M3K3_MOUSE - dbPTM
M3K3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID M3K3_MOUSE
UniProt AC Q61084
Protein Name Mitogen-activated protein kinase kinase kinase 3
Gene Name Map3k3
Organism Mus musculus (Mouse).
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 MDEQEALDSIMKDLVALQMSRRTRLSGYETMKNKDTGHPNRQSDVRIKFEHNGERRIIAFSRPVRYEDVEHKVTTVFGQPLDLHYMNNELSILLKNQDDLDKAIDILDRSSSMKSLRILLLSQDRNHTSSSPHSGVSRQVRIKPSQSAGDINTIYQAPEPRSRHLSVSSQNPGRSSPPPGYVPERQQHIARQGSYTSINSEGEFIPETSEQCMLDPLSSAENSLSGSCQSLDRSADSPSFRKSQMSRARSFPDNRKECSDRETQLYDKGVKGGTYPRRYHVSVHHKDYNDGRRTFPRIRRHQGNLFTLVPSSRSLSTNGENMGVAVQYLDPRGRLRSADSENALTVQERNVPTKSPSAPINWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEKILTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMSGTGIRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSHISEHGRDFLRRIFVEARQRPSAEELLTHHFAQLVY
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
20PhosphorylationDLVALQMSRRTRLSG
HHHHHHHHHCCCCCC
12.9729514104
23PhosphorylationALQMSRRTRLSGYET
HHHHHHCCCCCCHHH
34.5529176673
26PhosphorylationMSRRTRLSGYETMKN
HHHCCCCCCHHHHCC
35.7229176673
122PhosphorylationSLRILLLSQDRNHTS
HHHHEEECCCCCCCC
29.9724719451
128PhosphorylationLSQDRNHTSSSPHSG
ECCCCCCCCCCCCCC
33.5827681418
129PhosphorylationSQDRNHTSSSPHSGV
CCCCCCCCCCCCCCC
22.6723684622
130PhosphorylationQDRNHTSSSPHSGVS
CCCCCCCCCCCCCCC
49.3929899451
131PhosphorylationDRNHTSSSPHSGVSR
CCCCCCCCCCCCCCC
26.8026824392
134PhosphorylationHTSSSPHSGVSRQVR
CCCCCCCCCCCCCEE
44.2529472430
137PhosphorylationSSPHSGVSRQVRIKP
CCCCCCCCCCEEECC
22.1128066266
145PhosphorylationRQVRIKPSQSAGDIN
CCEEECCCCCCCCCC
31.5927742792
147PhosphorylationVRIKPSQSAGDINTI
EEECCCCCCCCCCEE
38.2625521595
153PhosphorylationQSAGDINTIYQAPEP
CCCCCCCEEEECCCC
22.7725619855
155PhosphorylationAGDINTIYQAPEPRS
CCCCCEEEECCCCCC
9.1525619855
162PhosphorylationYQAPEPRSRHLSVSS
EECCCCCCCCCCCCC
34.4629514104
166PhosphorylationEPRSRHLSVSSQNPG
CCCCCCCCCCCCCCC
17.5225521595
168PhosphorylationRSRHLSVSSQNPGRS
CCCCCCCCCCCCCCC
23.8821082442
169PhosphorylationSRHLSVSSQNPGRSS
CCCCCCCCCCCCCCC
31.6425619855
175PhosphorylationSSQNPGRSSPPPGYV
CCCCCCCCCCCCCCC
53.7827742792
176PhosphorylationSQNPGRSSPPPGYVP
CCCCCCCCCCCCCCC
39.8127087446
181PhosphorylationRSSPPPGYVPERQQH
CCCCCCCCCCHHHHH
20.7125619855
234PhosphorylationSCQSLDRSADSPSFR
CHHHCCCCCCCHHHH
35.7727180971
237PhosphorylationSLDRSADSPSFRKSQ
HCCCCCCCHHHHHHH
23.3526824392
239PhosphorylationDRSADSPSFRKSQMS
CCCCCCHHHHHHHHH
41.4526060331
249MethylationKSQMSRARSFPDNRK
HHHHHHHHCCCCCCH
37.4116186231
250PhosphorylationSQMSRARSFPDNRKE
HHHHHHHCCCCCCHH
39.9026824392
255MethylationARSFPDNRKECSDRE
HHCCCCCCHHCCHHC
43.4616186239
274PhosphorylationDKGVKGGTYPRRYHV
HCCCCCCCCCCEEEE
38.7323140645
294PhosphorylationDYNDGRRTFPRIRRH
CCCCCCCCCCCCEEC
36.3124719451
307PhosphorylationRHQGNLFTLVPSSRS
ECCCCEEEECCCCCC
29.9728285833
311PhosphorylationNLFTLVPSSRSLSTN
CEEEECCCCCCCCCC
30.7919367708
312PhosphorylationLFTLVPSSRSLSTNG
EEEECCCCCCCCCCC
21.5921454597
314PhosphorylationTLVPSSRSLSTNGEN
EECCCCCCCCCCCCC
28.7225266776
316PhosphorylationVPSSRSLSTNGENMG
CCCCCCCCCCCCCCE
22.5227180971
317PhosphorylationPSSRSLSTNGENMGV
CCCCCCCCCCCCCEE
53.1625266776
328PhosphorylationNMGVAVQYLDPRGRL
CCEEEEEEECCCCCC
13.3825777480
337PhosphorylationDPRGRLRSADSENAL
CCCCCCCCCCCCCCC
40.8127087446
340PhosphorylationGRLRSADSENALTVQ
CCCCCCCCCCCCEEE
32.2525521595
345PhosphorylationADSENALTVQERNVP
CCCCCCCEEECCCCC
20.1025619855
353PhosphorylationVQERNVPTKSPSAPI
EECCCCCCCCCCCCC
39.6123140645
355PhosphorylationERNVPTKSPSAPINW
CCCCCCCCCCCCCCC
26.9426824392
357PhosphorylationNVPTKSPSAPINWRR
CCCCCCCCCCCCCCC
54.4926060331
469PhosphorylationTESVTRKYTRQILEG
CHHHHHHHHHHHHHH
12.1225367039
470PhosphorylationESVTRKYTRQILEGM
HHHHHHHHHHHHHHH
21.0925367039
482PhosphorylationEGMSYLHSNMIVHRD
HHHHHHHCCCEECCC
26.0425367039
511PhosphorylationKLGDFGASKRLQTIC
ECCCCCCCCCCEEEE
20.7729176673
526PhosphorylationMSGTGIRSVTGTPYW
ECCCCEECCCCCCCE
23.3116407301
528PhosphorylationGTGIRSVTGTPYWMS
CCCEECCCCCCCEEC
36.2630635358
530PhosphorylationGIRSVTGTPYWMSPE
CEECCCCCCCEECCC
12.1130635358
532PhosphorylationRSVTGTPYWMSPEVI
ECCCCCCCEECCCCC
17.3730635358
535PhosphorylationTGTPYWMSPEVISGE
CCCCCEECCCCCCCC
12.0830635358
540PhosphorylationWMSPEVISGEGYGRK
EECCCCCCCCCCCCH
35.6530635358
544PhosphorylationEVISGEGYGRKADVW
CCCCCCCCCCHHHHH
14.9530635358
552PhosphorylationGRKADVWSLGCTVVE
CCHHHHHHHCCEEEH
18.0920531401
556PhosphorylationDVWSLGCTVVEMLTE
HHHHHCCEEEHHHHC
26.2820531401
562PhosphorylationCTVVEMLTEKPPWAE
CEEEHHHHCCCCHHH
40.4220531401
570PhosphorylationEKPPWAEYEAMAAIF
CCCCHHHHHHHHHHH
10.9720531401

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
PSP
337SPhosphorylationKinaseSGK1O00141
PSP
337SPhosphorylationKinaseSGK1Q9WVC6
Uniprot
526SPhosphorylationKinaseMAP2K3O09110
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
166SPhosphorylation

21183079
337SPhosphorylation

17242355

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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MP2K5_HUMANMAP2K5physical
10593883

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of M3K3_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337 AND SER-340, ANDMASS SPECTROMETRY.

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