M4K2_HUMAN - dbPTM
M4K2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID M4K2_HUMAN
UniProt AC Q12851
Protein Name Mitogen-activated protein kinase kinase kinase kinase 2
Gene Name MAP4K2
Organism Homo sapiens (Human).
Sequence Length 820
Subcellular Localization Cytoplasm. Basolateral cell membrane
Peripheral membrane protein. Golgi apparatus membrane
Peripheral membrane protein.
Protein Description Serine/threonine-protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Acts as a MAPK kinase kinase kinase (MAP4K) and is an upstream activator of the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway and to a lesser extent of the p38 MAPKs signaling pathway. Required for the efficient activation of JNKs by TRAF6-dependent stimuli, including pathogen-associated molecular patterns (PAMPs) such as polyinosine-polycytidine (poly(IC)), lipopolysaccharides (LPS), lipid A, peptidoglycan (PGN), or bacterial flagellin. To a lesser degree, IL-1 and engagement of CD40 also stimulate MAP4K2-mediated JNKs activation. The requirement for MAP4K2/GCK is most pronounced for LPS signaling, and extends to LPS stimulation of c-Jun phosphorylation and induction of IL-8. Enhances MAP3K1 oligomerization, which may relieve N-terminal mediated MAP3K1 autoinhibition and lead to activation following autophosphorylation. Mediates also the SAP/JNK signaling pathway and the p38 MAPKs signaling pathway through activation of the MAP3Ks MAP3K10/MLK2 and MAP3K11/MLK3. May play a role in the regulation of vesicle targeting or fusion. regulation of vesicle targeting or fusion..
Protein Sequence MALLRDVSLQDPRDRFELLQRVGAGTYGDVYKARDTVTSELAAVKIVKLDPGDDISSLQQEITILRECRHPNVVAYIGSYLRNDRLWICMEFCGGGSLQEIYHATGPLEERQIAYVCREALKGLHHLHSQGKIHRDIKGANLLLTLQGDVKLADFGVSGELTASVAKRRSFIGTPYWMAPEVAAVERKGGYNELCDVWALGITAIELGELQPPLFHLHPMRALMLMSKSSFQPPKLRDKTRWTQNFHHFLKLALTKNPKKRPTAEKLLQHPFTTQQLPRALLTQLLDKASDPHLGTPSPEDCELETYDMFPDTIHSRGQHGPAERTPSEIQFHQVKFGAPRRKETDPLNEPWEEEWTLLGKEELSGSLLQSVQEALEERSLTIRSASEFQELDSPDDTMGTIKRAPFLGPLPTDPPAEEPLSSPPGTLPPPPSGPNSSPLLPTAWATMKQREDPERSSCHGLPPTPKVHMGACFSKVFNGCPLRIHAAVTWIHPVTRDQFLVVGAEEGIYTLNLHELHEDTLEKLISHRCSWLYCVNNVLLSLSGKSTHIWAHDLPGLFEQRRLQQQVPLSIPTNRLTQRIIPRRFALSTKIPDTKGCLQCRVVRNPYTGATFLLAALPTSLLLLQWYEPLQKFLLLKNFSSPLPSPAGMLEPLVLDGKELPQVCVGAEGPEGPGCRVLFHVLPLEAGLTPDILIPPEGIPGSAQQVIQVDRDTILVSFERCVRIVNMQGEPTATLAPELTFDFPIETVVCLQDSVLAFWSHGMQGRSLDTNEVTQEITDETRIFRVLGAHRDIILESIPTDNPEAHSNLYILTGHQSTY
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
8PhosphorylationMALLRDVSLQDPRDR
CCCCCCCCCCCHHHH		25.3020873877
27PhosphorylationQRVGAGTYGDVYKAR
HHHCCCCCCCCCCCH		15.48-
32UbiquitinationGTYGDVYKARDTVTS
CCCCCCCCCHHCCCH		36.4721906983
32UbiquitinationGTYGDVYKARDTVTS
CCCCCCCCCHHCCCH		36.472190698
39PhosphorylationKARDTVTSELAAVKI
CCHHCCCHHEEEEEE		26.6919413330
45UbiquitinationTSELAAVKIVKLDPG
CHHEEEEEEEECCCC		36.74-
48UbiquitinationLAAVKIVKLDPGDDI
EEEEEEEECCCCCCH		51.12-
79PhosphorylationNVVAYIGSYLRNDRL
CHHHEEEHHHCCCEE		16.0724719451
80PhosphorylationVVAYIGSYLRNDRLW
HHHEEEHHHCCCEEE		12.4124719451
132UbiquitinationHHLHSQGKIHRDIKG
HHHHHCCCCCCCCCC		27.92-
158PhosphorylationKLADFGVSGELTASV
EECCCCCCCEEEHHH		27.2527251275
170PhosphorylationASVAKRRSFIGTPYW
HHHHHCCCCCCCCCC		25.8330108239
174PhosphorylationKRRSFIGTPYWMAPE
HCCCCCCCCCCCCHH		14.3730108239
176PhosphorylationRSFIGTPYWMAPEVA
CCCCCCCCCCCHHHH		13.9830108239
227PhosphorylationMRALMLMSKSSFQPP
HHHHHHHHCCCCCCC		25.98-
266UbiquitinationKKRPTAEKLLQHPFT
CCCCCHHHHHCCCCC		52.62-
273PhosphorylationKLLQHPFTTQQLPRA
HHHCCCCCHHHHHHH		28.3120071362
288UbiquitinationLLTQLLDKASDPHLG
HHHHHHHHHCCCCCC		50.16-
290PhosphorylationTQLLDKASDPHLGTP
HHHHHHHCCCCCCCC		58.3730108239
296PhosphorylationASDPHLGTPSPEDCE
HCCCCCCCCCHHHCE		27.2730576142
298PhosphorylationDPHLGTPSPEDCELE
CCCCCCCCHHHCEEE		40.5323401153
306PhosphorylationPEDCELETYDMFPDT
HHHCEEEEECCCCCC		37.1328796482
307PhosphorylationEDCELETYDMFPDTI
HHCEEEEECCCCCCC		8.9528796482
313PhosphorylationTYDMFPDTIHSRGQH
EECCCCCCCCCCCCC		22.3428060719
316PhosphorylationMFPDTIHSRGQHGPA
CCCCCCCCCCCCCCC		33.9728060719
326PhosphorylationQHGPAERTPSEIQFH
CCCCCCCCCCCEEEE		23.7530266825
327PhosphorylationHGPAERTPSEIQFHQ
CCCCCCCCCCEEEEE		35.8617192257
328PhosphorylationGPAERTPSEIQFHQV
CCCCCCCCCEEEEEC		46.8723401153
336UbiquitinationEIQFHQVKFGAPRRK
CEEEEECCCCCCCCC		31.35-
343UbiquitinationKFGAPRRKETDPLNE
CCCCCCCCCCCCCCC		67.27-
365PhosphorylationLLGKEELSGSLLQSV
HHCHHHHCHHHHHHH		29.6122199227
367PhosphorylationGKEELSGSLLQSVQE
CHHHHCHHHHHHHHH		23.6422199227
371PhosphorylationLSGSLLQSVQEALEE
HCHHHHHHHHHHHHH		26.2428060719
380PhosphorylationQEALEERSLTIRSAS
HHHHHHCCCEEECHH		32.9028450419
382PhosphorylationALEERSLTIRSASEF
HHHHCCCEEECHHHH		18.6527251275
385PhosphorylationERSLTIRSASEFQEL
HCCCEEECHHHHHCC		32.0922115753
387PhosphorylationSLTIRSASEFQELDS
CCEEECHHHHHCCCC		39.9425159151
394PhosphorylationSEFQELDSPDDTMGT
HHHHCCCCCCCCCCC		42.7425159151
398PhosphorylationELDSPDDTMGTIKRA
CCCCCCCCCCCCCCC		25.5330266825
401PhosphorylationSPDDTMGTIKRAPFL
CCCCCCCCCCCCCCC		16.7123403867
403UbiquitinationDDTMGTIKRAPFLGP
CCCCCCCCCCCCCCC		42.20-
422PhosphorylationPPAEEPLSSPPGTLP
CCCCCCCCCCCCCCC		52.0628348404
423PhosphorylationPAEEPLSSPPGTLPP
CCCCCCCCCCCCCCC		42.6828348404
427PhosphorylationPLSSPPGTLPPPPSG
CCCCCCCCCCCCCCC		41.6928348404
433PhosphorylationGTLPPPPSGPNSSPL
CCCCCCCCCCCCCCC		73.0628348404
437PhosphorylationPPPSGPNSSPLLPTA
CCCCCCCCCCCCCCH		36.1428348404
438PhosphorylationPPSGPNSSPLLPTAW
CCCCCCCCCCCCCHH		26.6328348404
457PhosphorylationQREDPERSSCHGLPP
CCCCCCCCCCCCCCC		35.3424719451
458PhosphorylationREDPERSSCHGLPPT
CCCCCCCCCCCCCCC		19.1626552605
465PhosphorylationSCHGLPPTPKVHMGA
CCCCCCCCCCCCCHH		33.5326552605
542PhosphorylationCVNNVLLSLSGKSTH
HHHCCHHHCCCCCCE		19.14-
544PhosphorylationNNVLLSLSGKSTHIW
HCCHHHCCCCCCEEE		40.58-
571PhosphorylationLQQQVPLSIPTNRLT
HHHCCCCCCCCCCCH		22.0528555341
574PhosphorylationQVPLSIPTNRLTQRI
CCCCCCCCCCCHHCC		31.1628555341
578PhosphorylationSIPTNRLTQRIIPRR
CCCCCCCHHCCCCHH		16.7428555341
591UbiquitinationRRFALSTKIPDTKGC
HHHCCCCCCCCCCCE		49.19-
596UbiquitinationSTKIPDTKGCLQCRV
CCCCCCCCCEEEEEE		55.81-
798PhosphorylationHRDIILESIPTDNPE
CCCEEEEECCCCCCC		30.3527080861
801PhosphorylationIILESIPTDNPEAHS
EEEEECCCCCCCHHC		46.9022210691
808PhosphorylationTDNPEAHSNLYILTG
CCCCCHHCCEEEEEC		35.2627080861
811PhosphorylationPEAHSNLYILTGHQS
CCHHCCEEEEECCCC		9.7227080861
814PhosphorylationHSNLYILTGHQSTY-
HCCEEEEECCCCCC-		24.0627080861
818PhosphorylationYILTGHQSTY-----
EEEECCCCCC-----		24.8127080861
819PhosphorylationILTGHQSTY------
EEECCCCCC------		27.0428450419
820PhosphorylationLTGHQSTY-------
EECCCCCC-------		23.0827080861
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

Oops, there are no upstream regulatory protein records of M4K2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
48Kubiquitylation

15456887
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 M4K2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
M3K1_HUMANMAP3K1physical
9712898
MP2K4_HUMANMAP2K4physical
9712898
TRAF2_HUMANTRAF2physical
9712898
ROA2_HUMANHNRNPA2B1physical
21900206
XRCC6_HUMANXRCC6physical
21900206
KAIN_HUMANSERPINA4physical
21900206
U1SBP_HUMANSNRNP35physical
21900206
NACAD_HUMANNACADphysical
21900206
DEFB1_HUMANDEFB1physical
21900206
PRDX4_HUMANPRDX4physical
21900206
M3K1_HUMANMAP3K1physical
11784851
M3K11_HUMANMAP3K11physical
11784851
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 M4K2_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-394, 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-8; SER-298; THR-326;SER-328 AND SER-394, 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-328, 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-394, AND MASSSPECTROMETRY.
"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-328, AND MASSSPECTROMETRY.

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