TAOK2_HUMAN - dbPTM
TAOK2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TAOK2_HUMAN
UniProt AC Q9UL54
Protein Name Serine/threonine-protein kinase TAO2
Gene Name TAOK2
Organism Homo sapiens (Human).
Sequence Length 1235
Subcellular Localization Cytoplasmic vesicle membrane
Multi-pass membrane protein . Cytoplasm, cytoskeleton. Nucleus. Catalytically active full-length phosphorylated isoform 1 localizes to microtubules in the cytoplasm predominantly on microtubule cables positioned around
Protein Description Serine/threonine-protein kinase involved in different processes such as membrane blebbing and apoptotic bodies formation DNA damage response and MAPK14/p38 MAPK stress-activated MAPK cascade. Phosphorylates itself, MBP, activated MAPK8, MAP2K3, MAP2K6 and tubulins. Activates the MAPK14/p38 MAPK signaling pathway through the specific activation and phosphorylation of the upstream MAP2K3 and MAP2K6 kinases. In response to DNA damage, involved in the G2/M transition DNA damage checkpoint by activating the p38/MAPK14 stress-activated MAPK cascade, probably by mediating phosphorylation of upstream MAP2K3 and MAP2K6 kinases. Isoform 1, but not isoform 2, plays a role in apoptotic morphological changes, including cell contraction, membrane blebbing and apoptotic bodies formation. This function, which requires the activation of MAPK8/JNK and nuclear localization of C-terminally truncated isoform 1, may be linked to the mitochondrial CASP9-associated death pathway. Isoform 1 binds to microtubules and affects their organization and stability independently of its kinase activity. Prevents MAP3K7-mediated activation of CHUK, and thus NF-kappa-B activation, but not that of MAPK8/JNK. May play a role in the osmotic stress-MAPK8 pathway. Isoform 2, but not isoform 1, is required for PCDH8 endocytosis. Following homophilic interactions between PCDH8 extracellular domains, isoform 2 phosphorylates and activates MAPK14/p38 MAPK which in turn phosphorylates isoform 2. This process leads to PCDH8 endocytosis and CDH2 cointernalization. Both isoforms are involved in MAPK14 phosphorylation..
Protein Sequence MPAGGRAGSLKDPDVAELFFKDDPEKLFSDLREIGHGSFGAVYFARDVRNSEVVAIKKMSYSGKQSNEKWQDIIKEVRFLQKLRHPNTIQYRGCYLREHTAWLVMEYCLGSASDLLEVHKKPLQEVEIAAVTHGALQGLAYLHSHNMIHRDVKAGNILLSEPGLVKLGDFGSASIMAPANSFVGTPYWMAPEVILAMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPVLQSGHWSEYFRNFVDSCLQKIPQDRPTSEVLLKHRFVLRERPPTVIMDLIQRTKDAVRELDNLQYRKMKKILFQEAPNGPGAEAPEEEEEAEPYMHRAGTLTSLESSHSVPSMSISASSQSSSVNSLADASDNEEEEEEEEEEEEEEEGPEAREMAMMQEGEHTVTSHSSIIHRLPGSDNLYDDPYQPEITPSPLQPPAAPAPTSTTSSARRRAYCRNRDHFATIRTASLVSRQIQEHEQDSALREQLSGYKRMRRQHQKQLLALESRLRGEREEHSARLQRELEAQRAGFGAEAEKLARRHQAIGEKEARAAQAEERKFQQHILGQQKKELAALLEAQKRTYKLRKEQLKEELQENPSTPKREKAEWLLRQKEQLQQCQAEEEAGLLRRQRQYFELQCRQYKRKMLLARHSLDQDLLREDLNKKQTQKDLECALLLRQHEATRELELRQLQAVQRTRAELTRLQHQTELGNQLEYNKRREQELRQKHAAQVRQQPKSLKVRAGQRPPGLPLPIPGALGPPNTGTPIEQQPCSPGQEAVLDQRMLGEEEEAVGERRILGKEGATLEPKQQRILGEESGAPSPSPQKHGSLVDEEVWGLPEEIEELRVPSLVPQERSIVGQEEAGTWSLWGKEDESLLDEEFELGWVQGPALTPVPEEEEEEEEGAPIGTPRDPGDGCPSPDIPPEPPPTHLRPCPASQLPGLLSHGLLAGLSFAVGSSSGLLPLLLLLLLPLLAAQGGGGLQAALLALEVGLVGLGASYLLLCTALHLPSSLFLLLAQGTALGAVLGLSWRRGLMGVPLGLGAAWLLAWPGLALPLVAMAAGGRWVRQQGPRVRRGISRLWLRVLLRLSPMAFRALQGCGAVGDRGLFALYPKTNKDGFRSRLPVPGPRRRNPRTTQHPLALLARVWVLCKGWNWRLARASQGLASHLPPWAIHTLASWGLLRGERPTRIPRLLPRSQRQLGPPASRQPLPGTLAGRRSRTRQSRALPPWR
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
9PhosphorylationPAGGRAGSLKDPDVA
CCCCCCCCCCCCCHH		31.1229255136
11UbiquitinationGGRAGSLKDPDVAEL
CCCCCCCCCCCHHHH		69.7629967540
21UbiquitinationDVAELFFKDDPEKLF
CHHHHHCCCCHHHHH		54.6229967540
26UbiquitinationFFKDDPEKLFSDLRE
HCCCCHHHHHHHHHH		61.2929967540
29PhosphorylationDDPEKLFSDLREIGH
CCHHHHHHHHHHHCC		46.2824719451
38PhosphorylationLREIGHGSFGAVYFA
HHHHCCCCCCCEEEE		18.16-
43PhosphorylationHGSFGAVYFARDVRN
CCCCCCEEEEECCCC		7.3228152594
60PhosphorylationVVAIKKMSYSGKQSN
EEEEEECCCCCCCCH		25.6522468782
61PhosphorylationVAIKKMSYSGKQSNE
EEEEECCCCCCCCHH		20.2422468782
64AcetylationKKMSYSGKQSNEKWQ
EECCCCCCCCHHHHH		44.617823363
69AcetylationSGKQSNEKWQDIIKE
CCCCCHHHHHHHHHH		55.177823377
69UbiquitinationSGKQSNEKWQDIIKE
CCCCCHHHHHHHHHH		55.1729967540
107PhosphorylationTAWLVMEYCLGSASD
HHHHHHHHHHCCHHH		3.7822817900
153 (in isoform 2)Ubiquitination-55.6621906983
153 (in isoform 1)Ubiquitination-55.6621906983
153UbiquitinationNMIHRDVKAGNILLS
CCCCCCCCCCCEEEC		55.6622817900
181PhosphorylationSIMAPANSFVGTPYW
EEEECCCCCCCCCCC		24.3422322096
185PhosphorylationPANSFVGTPYWMAPE
CCCCCCCCCCCCCCH		14.1127251275
187PhosphorylationNSFVGTPYWMAPEVI
CCCCCCCCCCCCHHE		13.9810559204
264UbiquitinationFVDSCLQKIPQDRPT
HHHHHHHHCCCCCCC		43.32-
277UbiquitinationPTSEVLLKHRFVLRE
CCHHHHHHHHHHHCC		28.6829967540
309PhosphorylationRELDNLQYRKMKKIL
HHHHHHHHHHHHHHH		18.5023917254
314UbiquitinationLQYRKMKKILFQEAP
HHHHHHHHHHHCCCC		40.94-
338PhosphorylationEEEEAEPYMHRAGTL
HHHCCCCCCCCCCCC		9.3229978859
344PhosphorylationPYMHRAGTLTSLESS
CCCCCCCCCCCCCCC		26.36-
347PhosphorylationHRAGTLTSLESSHSV
CCCCCCCCCCCCCCC		33.00-
375PhosphorylationVNSLADASDNEEEEE
HHHHCCCCCCHHHHH		41.3326657352
408PhosphorylationMMQEGEHTVTSHSSI
HHHCCCCEECCCHHH		22.6027080861
410PhosphorylationQEGEHTVTSHSSIIH
HCCCCEECCCHHHHH		23.1327080861
411PhosphorylationEGEHTVTSHSSIIHR
CCCCEECCCHHHHHC		19.6223312004
413PhosphorylationEHTVTSHSSIIHRLP
CCEECCCHHHHHCCC		24.0128857561
414PhosphorylationHTVTSHSSIIHRLPG
CEECCCHHHHHCCCC		21.8223312004
422PhosphorylationIIHRLPGSDNLYDDP
HHHCCCCCCCCCCCC		22.7629978859
426PhosphorylationLPGSDNLYDDPYQPE
CCCCCCCCCCCCCCC		25.2629978859
430PhosphorylationDNLYDDPYQPEITPS
CCCCCCCCCCCCCCC		43.6329978859
435PhosphorylationDPYQPEITPSPLQPP
CCCCCCCCCCCCCCC		18.9529978859
437PhosphorylationYQPEITPSPLQPPAA
CCCCCCCCCCCCCCC		29.5917192257
448PhosphorylationPPAAPAPTSTTSSAR
CCCCCCCCCCCHHHH		40.5925002506
449PhosphorylationPAAPAPTSTTSSARR
CCCCCCCCCCHHHHH		28.7325002506
450PhosphorylationAAPAPTSTTSSARRR
CCCCCCCCCHHHHHH		32.9225002506
451PhosphorylationAPAPTSTTSSARRRA
CCCCCCCCHHHHHHH		22.0525002506
452PhosphorylationPAPTSTTSSARRRAY
CCCCCCCHHHHHHHH		23.3022817900
453PhosphorylationAPTSTTSSARRRAYC
CCCCCCHHHHHHHHH		24.5725002506
468PhosphorylationRNRDHFATIRTASLV
CCCCCHHHHHHHHHH		15.2823312004
471PhosphorylationDHFATIRTASLVSRQ
CCHHHHHHHHHHHHH		19.4227251275
473PhosphorylationFATIRTASLVSRQIQ
HHHHHHHHHHHHHHH		28.7930266825
476PhosphorylationIRTASLVSRQIQEHE
HHHHHHHHHHHHHHH		24.6230266825
486PhosphorylationIQEHEQDSALREQLS
HHHHHHCHHHHHHHH		28.9719369195
493PhosphorylationSALREQLSGYKRMRR
HHHHHHHHHHHHHHH		39.5123403867
541UbiquitinationGFGAEAEKLARRHQA
CCHHHHHHHHHHHHH		55.2729967540
552UbiquitinationRHQAIGEKEARAAQA
HHHHHCHHHHHHHHH		52.0029967540
563UbiquitinationAAQAEERKFQQHILG
HHHHHHHHHHHHHHH		51.2929967540
573UbiquitinationQHILGQQKKELAALL
HHHHHHHHHHHHHHH		40.0929967540
595UbiquitinationKLRKEQLKEELQENP
HHCHHHHHHHHHHCC		49.1624816145
601UbiquitinationLKEELQENPSTPKRE
HHHHHHHCCCCCHHH		23.9024816145
602UbiquitinationKEELQENPSTPKREK
HHHHHHCCCCCHHHH		38.5424816145
603PhosphorylationEELQENPSTPKREKA
HHHHHCCCCCHHHHH		69.7723403867
604PhosphorylationELQENPSTPKREKAE
HHHHCCCCCHHHHHH		33.8021815630
609UbiquitinationPSTPKREKAEWLLRQ
CCCCHHHHHHHHHHH		56.4929967540
656PhosphorylationKMLLARHSLDQDLLR
HHHHHHHCCCHHHHH		28.2525850435
673UbiquitinationLNKKQTQKDLECALL
HCHHHHHHHHHHHHH		68.6129967540
722UbiquitinationGNQLEYNKRREQELR
HHHHHHHHHHHHHHH		52.5129967540
731UbiquitinationREQELRQKHAAQVRQ
HHHHHHHHHHHHHHH		28.8629967540
742 (in isoform 2)Phosphorylation-39.85-
746UbiquitinationQPKSLKVRAGQRPPG
CCCCCCCCCCCCCCC		31.2629967540
767PhosphorylationGALGPPNTGTPIEQQ
CCCCCCCCCCCCCCC		48.4827174698
769PhosphorylationLGPPNTGTPIEQQPC
CCCCCCCCCCCCCCC		21.0327174698
777PhosphorylationPIEQQPCSPGQEAVL
CCCCCCCCCCCHHHH		38.4517192257
821PhosphorylationQRILGEESGAPSPSP
HHHHCCCCCCCCCCC		35.6330266825
825PhosphorylationGEESGAPSPSPQKHG
CCCCCCCCCCCCCCC		37.1630266825
827PhosphorylationESGAPSPSPQKHGSL
CCCCCCCCCCCCCCC		44.2830266825
889 (in isoform 2)Phosphorylation-7.59-
894 (in isoform 2)Phosphorylation-30.78-
1002 (in isoform 2)Phosphorylation-17.9525849741
1011 (in isoform 2)Phosphorylation-32.9822617229
1014 (in isoform 2)Phosphorylation-46.1423911959
1016 (in isoform 2)Phosphorylation-4.0423911959
1031 (in isoform 2)Phosphorylation-15.8624117733
1033 (in isoform 2)Phosphorylation-19.4224719451
1033PhosphorylationLGAVLGLSWRRGLMG
HHHHHCHHHHCCCCC		19.4224719451
1034 (in isoform 2)Phosphorylation-10.0727251275
1035 (in isoform 2)Phosphorylation-21.2922617229
1038 (in isoform 2)Phosphorylation-2.2722617229
1048 (in isoform 2)Phosphorylation-8.82-
1126MethylationNKDGFRSRLPVPGPR
CCCCCHHCCCCCCCC		38.4630761315
1133MethylationRLPVPGPRRRNPRTT
CCCCCCCCCCCCCCC		56.9830761319
1210O-linked_GlycosylationRQLGPPASRQPLPGT
HHHCCCCHHCCCCCC		36.9030620550
1217PhosphorylationSRQPLPGTLAGRRSR
HHCCCCCCCCCCCCC		16.1122210691
1225PhosphorylationLAGRRSRTRQSRALP
CCCCCCCCCCCCCCC		34.0222210691
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
181SPhosphorylationKinaseTAO2Q9UL54
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
1031SPhosphorylation

-
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 TAOK2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MP2K3_HUMANMAP2K3physical
11279118
MP2K6_HUMANMAP2K6physical
11279118
TBB5_HUMANTUBBphysical
12639963
TBA1A_HUMANTUBA1Aphysical
12639963
M3K7_HUMANMAP3K7physical
16893890
KLH12_HUMANKLHL12physical
24722188
ZN363_HUMANRCHY1physical
24722188
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 TAOK2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-9; SER-181; SER-449;SER-473; SER-486; SER-493 AND SER-827, PHOSPHORYLATION [LARGE SCALEANALYSIS] AT SER-1011 (ISOFORM 2), AND MASS 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-9; SER-437; SER-486;SER-777; SER-825 AND SER-827, AND MASS SPECTROMETRY.
"Prostate-derived sterile 20-like kinase 1-alpha induces apoptosis.JNK-and caspase-dependent nuclear localization is a requirement formembrane blebbing.";
Zihni C., Mitsopoulos C., Tavares I.A., Baum B., Ridley A.J.,Morris J.D.;
J. Biol. Chem. 282:6484-6493(2007).
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-181,AUTOPHOSPHORYLATION, AND MUTAGENESIS OF LYS-57 AND ASP-919.

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