PlantTFDB
Plant Transcription Factor Database
v4.0
Previous version: v1.0, v2.0, v3.0
Transcription Factor Information
Basic Information | Signature Domain | Sequence | 
Basic Information? help Back to Top
TF ID AT3G24520.1
Common NameAT-HSFC1, HSF08, HSFC1, MOB24.9
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis
Family HSF
Protein Properties Length: 330aa    MW: 37714.1 Da    PI: 6.016
Description heat shock transcription factor C1
Gene Model
Gene Model ID Type Source Coding Sequence
AT3G24520.1genomeTAIRView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1HSF_DNA-bind111.94.4e-35181102103
                   HHHHHHHHHCTGGGTTTSEESSSSSEEEES-HHHHHHHTHHHHSTT--HHHHHHHHHHTTEEE---SSBTTTTXTTSEEEEESXXXXXXXXXXXXXX CS
  HSF_DNA-bind   2 FlkklyeiledeelkeliswsengnsfvvldeeefakkvLpkyFkhsnfaSFvRQLnmYgFkkvkdeekkskskekiweFkhksFkkgkkellekik 98 
                   F+ k+y++++d++++ li+w    nsf+v+d+ +f++++Lp yFkh+nf+SFvRQLn+YgF+kv+ ++         weF++++F +g+k+ll++i 
   AT3G24520.1  18 FIVKTYQMVNDPSTDWLITWGPAHNSFIVVDPLDFSQRILPAYFKHNNFSSFVRQLNTYGFRKVDPDR---------WEFANEHFLRGQKHLLNNIA 105
                   9********************999*****************************************999.........******************** PP

                   XXXXX CS
  HSF_DNA-bind  99 rkkse 103
                   r+k++
   AT3G24520.1 106 RRKHA 110
                   **975 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
SMARTSM004158.2E-5514107IPR000232Heat shock factor (HSF)-type, DNA-binding
SuperFamilySSF467852.72E-3315107IPR011991Winged helix-turn-helix DNA-binding domain
Gene3DG3DSA:1.10.10.103.2E-3715107IPR011991Winged helix-turn-helix DNA-binding domain
PfamPF004474.4E-3018107IPR000232Heat shock factor (HSF)-type, DNA-binding
PRINTSPR000562.2E-181841IPR000232Heat shock factor (HSF)-type, DNA-binding
PRINTSPR000562.2E-185668IPR000232Heat shock factor (HSF)-type, DNA-binding
PROSITE patternPS0043405781IPR000232Heat shock factor (HSF)-type, DNA-binding
PRINTSPR000562.2E-186981IPR000232Heat shock factor (HSF)-type, DNA-binding
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0006355Biological Processregulation of transcription, DNA-templated
GO:0006970Biological Processresponse to osmotic stress
GO:0009737Biological Processresponse to abscisic acid
GO:0005634Cellular Componentnucleus
GO:0003700Molecular Functiontranscription factor activity, sequence-specific DNA binding
GO:0043565Molecular Functionsequence-specific DNA binding
Plant Ontology ? help Back to Top
PO Term PO Category PO Description
PO:0000013anatomycauline leaf
PO:0000037anatomyshoot apex
PO:0000230anatomyinflorescence meristem
PO:0000293anatomyguard cell
PO:0008019anatomyleaf lamina base
PO:0009005anatomyroot
PO:0009025anatomyvascular leaf
PO:0009029anatomystamen
PO:0009030anatomycarpel
PO:0009046anatomyflower
PO:0009047anatomystem
PO:0009052anatomyflower pedicel
PO:0020030anatomycotyledon
PO:0020100anatomyhypocotyl
PO:0020137anatomyleaf apex
PO:0007095developmental stageLP.08 eight leaves visible stage
PO:0007115developmental stageLP.04 four leaves visible stage
PO:0007123developmental stageLP.06 six leaves visible stage
PO:0007611developmental stagepetal differentiation and expansion stage
PO:0007616developmental stageflowering stage
Sequence ? help Back to Top
Protein Sequence    Length: 330 aa     Download sequence    Send to blast
MEDDNSNNNN NNNVIAPFIV KTYQMVNDPS TDWLITWGPA HNSFIVVDPL DFSQRILPAY  60
FKHNNFSSFV RQLNTYGFRK VDPDRWEFAN EHFLRGQKHL LNNIARRKHA RGMYGQDLED  120
GEIVREIERL KEEQRELEAE IQRMNRRIEA TEKRPEQMMA FLYKVVEDPD LLPRMMLEKE  180
RTKQQQQVSD KKKRRVTMST VKSEEEEVEE DEGRVFRVMS SSTPSPSSTE NLYRNHSPDG  240
WIVPMTQGQF GSYETGLVAK SMLSNSTSST SSSLTSTFSL PESVNGGGGG GCGSIQGERR  300
YKETATFGGV VESNPPTTPP YPFSLFRGGF
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
5d5u_B7e-261510726129Heat shock factor protein 1
5d5v_B7e-261510726129Heat shock factor protein 1
5d5v_D7e-261510726129Heat shock factor protein 1
Search in ModeBase
Nucleic Localization Signal ? help Back to Top
NLS
No. Start End Sequence
1190194KKKRR
2190195KKKRRV
Expression -- UniGene ? help Back to Top
UniGene ID E-value Expressed in
At.256070.0root
Expression -- Microarray ? help Back to Top
Source ID E-value
GEO425651640.0
Genevisible258139_at0.0
Expression AtlasAT3G24520-
AtGenExpressAT3G24520-
Functional Description ? help Back to Top
Source Description
TAIRmember of Heat Stress Transcription Factor (Hsf) family
UniProtTranscriptional regulator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE).
Binding Motif ? help Back to Top
Motif ID Method Source Motif file
MP00379DAP27203113Download
Motif logo
Cis-element ? help Back to Top
SourceLink
PlantRegMapAT3G24520.1
Regulation -- PlantRegMap ? help Back to Top
Source Upstream Regulator Target Gene
PlantRegMapRetrieveRetrieve
Regulation -- Hormone ? help Back to Top
Source Hormone
AHDabscisic acid
Interaction ? help Back to Top
Source Intact With
IntActSearch Q9LV52
Phenotype -- Mutation ? help Back to Top
Source ID
T-DNA ExpressAT3G24520
Annotation -- Nucleotide ? help Back to Top
Source Hit ID E-value Description
GenBankAY0726140.0AY072614.1 Arabidopsis thaliana AT3g24520/MOB24_5 mRNA, complete cds.
GenBankAY0561110.0AY056111.1 Arabidopsis thaliana AT3g24520/MOB24_5 mRNA, complete cds.
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqNP_189095.10.0heat stress transcription factor C-1
SwissprotQ9LV520.0HSFC1_ARATH; Heat stress transcription factor C-1
TrEMBLG0XQD10.0G0XQD1_ARATH; Heat shock factor
STRINGAT3G24520.10.0(Arabidopsis thaliana)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
Representative plantOGRP9617233
MalvidsOGEM67752743
Publications ? help Back to Top
  1. Riechmann JL, et al.
    Arabidopsis transcription factors: genome-wide comparative analysis among eukaryotes.
    Science, 2000. 290(5499): p. 2105-10
    [PMID:11118137]
  2. Nover L, et al.
    Arabidopsis and the heat stress transcription factor world: how many heat stress transcription factors do we need?
    Cell Stress Chaperones, 2001. 6(3): p. 177-89
    [PMID:11599559]
  3. Yamada K, et al.
    Empirical analysis of transcriptional activity in the Arabidopsis genome.
    Science, 2003. 302(5646): p. 842-6
    [PMID:14593172]
  4. Rizhsky L, et al.
    When defense pathways collide. The response of Arabidopsis to a combination of drought and heat stress.
    Plant Physiol., 2004. 134(4): p. 1683-96
    [PMID:15047901]
  5. Wang R, et al.
    Genomic analysis of the nitrate response using a nitrate reductase-null mutant of Arabidopsis.
    Plant Physiol., 2004. 136(1): p. 2512-22
    [PMID:15333754]
  6. Lee BH,Henderson DA,Zhu JK
    The Arabidopsis cold-responsive transcriptome and its regulation by ICE1.
    Plant Cell, 2005. 17(11): p. 3155-75
    [PMID:16214899]
  7. Lou Y,Gou JY,Xue HW
    PIP5K9, an Arabidopsis phosphatidylinositol monophosphate kinase, interacts with a cytosolic invertase to negatively regulate sugar-mediated root growth.
    Plant Cell, 2007. 19(1): p. 163-81
    [PMID:17220200]
  8. Xin Z,Mandaokar A,Chen J,Last RL,Browse J
    Arabidopsis ESK1 encodes a novel regulator of freezing tolerance.
    Plant J., 2007. 49(5): p. 786-99
    [PMID:17316173]
  9. Chawade A,Br
    Putative cold acclimation pathways in Arabidopsis thaliana identified by a combined analysis of mRNA co-expression patterns, promoter motifs and transcription factors.
    BMC Genomics, 2007. 8: p. 304
    [PMID:17764576]
  10. Guo J, et al.
    Genome-wide analysis of heat shock transcription factor families in rice and Arabidopsis.
    J Genet Genomics, 2008. 35(2): p. 105-18
    [PMID:18407058]
  11. Arabidopsis Interactome Mapping Consortium
    Evidence for network evolution in an Arabidopsis interactome map.
    Science, 2011. 333(6042): p. 601-7
    [PMID:21798944]