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Reviewed, UniProtKB/Swiss-Prot Q03933 (HSF2_HUMAN)

Last modified June 16, 2009. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Heat shock factor protein 2
      Short name=HSF 2
Alternative name(s):
    Heat shock transcription factor 2
      Short name=HSTF 2
Gene names
Name: HSF2
Synonyms: HSTF2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length536 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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.

Subunit structure

DNA-binding homotrimer in stressed or heat shocked cells, otherwise found as a homodimer.

Subcellular location

Cytoplasm. Nucleus. Note: Cytoplasmic during normal growth and moves to the nucleus upon activation. Ref.5

Sequence similarities

Belongs to the HSF family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 536536Heat shock factor protein 2
PRO_0000124569

Regions

DNA binding7 – 112106 By similarity
Region119 – 19274Hydrophobic repeat HR-A/B
Region360 – 38526Hydrophobic repeat HR-C
Motif108 – 12215Nuclear localization signal Potential
Motif195 – 21016Nuclear localization signal Potential
Compositional bias170 – 1734Poly-Gln

Experimental info

Mutagenesis1091R → G: Fails to translocate to nucleus.
Mutagenesis196 – 1983RKR → ASS: Fails to translocate to nucleus.

Sequences

Sequence LengthMass (Da)Tools
Q03933-1 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 00DFD05CFD9DF0D3

FASTA53660,348
        10         20         30         40         50         60 
MKQSSNVPAF LSKLWTLVEE THTNEFITWS QNGQSFLVLD EQRFAKEILP KYFKHNNMAS 

        70         80         90        100        110        120 
FVRQLNMYGF RKVVHIDSGI VKQERDGPVE FQHPYFKQGQ DDLLENIKRK VSSSKPEENK 

       130        140        150        160        170        180 
IRQEDLTKII SSAQKVQIKQ ETIESRLSEL KSENESLWKE VSELRAKHAQ QQQVIRKIVQ 

       190        200        210        220        230        240 
FIVTLVQNNQ LVSLKRKRPL LLNTNGAQKK NLFQHIVKEP TDNHHHKVPH SRTEGLKPRE 

       250        260        270        280        290        300 
RISDDIIIYD VTDDNADEEN IPVIPETNED VISDPSNCSQ YPDIVIVEDD NEDEYAPVIQ 

       310        320        330        340        350        360 
SGEQNEPARE SLSSGSDGSS PLMSSAVQLN GSSSLTSEDP VTMMDSILND NINLLGKVEL 

       370        380        390        400        410        420 
LDYLDSIDCS LEDFQAMLSG RQFSIDPDLL VDLFTSSVQM NPTDYINNTK SENKGLETTK 

       430        440        450        460        470        480 
NNVVQPVSEE GRKSKSKPDK QLIQYTAFPL LAFLDGNPAS SVEQASTTAS SEVLSSVDKP 

       490        500        510        520        530 
IEVDELLDSS LDPEPTQSKL VRLEPLTEAE ASEATLFYLC ELAPAPLDSD MPLLDS 

« Hide

References

« Hide 'large scale' references
[1]"Isolation of a cDNA for HSF2: evidence for two heat shock factor genes in humans."
Schuetz T.J., Gallo G.J., Sheldon L., Tempst P., Kingston R.E.
Proc. Natl. Acad. Sci. U.S.A. 88:6911-6915(1991) [PubMed: 1871106] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 65-71.
[2]NIEHS SNPs program
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed: 14574404] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"Hydrophobic coiled-coil domains regulate the subcellular localization of human heat shock factor 2."
Sheldon L., Kingston R.E.
Genes Dev. 7:1549-1558(1993) [PubMed: 8339932] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

M65217 mRNA. Translation: AAA36017.1.
DQ492684 Genomic DNA. Translation: ABF47087.1.
AL121954, Z99129 Genomic DNA. Translation: CAC14262.2.
Z99129, AL121954 Genomic DNA. Translation: CAI20560.1.
BC112323 mRNA. Translation: AAI12324.1.
BC121051 mRNA. Translation: AAI21052.1.
IPIIPI00012878.
PIRA41138.
RefSeqNP_004497.1.
UniGeneHs.158195

3D structure databases

HSSPHSSP built from PDB template 3HTS based on UniProtKB P22121.
ModBaseSearch...

PTM databases

PhosphoSiteQ03933.

Proteomic databases

PRIDEQ03933.

Genome annotation databases

EnsemblENSG00000025156. Homo sapiens. [Contig view]
GeneID3298.

Organism-specific databases

GeneCardsGC06P122762.
HGNCHGNC:5225. HSF2.
HPACAB016067.
MIM140581. gene.
PharmGKBPA29494.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ03933.
HOVERGENQ03933.
OMAQ03933. NCSQYPD.

Gene expression databases

ArrayExpressQ03933.
BgeeQ03933.
CleanExHS_HSF2.
GermOnlineENSG00000025156. Homo sapiens.

Family and domain databases

InterProIPR000232. HSF_DNA_bd.
IPR010542. Vert_HS_TF.
IPR011991. Wing_hlx_DNA_bd.
[Graphical view]
Gene3DG3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
PfamPF00447. HSF_DNA-bind. 1 hit.
PF06546. Vert_HS_TF. 1 hit.
[Graphical view]
PRINTSPR00056. HSFDOMAIN.
ProDomPD001788. HSF_DNA_bind. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00415. HSF. 1 hit.
[Graphical view]
PROSITEPS00434. HSF_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio13083.
SOURCESearch...

Entry information

Entry nameHSF2_HUMAN
AccessionPrimary (citable) accession number: Q03933
Secondary accession number(s): Q2M1K4, Q9H445
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 16, 2009
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents