M3K3_HUMAN - dbPTM
M3K3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID M3K3_HUMAN
UniProt AC Q99759
Protein Name Mitogen-activated protein kinase kinase kinase 3
Gene Name MAP3K3
Organism Homo sapiens (Human).
Sequence Length 626
Subcellular Localization
Protein Description Component of a protein kinase signal transduction cascade. Mediates activation of the NF-kappa-B, AP1 and DDIT3 transcriptional regulators..
Protein Sequence MDEQEALNSIMNDLVALQMNRRHRMPGYETMKNKDTGHSNRQSDVRIKFEHNGERRIIAFSRPVKYEDVEHKVTTVFGQPLDLHYMNNELSILLKNQDDLDKAIDILDRSSSMKSLRILLLSQDRNHNSSSPHSGVSRQVRIKASQSAGDINTIYQPPEPRSRHLSVSSQNPGRSSPPPGYVPERQQHIARQGSYTSINSEGEFIPETSEQCMLDPLSSAENSLSGSCQSLDRSADSPSFRKSRMSRAQSFPDNRQEYSDRETQLYDKGVKGGTYPRRYHVSVHHKDYSDGRRTFPRIRRHQGNLFTLVPSSRSLSTNGENMGLAVQYLDPRGRLRSADSENALSVQERNVPTKSPSAPINWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEKTLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSHISEHGRDFLRRIFVEARQRPSAEELLTHHFAQLMY
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
28PhosphorylationRRHRMPGYETMKNKD
HHCCCCCCHHCCCCC		11.4529083192
30PhosphorylationHRMPGYETMKNKDTG
CCCCCCHHCCCCCCC		25.5929083192
36PhosphorylationETMKNKDTGHSNRQS
HHCCCCCCCCCCCCC		38.1022210691
39PhosphorylationKNKDTGHSNRQSDVR
CCCCCCCCCCCCCEE		34.7422210691
50 (in isoform 2)Phosphorylation-31.2924275569
55 (in isoform 2)Phosphorylation-36.1725159151
57 (in isoform 2)Phosphorylation-3.1424275569
59 (in isoform 2)Phosphorylation-8.2624275569
102UbiquitinationKNQDDLDKAIDILDR
CCHHHHHHHHHHHHH		55.31-
122PhosphorylationSLRILLLSQDRNHNS
HHHHHHHCCCCCCCC		29.9729214152
129PhosphorylationSQDRNHNSSSPHSGV
CCCCCCCCCCCCCCC		25.3327732954
130PhosphorylationQDRNHNSSSPHSGVS
CCCCCCCCCCCCCCC		53.8818691976
131PhosphorylationDRNHNSSSPHSGVSR
CCCCCCCCCCCCCCH		26.8426055452
134PhosphorylationHNSSSPHSGVSRQVR
CCCCCCCCCCCHHHE		44.2527732954
137PhosphorylationSSPHSGVSRQVRIKA
CCCCCCCCHHHEEEE		22.1127732954
145PhosphorylationRQVRIKASQSAGDIN
HHHEEEECCCCCCCC		21.4821945579
147PhosphorylationVRIKASQSAGDINTI
HEEEECCCCCCCCCC		31.5521945579
153PhosphorylationQSAGDINTIYQPPEP
CCCCCCCCCCCCCCC		22.7721945579
155PhosphorylationAGDINTIYQPPEPRS
CCCCCCCCCCCCCCC		16.9621945579
162PhosphorylationYQPPEPRSRHLSVSS
CCCCCCCCCCCCCCC		34.4618691976
162 (in isoform 2)Phosphorylation-34.4627251275
166PhosphorylationEPRSRHLSVSSQNPG
CCCCCCCCCCCCCCC		17.5223401153
168PhosphorylationRSRHLSVSSQNPGRS
CCCCCCCCCCCCCCC		23.8822115753
169PhosphorylationSRHLSVSSQNPGRSS
CCCCCCCCCCCCCCC		31.6423401153
175PhosphorylationSSQNPGRSSPPPGYV
CCCCCCCCCCCCCCC		53.7823401153
176PhosphorylationSQNPGRSSPPPGYVP
CCCCCCCCCCCCCCC		39.8123401153
176 (in isoform 2)Phosphorylation-39.8127642862
178 (in isoform 2)Phosphorylation-36.5824719451
181PhosphorylationRSSPPPGYVPERQQH
CCCCCCCCCCHHHHH		20.7123403867
186 (in isoform 2)Phosphorylation-37.2327642862
194PhosphorylationQHIARQGSYTSINSE
HHHHHCCCCCEECCC		19.52-
197PhosphorylationARQGSYTSINSEGEF
HHCCCCCEECCCCCC		16.1318691976
197 (in isoform 2)Phosphorylation-16.1324719451
199 (in isoform 2)Phosphorylation-33.5024719451
200 (in isoform 2)Phosphorylation-45.3627251275
207 (in isoform 2)Phosphorylation-61.2124719451
234PhosphorylationSCQSLDRSADSPSFR
CHHHCCCCCCCHHHH		35.7717192257
237PhosphorylationSLDRSADSPSFRKSR
HCCCCCCCHHHHHHH		23.3523401153
239PhosphorylationDRSADSPSFRKSRMS
CCCCCCHHHHHHHHH		41.4523403867
250PhosphorylationSRMSRAQSFPDNRQE
HHHHHHHHCCCCHHH		37.4523401153
259PhosphorylationPDNRQEYSDRETQLY
CCCHHHHCHHCCHHH		29.4623186163
263PhosphorylationQEYSDRETQLYDKGV
HHHCHHCCHHHHCCC		25.4324719451
266PhosphorylationSDRETQLYDKGVKGG
CHHCCHHHHCCCCCC		13.0424719451
268 (in isoform 2)Phosphorylation-52.6324719451
274PhosphorylationDKGVKGGTYPRRYHV
HCCCCCCCCCCEEEE		38.7328102081
275PhosphorylationKGVKGGTYPRRYHVS
CCCCCCCCCCEEEEE		9.6828102081
281 (in isoform 2)Phosphorylation-4.7924719451
288PhosphorylationVSVHHKDYSDGRRTF
EEEECCCCCCCCCCC		17.2923403867
289PhosphorylationSVHHKDYSDGRRTFP
EEECCCCCCCCCCCC		43.6623403867
294PhosphorylationDYSDGRRTFPRIRRH
CCCCCCCCCCCCEEC		36.3123401153
294 (in isoform 2)Phosphorylation-36.3124719451
297 (in isoform 2)Phosphorylation-30.7524719451
305 (in isoform 2)Phosphorylation-4.4224719451
306 (in isoform 2)Phosphorylation-6.0224719451
311PhosphorylationNLFTLVPSSRSLSTN
CEEEECCCCCCCCCC		30.7925849741
312PhosphorylationLFTLVPSSRSLSTNG
EEEECCCCCCCCCCC		21.5925849741
314PhosphorylationTLVPSSRSLSTNGEN
EECCCCCCCCCCCCC		28.7222617229
316PhosphorylationVPSSRSLSTNGENMG
CCCCCCCCCCCCCCE		22.5222115753
317PhosphorylationPSSRSLSTNGENMGL
CCCCCCCCCCCCCEE		53.1627273156
325 (in isoform 2)Phosphorylation-4.8027251275
337PhosphorylationDPRGRLRSADSENAL
CCCCCCCCCCCCCCC		40.8127273156
340PhosphorylationGRLRSADSENALSVQ
CCCCCCCCCCCCCHH		32.2529255136
343 (in isoform 2)Phosphorylation-9.3627251275
345PhosphorylationADSENALSVQERNVP
CCCCCCCCHHHCCCC		21.2423403867
345 (in isoform 2)Phosphorylation-21.2424719451
348 (in isoform 2)Phosphorylation-44.0327251275
353PhosphorylationVQERNVPTKSPSAPI
HHHCCCCCCCCCCCC		39.6123403867
355PhosphorylationERNVPTKSPSAPINW
HCCCCCCCCCCCCCC		26.9423401153
357PhosphorylationNVPTKSPSAPINWRR
CCCCCCCCCCCCCCC		54.4928102081
366UbiquitinationPINWRRGKLLGQGAF
CCCCCCCCCCCCCCC		38.43-
368 (in isoform 2)Phosphorylation-5.6924719451
371 (in isoform 2)Phosphorylation-22.5224719451
384PhosphorylationYLCYDVDTGRELASK
EEEEECCCCCCHHHH		37.6818691976
386 (in isoform 2)Phosphorylation-37.5424719451
391UbiquitinationTGRELASKQVQFDPD
CCCCHHHHCCCCCCC		49.21-
397 (in isoform 2)Ubiquitination-45.31-
404UbiquitinationPDSPETSKEVSALEC
CCCCCHHHHHHHHHH		70.34-
417UbiquitinationECEIQLLKNLQHERI
HHHHHHHHHCCHHHH		65.29-
427PhosphorylationQHERIVQYYGCLRDR
CHHHHHHHHHHHHHH		7.3118083107
428PhosphorylationHERIVQYYGCLRDRA
HHHHHHHHHHHHHHH		5.5818083107
438PhosphorylationLRDRAEKTLTIFMEY
HHHHHHHHEEEEEEC		22.1929759185
440PhosphorylationDRAEKTLTIFMEYMP
HHHHHHEEEEEECCC		19.8729759185
445PhosphorylationTLTIFMEYMPGGSVK
HEEEEEECCCCCCHH		9.2329759185
456UbiquitinationGSVKDQLKAYGALTE
CCHHHHHHHHCCCCH		33.65-
458PhosphorylationVKDQLKAYGALTESV
HHHHHHHHCCCCHHH		11.0128152594
464PhosphorylationAYGALTESVTRKYTR
HHCCCCHHHHHHHHH		24.4519060867
470PhosphorylationESVTRKYTRQILEGM
HHHHHHHHHHHHHHH		21.0924719451
482PhosphorylationEGMSYLHSNMIVHRD
HHHHHHHCCCEECCC		26.0424719451
491UbiquitinationMIVHRDIKGANILRD
CEECCCCCCCCCEEC		57.15-
499PhosphorylationGANILRDSAGNVKLG
CCCCEECCCCCEECC		31.4823403867
504UbiquitinationRDSAGNVKLGDFGAS
ECCCCCEECCCCCCC		51.24-
511PhosphorylationKLGDFGASKRLQTIC
ECCCCCCCCCCEEEE		20.77-
512UbiquitinationLGDFGASKRLQTICM
CCCCCCCCCCEEEEE		57.50-
516PhosphorylationGASKRLQTICMSGTG
CCCCCCEEEEECCCC		22.2720448038
520PhosphorylationRLQTICMSGTGMRSV
CCEEEEECCCCCCCC		28.8820448038
526PhosphorylationMSGTGMRSVTGTPYW
ECCCCCCCCCCCCCC		18.3526657352
528PhosphorylationGTGMRSVTGTPYWMS
CCCCCCCCCCCCCCC		36.2628857561
530PhosphorylationGMRSVTGTPYWMSPE
CCCCCCCCCCCCCCE		12.1128857561
557 (in isoform 2)Phosphorylation-3.9027251275
590PhosphorylationPTNPQLPSHISEHGR
CCCCCCCHHHHHHHH		41.8826307563
593PhosphorylationPQLPSHISEHGRDFL
CCCCHHHHHHHHHHH		20.3726307563
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
166SPhosphorylationKinaseSGK1O00141
Uniprot
166SPhosphorylationKinaseSGK-FAMILY-GPS
166SPhosphorylationKinaseSGK_GROUP-PhosphoELM
337SPhosphorylationKinaseSGK1O00141
Uniprot
337SPhosphorylationKinaseSGK-FAMILY-GPS
337SPhosphorylationKinaseSGK_GROUP-PhosphoELM
526SPhosphorylationKinaseMAP3K3Q99759
GPS
-KUbiquitinationE3 ubiquitin ligaseXIAPP98170
PMID:24975362
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
166SPhosphorylation

12761204
337SPhosphorylation

12761204
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 M3K3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MP2K5_HUMANMAP2K5physical
11073940
1433G_HUMANYWHAGphysical
14743216
PDRG1_HUMANPDRG1physical
14743216
CDC37_HUMANCDC37physical
14743216
HSP74_HUMANHSPA4physical
14743216
MARK2_HUMANMARK2physical
14743216
PFD2_HUMANPFDN2physical
14743216
TRAF7_HUMANTRAF7physical
14743216
MP2K5_HUMANMAP2K5physical
14743216
ZBT16_HUMANZBTB16physical
16169070
1433E_HUMANYWHAEphysical
9452471
GAB1_HUMANGAB1physical
12065326
VWF_HUMANVWFphysical
20936779
CSN5_HUMANCOPS5physical
20936779
HS90A_HUMANHSP90AA1physical
19560753
SQSTM_HUMANSQSTM1physical
19903815
MP2K5_HUMANMAP2K5physical
19903815
TRAF6_HUMANTRAF6physical
19903815
TM1L1_HUMANTOM1L1physical
21900206
SMUF1_HUMANSMURF1physical
19318350
M3K7_HUMANMAP3K7physical
19843958
TRAF6_HUMANTRAF6physical
19843958
RIPK1_HUMANRIPK1physical
11429546
M3K3_HUMANMAP3K3physical
15001576
MP2K4_HUMANMAP2K4physical
9162092
MP2K3_HUMANMAP2K3physical
9162092
MP2K5_HUMANMAP2K5physical
12813044
M3K7_HUMANMAP3K7physical
16260783
IRAK1_HUMANIRAK1physical
17197697
MP2K5_HUMANMAP2K5physical
16861740
XIAP_HUMANXIAPphysical
24975362
MBP_HUMANMBPphysical
24975362
MP2K5_HUMANMAP2K5physical
24975362
MP2K7_HUMANMAP2K7physical
24975362
GLRX3_HUMANGLRX3physical
25416956
NBR1_HUMANNBR1physical
25043814
MP2K5_HUMANMAP2K5physical
25241761
FLNA_HUMANFLNAphysical
25241761
IKKA_HUMANCHUKphysical
25241761
TRAF6_HUMANTRAF6physical
25241761
KAPCA_HUMANPRKACAphysical
25241761
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
There are no disease associations of PTM sites.
Regulatory Network of M3K3_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-337 AND SER-340, 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-129; SER-130; SER-145;SER-147; SER-166; SER-168; SER-175; SER-176; SER-237; SER-250;SER-311; SER-314; SER-316; THR-317; SER-337; SER-340; THR-353;SER-355; SER-464 AND SER-526, 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-340, AND MASSSPECTROMETRY.
"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-131; SER-166; SER-234;SER-237; SER-250; SER-337; SER-340 AND SER-355, 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-166, 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 TYR-288; SER-289 ANDTHR-294, AND MASS SPECTROMETRY.
"Inhibition of mitogen-activated kinase kinase kinase 3 activitythrough phosphorylation by the serum- and glucocorticoid-inducedkinase 1.";
Chun J., Kwon T., Kim D.J., Park I., Chung G., Lee E.J., Hong S.K.,Chang S.I., Kim H.Y., Kang S.S.;
J. Biochem. 133:103-108(2003).
Cited for: PHOSPHORYLATION AT SER-166 AND SER-337 BY SGK1.

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