M4K5_HUMAN - dbPTM
M4K5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID M4K5_HUMAN
UniProt AC Q9Y4K4
Protein Name Mitogen-activated protein kinase kinase kinase kinase 5
Gene Name MAP4K5
Organism Homo sapiens (Human).
Sequence Length 846
Subcellular Localization Cytoplasm .
Protein Description May play a role in the response to environmental stress. Appears to act upstream of the JUN N-terminal pathway..
Protein Sequence MEAPLRPAADILRRNPQQDYELVQRVGSGTYGDVYKARNVHTGELAAVKIIKLEPGDDFSLIQQEIFMVKECKHCNIVAYFGSYLSREKLWICMEYCGGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHTKGKMHRDIKGANILLTDHGDVKLADFGVAAKITATIAKRKSFIGTPYWMAPEVAAVEKNGGYNQLCDIWAVGITAIELGELQPPMFDLHPMRALFLMSKSNFQPPKLKDKTKWSSTFHNFVKIALTKNPKKRPTAERLLTHTFVAQPGLSRALAVELLDKVNNPDNHAHYTEADDDDFEPHAIIRHTIRSTNRNARAERTASEINFDKLQFEPPLRKETEARDEMGLSSDPNFMLQWNPFVDGANTGKSTSKRAIPPPLPPKPRISSYPEDNFPDEEKASTIKHCPDSESRAPQILRRQSSPSCGPVAETSSIGNGDGISKLMSENTEGSAQAPQLPRKKDKRDFPKPAINGLPPTPKVLMGACFSKVFDGCPLKINCATSWIHPDTKDQYIIFGTEDGIYTLNLNELHEATMEQLFPRKCTWLYVINNTLMSLSVGKTFQLYSHNLIALFEHAKKPGLAAHIQTHRFPDRILPRKFALTTKIPDTKGCHKCCIVRNPYTGHKYLCGALQSGIVLLQWYEPMQKFMLIKHFDFPLPSPLNVFEMLVIPEQEYPMVCVAISKGTESNQVVQFETINLNSASSWFTEIGAGSQQLDSIHVTQLERDTVLVCLDKFVKIVNLQGKLKSSKKLASELSFDFRIESVVCLQDSVLAFWKHGMQGKSFKSDEVTQEISDETRVFRLLGSDRVVVLESRPTENPTAHSNLYILAGHENSY
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
20PhosphorylationRRNPQQDYELVQRVG
HHCHHHCHHHHHHHC		13.5628796482
30PhosphorylationVQRVGSGTYGDVYKA
HHHHCCCCCCCEEEE		26.4828152594
31PhosphorylationQRVGSGTYGDVYKAR
HHHCCCCCCCEEEEC		18.1727155012
35PhosphorylationSGTYGDVYKARNVHT
CCCCCCEEEECCCCC		12.0428152594
36UbiquitinationGTYGDVYKARNVHTG
CCCCCEEEECCCCCC		40.49-
134MalonylationGLAYLHTKGKMHRDI
HHHHHHHCCCCCCCC		45.8726320211
134AcetylationGLAYLHTKGKMHRDI
HHHHHHHCCCCCCCC		45.8719608861
142UbiquitinationGKMHRDIKGANILLT
CCCCCCCCCCCEEEE		57.15-
166PhosphorylationFGVAAKITATIAKRK
HCHHHEEHHHHHHCC		19.6228060719
168PhosphorylationVAAKITATIAKRKSF
HHHEEHHHHHHCCCC		16.9028060719
171UbiquitinationKITATIAKRKSFIGT
EEHHHHHHCCCCCCC		57.41-
174PhosphorylationATIAKRKSFIGTPYW
HHHHHCCCCCCCCCC		26.5725106551
178PhosphorylationKRKSFIGTPYWMAPE
HCCCCCCCCCCCCHH		14.3725106551
267PhosphorylationKNPKKRPTAERLLTH
CCCCCCCCHHHHHHH		45.22-
303PhosphorylationNPDNHAHYTEADDDD
CCCCCCCCCCCCCCC		13.6827642862
304PhosphorylationPDNHAHYTEADDDDF
CCCCCCCCCCCCCCC		18.1627251275
320PhosphorylationPHAIIRHTIRSTNRN
HHHHHHHHHHHCCCC		14.2927251275
333PhosphorylationRNARAERTASEINFD
CCHHHHHHHHHCCCC		26.4930266825
335PhosphorylationARAERTASEINFDKL
HHHHHHHHHCCCCCC		38.0919664994
341UbiquitinationASEINFDKLQFEPPL
HHHCCCCCCCCCCCC		39.80-
379PhosphorylationPFVDGANTGKSTSKR
CCCCCCCCCCCCCCC		45.5127251275
382PhosphorylationDGANTGKSTSKRAIP
CCCCCCCCCCCCCCC		38.9823312004
383PhosphorylationGANTGKSTSKRAIPP
CCCCCCCCCCCCCCC		41.5823312004
384PhosphorylationANTGKSTSKRAIPPP
CCCCCCCCCCCCCCC		27.5123312004
399PhosphorylationLPPKPRISSYPEDNF
CCCCCCCCCCCCCCC		25.7128102081
400PhosphorylationPPKPRISSYPEDNFP
CCCCCCCCCCCCCCC		42.1928355574
401PhosphorylationPKPRISSYPEDNFPD
CCCCCCCCCCCCCCC		12.1225159151
411UbiquitinationDNFPDEEKASTIKHC
CCCCCHHHHHCCCCC		45.66-
413PhosphorylationFPDEEKASTIKHCPD
CCCHHHHHCCCCCCC		41.5628060719
414PhosphorylationPDEEKASTIKHCPDS
CCHHHHHCCCCCCCC		38.6128060719
421PhosphorylationTIKHCPDSESRAPQI
CCCCCCCCCCHHHHH		23.7126074081
423PhosphorylationKHCPDSESRAPQILR
CCCCCCCCHHHHHHH		37.3826074081
433PhosphorylationPQILRRQSSPSCGPV
HHHHHHCCCCCCCCC		42.2623401153
434PhosphorylationQILRRQSSPSCGPVA
HHHHHCCCCCCCCCC		16.7023927012
436PhosphorylationLRRQSSPSCGPVAET
HHHCCCCCCCCCCCC		33.3823401153
443PhosphorylationSCGPVAETSSIGNGD
CCCCCCCCCCCCCCC		20.3123927012
444PhosphorylationCGPVAETSSIGNGDG
CCCCCCCCCCCCCCH		16.0923927012
445PhosphorylationGPVAETSSIGNGDGI
CCCCCCCCCCCCCHH		41.7723927012
453PhosphorylationIGNGDGISKLMSENT
CCCCCHHHHHHHCCC		25.8523927012
456SulfoxidationGDGISKLMSENTEGS
CCHHHHHHHCCCCCC		5.6221406390
500UbiquitinationLMGACFSKVFDGCPL
HHHHHHHHHHCCCCE		27.0321906983
508UbiquitinationVFDGCPLKINCATSW
HHCCCCEEEEEECEE		19.60-
558PhosphorylationPRKCTWLYVINNTLM
CCCCEEEEEECCEEE		7.2819702290
589UbiquitinationALFEHAKKPGLAAHI
HHHHHCCCCCHHHHH		45.13-
598PhosphorylationGLAAHIQTHRFPDRI
CHHHHHHCCCCCCCC		17.8928555341
609UbiquitinationPDRILPRKFALTTKI
CCCCCCCCEEEECCC		32.80-
615UbiquitinationRKFALTTKIPDTKGC
CCEEEECCCCCCCCC		47.18-
624UbiquitinationPDTKGCHKCCIVRNP
CCCCCCCCEEEECCC		34.57-
748UbiquitinationVCLDKFVKIVNLQGK
EEHHHHHHHHCCCCC		44.03-
755UbiquitinationKIVNLQGKLKSSKKL
HHHCCCCCCCCCHHH		39.52-
793UbiquitinationWKHGMQGKSFKSDEV
HHCCCCCCCCCCCHH		35.51-
796UbiquitinationGMQGKSFKSDEVTQE
CCCCCCCCCCHHHHH		65.18-
816PhosphorylationRVFRLLGSDRVVVLE
HHHHHCCCCEEEEEE		23.3918452278
845PhosphorylationILAGHENSY------
EEECCCCCC------		29.2729523821
846PhosphorylationLAGHENSY-------
EECCCCCC-------		33.8726471730
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 ligaseSMURF1Q9HCE7
PMID:20804422
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of M4K5_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 M4K5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CRK_HUMANCRKphysical
10648385
CRKL_HUMANCRKLphysical
10648385
TRAF2_HUMANTRAF2physical
10477597
HCK_HUMANHCKphysical
20936779
CSN5_HUMANCOPS5physical
20936779
ZN440_HUMANZNF440physical
20936779
SETB1_HUMANSETDB1physical
21900206
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 M4K5_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-335, AND MASSSPECTROMETRY.
"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-335, AND MASSSPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-401, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-31, AND MASSSPECTROMETRY.

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