M3K12_HUMAN - dbPTM
M3K12_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID M3K12_HUMAN
UniProt AC Q12852
Protein Name Mitogen-activated protein kinase kinase kinase 12
Gene Name MAP3K12
Organism Homo sapiens (Human).
Sequence Length 859
Subcellular Localization Cytoplasm. Membrane
Peripheral membrane protein.
Protein Description May be an activator of the JNK/SAPK pathway. Phosphorylates beta-casein, histone 1 and myelin basic protein in vitro..
Protein Sequence MACLHETRTPSPSFGGFVSTLSEASMRKLDPDTSDCTPEKDLTPTHVLQLHEQDAGGPGGAAGSPESRASRVRADEVRLQCQSGSGFLEGLFGCLRPVWTMIGKAYSTEHKQQQEDLWEVPFEEILDLQWVGSGAQGAVFLGRFHGEEVAVKKVRDLKETDIKHLRKLKHPNIITFKGVCTQAPCYCILMEFCAQGQLYEVLRAGRPVTPSLLVDWSMGIAGGMNYLHLHKIIHRDLKSPNMLITYDDVVKISDFGTSKELSDKSTKMSFAGTVAWMAPEVIRNEPVSEKVDIWSFGVVLWELLTGEIPYKDVDSSAIIWGVGSNSLHLPVPSSCPDGFKILLRQCWNSKPRNRPSFRQILLHLDIASADVLSTPQETYFKSQAEWREEVKLHFEKIKSEGTCLHRLEEELVMRRREELRHALDIREHYERKLERANNLYMELNALMLQLELKERELLRREQALERRCPGLLKPHPSRGLLHGNTMEKLIKKRNVPQKLSPHSKRPDILKTESLLPKLDAALSGVGLPGCPKGPPSPGRSRRGKTRHRKASAKGSCGDLPGLRTAVPPHEPGGPGSPGGLGGGPSAWEACPPALRGLHHDLLLRKMSSSSPDLLSAALGSRGRGATGGAGDPGSPPPARGDTPPSEGSAPGSTSPDSPGGAKGEPPPPVGPGEGVGLLGTGREGTSGRGGSRAGSQHLTPAALLYRAAVTRSQKRGISSEEEEGEVDSEVELTSSQRWPQSLNMRQSLSTFSSENPSDGEEGTASEPSPSGTPEVGSTNTDERPDERSDDMCSQGSEIPLDPPPSEVIPGPEPSSLPIPHQELLRERGPPNSEDSDCDSTELDNSNSVDALRPPASLPP
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
7Phosphorylation-MACLHETRTPSPSF
-CCCCCCCCCCCCCC
29.1522199227
9PhosphorylationACLHETRTPSPSFGG
CCCCCCCCCCCCCCH
35.2225850435
11PhosphorylationLHETRTPSPSFGGFV
CCCCCCCCCCCCHHH
32.3422199227
13PhosphorylationETRTPSPSFGGFVST
CCCCCCCCCCHHHHH
40.6425850435
19PhosphorylationPSFGGFVSTLSEASM
CCCCHHHHHHCHHHH
22.7527732954
20PhosphorylationSFGGFVSTLSEASMR
CCCHHHHHHCHHHHH
29.0627732954
37PhosphorylationDPDTSDCTPEKDLTP
CCCCCCCCCCCCCCC
39.20-
43 (in isoform 2)Phosphorylation-35.9522199227
43PhosphorylationCTPEKDLTPTHVLQL
CCCCCCCCCCEEEEE
35.95-
45 (in isoform 2)Phosphorylation-21.2727732954
163UbiquitinationDLKETDIKHLRKLKH
CCCCCCHHHHHHCCC
39.12-
253PhosphorylationYDDVVKISDFGTSKE
HHHEEEHHHCCCCHH
22.5924905233
257PhosphorylationVKISDFGTSKELSDK
EEHHHCCCCHHHCCC
36.3024905233
258PhosphorylationKISDFGTSKELSDKS
EHHHCCCCHHHCCCC
25.2224905233
262PhosphorylationFGTSKELSDKSTKMS
CCCCHHHCCCCCCCC
44.0524905233
265PhosphorylationSKELSDKSTKMSFAG
CHHHCCCCCCCCHHH
37.9524905233
266PhosphorylationKELSDKSTKMSFAGT
HHHCCCCCCCCHHHH
36.1824905233
269PhosphorylationSDKSTKMSFAGTVAW
CCCCCCCCHHHHHHH
17.3228348404
477PhosphorylationGLLKPHPSRGLLHGN
CCCCCCCCCCCCCCC
35.63-
500PhosphorylationRNVPQKLSPHSKRPD
CCCCCCCCCCCCCCC
27.8323312004
503PhosphorylationPQKLSPHSKRPDILK
CCCCCCCCCCCCHHH
33.4730576142
533PhosphorylationGLPGCPKGPPSPGRS
CCCCCCCCCCCCCCC
25.2127251275
536PhosphorylationGCPKGPPSPGRSRRG
CCCCCCCCCCCCCCC
43.0222617229
551PhosphorylationKTRHRKASAKGSCGD
CCCCHHHCCCCCCCC
33.2828555341
555PhosphorylationRKASAKGSCGDLPGL
HHHCCCCCCCCCCCC
17.7728985074
588PhosphorylationGGGPSAWEACPPALR
CCCCCHHHHCCHHHH
39.8627251275
607PhosphorylationDLLLRKMSSSSPDLL
HHHHHHHHCCCHHHH
30.0625850435
608PhosphorylationLLLRKMSSSSPDLLS
HHHHHHHCCCHHHHH
31.1922199227
609PhosphorylationLLRKMSSSSPDLLSA
HHHHHHCCCHHHHHH
38.2930576142
610PhosphorylationLRKMSSSSPDLLSAA
HHHHHCCCHHHHHHH
25.1222199227
615PhosphorylationSSSPDLLSAALGSRG
CCCHHHHHHHHCCCC
20.8422199227
620PhosphorylationLLSAALGSRGRGATG
HHHHHHCCCCCCCCC
32.2022199227
634PhosphorylationGGAGDPGSPPPARGD
CCCCCCCCCCCCCCC
39.3529255136
640PhosphorylationGSPPPARGDTPPSEG
CCCCCCCCCCCCCCC
45.2927251275
642PhosphorylationPPPARGDTPPSEGSA
CCCCCCCCCCCCCCC
39.67-
645PhosphorylationARGDTPPSEGSAPGS
CCCCCCCCCCCCCCC
56.65-
652PhosphorylationSEGSAPGSTSPDSPG
CCCCCCCCCCCCCCC
25.3427732954
653PhosphorylationEGSAPGSTSPDSPGG
CCCCCCCCCCCCCCC
50.6327732954
654PhosphorylationGSAPGSTSPDSPGGA
CCCCCCCCCCCCCCC
28.5427732954
657PhosphorylationPGSTSPDSPGGAKGE
CCCCCCCCCCCCCCC
28.9127732954
695PhosphorylationRGGSRAGSQHLTPAA
CCCCCCCCCCCCHHH
17.2821712546
699PhosphorylationRAGSQHLTPAALLYR
CCCCCCCCHHHHHHH
14.5721712546
728PhosphorylationEEEGEVDSEVELTSS
CCCCCCCCCEEECCC
49.0327251275
757PhosphorylationTFSSENPSDGEEGTA
HCCCCCCCCCCCCCC
70.5922817900
788PhosphorylationDERPDERSDDMCSQG
CCCCCCCCCCCHHCC
35.6022210691
793PhosphorylationERSDDMCSQGSEIPL
CCCCCCHHCCCCCCC
30.8222210691
796PhosphorylationDDMCSQGSEIPLDPP
CCCHHCCCCCCCCCC
25.3922210691

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:16931512

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of M3K12_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 M3K12_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
JIP1_HUMANMAPK8IP1physical
10490659
JIP2_HUMANMAPK8IP2physical
10490659
MP2K7_HUMANMAP2K7physical
10187804

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 M3K12_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-634 AND SER-757, ANDMASS SPECTROMETRY.

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