MP2K1_RAT - dbPTM
MP2K1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MP2K1_RAT
UniProt AC Q01986
Protein Name Dual specificity mitogen-activated protein kinase kinase 1
Gene Name Map2k1
Organism Rattus norvegicus (Rat).
Sequence Length 393
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body . Cytoplasm . Nucleus . Membrane
Peripheral membrane protein . Localizes at centrosomes during prometapha
Protein Description Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Binding of extracellular ligands such as growth factors, cytokines and hormones to their cell-surface receptors activates RAS and this initiates RAF1 activation. RAF1 then further activates the dual-specificity protein kinases MAP2K1/MEK1 and MAP2K2/MEK2. Both MAP2K1/MEK1 and MAP2K2/MEK2 function specifically in the MAPK/ERK cascade, and catalyze the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in the extracellular signal-regulated kinases MAPK3/ERK1 and MAPK1/ERK2, leading to their activation and further transduction of the signal within the MAPK/ERK cascade. Depending on the cellular context, this pathway mediates diverse biological functions such as cell growth, adhesion, survival and differentiation, predominantly through the regulation of transcription, metabolism and cytoskeletal rearrangements. One target of the MAPK/ERK cascade is peroxisome proliferator-activated receptor gamma (PPARG), a nuclear receptor that promotes differentiation and apoptosis. MAP2K1/MEK1 has been shown to export PPARG from the nucleus. The MAPK/ERK cascade is also involved in the regulation of endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC), as well as in the fragmentation of the Golgi apparatus during mitosis..
Protein Sequence MPKKKPTPIQLNPAPDGSAVNGTSSAETNLEALQKKLEELELDEQQRKRLEAFLTQKQKVGELKDDDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIPPPDAKELELLFGCQVEGDAAETPPRPRTPGRPLSSYGMDSRPPMAIFELLDYIVNEPPPKLPSGVFSLEFQDFVNKCLIKNPAERADLKQLMVHAFIKRSDAEEVDFAGWLCSTIGLNQPSTPTHAASI
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
7Phosphorylation-MPKKKPTPIQLNPA
-CCCCCCCCCCCCCC		41.7325575281
18PhosphorylationLNPAPDGSAVNGTSS
CCCCCCCCCCCCCCC		36.1025575281
23PhosphorylationDGSAVNGTSSAETNL
CCCCCCCCCCHHHHH		17.8225575281
24PhosphorylationGSAVNGTSSAETNLE
CCCCCCCCCHHHHHH		29.0225575281
25PhosphorylationSAVNGTSSAETNLEA
CCCCCCCCHHHHHHH		29.9325575281
64SuccinylationKQKVGELKDDDFEKI
HHHHCCCCCCCHHHH		55.6026843850
72PhosphorylationDDDFEKISELGAGNG
CCCHHHHHHCCCCCC		37.5223984901
104AcetylationKLIHLEIKPAIRNQI
EEHHHHCCHHHHHHH		21.0122902405
192UbiquitinationKIMHRDVKPSNILVN
CCCCCCCCHHHEEEC		47.20-
212PhosphorylationKLCDFGVSGQLIDSM
EECCCCCCHHHHHHH		22.6222817900
218PhosphorylationVSGQLIDSMANSFVG
CCHHHHHHHHHHCCC		16.8917314031
222PhosphorylationLIDSMANSFVGTRSY
HHHHHHHHCCCCCCC		16.2723712012
226PhosphorylationMANSFVGTRSYMSPE
HHHHCCCCCCCCCHH		15.9027097102
229PhosphorylationSFVGTRSYMSPERLQ
HCCCCCCCCCHHHHC		9.7926022182
286PhosphorylationVEGDAAETPPRPRTP
EECCCCCCCCCCCCC		33.5922108457
292PhosphorylationETPPRPRTPGRPLSS
CCCCCCCCCCCCCHH		32.5522817900
298PhosphorylationRTPGRPLSSYGMDSR
CCCCCCCHHCCCCCC		24.9722817900
299PhosphorylationTPGRPLSSYGMDSRP
CCCCCCHHCCCCCCC		33.1323984901
300PhosphorylationPGRPLSSYGMDSRPP
CCCCCHHCCCCCCCC		17.0623984901
304PhosphorylationLSSYGMDSRPPMAIF
CHHCCCCCCCCCHHH		37.4823984901
316PhosphorylationAIFELLDYIVNEPPP
HHHHHHHHHHCCCCC		13.5123984901
353AcetylationPAERADLKQLMVHAF
HHHHCCHHHHHHHHH		41.7722902405
385PhosphorylationTIGLNQPSTPTHAAS
HHCCCCCCCCCCCCC		36.9423984901
386PhosphorylationIGLNQPSTPTHAASI
HCCCCCCCCCCCCCC		38.6022817900
388PhosphorylationLNQPSTPTHAASI--
CCCCCCCCCCCCC--		25.0023984901
392PhosphorylationSTPTHAASI------
CCCCCCCCC------		29.6123984901
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
218SPhosphorylationKinaseRAF1P11345
GPS
218SPhosphorylationKinaseRAF-Uniprot
218SPhosphorylationKinaseBRAFF1M9C3
PSP
218SPhosphorylationKinaseMAP3K1P53349
GPS
218SPhosphorylationKinaseMAP2K1Q01986
GPS
222SPhosphorylationKinaseRAF1P11345
GPS
222SPhosphorylationKinaseBRAFF1M9C3
PSP
222SPhosphorylationKinaseMAP3K1P53349
GPS
222SPhosphorylationKinaseRAF-Uniprot
222SPhosphorylationKinaseMAP2K1Q01986
GPS
286TPhosphorylationKinaseCDK1P06493
PSP
286TPhosphorylationKinaseMAPK-FAMILY-GPS
286TPhosphorylationKinaseCDK5Q03114
GPS
286TPhosphorylationKinaseCDK12Q3MJK5
GPS
292TPhosphorylationKinaseCDK1P06493
PSP
292TPhosphorylationKinaseMAPK1P63086
Uniprot
292TPhosphorylationKinaseCDK12Q3MJK5
GPS
292TPhosphorylationKinaseMAPK-FAMILY-GPS
298SPhosphorylationKinasePAK-SUBFAMILY-GPS
298SPhosphorylationKinasePAK-Uniprot
298SPhosphorylationKinasePAK3Q62829
PSP
298SPhosphorylationKinasePAK3O75914
PSP
298SPhosphorylationKinasePAK2Q64303
PSP
298SPhosphorylationKinasePAK1P35465
PSP
386TPhosphorylationKinaseMAPK-FAMILY-GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
218SPhosphorylation

14993270
218SPhosphorylation

10769026
222SPhosphorylation

14993270
222SPhosphorylation

10769026
292TPhosphorylation

14993270
292TPhosphorylation

14993270
298SPhosphorylation

12876277
298SPhosphorylation

12876277
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 MP2K1_RAT !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MK01_XENLAmapk1-aphysical
8026469
MBP_HUMANMBPphysical
12624112
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MP2K1_RAT

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Mitogen-activated protein kinase feedback phosphorylation regulatesMEK1 complex formation and activation during cellular adhesion.";
Eblen S.T., Slack-Davis J.K., Tarcsafalvi A., Parsons J.T.,Weber M.J., Catling A.D.;
Mol. Cell. Biol. 24:2308-2317(2004).
Cited for: PHOSPHORYLATION AT THR-292 AND SER-298, INTERACTION WITH MAPK1/ERK2,AND ENZYME REGULATION.
"PAK1 phosphorylation of MEK1 regulates fibronectin-stimulated MAPKactivation.";
Slack-Davis J.K., Eblen S.T., Zecevic M., Boerner S.A.,Tarcsafalvi A., Diaz H.B., Marshall M.S., Weber M.J., Parsons J.T.,Catling A.D.;
J. Cell Biol. 162:281-291(2003).
Cited for: PHOSPHORYLATION AT SER-298, AND ENZYME REGULATION.

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