ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P63085


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name MK01_MOUSE
Primary accession number P63085
Secondary accession numbers P27703 Q3V1U6
Integrated into Swiss-Prot on September 13, 2004
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    September 2, 2008 (Entry version 63)
Name and origin of the protein
Protein name Mitogen-activated protein kinase 1
Synonyms EC 2.7.11.24
Extracellular signal-regulated kinase 2
ERK-2
Mitogen-activated protein kinase 2
MAP kinase 2
MAPK 2
p42-MAPK
ERT1
Gene name
Name: Mapk1
Synonyms: Erk2, Mapk, Prkm1
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Swiss;
TISSUE=Fibroblast;
DOI=10.1093/nar/19.13.3743; PubMed=1649458 [NCBI, ExPASy, EBI, Israel, Japan]
Her J.-H., Wu J.-S., Rall T.B., Sturgill T.W., Weber M.J.;
"Sequence of pp42/MAP kinase, a serine/threonine kinase regulated by tyrosine phosphorylation.";
Nucleic Acids Res. 19:3743-3743(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD;
TISSUE=Brain, Head, Thymus, and Urinary bladder;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 54-65; 76-89; 137-146 AND 171-189, AND MASS SPECTROMETRY.
TISSUE=Hippocampus;
Lubec G., Klug S.;
Submitted (MAR-2007) to UniProtKB.
[5]
PROTEIN SEQUENCE OF 137-146 AND 193-201, AND MASS SPECTROMETRY.
STRAIN=C57BL/6;
TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 152-190.
STRAIN=CBA;
TISSUE=Bone marrow;
DOI=10.1016/0378-1119(93)90411-U; PubMed=8444355 [NCBI, ExPASy, EBI, Israel, Japan]
Ershler M.A., Nagorskaya T.V., Visser J.W.M., Belyavsky A.V.;
"Novel CDC2-related protein kinases produced in murine hematopoietic stem cells.";
Gene 124:305-306(1993).
[7]
PHOSPHORYLATION AT THR-183 AND TYR-185, AND PARTIAL PROTEIN SEQUENCE.
PubMed=1849075 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Identification of the regulatory phosphorylation sites in pp42/mitogen-activated protein kinase (MAP kinase).";
EMBO J. 10:885-892(1991).
[8]
INTERACTION WITH MORG1.
DOI=10.1073/pnas.0305894101; PubMed=15118098 [NCBI, ExPASy, EBI, Israel, Japan]
Vomastek T., Schaeffer H.-J., Tarcsafalvi A., Smolkin M.E., Bissonette E.A., Weber M.J.;
"Modular construction of a signaling scaffold: MORG1 interacts with components of the ERK cascade and links ERK signaling to specific agonists.";
Proc. Natl. Acad. Sci. U.S.A. 101:6981-6986(2004).
[9]
PHOSPHORYLATION OF SPZ1.
DOI=10.1158/0008-5472.CAN-04-3658; PubMed=15899793 [NCBI, ExPASy, EBI, Israel, Japan]
Hsu S.-H., Hsieh-Li H.-M., Huang H.-Y., Huang P.-H., Li H.;
"bHLH-zip transcription factor Spz1 mediates mitogen-activated protein kinase cell proliferation, transformation, and tumorigenesis.";
Cancer Res. 65:4041-4050(2005).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, AND MASS SPECTROMETRY.
TISSUE=Mast cell;
PubMed=17947660 [NCBI, ExPASy, EBI, Israel, Japan]
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling.";
J. Immunol. 179:5864-5876(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0608638104; PubMed=17389395 [NCBI, ExPASy, EBI, Israel, Japan]
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
"Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks.";
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, AND MASS SPECTROMETRY.
TISSUE=Brain;
DOI=10.1021/pr0701254; PubMed=18034455 [NCBI, ExPASy, EBI, Israel, Japan]
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1073/pnas.0609836104; PubMed=17242355 [NCBI, ExPASy, EBI, Israel, Japan]
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X58712; CAA41548.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK035386; BAC29053.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK048127; BAC33251.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK087925; BAC40044.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK132241; BAE21053.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC058258; AAH58258.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D10939; BAA01733.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S16444; S16444.
RefSeq NP_001033752.1; -.
NP_036079.1; -.
UniGene Mm.196581
3D structure databases
SMR P63085; 9-353, 10-354.
ModBase P63085.
Protein-protein interaction databases
IntAct P63085; -.
PTM databases
PhosphoSite P63085; -.
Organism-specific databases
MGI MGI:1346858; Mapk1.
Gene expression databases
ArrayExpress P63085; -.
CleanEx MM_MAPK1; -.
GermOnline ENSMUSG00000063358; Mus musculus.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from MGI).
GO:0005654; Cellular component: nucleoplasm (inferred from experiment from Reactome).
GO:0016908; Molecular function: MAP kinase 2 activity (inferred from direct assay from MGI).
GO:0001784; Molecular function: phosphotyrosine binding (inferred from mutant phenotype from MGI).
GO:0003700; Molecular function: transcription factor activity (inferred from experiment from Reactome).
GO:0050853; Biological process: B cell receptor signaling pathway (inferred from direct assay from MGI).
GO:0019858; Biological process: cytosine metabolic process (inferred from direct assay from MGI).
GO:0031663; Biological process: lipopolysaccharide-mediated signaling pathway (inferred from direct assay from MGI).
GO:0000165; Biological process: MAPKKK cascade (inferred from direct assay from MGI).
GO:0045596; Biological process: negative regulation of cell differentiation (inferred from genetic interaction from MGI).
GO:0009887; Biological process: organ morphogenesis (inferred from direct assay from MGI).
GO:0006468; Biological process: protein amino acid phosphorylation (inferred from direct assay from MGI).
GO:0006974; Biological process: response to DNA damage stimulus (inferred from direct assay from MGI).
GO:0043330; Biological process: response to exogenous dsRNA (inferred from direct assay from MGI).
GO:0032496; Biological process: response to lipopolysaccharide (inferred from direct assay from MGI).
GO:0050852; Biological process: T cell receptor signaling pathway (inferred from direct assay from MGI).
QuickGo view.
Family and domain databases
InterPro IPR008349; Erk_1_2_MAPK.
IPR003527; MAP_kin_CS.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.
Pfam PF00069; Pkinase; 1.
Pfam graphical view of domain structure.
PRINTS PR01770; ERK1ERK2MAPK.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00220; S_TKc; 1.
SMART graphical view of domain structure.
PROSITE PS01351; MAPK; 1.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P63085.
Genome annotation databases
Ensembl ENSMUSG00000063358; Mus musculus. [Contig view]
GeneID 26413; -.
KEGG mmu:26413; -.
NMPDR fig|10090.3.peg.30922; -.
Phylogenomic databases
HOGENOM P63085; -.
HOVERGEN P63085; -.
Other
SOURCE Mapk1; Mus musculus.
ProtoNet P63085.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; ATP-binding; Cell cycle; Direct protein sequencing; Kinase; Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   358  357     Mitogen-activated protein kinase 1. PRO_0000186248
DOMAIN   23   311  289     Protein kinase. 
NP_BIND   29    37  9     ATP (By similarity). 
MOTIF   183   185  3     TXY. 
COMPBIAS   2     7  6     Poly-Ala. 
ACT_SITE   147   147        Proton acceptor (By similarity). 
BINDING   52    52        ATP (By similarity). 
MOD_RES   2     2        N-acetylalanine (By similarity). 
MOD_RES   183   183        Phosphothreonine. 
MOD_RES   185   185        Phosphotyrosine. 
MOD_RES   188   188        Phosphothreonine (By similarity). 
Sequence information
Length: 358 AA [This is the length of the unprocessed precursor] Molecular weight: 41276 Da [This is the MW of the unprocessed precursor] CRC64: 3BBCF22471EDBA0B [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAAAAAAGPE MVRGQVFDVG PRYTNLSYIG EGAYGMVCSA YDNLNKVRVA IKKISPFEHQ 

        70         80         90        100        110        120 
TYCQRTLREI KILLRFRHEN IIGINDIIRA PTIEQMKDVY IVQDLMETDL YKLLKTQHLS 

       130        140        150        160        170        180 
NDHICYFLYQ ILRGLKYIHS ANVLHRDLKP SNLLLNTTCD LKICDFGLAR VADPDHDHTG 

       190        200        210        220        230        240 
FLTEYVATRW YRAPEIMLNS KGYTKSIDIW SVGCILAEML SNRPIFPGKH YLDQLNHILG 

       250        260        270        280        290        300 
ILGSPSQEDL NCIINLKARN YLLSLPHKNK VPWNRLFPNA DSKALDLLDK MLTFNPHKRI 

       310        320        330        340        350 
EVEQALAHPY LEQYYDPSDE PIAEAPFKFD MELDDLPKEK LKELIFEETA RFQPGYRS 

P63085 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!