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Protein

Mitogen-activated protein kinase HOG1

Gene

HOG1

Organism
Cryphonectria parasitica (Chesnut blight fungus) (Endothia parasitica)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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). Involved in the virulence and conidia formation. Mediates tannic acid-induced laccase expression and cryparin expression.By similarity1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+By similarity

Enzyme regulationi

Activated by tyrosine and threonine phosphorylation (By similarity). Hypoviruses like CHV1-EP713 induce inactivation by lowering the degree of phosphorylation in response to various environmental stresses.By similarity1 Publication

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

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
OrganismiCryphonectria parasitica (Chesnut blight fungus) (Endothia parasitica)
Taxonomic identifieri5116 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeDiaporthalesCryphonectriaceaeCryphonectria-Endothia complexCryphonectria

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 358358Mitogen-activated protein kinase HOG1PRO_0000289686Add
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). Phosphorylated in response of osmotic stress.By similarity1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ875L0.

Structurei

3D structure databases

ProteinModelPortaliQ875L0.
SMRiQ875L0. 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

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

OMAiIRTQIFG.

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.
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.

Q875L0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEFVRAQIF GTTFEITSRY SDLQPVGMGA FGLVCSARDQ LTNQNVAIKK
60 70 80 90 100
IMKPFSTPVL AKRTYRELKL LKHLRHENII SLSDIFISPL EDIYFVTELL
110 120 130 140 150
GTDLHRLLTS RPLEKQFIQY FLYQIMRGLK YVHSAGVVHR DLKPSNILVN
160 170 180 190 200
ENCDLKICDF GLARIQDPQM TGYVSTRYYR APEIMLTWQK YDVEVDIWSA
210 220 230 240 250
GCIFAEMLEG KPLFPGKDHV NQFSIITELL GTPPDDVINT IASENTLRFV
260 270 280 290 300
KSLPKRERQP LASKFKNADE QAVDLLERML VFDPKKRITA SDALAHEYLA
310 320 330 340 350
PYHDPTDEPV AEEKFDWSFN DADLPVDTWK IMMYSEILDY HNVDASGASA

AMGEFNGQ
Length:358
Mass (Da):40,945
Last modified:June 1, 2003 - v1
Checksum:iD4B52064CF00B7C3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY166687 Genomic DNA. Translation: AAO27796.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY166687 Genomic DNA. Translation: AAO27796.1.

3D structure databases

ProteinModelPortaliQ875L0.
SMRiQ875L0. Positions 3-343.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ875L0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

OMAiIRTQIFG.

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.
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...

Publicationsi

  1. "Characterization of HOG1 homologue, CpMK1, from Cryphonectria parasitica and evidence for hypovirus-mediated perturbation of its phosphorylation in response to hypertonic stress."
    Park S.-M., Choi E.-S., Kim M.-J., Cha B.-J., Yang M.-S., Kim D.-H.
    Mol. Microbiol. 51:1267-1277(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PHOSPHORYLATION, ENZYME REGULATION.
    Strain: ATCC 38755 / EP155.

Entry informationi

Entry nameiHOG1_CRYPA
AccessioniPrimary (citable) accession number: Q875L0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: June 1, 2003
Last modified: July 22, 2015
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.