MK01_MOUSE - dbPTM
MK01_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MK01_MOUSE
UniProt AC P63085
Protein Name Mitogen-activated protein kinase 1
Gene Name Mapk1
Organism Mus musculus (Mouse).
Sequence Length 358
Subcellular Localization Cytoplasm, cytoskeleton, spindle. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm. Membrane, caveola . Associated with the spindle during prometaphase and metaphase (By similarity). PEA15-binding and phosphoryla
Protein Description Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context, the MAPK/ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK/ERK cascade plays also a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localized in the nucleus, and seem to participate in the regulation of transcription upon stimulation. However, other substrates are found in the cytosol as well as in other cellular organelles, and those are responsible for processes such as translation, mitosis and apoptosis. Moreover, the MAPK/ERK cascade is also involved in the regulation of the 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. The substrates include transcription factors (such as ATF2, BCL6, ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as CANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of apoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG), regulators of translation (such as EIF4EBP1) and a variety of other signaling-related molecules (like ARHGEF2, DCC, FRS2 or GRB10). Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2, RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2, RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases (such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which enable the propagation the MAPK/ERK signal to additional cytosolic and nuclear targets, thereby extending the specificity of the cascade. Mediates phosphorylation of TPR in respons to EGF stimulation. May play a role in the spindle assembly checkpoint. Phosphorylates PML and promotes its interaction with PIN1, leading to PML degradation. Phosphorylates CDK2AP2 (By similarity).; Acts as a transcriptional repressor. Binds to a [GC]AAA[GC] consensus sequence. Repress the expression of interferon gamma-induced genes. Seems to bind to the promoter of CCL5, DMP1, IFIH1, IFITM1, IRF7, IRF9, LAMP3, OAS1, OAS2, OAS3 and STAT1. Transcriptional activity is independent of kinase activity..
Protein Sequence MAAAAAAGPEMVRGQVFDVGPRYTNLSYIGEGAYGMVCSAYDNLNKVRVAIKKISPFEHQTYCQRTLREIKILLRFRHENIIGINDIIRAPTIEQMKDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVADPDHDHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDLNCIINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQYYDPSDEPIAEAPFKFDMELDDLPKEKLKELIFEETARFQPGYRS
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------MAAAAAAGP
------CCHHHHCCH		13.05-
27PhosphorylationGPRYTNLSYIGEGAY
CCCCCCCEEECCCCH		19.44-
63S-nitrosocysteinePFEHQTYCQRTLREI
CCCCHHHHHHHHHHH		2.21-
63S-nitrosylationPFEHQTYCQRTLREI
CCCCHHHHHHHHHHH		2.2120925432
63GlutathionylationPFEHQTYCQRTLREI
CCCCHHHHHHHHHHH		2.2124333276
108PhosphorylationIVQDLMETDLYKLLK
EEECHHHCCHHHHHH		19.83-
111PhosphorylationDLMETDLYKLLKTQH
CHHHCCHHHHHHHCC		11.47-
136AcetylationYQILRGLKYIHSANV
HHHHHHCHHHHHCCC		45.0122826441
149UbiquitinationNVLHRDLKPSNLLLN
CCCCCCCCHHHEECC		51.1722790023
149AcetylationNVLHRDLKPSNLLLN
CCCCCCCCHHHEECC		51.1722826441
151PhosphorylationLHRDLKPSNLLLNTT
CCCCCCHHHEECCCC		38.2226239621
157PhosphorylationPSNLLLNTTCDLKIC
HHHEECCCCCCEEEC		28.8626239621
158PhosphorylationSNLLLNTTCDLKICD
HHEECCCCCCEEECC		11.7126239621
159S-nitrosylationNLLLNTTCDLKICDF
HEECCCCCCEEECCC		5.6222178444
159GlutathionylationNLLLNTTCDLKICDF
HEECCCCCCEEECCC		5.6224333276
159S-nitrosocysteineNLLLNTTCDLKICDF
HEECCCCCCEEECCC		5.62-
179PhosphorylationADPDHDHTGFLTEYV
CCCCCCCCCHHHHHH		35.3722322096
183PhosphorylationHDHTGFLTEYVATRW
CCCCCHHHHHHHHCC		24.0227087446
185PhosphorylationHTGFLTEYVATRWYR
CCCHHHHHHHHCCCC		7.0827087446
188PhosphorylationFLTEYVATRWYRAPE
HHHHHHHHCCCCCCE		16.2227087446
191PhosphorylationEYVATRWYRAPEIML
HHHHHCCCCCCEEHH		8.1323608596
200PhosphorylationAPEIMLNSKGYTKSI
CCEEHHCCCCCCCCH		24.4023608596
201UbiquitinationPEIMLNSKGYTKSID
CEEHHCCCCCCCCHH		55.6622790023
244PhosphorylationHILGILGSPSQEDLN
HHHHHCCCCCHHHHH		20.2426643407
246PhosphorylationLGILGSPSQEDLNCI
HHHCCCCCHHHHHHH		48.1526643407
257UbiquitinationLNCIINLKARNYLLS
HHHHHHHHHHHHHHH		40.59-
261PhosphorylationINLKARNYLLSLPHK
HHHHHHHHHHHCCCC		11.9429514104
270UbiquitinationLSLPHKNKVPWNRLF
HHCCCCCCCCHHHCC		55.2527667366
282PhosphorylationRLFPNADSKALDLLD
HCCCCCCHHHHHHHH		19.88-
358PhosphorylationRFQPGYRS-------
CCCCCCCC-------		35.7727149854
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
27SPhosphorylationKinaseSGK1Q9WVC6
Uniprot
183TPhosphorylationKinaseMEK1Q02750
PSP
183TPhosphorylationKinaseMEK1P31938
PSP
183TPhosphorylationKinaseMEK1P29678
PSP
183TPhosphorylationKinaseMEK1Q01986
PSP
183TPhosphorylationKinaseMAP2K2Q63932
Uniprot
185YPhosphorylationKinaseLCKP06240
PSP
185YPhosphorylationKinaseERK2P63085
PSP
185YPhosphorylationKinaseMAPK1P63086
GPS
185YPhosphorylationKinaseMEK1Q02750
PSP
185YPhosphorylationKinaseMEK1P31938
PSP
185YPhosphorylationKinaseMEK1P29678
PSP
185YPhosphorylationKinaseMEK1Q01986
PSP
185YPhosphorylationKinaseMAP2K2Q63932
Uniprot
-KUbiquitinationE3 ubiquitin ligaseMap3k1P53349
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
183TPhosphorylation

1849075
183TPhosphorylation

1849075
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 MK01_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KLF11_HUMANKLF11physical
12006497
P53_HUMANTP53physical
10958792
TOP2A_MOUSETop2aphysical
10207078
ELK1_MOUSEElk1physical
11435472
VIF_HV1B1vifphysical
9792705
VIF_HV1BRvifphysical
9792705
VIF_HV1H2vifphysical
9792705
SQSTM_MOUSESqstm1physical
16517408
CAN2_MOUSECapn2physical
14993287
4EBP1_MOUSEEif4ebp1physical
8939971
4EBP2_MOUSEEif4ebp2physical
8939971
ELK1_MOUSEElk1physical
15767678
MAP2_MOUSEMetap2physical
15544353
MBP_MOUSEMbpphysical
15544353
FER_MOUSEFert2physical
15567065
PAXI_MOUSEPxnphysical
14636584
B2CL1_HUMANBCL2L1physical
16282323
ATF2_MOUSEAtf2physical
15192015
MK06_MOUSEMapk6genetic
21505187
NANOG_MOUSENanogphysical
24793005
KS6A3_MOUSERps6ka3physical
24793005
ELK1_MOUSEElk1physical
9687507
TNR1A_MOUSETnfrsf1aphysical
15865443
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MK01_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, ANDMASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, ANDMASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, ANDMASS SPECTROMETRY.
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, ANDMASS SPECTROMETRY.
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling.";
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.;
J. Immunol. 179:5864-5876(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, ANDMASS SPECTROMETRY.
"Identification of the regulatory phosphorylation sites inpp42/mitogen-activated protein kinase (MAP kinase).";
Payne D.M., Rossomando A.J., Martino P., Erickson A.K., Her J.-H.,Shabanowitz J., Hunt D.F., Weber M.J., Sturgill T.W.;
EMBO J. 10:885-892(1991).
Cited for: PHOSPHORYLATION AT THR-183 AND TYR-185, AND PARTIAL PROTEIN SEQUENCE.

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