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P26696 (MK01_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Mitogen-activated protein kinase 1

Short name=MAP kinase 1
Short name=MAPK 1
EC=2.7.11.24
Alternative name(s):
M phase MAP kinase
Myelin basic protein kinase
Short name=MBP kinase
Myelin xP42 protein kinase
Gene names
Name:mapk1
Synonyms:mpk1
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length361 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the MAPK/ERK cascade. Depending on the cellular context, this 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. Many of the 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. Phosphorylates microtubule-associated protein 2 (MAP2), myelin basic protein (MBP) and Elk-1. Phosphorylates dual specificity protein phosphatase 1 (DUSP1) during meiosis, increasing its stability. Activated by M phase promoting factor (MPF). Plays a role in the spindle assembly checkpoint. Ref.2 Ref.5 Ref.6

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Enzyme regulation

Activated by tyrosine phosphorylation during the M phase of the meiotic cell cycle. Dephosphorylated and inactivated by DUSP1. Ref.2 Ref.4 Ref.5 Ref.6

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Cytoplasm. Cytoplasmcytoskeletonspindle. Note: Associated with the spindle during prometaphase and metaphase in cultured XTC cells. Ref.5

Tissue specificity

Expressed in the central nervous system, kidney, liver, intestine and the hematopoietic system. Also found in heart, muscle, pancreas and lung. Ref.2

Developmental stage

Is expressed in the early oocyte and is maintained at a constant level during embryogenesis. Its level declines at the mid-blastula transition. Ref.2

Domain

The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

Post-translational modification

Dually phosphorylated on Thr-188 and Tyr-190, which activates the enzyme. Ref.4

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 361361Mitogen-activated protein kinase 1
PRO_0000186250

Regions

Domain28 – 316289Protein kinase
Nucleotide binding34 – 429ATP By similarity
Motif188 – 1903TXY
Compositional bias2 – 65Poly-Ala

Sites

Active site1521Proton acceptor By similarity
Binding site571ATP Probable

Amino acid modifications

Modified residue1881Phosphothreonine Ref.4
Modified residue1901Phosphotyrosine Ref.4

Experimental info

Mutagenesis571K → R: Inactivation. Ref.4
Mutagenesis861I → Y: Inactivation. Ref.4
Mutagenesis1881T → V or D: No effect on Tyr phosphorylation. Ref.4
Mutagenesis1901Y → F: Affects Thr phosphorylation. Ref.4
Sequence conflict5 – 73GAA → AAS in AAA50002. Ref.1
Sequence conflict291I → T in AAA50002. Ref.1
Sequence conflict321A → S in AAA50002. Ref.1
Sequence conflict47 – 493DNV → CNI in AAA50002. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P26696 [UniParc].

Last modified November 14, 2006. Version 3.
Checksum: D14EFF145A183EC6

FASTA36141,257
        10         20         30         40         50         60 
MAAAGAASNP GGGPEMVRGQ AFDVGPRYIN LAYIGEGAYG MVCSAHDNVN KVRVAIKKIS 

        70         80         90        100        110        120 
PFEHQTYCQR TLREIKILLR FKHENIIGIN DIIRAPTIEQ MKDVYIVQDL METDLYKLLK 

       130        140        150        160        170        180 
TQHLSNDHIC YFLYQILRGL KYIHSANVLH RDLKPSNLLL NTTCDLKICD FGLARVADPD 

       190        200        210        220        230        240 
HDHTGFLTEY VATRWYRAPE IMLNSKGYTK SIDIWSVGCI LAEMLSNRPI FPGKHYLDQL 

       250        260        270        280        290        300 
NHILGILGSP SQEDLNCIIN LKARNYLLSL PHKNKVPWNR LFPNADPKAL DLLDKMLTFN 

       310        320        330        340        350        360 
PHKRIEVEAA LAHPYLEQYY DPSDEPVAEA PFKFEMELDD LPKETLKELI FEETARFQPG 


Y 

« Hide

References

« Hide 'large scale' references
[1]"Tyrosine phosphorylation and activation of homologous protein kinases during oocyte maturation and mitogenic activation of fibroblasts."
Posada J., Sanghera J., Pelech S., Aebersold R., Cooper J.A.
Mol. Cell. Biol. 11:2517-2528(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Ovary.
[2]"Xenopus M phase MAP kinase: isolation of its cDNA and activation by MPF."
Gotoh Y., Moriyama K., Matsuda S., Okumura E., Kishimoto T., Kawasaki H., Suzuki K., Yahara I., Sakai H., Nishida E.
EMBO J. 10:2661-2668(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Oocyte.
[3]NIH - Xenopus Gene Collection (XGC) project
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Tail bud.
[4]"Requirements for phosphorylation of MAP kinase during meiosis in Xenopus oocytes."
Posada J., Cooper J.A.
Science 255:212-215(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-188 AND TYR-190, MUTAGENESIS OF LYS-57; ILE-86; THR-188 AND TYR-190, ENZYME REGULATION.
[5]"A role for mitogen-activated protein kinase in the spindle assembly checkpoint in XTC cells."
Wang X.M., Zhai Y., Ferrell J.E. Jr.
J. Cell Biol. 137:433-443(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION.
[6]"Activation of p42 mitogen-activated protein kinase (MAPK), but not c-Jun NH(2)-terminal kinase, induces phosphorylation and stabilization of MAPK phosphatase XCL100 in Xenopus oocytes."
Sohaskey M.L., Ferrell J.E. Jr.
Mol. Biol. Cell 13:454-468(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M60977 mRNA. Translation: AAA50002.1.
X59813 mRNA. Translation: CAA42482.1.
BC060748 mRNA. Translation: AAH60748.1.
PIRA39754.
RefSeqNP_001083548.1. NM_001090079.1.
UniGeneXl.1680.
Xl.874.

3D structure databases

ProteinModelPortalP26696.
SMRP26696. Positions 18-361.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid100311. 3 interactions.
IntActP26696. 1 interaction.
MINTMINT-86973.

Proteomic databases

PRIDEP26696.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID398985.
KEGGxla:398985.

Organism-specific databases

CTD398985.
XenbaseXB-GENE-865273. mapk1.

Phylogenomic databases

HOVERGENHBG014652.
KOK04371.

Enzyme and pathway databases

BRENDA2.7.11.24. 6726.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008349. MAPK_ERK1/2.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSPR01770. ERK1ERK2MAPK.
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMK01_XENLA
AccessionPrimary (citable) accession number: P26696
Secondary accession number(s): Q5D061
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: November 14, 2006
Last modified: June 11, 2014
This is version 105 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families