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Protein

Heat shock factor protein

Gene

Hsf

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi46 – 150105Add
BLAST

GO - Molecular functioni

  • DNA binding Source: FlyBase
  • identical protein binding Source: IntAct
  • sequence-specific DNA binding Source: FlyBase
  • transcription factor activity, sequence-specific DNA binding Source: FlyBase

GO - Biological processi

  • defense response to bacterium Source: FlyBase
  • defense response to fungus Source: FlyBase
  • negative regulation of transcription, DNA-templated Source: FlyBase
  • neurogenesis Source: FlyBase
  • positive regulation of DNA binding Source: FlyBase
  • positive regulation of transcription, DNA-templated Source: FlyBase
  • positive regulation of transcription from RNA polymerase II promoter Source: FlyBase
  • response to heat Source: FlyBase
  • response to methotrexate Source: FlyBase
  • 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-DME-3371453. Regulation of HSF1-mediated heat shock response.
R-DME-3371511. HSF1 activation.
R-DME-3371568. Attenuation phase.
R-DME-3371571. HSF1-dependent transactivation.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock factor protein
Short name:
HSF
Alternative name(s):
Heat shock transcription factor
Short name:
HSTF
Gene namesi
Name:Hsf
ORF Names:CG5748
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0001222. Hsf.

Subcellular locationi

GO - Cellular componenti

  • chromatin Source: FlyBase
  • nucleus Source: FlyBase
  • polytene chromosome Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 691691Heat shock factor proteinPRO_0000124578Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei256 – 2561Phosphoserine1 Publication
Modified residuei258 – 2581Phosphothreonine1 Publication
Modified residuei260 – 2601Phosphoserine1 Publication
Modified residuei283 – 2831Phosphoserine1 Publication
Modified residuei299 – 2991Phosphoserine1 Publication
Modified residuei580 – 5801Phosphoserine1 Publication

Post-translational modificationi

Exhibits temperature-dependent phosphorylation.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP22813.

PTM databases

iPTMnetiP22813.

Expressioni

Gene expression databases

BgeeiP22813.
ExpressionAtlasiP22813. differential.
GenevisibleiP22813. DM.

Interactioni

Subunit structurei

Homotrimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-130048,EBI-130048

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi62751. 9 interactions.
DIPiDIP-20041N.
IntActiP22813. 2 interactions.
MINTiMINT-994897.

Structurei

Secondary structure

1
691
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi50 – 578Combined sources
Beta strandi58 – 603Combined sources
Turni61 – 655Combined sources
Beta strandi66 – 694Combined sources
Turni70 – 723Combined sources
Beta strandi74 – 763Combined sources
Turni82 – 876Combined sources
Turni89 – 924Combined sources
Helixi97 – 10711Combined sources
Beta strandi115 – 1173Combined sources
Beta strandi128 – 1303Combined sources
Turni142 – 1443Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HKSNMR-A43-148[»]
1HKTNMR-A43-148[»]
ProteinModelPortaliP22813.
SMRiP22813. Positions 43-148.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22813.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi16 – 2611Poly-GluAdd
BLAST

Sequence similaritiesi

Belongs to the HSF family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000001182.
InParanoidiP22813.
KOiK09414.
OrthoDBiEOG7353WM.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR027072. HSF1.
IPR000232. HSF_DNA-bd.
IPR027725. HSF_fam.
IPR010542. Vert_HSTF_C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10015. PTHR10015. 2 hits.
PTHR10015:SF182. PTHR10015:SF182. 2 hits.
PfamiPF00447. HSF_DNA-bind. 1 hit.
PF06546. Vert_HS_TF. 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.

P22813-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRSRSSAKA VQFKHESEEE EEDEEEQLPS RRMHSYGDAA AIGSGVPAFL
60 70 80 90 100
AKLWRLVDDA DTNRLICWTK DGQSFVIQNQ AQFAKELLPL NYKHNNMASF
110 120 130 140 150
IRQLNMYGFH KITSIDNGGL RFDRDEIEFS HPFFKRNSPF LLDQIKRKIS
160 170 180 190 200
NNKNGDDKGV LKPEAMSKIL TDVKVMRGRQ DNLDSRFSAM KQENEVLWRE
210 220 230 240 250
IASLRQKHAK QQQIVNKLIQ FLITIVQPSR NMSGVKRHVQ LMINNTPEID
260 270 280 290 300
RARTTSETES ESGGGPVIHE LREELLDEVM NPSPAGYTAA SHYDQESVSP
310 320 330 340 350
PAVERPRSNM SISSHNVDYS NQSVEDLLLQ GNGTAGGNIL VGGAASPMAQ
360 370 380 390 400
SVSQSPAQHD VYTVTEAPDS HVQEVPNSPP YYEEQNVLTT PMVREQEQQK
410 420 430 440 450
RQQLKENNKL RRQAGDVILD AGDILVDSSS PKAQRTSIQH STQPDVMVQP
460 470 480 490 500
MIIKSEPENS SGLMDLMTPA NDLYSVNFIS EDMPTDIFED ALLPDGVEEA
510 520 530 540 550
AKLDQQQKFG QSTVSSGKFA SNFDVPTNST LLDANQASTS KAAAKAQASE
560 570 580 590 600
EEGMAVAKYS GAENGNNRDT NNSQLLRMAS VDELHGHLES MQDELETLKD
610 620 630 640 650
LLRGDGVAID QNMLMGLFND SDLMDNYGLS FPNDSISSEK KAPSGSELIS
660 670 680 690
YQPMYDLSDI LDTDDGNNDQ EASRRQMQTQ SSVLNTPRHE L
Length:691
Mass (Da):76,933
Last modified:August 1, 1991 - v1
Checksum:iE013428B22C98D35
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60070 mRNA. Translation: AAA28642.1.
AE013599 Genomic DNA. Translation: AAF57749.1.
PIRiA36295.
RefSeqiNP_476575.1. NM_057227.5.
UniGeneiDm.4107.

Genome annotation databases

EnsemblMetazoaiFBtr0086782; FBpp0085961; FBgn0001222.
GeneIDi37068.
KEGGidme:Dmel_CG5748.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60070 mRNA. Translation: AAA28642.1.
AE013599 Genomic DNA. Translation: AAF57749.1.
PIRiA36295.
RefSeqiNP_476575.1. NM_057227.5.
UniGeneiDm.4107.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HKSNMR-A43-148[»]
1HKTNMR-A43-148[»]
ProteinModelPortaliP22813.
SMRiP22813. Positions 43-148.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi62751. 9 interactions.
DIPiDIP-20041N.
IntActiP22813. 2 interactions.
MINTiMINT-994897.

PTM databases

iPTMnetiP22813.

Proteomic databases

PRIDEiP22813.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0086782; FBpp0085961; FBgn0001222.
GeneIDi37068.
KEGGidme:Dmel_CG5748.

Organism-specific databases

CTDi37068.
FlyBaseiFBgn0001222. Hsf.

Phylogenomic databases

GeneTreeiENSGT00390000001182.
InParanoidiP22813.
KOiK09414.
OrthoDBiEOG7353WM.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP22813.
GenomeRNAii37068.
PROiP22813.

Gene expression databases

BgeeiP22813.
ExpressionAtlasiP22813. differential.
GenevisibleiP22813. DM.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR027072. HSF1.
IPR000232. HSF_DNA-bd.
IPR027725. HSF_fam.
IPR010542. Vert_HSTF_C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10015. PTHR10015. 2 hits.
PTHR10015:SF182. PTHR10015:SF182. 2 hits.
PfamiPF00447. HSF_DNA-bind. 1 hit.
PF06546. Vert_HS_TF. 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. "Molecular cloning and expression of a hexameric Drosophila heat shock factor subject to negative regulation."
    Clos J., Westwood J.T., Becker P.B., Wilson S., Lambert K., Wu C.
    Cell 63:1085-1097(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256; THR-258; SER-260; SER-283; SER-299 AND SER-580, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  5. "Solution structure of the DNA-binding domain of Drosophila heat shock transcription factor."
    Vuister G.W., Kim S.-J., Orosz A., Marquardt J., Wu C., Bax A.
    Nat. Struct. Biol. 1:605-613(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 43-150.

Entry informationi

Entry nameiHSF_DROME
AccessioniPrimary (citable) accession number: P22813
Secondary accession number(s): Q9V8C1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: June 8, 2016
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.