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Mitogen-activated protein kinase HOG1 (MAP kinase HOG1) (EC 2.7.11.24)

 HOG1_KLULA              Reviewed;         444 AA.
Q6CJA8;
29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
16-AUG-2004, sequence version 1.
23-MAY-2018, entry version 105.
RecName: Full=Mitogen-activated protein kinase HOG1;
Short=MAP kinase HOG1;
EC=2.7.11.24;
Name=HOG1; OrderedLocusNames=KLLA0F20053g;
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC
1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
NCBI_TaxID=284590;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
WM37;
PubMed=15229592; DOI=10.1038/nature02579;
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
Wincker P., Souciet J.-L.;
"Genome evolution in yeasts.";
Nature 430:35-44(2004).
-!- FUNCTION: Mitogen-activated protein kinase involved in a signal
transduction pathway that is activated by changes in the
osmolarity of the extracellular environment. Controls osmotic
regulation of transcription of target genes (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Activated by tyrosine and threonine
phosphorylation. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}.
-!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
whose phosphorylation activates the MAP kinases.
-!- PTM: Dually phosphorylated on Thr-173 and Tyr-175, which activates
the enzyme. {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. MAP kinase subfamily. HOG1 sub-subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00159}.
-----------------------------------------------------------------------
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EMBL; CR382126; CAG98689.1; -; Genomic_DNA.
RefSeq; XP_455981.1; XM_455981.1.
ProteinModelPortal; Q6CJA8; -.
SMR; Q6CJA8; -.
STRING; 284590.XP_455981.1; -.
EnsemblFungi; CAG98689; CAG98689; KLLA0_F20053g.
GeneID; 2895492; -.
KEGG; kla:KLLA0F20053g; -.
eggNOG; KOG0660; Eukaryota.
eggNOG; ENOG410XNY0; LUCA.
HOGENOM; HOG000233024; -.
InParanoid; Q6CJA8; -.
KO; K04441; -.
OMA; DVIDTIC; -.
OrthoDB; EOG092C2FL8; -.
Proteomes; UP000000598; Chromosome F.
GO; GO:0005743; C:mitochondrial inner membrane; IEA:EnsemblFungi.
GO; GO:0005758; C:mitochondrial intermembrane space; IEA:EnsemblFungi.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005516; F:calmodulin binding; IEA:EnsemblFungi.
GO; GO:0003682; F:chromatin binding; IEA:EnsemblFungi.
GO; GO:0016909; F:SAP kinase activity; IEA:EnsemblFungi.
GO; GO:0010846; P:activation of reciprocal meiotic recombination; IEA:EnsemblFungi.
GO; GO:0034605; P:cellular response to heat; IEA:EnsemblFungi.
GO; GO:0031670; P:cellular response to nutrient; IEA:EnsemblFungi.
GO; GO:0006972; P:hyperosmotic response; IEA:EnsemblFungi.
GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IEA:EnsemblFungi.
GO; GO:0010515; P:negative regulation of induction of conjugation with cellular fusion; IEA:EnsemblFungi.
GO; GO:0007231; P:osmosensory signaling pathway; IEA:EnsemblFungi.
GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IEA:EnsemblFungi.
GO; GO:1903694; P:positive regulation of mitotic G1 cell cycle arrest in response to nitrogen starvation; IEA:EnsemblFungi.
GO; GO:2001165; P:positive regulation of phosphorylation of RNA polymerase II C-terminal domain serine 2 residues; IEA:EnsemblFungi.
GO; GO:0042307; P:positive regulation of protein import into nucleus; IEA:EnsemblFungi.
GO; GO:1903643; P:positive regulation of recombination hotspot binding; IEA:EnsemblFungi.
GO; GO:0061393; P:positive regulation of transcription from RNA polymerase II promoter in response to osmotic stress; IEA:EnsemblFungi.
GO; GO:0036091; P:positive regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IEA:EnsemblFungi.
GO; GO:0050821; P:protein stabilization; IEA:EnsemblFungi.
GO; GO:1903715; P:regulation of aerobic respiration; IEA:EnsemblFungi.
GO; GO:1990611; P:regulation of cytoplasmic translational initiation in response to stress; IEA:EnsemblFungi.
GO; GO:0016241; P:regulation of macroautophagy; IEA:EnsemblFungi.
GO; GO:0033262; P:regulation of nuclear cell cycle DNA replication; IEA:EnsemblFungi.
GO; GO:0046685; P:response to arsenic-containing substance; IEA:EnsemblFungi.
GO; GO:0051403; P:stress-activated MAPK cascade; IEA:EnsemblFungi.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd07856; STKc_Sty1_Hog1; 1.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR003527; MAP_kinase_CS.
InterPro; IPR008352; MAPK_p38-like.
InterPro; IPR038783; MAPK_Sty1/Hog1.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR24055:SF247; PTHR24055:SF247; 1.
Pfam; PF00069; Pkinase; 1.
PRINTS; PR01773; P38MAPKINASE.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS01351; MAPK; 1.
PROSITE; PS00221; MIP; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
3: Inferred from homology;
Activator; ATP-binding; Complete proteome; Cytoplasm; Kinase;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transcription;
Transcription regulation; Transferase.
CHAIN 1 444 Mitogen-activated protein kinase HOG1.
/FTId=PRO_0000289694.
DOMAIN 22 301 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 28 36 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 173 175 TXY.
COMPBIAS 374 403 Gln-rich.
ACT_SITE 143 143 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 51 51 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 173 173 Phosphothreonine. {ECO:0000250}.
MOD_RES 175 175 Phosphotyrosine. {ECO:0000250}.
SEQUENCE 444 AA; 50298 MW; CEA1CB7A1849891D CRC64;
MSNEEFIRTQ IFGTVFEITN RYTNLNPVGM GAFGLVCSAT DTLTSQPVAI KKIMKPFSTS
VLAKRTYREL KLLKHLRHEN LICLEDIFLS PLEDIYFVTE LQGTDLHRLL QTRPLEKQFV
QYFLYQILRG LKYVHSAGVI HRDLKPSNIL INENCDLKIC DFGLARIQDP QMTGYVSTRY
YRAPEIMLTW QKYNVEVDIW SAGCIFAEMI EGKPLFPGKD HVHQFSIITD LLGSPPKDVI
DTICSENTLK FVTSLPHRDP VPFSSRFQNL EPDAIDLLEK MLVFDPKKRI TAADALAHPY
LSPYHDPTDE PIAEAKFDWN FNDADLPVDT WRVMMYSEIL DFHQIGDPQI NTNATFDDQV
AAATVAAAEA ASKQQQQQQH QTEEQTQQTI ASTPPQAQVT PQQLESGANS NSNSNPSFSI
GPDPANETLT NFANQADQYV SKFK


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