TAOK1_HUMAN - dbPTM
TAOK1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TAOK1_HUMAN
UniProt AC Q7L7X3
Protein Name Serine/threonine-protein kinase TAO1
Gene Name TAOK1
Organism Homo sapiens (Human).
Sequence Length 1001
Subcellular Localization Cytoplasm .
Protein Description Serine/threonine-protein kinase involved in various processes such as p38/MAPK14 stress-activated MAPK cascade, DNA damage response and regulation of cytoskeleton stability. Phosphorylates MAP2K3, MAP2K6 and MARK2. Acts as an activator of the p38/MAPK14 stress-activated MAPK cascade by mediating phosphorylation and subsequent activation of the upstream MAP2K3 and MAP2K6 kinases. Involved in G-protein coupled receptor signaling to p38/MAPK14. 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 MAP2K3 and MAP2K6. Acts as a regulator of cytoskeleton stability by phosphorylating 'Thr-208' of MARK2, leading to activate MARK2 kinase activity and subsequent phosphorylation and detachment of MAPT/TAU from microtubules. Also acts as a regulator of apoptosis: regulates apoptotic morphological changes, including cell contraction, membrane blebbing and apoptotic bodies formation via activation of the MAPK8/JNK cascade..
Protein Sequence MPSTNRAGSLKDPEIAELFFKEDPEKLFTDLREIGHGSFGAVYFARDVRTNEVVAIKKMSYSGKQSTEKWQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEYCLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHTMIHRDIKAGNILLTEPGQVKLADFGSASMASPANSFVGTPYWMAPEVILAMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPTLQSNEWSDYFRNFVDSCLQKIPQDRPTSEELLKHIFVLRERPETVLIDLIQRTKDAVRELDNLQYRKMKKLLFQEAHNGPAVEAQEEEEEQDHGVGRTGTVNSVGSNQSIPSMSISASSQSSSVNSLPDVSDDKSELDMMEGDHTVMSNSSVIHLKPEEENYREEGDPRTRASDPQSPPQVSRHKSHYRNREHFATIRTASLVTRQMQEHEQDSELREQMSGYKRMRRQHQKQLMTLENKLKAEMDEHRLRLDKDLETQRNNFAAEMEKLIKKHQAAMEKEAKVMSNEEKKFQQHIQAQQKKELNSFLESQKREYKLRKEQLKEELNENQSTPKKEKQEWLSKQKENIQHFQAEEEANLLRRQRQYLELECRRFKRRMLLGRHNLEQDLVREELNKRQTQKDLEHAMLLRQHESMQELEFRHLNTIQKMRCELIRLQHQTELTNQLEYNKRRERELRRKHVMEVRQQPKSLKSKELQIKKQFQDTCKIQTRQYKALRNHLLETTPKSEHKAVLKRLKEEQTRKLAILAEQYDHSINEMLSTQALRLDEAQEAECQVLKMQLQQELELLNAYQSKIKMQAEAQHDRELRELEQRVSLRRALLEQKIEEEMLALQNERTERIRSLLERQAREIEAFDSESMRLGFSNMVLSNLSPEAFSHSYPGASGWSHNPTGGPGPHWGHPMGGPPQAWGHPMQGGPQPWGHPSGPMQGVPRGSSMGVRNSPQALRRTASGGRTEQGMSRSTSVTSQISNGSHMSYT
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
3Phosphorylation-----MPSTNRAGSL
-----CCCCCCCCCC		50.6129514088
4Phosphorylation----MPSTNRAGSLK
----CCCCCCCCCCC		39.1829514088
9PhosphorylationPSTNRAGSLKDPEIA
CCCCCCCCCCCHHHH		31.1229255136
21UbiquitinationEIAELFFKEDPEKLF
HHHHHHCCCCHHHHC		54.60-
29PhosphorylationEDPEKLFTDLREIGH
CCHHHHCCCHHHHCC		44.5630387612
38PhosphorylationLREIGHGSFGAVYFA
HHHHCCCCCCCEEEE		18.1630387612
43PhosphorylationHGSFGAVYFARDVRT
CCCCCCEEEEECCCC		7.3228152594
60PhosphorylationVVAIKKMSYSGKQST
EEEEEEECCCCCCCH		25.6522468782
61PhosphorylationVAIKKMSYSGKQSTE
EEEEEECCCCCCCHH		20.2422468782
66PhosphorylationMSYSGKQSTEKWQDI
ECCCCCCCHHHHHHH		41.8630266825
67PhosphorylationSYSGKQSTEKWQDII
CCCCCCCHHHHHHHH		38.8130266825
69UbiquitinationSGKQSTEKWQDIIKE
CCCCCHHHHHHHHHH		50.69-
84UbiquitinationVKFLQRIKHPNSIEY
HHHHHHCCCCCCCCC		56.02-
107PhosphorylationTAWLVMEYCLGSASD
HHHHHHHHHHCCHHH		3.7822817900
172PhosphorylationVKLADFGSASMASPA
EEECCCCCCCCCCCC		19.7129523821
174PhosphorylationLADFGSASMASPANS
ECCCCCCCCCCCCCC		19.3129523821
177PhosphorylationFGSASMASPANSFVG
CCCCCCCCCCCCCCC		18.8626074081
181PhosphorylationSMASPANSFVGTPYW
CCCCCCCCCCCCCCC		24.3422322096
185PhosphorylationPANSFVGTPYWMAPE
CCCCCCCCCCCCCCH		14.1125627689
187PhosphorylationNSFVGTPYWMAPEVI
CCCCCCCCCCCCHHE		13.9828464451
202PhosphorylationLAMDEGQYDGKVDVW
EECCCCCCCCCEEEE		37.2028270605
269MethylationLQKIPQDRPTSEELL
HHHCCCCCCCHHHHH		31.02115918189
288O-linked_GlycosylationVLRERPETVLIDLIQ
HHCCCCCCHHHHHHH		24.2430620550
309PhosphorylationRELDNLQYRKMKKLL
HHHHHHHHHHHHHHH		18.5022817900
406PhosphorylationLKPEEENYREEGDPR
ECCHHHCCCCCCCCC		23.7622817900
414PhosphorylationREEGDPRTRASDPQS
CCCCCCCCCCCCCCC		35.6630576142
417PhosphorylationGDPRTRASDPQSPPQ
CCCCCCCCCCCCCCC		46.6722167270
421PhosphorylationTRASDPQSPPQVSRH
CCCCCCCCCCCHHHC		43.8919664994
426PhosphorylationPQSPPQVSRHKSHYR
CCCCCCHHHCHHHHC		24.3429255136
432PhosphorylationVSRHKSHYRNREHFA
HHHCHHHHCCHHHHH		19.3722817900
440PhosphorylationRNREHFATIRTASLV
CCHHHHHHHHHHHHH		15.2830576142
443PhosphorylationEHFATIRTASLVTRQ
HHHHHHHHHHHHHHH		19.4230266825
445PhosphorylationFATIRTASLVTRQMQ
HHHHHHHHHHHHHHH		23.8223401153
448PhosphorylationIRTASLVTRQMQEHE
HHHHHHHHHHHHHHH		22.0723403867
458PhosphorylationMQEHEQDSELREQMS
HHHHHHCHHHHHHHH		37.9224719451
465PhosphorylationSELREQMSGYKRMRR
HHHHHHHHHHHHHHH		38.3726546556
480PhosphorylationQHQKQLMTLENKLKA
HHHHHHHHHHHHHHH		39.2428060719
484UbiquitinationQLMTLENKLKAEMDE
HHHHHHHHHHHHHHH		41.82-
502PhosphorylationRLDKDLETQRNNFAA
HHCHHHHHHHHHHHH		39.8817396146
546AcetylationHIQAQQKKELNSFLE
HHHHHHHHHHHHHHH		64.2030592843
554PhosphorylationELNSFLESQKREYKL
HHHHHHHHHHHHHHH		43.0517396146
575PhosphorylationEELNENQSTPKKEKQ
HHHHHCCCCCHHHHH		59.2524732914
576PhosphorylationELNENQSTPKKEKQE
HHHHCCCCCHHHHHH		29.3925849741
587UbiquitinationEKQEWLSKQKENIQH
HHHHHHHHHHHHHHH		64.32-
610PhosphorylationLLRRQRQYLELECRR
HHHHHHHHHHHHHHH		12.3425884760
643PhosphorylationEELNKRQTQKDLEHA
HHHHHHHHHHHHHHH		41.4417396146
669PhosphorylationLEFRHLNTIQKMRCE
HHHHHHHHHHHHHHH		31.0123403867
670 (in isoform 2)Ubiquitination-3.4521906983
714PhosphorylationEVRQQPKSLKSKELQ
HHHHCCCCCCCCHHH		47.9523898821
717PhosphorylationQQPKSLKSKELQIKK
HCCCCCCCCHHHHHH		36.3323898821
718UbiquitinationQPKSLKSKELQIKKQ
CCCCCCCCHHHHHHH		61.94-
734PhosphorylationQDTCKIQTRQYKALR
HHHHHHHHHHHHHHH		24.18-
750UbiquitinationHLLETTPKSEHKAVL
HHHHCCCHHHHHHHH		67.40-
751PhosphorylationLLETTPKSEHKAVLK
HHHCCCHHHHHHHHH		46.2528555341
785PhosphorylationSINEMLSTQALRLDE
HHHHHHHHHCCCCCH		17.5617396146
818UbiquitinationLLNAYQSKIKMQAEA
HHHHHHHHHHHHHHH		30.712190698
818 (in isoform 1)Ubiquitination-30.7121906983
820AcetylationNAYQSKIKMQAEAQH
HHHHHHHHHHHHHHH		28.7925953088
839O-linked_GlycosylationRELEQRVSLRRALLE
HHHHHHHHHHHHHHH		20.5330620550
853SulfoxidationEQKIEEEMLALQNER
HHHHHHHHHHHHHHH		2.7621406390
883SulfoxidationEAFDSESMRLGFSNM
HCCCCHHHHHHCCCC		3.4421406390
958PhosphorylationMQGVPRGSSMGVRNS
CCCCCCCCCCCCCCC		20.5923927012
959PhosphorylationQGVPRGSSMGVRNSP
CCCCCCCCCCCCCCH		23.5223927012
965PhosphorylationSSMGVRNSPQALRRT
CCCCCCCCHHHHHHH		14.0722167270
972PhosphorylationSPQALRRTASGGRTE
CHHHHHHHCCCCCCC		20.8128450419
974PhosphorylationQALRRTASGGRTEQG
HHHHHHCCCCCCCCC		40.9627422710
978PhosphorylationRTASGGRTEQGMSRS
HHCCCCCCCCCCCCC		35.6222199227
983PhosphorylationGRTEQGMSRSTSVTS
CCCCCCCCCCEEECC		29.8822199227
985PhosphorylationTEQGMSRSTSVTSQI
CCCCCCCCEEECCCC		20.0930576142
986PhosphorylationEQGMSRSTSVTSQIS
CCCCCCCEEECCCCC		26.5530576142
987PhosphorylationQGMSRSTSVTSQISN
CCCCCCEEECCCCCC		25.3330576142
989PhosphorylationMSRSTSVTSQISNGS
CCCCEEECCCCCCCC		18.0629978859
990PhosphorylationSRSTSVTSQISNGSH
CCCEEECCCCCCCCC		24.3017396146
993PhosphorylationTSVTSQISNGSHMSY
EEECCCCCCCCCCCC		27.7428450419
996PhosphorylationTSQISNGSHMSYT--
CCCCCCCCCCCCC--		21.9228450419
999PhosphorylationISNGSHMSYT-----
CCCCCCCCCC-----		21.8728450419
1000PhosphorylationSNGSHMSYT------
CCCCCCCCC------		14.6420068231
1001PhosphorylationNGSHMSYT-------
CCCCCCCC-------		25.4828450419
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
440TPhosphorylationKinaseMST3Q9Y6E0
PSP
643TPhosphorylationKinaseATMQ13315
PSP
785TPhosphorylationKinaseATMQ13315
PSP
990SPhosphorylationKinaseATMQ13315
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TAOK1_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 TAOK1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
M3K7_HUMANMAP3K7physical
16893890
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 TAOK1_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-421, AND MASSSPECTROMETRY.
"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; TYR-43; SER-177;SER-181; SER-421; SER-445; THR-480; THR-669; SER-958; SER-959 ANDSER-965, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, AND MASSSPECTROMETRY.
"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-9; SER-421 AND SER-445,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-421, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, AND MASSSPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421 AND SER-965, ANDMASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, 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-959, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, AND MASSSPECTROMETRY.

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