M4K1_HUMAN - dbPTM
M4K1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID M4K1_HUMAN
UniProt AC Q92918
Protein Name Mitogen-activated protein kinase kinase kinase kinase 1
Gene Name MAP4K1
Organism Homo sapiens (Human).
Sequence Length 833
Subcellular Localization
Protein Description Serine/threonine-protein kinase, which may play a role in the response to environmental stress. Appears to act upstream of the JUN N-terminal pathway. May play a role in hematopoietic lineage decisions and growth regulation. Able to autophosphorylate..
Protein Sequence MDVVDPDIFNRDPRDHYDLLQRLGGGTYGEVFKARDKVSGDLVALKMVKMEPDDDVSTLQKEILILKTCRHANIVAYHGSYLWLQKLWICMEFCGAGSLQDIYQVTGSLSELQISYVCREVLQGLAYLHSQKKIHRDIKGANILINDAGEVRLADFGISAQIGATLARRLSFIGTPYWMAPEVAAVALKGGYNELCDIWSLGITAIELAELQPPLFDVHPLRVLFLMTKSGYQPPRLKEKGKWSAAFHNFIKVTLTKSPKKRPSATKMLSHQLVSQPGLNRGLILDLLDKLKNPGKGPSIGDIEDEEPELPPAIPRRIRSTHRSSSLGIPDADCCRRHMEFRKLRGMETRPPANTARLQPPRDLRSSSPRKQLSESSDDDYDDVDIPTPAEDTPPPLPPKPKFRSPSDEGPGSMGDDGQLSPGVLVRCASGPPPNSPRPGPPPSTSSPHLTAHSEPSLWNPPSRELDKPPLLPPKKEKMKRKGCALLVKLFNGCPLRIHSTAAWTHPSTKDQHLLLGAEEGIFILNRNDQEATLEMLFPSRTTWVYSINNVLMSLSGKTPHLYSHSILGLLERKETRAGNPIAHISPHRLLARKNMVSTKIQDTKGCRACCVAEGASSGGPFLCGALETSVVLLQWYQPMNKFLLVRQVLFPLPTPLSVFALLTGPGSELPAVCIGVSPGRPGKSVLFHTVRFGALSCWLGEMSTEHRGPVQVTQVEEDMVMVLMDGSVKLVTPEGSPVRGLRTPEIPMTEAVEAVAMVGGQLQAFWKHGVQVWALGSDQLLQELRDPTLTFRLLGSPRLECSGTISPHCNLLLPGSSNSPASASRVAGITGL
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
17PhosphorylationNRDPRDHYDLLQRLG
CCCCCHHHHHHHHHC		16.7528796482
27PhosphorylationLQRLGGGTYGEVFKA
HHHHCCCCHHHHHHH		31.4629978859
28PhosphorylationQRLGGGTYGEVFKAR
HHHCCCCHHHHHHHH		17.9829978859
33UbiquitinationGTYGEVFKARDKVSG
CCHHHHHHHHHCCCC		47.9229967540
37UbiquitinationEVFKARDKVSGDLVA
HHHHHHHCCCCCEEE		32.5229967540
46UbiquitinationSGDLVALKMVKMEPD
CCCEEEEEEEECCCC		31.7329967540
49UbiquitinationLVALKMVKMEPDDDV
EEEEEEEECCCCCCH		33.7629967540
165PhosphorylationISAQIGATLARRLSF
CCHHHHHHHHHHHHC		18.7524362026
171PhosphorylationATLARRLSFIGTPYW
HHHHHHHHCCCCCCC		17.0128450419
175PhosphorylationRRLSFIGTPYWMAPE
HHHHCCCCCCCCCHH		14.3728450419
177PhosphorylationLSFIGTPYWMAPEVA
HHCCCCCCCCCHHHH		13.9828450419
230PhosphorylationVLFLMTKSGYQPPRL
HEEEEECCCCCCCCH		33.3026657352
232PhosphorylationFLMTKSGYQPPRLKE
EEEECCCCCCCCHHH		25.5711278340
258PhosphorylationIKVTLTKSPKKRPSA
EEEEECCCCCCCCCH		36.39-
296UbiquitinationDKLKNPGKGPSIGDI
HHHCCCCCCCCCCCC		69.7529967540
320PhosphorylationAIPRRIRSTHRSSSL
CCCCCHHCCCCCCCC		26.62-
324PhosphorylationRIRSTHRSSSLGIPD
CHHCCCCCCCCCCCC		19.3723401153
325PhosphorylationIRSTHRSSSLGIPDA
HHCCCCCCCCCCCCH		29.5528450419
326PhosphorylationRSTHRSSSLGIPDAD
HCCCCCCCCCCCCHH		31.6823401153
349PhosphorylationRKLRGMETRPPANTA
HHHCCCCCCCCCCCC		39.31-
355PhosphorylationETRPPANTARLQPPR
CCCCCCCCCCCCCCC		18.4324362026
366PhosphorylationQPPRDLRSSSPRKQL
CCCCHHCCCCCCHHH		42.3315302935
368PhosphorylationPRDLRSSSPRKQLSE
CCHHCCCCCCHHHCC		29.9415302935
374PhosphorylationSSPRKQLSESSDDDY
CCCCHHHCCCCCCCC		32.7017192257
376PhosphorylationPRKQLSESSDDDYDD
CCHHHCCCCCCCCCC		35.3717192257
377PhosphorylationRKQLSESSDDDYDDV
CHHHCCCCCCCCCCC		40.7917192257
381PhosphorylationSESSDDDYDDVDIPT
CCCCCCCCCCCCCCC		22.4917192257
388PhosphorylationYDDVDIPTPAEDTPP
CCCCCCCCCCCCCCC		35.1522210691
393PhosphorylationIPTPAEDTPPPLPPK
CCCCCCCCCCCCCCC		29.2428111955
405PhosphorylationPPKPKFRSPSDEGPG
CCCCCCCCCCCCCCC		31.7122115753
407PhosphorylationKPKFRSPSDEGPGSM
CCCCCCCCCCCCCCC		49.9222115753
413PhosphorylationPSDEGPGSMGDDGQL
CCCCCCCCCCCCCCC		23.7921082442
421PhosphorylationMGDDGQLSPGVLVRC
CCCCCCCCCCEEEEE		16.2423401153
430PhosphorylationGVLVRCASGPPPNSP
CEEEEECCCCCCCCC		56.3028450419
436PhosphorylationASGPPPNSPRPGPPP
CCCCCCCCCCCCCCC		28.2328450419
444PhosphorylationPRPGPPPSTSSPHLT
CCCCCCCCCCCCCCC		46.8528450419
445PhosphorylationRPGPPPSTSSPHLTA
CCCCCCCCCCCCCCC		38.7123684312
446PhosphorylationPGPPPSTSSPHLTAH
CCCCCCCCCCCCCCC		46.3328450419
447PhosphorylationGPPPSTSSPHLTAHS
CCCCCCCCCCCCCCC		19.2128450419
451PhosphorylationSTSSPHLTAHSEPSL
CCCCCCCCCCCCCHH		21.2028450419
454PhosphorylationSPHLTAHSEPSLWNP
CCCCCCCCCCHHCCC		49.0628450419
457PhosphorylationLTAHSEPSLWNPPSR
CCCCCCCHHCCCCCC		41.8028450419
463PhosphorylationPSLWNPPSRELDKPP
CHHCCCCCCCCCCCC		39.3828450419
563PhosphorylationSGKTPHLYSHSILGL
CCCCCHHHHHHHHHH		10.9928064214
586PhosphorylationGNPIAHISPHRLLAR
CCCCCCCCHHHHHHH		12.5624362026
594UbiquitinationPHRLLARKNMVSTKI
HHHHHHHHCCCCCCC		43.7329967540
598PhosphorylationLARKNMVSTKIQDTK
HHHHCCCCCCCCCCC		17.14-
599PhosphorylationARKNMVSTKIQDTKG
HHHCCCCCCCCCCCC		22.28-
600UbiquitinationRKNMVSTKIQDTKGC
HHCCCCCCCCCCCCC		30.7529967540
697PhosphorylationTVRFGALSCWLGEMS
EEEHHHHHHHHHCCC		11.6030257219
733PhosphorylationDGSVKLVTPEGSPVR
CCEEEEECCCCCCCC		26.5130108239
737PhosphorylationKLVTPEGSPVRGLRT
EEECCCCCCCCCCCC		20.6830576142
797PhosphorylationLTFRLLGSPRLECSG
EEEEECCCCCCEECC		13.5520562096
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
165TPhosphorylationKinaseMAP4K1Q92918
GPS
171SPhosphorylationKinasePRKD1Q15139
PSP
381YPhosphorylationKinaseSYKP43405
GPS
381YPhosphorylationKinaseSYKQ15046
PhosphoELM
-KUbiquitinationE3 ubiquitin ligaseFBXW8Q8N3Y1
PMID:24658274
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of M4K1_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 M4K1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GRB2_HUMANGRB2physical
9346925
NCK1_HUMANNCK1physical
9346925
EGFR_HUMANEGFRphysical
9346925
M3K7_HUMANMAP3K7physical
10224067
M3K11_HUMANMAP3K11physical
11053428
CRK_HUMANCRKphysical
9891069
CRKL_HUMANCRKLphysical
9891069
GRB2_HUMANGRB2physical
11279207
PP4C_HUMANPPP4Cphysical
15364934
SPY1_HUMANSPRY1physical
19915061
NCK1_HUMANNCK1physical
22974441
TM101_HUMANTMEM101physical
21988832
SKP1_HUMANSKP1physical
24362026
RBX1_HUMANRBX1physical
24362026
CUL7_HUMANCUL7physical
24362026
FBXW8_HUMANFBXW8physical
24362026
FBXW7_HUMANFBXW7physical
24362026
M4K1_HUMANMAP4K1physical
24362026
PP4C_HUMANPPP4Cphysical
24362026
CAR11_HUMANCARD11physical
19706536
M4K1_HUMANMAP4K1physical
19706536
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 M4K1_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-405; SER-407; SER-413AND SER-421, 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-324; SER-374; SER-376;SER-377; SER-421 AND SER-586, AND MASS SPECTROMETRY.
"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-374; SER-376; TYR-381;SER-407; SER-413; SER-421 AND SER-586, AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366 AND SER-368, ANDMASS SPECTROMETRY.

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