PhosphorylationPEHTKSIYTRSVVES
HHCCCCCHHHHHHHH		11.82-
218PhosphorylationEHTKSIYTRSVVESI
HCCCCCHHHHHHHHH		18.13-
220PhosphorylationTKSIYTRSVVESIAS
CCCCHHHHHHHHHCC		23.7927499020
236PhosphorylationAVPNKEVTPPSAENA
CCCCCCCCCCCCCCC		30.4922210691
239PhosphorylationNKEVTPPSAENANSS
CCCCCCCCCCCCCCC		49.7922210691
257AcetylationRNTDRQRKKSKMTDE
CCCHHHHHHHCCCHH		53.7319822031
259PhosphorylationTDRQRKKSKMTDEEI
CHHHHHHHCCCHHHH		30.6017077177
269AcetylationTDEEILEKLRSIVSV
CHHHHHHHHHHHHCC		45.8419822041
272PhosphorylationEILEKLRSIVSVGDP
HHHHHHHHHHCCCCC		37.4728348404
275PhosphorylationEKLRSIVSVGDPKKK
HHHHHHHCCCCCCCC		20.79-
284PhosphorylationGDPKKKYTRFEKIGQ
CCCCCCEECCEEECC		37.4529496963
298PhosphorylationQGASGTVYTALDIAT
CCCCCCEEEEEHHHC		6.02-
322UbiquitinationNLQQQPKKELIINEI
CCCCCCCHHHEEEEH		65.52-
404UbiquitinationQVIHRDIKSDNILLG
CCEECCCCCCCEEEC		56.92-
412SulfoxidationSDNILLGMDGSVKLT
CCCEEECCCCCEEEC		5.4921406390
418 (in isoform 2)Ubiquitination-5.3521890473
421 (in isoform 2)Phosphorylation-7.3311278486
425 (in isoform 3)Ubiquitination-11.10-
428PhosphorylationFGFCAQITPEQSKRS
CCEEEECCHHHHCCC		14.5325159151
432PhosphorylationAQITPEQSKRSTMVG
EECCHHHHCCCCCCC		28.5128787133
433AcetylationQITPEQSKRSTMVGT
ECCHHHHCCCCCCCC		50.4924179677
433 (in isoform 1)Ubiquitination-50.4921890473
433UbiquitinationQITPEQSKRSTMVGT
ECCHHHHCCCCCCCC		50.4921906983
435PhosphorylationTPEQSKRSTMVGTPY
CHHHHCCCCCCCCCC		25.2927461979
436PhosphorylationPEQSKRSTMVGTPYW
HHHHCCCCCCCCCCC		21.6522153498
440PhosphorylationKRSTMVGTPYWMAPE
CCCCCCCCCCCCCCH		11.2023401153
442PhosphorylationSTMVGTPYWMAPEVV
CCCCCCCCCCCCHHH		13.9823401153
450PhosphorylationWMAPEVVTRKAYGPK
CCCCHHHCCCCCCCC		31.4623401153
477PhosphorylationMVEGEPPYLNENPLR
ECCCCCCCCCCCHHH		32.64-
487PhosphorylationENPLRALYLIATNGT
CCHHHHHHHHHCCCC		8.6219534553
511 (in isoform 2)Ubiquitination-4.6521890473
520 (in isoform 2)Ubiquitination-30.2321890473
524PhosphorylationMDVDRRGSAKELLQH
CCCCCCCCHHHHHCC		34.0623312004
526UbiquitinationVDRRGSAKELLQHPF
CCCCCCHHHHHCCHH		51.062190698
526 (in isoform 1)Ubiquitination-51.0621890473
535UbiquitinationLLQHPFLKLAKPLSS
HHCCHHHHHHCCHHH		46.9421890473
535AcetylationLLQHPFLKLAKPLSS
HHCCHHHHHHCCHHH		46.9425953088
535 (in isoform 1)Ubiquitination-46.9421890473
535UbiquitinationLLQHPFLKLAKPLSS
HHCCHHHHHHCCHHH		46.94-
541PhosphorylationLKLAKPLSSLTPLII
HHHHCCHHHCHHHHH		31.6520068231
541UbiquitinationLKLAKPLSSLTPLII
HHHHCCHHHCHHHHH		31.6521890473
556UbiquitinationAAKEAIKNSSR----
HHHHHHHCCCC----		38.8221890473
558PhosphorylationKEAIKNSSR------
HHHHHCCCC------		51.94-
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
50SPhosphorylationKinasePAK3 ISOFORM 2-GPS
139SPhosphorylationKinasePAK3O75914
PhosphoELM
421TPhosphorylationKinasePAK3O75914
PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PAK3_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 PAK3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARHG7_HUMANARHGEF7physical
9726964
ITSN1_HUMANITSN1physical
15824104
CDC42_HUMANCDC42physical
15824104
RAC1_HUMANRAC1physical
25301945
PAK3_HUMANPAK3physical
18082144
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
300558Mental retardation, X-linked 30 (MRX30)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PAK3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-535, AND MASS SPECTROMETRY.

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