MAPK2_HUMAN - dbPTM
MAPK2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MAPK2_HUMAN
UniProt AC P49137
Protein Name MAP kinase-activated protein kinase 2
Gene Name MAPKAPK2
Organism Homo sapiens (Human).
Sequence Length 400
Subcellular Localization Cytoplasm . Nucleus . Phosphorylation and subsequent activation releases the autoinhibitory helix, resulting in the export from the nucleus into the cytoplasm.
Protein Description Stress-activated serine/threonine-protein kinase involved in cytokine production, endocytosis, reorganization of the cytoskeleton, cell migration, cell cycle control, chromatin remodeling, DNA damage response and transcriptional regulation. Following stress, it is phosphorylated and activated by MAP kinase p38-alpha/MAPK14, leading to phosphorylation of substrates. Phosphorylates serine in the peptide sequence, Hyd-X-R-X(2)-S, where Hyd is a large hydrophobic residue. Phosphorylates ALOX5, CDC25B, CDC25C, CEP131, ELAVL1, HNRNPA0, HSP27/HSPB1, KRT18, KRT20, LIMK1, LSP1, PABPC1, PARN, PDE4A, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36. Phosphorylates HSF1; leading to the interaction with HSP90 proteins and inhibiting HSF1 homotrimerization, DNA-binding and transactivation activities. [PubMed: 16278218 Mediates phosphorylation of HSP27/HSPB1 in response to stress, leading to the dissociation of HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impairment of their chaperone activities and ability to protect against oxidative stress effectively. Involved in inflammatory response by regulating tumor necrosis factor (TNF) and IL6 production post-transcriptionally: acts by phosphorylating AU-rich elements (AREs)-binding proteins ELAVL1, HNRNPA0, PABPC1 and TTP/ZFP36, leading to the regulation of the stability and translation of TNF and IL6 mRNAs. Phosphorylation of TTP/ZFP36, a major post-transcriptional regulator of TNF, promotes its binding to 14-3-3 proteins and reduces its ARE mRNA affinity, leading to inhibition of dependent degradation of ARE-containing transcripts. Phosphorylates CEP131 in response to cellular stress induced by ultraviolet irradiation which promotes binding of CEP131 to 14-3-3 proteins and inhibits formation of novel centriolar satellites]
Protein Sequence MLSNSQGQSPPVPFPAPAPPPQPPTPALPHPPAQPPPPPPQQFPQFHVKSGLQIKKNAIIDDYKVTSQVLGLGINGKVLQIFNKRTQEKFALKMLQDCPKARREVELHWRASQCPHIVRIVDVYENLYAGRKCLLIVMECLDGGELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDFGFAKETTSHNSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISPGMKTRIRMGQYEFPNPEWSEVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQSTKVPQTPLHTSRVLKEDKERWEDVKEEMTSALATMRVDYEQIKIKKIEDASNPLLLKRRKKARALEAAALAH
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
3Phosphorylation-----MLSNSQGQSP
-----CCCCCCCCCC		32.8928348404
5Phosphorylation---MLSNSQGQSPPV
---CCCCCCCCCCCC		32.1028348404
9PhosphorylationLSNSQGQSPPVPFPA
CCCCCCCCCCCCCCC		37.6922817900
25PhosphorylationAPPPQPPTPALPHPP
CCCCCCCCCCCCCCC		28.0722817900
56UbiquitinationKSGLQIKKNAIIDDY
CCCCEEECCEEECCC		53.9229967540
63PhosphorylationKNAIIDDYKVTSQVL
CCEEECCCCHHHHHC		12.0122817900
64AcetylationNAIIDDYKVTSQVLG
CEEECCCCHHHHHCC		46.1323236377
66PhosphorylationIIDDYKVTSQVLGLG
EECCCCHHHHHCCCC		14.86-
67PhosphorylationIDDYKVTSQVLGLGI
ECCCCHHHHHCCCCC		22.6827251275
84AcetylationKVLQIFNKRTQEKFA
EEEEHHCHHHHHHHH		46.1825953088
84UbiquitinationKVLQIFNKRTQEKFA
EEEEHHCHHHHHHHH		46.1829967540
93UbiquitinationTQEKFALKMLQDCPK
HHHHHHHHHHHHCHH		33.8529967540
98S-palmitoylationALKMLQDCPKARREV
HHHHHHHCHHHHHHH		2.1029575903
100UbiquitinationKMLQDCPKARREVEL
HHHHHCHHHHHHHHH		61.94-
159PhosphorylationDRGDQAFTEREASEI
HCCCHHCCHHHHHHH		36.8326546556
188UbiquitinationNIAHRDVKPENLLYT
CCCCCCCCHHHCEEC		51.40-
204UbiquitinationKRPNAILKLTDFGFA
CCCCEEEEECCCCCC		43.1329967540
206PhosphorylationPNAILKLTDFGFAKE
CCEEEEECCCCCCCC		27.917592979
212UbiquitinationLTDFGFAKETTSHNS
ECCCCCCCCCCCCCC		54.0229967540
214UbiquitinationDFGFAKETTSHNSLT
CCCCCCCCCCCCCCC		32.6524816145
214PhosphorylationDFGFAKETTSHNSLT
CCCCCCCCCCCCCCC		32.6521945579
215PhosphorylationFGFAKETTSHNSLTT
CCCCCCCCCCCCCCC		29.1321945579
216PhosphorylationGFAKETTSHNSLTTP
CCCCCCCCCCCCCCC		28.2621945579
219PhosphorylationKETTSHNSLTTPCYT
CCCCCCCCCCCCCCC		22.9721945579
221PhosphorylationTTSHNSLTTPCYTPY
CCCCCCCCCCCCCCC		28.6321945579
222PhosphorylationTSHNSLTTPCYTPYY
CCCCCCCCCCCCCCE		19.3623401153
222O-linked_GlycosylationTSHNSLTTPCYTPYY
CCCCCCCCCCCCCCE		19.36OGP
225PhosphorylationNSLTTPCYTPYYVAP
CCCCCCCCCCCEECH		16.3821945579
226PhosphorylationSLTTPCYTPYYVAPE
CCCCCCCCCCEECHH		16.1321945579
228PhosphorylationTTPCYTPYYVAPEVL
CCCCCCCCEECHHHH		11.6321945579
229PhosphorylationTPCYTPYYVAPEVLG
CCCCCCCEECHHHHC		7.4321945579
240PhosphorylationEVLGPEKYDKSCDMW
HHHCCHHCCCCCCHH		27.2623312004
272PhosphorylationSNHGLAISPGMKTRI
CCCCCEECCCCCCEE		15.1422817900
307UbiquitinationMLIRNLLKTEPTQRM
HHHHHHHCCCCCCCC		54.7524816145
311PhosphorylationNLLKTEPTQRMTITE
HHHCCCCCCCCCHHH		23.6824532841
317PhosphorylationPTQRMTITEFMNHPW
CCCCCCHHHHHCCCH		17.6322322096
328PhosphorylationNHPWIMQSTKVPQTP
CCCHHHCCCCCCCCC		16.8919060867
329PhosphorylationHPWIMQSTKVPQTPL
CCHHHCCCCCCCCCC		21.1222322096
334PhosphorylationQSTKVPQTPLHTSRV
CCCCCCCCCCCHHHH		23.0322322096
338PhosphorylationVPQTPLHTSRVLKED
CCCCCCCHHHHHHHH		26.3822322096
339PhosphorylationPQTPLHTSRVLKEDK
CCCCCCHHHHHHHHH		15.0526552605
353UbiquitinationKERWEDVKEEMTSAL
HHHHHHHHHHHHHHH		61.3529967540
353SumoylationKERWEDVKEEMTSAL
HHHHHHHHHHHHHHH		61.3521131586
353SumoylationKERWEDVKEEMTSAL
HHHHHHHHHHHHHHH		61.35-
358PhosphorylationDVKEEMTSALATMRV
HHHHHHHHHHHHCCC		21.7028555341
367PhosphorylationLATMRVDYEQIKIKK
HHHCCCCHHHHEEEE		13.5828796482
371UbiquitinationRVDYEQIKIKKIEDA
CCCHHHHEEEEHHHC		48.4429967540
374UbiquitinationYEQIKIKKIEDASNP
HHHHEEEEHHHCCCH		55.5929967540
385UbiquitinationASNPLLLKRRKKARA
CCCHHHHHHHHHHHH		50.5629967540
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
9SPhosphorylationKinaseMAPK1P28482
GPS
25TPhosphorylationKinaseMAPK_GROUP-PhosphoELM
25TPhosphorylationKinaseMAPK-FAMILY-GPS
25TPhosphorylationKinaseMAPK14Q16539
GPS
25TPhosphorylationKinaseMAPK1P28482
GPS
25TPhosphorylationKinaseGRK1Q15835
GPS
222TPhosphorylationKinaseMAPK1P28482
GPS
222TPhosphorylationKinaseMK14Q16539
PhosphoELM
222TPhosphorylationKinaseGRK1Q15835
GPS
222TPhosphorylationKinaseMAPK_GROUP-PhosphoELM
222TPhosphorylationKinaseMAPK-FAMILY-GPS
272SPhosphorylationKinaseMAPK_GROUP-PhosphoELM
272SPhosphorylationKinaseMAPK1P28482
GPS
272SPhosphorylationKinaseMK14Q16539
PhosphoELM
272SPhosphorylationKinaseGRK1Q15835
GPS
272SPhosphorylationKinaseMAPK-FAMILY-GPS
334TPhosphorylationKinaseMAPK_GROUP-PhosphoELM
334TPhosphorylationKinaseMK14Q16539
PhosphoELM
334TPhosphorylationKinaseMAPK-FAMILY-GPS
334TPhosphorylationKinaseMAPK1P28482
GPS
334TPhosphorylationKinaseGRK1Q15835
GPS
338TPhosphorylationKinaseMAPK2P49137
PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
222TPhosphorylation

8846784
272SPhosphorylation

8846784
334TPhosphorylation

8846784
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 MAPK2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SHC1_HUMANSHC1physical
15094067
PHC2_HUMANPHC2physical
15094067
TSC2_RATTsc2physical
12582162
EGF_HUMANEGFgenetic
9687510
AKT1_HUMANAKT1physical
11042204
HSPB1_HUMANHSPB1physical
11042204
MK14_HUMANMAPK14physical
11042204
ETV1_HUMANETV1physical
11551945
MK14_HUMANMAPK14physical
21675959
PHC2_HUMANPHC2physical
21675959
MK01_HUMANMAPK1physical
21675959
MAPK2_HUMANMAPKAPK2physical
21675959
MK03_HUMANMAPK3physical
21675959
MAPK5_HUMANMAPKAPK5physical
21675959
CSK2B_HUMANCSNK2Bphysical
21675959
HSPB1_HUMANHSPB1physical
11839738
TISB_HUMANZFP36L1physical
17030608
HSPB1_HUMANHSPB1physical
14499342
LIMK1_HUMANLIMK1physical
16456544
HSF1_HUMANHSF1physical
16278218
HSPB1_HUMANHSPB1physical
10383393
HSPB1_MOUSEHspb1physical
10383393
LOX5_HUMANALOX5physical
11844797
HSPB1_HUMANHSPB1physical
11844797
ROA0_HUMANHNRNPA0physical
12456657
MPIP2_HUMANCDC25Bphysical
15629715
CHK1_HUMANCHEK1genetic
20932473
PARN_HUMANPARNphysical
20932473
HSPB1_HUMANHSPB1physical
8774846
PABP1_HUMANPABPC1physical
12565831
UB2J1_HUMANUBE2J1physical
24020373
MK11_HUMANMAPK11physical
11551945
DESM_HUMANDESphysical
15094067
MK14_HUMANMAPK14physical
17395714
MK14_HUMANMAPK14physical
17255097
UB2J1_MOUSEUbe2j1physical
24020373
MAPK2_HUMANMAPKAPK2physical
20057052
MK14_HUMANMAPK14physical
10581204
PIAS2_HUMANPIAS2physical
23202365
HSPB1_HUMANHSPB1physical
17170118
DDX5_HUMANDDX5physical
23482664
LSP1_HUMANLSP1physical
8995217
TIF1B_HUMANTRIM28physical
23740979
1433Z_HUMANYWHAZphysical
12861023
HSPB1_HUMANHSPB1physical
8995385
MAPK2_HUMANMAPKAPK2physical
8995385
MK01_HUMANMAPK1physical
8995385
TTP_HUMANZFP36physical
14688255
HSPB1_HUMANHSPB1physical
14688255
HSPB1_HUMANHSPB1physical
21131586
ATF1_HUMANATF1physical
11335727
PDE4A_RATPde4aphysical
21323643
TTP_MOUSEZfp36physical
20595389
AGO2_HUMANAGO2physical
18476811
TISB_HUMANZFP36L1physical
18326031
HSPB1_HUMANHSPB1physical
18326031
TTP_HUMANZFP36physical
18326031
PLK1_HUMANPLK1physical
18695677
MAPK2_HUMANMAPKAPK2physical
18695677
CPZIP_HUMANRCSD1physical
15850461
MK14_MOUSEMapk14physical
15287722
HSPB1_HUMANHSPB1physical
12740362
ARPC5_HUMANARPC5physical
12829704
HSPB1_HUMANHSPB1physical
12829704
HSPB1_HUMANHSPB1physical
10978313
MK14_HUMANMAPK14physical
10922375
HSPB1_HUMANHSPB1physical
15850461
MDM2_HUMANMDM2physical
15688025
CP131_HUMANCEP131physical
26616734
HSPB1_HUMANHSPB1physical
26616734
BECN1_HUMANBECN1physical
25693418
TRI29_HUMANTRIM29physical
24469230
B2CL1_HUMANBCL2L1physical
22617334
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 MAPK2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Identification of novel phosphorylation sites required for activationof MAPKAP kinase-2.";
Ben-Levy R., Leighton I.A., Doza Y.N., Attwood P., Morrice N.,Marshall C.J., Cohen P.;
EMBO J. 14:5920-5930(1995).
Cited for: PHOSPHORYLATION AT SER-9; THR-25; THR-222; SER-272 AND THR-334, ANDMUTAGENESIS OF ASP-207; THR-222; SER-272 AND THR-334.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-63, AND MASSSPECTROMETRY.
Sumoylation
ReferencePubMed
"MK2 SUMOylation regulates actin filament remodeling and subsequentmigration in endothelial cells by inhibiting MK2 kinase and HSP27phosphorylation.";
Chang E., Heo K.S., Woo C.H., Lee H., Le N.T., Thomas T.N.,Fujiwara K., Abe J.;
Blood 117:2527-2537(2011).
Cited for: SUMOYLATION AT LYS-353, AND MUTAGENESIS OF LYS-353.

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