M3K9_HUMAN - dbPTM
M3K9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID M3K9_HUMAN
UniProt AC P80192
Protein Name Mitogen-activated protein kinase kinase kinase 9
Gene Name MAP3K9
Organism Homo sapiens (Human).
Sequence Length 1104
Subcellular Localization
Protein Description Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade through the phosphorylation of MAP2K4/MKK4 and MAP2K7/MKK7 which in turn activate the JNKs. The MKK/JNK signaling pathway regulates stress response via activator protein-1 (JUN) and GATA4 transcription factors. Plays also a role in mitochondrial death signaling pathway, including the release cytochrome c, leading to apoptosis..
Protein Sequence MEPSRALLGCLASAAAAAPPGEDGAGAGAEEEEEEEEEAAAAVGPGELGCDAPLPYWTAVFEYEAAGEDELTLRLGDVVEVLSKDSQVSGDEGWWTGQLNQRVGIFPSNYVTPRSAFSSRCQPGGEDPSCYPPIQLLEIDFAELTLEEIIGIGGFGKVYRAFWIGDEVAVKAARHDPDEDISQTIENVRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVMEFARGGPLNRVLSGKRIPPDILVNWAVQIARGMNYLHDEAIVPIIHRDLKSSNILILQKVENGDLSNKILKITDFGLAREWHRTTKMSAAGTYAWMAPEVIRASMFSKGSDVWSYGVLLWELLTGEVPFRGIDGLAVAYGVAMNKLALPIPSTCPEPFAKLMEDCWNPDPHSRPSFTNILDQLTTIEESGFFEMPKDSFHCLQDNWKHEIQEMFDQLRAKEKELRTWEEELTRAALQQKNQEELLRRREQELAEREIDILERELNIIIHQLCQEKPRVKKRKGKFRKSRLKLKDGNRISLPSDFQHKFTVQASPTMDKRKSLINSRSSPPASPTIIPRLRAIQLTPGESSKTWGRSSVVPKEEGEEEEKRAPKKKGRTWGPGTLGQKELASGDEGSPQRREKANGLSTPSESPHFHLGLKSLVDGYKQWSSSAPNLVKGPRSSPALPGFTSLMEMEDEDSEGPGSGESRLQHSPSQSYLCIPFPRGEDGDGPSSDGIHEEPTPVNSATSTPQLTPTNSLKRGGAHHRRCEVALLGCGAVLAATGLGFDLLEAGKCQLLPLEEPEPPAREEKKRREGLFQRSSRPRRSTSPPSRKLFKKEEPMLLLGDPSASLTLLSLSSISECNSTRSLLRSDSDEIVVYEMPVSPVEAPPLSPCTHNPLVNVRVERFKRDPNQSLTPTHVTLTTPSQPSSHRRTPSDGALKPETLLASRSPSSNGLSPSPGAGMLKTPSPSRDPGEFPRLPDPNVVFPPTPRRWNTQQDSTLERPKTLEFLPRPRPSANRQRLDPWWFVSPSHARSTSPANSSSTETPSNLDSCFASSSSTVEERPGLPALLPFQAGPLPPTERTLLDLDAEGQSQDSTVPLCRAELNTHRPAPYEIQQEFWS
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
110PhosphorylationVGIFPSNYVTPRSAF
CCEECCCCCCHHHHH		15.2727642862
118PhosphorylationVTPRSAFSSRCQPGG
CCHHHHHHCCCCCCC		19.3124719451
193UbiquitinationENVRQEAKLFAMLKH
HHHHHHHHHHHHHHC		43.30-
304PhosphorylationLAREWHRTTKMSAAG
HHHHHHHCCCCCCCC		20.2015610029
305PhosphorylationAREWHRTTKMSAAGT
HHHHHHCCCCCCCCH		25.3815610029
308PhosphorylationWHRTTKMSAAGTYAW
HHHCCCCCCCCHHHH		19.2715610029
312PhosphorylationTKMSAAGTYAWMAPE
CCCCCCCHHHHHCHH		12.8215610029
452PhosphorylationRTWEEELTRAALQQK
HHHHHHHHHHHHHHH		22.88-
519PhosphorylationLKDGNRISLPSDFQH
CCCCCEECCCCCCCC		30.8730266825
522PhosphorylationGNRISLPSDFQHKFT
CCEECCCCCCCCCEE		57.2430266825
529PhosphorylationSDFQHKFTVQASPTM
CCCCCCEEEEECCCC		19.2630266825
533PhosphorylationHKFTVQASPTMDKRK
CCEEEEECCCCHHHH		12.1030266825
535PhosphorylationFTVQASPTMDKRKSL
EEEEECCCCHHHHHH		35.1930266825
541PhosphorylationPTMDKRKSLINSRSS
CCCHHHHHHHHCCCC		38.2223090842
545PhosphorylationKRKSLINSRSSPPAS
HHHHHHHCCCCCCCC		26.9223090842
547PhosphorylationKSLINSRSSPPASPT
HHHHHCCCCCCCCCC		47.2030266825
548PhosphorylationSLINSRSSPPASPTI
HHHHCCCCCCCCCCC		33.5230266825
552PhosphorylationSRSSPPASPTIIPRL
CCCCCCCCCCCHHHE		28.4930266825
554PhosphorylationSSPPASPTIIPRLRA
CCCCCCCCCHHHEEE		29.1030266825
565PhosphorylationRLRAIQLTPGESSKT
HEEEEECCCCCCCCC		16.9317192257
576PhosphorylationSSKTWGRSSVVPKEE
CCCCCCCCCCCCHHH		24.4430624053
577PhosphorylationSKTWGRSSVVPKEEG
CCCCCCCCCCCHHHC		26.2730624053
594AcetylationEEKRAPKKKGRTWGP
HHHHCCCCCCCCCCC		60.447377509
595AcetylationEKRAPKKKGRTWGPG
HHHCCCCCCCCCCCC		60.807377519
598PhosphorylationAPKKKGRTWGPGTLG
CCCCCCCCCCCCCCC		43.3628176443
607AcetylationGPGTLGQKELASGDE
CCCCCCHHHHCCCCC		53.5511922609
616PhosphorylationLASGDEGSPQRREKA
HCCCCCCCHHHHHHH		18.80-
630PhosphorylationANGLSTPSESPHFHL
HCCCCCCCCCCCCCC		51.2828450419
632PhosphorylationGLSTPSESPHFHLGL
CCCCCCCCCCCCCCH		28.1928450419
652PhosphorylationGYKQWSSSAPNLVKG
HHHHHHCCCCCCCCC		42.0822617229
658UbiquitinationSSAPNLVKGPRSSPA
CCCCCCCCCCCCCCC		67.38-
693PhosphorylationGESRLQHSPSQSYLC
CCCCCCCCCCCCEEE		17.1825849741
695PhosphorylationSRLQHSPSQSYLCIP
CCCCCCCCCCEEEEE		34.4728464451
697PhosphorylationLQHSPSQSYLCIPFP
CCCCCCCCEEEEECC		25.1425106551
698PhosphorylationQHSPSQSYLCIPFPR
CCCCCCCEEEEECCC		9.6528464451
707PhosphorylationCIPFPRGEDGDGPSS
EEECCCCCCCCCCCC		61.1624719451
709PhosphorylationPFPRGEDGDGPSSDG
ECCCCCCCCCCCCCC		37.1627251275
807PhosphorylationRSSRPRRSTSPPSRK
CCCCCCCCCCCCCHH		34.2223663014
808PhosphorylationSSRPRRSTSPPSRKL
CCCCCCCCCCCCHHH		43.3623663014
809PhosphorylationSRPRRSTSPPSRKLF
CCCCCCCCCCCHHHC		35.7423663014
812PhosphorylationRRSTSPPSRKLFKKE
CCCCCCCCHHHCCCC		45.4923663014
852PhosphorylationSTRSLLRSDSDEIVV
CCHHHHHCCCCCEEE		41.2428348404
854PhosphorylationRSLLRSDSDEIVVYE
HHHHHCCCCCEEEEE		38.0928348404
915PhosphorylationQPSSHRRTPSDGALK
CCCCCCCCCCCCCCC		27.4030266825
917PhosphorylationSSHRRTPSDGALKPE
CCCCCCCCCCCCCHH		48.3330266825
925PhosphorylationDGALKPETLLASRSP
CCCCCHHHHCCCCCC		35.2827251275
929PhosphorylationKPETLLASRSPSSNG
CHHHHCCCCCCCCCC		33.0123927012
931PhosphorylationETLLASRSPSSNGLS
HHHCCCCCCCCCCCC		27.0019060867
934PhosphorylationLASRSPSSNGLSPSP
CCCCCCCCCCCCCCC		38.0021082442
938PhosphorylationSPSSNGLSPSPGAGM
CCCCCCCCCCCCCCC		25.40-
948PhosphorylationPGAGMLKTPSPSRDP
CCCCCCCCCCCCCCC		25.66-
952PhosphorylationMLKTPSPSRDPGEFP
CCCCCCCCCCCCCCC		54.3628258704
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
304TPhosphorylationKinaseMAP3K9P80192
GPS
308SPhosphorylationKinaseMAP3K9P80192
GPS
312TPhosphorylationKinaseMAP3K9P80192
GPS
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:20804422
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
304TPhosphorylation

15610029
308SPhosphorylation

15610029
312TPhosphorylation

15610029
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 M3K9_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HS90A_HUMANHSP90AA1physical
22939624
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 M3K9_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 THR-529; SER-533; THR-535;SER-547; SER-552; THR-565; SER-652; SER-693; SER-695; THR-915; SER-917AND SER-929, AND MASS SPECTROMETRY.
"Phosphoregulation of mixed-lineage kinase 1 activity by multiplephosphorylation in the activation loop.";
Durkin J.T., Holskin B.P., Kopec K.K., Reed M.S., Spais C.M.,Steffy B.M., Gessner G., Angeles T.S., Pohl J., Ator M.A., Meyer S.L.;
Biochemistry 43:16348-16355(2004).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION,PHOSPHORYLATION AT THR-304; THR-305; SER-308 AND THR-312, ANDMUTAGENESIS OF LYS-171; THR-304; THR-305; SER-308 AND THR-312.
"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 THR-565, AND MASSSPECTROMETRY.

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