| General information | | DisProt: | DP00036 | | Name: | Heat shock factor protein | | Synonym(s): | HSF_KLULA
HSF
Heat shock transcription factor
HSTF
| | First appeared in release: | Release 1.0 (08/01/2003) | | UniProt: | P22121 | | UniGene: | | | SwissProt: | HSF_KLULA | | TrEMBL: | | | NCBI (GI): | 123686 | | Source organism: | Kluyveromyces lactis (Yeast) (Candida sphaerica) | | Sequence length: | 677 | | Percent disordered: | 32% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MGHNDSVETM DEISNPNNIL LPHDGTGLDA TGISGSQEPY GMVDVLNPDS LKDDSNVDEP - 60
LIEDIVNPSL DPEGVVSAEP SNEVGTPLLQ QPISLDHVIT RPASAGGVYS IGNSSTSSAA - 120
KLSDGDLTNA TDPLLNNAHG HGQPSSESQS HSNGYHKQGQ SQQPLLSLNK RKLLAKAHVD - 180
KHHSKKKLST TRARPAFVNK LWSMVNDKSN EKFIHWSTSG ESIVVPNRER FVQEVLPKYF - 240
KHSNFASFVR QLNMYGWHKV QDVKSGSMLS NNDSRWEFEN ENFKRGKEYL LENIVRQKSN - 300
TNILGGTTNA EVDIHILLNE LETVKYNQLA IAEDLKRITK DNEMLWKENM MARERHQSQQ - 360
QVLEKLLRFL SSVFGPNSAK TIGNGFQPDL IHELSDMQVN HMSNNNHNNT GNINPNAYHN - 420
ETDDPMANVF GPLTPTDQGK VPLQDYKLRP RLLLKNRSMS SSSSSNLNQR QSPQNRIVGQ - 480
SPPPQQQQQQ QQQQGQPQGQ QFSYPIQGGN QMMNQLGSPI GTQVGSPVGS QYGNQYGNQY - 540
SNQFGNQLQQ QTSRPALHHG SNGEIRELTP SIVSSDSPDP AFFQDLQNNI DKQEESIQEI - 600
QDWITKLNPG PGEDGNTPIF PELNMPSYFA NTGGSGQSEQ PSDYGDSQIE ELRNSRLHEP - 660
DRSFEEKNNG QKRRRAA
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| Functional narrative |
DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. Also required for growth at normal temperatures.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | N-terminal | | Location: | 1 - 195 | | Length: | 195 | | Region sequence: |
MGHNDSVETMDEISNPNNILLPHDGTGLDATGISGSQEPYGMVDVLNPDSLKDDSNVDEP
LIEDIVNPSLDPEGVVSAEPSNEVGTPLLQQPISLDHVITRPASAGGVYSIGNSSTSSAA
KLSDGDLTNATDPLLNNAHGHGQPSSESQSHSNGYHKQGQSQQPLLSLNKRKLLAKAHVD
KHHSKKKLSTTRARP | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | | | Functional subclasses: | Protein-DNA binding
Transactivation (transcriptional activation)
| Detection methods:
- Nuclear magnetic resonance (NMR) (pH: 3.4; D2O 10 %; H2O 90 %; KH2PO4 10 mM; Protein (3-5 mM))
- Nuclear magnetic resonance (NMR) (pH: 5.75; D2O 10 %; H2O 90 %; KH2PO4 10 mM; Protein (3-5 mM))
- Circular dichroism (CD) spectroscopy, far-UV (298 K; pH: 7; sodium phosphate 25 mM)
| References:
- Cho HS, Liu CW, Damberger FF, Pelton JG, Nelson HC, Wemmer DE. "Yeast heat shock transcription factor N-terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy." Protein Sci. 1996; 5(2): 262-9. PubMed: 8745404
| Comments:
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| Region 2 | | Type: | Disordered | | Name: | Omega loop | | Location: | 217 - 222 | | Length: | 6 | | Region sequence: |
STSGES | | Modification type: | Fragment
| | PDB: | 2HSF:A | | Structural/functional type: | | | Functional classes: | | | Functional subclasses: | Protein-DNA binding
Transactivation (transcriptional activation)
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 3.4; H2O/D2O (90/10); Potassium phosphate buffer 10 mM; Protein (2-4mM))
| References:
- Damberger FF, Pelton JG, Harrison CJ, Nelson HC, Wemmer DE. "Solution structure of the DNA-binding domain of the heat shock transcription factor determined by multidimensional heteronuclear magnetic resonance spectroscopy." Protein Sci. 1994; 3(10): 1806-21. PubMed: 7849597
| Comments:The fragment used for solution structure determination was the DNA-binding domain.(aa194-aa282)
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| Region 3 | | Type: | Disordered | | Name: | L1 | | Location: | 260 - 276 | | Length: | 17 | | Region sequence: |
VQDVKSGSMLSNNDSRW | | Modification type: | Fragment
| | PDB: | 2HSF:A | | Structural/functional type: | | | Functional classes: | | | Functional subclasses: | Transactivation (transcriptional activation)
Protein-DNA binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 3.4; H2O/D2O (90/10); Potassium phosphate buffer 10 mM; protein (2-4 mM))
| References:
- Damberger FF, Pelton JG, Harrison CJ, Nelson HC, Wemmer DE. "Solution structure of the DNA-binding domain of the heat shock transcription factor determined by multidimensional heteronuclear magnetic resonance spectroscopy." Protein Sci. 1994; 3(10): 1806-21. PubMed: 7849597
| Comments:The fragment used for solution structure determination was the DNA-binding domain.(aa194-aa282)
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| Region 4 | | Type: | Disordered | | Name: | | | Location: | 268 - 271 | | Length: | 4 | | Region sequence: |
MLSN | | Modification type: | Fragment
| | PDB: | | | Structural/functional type: | | | Functional classes: | | | Functional subclasses: | Transactivation (transcriptional activation)
Protein-DNA binding
| Detection methods:
- X-ray crystallography (281 K; Ammonium acetate 200 mM; PEG4000 (25-30%); Sodium acetate (pH 4.6) 100 mM)
| References:
- Harrison CJ, Bohm AA, Nelson HC. "Crystal structure of the DNA binding domain of the heat shock transcription factor." Science. 1994; 263(5144): 224-7. PubMed: 8284672
| Comments:The fragment used for solution structure determination was the DNA-binding domain.(aa194-aa282)
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| References |
- Jakobsen BK, Pelham HR. "A conserved heptapeptide restrains the activity of the yeast heat shock transcription factor." Embo J. 1991; 10(2): 369-75. PubMed: 1899375
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| Comments |
In the Damberger and Harrison papers the sequences listed are one residue off from the referenced sequence. Regions 2 and 3 are shown as residues 217-222 and 261-277 respectively, but the sequences correspond to residues 216-221 and 260-276 in the referenced sequence. Region 4 is shown as residues 269-272 in the Harrison paper, but correspond to residues 268-271 in the referenced sequence.
AV 6-28-2010 PubMed: 1899375
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