M3K11_HUMAN - dbPTM
M3K11_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID M3K11_HUMAN
UniProt AC Q16584
Protein Name Mitogen-activated protein kinase kinase kinase 11
Gene Name MAP3K11 {ECO:0000312|HGNC:HGNC:6850}
Organism Homo sapiens (Human).
Sequence Length 847
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Location is cell cycle dependent.
Protein Description Activates the JUN N-terminal pathway. Required for serum-stimulated cell proliferation and for mitogen and cytokine activation of MAPK14 (p38), MAPK3 (ERK) and MAPK8 (JNK1) through phosphorylation and activation of MAP2K4/MKK4 and MAP2K7/MKK7. Plays a role in mitogen-stimulated phosphorylation and activation of BRAF, but does not phosphorylate BRAF directly. Influences microtubule organization during the cell cycle..
Protein Sequence MEPLKSLFLKSPLGSWNGSGSGGGGGGGGGRPEGSPKAAGYANPVWTALFDYEPSGQDELALRKGDRVEVLSRDAAISGDEGWWAGQVGGQVGIFPSNYVSRGGGPPPCEVASFQELRLEEVIGIGGFGKVYRGSWRGELVAVKAARQDPDEDISVTAESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVMEYAAGGPLSRALAGRRVPPHVLVNWAVQIARGMHYLHCEALVPVIHRDLKSNNILLLQPIESDDMEHKTLKITDFGLAREWHKTTQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGIDCLAVAYGVAVNKLTLPIPSTCPEPFAQLMADCWAQDPHRRPDFASILQQLEALEAQVLREMPRDSFHSMQEGWKREIQGLFDELRAKEKELLSREEELTRAAREQRSQAEQLRRREHLLAQWELEVFERELTLLLQQVDRERPHVRRRRGTFKRSKLRARDGGERISMPLDFKHRITVQASPGLDRRRNVFEVGPGDSPTFPRFRAIQLEPAEPGQAWGRQSPRRLEDSSNGERRACWAWGPSSPKPGEAQNGRRRSRMDEATWYLDSDDSSPLGSPSTPPALNGNPPRPSLEPEEPKRPVPAERGSSSGTPKLIQRALLRGTALLASLGLGRDLQPPGGPGRERGESPTTPPTPTPAPCPTEPPPSPLICFSLKTPDSPPTPAPLLLDLGIPVGQRSAKSPRREEEPRGGTVSPPPGTSRSAPGTPGTPRSPPLGLISRPRPSPLRSRIDPWSFVSAGPRPSPLPSPQPAPRRAPWTLFPDSDPFWDSPPANPFQGGPQDCRAQTKDMGAQAPWVPEAGP
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
6Phosphorylation--MEPLKSLFLKSPL
--CCCCHHHCCCCCC		31.8523312004
7Ubiquitination-MEPLKSLFLKSPLG
-CCCCHHHCCCCCCC		5.80-
11PhosphorylationLKSLFLKSPLGSWNG
CHHHCCCCCCCCCCC		27.7517192257
15PhosphorylationFLKSPLGSWNGSGSG
CCCCCCCCCCCCCCC		25.6727486199
19PhosphorylationPLGSWNGSGSGGGGG
CCCCCCCCCCCCCCC		26.9423403867
21PhosphorylationGSWNGSGSGGGGGGG
CCCCCCCCCCCCCCC		35.6423403867
35PhosphorylationGGGRPEGSPKAAGYA
CCCCCCCCCCCCCCC		22.8921712546
52PhosphorylationVWTALFDYEPSGQDE
CEEEECCCCCCCCCC		23.5427642862
155PhosphorylationQDPDEDISVTAESVR
CCCCCCCCCCHHHHH		26.2422210691
157PhosphorylationPDEDISVTAESVRQE
CCCCCCCCHHHHHHH		20.2322210691
160PhosphorylationDISVTAESVRQEARL
CCCCCHHHHHHHHHH		21.8222210691
242UbiquitinationVPVIHRDLKSNNILL
HHHHCCCCCCCCEEE		7.08-
261UbiquitinationESDDMEHKTLKITDF
CCCCCCCCEEEECHH		42.10-
264UbiquitinationDMEHKTLKITDFGLA
CCCCCEEEECHHHHH		49.11-
277PhosphorylationLAREWHKTTQMSAAG
HHHHHHHHCCCCCCH		14.9016831194
281PhosphorylationWHKTTQMSAAGTYAW
HHHHCCCCCCHHHEE		12.7316831194
394PhosphorylationMPRDSFHSMQEGWKR
CCHHHHHHHHHHHHH		21.8322817900
419PhosphorylationAKEKELLSREEELTR
HHHHHHHHHHHHHHH		50.7124719451
477PhosphorylationHVRRRRGTFKRSKLR
CHHHCCCCCCHHHHC		24.95-
493PhosphorylationRDGGERISMPLDFKH
CCCCCEECCCCCCCC		22.1429496963
499UbiquitinationISMPLDFKHRITVQA
ECCCCCCCCEEEEEE		31.47-
503PhosphorylationLDFKHRITVQASPGL
CCCCCEEEEEECCCC		13.4123403867
507PhosphorylationHRITVQASPGLDRRR
CEEEEEECCCCCCCC		11.4723401153
512MethylationQASPGLDRRRNVFEV
EECCCCCCCCCEEEC		44.4930760381
524PhosphorylationFEVGPGDSPTFPRFR
EECCCCCCCCCCCEE		31.5829255136
526PhosphorylationVGPGDSPTFPRFRAI
CCCCCCCCCCCEEEE		50.6630266825
548PhosphorylationGQAWGRQSPRRLEDS
CCCCCCCCCCCCCCC		21.0022617229
555PhosphorylationSPRRLEDSSNGERRA
CCCCCCCCCCCCEEE		19.1422817900
556PhosphorylationPRRLEDSSNGERRAC
CCCCCCCCCCCEEEE		62.2622817900
569PhosphorylationACWAWGPSSPKPGEA
EEEEECCCCCCCCCC		56.1623401153
570PhosphorylationCWAWGPSSPKPGEAQ
EEEECCCCCCCCCCC		39.8223403867
624UbiquitinationSLEPEEPKRPVPAER
CCCCCCCCCCCCCCC		73.03-
654PhosphorylationRGTALLASLGLGRDL
HHHHHHHHCCCCCCC		23.9622817900
674PhosphorylationPGRERGESPTTPPTP
CCCCCCCCCCCCCCC		30.3020145118
677PhosphorylationERGESPTTPPTPTPA
CCCCCCCCCCCCCCC		30.5622817900
680PhosphorylationESPTTPPTPTPAPCP
CCCCCCCCCCCCCCC		40.7827251275
682PhosphorylationPTTPPTPTPAPCPTE
CCCCCCCCCCCCCCC		34.2627251275
688PhosphorylationPTPAPCPTEPPPSPL
CCCCCCCCCCCCCCE		68.7727251275
693PhosphorylationCPTEPPPSPLICFSL
CCCCCCCCCEEEEEE		37.8026657352
702PhosphorylationLICFSLKTPDSPPTP
EEEEEECCCCCCCCC		37.3129255136
705PhosphorylationFSLKTPDSPPTPAPL
EEECCCCCCCCCCCC		33.7029255136
708PhosphorylationKTPDSPPTPAPLLLD
CCCCCCCCCCCCEEE		35.1530278072
724PhosphorylationGIPVGQRSAKSPRRE
CCCCCCCCCCCCCCC		31.9622817900
727PhosphorylationVGQRSAKSPRREEEP
CCCCCCCCCCCCCCC		24.2922817900
738PhosphorylationEEEPRGGTVSPPPGT
CCCCCCCCCCCCCCC		22.1927794612
740PhosphorylationEPRGGTVSPPPGTSR
CCCCCCCCCCCCCCC		31.3729255136
745PhosphorylationTVSPPPGTSRSAPGT
CCCCCCCCCCCCCCC		27.0923403867
746PhosphorylationVSPPPGTSRSAPGTP
CCCCCCCCCCCCCCC		30.1023403867
748PhosphorylationPPPGTSRSAPGTPGT
CCCCCCCCCCCCCCC		38.2830266825
752PhosphorylationTSRSAPGTPGTPRSP
CCCCCCCCCCCCCCC		19.9330266825
755PhosphorylationSAPGTPGTPRSPPLG
CCCCCCCCCCCCCCC		19.4126055452
758PhosphorylationGTPGTPRSPPLGLIS
CCCCCCCCCCCCCCC		31.8830266825
765PhosphorylationSPPLGLISRPRPSPL
CCCCCCCCCCCCCCC		41.0718691976
770PhosphorylationLISRPRPSPLRSRID
CCCCCCCCCCHHCCC		37.5322817900
774PhosphorylationPRPSPLRSRIDPWSF
CCCCCCHHCCCCCCC		41.0724719451
780PhosphorylationRSRIDPWSFVSAGPR
HHCCCCCCCCCCCCC		22.5928634298
783PhosphorylationIDPWSFVSAGPRPSP
CCCCCCCCCCCCCCC		26.0423312004
789PhosphorylationVSAGPRPSPLPSPQP
CCCCCCCCCCCCCCC		40.1126846344
793PhosphorylationPRPSPLPSPQPAPRR
CCCCCCCCCCCCCCC		43.8029255136
815PhosphorylationDSDPFWDSPPANPFQ
CCCCCCCCCCCCCCC		24.3117192257
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
277TPhosphorylationKinaseMAP3K11Q16584
GPS
281SPhosphorylationKinaseMAP3K11Q16584
GPS
281SPhosphorylationKinaseM4K1Q92918
PhosphoELM
674SPhosphorylationKinaseAKT1P31749
PSP
674SPhosphorylationKinaseAKT-FAMILY-GPS
674SPhosphorylationKinasePKB_GROUP-PhosphoELM
705SPhosphorylationKinaseMAPK3P27361
GPS
758SPhosphorylationKinaseMAPK3P27361
GPS
789SPhosphorylationKinaseGSK3AP49840
GPS
789SPhosphorylationKinaseGSK3BP49841
PSP
793SPhosphorylationKinaseGSK3AP49840
GPS
793SPhosphorylationKinaseGSK3BP49841
PSP
-KUbiquitinationE3 ubiquitin ligaseTRAF6Q9Y4K3
PMID:23172226
-KUbiquitinationE3 ubiquitin ligaseSTUB1Q9UNE7
PMID:24912674
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
277TPhosphorylation

11053428
555SPhosphorylation

11969422
556SPhosphorylation

11969422
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 M3K11_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KIF17_HUMANKIF17physical
9427749
KIF3A_HUMANKIF3Aphysical
9427749
KIFA3_HUMANKIFAP3physical
9427749
KIF3B_HUMANKIF3Bphysical
9427749
JIP1_HUMANMAPK8IP1physical
10490659
JIP2_HUMANMAPK8IP2physical
10490659
AKT1_HUMANAKT1physical
12458207
IKKB_HUMANIKBKBphysical
10713178
IKKA_HUMANCHUKphysical
10713178
MP2K4_HUMANMAP2K4physical
10187804
MP2K7_HUMANMAP2K7physical
10187804
CSN5_HUMANCOPS5physical
20936779
TRAF6_HUMANTRAF6physical
23172226
M3K11_HUMANMAP3K11physical
23172226
JIP1_HUMANMAPK8IP1physical
23172226
HS90A_HUMANHSP90AA1physical
15001580
CDC37_HUMANCDC37physical
15001580
HS90B_HUMANHSP90AB1physical
15001580
MP2K7_HUMANMAP2K7physical
15001580
PIN1_HUMANPIN1physical
21988832
HSP74_HUMANHSPA4physical
24912674
HS90A_HUMANHSP90AA1physical
24912674
CHIP_HUMANSTUB1physical
24912674
M3K21_HUMANKIAA1804physical
28757353
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 M3K11_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-789 AND SER-793, 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 SER-35; SER-394; SER-493;SER-507; SER-524; SER-548; SER-569; THR-677; THR-680; SER-693;THR-702; SER-705; SER-740; SER-748; THR-755; SER-758; SER-789 ANDSER-793, 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-789 AND SER-793, 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-35; SER-493; SER-507;SER-524; SER-548; SER-705; THR-708; THR-738; SER-740; SER-748;THR-752; THR-755; SER-758; SER-793 AND SER-815, AND MASS SPECTROMETRY.
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry.";
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.;
Mol. Cell. Proteomics 6:537-547(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-738; SER-740 ANDSER-746, AND MASS 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-507, AND MASSSPECTROMETRY.
"Identification of in vivo phosphorylation sites of MLK3 by massspectrometry and phosphopeptide mapping.";
Vacratsis P.O., Phinney B.S., Gage D.A., Gallo K.A.;
Biochemistry 41:5613-5624(2002).
Cited for: PHOSPHORYLATION AT SER-524; SER-555; SER-556; SER-654; SER-705;SER-724; SER-727; SER-740; SER-758; SER-770 AND SER-793.
"The kinase activation loop is the key to mixed lineage kinase-3activation via both autophosphorylation and hematopoietic progenitorkinase 1 phosphorylation.";
Leung I.W.L., Lassam N.J.;
J. Biol. Chem. 276:1961-1967(2001).
Cited for: ENZYME REGULATION, PHOSPHORYLATION AT THR-277 AND SER-281, ANDMUTAGENESIS OF LYS-144; THR-277; THR-278 AND SER-281.

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