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Mitogen-activated protein kinase 1 (MAP kinase 1) (MAPK 1) (EC 2.7.11.24) (M phase MAP kinase) (Myelin basic protein kinase) (MBP kinase) (Myelin xP42 protein kinase)

 MK01_XENLA              Reviewed;         361 AA.
P26696; Q5D061;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
14-NOV-2006, sequence version 3.
22-NOV-2017, entry version 125.
RecName: Full=Mitogen-activated protein kinase 1;
Short=MAP kinase 1;
Short=MAPK 1;
EC=2.7.11.24;
AltName: Full=M phase MAP kinase;
AltName: Full=Myelin basic protein kinase;
Short=MBP kinase;
AltName: Full=Myelin xP42 protein kinase;
Name=mapk1; Synonyms=mpk1;
Xenopus laevis (African clawed frog).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
Xenopus.
NCBI_TaxID=8355;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Ovary;
PubMed=1708093; DOI=10.1128/MCB.11.5.2517;
Posada J., Sanghera J., Pelech S., Aebersold R., Cooper J.A.;
"Tyrosine phosphorylation and activation of homologous protein kinases
during oocyte maturation and mitogenic activation of fibroblasts.";
Mol. Cell. Biol. 11:2517-2528(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, ENZYME
REGULATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
TISSUE=Oocyte;
PubMed=1714387;
Gotoh Y., Moriyama K., Matsuda S., Okumura E., Kishimoto T.,
Kawasaki H., Suzuki K., Yahara I., Sakai H., Nishida E.;
"Xenopus M phase MAP kinase: isolation of its cDNA and activation by
MPF.";
EMBO J. 10:2661-2668(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Tail bud;
NIH - Xenopus Gene Collection (XGC) project;
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
[4]
PHOSPHORYLATION AT THR-188 AND TYR-190, MUTAGENESIS OF LYS-57; ILE-86;
THR-188 AND TYR-190, AND ENZYME REGULATION.
PubMed=1313186; DOI=10.1126/science.1313186;
Posada J., Cooper J.A.;
"Requirements for phosphorylation of MAP kinase during meiosis in
Xenopus oocytes.";
Science 255:212-215(1992).
[5]
FUNCTION, SUBCELLULAR LOCATION, AND ENZYME REGULATION.
PubMed=9128253; DOI=10.1083/jcb.137.2.433;
Wang X.M., Zhai Y., Ferrell J.E. Jr.;
"A role for mitogen-activated protein kinase in the spindle assembly
checkpoint in XTC cells.";
J. Cell Biol. 137:433-443(1997).
[6]
FUNCTION, AND ENZYME REGULATION.
PubMed=11854404; DOI=10.1091/mbc.01-11-0553;
Sohaskey M.L., Ferrell J.E. Jr.;
"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.";
Mol. Biol. Cell 13:454-468(2002).
[7]
INTERACTION WITH CDK2AP2.
PubMed=12944431; DOI=10.1242/dev.00731;
Terret M.E., Lefebvre C., Djiane A., Rassinier P., Moreau J., Maro B.,
Verlhac M.H.;
"DOC1R: a MAP kinase substrate that control microtubule organization
of metaphase II mouse oocytes.";
Development 130:5169-5177(2003).
-!- 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. {ECO:0000269|PubMed:11854404,
ECO:0000269|PubMed:1714387, ECO:0000269|PubMed:9128253}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Activated by tyrosine phosphorylation during
the M phase of the meiotic cell cycle. Dephosphorylated and
inactivated by DUSP1. {ECO:0000269|PubMed:11854404,
ECO:0000269|PubMed:1313186, ECO:0000269|PubMed:1714387,
ECO:0000269|PubMed:9128253}.
-!- SUBUNIT: Interacts with CDK2AP2 (PubMed:12944431).
{ECO:0000269|PubMed:12944431}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000250}. Cytoplasm
{ECO:0000269|PubMed:9128253}. Cytoplasm, cytoskeleton, spindle
{ECO:0000269|PubMed:9128253}. Note=Associated with the spindle
during prometaphase and metaphase in cultured XTC cells.
-!- TISSUE SPECIFICITY: Expressed in the central nervous system,
kidney, liver, intestine and the hematopoietic system. Also found
in heart, muscle, pancreas and lung. {ECO:0000269|PubMed:1714387}.
-!- 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.
{ECO:0000269|PubMed:1714387}.
-!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
whose phosphorylation activates the MAP kinases.
-!- PTM: Dually phosphorylated on Thr-188 and Tyr-190, which activates
the enzyme. {ECO:0000269|PubMed:1313186}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. MAP kinase subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M60977; AAA50002.1; -; mRNA.
EMBL; X59813; CAA42482.1; -; mRNA.
EMBL; BC060748; AAH60748.1; -; mRNA.
PIR; A39754; A39754.
RefSeq; NP_001083548.1; NM_001090079.1.
UniGene; Xl.1680; -.
UniGene; Xl.874; -.
ProteinModelPortal; P26696; -.
SMR; P26696; -.
BioGrid; 100311; 3.
IntAct; P26696; 1.
MINT; MINT-86973; -.
iPTMnet; P26696; -.
MaxQB; P26696; -.
PRIDE; P26696; -.
GeneID; 398985; -.
KEGG; xla:398985; -.
CTD; 398985; -.
Xenbase; XB-GENE-865273; mapk1.
HOVERGEN; HBG014652; -.
KO; K04371; -.
BRENDA; 2.7.11.24; 6725.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007094; P:mitotic spindle assembly checkpoint; IMP:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; ISS:UniProtKB.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
GO; GO:0031647; P:regulation of protein stability; IDA:UniProtKB.
GO; GO:0070849; P:response to epidermal growth factor; ISS:UniProtKB.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR003527; MAP_kinase_CS.
InterPro; IPR008349; MAPK_ERK1/2.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
PRINTS; PR01770; ERK1ERK2MAPK.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS01351; MAPK; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Apoptosis; ATP-binding; Cell cycle; Cytoplasm; Cytoskeleton;
Direct protein sequencing; Kinase; Nucleotide-binding; Phosphoprotein;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 361 Mitogen-activated protein kinase 1.
/FTId=PRO_0000186250.
DOMAIN 28 316 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 34 42 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 188 190 TXY.
COMPBIAS 2 6 Poly-Ala.
ACT_SITE 152 152 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 57 57 ATP. {ECO:0000305}.
MOD_RES 188 188 Phosphothreonine.
{ECO:0000269|PubMed:1313186}.
MOD_RES 190 190 Phosphotyrosine.
{ECO:0000269|PubMed:1313186}.
MUTAGEN 57 57 K->R: Inactivation.
{ECO:0000269|PubMed:1313186}.
MUTAGEN 86 86 I->Y: Inactivation.
{ECO:0000269|PubMed:1313186}.
MUTAGEN 188 188 T->V,D: No effect on Tyr phosphorylation.
{ECO:0000269|PubMed:1313186}.
MUTAGEN 190 190 Y->F: Affects Thr phosphorylation.
{ECO:0000269|PubMed:1313186}.
CONFLICT 5 7 GAA -> AAS (in Ref. 1; AAA50002).
{ECO:0000305}.
CONFLICT 29 29 I -> T (in Ref. 1; AAA50002).
{ECO:0000305}.
CONFLICT 32 32 A -> S (in Ref. 1; AAA50002).
{ECO:0000305}.
CONFLICT 47 49 DNV -> CNI (in Ref. 1; AAA50002).
{ECO:0000305}.
SEQUENCE 361 AA; 41257 MW; D14EFF145A183EC6 CRC64;
MAAAGAASNP GGGPEMVRGQ AFDVGPRYIN LAYIGEGAYG MVCSAHDNVN KVRVAIKKIS
PFEHQTYCQR TLREIKILLR FKHENIIGIN DIIRAPTIEQ MKDVYIVQDL METDLYKLLK
TQHLSNDHIC YFLYQILRGL KYIHSANVLH RDLKPSNLLL NTTCDLKICD FGLARVADPD
HDHTGFLTEY VATRWYRAPE IMLNSKGYTK SIDIWSVGCI LAEMLSNRPI FPGKHYLDQL
NHILGILGSP SQEDLNCIIN LKARNYLLSL PHKNKVPWNR LFPNADPKAL DLLDKMLTFN
PHKRIEVEAA LAHPYLEQYY DPSDEPVAEA PFKFEMELDD LPKETLKELI FEETARFQPG
Y


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