Mitogen-activated protein kinase 1 - Xenopus laevis (African clawed frog)

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P26696 (MK01_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 96. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	361 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm › cytoskeleton › centrosome By similarity. Cytoplasm. Cytoplasm › cytoskeleton › spindle. 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.

Ontologies

Keywords
Biological process	Apoptosis Cell cycle
Cellular component	Cytoplasm Cytoskeleton
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	MAPK cascade Inferred from electronic annotation. Source: GOC apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cell cycle Inferred from electronic annotation. Source: UniProtKB-KW response to epidermal growth factor stimulus Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from sequence or structural similarity. Source: UniProtKB spindle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW MAP kinase activity Inferred from electronic annotation. Source: EC protein serine/threonine kinase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 361

361

Mitogen-activated protein kinase 1

PRO_0000186250

Regions

Domain

28 – 316

289

Protein kinase

Nucleotide binding

34 – 42

ATP By similarity

Motif

188 – 190

TXY

Compositional bias

2 – 6

Poly-Ala

Sites

Active site

152

Proton acceptor By similarity

Binding site

ATP Probable

Amino acid modifications

Modified residue

188

Phosphothreonine Ref.4

Modified residue

190

Phosphotyrosine Ref.4

Experimental info

Mutagenesis

K → R: Inactivation. Ref.4

Mutagenesis

I → Y: Inactivation. Ref.4

Mutagenesis

188

T → V or D: No effect on Tyr phosphorylation. Ref.4

Mutagenesis

190

Y → F: Affects Thr phosphorylation. Ref.4

Sequence conflict

5 – 7

GAA → AAS in AAA50002. Ref.1

Sequence conflict

I → T in AAA50002. Ref.1

Sequence conflict

A → S in AAA50002. Ref.1

Sequence conflict

47 – 49

DNV → CNI in AAA50002. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P26696 [UniParc].

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

361

41,257

        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' referencesShow '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.
PIR	A39754.
RefSeq	NP_001083548.1. NM_001090079.1.
UniGene	Xl.1680. Xl.874.
3D structure databases
ProteinModelPortal	P26696.
SMR	P26696. Positions 18-361.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-86973.
Proteomic databases
PRIDE	P26696.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	398985.
KEGG	xla:398985.
Organism-specific databases
CTD	398985.
Xenbase	XB-GENE-865273. mapk1.
Phylogenomic databases
HOVERGEN	HBG014652.
KO	K04371.
Enzyme and pathway databases
BRENDA	2.7.11.24. 6726.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR003527. MAP_kinase_CS. IPR008349. MAPK_ERK1/2. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
PRINTS	PR01770. ERK1ERK2MAPK.
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS01351. MAPK. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL4842.

Entry information

Entry name

MK01_XENLA

Accession

Primary (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:	May 1, 2013
This is version 96 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents