MK01_XENLA
ID MK01_XENLA Reviewed; 361 AA.
AC P26696; Q5D061;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Mitogen-activated protein kinase 1;
DE Short=MAP kinase 1;
DE Short=MAPK 1;
DE EC=2.7.11.24;
DE AltName: Full=M phase MAP kinase;
DE AltName: Full=Myelin basic protein kinase;
DE Short=MBP kinase;
DE AltName: Full=Myelin xP42 protein kinase;
GN Name=mapk1; Synonyms=mpk1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=1708093; DOI=10.1128/mcb.11.5.2517-2528.1991;
RA Posada J., Sanghera J., Pelech S., Aebersold R., Cooper J.A.;
RT "Tyrosine phosphorylation and activation of homologous protein kinases
RT during oocyte maturation and mitogenic activation of fibroblasts.";
RL Mol. Cell. Biol. 11:2517-2528(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, ACTIVITY
RP REGULATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Oocyte;
RX PubMed=1714387; DOI=10.1002/j.1460-2075.1991.tb07809.x;
RA Gotoh Y., Moriyama K., Matsuda S., Okumura E., Kishimoto T., Kawasaki H.,
RA Suzuki K., Yahara I., Sakai H., Nishida E.;
RT "Xenopus M phase MAP kinase: isolation of its cDNA and activation by MPF.";
RL EMBO J. 10:2661-2668(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tail bud;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION AT THR-188 AND TYR-190, MUTAGENESIS OF LYS-57; ILE-86;
RP THR-188 AND TYR-190, AND ACTIVITY REGULATION.
RX PubMed=1313186; DOI=10.1126/science.1313186;
RA Posada J., Cooper J.A.;
RT "Requirements for phosphorylation of MAP kinase during meiosis in Xenopus
RT oocytes.";
RL Science 255:212-215(1992).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
RX PubMed=9128253; DOI=10.1083/jcb.137.2.433;
RA Wang X.M., Zhai Y., Ferrell J.E. Jr.;
RT "A role for mitogen-activated protein kinase in the spindle assembly
RT checkpoint in XTC cells.";
RL J. Cell Biol. 137:433-443(1997).
RN [6]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=11854404; DOI=10.1091/mbc.01-11-0553;
RA Sohaskey M.L., Ferrell J.E. Jr.;
RT "Activation of p42 mitogen-activated protein kinase (MAPK), but not c-Jun
RT NH(2)-terminal kinase, induces phosphorylation and stabilization of MAPK
RT phosphatase XCL100 in Xenopus oocytes.";
RL Mol. Biol. Cell 13:454-468(2002).
RN [7]
RP INTERACTION WITH CDK2AP2.
RX PubMed=12944431; DOI=10.1242/dev.00731;
RA Terret M.E., Lefebvre C., Djiane A., Rassinier P., Moreau J., Maro B.,
RA Verlhac M.H.;
RT "DOC1R: a MAP kinase substrate that control microtubule organization of
RT metaphase II mouse oocytes.";
RL Development 130:5169-5177(2003).
CC -!- FUNCTION: Serine/threonine kinase which acts as an essential component
CC of the MAP kinase signal transduction pathway. Plays an important role
CC in the MAPK/ERK cascade. Depending on the cellular context, this
CC cascade mediates diverse biological functions such as cell growth,
CC adhesion, survival and differentiation through the regulation of
CC transcription, translation, cytoskeletal rearrangements. The MAPK/ERK
CC cascade also plays a role in initiation and regulation of meiosis,
CC mitosis, and postmitotic functions in differentiated cells by
CC phosphorylating a number of transcription factors. Many of the
CC substrates are localized in the nucleus, and seem to participate in the
CC regulation of transcription upon stimulation. However, other substrates
CC are found in the cytosol as well as in other cellular organelles, and
CC those are responsible for processes such as translation, mitosis and
CC apoptosis. Moreover, the MAPK/ERK cascade is also involved in the
CC regulation of the endosomal dynamics, including lysosome processing and
CC endosome cycling through the perinuclear recycling compartment (PNRC);
CC as well as in the fragmentation of the Golgi apparatus during mitosis.
CC Phosphorylates microtubule-associated protein 2 (MAP2), myelin basic
CC protein (MBP) and Elk-1. Phosphorylates dual specificity protein
CC phosphatase 1 (DUSP1) during meiosis, increasing its stability.
CC Activated by M phase promoting factor (MPF). Plays a role in the
CC spindle assembly checkpoint. {ECO:0000269|PubMed:11854404,
CC ECO:0000269|PubMed:1714387, ECO:0000269|PubMed:9128253}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.24;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by tyrosine phosphorylation during the M
CC phase of the meiotic cell cycle. Dephosphorylated and inactivated by
CC DUSP1. {ECO:0000269|PubMed:11854404, ECO:0000269|PubMed:1313186,
CC ECO:0000269|PubMed:1714387, ECO:0000269|PubMed:9128253}.
CC -!- SUBUNIT: Interacts with CDK2AP2 (PubMed:12944431).
CC {ECO:0000269|PubMed:12944431}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250}. Cytoplasm
CC {ECO:0000269|PubMed:9128253}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:9128253}. Note=Associated with the spindle during
CC prometaphase and metaphase in cultured XTC cells.
CC -!- TISSUE SPECIFICITY: Expressed in the central nervous system, kidney,
CC liver, intestine and the hematopoietic system. Also found in heart,
CC muscle, pancreas and lung. {ECO:0000269|PubMed:1714387}.
CC -!- DEVELOPMENTAL STAGE: Is expressed in the early oocyte and is maintained
CC at a constant level during embryogenesis. Its level declines at the
CC mid-blastula transition. {ECO:0000269|PubMed:1714387}.
CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Dually phosphorylated on Thr-188 and Tyr-190, which activates the
CC enzyme. {ECO:0000269|PubMed:1313186}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MAP kinase subfamily. {ECO:0000305}.
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DR EMBL; M60977; AAA50002.1; -; mRNA.
DR EMBL; X59813; CAA42482.1; -; mRNA.
DR EMBL; BC060748; AAH60748.1; -; mRNA.
DR PIR; A39754; A39754.
DR RefSeq; NP_001083548.1; NM_001090079.1.
DR AlphaFoldDB; P26696; -.
DR SMR; P26696; -.
DR BioGRID; 100311; 3.
DR IntAct; P26696; 1.
DR MINT; P26696; -.
DR iPTMnet; P26696; -.
DR MaxQB; P26696; -.
DR DNASU; 398985; -.
DR GeneID; 398985; -.
DR KEGG; xla:398985; -.
DR CTD; 398985; -.
DR Xenbase; XB-GENE-865273; mapk1.S.
DR OMA; VPRWYRA; -.
DR OrthoDB; 741207at2759; -.
DR BRENDA; 2.7.11.24; 6725.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 398985; Expressed in brain and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISS:UniProtKB.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0031647; P:regulation of protein stability; IDA:UniProtKB.
DR GO; GO:0070849; P:response to epidermal growth factor; ISS:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003527; MAP_kinase_CS.
DR InterPro; IPR008349; MAPK_ERK1/2.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR01770; ERK1ERK2MAPK.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS01351; MAPK; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Apoptosis; ATP-binding; Cell cycle; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..361
FT /note="Mitogen-activated protein kinase 1"
FT /id="PRO_0000186250"
FT DOMAIN 28..316
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 188..190
FT /note="TXY"
FT ACT_SITE 152
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 34..42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MOD_RES 188
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:1313186"
FT MOD_RES 190
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:1313186"
FT MUTAGEN 57
FT /note="K->R: Inactivation."
FT /evidence="ECO:0000269|PubMed:1313186"
FT MUTAGEN 86
FT /note="I->Y: Inactivation."
FT /evidence="ECO:0000269|PubMed:1313186"
FT MUTAGEN 188
FT /note="T->V,D: No effect on Tyr phosphorylation."
FT /evidence="ECO:0000269|PubMed:1313186"
FT MUTAGEN 190
FT /note="Y->F: Affects Thr phosphorylation."
FT /evidence="ECO:0000269|PubMed:1313186"
FT CONFLICT 5..7
FT /note="GAA -> AAS (in Ref. 1; AAA50002)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="I -> T (in Ref. 1; AAA50002)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="A -> S (in Ref. 1; AAA50002)"
FT /evidence="ECO:0000305"
FT CONFLICT 47..49
FT /note="DNV -> CNI (in Ref. 1; AAA50002)"
FT /evidence="ECO:0000305"
SQ 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
