MP2K5_HUMAN - dbPTM
MP2K5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MP2K5_HUMAN
UniProt AC Q13163
Protein Name Dual specificity mitogen-activated protein kinase kinase 5
Gene Name MAP2K5
Organism Homo sapiens (Human).
Sequence Length 448
Subcellular Localization
Protein Description Acts as a scaffold for the formation of a ternary MAP3K2/MAP3K3-MAP3K5-MAPK7 signaling complex. Activation of this pathway appears to play a critical role in protecting cells from stress-induced apoptosis, neuronal survival and cardiac development and angiogenesis..
Protein Sequence MLWLALGPFPAMENQVLVIRIKIPNSGAVDWTVHSGPQLLFRDVLDVIGQVLPEATTTAFEYEDEDGDRITVRSDEEMKAMLSYYYSTVMEQQVNGQLIEPLQIFPRACKPPGERNIHGLKVNTRAGPSQHSSPAVSDSLPSNSLKKSSAELKKILANGQMNEQDIRYRDTLGHGNGGTVYKAYHVPSGKILAVKVILLDITLELQKQIMSELEILYKCDSSYIIGFYGAFFVENRISICTEFMDGGSLDVYRKMPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVNSIAKTYVGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPYPQIQKNQGSLMPLQLLQCIVDEDSPVLPVGEFSEPFVHFITQCMRKQPKERPAPEELMGHPFIVQFNDGNAAVVSMWVCRALEERRSQQGPP
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
71PhosphorylationDEDGDRITVRSDEEM
CCCCCEEEECCHHHH
15.68-
121UbiquitinationERNIHGLKVNTRAGP
CCCCCCEEEECCCCC
37.72-
125MethylationHGLKVNTRAGPSQHS
CCEEEECCCCCCCCC
32.13115483133
129PhosphorylationVNTRAGPSQHSSPAV
EECCCCCCCCCCCCC
39.3425159151
132PhosphorylationRAGPSQHSSPAVSDS
CCCCCCCCCCCCCCC
30.3121815630
133PhosphorylationAGPSQHSSPAVSDSL
CCCCCCCCCCCCCCC
18.1125159151
137PhosphorylationQHSSPAVSDSLPSNS
CCCCCCCCCCCCCCC
24.4829396449
142PhosphorylationAVSDSLPSNSLKKSS
CCCCCCCCCCCCCCH
44.3218691976
144PhosphorylationSDSLPSNSLKKSSAE
CCCCCCCCCCCCHHH
46.0025627689
146UbiquitinationSLPSNSLKKSSAELK
CCCCCCCCCCHHHHH
50.89-
148PhosphorylationPSNSLKKSSAELKKI
CCCCCCCCHHHHHHH
32.9418691976
149PhosphorylationSNSLKKSSAELKKIL
CCCCCCCHHHHHHHH
34.3422817900
154UbiquitinationKSSAELKKILANGQM
CCHHHHHHHHHCCCC
56.42-
202PhosphorylationKVILLDITLELQKQI
EEHHHHHHHHHHHHH
17.5326074081
211PhosphorylationELQKQIMSELEILYK
HHHHHHHHHHHHHHH
40.4326074081
217PhosphorylationMSELEILYKCDSSYI
HHHHHHHHHCCCCCE
18.4126074081
298UbiquitinationVNTRGQVKLCDFGVS
ECCCCCEEECCCCCC
35.19-
305PhosphorylationKLCDFGVSTQLVNSI
EECCCCCCHHHHHHH
15.7128102081
306PhosphorylationLCDFGVSTQLVNSIA
ECCCCCCHHHHHHHH
24.4222210691
311PhosphorylationVSTQLVNSIAKTYVG
CCHHHHHHHHHHCCC
19.2225159151
315PhosphorylationLVNSIAKTYVGTNAY
HHHHHHHHCCCCCCE
17.8925159151
316PhosphorylationVNSIAKTYVGTNAYM
HHHHHHHCCCCCCEE
9.0019060867

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
129SPhosphorylationKinaseMAPK7Q13164
GPS
137SPhosphorylationKinaseMAPK7Q13164
GPS
142SPhosphorylationKinaseMAPK7Q13164
GPS
149SPhosphorylationKinaseMAPK7Q13164
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MP2K5_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 MP2K5_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
M3K2_HUMANMAP3K2physical
11073940
M3K3_HUMANMAP3K3physical
11073940
KPCZ_HUMANPRKCZphysical
11158308
MK07_HUMANMAPK7physical
7759517
MP2K5_HUMANMAP2K5physical
7759517
M3K3_MOUSEMap3k3physical
10593883
1433Z_HUMANYWHAZphysical
20936779
MRCKB_HUMANCDC42BPBphysical
20936779
ENOA_HUMANENO1physical
15805119
SQSTM_HUMANSQSTM1physical
19903815
M3K2_HUMANMAP3K2physical
19903815
ASGL1_HUMANASRGL1physical
21900206
KPCI_HUMANPRKCIphysical
12813044
SQSTM_HUMANSQSTM1physical
12813044
M3K3_HUMANMAP3K3physical
12813044
PAR6A_HUMANPARD6Aphysical
12813044
XRCC6_HUMANXRCC6physical
21988832
RL28_HUMANRPL28physical
21988832
M3K2_HUMANMAP3K2physical
21988832
M3K2_HUMANMAP3K2physical
24975362
MK07_HUMANMAPK7physical
24975362
MK07_HUMANMAPK7physical
28514442
M3K2_HUMANMAP3K2physical
28514442
M3K3_HUMANMAP3K3physical
28514442
TRAF7_HUMANTRAF7physical
28514442
CJ088_HUMANC10orf88physical
28514442
CDC37_HUMANCDC37physical
28514442

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 MP2K5_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-137; SER-148; SER-149;SER-311; THR-315 AND TYR-316, AND MASS 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-133, AND MASSSPECTROMETRY.
"Components of a new human protein kinase signal transductionpathway.";
Zhou G., Bao Z.Q., Dixon J.E.;
J. Biol. Chem. 270:12665-12669(1995).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, INTERACTION WITHERK5 AND MAPK7, MUTAGENESIS OF LYS-195; SER-311 AND THR-315, ANDPHOSPHORYLATION AT SER-311 AND THR-315.

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