UniProtKB - P38532 (HSF1_MOUSE)
Heat shock factor protein 1
Hsf1
Functioni
Functions as a stress-inducible and DNA-binding transcription factor that plays a central role in the transcriptional activation of the heat shock response (HSR), leading to the expression of a large class of molecular chaperones heat shock proteins (HSPs) that protect cells from cellular insults' damage. In unstressed cells, is present in a HSP90-containing multichaperone complex that maintains it in a non-DNA-binding inactivated monomeric form. Upon exposure to heat and other stress stimuli, undergoes homotrimerization and activates HSP gene transcription through binding to site-specific heat shock elements (HSEs) present in the promoter regions of HSP genes. Upon heat shock stress, forms a chromatin-associated complex with TTC5/STRAP and p300/EP300 to stimulate HSR transcription, therefore increasing cell survival. Activation is reversible, and during the attenuation and recovery phase period of the HSR, returns to its unactivated form. Binds to inverted 5'-NGAAN-3' pentamer DNA sequences. Binds to chromatin at heat shock gene promoters. Plays also several other functions independently of its transcriptional activity. Involved in the repression of Ras-induced transcriptional activation of the c-fos gene in heat-stressed cells. Positively regulates pre-mRNA 3'-end processing and polyadenylation of HSP70 mRNA upon heat-stressed cells in a symplekin (SYMPK)-dependent manner. Plays a role in nuclear export of stress-induced HSP70 mRNA. Plays a role in the regulation of mitotic progression. Plays also a role as a negative regulator of non-homologous end joining (NHEJ) repair activity in a DNA damage-dependent manner. Involved in stress-induced cancer cell proliferation in a IER5-dependent manner.
By similarityGO - Molecular functioni
- chromatin binding Source: MGI
- chromatin DNA binding Source: UniProtKB
- DNA binding Source: MGI
- DNA-binding transcription factor activity Source: GO_Central
- DNA-binding transcription factor activity, RNA polymerase II-specific Source: MGI
- DNA-binding transcription repressor activity, RNA polymerase II-specific Source: MGI
- general transcription initiation factor binding Source: MGI
- heat shock protein binding Source: UniProtKB
- Hsp90 protein binding Source: UniProtKB
- identical protein binding Source: UniProtKB
- promoter-specific chromatin binding Source: UniProtKB
- protein heterodimerization activity Source: UniProtKB
- protein kinase binding Source: MGI
- protein self-association Source: UniProtKB
- RNA polymerase II cis-regulatory region sequence-specific DNA binding Source: MGI
- RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding Source: MGI
- sequence-specific DNA binding Source: MGI
- sequence-specific double-stranded DNA binding Source: MGI
- sequence-specific single stranded DNA binding Source: MGI
- STAT family protein binding Source: MGI
- transcription cis-regulatory region binding Source: MGI
- translation elongation factor binding Source: UniProtKB
GO - Biological processi
- cellular response to amino acid stimulus Source: MGI
- cellular response to angiotensin Source: MGI
- cellular response to cadmium ion Source: UniProtKB
- cellular response to copper ion Source: UniProtKB
- cellular response to diamide Source: UniProtKB
- cellular response to estradiol stimulus Source: MGI
- cellular response to gamma radiation Source: UniProtKB
- cellular response to heat Source: UniProtKB
- cellular response to hydrogen peroxide Source: MGI
- cellular response to organic cyclic compound Source: MGI
- cellular response to radiation Source: MGI
- cellular response to sodium arsenite Source: UniProtKB
- cellular response to unfolded protein Source: UniProtKB
- defense response Source: MGI
- DNA repair Source: UniProtKB-KW
- embryonic placenta development Source: MGI
- embryonic process involved in female pregnancy Source: MGI
- female meiotic nuclear division Source: MGI
- in utero embryonic development Source: MGI
- MAPK cascade Source: UniProtKB
- mRNA processing Source: UniProtKB-KW
- mRNA transcription Source: MGI
- mRNA transport Source: UniProtKB-KW
- negative regulation of cardiac muscle cell apoptotic process Source: MGI
- negative regulation of cell population proliferation Source: MGI
- negative regulation of double-strand break repair via nonhomologous end joining Source: UniProtKB
- negative regulation of gene expression Source: MGI
- negative regulation of inclusion body assembly Source: MGI
- negative regulation of neuron death Source: MGI
- negative regulation of protein-containing complex assembly Source: UniProtKB
- negative regulation of transcription by RNA polymerase II Source: UniProtKB
- negative regulation of tumor necrosis factor production Source: MGI
- positive regulation of apoptotic DNA fragmentation Source: MGI
- positive regulation of cell population proliferation Source: UniProtKB
- positive regulation of cold-induced thermogenesis Source: YuBioLab
- positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
- positive regulation of DNA-binding transcription factor activity Source: MGI
- positive regulation of gene expression Source: CACAO
- positive regulation of inclusion body assembly Source: MGI
- positive regulation of macrophage differentiation Source: MGI
- positive regulation of microtubule binding Source: MGI
- positive regulation of mitotic cell cycle Source: UniProtKB
- positive regulation of mRNA polyadenylation Source: UniProtKB
- positive regulation of multicellular organism growth Source: MGI
- positive regulation of transcription by RNA polymerase II Source: UniProtKB
- positive regulation of transcription from RNA polymerase II promoter in response to heat stress Source: UniProtKB
- positive regulation of tyrosine phosphorylation of STAT protein Source: MGI
- protein-containing complex assembly Source: UniProtKB
- protein phosphorylation Source: MGI
- regulation of cellular response to heat Source: UniProtKB
- regulation of transcription by RNA polymerase II Source: GO_Central
- response to estradiol Source: MGI
- response to heat Source: MGI
- response to lipopolysaccharide Source: MGI
- response to testosterone Source: MGI
- spermatogenesis Source: MGI
Keywordsi
Molecular function | Activator, DNA-binding |
Biological process | DNA damage, DNA repair, mRNA processing, mRNA transport, Stress response, Transcription, Transcription regulation, Transport |
Enzyme and pathway databases
Reactomei | R-MMU-3371453, Regulation of HSF1-mediated heat shock response R-MMU-3371511, HSF1 activation R-MMU-3371568, Attenuation phase R-MMU-3371571, HSF1-dependent transactivation |
Names & Taxonomyi
Protein namesi | Recommended name: Heat shock factor protein 1By similarityShort name: HSF 1 Alternative name(s): Heat shock transcription factor 1By similarity Short name: HSTF 1 |
Gene namesi | Name:Hsf1Imported |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:96238, Hsf1 |
VEuPathDBi | HostDB:ENSMUSG00000022556 |
Subcellular locationi
Nucleus
- Nucleus 1 Publication
- nucleoplasm By similarity
Cytoskeleton
- spindle pole By similarity
- centrosome By similarity
Cytoplasm and Cytosol
- Cytoplasm 1 Publication
Other locations
- perinuclear region By similarity
- kinetochore By similarity
Note: The monomeric form is cytoplasmic in unstressed cells (PubMed:26159920). Predominantly nuclear protein in both unstressed and heat shocked cells. Translocates in the nucleus upon heat shock. Nucleocytoplasmic shuttling protein. Colocalizes with IER5 in the nucleus. Colocalizes with BAG3 to the nucleus upon heat stress. Localizes in subnuclear granules called nuclear stress bodies (nSBs) upon heat shock. Colocalizes with SYMPK and SUMO1 in nSBs upon heat shock. Colocalizes with PRKACA/PKA in the nucleus and nSBs upon heat shock. Relocalizes from the nucleus to the cytoplasm during the attenuation and recovery phase period of the heat shock response. Translocates in the cytoplasm in a YWHAE- and XPO1/CRM1-dependent manner. Together with histone H2AX, redistributed in discrete nuclear DNA damage-induced foci after ionizing radiation (IR). Colocalizes with calcium-responsive transactivator SS18L1 at kinetochore region on the mitotic chromosomes. Colocalizes with gamma tubulin at centrosome. Localizes at spindle pole in metaphase. Colocalizes with PLK1 at spindle poles during prometaphase.By similarity1 Publication
Cytoskeleton
- centrosome Source: UniProtKB
- mitotic spindle pole Source: UniProtKB
Cytosol
- cytosol Source: MGI
Nucleus
- nuclear stress granule Source: UniProtKB
- nucleoplasm Source: UniProtKB
- nucleus Source: MGI
- PML body Source: UniProtKB
- pronucleus Source: MGI
Other locations
- chaperone complex Source: UniProtKB
- cytoplasm Source: MGI
- euchromatin Source: MGI
- heterochromatin Source: MGI
- kinetochore Source: UniProtKB
- perinuclear region of cytoplasm Source: UniProtKB
- protein-containing complex Source: MGI
- ribonucleoprotein complex Source: UniProtKB
Keywords - Cellular componenti
Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, NucleusPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000124568 | 1 – 525 | Heat shock factor protein 1Add BLAST | 525 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 1 | N-acetylmethionineBy similarity | 1 | |
Modified residuei | 80 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 91 | N6-acetyllysine; alternateBy similarity | 1 | |
Cross-linki | 91 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity | ||
Modified residuei | 118 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 121 | Phosphoserine; by MAPKAPK2By similarity | 1 | |
Cross-linki | 126 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Cross-linki | 131 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Modified residuei | 142 | Phosphothreonine; by CK2By similarity | 1 | |
Modified residuei | 150 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 188 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 208 | N6-acetyllysine; alternateBy similarity | 1 | |
Cross-linki | 208 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity | ||
Modified residuei | 216 | Phosphoserine; by PLK1By similarity | 1 | |
Cross-linki | 224 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Modified residuei | 230 | Phosphoserine; by CAMK2ABy similarity | 1 | |
Modified residuei | 275 | PhosphoserineBy similarity | 1 | |
Modified residuei | 292 | PhosphoserineBy similarity | 1 | |
Modified residuei | 298 | N6-acetyllysine; alternateBy similarity | 1 | |
Cross-linki | 298 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity | ||
Cross-linki | 298 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity | ||
Modified residuei | 303 | PhosphoserineCombined sources | 1 | |
Modified residuei | 307 | PhosphoserineCombined sources | 1 | |
Modified residuei | 314 | PhosphoserineBy similarity | 1 | |
Modified residuei | 319 | PhosphoserineBy similarity | 1 | |
Modified residuei | 320 | Phosphoserine; by PKABy similarity | 1 | |
Modified residuei | 323 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 326 | Phosphoserine; by MAPK12By similarity | 1 | |
Modified residuei | 345 | PhosphoserineBy similarity | 1 | |
Modified residuei | 415 | Phosphoserine; by PLK1By similarity | 1 | |
Modified residuei | 440 | PhosphoserineBy similarity | 1 | |
Modified residuei | 520 | N6-acetyllysineBy similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
jPOSTi | P38532 |
MaxQBi | P38532 |
PaxDbi | P38532 |
PeptideAtlasi | P38532 |
PRIDEi | P38532 |
ProteomicsDBi | 273389 [P38532-1] 273390 [P38532-2] |
PTM databases
iPTMneti | P38532 |
PhosphoSitePlusi | P38532 |
Expressioni
Gene expression databases
Bgeei | ENSMUSG00000022556, Expressed in secondary oocyte and 301 other tissues |
ExpressionAtlasi | P38532, baseline and differential |
Genevisiblei | P38532, MM |
Interactioni
Subunit structurei
Monomer; cytoplasmic latent and transcriptionally inactive monomeric form in unstressed cells. Homotrimer; in response to stress, such as heat shock, homotrimerizes and translocates into the nucleus, binds to heat shock element (HSE) sequences in promoter of heat shock protein (HSP) genes and acquires transcriptional ability.
Interacts (via monomeric form) with FKBP4; this interaction occurs in unstressed cells. Associates (via monomeric form) with HSP90 proteins in a multichaperone complex in unnstressed cell; this association maintains HSF1 in a non-DNA-binding and transcriptional inactive form by preventing HSF1 homotrimerization. Homotrimeric transactivation activity is modulated by protein-protein interactions and post-translational modifications.
Interacts with HSP90AA1; this interaction is decreased in a IER5-dependent manner, promoting HSF1 accumulation in the nucleus, homotrimerization and DNA-binding activities. Part (via regulatory domain in the homotrimeric form) of a large heat shock-induced HSP90-dependent multichaperone complex at least composed of FKBP4, FKBP5, HSP90 proteins, PPID, PPP5C and PTGES3; this association maintains the HSF1 homotrimeric DNA-bound form in a transcriptionally inactive form.
Interacts with BAG3 (via BAG domain); this interaction occurs in normal and heat-shocked cells promoting nuclear shuttling of HSF1 in a BAG3-dependent manner.
Interacts (via homotrimeric and hyperphosphorylated form) with FKBP4; this interaction occurs upon heat shock in a HSP90-dependent multichaperone complex.
Interacts (via homotrimeric form preferentially) with EEF1A proteins. In heat shocked cells, stress-denatured proteins compete with HSF1 homotrimeric DNA-bound form for association of the HSP90-dependent multichaperone complex, and hence alleviating repression of HSF1-mediated transcriptional activity.
Interacts (via homotrimeric form preferentially) with DAXX; this interaction relieves homotrimeric HSF1 from repression of its transcriptional activity by HSP90-dependent multichaperone complex upon heat shock.
Interacts (via D domain and preferentially with hyperphosphorylated form) with JNK1; this interaction occurs under both normal growth conditions and immediately upon heat shock.
Interacts (via D domain and preferentially with hyperphosphorylated form) with MAPK3; this interaction occurs upon heat shock.
Interacts with IER5 (via central region); this interaction promotes PPP2CA-induced dephosphorylation on Ser-121, Ser-307, Ser-314 and Thr-323 and HSF1 transactivation activity.
Found in a ribonucleoprotein complex composed of the HSF1 homotrimeric form, translation elongation factor eEF1A proteins and non-coding RNA heat shock RNA-1 (HSR1); this complex occurs upon heat shock and stimulates HSF1 DNA-binding activity.
Interacts (via transactivation domain) with HSPA1A/HSP70 and DNAJB1; these interactions result in the inhibition of heat shock- and HSF1-induced transcriptional activity during the attenuation and recovery phase from heat shock.
Interacts (via Ser-303 and Ser-307 phosphorylated form) with YWHAE; this interaction promotes HSF1 sequestration in the cytoplasm in an ERK-dependent manner.
Found in a complex with IER5 and PPP2CA.
Interacts with TPR; this interaction increases upon heat shock and stimulates export of HSP70 mRNA.
Interacts with SYMPK (via N-terminus) and CSTF2; these interactions occur upon heat shock.
Interacts (via transactivation domain) with HSPA8.
Interacts with EEF1D; this interaction occurs at heat shock promoter element (HSE) sequences.
Interacts with MAPKAPK2.
Interacts with PRKACA/PKA.
Interacts (via transactivation domain) with GTF2A2.
Interacts (via transactivation domain) with GTF2B.
Interacts (via transactivation domain) with TBP.
Interacts with CDK9, CCNT1 and EP300.
Interacts (via N-terminus) with XRCC5 (via N-terminus) and XRCC6 (via N-terminus); these interactions are direct and prevent XRCC5/XRCC6 heterodimeric binding and non-homologous end joining (NHEJ) repair activities induced by ionizing radiation (IR).
Interacts with PLK1; this interaction occurs during the early mitotic period, increases upon heat shock but does not modulate neither HSF1 homotrimerization and DNA-binding activities.
Interacts (via Ser-216 phosphorylated form) with CDC20; this interaction occurs in mitosis in a MAD2L1-dependent manner and prevents PLK1-stimulated degradation of HSF1 by blocking the recruitment of the SCF(BTRC) ubiquitin ligase complex.
Interacts with MAD2L1; this interaction occurs in mitosis.
Interacts with BTRC; this interaction occurs during mitosis, induces its ubiquitin-dependent degradation following stimulus-dependent phosphorylation at Ser-216, a process inhibited by CDC20.
Interacts with HSP90AA1 and HSP90AB1.
Forms a complex with TTC5/STRAP and p300/EP300; these interactions augment chromatin-bound HSF1 and p300/EP300 histone acetyltransferase activity (By similarity).
By similarityGO - Molecular functioni
- general transcription initiation factor binding Source: MGI
- heat shock protein binding Source: UniProtKB
- Hsp90 protein binding Source: UniProtKB
- identical protein binding Source: UniProtKB
- protein heterodimerization activity Source: UniProtKB
- protein kinase binding Source: MGI
- protein self-association Source: UniProtKB
- STAT family protein binding Source: MGI
- translation elongation factor binding Source: UniProtKB
Protein-protein interaction databases
BioGRIDi | 200443, 14 interactors |
IntActi | P38532, 13 interactors |
MINTi | P38532 |
STRINGi | 10090.ENSMUSP00000072617 |
Chemistry databases
BindingDBi | P38532 |
Miscellaneous databases
RNActi | P38532, protein |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 15 – 120 | DNA-binding domainBy similarityAdd BLAST | 106 | |
Regioni | 130 – 203 | Hydrophobic repeat HR-A/BBy similarityAdd BLAST | 74 | |
Regioni | 203 – 224 | D domainBy similarityAdd BLAST | 22 | |
Regioni | 221 – 310 | Regulatory domainBy similarityAdd BLAST | 90 | |
Regioni | 272 – 327 | DisorderedSequence analysisAdd BLAST | 56 | |
Regioni | 340 – 365 | DisorderedSequence analysisAdd BLAST | 26 | |
Regioni | 367 – 525 | Transactivation domainBy similarityAdd BLAST | 159 | |
Regioni | 380 – 405 | Hydrophobic repeat HR-CBy similarityAdd BLAST | 26 | |
Regioni | 441 – 460 | DisorderedSequence analysisAdd BLAST | 20 | |
Regioni | 495 – 525 | DisorderedSequence analysisAdd BLAST | 31 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 408 – 416 | 9aaTADBy similarity | 9 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 340 – 360 | Polar residuesSequence analysisAdd BLAST | 21 |
Domaini
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG0627, Eukaryota |
GeneTreei | ENSGT00940000158421 |
HOGENOMi | CLU_038829_2_0_1 |
InParanoidi | P38532 |
OMAi | LICWSPQ |
PhylomeDBi | P38532 |
TreeFami | TF330401 |
Family and domain databases
Gene3Di | 1.10.10.10, 1 hit |
InterProi | View protein in InterPro IPR000232, HSF_DNA-bd IPR027725, HSF_fam IPR010542, Vert_HSTF_C IPR036388, WH-like_DNA-bd_sf IPR036390, WH_DNA-bd_sf |
PANTHERi | PTHR10015, PTHR10015, 1 hit |
Pfami | View protein in Pfam PF00447, HSF_DNA-bind, 1 hit PF06546, Vert_HS_TF, 1 hit |
PRINTSi | PR00056, HSFDOMAIN |
SMARTi | View protein in SMART SM00415, HSF, 1 hit |
SUPFAMi | SSF46785, SSF46785, 1 hit |
PROSITEi | View protein in PROSITE PS00434, HSF_DOMAIN, 1 hit |
s (2+)i Sequence
Sequence statusi: Complete.
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 2 described isoforms and 8 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MDLAVGPGAA GPSNVPAFLT KLWTLVSDPD TDALICWSPS GNSFHVFDQG
60 70 80 90 100
QFAKEVLPKY FKHNNMASFV RQLNMYGFRK VVHIEQGGLV KPERDDTEFQ
110 120 130 140 150
HPCFLRGQEQ LLENIKRKVT SVSTLKSEDI KIRQDSVTRL LTDVQLMKGK
160 170 180 190 200
QECMDSKLLA MKHENEALWR EVASLRQKHA QQQKVVNKLI QFLISLVQSN
210 220 230 240 250
RILGVKRKIP LMLSDSNSAH SVPKYGRQYS LEHVHGPGPY SAPSPAYSSS
260 270 280 290 300
SLYSSDAVTS SGPIISDITE LAPTSPLASP GRSIDERPLS SSTLVRVKQE
310 320 330 340 350
PPSPPHSPRV LEASPGRPSS MDTPLSPTAF IDSILRESEP TPAASNTAPM
360 370 380 390 400
DTTGAQAPAL PTPSTPEKCL SVACLDKNEL SDHLDAMDSN LDNLQTMLTS
410 420 430 440 450
HGFSVDTSAL LDLFSPSVTM PDMSLPDLDS SLASIQELLS PQEPPRPIEA
460 470 480 490 500
ENSNPDSGKQ LVHYTAQPLF LLDPDAVDTG SSELPVLFEL GESSYFSEGD
510 520
DYTDDPTISL LTGTEPHKAK DPTVS
Computationally mapped potential isoform sequencesi
There are 8 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A075F5C6 | A0A075F5C6_MOUSE | Heat shock factor protein 1 | Hsf1 | 531 | Annotation score: | ||
A0A2R8W6L8 | A0A2R8W6L8_MOUSE | Heat shock factor protein 1 | Hsf1 | 438 | Annotation score: | ||
Q52L52 | Q52L52_MOUSE | Heat shock factor protein 1 | Hsf1 | 477 | Annotation score: | ||
A0A2I3BQX3 | A0A2I3BQX3_MOUSE | Heat shock factor protein 1 | Hsf1 | 172 | Annotation score: | ||
A0A2I3BR06 | A0A2I3BR06_MOUSE | Heat shock factor protein 1 | Hsf1 | 218 | Annotation score: | ||
A0A2I3BQV9 | A0A2I3BQV9_MOUSE | Heat shock factor protein 1 | Hsf1 | 142 | Annotation score: | ||
A0A2I3BRL6 | A0A2I3BRL6_MOUSE | Heat shock factor protein 1 | Hsf1 | 107 | Annotation score: | ||
A0A2I3BS48 | A0A2I3BS48_MOUSE | Heat shock factor protein 1 | Hsf1 | 78 | Annotation score: |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_002416 | 413 – 434 | Missing in isoform 1. 2 PublicationsAdd BLAST | 22 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X61753 mRNA Translation: CAA43892.1 BC013716 mRNA Translation: AAH13716.1 AF059275 Genomic DNA Translation: AAC80425.1 |
CCDSi | CCDS27572.1 [P38532-2] CCDS88787.1 [P38532-1] |
PIRi | A40583 |
RefSeqi | NP_001318083.1, NM_001331154.1 [P38532-1] NP_032322.1, NM_008296.3 [P38532-2] |
Genome annotation databases
Ensembli | ENSMUST00000072838; ENSMUSP00000072617; ENSMUSG00000022556 [P38532-2] ENSMUST00000227478; ENSMUSP00000154602; ENSMUSG00000022556 [P38532-1] |
GeneIDi | 15499 |
KEGGi | mmu:15499 |
UCSCi | uc056yzg.1, mouse [P38532-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X61753 mRNA Translation: CAA43892.1 BC013716 mRNA Translation: AAH13716.1 AF059275 Genomic DNA Translation: AAC80425.1 |
CCDSi | CCDS27572.1 [P38532-2] CCDS88787.1 [P38532-1] |
PIRi | A40583 |
RefSeqi | NP_001318083.1, NM_001331154.1 [P38532-1] NP_032322.1, NM_008296.3 [P38532-2] |
3D structure databases
AlphaFoldDBi | P38532 |
BMRBi | P38532 |
SMRi | P38532 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 200443, 14 interactors |
IntActi | P38532, 13 interactors |
MINTi | P38532 |
STRINGi | 10090.ENSMUSP00000072617 |
Chemistry databases
BindingDBi | P38532 |
ChEMBLi | CHEMBL5313 |
PTM databases
iPTMneti | P38532 |
PhosphoSitePlusi | P38532 |
Proteomic databases
jPOSTi | P38532 |
MaxQBi | P38532 |
PaxDbi | P38532 |
PeptideAtlasi | P38532 |
PRIDEi | P38532 |
ProteomicsDBi | 273389 [P38532-1] 273390 [P38532-2] |
Protocols and materials databases
Antibodypediai | 1848, 1766 antibodies from 49 providers |
DNASUi | 15499 |
Genome annotation databases
Ensembli | ENSMUST00000072838; ENSMUSP00000072617; ENSMUSG00000022556 [P38532-2] ENSMUST00000227478; ENSMUSP00000154602; ENSMUSG00000022556 [P38532-1] |
GeneIDi | 15499 |
KEGGi | mmu:15499 |
UCSCi | uc056yzg.1, mouse [P38532-1] |
Organism-specific databases
CTDi | 3297 |
MGIi | MGI:96238, Hsf1 |
VEuPathDBi | HostDB:ENSMUSG00000022556 |
Phylogenomic databases
eggNOGi | KOG0627, Eukaryota |
GeneTreei | ENSGT00940000158421 |
HOGENOMi | CLU_038829_2_0_1 |
InParanoidi | P38532 |
OMAi | LICWSPQ |
PhylomeDBi | P38532 |
TreeFami | TF330401 |
Enzyme and pathway databases
Reactomei | R-MMU-3371453, Regulation of HSF1-mediated heat shock response R-MMU-3371511, HSF1 activation R-MMU-3371568, Attenuation phase R-MMU-3371571, HSF1-dependent transactivation |
Miscellaneous databases
BioGRID-ORCSi | 15499, 5 hits in 76 CRISPR screens |
ChiTaRSi | Hsf1, mouse |
PROi | PR:P38532 |
RNActi | P38532, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000022556, Expressed in secondary oocyte and 301 other tissues |
ExpressionAtlasi | P38532, baseline and differential |
Genevisiblei | P38532, MM |
Family and domain databases
Gene3Di | 1.10.10.10, 1 hit |
InterProi | View protein in InterPro IPR000232, HSF_DNA-bd IPR027725, HSF_fam IPR010542, Vert_HSTF_C IPR036388, WH-like_DNA-bd_sf IPR036390, WH_DNA-bd_sf |
PANTHERi | PTHR10015, PTHR10015, 1 hit |
Pfami | View protein in Pfam PF00447, HSF_DNA-bind, 1 hit PF06546, Vert_HS_TF, 1 hit |
PRINTSi | PR00056, HSFDOMAIN |
SMARTi | View protein in SMART SM00415, HSF, 1 hit |
SUPFAMi | SSF46785, SSF46785, 1 hit |
PROSITEi | View protein in PROSITE PS00434, HSF_DOMAIN, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | HSF1_MOUSE | |
Accessioni | P38532Primary (citable) accession number: P38532 Secondary accession number(s): O70462 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1994 |
Last sequence update: | August 30, 2002 | |
Last modified: | May 25, 2022 | |
This is version 187 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - SIMILARITY comments
Index of protein domains and families