PAK5_HUMAN - dbPTM
PAK5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PAK5_HUMAN
UniProt AC Q9P286
Protein Name Serine/threonine-protein kinase PAK 5 {ECO:0000305}
Gene Name PAK5 {ECO:0000312|HGNC:HGNC:15916}
Organism Homo sapiens (Human).
Sequence Length 719
Subcellular Localization Mitochondrion. Cytoplasm. Nucleus. Shuttles between the nucleus and the mitochondria, and mitochondrial localization is essential for the role in cell survival.
Protein Description Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, 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 the proto-oncogene RAF1 and stimulates its kinase activity. Promotes cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Phosphorylates CTNND1, probably to regulate cytoskeletal organization and cell morphology. Keeps microtubules stable through MARK2 inhibition and destabilizes the F-actin network leading to the disappearance of stress fibers and focal adhesions..
Protein Sequence MFGKKKKKIEISGPSNFEHRVHTGFDPQEQKFTGLPQQWHSLLADTANRPKPMVDPSCITPIQLAPMKTIVRGNKPCKETSINGLLEDFDNISVTRSNSLRKESPPTPDQGASSHGPGHAEENGFITFSQYSSESDTTADYTTEKYREKSLYGDDLDPYYRGSHAAKQNGHVMKMKHGEAYYSEVKPLKSDFARFSADYHSHLDSLSKPSEYSDLKWEYQRASSSSPLDYSFQFTPSRTAGTSGCSKESLAYSESEWGPSLDDYDRRPKSSYLNQTSPQPTMRQRSRSGSGLQEPMMPFGASAFKTHPQGHSYNSYTYPRLSEPTMCIPKVDYDRAQMVLSPPLSGSDTYPRGPAKLPQSQSKSGYSSSSHQYPSGYHKATLYHHPSLQSSSQYISTASYLSSLSLSSSTYPPPSWGSSSDQQPSRVSHEQFRAALQLVVSPGDPREYLANFIKIGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRRELLFNEVVIMRDYHHDNVVDMYSSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPKRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRDSLPPRVKDLHKVSSVLRGFLDLMLVREPSQRATAQELLGHPFLKLAGPPSCIVPLMRQYRHH
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
104PhosphorylationSNSLRKESPPTPDQG
CCCCCCCCCCCCCCC
-
107PhosphorylationLRKESPPTPDQGASS
CCCCCCCCCCCCCCC
-
113PhosphorylationPTPDQGASSHGPGHA
CCCCCCCCCCCCCCC
30576142
127PhosphorylationAEENGFITFSQYSSE
CHHCCEEEEEECCCC
30576142
141PhosphorylationESDTTADYTTEKYRE
CCCCCCCCCCHHHHH
30576142
150PhosphorylationTEKYREKSLYGDDLD
CHHHHHHHCCCCCCC
27732954
152PhosphorylationKYREKSLYGDDLDPY
HHHHHHCCCCCCCHH
27732954
159PhosphorylationYGDDLDPYYRGSHAA
CCCCCCHHHCCHHHH
25884760
160PhosphorylationGDDLDPYYRGSHAAK
CCCCCHHHCCHHHHH
22817900
167AcetylationYRGSHAAKQNGHVMK
HCCHHHHHHCCEEEE
11794157
182PhosphorylationMKHGEAYYSEVKPLK
CCCCCEECCCCCCCC
25884760
183PhosphorylationKHGEAYYSEVKPLKS
CCCCEECCCCCCCCC
25884760
223PhosphorylationKWEYQRASSSSPLDY
CCEEECCCCCCCCCE
27732954
224PhosphorylationWEYQRASSSSPLDYS
CEEECCCCCCCCCEE
22617229
225PhosphorylationEYQRASSSSPLDYSF
EEECCCCCCCCCEEE
27732954
226PhosphorylationYQRASSSSPLDYSFQ
EECCCCCCCCCEEEE
22617229
230PhosphorylationSSSSPLDYSFQFTPS
CCCCCCCEEEEECCC
27732954
231PhosphorylationSSSPLDYSFQFTPSR
CCCCCCEEEEECCCC
27732954
235PhosphorylationLDYSFQFTPSRTAGT
CCEEEEECCCCCCCC
27732954
237PhosphorylationYSFQFTPSRTAGTSG
EEEEECCCCCCCCCC
27732954
249PhosphorylationTSGCSKESLAYSESE
CCCCCHHHHCCCCCC
27732954
252PhosphorylationCSKESLAYSESEWGP
CCHHHHCCCCCCCCC
27732954
253PhosphorylationSKESLAYSESEWGPS
CHHHHCCCCCCCCCC
27732954
255PhosphorylationESLAYSESEWGPSLD
HHHCCCCCCCCCCHH
27732954
270PhosphorylationDYDRRPKSSYLNQTS
HCCCCCCCHHCCCCC
27732954
271PhosphorylationYDRRPKSSYLNQTSP
CCCCCCCHHCCCCCC
27732954
272PhosphorylationDRRPKSSYLNQTSPQ
CCCCCCHHCCCCCCC
22817900
276PhosphorylationKSSYLNQTSPQPTMR
CCHHCCCCCCCCCCC
27732954
277PhosphorylationSSYLNQTSPQPTMRQ
CHHCCCCCCCCCCCC
27732954
281PhosphorylationNQTSPQPTMRQRSRS
CCCCCCCCCCCCCCC
29083192
285MethylationPQPTMRQRSRSGSGL
CCCCCCCCCCCCCCC
24161617
285DimethylationPQPTMRQRSRSGSGL
CCCCCCCCCCCCCCC
-
286PhosphorylationQPTMRQRSRSGSGLQ
CCCCCCCCCCCCCCC
25884760
288PhosphorylationTMRQRSRSGSGLQEP
CCCCCCCCCCCCCCC
27732954
290PhosphorylationRQRSRSGSGLQEPMM
CCCCCCCCCCCCCCC
25884760
345PhosphorylationMVLSPPLSGSDTYPR
EEECCCCCCCCCCCC
-
347PhosphorylationLSPPLSGSDTYPRGP
ECCCCCCCCCCCCCC
-
349PhosphorylationPPLSGSDTYPRGPAK
CCCCCCCCCCCCCCC
-
350PhosphorylationPLSGSDTYPRGPAKL
CCCCCCCCCCCCCCC
-
551PhosphorylationQIATVCLSVLRALSY
HHHHHHHHHHHHHHH
24719451
573PhosphorylationHRDIKSDSILLTSDG
CCCCCCCEEEEECCC
22817900
602PhosphorylationKEVPKRKSLVGTPYW
CCCCCCCCCCCCCCC
22322096
606PhosphorylationKRKSLVGTPYWMAPE
CCCCCCCCCCCCCHH
25106551
608PhosphorylationKSLVGTPYWMAPEVI
CCCCCCCCCCCHHHH
28176443
616PhosphorylationWMAPEVISRLPYGTE
CCCHHHHHCCCCCCC
28176443
658PhosphorylationAMRRIRDSLPPRVKD
HHHHHHHCCCCCHHH
24719451

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
573SPhosphorylationKinasePAK5Q9P286
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PAK5_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 PAK5_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LZTS2_HUMANLZTS2physical
16189514
S10A9_HUMANS100A9physical
17353931
S10A7_HUMANS100A7physical
17353931
RFA3_HUMANRPA3physical
17353931
AP2S1_HUMANAP2S1physical
17353931
TAP26_HUMANCCDC59physical
17353931
RAC1_HUMANRAC1physical
11756552
CDC42_HUMANCDC42physical
11756552
CARD9_HUMANCARD9physical
25416956
LENG1_HUMANLENG1physical
25416956
GCC1_HUMANGCC1physical
25416956
ARMC7_HUMANARMC7physical
25416956
ATPF2_HUMANATPAF2physical
25416956
INKA1_HUMANFAM212Aphysical
25416956
PAK5_HUMANPAK7physical
27499296
MIPEP_HUMANMIPEPphysical
27499296
COA7_HUMANCOA7physical
27499296
IDE_HUMANIDEphysical
27499296
CHCH2_HUMANCHCHD2physical
27499296
HTRA2_HUMANHTRA2physical
27499296
MPPA_HUMANPMPCAphysical
27499296
XPP3_HUMANXPNPEP3physical
27499296
TTC19_HUMANTTC19physical
27499296
ATP5H_HUMANATP5Hphysical
27499296
MPPB_HUMANPMPCBphysical
27499296
CLPB_HUMANCLPBphysical
27499296
GLUCM_HUMANC14orf159physical
27499296
NDUV1_HUMANNDUFV1physical
27499296
PREP_HUMANPITRM1physical
27499296
SCOT1_HUMANOXCT1physical
27499296
PDIP2_HUMANPOLDIP2physical
27499296
ATPO_HUMANATP5Ophysical
27499296
C1QBP_HUMANC1QBPphysical
27499296
PAK4_HUMANPAK4physical
28514442
ARHGB_HUMANARHGEF11physical
28514442
CARL1_HUMANLRRC16Aphysical
28514442
ARHG2_HUMANARHGEF2physical
28514442
MAP12_HUMANMETAP1Dphysical
28514442
TBD2B_HUMANTBC1D2Bphysical
28514442
TANC2_HUMANTANC2physical
28514442
OBSL1_HUMANOBSL1physical
28514442
SPT5H_HUMANSUPT5Hphysical
28514442
AMZ2_HUMANAMZ2physical
28514442
FBLN1_HUMANFBLN1physical
28514442
ZN598_HUMANZNF598physical
28514442
AURKA_HUMANAURKAphysical
28514442
GMPPA_HUMANGMPPAphysical
28514442
1433Z_HUMANYWHAZphysical
28514442
RM39_HUMANMRPL39physical
28514442
PLK1_HUMANPLK1physical
28514442
GALD1_HUMANPDDC1physical
28514442
UBP7_HUMANUSP7physical
28514442
RBM6_HUMANRBM6physical
28514442
UBR2_HUMANUBR2physical
28514442
SPT4H_HUMANSUPT4H1physical
28514442
CC138_HUMANCCDC138physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PAK5_HUMAN

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Related Literatures of Post-Translational Modification

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