MK07_HUMAN - dbPTM
MK07_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MK07_HUMAN
UniProt AC Q13164
Protein Name Mitogen-activated protein kinase 7
Gene Name MAPK7
Organism Homo sapiens (Human).
Sequence Length 816
Subcellular Localization Cytoplasm. Nucleus. Nucleus, PML body. Translocates to the nucleus upon activation.
Protein Description Plays a role in various cellular processes such as proliferation, differentiation and cell survival. The upstream activator of MAPK7 is the MAPK kinase MAP2K5. Upon activation, it translocates to the nucleus and phosphorylates various downstream targets including MEF2C. EGF activates MAPK7 through a Ras-independent and MAP2K5-dependent pathway. May have a role in muscle cell differentiation. May be important for endothelial function and maintenance of blood vessel integrity. MAP2K5 and MAPK7 interact specifically with one another and not with MEK1/ERK1 or MEK2/ERK2 pathways. Phosphorylates SGK1 at Ser-78 and this is required for growth factor-induced cell cycle progression. Involved in the regulation of p53/TP53 by disrupting the PML-MDM2 interaction..
Protein Sequence MAEPLKEEDGEDGSAEPPGPVKAEPAHTAASVAAKNLALLKARSFDVTFDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYGEFKSVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPAEHQYFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQAVGAERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFLAKYHDPDDEPDCAPPFDFAFDREALTRERIKEAIVAEIEDFHARREGIRQQIRFQPSLQPVASEPGCPDVEMPSPWAPSGDCAMESPPPAPPPCPGPAPDTIDLTLQPPPPVSEPAPPKKDGAISDNTKAALKAALLKSLRSRLRDGPSAPLEAPEPRKPVTAQERQREREEKRRRRQERAKEREKRRQERERKERGAGASGGPSTDPLAGLVLSDNDRSLLERWTRMARPAAPALTSVPAPAPAPTPTPTPVQPTSPPPGPVAQPTGPQPQSAGSTSGPVPQPACPPPGPAPHPTGPPGPIPVPAPPQIATSTSLLAAQSLVPPPGLPGSSTPGVLPYFPPGLPPPDAGGAPQSSMSESPDVNLVTQQLSKSQVEDPLPPVFSGTPKGSGAGYGVGFDLEEFLNQSFDMGVADGPQDGQADSASLSASLLADWLEGHGMNPADIESLQREIQMDSPMLLADLPDLQDP
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
2Acetylation------MAEPLKEED
------CCCCCCCCC		27.41-
6Sumoylation--MAEPLKEEDGEDG
--CCCCCCCCCCCCC		70.54-
14PhosphorylationEEDGEDGSAEPPGPV
CCCCCCCCCCCCCCC		41.6128348404
22SumoylationAEPPGPVKAEPAHTA
CCCCCCCCCCCCCHH		50.60-
28PhosphorylationVKAEPAHTAASVAAK
CCCCCCCHHHHHHHH		26.4812628002
31PhosphorylationEPAHTAASVAAKNLA
CCCCHHHHHHHHHHH		15.1521924351
35AcetylationTAASVAAKNLALLKA
HHHHHHHHHHHHHHH		42.6419608861
70PhosphorylationNGAYGVVSSARRRLT
CCHHHHHHHHHHHHC		18.84-
71PhosphorylationGAYGVVSSARRRLTG
CHHHHHHHHHHHHCC		17.74-
84AcetylationTGQQVAIKKIPNAFD
CCCEEEEECCCCHHH		34.6125953088
110UbiquitinationLKILKHFKHDNIIAI
HHHHHHCCCCCEEEE		50.17-
118UbiquitinationHDNIIAIKDILRPTV
CCCEEEEEHHHCCCC		29.69-
184UbiquitinationQVIHRDLKPSNLLVN
EEECCCCCHHHEEEC		51.17-
209PhosphorylationGMARGLCTSPAEHQY
CCCCCCCCCHHHHHH		42.6726356563
210PhosphorylationMARGLCTSPAEHQYF
CCCCCCCCHHHHHHH		22.5528152594
216PhosphorylationTSPAEHQYFMTEYVA
CCHHHHHHHHHHHHH		9.3828152594
218PhosphorylationPAEHQYFMTEYVATR
HHHHHHHHHHHHHHC		2.0711739740
219PhosphorylationAEHQYFMTEYVATRW
HHHHHHHHHHHHHCH		17.7922322096
220PhosphorylationEHQYFMTEYVATRWY
HHHHHHHHHHHHCHH		26.6511739740
221DephosphorylationHQYFMTEYVATRWYR
HHHHHHHHHHHCHHC		6.0412042304
221PhosphorylationHQYFMTEYVATRWYR
HHHHHHHHHHHCHHC		6.0427273156
224PhosphorylationFMTEYVATRWYRAPE
HHHHHHHHCHHCCHH		16.2221082442
267PhosphorylationQLFPGKNYVHQLQLI
CCCCCCCHHHHHHHH		11.6424043423
280PhosphorylationLIMMVLGTPSPAVIQ
HHHHHHCCCCHHHHH		19.2124043423
282PhosphorylationMMVLGTPSPAVIQAV
HHHHCCCCHHHHHHH		25.9024043423
300PhosphorylationRVRAYIQSLPPRQPV
HHHHHHHCCCCCCCC		33.0324719451
322PhosphorylationGADRQALSLLGRMLR
CCCHHHHHHHHHHHH		25.2721924351
337PhosphorylationFEPSARISAAAALRH
CCCHHHHHHHHHHHC		13.3029691806
378UbiquitinationALTRERIKEAIVAEI
HHCHHHHHHHHHHHH		47.52-
421PhosphorylationCPDVEMPSPWAPSGD
CCCCCCCCCCCCCCC		31.5921924351
433PhosphorylationSGDCAMESPPPAPPP
CCCCCCCCCCCCCCC		29.6221924351
472PhosphorylationPKKDGAISDNTKAAL
CCCCCCCCHHHHHHH		25.0321924351
476UbiquitinationGAISDNTKAALKAAL
CCCCHHHHHHHHHHH		37.61-
480MethylationDNTKAALKAALLKSL
HHHHHHHHHHHHHHH		27.21-
485MethylationALKAALLKSLRSRLR
HHHHHHHHHHHHHHC		48.58-
486PhosphorylationLKAALLKSLRSRLRD
HHHHHHHHHHHHHCC		29.0524117733
496PhosphorylationSRLRDGPSAPLEAPE
HHHCCCCCCCCCCCC		48.3122267842
552PhosphorylationAGASGGPSTDPLAGL
CCCCCCCCCCCCCCE		49.0327732954
553PhosphorylationGASGGPSTDPLAGLV
CCCCCCCCCCCCCEE		44.7827732954
562PhosphorylationPLAGLVLSDNDRSLL
CCCCEECCCCCHHHH		27.2127732954
567PhosphorylationVLSDNDRSLLERWTR
ECCCCCHHHHHHHHH		39.9220667468
584PhosphorylationRPAAPALTSVPAPAP
CCCCCCCCCCCCCCC		29.7720058876
594PhosphorylationPAPAPAPTPTPTPVQ
CCCCCCCCCCCCCCC		41.7319664994
707PhosphorylationPQSSMSESPDVNLVT
CCCCCCCCCCHHHHH		21.0621924351
718PhosphorylationNLVTQQLSKSQVEDP
HHHHHHHHHHHCCCC		26.3921924351
720PhosphorylationVTQQLSKSQVEDPLP
HHHHHHHHHCCCCCC		35.7625159151
731PhosphorylationDPLPPVFSGTPKGSG
CCCCCCCCCCCCCCC		41.8325159151
733PhosphorylationLPPVFSGTPKGSGAG
CCCCCCCCCCCCCCC		22.1919664994
737PhosphorylationFSGTPKGSGAGYGVG
CCCCCCCCCCCCCCC		31.4326074081
754PhosphorylationLEEFLNQSFDMGVAD
HHHHHHHCCCCCCCC		23.3421924351
770PhosphorylationPQDGQADSASLSASL
CCCCCCCCHHHHHHH		23.8321924351
772PhosphorylationDGQADSASLSASLLA
CCCCCCHHHHHHHHH		27.1521924351
774PhosphorylationQADSASLSASLLADW
CCCCHHHHHHHHHHH		17.2021924351
776PhosphorylationDSASLSASLLADWLE
CCHHHHHHHHHHHHH		22.1221924351
803PhosphorylationQREIQMDSPMLLADL
HHHHHCCCCCCCCCC		13.5820667468
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
28TPhosphorylationKinaseMAPK7Q13164
GPS
219TPhosphorylationKinaseMAP2K5Q13163
GPS
221YPhosphorylationKinaseMAP2K5Q13163
GPS
421SPhosphorylationKinaseMAPK7Q13164
GPS
433SPhosphorylationKinaseMAPK7Q13164
GPS
496SPhosphorylationKinaseRPS6KA1Q15418
GPS
496SPhosphorylationKinaseMAPK7Q13164
GPS
731SPhosphorylationKinaseMAPK7Q13164
GPS
733TPhosphorylationKinaseMAPK1P28482
GPS
733TPhosphorylationKinaseMAPK3P27361
GPS
733TPhosphorylationKinaseMAPK7Q13164
GPS
770SPhosphorylationKinaseMAPK7Q13164
GPS
772SPhosphorylationKinaseMAPK7Q13164
GPS
774SPhosphorylationKinaseMAPK7Q13164
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
219TPhosphorylation

22869143
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 MK07_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
1433E_HUMANYWHAEphysical
14679215
1433B_HUMANYWHABphysical
14679215
CXA1_HUMANGJA1physical
12637502
SGK1_HUMANSGK1physical
11254654
PTPRR_HUMANPTPRRphysical
12042304
RAF1_HUMANRAF1physical
10531364
MEF2A_HUMANMEF2Aphysical
9753748
MEF2D_HUMANMEF2Dphysical
9753748
MEF2C_HUMANMEF2Cphysical
9753748
MK07_HUMANMAPK7physical
7759517
GOGB1_HUMANGOLGB1physical
20936779
FOS_HUMANFOSphysical
17018293
ETS1_HUMANETS1physical
12048211
A4_HUMANAPPphysical
21832049
PML_HUMANPMLphysical
20832753
GANAB_HUMANGANABphysical
23428871
ENPL_HUMANHSP90B1physical
23428871
HS90B_HUMANHSP90AB1physical
23428871
GRP78_HUMANHSPA5physical
23428871
HSP74_HUMANHSPA4physical
23428871
KPYM_HUMANPKMphysical
23428871
ATPA_HUMANATP5A1physical
23428871
PP2BA_HUMANPPP3CAphysical
23428871
FSCN1_HUMANFSCN1physical
23428871
TBB5_HUMANTUBBphysical
23428871
ACTB_HUMANACTBphysical
23428871
G3P_HUMANGAPDHphysical
23428871
LDHC_HUMANLDHCphysical
23428871
MYLK2_HUMANMYLK2physical
23428871
1433E_HUMANYWHAEphysical
23428871
1433Z_HUMANYWHAZphysical
23428871
1433G_HUMANYWHAGphysical
23428871
1433F_HUMANYWHAHphysical
23428871
CDC37_HUMANCDC37physical
23428871
BAG3_HUMANBAG3physical
23824909
SH22A_HUMANSH2D2Aphysical
21988832
NR1I2_HUMANNR1I2physical
21988832
PFD1_HUMANPFDN1physical
23602568
MK07_HUMANMAPK7physical
23602568
PFD3_HUMANVBP1physical
23602568
PFD2_HUMANPFDN2physical
23602568
PFD6_HUMANPFDN6physical
23602568
PFD5_HUMANPFDN5physical
23602568
PFD4_HUMANPFDN4physical
23602568
PLAK_HUMANJUPphysical
23602568
DSC1_HUMANDSC1physical
23602568
DSG1_HUMANDSG1physical
23602568
G3P_HUMANGAPDHphysical
23602568
PML_HUMANPMLphysical
22869143
P53_HUMANTP53physical
22869143
M3K2_HUMANMAP3K2physical
24975362
MP2K5_HUMANMAP2K5physical
24975362
NF2L2_HUMANNFE2L2physical
23043106
KPCZ_HUMANPRKCZphysical
20538799
UBE2C_HUMANUBE2Cphysical
25416956
GPSM3_HUMANGPSM3physical
21516116
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 MK07_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 TYR-221; SER-731 ANDTHR-733, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-720 AND THR-733, ANDMASS SPECTROMETRY.
"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-221, AND MASSSPECTROMETRY.

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