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Reviewed, UniProtKB/Swiss-Prot P26696 (MK01_XENLA)

Last modified September 1, 2009. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Mitogen-activated protein kinase 1
    EC=2.7.11.24
Alternative name(s):
    Myelin xP42 protein kinase
    Myelin basic protein kinase
      Short name=MBP kinase
    M phase MAP kinase
Gene names
Name: mapk1
Synonyms: mpk1
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

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Protein attributes

Sequence length361 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Phosphorylates microtubule-associated protein 2 (MAP2). Myelin basic protein (MBP), and Elk-1; may promote entry in the cell cycle. Activated by M phase promoting factor (MPF).

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. Ref.4

Tissue specificity

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

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.

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.

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Ontologies

Keywords
   Biological processCell cycle
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

protein amino acid phosphorylation

Inferred from electronic annotation. Source: InterPro

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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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

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Sequences

Sequence LengthMass (Da)Tools
P26696-1 [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

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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: 1708093] [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: 1714387] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
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: Embryo.
[4]"Requirements for phosphorylation of MAP kinase during meiosis in Xenopus oocytes."
Posada J., Cooper J.A.
Science 255:212-215(1992) [PubMed: 1313186] [Abstract]
Cited for: PHOSPHORYLATION AT THR-188 AND TYR-190, MUTAGENESIS OF LYS-57; ILE-86; THR-188 AND TYR-190, ENZYME REGULATION.

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Cross-references

Sequence databases

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

3D structure databases

HSSPHSSP built from PDB template 1ERK based on UniProtKB P27703.
SMRP26696. Positions 15-359.
ModBaseSearch...

Genome annotation databases

GeneID398985.
KEGGxla:398985.

Organism-specific databases

CTD398985.
XenbaseXB-FEAT-479466. mapk1.

Phylogenomic databases

HOVERGENP26696.

Enzyme and pathway databases

BRENDA2.7.11.24. 648.

Family and domain databases

InterProIPR008349. Erk_1_2_MAPK.
IPR003527. MAP_kinase_CS.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
IPR002290. Ser_thr_pkinase.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSPR01770. ERK1ERK2MAPK.
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
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...

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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: September 1, 2009
This is version 75 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectXenopus annotation project

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents