Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Heat shock factor protein 1 (HSF 1) (Heat shock transcription factor 1) (HSTF 1)

 HSF1_BOVIN              Reviewed;         525 AA.
Q08DJ8;
28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
31-OCT-2006, sequence version 1.
12-SEP-2018, entry version 101.
RecName: Full=Heat shock factor protein 1 {ECO:0000250|UniProtKB:Q00613};
Short=HSF 1;
AltName: Full=Heat shock transcription factor 1 {ECO:0000250|UniProtKB:Q00613};
Short=HSTF 1;
Name=HSF1 {ECO:0000250|UniProtKB:Q00613};
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Brain cortex;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Function 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.
Activation is reversible, and during the attenuation and recovery
phase period of the heat shock response, 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.
{ECO:0000250|UniProtKB:Q00613}.
-!- SUBUNIT: 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-324 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 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, a
process inhibited by CDC20. Interacts with HSP90AA1 and HSP90AB1.
{ECO:0000250|UniProtKB:Q00613}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q00613}.
Cytoplasm {ECO:0000250|UniProtKB:Q00613}. Nucleus, nucleoplasm
{ECO:0000250|UniProtKB:Q00613}. Cytoplasm, perinuclear region
{ECO:0000250|UniProtKB:Q00613}. Cytoplasm, cytoskeleton, spindle
pole {ECO:0000250|UniProtKB:Q00613}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome
{ECO:0000250|UniProtKB:Q00613}. Chromosome, centromere,
kinetochore {ECO:0000250|UniProtKB:Q00613}. Note=The monomeric
form is cytoplasmic in unstressed cells. 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.
{ECO:0000250|UniProtKB:Q00613}.
-!- DOMAIN: In unstressed cells, spontaneous homotrimerization is
inhibited. Intramolecular interactions between the hydrophobic
repeat HR-A/B and HR-C regions are necessary to maintain HSF1 in
the inactive, monomeric conformation. Furthermore, intramolecular
interactions between the regulatory domain and the nonadjacent
transactivation domain prevents transcriptional activation, a
process that is relieved upon heat shock. The regulatory domain is
necessary for full repression of the transcriptional activation
domain in unstressed cells through its phosphorylation on Ser-303
and Ser-307. In heat stressed cells, HSF1 homotrimerization occurs
through formation of a three-stranded coiled-coil structure
generated by intermolecular interactions between HR-A/B regions
allowing DNA-binding activity. The D domain is necessary for
translocation to the nucleus, interaction with JNK1 and MAPK3 and
efficient JNK1- and MAPK3-dependent phosphorylation. The
regulatory domain confers heat shock inducibility on the
transcriptional transactivation domain. The regulatory domain is
necessary for transcriptional activation through its
phosphorylation on Ser-230 upon heat shock. 9aaTAD is a
transactivation motif present in a large number of yeast and
animal transcription factors. {ECO:0000250|UniProtKB:Q00613}.
-!- PTM: Phosphorylated. Phosphorylated in unstressed cells; this
phosphorylation is constitutive and implicated in the repression
of HSF1 transcriptional activity. Phosphorylated on Ser-121 by
MAPKAPK2; this phosphorylation promotes interaction with HSP90
proteins and inhibits HSF1 homotrimerization, DNA-binding and
transactivation activities. Phosphorylation on Ser-303 by
GSK3B/GSK3-beta and on Ser-307 by MAPK3 within the regulatory
domain is involved in the repression of HSF1 transcriptional
activity and occurs in a RAF1-dependent manner. Phosphorylation on
Ser-303 and Ser-307 increases HSF1 nuclear export in a YWHAE- and
XPO1/CRM1-dependent manner. Phosphorylation on Ser-307 is a
prerequisite for phosphorylation on Ser-303. According to, Ser-303
is not phosphorylated in unstressed cells. Phosphorylated on Ser-
415 by PLK1; phosphorylation promotes nuclear translocation upon
heat shock. Hyperphosphorylated upon heat shock and during the
attenuation and recovery phase period of the heat shock response.
Phosphorylated on Thr-142; this phosphorylation increases HSF1
transactivation activity upon heat shock. Phosphorylation on Ser-
230 by CAMK2A; this phosphorylation enhances HSF1 transactivation
activity upon heat shock. Phosphorylation on Ser-327 by MAPK12;
this phosphorylation enhances HSF1 nuclear translocation,
homotrimerization and transactivation activities upon heat shock.
Phosphorylated on Ser-320 by PRKACA/PKA; this phosphorylation
promotes nuclear localization and transcriptional activity upon
heat shock. Phosphorylated on Ser-359 by MAPK8; this
phosphorylation occurs upon heat shock, induces HSF1 translocation
into nuclear stress bodies and negatively regulates
transactivation activity. Neither basal nor stress-inducible
phosphorylation on Ser-230, Ser-292, Ser-303, Ser-307, Ser-314,
Ser-319, Ser-320, Thr-324, Ser-327, Ser-339, Ser-346, Ser-359 and
Ser-364 within the regulatory domain is involved in the regulation
of HSF1 subcellular localization or DNA-binding activity; however,
it negatively regulates HSF1 transactivation activity.
Phosphorylated by PLK1 in the early mitotic period; this
phosphorylation regulates HSF1 localization to the spindle pole,
the recruitment of the SCF(BTRC) ubiquitin ligase complex inducing
HSF1 degradation, and hence mitotic progression. Dephosphorylated
on Ser-121, Ser-307, Ser-314, Thr-324 by phosphatase PPP2CA in an
IER5-dependent manner, leading to HSF1-mediated transactivation
activity. {ECO:0000250|UniProtKB:Q00613}.
-!- PTM: Sumoylated with SUMO1 and SUMO2 upon heat shock in a ERK2-
dependent manner. Sumoylated by SUMO1 on Lys-298; sumoylation
occurs upon heat shock and promotes its localization to nuclear
stress bodies and DNA-binding activity. Phosphorylation on Ser-303
and Ser-307 is probably a prerequisite for sumoylation.
{ECO:0000250|UniProtKB:Q00613}.
-!- PTM: Acetylated on Lys-118; this acetylation is decreased in a
IER5-dependent manner. Acetylated on Lys-118, Lys-208 and Lys-298;
these acetylations occur in a EP300-dependent manner. Acetylated
on Lys-80; this acetylation inhibits DNA-binding activity upon
heat shock. Deacetylated on Lys-80 by SIRT1; this deacetylation
increases DNA-binding activity. {ECO:0000250|UniProtKB:Q00613}.
-!- PTM: Ubiquitinated by SCF(BTRC) and degraded following stimulus-
dependent phosphorylation by PLK1 in mitosis. Polyubiquitinated.
Undergoes proteasomal degradation upon heat shock and during the
attenuation and recovery phase period of the heat shock response.
{ECO:0000250|UniProtKB:Q00613}.
-!- SIMILARITY: Belongs to the HSF family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; BC123711; AAI23712.1; -; mRNA.
RefSeq; NP_001070277.1; NM_001076809.1.
UniGene; Bt.61991; -.
ProteinModelPortal; Q08DJ8; -.
SMR; Q08DJ8; -.
STRING; 9913.ENSBTAP00000027654; -.
PaxDb; Q08DJ8; -.
PRIDE; Q08DJ8; -.
Ensembl; ENSBTAT00000027654; ENSBTAP00000027654; ENSBTAG00000020751.
GeneID; 506235; -.
KEGG; bta:506235; -.
CTD; 3297; -.
VGNC; VGNC:29981; HSF1.
eggNOG; KOG0627; Eukaryota.
eggNOG; COG5169; LUCA.
GeneTree; ENSGT00390000001182; -.
HOGENOM; HOG000253917; -.
HOVERGEN; HBG005999; -.
InParanoid; Q08DJ8; -.
KO; K09414; -.
OMA; QFSLEHV; -.
OrthoDB; EOG091G087O; -.
TreeFam; TF330401; -.
Reactome; R-BTA-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-BTA-3371511; HSF1 activation.
Reactome; R-BTA-3371568; Attenuation phase.
Reactome; R-BTA-3371571; HSF1-dependent transactivation.
Proteomes; UP000009136; Chromosome 14.
Bgee; ENSBTAG00000020751; Expressed in 9 organ(s), highest expression level in skeletal muscle tissue.
GO; GO:0005813; C:centrosome; ISS:UniProtKB.
GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
GO; GO:0097431; C:mitotic spindle pole; ISS:UniProtKB.
GO; GO:0097165; C:nuclear stress granule; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0016605; C:PML body; ISS:UniProtKB.
GO; GO:0045120; C:pronucleus; IEA:Ensembl.
GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0031072; F:heat shock protein binding; ISS:UniProtKB.
GO; GO:0051879; F:Hsp90 protein binding; ISS:UniProtKB.
GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
GO; GO:0001162; F:RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0061770; F:translation elongation factor binding; ISS:UniProtKB.
GO; GO:0034622; P:cellular protein-containing complex assembly; ISS:UniProtKB.
GO; GO:0071276; P:cellular response to cadmium ion; ISS:UniProtKB.
GO; GO:0071280; P:cellular response to copper ion; ISS:UniProtKB.
GO; GO:0072738; P:cellular response to diamide; ISS:UniProtKB.
GO; GO:0071480; P:cellular response to gamma radiation; ISS:UniProtKB.
GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
GO; GO:1903936; P:cellular response to sodium arsenite; ISS:UniProtKB.
GO; GO:0034620; P:cellular response to unfolded protein; ISS:UniProtKB.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0001892; P:embryonic placenta development; IEA:Ensembl.
GO; GO:0060136; P:embryonic process involved in female pregnancy; IEA:Ensembl.
GO; GO:0007143; P:female meiotic nuclear division; IEA:Ensembl.
GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0009299; P:mRNA transcription; IEA:Ensembl.
GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:2001033; P:negative regulation of double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IEA:Ensembl.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISS:UniProtKB.
GO; GO:1900365; P:positive regulation of mRNA polyadenylation; ISS:UniProtKB.
GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0061408; P:positive regulation of transcription from RNA polymerase II promoter in response to heat stress; ISS:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
GO; GO:0070207; P:protein homotrimerization; ISS:UniProtKB.
GO; GO:1900034; P:regulation of cellular response to heat; ISS:UniProtKB.
GO; GO:0043497; P:regulation of protein heterodimerization activity; ISS:UniProtKB.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR000232; HSF_DNA-bd.
InterPro; IPR027725; HSF_fam.
InterPro; IPR010542; Vert_HSTF_C.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
PANTHER; PTHR10015; PTHR10015; 1.
Pfam; PF00447; HSF_DNA-bind; 1.
Pfam; PF06546; Vert_HS_TF; 1.
PRINTS; PR00056; HSFDOMAIN.
SMART; SM00415; HSF; 1.
SUPFAM; SSF46785; SSF46785; 1.
PROSITE; PS00434; HSF_DOMAIN; 1.
2: Evidence at transcript level;
Acetylation; Activator; Centromere; Chromosome; Complete proteome;
Cytoplasm; Cytoskeleton; DNA damage; DNA repair; DNA-binding;
Isopeptide bond; Kinetochore; mRNA processing; mRNA transport;
Nucleus; Phosphoprotein; Reference proteome; Stress response;
Transcription; Transcription regulation; Transport; Ubl conjugation.
CHAIN 1 525 Heat shock factor protein 1.
/FTId=PRO_0000260263.
REGION 15 120 DNA-binding domain.
{ECO:0000250|UniProtKB:Q00613}.
REGION 130 203 Hydrophobic repeat HR-A/B.
{ECO:0000250|UniProtKB:Q00613}.
REGION 203 224 D domain. {ECO:0000250|UniProtKB:Q00613}.
REGION 221 310 Regulatory domain.
{ECO:0000250|UniProtKB:Q00613}.
REGION 367 525 Transactivation domain.
{ECO:0000250|UniProtKB:Q00613}.
REGION 380 405 Hydrophobic repeat HR-C.
{ECO:0000250|UniProtKB:Q00613}.
MOTIF 408 416 9aaTAD. {ECO:0000250|UniProtKB:Q00613}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q00613}.
MOD_RES 80 80 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q00613}.
MOD_RES 91 91 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q00613}.
MOD_RES 118 118 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q00613}.
MOD_RES 121 121 Phosphoserine; by MAPKAPK2.
{ECO:0000250|UniProtKB:Q00613}.
MOD_RES 142 142 Phosphothreonine; by CK2.
{ECO:0000250|UniProtKB:Q00613}.
MOD_RES 150 150 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q00613}.
MOD_RES 188 188 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q00613}.
MOD_RES 208 208 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q00613}.
MOD_RES 230 230 Phosphoserine; by CAMK2A.
{ECO:0000250|UniProtKB:Q00613}.
MOD_RES 275 275 Phosphoserine.
{ECO:0000250|UniProtKB:Q00613}.
MOD_RES 292 292 Phosphoserine.
{ECO:0000250|UniProtKB:Q00613}.
MOD_RES 298 298 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q00613}.
MOD_RES 303 303 Phosphoserine; by GSK3-beta.
{ECO:0000250|UniProtKB:Q00613}.
MOD_RES 307 307 Phosphoserine; by MAPK3.
{ECO:0000250|UniProtKB:Q00613}.
MOD_RES 314 314 Phosphoserine.
{ECO:0000250|UniProtKB:Q00613}.
MOD_RES 319 319 Phosphoserine.
{ECO:0000250|UniProtKB:Q00613}.
MOD_RES 320 320 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:Q00613}.
MOD_RES 324 324 Phosphothreonine.
{ECO:0000250|UniProtKB:Q00613}.
MOD_RES 327 327 Phosphoserine; by MAPK12.
{ECO:0000250|UniProtKB:Q00613}.
MOD_RES 346 346 Phosphoserine.
{ECO:0000250|UniProtKB:Q00613}.
MOD_RES 359 359 Phosphoserine; by MAPK8.
{ECO:0000250|UniProtKB:Q00613}.
MOD_RES 415 415 Phosphoserine; by PLK1.
{ECO:0000250|UniProtKB:Q00613}.
MOD_RES 440 440 Phosphoserine.
{ECO:0000250|UniProtKB:Q00613}.
MOD_RES 520 520 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q00613}.
CROSSLNK 91 91 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q00613}.
CROSSLNK 131 131 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q00613}.
CROSSLNK 208 208 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q00613}.
CROSSLNK 224 224 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q00613}.
CROSSLNK 298 298 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
{ECO:0000250|UniProtKB:Q00613}.
CROSSLNK 298 298 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q00613}.
SEQUENCE 525 AA; 56702 MW; 985CF9E968B0040B CRC64;
MDLPVGPGAA GPSNVPAFLT KLWTLVSDPD TDALICWSPS GNSFHVLDQG QFAKEVLPKY
FKHSNMASFV RQLNMYGFRK VVHIEQGGLV KPERDDTEFQ HPCFLRGQEQ LLENIKRKVT
SVSTLRSEDI KIRQDSVTKL LTDVQLMKGK QESMDSKLLA MKHENEALWR EVASLRQKHA
QQQKVVNKLI QFLISLVQSN RILGVKRKIP LMLNDGGPAH PMPKYGRQYS LEHIHGPGPY
PAPSPAYSGS SLYSPDAVTS SGPIISDITE LAPGSPVASS GGSVDERPLS SSPLVRVKEE
PPSPPQSPRA EGASPGRPSS MVETPLSPTT LIDSILRESE PTPVASTTPL VDTGGRPPSP
LPASAPEKCL SVACLDKTEL SDHLDAMDSN LDNLQTMLTS HGFSVDTSTL LDLFSPSVTV
PDMSLPDLDS SLASIQELLS PQEPPRPLEA EKSSPDSGKQ LVHYTAQPLL LLDPGSVDVG
SSDLPVLFEL GEGSYFSEGD DYSDDPTISL LTGSEPPKAK DPTVS


Related products :

Catalog number Product name Quantity
U0435h CLIA Heat shock factor protein 1,Heat shock transcription factor 1,Homo sapiens,HSF 1,HSF1,HSTF 1,HSTF1,Human 96T
E0435h ELISA Heat shock factor protein 1,Heat shock transcription factor 1,Homo sapiens,HSF 1,HSF1,HSTF 1,HSTF1,Human 96T
E0435h ELISA kit Heat shock factor protein 1,Heat shock transcription factor 1,Homo sapiens,HSF 1,HSF1,HSTF 1,HSTF1,Human 96T
E0435m ELISA Heat shock factor protein 1,Heat shock transcription factor 1,HSF 1,Hsf1,HSTF 1,Mouse,Mus musculus 96T
E0435m ELISA kit Heat shock factor protein 1,Heat shock transcription factor 1,HSF 1,Hsf1,HSTF 1,Mouse,Mus musculus 96T
U0435m CLIA Heat shock factor protein 1,Heat shock transcription factor 1,HSF 1,Hsf1,HSTF 1,Mouse,Mus musculus 96T
E0435b ELISA Bos taurus,Bovine,Heat shock factor protein 1,Heat shock transcription factor 1,HSF 1,HSF1,HSTF 1 96T
U0435b CLIA Bos taurus,Bovine,Heat shock factor protein 1,Heat shock transcription factor 1,HSF 1,HSF1,HSTF 1 96T
E0435b ELISA kit Bos taurus,Bovine,Heat shock factor protein 1,Heat shock transcription factor 1,HSF 1,HSF1,HSTF 1 96T
E0435c ELISA kit Chicken,Gallus gallus,Heat shock factor protein 1,Heat shock transcription factor 1,HSF 1,HSF 3A,HSF1,HSTF 1,HSTF 3A 96T
U0435c CLIA Chicken,Gallus gallus,Heat shock factor protein 1,Heat shock transcription factor 1,HSF 1,HSF 3A,HSF1,HSTF 1,HSTF 3A 96T
E0435c ELISA Chicken,Gallus gallus,Heat shock factor protein 1,Heat shock transcription factor 1,HSF 1,HSF 3A,HSF1,HSTF 1,HSTF 3A 96T
18-003-43825 Heat shock factor protein 4 - HSF 4; Heat shock transcription factor 4; HSTF 4; hHSF4 Polyclonal 0.1 mg Protein A
18-003-43943 Heat shock factor protein 1 - HSF 1; Heat shock transcription factor 1; HSTF 1 Polyclonal 0.1 mg Protein A
18-003-43942 Heat shock factor protein 1 - HSF 1; Heat shock transcription factor 1; HSTF 1 Polyclonal 0.05 mg Aff Pur
18-003-43304 Heat shock factor protein 1 - HSF 1; Heat shock transcription factor 1; HSTF 1 Polyclonal 0.05 mg Aff Pur
20-372-60242 heat shock transcription factor 2. mRNA (cDNA clone IMAGE 3684733). complete cds - Mouse monoclonal anti-human HSF2 antibody; HSF 2; Heat shock transcription factor 2; HSTF 2 Monoclonal 0.1 mg
20-372-60110 heat shock transcription factor 1 (HSF1). mRNA - Mouse monoclonal anti-human HSF1 antibody; HSF 1; Heat shock transcription factor 1; HSTF 1 Monoclonal 0.1 mg
18-785-210203 HSF1 (Ab-307) - HSF 1; Heat shock transcription factor 1; HSTF 1 Polyclonal 0.1 mg
18-785-210204 HSF1 (Ab-303) - HSF 1; Heat shock transcription factor 1; HSTF 1 Polyclonal 0.05 mg
18-785-210204 HSF1 (Ab-303) - HSF 1; Heat shock transcription factor 1; HSTF 1 Polyclonal 0.1 mg
18-785-210203 HSF1 (Ab-307) - HSF 1; Heat shock transcription factor 1; HSTF 1 Polyclonal 0.05 mg
27-259 HSF2 binds specifically to the heat-shock element and has homology to HSFs of other species. Heat shock transcription factors activate heat-shock response genes under conditions of heat or other stres 0.05 mg
31-175 HSF1 is a heat-shock transcription factor. Transcription of heat-shock genes is rapidly induced after temperature stress. Hsp90, by itself and_or associated with multichaperone complexes, is a major r 0.05 mg
18-785-210202 HSF1 (phospho-Ser303) - HSF 1; Heat shock transcription factor 1; HSTF 1 Polyclonal 0.05 mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur