M3K2_HUMAN - dbPTM
M3K2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID M3K2_HUMAN
UniProt AC Q9Y2U5
Protein Name Mitogen-activated protein kinase kinase kinase 2
Gene Name MAP3K2
Organism Homo sapiens (Human).
Sequence Length 619
Subcellular Localization Cytoplasm . Nucleus . Upon EGF stimulation, translocates into the nucleus.
Protein Description Component of a protein kinase signal transduction cascade. Regulates the JNK and ERK5 pathways by phosphorylating and activating MAP2K5 and MAP2K7 (By similarity). Plays a role in caveolae kiss-and-run dynamics..
Protein Sequence MDDQQALNSIMQDLAVLHKASRPALSLQETRKAKSSSPKKQNDVRVKFEHRGEKRILQFPRPVKLEDLRSKAKIAFGQSMDLHYTNNELVIPLTTQDDLDKAVELLDRSIHMKSLKILLVINGSTQATNLEPLPSLEDLDNTVFGAERKKRLSIIGPTSRDRSSPPPGYIPDELHQVARNGSFTSINSEGEFIPESMDQMLDPLSLSSPENSGSGSCPSLDSPLDGESYPKSRMPRAQSYPDNHQEFSDYDNPIFEKFGKGGTYPRRYHVSYHHQEYNDGRKTFPRARRTQGTSLRSPVSFSPTDHSLSTSSGSSIFTPEYDDSRIRRRGSDIDNPTLTVMDISPPSRSPRAPTNWRLGKLLGQGAFGRVYLCYDVDTGRELAVKQVQFDPDSPETSKEVNALECEIQLLKNLLHERIVQYYGCLRDPQEKTLSIFMEYMPGGSIKDQLKAYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSTGNVKLGDFGASKRLQTICLSGTGMKSVTGTPYWMSPEVISGEGYGRKADIWSVACTVVEMLTEKPPWAEFEAMAAIFKIATQPTNPKLPPHVSDYTRDFLKRIFVEAKLRPSADELLRHMFVHYH
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
26PhosphorylationKASRPALSLQETRKA
HHCCCCCCHHHHHHH		30.0721712546
30PhosphorylationPALSLQETRKAKSSS
CCCCHHHHHHHHCCC		25.2227732954
35PhosphorylationQETRKAKSSSPKKQN
HHHHHHHCCCCCCCC		40.6924719451
37PhosphorylationTRKAKSSSPKKQNDV
HHHHHCCCCCCCCCC		48.0723403867
79PhosphorylationAKIAFGQSMDLHYTN
HHHHHCCCEEEECCC		18.0428348404
85PhosphorylationQSMDLHYTNNELVIP
CCEEEECCCCEEEEE		22.3328348404
109PhosphorylationAVELLDRSIHMKSLK
HHHHHHHHHHHCCCE		19.2628348404
135PhosphorylationTNLEPLPSLEDLDNT
CCCCCCCCHHHHCCC		52.66-
153PhosphorylationAERKKRLSIIGPTSR
HHHHCCEEEECCCCC		19.0529255136
158PhosphorylationRLSIIGPTSRDRSSP
CEEEECCCCCCCCCC		31.0523927012
159PhosphorylationLSIIGPTSRDRSSPP
EEEECCCCCCCCCCC		35.0023927012
163PhosphorylationGPTSRDRSSPPPGYI
CCCCCCCCCCCCCCC		52.0329255136
164PhosphorylationPTSRDRSSPPPGYIP
CCCCCCCCCCCCCCC		42.1729255136
169PhosphorylationRSSPPPGYIPDELHQ
CCCCCCCCCCHHHHH		18.3023927012
216PhosphorylationPENSGSGSCPSLDSP
CCCCCCCCCCCCCCC		25.2624275569
228PhosphorylationDSPLDGESYPKSRMP
CCCCCCCCCCHHHCC		52.8724719451
229PhosphorylationSPLDGESYPKSRMPR
CCCCCCCCCHHHCCC		15.4626074081
232PhosphorylationDGESYPKSRMPRAQS
CCCCCCHHHCCCCHH		29.3426074081
239PhosphorylationSRMPRAQSYPDNHQE
HHCCCCHHCCCCCCC		37.3322167270
240PhosphorylationRMPRAQSYPDNHQEF
HCCCCHHCCCCCCCC		11.5223927012
248PhosphorylationPDNHQEFSDYDNPIF
CCCCCCCCCCCCHHH		34.2123927012
250PhosphorylationNHQEFSDYDNPIFEK
CCCCCCCCCCHHHHH		19.2023927012
257UbiquitinationYDNPIFEKFGKGGTY
CCCHHHHHCCCCCCC		48.98-
260MethylationPIFEKFGKGGTYPRR
HHHHHCCCCCCCCCE		58.25-
263PhosphorylationEKFGKGGTYPRRYHV
HHCCCCCCCCCEEEE		38.7323312004
264PhosphorylationKFGKGGTYPRRYHVS
HCCCCCCCCCEEEEE		9.6828102081
283PhosphorylationEYNDGRKTFPRARRT
HHCCCCCCCCCCCCC		37.1924719451
290PhosphorylationTFPRARRTQGTSLRS
CCCCCCCCCCCCCCC		26.2923663014
293PhosphorylationRARRTQGTSLRSPVS
CCCCCCCCCCCCCCC		18.1223663014
294PhosphorylationARRTQGTSLRSPVSF
CCCCCCCCCCCCCCC		28.7223663014
297PhosphorylationTQGTSLRSPVSFSPT
CCCCCCCCCCCCCCC		34.6421082442
300PhosphorylationTSLRSPVSFSPTDHS
CCCCCCCCCCCCCCC		24.3221082442
302PhosphorylationLRSPVSFSPTDHSLS
CCCCCCCCCCCCCCC		21.2721082442
304PhosphorylationSPVSFSPTDHSLSTS
CCCCCCCCCCCCCCC		45.1823401153
307PhosphorylationSFSPTDHSLSTSSGS
CCCCCCCCCCCCCCC		27.1623663014
309PhosphorylationSPTDHSLSTSSGSSI
CCCCCCCCCCCCCCC		29.2921082442
310PhosphorylationPTDHSLSTSSGSSIF
CCCCCCCCCCCCCCC		32.0021082442
311PhosphorylationTDHSLSTSSGSSIFT
CCCCCCCCCCCCCCC		29.3527794612
312PhosphorylationDHSLSTSSGSSIFTP
CCCCCCCCCCCCCCC		42.6621082442
314PhosphorylationSLSTSSGSSIFTPEY
CCCCCCCCCCCCCCC		23.3921082442
315PhosphorylationLSTSSGSSIFTPEYD
CCCCCCCCCCCCCCC		25.8321082442
318PhosphorylationSSGSSIFTPEYDDSR
CCCCCCCCCCCCCHH		17.3423663014
321PhosphorylationSSIFTPEYDDSRIRR
CCCCCCCCCCHHHHH		26.6728796482
324PhosphorylationFTPEYDDSRIRRRGS
CCCCCCCHHHHHCCC		27.0628796482
331PhosphorylationSRIRRRGSDIDNPTL
HHHHHCCCCCCCCCE		29.5829255136
337PhosphorylationGSDIDNPTLTVMDIS
CCCCCCCCEEEEECC		41.1230266825
339PhosphorylationDIDNPTLTVMDISPP
CCCCCCEEEEECCCC		19.0930266825
344PhosphorylationTLTVMDISPPSRSPR
CEEEEECCCCCCCCC		26.8830266825
347PhosphorylationVMDISPPSRSPRAPT
EEECCCCCCCCCCCC		49.1030266825
349PhosphorylationDISPPSRSPRAPTNW
ECCCCCCCCCCCCCC		24.0730266825
360UbiquitinationPTNWRLGKLLGQGAF
CCCCHHHHHHCCCCC		45.17-
385UbiquitinationTGRELAVKQVQFDPD
CCCEEEEEEEECCCC		38.8621890473
411UbiquitinationECEIQLLKNLLHERI
HHHHHHHHHHHHHHH		54.89-
432PhosphorylationLRDPQEKTLSIFMEY
CCCCCCCCHHHHHHH		25.61-
450UbiquitinationGSIKDQLKAYGALTE
CCHHHHHHHHCCCCC		33.65-
452PhosphorylationIKDQLKAYGALTENV
HHHHHHHHCCCCCCH		11.0124248375
460PhosphorylationGALTENVTRKYTRQI
CCCCCCHHHHHHHHH		32.7824248375
485UbiquitinationMIVHRDIKGANILRD
CEECCCCCCCCCEEC		57.15-
493PhosphorylationGANILRDSTGNVKLG
CCCCEECCCCCEECC		31.60-
498UbiquitinationRDSTGNVKLGDFGAS
ECCCCCEECCCCCCC		51.24-
505PhosphorylationKLGDFGASKRLQTIC
ECCCCCCCCCEEEEE		20.77-
506UbiquitinationLGDFGASKRLQTICL
CCCCCCCCCEEEEEE		57.50-
514PhosphorylationRLQTICLSGTGMKSV
CEEEEEECCCCCCCC		29.8725159151
516PhosphorylationQTICLSGTGMKSVTG
EEEEECCCCCCCCCC		30.6325159151
518SulfoxidationICLSGTGMKSVTGTP
EEECCCCCCCCCCCC		2.6921406390
520PhosphorylationLSGTGMKSVTGTPYW
ECCCCCCCCCCCCCE		18.9326657352
522PhosphorylationGTGMKSVTGTPYWMS
CCCCCCCCCCCCEEC		42.2928857561
524PhosphorylationGMKSVTGTPYWMSPE
CCCCCCCCCCEECCC		12.1128857561
581UbiquitinationATQPTNPKLPPHVSD
HCCCCCCCCCCCHHH		75.57-
602UbiquitinationKRIFVEAKLRPSADE
HHHHHHHCCCCCHHH		31.3621890473
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
-KUbiquitinationE3 ubiquitin ligaseSTUB1Q9UNE7
PMID:20588253
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:20804422
-KUbiquitinationE3 ubiquitin ligaseXIAPP98170
PMID:18761086
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of M3K2_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 M3K2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MP2K5_HUMANMAP2K5physical
11073940
SH22A_HUMANSH2D2Aphysical
11073940
MP2K7_HUMANMAP2K7physical
10713157
MP2K4_HUMANMAP2K4physical
10713157
MK08_HUMANMAPK8physical
10713157
XIAP_HUMANXIAPphysical
18761086
PIBF1_HUMANPIBF1physical
20936779
MP2K5_HUMANMAP2K5physical
19903815
CHIP_HUMANSTUB1physical
20588253
CHIP_MOUSEStub1physical
20588253
MP2K4_MOUSEMap2k4physical
20588253
SMUF1_HUMANSMURF1physical
19318350
M3K2_HUMANMAP3K2physical
15001576
M3K2_HUMANMAP3K2physical
9162092
MP2K3_HUMANMAP2K3physical
9162092
MP2K4_HUMANMAP2K4physical
9162092
STK38_HUMANSTK38physical
17906693
M3K2_HUMANMAP3K2physical
17906693
MP2K4_HUMANMAP2K4physical
17906693
XIAP_HUMANXIAPphysical
24975362
MP2K5_HUMANMAP2K5physical
24975362
M3K2_HUMANMAP3K2physical
24975362
M3K3_HUMANMAP3K3physical
24975362
MP2K7_HUMANMAP2K7physical
24975362
1433S_HUMANSFNphysical
26496610
M3K3_HUMANMAP3K3physical
26496610
STX3_HUMANSTX3physical
26496610
1433B_HUMANYWHABphysical
26496610
1433E_HUMANYWHAEphysical
26496610
1433G_HUMANYWHAGphysical
26496610
1433Z_HUMANYWHAZphysical
26496610
1433T_HUMANYWHAQphysical
26496610
TRAF7_HUMANTRAF7physical
26496610
CTNB1_HUMANCTNNB1physical
26884171
CBY1_HUMANCBY1physical
27173435
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
DB06616Bosutinib
Regulatory Network of M3K2_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-239; SER-331 ANDSER-344, AND MASS 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-26; SER-153; THR-158;SER-163; SER-239; SER-248; THR-293; SER-294; SER-297; SER-300;SER-302; SER-309; THR-310; SER-312; SER-314; SER-315; SER-331;THR-337; SER-344; SER-347; SER-349 AND SER-514, 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-153; SER-159 ANDSER-164, 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-153; SER-239; SER-331;SER-344 AND SER-349, AND MASS SPECTROMETRY.
"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-163; SER-164 ANDSER-297, AND MASS SPECTROMETRY.
"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-164, 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-164, AND MASSSPECTROMETRY.

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