MP2K2_XENLA
ID MP2K2_XENLA Reviewed; 446 AA.
AC Q07192;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Dual specificity mitogen-activated protein kinase kinase 2;
DE Short=MAP kinase kinase 2;
DE Short=MAPKK 2;
DE EC=2.7.12.2;
DE AltName: Full=MAPK-ERK kinase 2;
DE Flags: Fragment;
GN Name=map2k2; Synonyms=mek2;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Embryo;
RX PubMed=8395011; DOI=10.1128/mcb.13.9.5738-5748.1993;
RA Yashar B.M., Kelley C., Yee K., Errede B., Zon L.I.;
RT "Novel members of the mitogen-activated protein kinase activator family in
RT Xenopus laevis.";
RL Mol. Cell. Biol. 13:5738-5748(1993).
CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and
CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases.
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=2.7.12.2;
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=2.7.12.2;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.2;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q07192-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q07192-2; Sequence=VSP_004876;
CC -!- TISSUE SPECIFICITY: Expressed abundantly in the adult brain and muscle.
CC -!- DEVELOPMENTAL STAGE: It is initially expressed in the dorsal region of
CC the embryo in a diffuse pattern at stage 17. Subsequently expression
CC occurs in the early stages of development of the central nervous
CC system, including the brain, spinal cord and eye. Later (stage 24)
CC expression is found in the hindbrain, midbrain and forebrain and the
CC somites. By stage 32, the expression is detected in the cranial
CC neurons. Expression in the brain is increased, while expression in the
CC spinal cord has decreased by stage 37.
CC -!- PTM: MAPKK is itself dependent on Ser/Thr phosphorylation for activity
CC catalyzed by MAP kinase kinase kinases.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
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DR EMBL; Z22736; CAA80430.1; -; mRNA.
DR PIR; A54694; A54694.
DR PIR; S36039; S36039.
DR AlphaFoldDB; Q07192; -.
DR SMR; Q07192; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004708; F:MAP kinase 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; IEA:UniProtKB-KW.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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 SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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 Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Tyrosine-protein kinase.
FT CHAIN <1..446
FT /note="Dual specificity mitogen-activated protein kinase
FT kinase 2"
FT /id="PRO_0000086377"
FT DOMAIN 149..414
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 27..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 276
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 155..163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 304
FT /note="Phosphoserine; by RAF"
FT /evidence="ECO:0000250"
FT MOD_RES 308
FT /note="Phosphothreonine; by RAF"
FT /evidence="ECO:0000250"
FT VAR_SEQ 51
FT /note="G -> GLQINLCDNTQS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8395011"
FT /id="VSP_004876"
FT MUTAGEN 178
FT /note="K->R: Loss of activity."
FT NON_TER 1
SQ SEQUENCE 446 AA; 50100 MW; 9E6B5DCA069856F2 CRC64;
AQWGLLHCSL HLVANILTMA TSNPSGSSGS SAGLGFQGQS QQHSTVNSMQ GKRKALKLNF
ANPAFKSTAK FTLNPTIQST HVMHKLDAIR KLETSYQKQD LRTSGAKALS TNEQATKNRL
ERLRTHSIES SGKLKLSPEQ HWDFTAEDLK DLGEIGRGAY GSVNKMSHTP SGQIMAVKRI
RSTVDEKEQK QLLMDLDVVM RSSDCPYIVQ FYGALFREGD CWICMELMAT SFDKFYKYVY
SFLDDVIPEE ILGKITLATV KALNHLKENL KIIHRDIKPS NILLDTNGNI KLCDFGISGQ
LVDSIAKTRD AGCRPYMAPE RIDPSASRQG YDVRSDVWSL GITLYELATG RFPYPKWNSV
FDQLTQVVKG DPPQLSNSEE REFSPSFTSF VNQCLTKDES KRPKYKELLK HPFILMYEER
TVDVAGYVGK ILEQMPVSPS SPMYVD
