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Protein

Heat stress transcription factor A-2

Gene

HSFA2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcriptional activator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE). Involved in heat stress responses. Seems to be involved in other environmental stress responses. Activates ascorbate peroxidase 2 (APX2) in addition to several heat shock protein (HSPs).3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi42 – 13695By similarityAdd
BLAST

GO - Molecular functioni

  • sequence-specific DNA binding Source: InterPro
  • transcription factor activity, sequence-specific DNA binding Source: TAIR
  • transcription regulatory region DNA binding Source: TAIR

GO - Biological processi

  • cellular response to heat Source: TAIR
  • cellular response to hypoxia Source: TAIR
  • cellular response to unfolded protein Source: TAIR
  • heat acclimation Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • response to chitin Source: TAIR
  • response to heat Source: TAIR
  • response to high light intensity Source: TAIR
  • response to hydrogen peroxide Source: TAIR
  • response to hypoxia Source: TAIR
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Stress response, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-ATH-3371453. Regulation of HSF1-mediated heat shock response.
R-ATH-3371511. HSF1 activation.
R-ATH-3371568. Attenuation phase.
R-ATH-3371571. HSF1-dependent transactivation.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat stress transcription factor A-2
Short name:
AtHsfA2
Alternative name(s):
AtHsf-04
Gene namesi
Name:HSFA2
Synonyms:HSF04
Ordered Locus Names:At2g26150
ORF Names:T19L18.4
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G26150.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus 1 Publication

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Heat-sensitive phenotype.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi5 – 51K → R: No effect on SUMO1 binding. 1 Publication
Mutagenesisi167 – 1671K → R: Reduces SUMO1 binding efficiency. 1 Publication
Mutagenesisi269 – 2691K → R: Increases SUMO1 binding efficiency. 1 Publication
Mutagenesisi315 – 3151K → R: Loss of sumoylation. Loss of SUMO1 binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 345345Heat stress transcription factor A-2PRO_0000270802Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki315 – 315Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

Post-translational modificationi

Exhibits temperature-dependent phosphorylation.By similarity
Sumoylated at Lys-315. Sumoylation represses its function.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiO80982.
PRIDEiO80982.

PTM databases

iPTMnetiO80982.

Expressioni

Inductioni

By heat stress, high light and hydrogen peroxide (H2O2).3 Publications

Gene expression databases

ExpressionAtlasiO80982. baseline and differential.
GenevisibleiO80982. AT.

Interactioni

Subunit structurei

Homotrimer (By similarity). Interacts with SUMO1.By similarity1 Publication

Protein-protein interaction databases

BioGridi2507. 6 interactions.
IntActiO80982. 2 interactions.
MINTiMINT-8152620.
STRINGi3702.AT2G26150.1.

Structurei

3D structure databases

ProteinModelPortaliO80982.
SMRiO80982. Positions 43-117.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni150 – 21667Hydrophobic repeat HR-A/BAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi230 – 24516Bipartite nuclear localization signalSequence analysisAdd
BLAST
Motifi273 – 28210AHA1
Motifi324 – 33310AHA2
Motifi334 – 3418Nuclear export signalSequence analysis

Domaini

The hydrophobic-rich region (HR-A/B) corresponds to the oligomerization domain. AHA motifs are transcriptional activator elements.1 Publication

Sequence similaritiesi

Belongs to the HSF family. Class A subfamily.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0627. Eukaryota.
COG5169. LUCA.
HOGENOMiHOG000237979.
InParanoidiO80982.
OMAiMMTFLAK.
PhylomeDBiO80982.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR000232. HSF_DNA-bd.
IPR027725. HSF_fam.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10015. PTHR10015. 1 hit.
PfamiPF00447. HSF_DNA-bind. 1 hit.
[Graphical view]
PRINTSiPR00056. HSFDOMAIN.
SMARTiSM00415. HSF. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS00434. HSF_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: O80982-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEELKVEMEE ETVTFTGSVA ASSSVGSSSS PRPMEGLNET GPPPFLTKTY
60 70 80 90 100
EMVEDPATDT VVSWSNGRNS FVVWDSHKFS TTLLPRYFKH SNFSSFIRQL
110 120 130 140 150
NTYGFRKIDP DRWEFANEGF LAGQKHLLKN IKRRRNMGLQ NVNQQGSGMS
160 170 180 190 200
CVEVGQYGFD GEVERLKRDH GVLVAEVVRL RQQQHSSKSQ VAAMEQRLLV
210 220 230 240 250
TEKRQQQMMT FLAKALNNPN FVQQFAVMSK EKKSLFGLDV GRKRRLTSTP
260 270 280 290 300
SLGTMEENLL HDQEFDRMKD DMEMLFAAAI DDEANNSMPT KEEQCLEAMN
310 320 330 340
VMMRDGNLEA ALDVKVEDLV GSPLDWDSQD LHDMVDQMGF LGSEP
Length:345
Mass (Da):39,114
Last modified:November 1, 1998 - v1
Checksum:i455FAB34582D7150
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC004747 Genomic DNA. Translation: AAC31222.1.
CP002685 Genomic DNA. Translation: AEC07800.1.
AK118744 mRNA. Translation: BAC43337.1.
PIRiT02609.
RefSeqiNP_180184.1. NM_128173.2. [O80982-1]
UniGeneiAt.38933.

Genome annotation databases

EnsemblPlantsiAT2G26150.1; AT2G26150.1; AT2G26150. [O80982-1]
GeneIDi817155.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC004747 Genomic DNA. Translation: AAC31222.1.
CP002685 Genomic DNA. Translation: AEC07800.1.
AK118744 mRNA. Translation: BAC43337.1.
PIRiT02609.
RefSeqiNP_180184.1. NM_128173.2. [O80982-1]
UniGeneiAt.38933.

3D structure databases

ProteinModelPortaliO80982.
SMRiO80982. Positions 43-117.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi2507. 6 interactions.
IntActiO80982. 2 interactions.
MINTiMINT-8152620.
STRINGi3702.AT2G26150.1.

PTM databases

iPTMnetiO80982.

Proteomic databases

PaxDbiO80982.
PRIDEiO80982.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G26150.1; AT2G26150.1; AT2G26150. [O80982-1]
GeneIDi817155.

Organism-specific databases

TAIRiAT2G26150.

Phylogenomic databases

eggNOGiKOG0627. Eukaryota.
COG5169. LUCA.
HOGENOMiHOG000237979.
InParanoidiO80982.
OMAiMMTFLAK.
PhylomeDBiO80982.

Enzyme and pathway databases

ReactomeiR-ATH-3371453. Regulation of HSF1-mediated heat shock response.
R-ATH-3371511. HSF1 activation.
R-ATH-3371568. Attenuation phase.
R-ATH-3371571. HSF1-dependent transactivation.

Miscellaneous databases

PROiO80982.

Gene expression databases

ExpressionAtlasiO80982. baseline and differential.
GenevisibleiO80982. AT.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR000232. HSF_DNA-bd.
IPR027725. HSF_fam.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10015. PTHR10015. 1 hit.
PfamiPF00447. HSF_DNA-bind. 1 hit.
[Graphical view]
PRINTSiPR00056. HSFDOMAIN.
SMARTiSM00415. HSF. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS00434. HSF_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Arabidopsis and the heat stress transcription factor world: how many heat stress transcription factors do we need?"
    Nover L., Bharti K., Doering P., Mishra S.K., Ganguli A., Scharf K.-D.
    Cell Stress Chaperones 6:177-189(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE, DOMAIN AHA.
  5. "Arabidopsis heat shock transcription factor A2 as a key regulator in response to several types of environmental stress."
    Nishizawa A., Yabuta Y., Yoshida E., Maruta T., Yoshimura K., Shigeoka S.
    Plant J. 48:535-547(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  6. "The heat stress transcription factor HsfA2 serves as a regulatory amplifier of a subset of genes in the heat stress response in Arabidopsis."
    Schramm F., Ganguli A., Kiehlmann E., Englich G., Walch D., von Koskull-Doering P.
    Plant Mol. Biol. 60:759-772(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  7. "A heat-inducible transcription factor, HsfA2, is required for extension of acquired thermotolerance in Arabidopsis."
    Charng Y.-Y., Liu H.-C., Liu N.-Y., Chi W.-T., Wang C.-N., Chang S.-H., Wang T.-T.
    Plant Physiol. 143:251-262(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  8. "Genome-wide analysis of heat shock transcription factor families in rice and Arabidopsis."
    Guo J., Wu J., Ji Q., Wang C., Luo L., Yuan Y., Wang Y., Wang J.
    J. Genet. Genomics 35:105-118(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.
  9. "Sumoylation of Arabidopsis heat shock factor A2 (HsfA2) modifies its activity during acquired thermotholerance."
    Cohen-Peer R., Schuster S., Meiri D., Breiman A., Avni A.
    Plant Mol. Biol. 74:33-45(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SUMO1, SUBCELLULAR LOCATION, SUMOYLATION AT LYS-315, DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-5; LYS-167; LYS-269 AND LYS-315.

Entry informationi

Entry nameiHSFA2_ARATH
AccessioniPrimary (citable) accession number: O80982
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: November 1, 1998
Last modified: February 17, 2016
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Plants overexpressing HSFA2 show increased tolerance to combined environmental stresses.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. 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.