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Q6C4M9

- HOG1_YARLI

UniProt

Q6C4M9 - HOG1_YARLI

Protein

Mitogen-activated protein kinase HOG1

Gene

HOG1

Organism
Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (16 Aug 2004)
      Previous versions | rss
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    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

    Magnesium.By similarity

    Enzyme regulationi

    Activated by tyrosine and threonine phosphorylation.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei49 – 491ATPPROSITE-ProRule annotation
    Active sitei141 – 1411Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi26 – 349ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. MAP kinase activity Source: UniProtKB-EC

    GO - Biological processi

    1. regulation of transcription, DNA-templated Source: UniProtKB-KW
    2. transcription, DNA-templated Source: UniProtKB-KW

    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:YALI0E25135g
    OrganismiYarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
    Taxonomic identifieri284591 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDipodascaceaeYarrowia
    ProteomesiUP000001300: Chromosome E

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 386386Mitogen-activated protein kinase HOG1PRO_0000289709Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei171 – 1711PhosphothreonineBy similarity
    Modified residuei173 – 1731PhosphotyrosineBy similarity

    Post-translational modificationi

    Dually phosphorylated on Thr-171 and Tyr-173, which activates the enzyme.By similarity

    Keywords - PTMi

    Phosphoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi4952.Q6C4M9.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6C4M9.
    SMRiQ6C4M9. Positions 3-343.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini20 – 299280Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi171 – 1733TXY

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi350 – 38637Gln-richAdd
    BLAST

    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

    eggNOGiCOG0515.
    HOGENOMiHOG000233024.
    KOiK04441.
    OMAiMEEQFNG.
    OrthoDBiEOG7K3TWD.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR003527. MAP_kinase_CS.
    IPR008352. MAPK_p38.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    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.

    Q6C4M9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADFIRTQIF GTCFEITSRY VDLNPVGMGA FGLVCSAKDQ LTDQNVAIKK    50
    IMKPFGTPVL SKRTYRELKL LKHLRHENLI CLSDIFISPL EDIYFVTELL 100
    GTDLHRLLMT RPLEKQFIQY FLYQILRGLK YVHSAGVVHR DLKPSNILVN 150
    ENCDLKICDF GLARIQDTQM TGYVSTRYYR APEIMLTWQK YDVEVDIWST 200
    GCIFAEMLEG KPLFPGKDHV HQFSIITELL GSPPEDVIHT ICSENTLRFV 250
    RTLPRRERIP LASKFRNADP EAIDLMEKML VFDPKKRITA AEALAHPYLA 300
    PYHDPSDEPV AEERFDWSFN DADLPVDTWK VMMYSEILDF HNVDIDVNGQ 350
    PPQGQFEQVH AQAQAAVAQN EAARAREQEQ QQQEQQ 386
    Length:386
    Mass (Da):44,482
    Last modified:August 16, 2004 - v1
    Checksum:iD7026B1E6774CDB2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR382131 Genomic DNA. Translation: CAG79982.1.
    RefSeqiXP_504383.1. XM_504383.1.

    Genome annotation databases

    EnsemblFungiiCAG79982; CAG79982; YALI0_E25135g.
    GeneIDi2912707.
    KEGGiyli:YALI0E25135g.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR382131 Genomic DNA. Translation: CAG79982.1 .
    RefSeqi XP_504383.1. XM_504383.1.

    3D structure databases

    ProteinModelPortali Q6C4M9.
    SMRi Q6C4M9. Positions 3-343.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 4952.Q6C4M9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CAG79982 ; CAG79982 ; YALI0_E25135g .
    GeneIDi 2912707.
    KEGGi yli:YALI0E25135g.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233024.
    KOi K04441.
    OMAi MEEQFNG.
    OrthoDBi EOG7K3TWD.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR003527. MAP_kinase_CS.
    IPR008352. MAPK_p38.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    PRINTSi PR01773. P38MAPKINASE.
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS01351. MAPK. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Entry informationi

    Entry nameiHOG1_YARLI
    AccessioniPrimary (citable) accession number: Q6C4M9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 29, 2007
    Last sequence update: August 16, 2004
    Last modified: October 1, 2014
    This is version 79 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

    External Data

    Dasty 3