M3K10_HUMAN - dbPTM
M3K10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID M3K10_HUMAN
UniProt AC Q02779
Protein Name Mitogen-activated protein kinase kinase kinase 10
Gene Name MAP3K10
Organism Homo sapiens (Human).
Sequence Length 954
Subcellular Localization
Protein Description Activates the JUN N-terminal pathway..
Protein Sequence MEEEEGAVAKEWGTTPAGPVWTAVFDYEAAGDEELTLRRGDRVQVLSQDCAVSGDEGWWTGQLPSGRVGVFPSNYVAPGAPAAPAGLQLPQEIPFHELQLEEIIGVGGFGKVYRALWRGEEVAVKAARLDPEKDPAVTAEQVCQEARLFGALQHPNIIALRGACLNPPHLCLVMEYARGGALSRVLAGRRVPPHVLVNWAVQVARGMNYLHNDAPVPIIHRDLKSINILILEAIENHNLADTVLKITDFGLAREWHKTTKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMNKLTLPIPSTCPEPFARLLEECWDPDPHGRPDFGSILKRLEVIEQSALFQMPLESFHSLQEDWKLEIQHMFDDLRTKEKELRSREEELLRAAQEQRFQEEQLRRREQELAEREMDIVERELHLLMCQLSQEKPRVRKRKGNFKRSRLLKLREGGSHISLPSGFEHKITVQASPTLDKRKGSDGASPPASPSIIPRLRAIRLTPVDCGGSSSGSSSGGSGTWSRGGPPKKEELVGGKKKGRTWGPSSTLQKERVGGEERLKGLGEGSKQWSSSAPNLGKSPKHTPIAPGFASLNEMEEFAEAEDGGSSVPPSPYSTPSYLSVPLPAEPSPGARAPWEPTPSAPPARWGHGARRRCDLALLGCATLLGAVGLGADVAEARAADGEEQRRWLDGLFFPRAGRFPRGLSPPARPHGRREDVGPGLGLAPSATLVSLSSVSDCNSTRSLLRSDSDEAAPAAPSPPPSPPAPTPTPSPSTNPLVDLELESFKKDPRQSLTPTHVTAACAVSRGHRRTPSDGALGQRGPPEPAGHGPGPRDLLDFPRLPDPQALFPARRRPPEFPGRPTTLTFAPRPRPAASRPRLDPWKLVSFGRTLTISPPSRPDTPESPGPPSVQPTLLDMDMEGQNQDSTVPLCGAHGSH
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
225PhosphorylationIIHRDLKSINILILE
EECCCHHHCCEEEHH
28.3224719451
258PhosphorylationLAREWHKTTKMSAAG
HHHHHHHCCCCCCCC
20.82-
259PhosphorylationAREWHKTTKMSAAGT
HHHHHHCCCCCCCCH
29.5624260401
262PhosphorylationWHKTTKMSAAGTYAW
HHHCCCCCCCCHHHH
19.2721082442
266PhosphorylationTKMSAAGTYAWMAPE
CCCCCCCHHHHHCHH
12.8215610029
281PhosphorylationVIRLSLFSKSSDVWS
HHHHHHCCCCCCHHH
36.6024719451
352PhosphorylationHGRPDFGSILKRLEV
CCCCCHHHHHHHHHH
25.4124719451
446PhosphorylationHLLMCQLSQEKPRVR
HHHHHHHCCCCCCHH
15.49-
489PhosphorylationHKITVQASPTLDKRK
EEEEEEECCCCCCCC
11.0025159151
491PhosphorylationITVQASPTLDKRKGS
EEEEECCCCCCCCCC
45.1325627689
498PhosphorylationTLDKRKGSDGASPPA
CCCCCCCCCCCCCCC
35.5922199227
502PhosphorylationRKGSDGASPPASPSI
CCCCCCCCCCCCCCH
36.6222199227
506PhosphorylationDGASPPASPSIIPRL
CCCCCCCCCCHHHHC
25.5922199227
508PhosphorylationASPPASPSIIPRLRA
CCCCCCCCHHHHCCE
30.5622199227
558PhosphorylationGGKKKGRTWGPSSTL
CCCCCCCCCCCCCCC
43.3622817900
588PhosphorylationEGSKQWSSSAPNLGK
CCCCCCCCCCCCCCC
27.7924719451
589PhosphorylationGSKQWSSSAPNLGKS
CCCCCCCCCCCCCCC
42.0825307156
722PhosphorylationGRFPRGLSPPARPHG
CCCCCCCCCCCCCCC
31.4928555341
775PhosphorylationEAAPAAPSPPPSPPA
CCCCCCCCCCCCCCC
45.3625921289
779PhosphorylationAAPSPPPSPPAPTPT
CCCCCCCCCCCCCCC
49.6525921289
809PhosphorylationFKKDPRQSLTPTHVT
HCCCCCCCCCCCHHH
35.17-
828PhosphorylationVSRGHRRTPSDGALG
HHCCCCCCCCCCCCC
27.4027251275
830PhosphorylationRGHRRTPSDGALGQR
CCCCCCCCCCCCCCC
48.3322817900
857MethylationRDLLDFPRLPDPQAL
HHHCCCCCCCCHHHH
59.87-

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
262SPhosphorylationKinaseMAP4K1Q92918
Uniprot
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:20804422

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of M3K10_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 M3K10_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NDF1_HUMANNEUROD1physical
12881483
RAC1_HUMANRAC1physical
9427749
CDC42_HUMANCDC42physical
9427749
KIF17_HUMANKIF17physical
9427749
KIF3A_HUMANKIF3Aphysical
9427749
KIFA3_HUMANKIFAP3physical
9427749
1433E_HUMANYWHAEphysical
9427749
HPCA_HUMANHPCAphysical
9427749
HD_HUMANHTTphysical
10801775
JIP1_HUMANMAPK8IP1physical
10490659
JIP2_HUMANMAPK8IP2physical
10490659
DYN1_HUMANDNM1physical
9742220
CLH1_HUMANCLTCphysical
12105200
ABL2_HUMANABL2physical
20936779
M3K21_HUMANKIAA1804physical
20936779
CSN2_HUMANCOPS2physical
15062575
M3K10_HUMANMAP3K10physical
11278395
MP2K4_HUMANMAP2K4physical
9182538

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 M3K10_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-506, 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-489; SER-498; SER-502;SER-506; SER-508; THR-558; SER-588; SER-589; THR-828 AND SER-830, ANDMASS 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-489, AND MASSSPECTROMETRY.

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