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Protein

Mitogen-activated protein kinase HOG1

Gene

HOG1

Organism
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+By similarity

Enzyme regulationi

Activated by tyrosine and threonine phosphorylation.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei52ATPPROSITE-ProRule annotation1
Active sitei144Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi29 – 37ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase HOG1 (EC:2.7.11.24)
Short name:
MAP kinase HOG1
Gene namesi
Name:HOG1
Ordered Locus Names:CAGL0M11748g
OrganismiCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
Taxonomic identifieri284593 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeNakaseomycesNakaseomyces/Candida clade
Proteomesi
  • UP000002428 Componenti: Chromosome M

Organism-specific databases

CGDiCAL0136993. HOG1.
EuPathDBiFungiDB:CAGL0M11748g.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001863291 – 447Mitogen-activated protein kinase HOG1Add BLAST447

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei174PhosphothreonineBy similarity1
Modified residuei176PhosphotyrosineBy similarity1

Post-translational modificationi

Dually phosphorylated on Thr-174 and Tyr-176, which activates the enzyme.By similarity

Keywords - PTMi

Phosphoprotein

Interactioni

Protein-protein interaction databases

STRINGi284593.XP_449852.1.

Structurei

3D structure databases

ProteinModelPortaliQ6FIU2.
SMRiQ6FIU2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini23 – 302Protein kinasePROSITE-ProRule annotationAdd BLAST280

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi174 – 176TXY3

Domaini

The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. MAP kinase subfamily. HOG1 sub-subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0660. Eukaryota.
ENOG410XNY0. LUCA.
HOGENOMiHOG000233024.
InParanoidiQ6FIU2.
KOiK04441.
OMAiLSHEYLA.
OrthoDBiEOG092C2FL8.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008352. MAPK_p38.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01773. P38MAPKINASE.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6FIU2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATNEEFIRT QIFGTVFEIT NRYSDLNPVG MGAFGLVCSA TDTLTNQQVA
60 70 80 90 100
IKKIMKPFAT AVLAKRTYRE LKLLKHLRHE NLICLQDIFL SPLEDIYFVT
110 120 130 140 150
ELQGTDLHRL LQTRPLEKQF VQYFHYQILR GLKYVHSAGV VHRDLKPSNI
160 170 180 190 200
LINENCDLKI CDFGLARIQD PQMTGYVSTR YYRAPEIMLT WQKYDVEVDI
210 220 230 240 250
WSAGCIFAEM IEGKPLFPGK DHVHQFSIIT DLLGSPPSDV IDTICSENTL
260 270 280 290 300
KFVTSLPHRD PIPFSERFKT VEPDAVDLLE KMLVFDPKKR ITAADALAHP
310 320 330 340 350
YLAPYHDPTD EPVAEAKFDW HFNDADLPVD TWRVMMYSEI LDFHKIGGTD
360 370 380 390 400
GQIDTSATFD DQVAAATVAA AQAQAHALAQ AQMSQNMIDP NQLLNEDGTP
410 420 430 440
VSGSIAENSS NSATTNLNGA AAGMNSASDT INEYANQAVH FANEFQQ
Length:447
Mass (Da):50,111
Last modified:July 19, 2004 - v1
Checksum:i9721E7EC5C05EF4F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR380959 Genomic DNA. Translation: CAG62832.1.
RefSeqiXP_449852.1. XM_449852.1.

Genome annotation databases

EnsemblFungiiCAG62832; CAG62832; CAGL0M11748g.
GeneIDi2891247.
KEGGicgr:CAGL0M11748g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR380959 Genomic DNA. Translation: CAG62832.1.
RefSeqiXP_449852.1. XM_449852.1.

3D structure databases

ProteinModelPortaliQ6FIU2.
SMRiQ6FIU2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi284593.XP_449852.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAG62832; CAG62832; CAGL0M11748g.
GeneIDi2891247.
KEGGicgr:CAGL0M11748g.

Organism-specific databases

CGDiCAL0136993. HOG1.
EuPathDBiFungiDB:CAGL0M11748g.

Phylogenomic databases

eggNOGiKOG0660. Eukaryota.
ENOG410XNY0. LUCA.
HOGENOMiHOG000233024.
InParanoidiQ6FIU2.
KOiK04441.
OMAiLSHEYLA.
OrthoDBiEOG092C2FL8.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008352. MAPK_p38.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01773. P38MAPKINASE.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHOG1_CANGA
AccessioniPrimary (citable) accession number: Q6FIU2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: July 19, 2004
Last modified: November 2, 2016
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.