TAOK3_HUMAN - dbPTM
TAOK3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TAOK3_HUMAN
UniProt AC Q9H2K8
Protein Name Serine/threonine-protein kinase TAO3
Gene Name TAOK3
Organism Homo sapiens (Human).
Sequence Length 898
Subcellular Localization Cytoplasm . Cell membrane
Peripheral membrane protein . Also localized to the peripheral cell membrane.
Protein Description Serine/threonine-protein kinase that acts as a regulator of the p38/MAPK14 stress-activated MAPK cascade and of the MAPK8/JNK cascade. Acts as an activator of the p38/MAPK14 stress-activated MAPK cascade. 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. Inhibits basal activity of MAPK8/JNK cascade and diminishes its activation in response epidermal growth factor (EGF)..
Protein Sequence MRKGVLKDPEIADLFYKDDPEELFIGLHEIGHGSFGAVYFATNAHTSEVVAIKKMSYSGKQTHEKWQDILKEVKFLRQLKHPNTIEYKGCYLKEHTAWLVMEYCLGSASDLLEVHKKPLQEVEIAAITHGALHGLAYLHSHALIHRDIKAGNILLTEPGQVKLADFGSASMASPANSFVGTPYWMAPEVILAMDEGQYDGKVDIWSLGITCIELAERKPPLFNMNAMSALYHIAQNDSPTLQSNEWTDSFRRFVDYCLQKIPQERPTSAELLRHDFVRRDRPLRVLIDLIQRTKDAVRELDNLQYRKMKKILFQETRNGPLNESQEDEEDSEHGTSLNREMDSLGSNHSIPSMSVSTGSQSSSVNSMQEVMDESSSELVMMHDDESTINSSSSVVHKKDHVFIRDEAGHGDPRPEPRPTQSVQSQALHYRNRERFATIKSASLVTRQIHEHEQENELREQMSGYKRMRRQHQKQLIALENKLKAEMDEHRLKLQKEVETHANNSSIELEKLAKKQVAIIEKEAKVAAADEKKFQQQILAQQKKDLTTFLESQKKQYKICKEKIKEEMNEDHSTPKKEKQERISKHKENLQHTQAEEEAHLLTQQRLYYDKNCRFFKRKIMIKRHEVEQQNIREELNKKRTQKEMEHAMLIRHDESTRELEYRQLHTLQKLRMDLIRLQHQTELENQLEYNKRRERELHRKHVMELRQQPKNLKAMEMQIKKQFQDTCKVQTKQYKALKNHQLEVTPKNEHKTILKTLKDEQTRKLAILAEQYEQSINEMMASQALRLDEAQEAECQALRLQLQQEMELLNAYQSKIKMQTEAQHERELQKLEQRVSLRRAHLEQKIEEELAALQKERSERIKNLLERQEREIETFDMESLRMGFGNLVTLDFPKEDYR
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
7Ubiquitination-MRKGVLKDPEIADL
-CCCCCCCCHHHHHH		69.68-
56PhosphorylationVVAIKKMSYSGKQTH
EEEEEECCCCCCCHH		25.6522468782
57PhosphorylationVAIKKMSYSGKQTHE
EEEEECCCCCCCHHH		20.2422468782
84PhosphorylationRQLKHPNTIEYKGCY
HHCCCCCCCCCCEEE		21.4520068231
88UbiquitinationHPNTIEYKGCYLKEH
CCCCCCCCEEEEHHH		29.70-
103PhosphorylationTAWLVMEYCLGSASD
HHHHHHHHHHCCHHH		3.78-
168PhosphorylationVKLADFGSASMASPA
EEECCCCCCCCCCCC		19.7129523821
170PhosphorylationLADFGSASMASPANS
ECCCCCCCCCCCCCC		19.3129523821
173PhosphorylationFGSASMASPANSFVG
CCCCCCCCCCCCCCC		18.8626074081
177PhosphorylationSMASPANSFVGTPYW
CCCCCCCCCCCCCCC		24.3422322096
181PhosphorylationPANSFVGTPYWMAPE
CCCCCCCCCCCCCCH		14.1125627689
183PhosphorylationNSFVGTPYWMAPEVI
CCCCCCCCCCCCHHE		13.9828464451
198PhosphorylationLAMDEGQYDGKVDIW
EECCCCCCCCCEEEE		37.2028270605
260UbiquitinationFVDYCLQKIPQERPT
HHHHHHHHCCCCCCC		43.32-
305PhosphorylationRELDNLQYRKMKKIL
HHHHHHHHHHHHHHH		18.5023917254
310UbiquitinationLQYRKMKKILFQETR
HHHHHHHHHHHHHCC		40.94-
316PhosphorylationKKILFQETRNGPLNE
HHHHHHHCCCCCCCC		20.7426074081
324PhosphorylationRNGPLNESQEDEEDS
CCCCCCCCCCCCCHH		37.4829255136
331PhosphorylationSQEDEEDSEHGTSLN
CCCCCCHHCCCCHHH		34.4729255136
335PhosphorylationEEDSEHGTSLNREMD
CCHHCCCCHHHHHHH		31.7629255136
336PhosphorylationEDSEHGTSLNREMDS
CHHCCCCHHHHHHHH		28.3929255136
343PhosphorylationSLNREMDSLGSNHSI
HHHHHHHHCCCCCCC		33.06-
346PhosphorylationREMDSLGSNHSIPSM
HHHHHCCCCCCCCCC		36.34-
349PhosphorylationDSLGSNHSIPSMSVS
HHCCCCCCCCCCCCC		40.21-
357PhosphorylationIPSMSVSTGSQSSSV
CCCCCCCCCCCCCCC		38.40-
359PhosphorylationSMSVSTGSQSSSVNS
CCCCCCCCCCCCCHH		27.2917478428
392PhosphorylationESTINSSSSVVHKKD
CCCCCCCCCEEECCC		27.2924275569
419PhosphorylationPRPEPRPTQSVQSQA
CCCCCCCCCCHHHHH		34.4520873877
421PhosphorylationPEPRPTQSVQSQALH
CCCCCCCCHHHHHHH		25.3020873877
424PhosphorylationRPTQSVQSQALHYRN
CCCCCHHHHHHHHHC		18.4423312004
429PhosphorylationVQSQALHYRNRERFA
HHHHHHHHHCHHHHH		15.5029978859
437PhosphorylationRNRERFATIKSASLV
HCHHHHHHHHHHHHH		26.6530576142
440PhosphorylationERFATIKSASLVTRQ
HHHHHHHHHHHHHHH		21.1730266825
442PhosphorylationFATIKSASLVTRQIH
HHHHHHHHHHHHHHH		30.3923401153
445PhosphorylationIKSASLVTRQIHEHE
HHHHHHHHHHHHHHH		23.3430266825
462PhosphorylationNELREQMSGYKRMRR
HHHHHHHHHHHHHHH		38.3724719451
486SulfoxidationENKLKAEMDEHRLKL
HHHHHHHHHHHHHHH		9.7730846556
505PhosphorylationETHANNSSIELEKLA
HHHCCCCCHHHHHHH		23.3921815630
514MalonylationELEKLAKKQVAIIEK
HHHHHHHHHHHHHHH		44.3826320211
532MalonylationVAAADEKKFQQQILA
HHHHCHHHHHHHHHH		46.4826320211
546PhosphorylationAQQKKDLTTFLESQK
HHHHHHHHHHHHHHH		26.1526074081
547PhosphorylationQQKKDLTTFLESQKK
HHHHHHHHHHHHHHH		33.2626074081
551PhosphorylationDLTTFLESQKKQYKI
HHHHHHHHHHHHHHH		49.8217478428
556PhosphorylationLESQKKQYKICKEKI
HHHHHHHHHHHHHHH		15.9426074081
572PhosphorylationEEMNEDHSTPKKEKQ
HHHCCCCCCCHHHHH		59.7425850435
573PhosphorylationEMNEDHSTPKKEKQE
HHCCCCCCCHHHHHH		35.3925849741
642UbiquitinationLNKKRTQKEMEHAML
HHHHHHHHHHHHHHH		59.42-
666PhosphorylationLEYRQLHTLQKLRMD
HHHHHHHHHHHHHHH		39.2028060719
669AcetylationRQLHTLQKLRMDLIR
HHHHHHHHHHHHHHH		40.9725953088
745PhosphorylationKNHQLEVTPKNEHKT
HHCCCEECCCCHHHH		21.1225159151
782PhosphorylationSINEMMASQALRLDE
HHHHHHHHHCCCCCH		9.70-
817UbiquitinationNAYQSKIKMQTEAQH
HHHHHHHHHHHHHHH		28.79-
830AcetylationQHERELQKLEQRVSL
HHHHHHHHHHHHHHH		67.6223749302
855UbiquitinationEELAALQKERSERIK
HHHHHHHHHHHHHHH		56.81-
877SulfoxidationREIETFDMESLRMGF
HHHHHCCHHHHHCCC		3.0921406390
889PhosphorylationMGFGNLVTLDFPKED
CCCCCEEEECCCHHH		24.6320068231
897PhosphorylationLDFPKEDYR------
ECCCHHHCC------		21.2228796482
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
324SPhosphorylationKinaseATMQ13315
Uniprot
359SPhosphorylationKinaseATMQ13315
PSP
551SPhosphorylationKinaseATMQ13315
PSP
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:20804422
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
324SPhosphorylation

17396146
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 TAOK3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRAF2_HUMANTRAF2physical
11278723
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 TAOK3_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-324 AND SER-331, 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 THR-316; SER-324; SER-331AND SER-442, 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-324 AND SER-442, 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-324 AND SER-331, ANDMASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-331, ANDMASS SPECTROMETRY.
"TAO kinases mediate activation of p38 in response to DNA damage.";
Raman M., Earnest S., Zhang K., Zhao Y., Cobb M.H.;
EMBO J. 26:2005-2014(2007).
Cited for: FUNCTION, PHOSPHORYLATION AT SER-324, INDUCTION, AND MUTAGENESIS OFASP-165 AND SER-324.

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