HUMAN:HSF1

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	HSF1 (synonyms: HSTF1)
Protein Name(s)	Heat shock factor protein 1 HSF 1 Heat shock transcription factor 1 HSTF 1
External Links
UniProt	Q00613
EMBL	M64673 AK290975 BT007351 AC110280 AF205589 BC014638
CCDS	CCDS6419.1
PIR	A41137
RefSeq	NP_005517.1
UniGene	Hs.530227
PDB	2LDU
PDBsum	2LDU
ProteinModelPortal	Q00613
SMR	Q00613
BioGrid	109530
DIP	DIP-35670N
IntAct	Q00613
MINT	MINT-230849
STRING	9606.ENSP00000332698
BindingDB	Q00613
ChEMBL	CHEMBL5869
PhosphoSite	Q00613
DMDM	462333
MaxQB	Q00613
PaxDb	Q00613
PRIDE	Q00613
DNASU	3297
Ensembl	ENST00000528838
GeneID	3297
KEGG	hsa:3297
UCSC	uc003zbt.4
CTD	3297
GeneCards	GC08P145515
HGNC	HGNC:5224
HPA	CAB004239 HPA008888
MIM	140580
neXtProt	NX_Q00613
PharmGKB	PA29493
eggNOG	COG5169
GeneTree	ENSGT00390000001182
HOGENOM	HOG000253917
HOVERGEN	HBG005999
InParanoid	Q00613
KO	K09414
OMA	LFLVDPG
PhylomeDB	Q00613
TreeFam	TF330401
Reactome	REACT_200624 REACT_200744 REACT_200775 REACT_200780
SignaLink	Q00613
ChiTaRS	HSF1
GeneWiki	HSF1
GenomeRNAi	3297
NextBio	13075
PRO	PR:Q00613
Proteomes	UP000005640
Bgee	Q00613
CleanEx	HS_HSF1
ExpressionAtlas	Q00613
Genevestigator	Q00613
GO	GO:0005737 GO:0005634 GO:0045120 GO:0043234 GO:0003682 GO:0000978 GO:0001078 GO:0001162 GO:0003700 GO:0034605 GO:0006952 GO:0001892 GO:0060136 GO:0007143 GO:0008285 GO:0000122 GO:0032720 GO:0040018 GO:0045944 GO:0006468 GO:0090231 GO:0032496 GO:0007283
Gene3D	1.10.10.10
InterPro	IPR027072 IPR000232 IPR027725 IPR010542 IPR011991
PANTHER	PTHR10015 PTHR10015:SF142
Pfam	PF00447 PF06546
PRINTS	PR00056
SMART	SM00415
PROSITE	PS00434

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
enables	GO:0000981	DNA-binding transcription factor activity, RNA polymerase II-specific	PMID:19274049^[1]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0000981	DNA-binding transcription factor activity, RNA polymerase II-specific	PMID:19274049^[1]	ECO:0000255	match to sequence model evidence used in manual assertion	InterPro:IPR000232	F		Seeded From UniProt	complete
enables	GO:0000981	DNA-binding transcription factor activity, RNA polymerase II-specific	GO_REF:0000113	ECO:0005556	multiple sequence alignment evidence used in manual assertion	UniProtKB:A0A096MK39 UniProtKB:F1MAF1	F		Seeded From UniProt	complete
involved_in	GO:0120162	positive regulation of cold-induced thermogenesis	PMID:26344102^[2]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P38532	P		Seeded From UniProt	complete
involved_in	GO:0034605	cellular response to heat	PMID:12917326^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:12917326^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000165	MAPK cascade	PMID:12917326^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:12917326^[3]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:12917326^[3]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:12917326^[3]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:10747973^[4]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0034605	cellular response to heat	PMID:10747973^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:10747973^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:10747973^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0097165	nuclear stress granule	PMID:10747973^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0061408	positive regulation of transcription from RNA polymerase II promoter in response to heat stress	PMID:10747973^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:11583998^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:11583998^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0034605	cellular response to heat	PMID:11583998^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1900034	regulation of cellular response to heat	PMID:11583998^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0031072	heat shock protein binding	PMID:11583998^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0051879	Hsp90 protein binding	PMID:11583998^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0034622	cellular protein-containing complex assembly	PMID:11583998^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0061408	positive regulation of transcription from RNA polymerase II promoter in response to heat stress	PMID:26754925^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:26754925^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:26754925^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0008284	positive regulation of cell population proliferation	PMID:26754925^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:16278218^[7]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:16278218^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0031072	heat shock protein binding	PMID:16278218^[7]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0019901	protein kinase binding	PMID:16278218^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P49137	F		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:12659875^[8]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0061408	positive regulation of transcription from RNA polymerase II promoter in response to heat stress	PMID:12659875^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:11514557^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:11514557^[9]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0071276	cellular response to cadmium ion	PMID:11514557^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0016605	PML body	PMID:11514557^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0097165	nuclear stress granule	PMID:11514557^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0034605	cellular response to heat	PMID:11514557^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:8455624^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:8455624^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0070207	protein homotrimerization	PMID:8455624^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034605	cellular response to heat	PMID:8455624^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:8455624^[10]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0051260	protein homooligomerization	PMID:8455624^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0061770	translation elongation factor binding	PMID:16554823^[11]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:16554823^[11]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:16554823^[11]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0034605	cellular response to heat	PMID:16554823^[11]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:1990904	ribonucleoprotein complex	PMID:16554823^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:10413683^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:10413683^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:10413683^[12]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0034605	cellular response to heat	PMID:10413683^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0061408	positive regulation of transcription from RNA polymerase II promoter in response to heat stress	PMID:12665592^[13]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:12665592^[13]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:12665592^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0097165	nuclear stress granule	PMID:12665592^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:9222587^[14]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0034605	cellular response to heat	PMID:9222587^[14]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:9222587^[14]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:9222587^[14]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:7935471^[15]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:7935471^[15]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0043621	protein self-association	PMID:7935471^[15]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0034605	cellular response to heat	PMID:7935471^[15]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0000776	kinetochore	PMID:18794143^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005813	centrosome	PMID:18794143^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0097431	mitotic spindle pole	PMID:18794143^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0045931	positive regulation of mitotic cell cycle	PMID:18794143^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0031490	chromatin DNA binding	PMID:21085490^[17]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	PMID:21085490^[17]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21085490^[17]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:21085490^[17]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21085490^[17]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0034605	cellular response to heat	PMID:21085490^[17]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034605	cellular response to heat	PMID:14707147^[18]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:14707147^[18]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0097165	nuclear stress granule	PMID:14707147^[18]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1900365	positive regulation of mRNA polyadenylation	PMID:14707147^[18]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:9341107^[19]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000122	negative regulation of transcription by RNA polymerase II	PMID:9341107^[19]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:9341107^[19]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0034605	cellular response to heat	PMID:9341107^[19]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:9341107^[19]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:10359787^[20]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0071276	cellular response to cadmium ion	PMID:10359787^[20]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034605	cellular response to heat	PMID:10359787^[20]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0097165	nuclear stress granule	PMID:10359787^[20]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	PMID:10359787^[20]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0031072	heat shock protein binding	PMID:9727490^[21]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:9727490^[21]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:9727490^[21]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0034605	cellular response to heat	PMID:9727490^[21]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0072738	cellular response to diamide	PMID:15016915^[22]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1903936	cellular response to sodium arsenite	PMID:15016915^[22]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071280	cellular response to copper ion	PMID:15016915^[22]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071276	cellular response to cadmium ion	PMID:15016915^[22]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0061408	positive regulation of transcription from RNA polymerase II promoter in response to heat stress	PMID:15016915^[22]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034620	cellular response to unfolded protein	PMID:15016915^[22]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:25963659^[23]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0071276	cellular response to cadmium ion	PMID:25963659^[23]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0061408	positive regulation of transcription from RNA polymerase II promoter in response to heat stress	PMID:25963659^[23]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0097165	nuclear stress granule	PMID:25963659^[23]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:1990841	promoter-specific chromatin binding	PMID:25963659^[23]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0043565	sequence-specific DNA binding	PMID:25963659^[23]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:26159920^[24]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:26159920^[24]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0034605	cellular response to heat	PMID:26159920^[24]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0009299	mRNA transcription	PMID:21597468^[25]	ECO:0000314	direct assay evidence used in manual assertion		P	has_input:(UniProtKB:P02511)\|has_input:(UniProtKB:P17066)	Seeded From UniProt	complete
involved_in	GO:0061408	positive regulation of transcription from RNA polymerase II promoter in response to heat stress	PMID:9499401^[26]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:9499401^[26]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0061408	positive regulation of transcription from RNA polymerase II promoter in response to heat stress	PMID:7760831^[27]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:7760831^[27]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0071480	cellular response to gamma radiation	PMID:26359349^[28]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:2001033	negative regulation of double-strand break repair via nonhomologous end joining	PMID:26359349^[28]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043497	regulation of protein heterodimerization activity	PMID:26359349^[28]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:26359349^[28]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0001227	DNA-binding transcription repressor activity, RNA polymerase II-specific	PMID:8926278^[29]	ECO:0000314	direct assay evidence used in manual assertion		F	occurs_at:(SO:0001952)	Seeded From UniProt	complete
enables	GO:0000978	RNA polymerase II proximal promoter sequence-specific DNA binding	PMID:8926278^[29]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0000122	negative regulation of transcription by RNA polymerase II	PMID:8926278^[29]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(NCBI_Gene:3553)	Seeded From UniProt	complete
involved_in	GO:0034605	cellular response to heat	PMID:17897941^[30]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0061408	positive regulation of transcription from RNA polymerase II promoter in response to heat stress	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000001154 UniProtKB:Q00613	P		Seeded From UniProt	complete
enables	GO:0043565	sequence-specific DNA binding	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0001222 MGI:MGI:1347058 MGI:MGI:3045337 MGI:MGI:96238 MGI:MGI:96239 PANTHER:PTN000001154 RGD:1310808 SGD:S000005666 UniProtKB:P38529 UniProtKB:P38531 UniProtKB:Q00613 ZFIN:ZDB-GENE-000616-16 ZFIN:ZDB-GENE-011128-1 ZFIN:ZDB-GENE-050306-18	F		Seeded From UniProt	complete
involved_in	GO:0034605	cellular response to heat	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:3045337 PANTHER:PTN000001154 RGD:620913 UniProtKB:O80982 UniProtKB:P38529 UniProtKB:P38531 UniProtKB:Q00613	P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	CGD:CAL0000195882 FB:FBgn0001222 MGI:MGI:3045337 MGI:MGI:96238 MGI:MGI:96239 PANTHER:PTN000001154 PomBase:SPAC2E12.02 PomBase:SPAC8C9.14 RGD:1310808 RGD:620913 SGD:S000001249 SGD:S000003041 SGD:S000005666 TAIR:locus:2005495 TAIR:locus:2075447 TAIR:locus:2117139 TAIR:locus:2144603 TAIR:locus:2149050 UniProtKB:I1LGH5 UniProtKB:I1MPZ9 UniProtKB:K7LH36 UniProtKB:O80982 UniProtKB:P38529 UniProtKB:P38530 UniProtKB:P38531 UniProtKB:Q00613 UniProtKB:Q43457 UniProtKB:Q5A287 UniProtKB:Q942D6 UniProtKB:Q9UBD0 WB:WBGene00002004	C		Seeded From UniProt	complete
enables	GO:0003700	DNA-binding transcription factor activity	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	CGD:CAL0000195882 FB:FBgn0001222 PANTHER:PTN000001154 SGD:S000001249 SGD:S000003041 TAIR:locus:2149050	F		Seeded From UniProt	complete
enables	GO:0000978	RNA polymerase II proximal promoter sequence-specific DNA binding	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:96238 MGI:MGI:96239 PANTHER:PTN000001154 PomBase:SPAC2E12.02 PomBase:SPAC8C9.14 SGD:S000005666 UniProtKB:Q00613	F		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:10561509^[32]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0001162	RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding	PMID:10561509^[32]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:29997244^[33]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q00613	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:26727490^[34]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q00613	F		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1990911	response to psychosocial stress	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	P		Seeded From UniProt	complete
involved_in	GO:1990910	response to hypobaric hypoxia	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	P		Seeded From UniProt	complete
enables	GO:1990841	promoter-specific chromatin binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	F		Seeded From UniProt	complete
involved_in	GO:1904845	cellular response to L-glutamine	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	P		Seeded From UniProt	complete
involved_in	GO:1904843	cellular response to nitroglycerin	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	P		Seeded From UniProt	complete
involved_in	GO:1904528	positive regulation of microtubule binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	P		Seeded From UniProt	complete
involved_in	GO:1904385	cellular response to angiotensin	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	P		Seeded From UniProt	complete
involved_in	GO:1902512	positive regulation of apoptotic DNA fragmentation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	P		Seeded From UniProt	complete
involved_in	GO:1901652	response to peptide	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	P		Seeded From UniProt	complete
involved_in	GO:1901215	negative regulation of neuron death	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	P		Seeded From UniProt	complete
enables	GO:0098847	sequence-specific single stranded DNA binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	F		Seeded From UniProt	complete
enables	GO:0097677	STAT family protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	F		Seeded From UniProt	complete
involved_in	GO:0090261	positive regulation of inclusion body assembly	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	P		Seeded From UniProt	complete
involved_in	GO:0090084	negative regulation of inclusion body assembly	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	P		Seeded From UniProt	complete
involved_in	GO:0071478	cellular response to radiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	P		Seeded From UniProt	complete
involved_in	GO:0071407	cellular response to organic cyclic compound	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	P		Seeded From UniProt	complete
involved_in	GO:0071392	cellular response to estradiol stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	P		Seeded From UniProt	complete
involved_in	GO:0071230	cellular response to amino acid stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	P		Seeded From UniProt	complete
involved_in	GO:0071222	cellular response to lipopolysaccharide	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	P		Seeded From UniProt	complete
involved_in	GO:0070301	cellular response to hydrogen peroxide	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	P		Seeded From UniProt	complete
involved_in	GO:0043280	positive regulation of cysteine-type endopeptidase activity involved in apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	P		Seeded From UniProt	complete
involved_in	GO:0043200	response to amino acid	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	P		Seeded From UniProt	complete
involved_in	GO:0042531	positive regulation of tyrosine phosphorylation of STAT protein	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	P		Seeded From UniProt	complete
involved_in	GO:0035865	cellular response to potassium ion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	P		Seeded From UniProt	complete
involved_in	GO:0035690	cellular response to drug	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	P		Seeded From UniProt	complete
involved_in	GO:0034605	cellular response to heat	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	P		Seeded From UniProt	complete
involved_in	GO:0033574	response to testosterone	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	P		Seeded From UniProt	complete
involved_in	GO:0032355	response to estradiol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	P		Seeded From UniProt	complete
enables	GO:0031072	heat shock protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	F		Seeded From UniProt	complete
involved_in	GO:0014823	response to activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	P		Seeded From UniProt	complete
involved_in	GO:0014070	response to organic cyclic compound	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	P		Seeded From UniProt	complete
involved_in	GO:0010667	negative regulation of cardiac muscle cell apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	P		Seeded From UniProt	complete
involved_in	GO:0010629	negative regulation of gene expression	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	P		Seeded From UniProt	complete
involved_in	GO:0010628	positive regulation of gene expression	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	P		Seeded From UniProt	complete
involved_in	GO:0010243	response to organonitrogen compound	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	P		Seeded From UniProt	complete
involved_in	GO:0009408	response to heat	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	P		Seeded From UniProt	complete
involved_in	GO:0007584	response to nutrient	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	P		Seeded From UniProt	complete
involved_in	GO:0006952	defense response	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	C		Seeded From UniProt	complete
part_of	GO:0000792	heterochromatin	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	C		Seeded From UniProt	complete
part_of	GO:0000791	euchromatin	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAF1 ensembl:ENSRNOP00000047030	C		Seeded From UniProt	complete
involved_in	GO:0120162	positive regulation of cold-induced thermogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P38532 ensembl:ENSMUSP00000072617	P		Seeded From UniProt	complete
involved_in	GO:0060136	embryonic process involved in female pregnancy	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P38532 ensembl:ENSMUSP00000072617	P		Seeded From UniProt	complete
part_of	GO:0045120	pronucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P38532 ensembl:ENSMUSP00000072617	C		Seeded From UniProt	complete
enables	GO:0043565	sequence-specific DNA binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P38532 ensembl:ENSMUSP00000072617	F		Seeded From UniProt	complete
involved_in	GO:0040018	positive regulation of multicellular organism growth	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P38532 ensembl:ENSMUSP00000072617	P		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P38532 ensembl:ENSMUSP00000072617	C		Seeded From UniProt	complete
involved_in	GO:0032720	negative regulation of tumor necrosis factor production	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P38532 ensembl:ENSMUSP00000072617	P		Seeded From UniProt	complete
involved_in	GO:0032496	response to lipopolysaccharide	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P38532 ensembl:ENSMUSP00000072617	P		Seeded From UniProt	complete
involved_in	GO:0009408	response to heat	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P38532 ensembl:ENSMUSP00000072617	P		Seeded From UniProt	complete
involved_in	GO:0008285	negative regulation of cell population proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P38532 ensembl:ENSMUSP00000072617	P		Seeded From UniProt	complete
involved_in	GO:0007283	spermatogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P38532 ensembl:ENSMUSP00000072617	P		Seeded From UniProt	complete
involved_in	GO:0007143	female meiotic nuclear division	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P38532 ensembl:ENSMUSP00000072617	P		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P38532 ensembl:ENSMUSP00000072617	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P38532 ensembl:ENSMUSP00000072617	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P38532 ensembl:ENSMUSP00000072617	C		Seeded From UniProt	complete
enables	GO:0003682	chromatin binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P38532 ensembl:ENSMUSP00000072617	F		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P38532 ensembl:ENSMUSP00000072617	F		Seeded From UniProt	complete
involved_in	GO:0001892	embryonic placenta development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P38532 ensembl:ENSMUSP00000072617	P		Seeded From UniProt	complete
involved_in	GO:0001701	in utero embryonic development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P38532 ensembl:ENSMUSP00000072617	P		Seeded From UniProt	complete
enables	GO:0000978	RNA polymerase II proximal promoter sequence-specific DNA binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P38532 ensembl:ENSMUSP00000072617	F		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR010542	F		Seeded From UniProt	complete
enables	GO:0003700	DNA-binding transcription factor activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000232 InterPro:IPR010542	F		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000232	C		Seeded From UniProt	complete
involved_in	GO:0006355	regulation of transcription, DNA-templated	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000232 InterPro:IPR010542	P		Seeded From UniProt	complete
enables	GO:0043565	sequence-specific DNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000232	F		Seeded From UniProt	complete
enables	GO:0003700	DNA-binding transcription factor activity	PMID:1871105^[35] PMID:10821850^[36]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:1900034	regulation of cellular response to heat	Reactome:R-HSA-3371571 Reactome:R-HSA-3371453	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-5324632 Reactome:R-HSA-4793925 Reactome:R-HSA-4793911 Reactome:R-HSA-3371591 Reactome:R-HSA-3371586 Reactome:R-HSA-3371531 Reactome:R-HSA-3371527 Reactome:R-HSA-3371435	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	Reactome:R-HSA-5333051 Reactome:R-HSA-5324617 Reactome:R-HSA-5082409 Reactome:R-HSA-5082405 Reactome:R-HSA-5082391 Reactome:R-HSA-5082387 Reactome:R-HSA-5082384 Reactome:R-HSA-5082369 Reactome:R-HSA-5082356 Reactome:R-HSA-4793819 Reactome:R-HSA-3371582 Reactome:R-HSA-3371554 Reactome:R-HSA-3371527 Reactome:R-HSA-3371518 Reactome:R-HSA-3371467	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005694	chromosome	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0158	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0227	P		Seeded From UniProt	complete
involved_in	GO:0051028	mRNA transport	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0509	P		Seeded From UniProt	complete
part_of	GO:0000775	chromosome, centromeric region	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0137	C		Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0234	P		Seeded From UniProt	complete
part_of	GO:0000776	kinetochore	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0995	C		Seeded From UniProt	complete
involved_in	GO:0006397	mRNA processing	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0507	P		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0238	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
part_of	GO:0005856	cytoskeleton	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0206	C		Seeded From UniProt	complete
part_of	GO:0000777	condensed chromosome kinetochore	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0149	C		Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0198	C		Seeded From UniProt	complete
part_of	GO:0005815	microtubule organizing center	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0048	C		Seeded From UniProt	complete
part_of	GO:0000922	spindle pole	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0448	C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0190	C		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Vaquerizas, JM et al. (2009) A census of human transcription factors: function, expression and evolution. Nat. Rev. Genet. 10 252-63 PubMed GONUTS page
↑ Ma, X et al. (2015) Celastrol Protects against Obesity and Metabolic Dysfunction through Activation of a HSF1-PGC1α Transcriptional Axis. Cell Metab. 22 695-708 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 Wang, X et al. (2003) Regulation of molecular chaperone gene transcription involves the serine phosphorylation, 14-3-3 epsilon binding, and cytoplasmic sequestration of heat shock factor 1. Mol. Cell. Biol. 23 6013-26 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 Dai, R et al. (2000) c-Jun NH2-terminal kinase targeting and phosphorylation of heat shock factor-1 suppress its transcriptional activity. J. Biol. Chem. 275 18210-8 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 ^5.6 Guo, Y et al. (2001) Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex. J. Biol. Chem. 276 45791-9 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 ^6.3 Asano, Y et al. (2016) IER5 generates a novel hypo-phosphorylated active form of HSF1 and contributes to tumorigenesis. Sci Rep 6 19174 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 Wang, X et al. (2006) Phosphorylation of HSF1 by MAPK-activated protein kinase 2 on serine 121, inhibits transcriptional activity and promotes HSP90 binding. J. Biol. Chem. 281 782-91 PubMed GONUTS page
↑ ^8.0 ^8.1 Soncin, F et al. (2003) Transcriptional activity and DNA binding of heat shock factor-1 involve phosphorylation on threonine 142 by CK2. Biochem. Biophys. Res. Commun. 303 700-6 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 ^9.3 ^9.4 ^9.5 Hong, Y et al. (2001) Regulation of heat shock transcription factor 1 by stress-induced SUMO-1 modification. J. Biol. Chem. 276 40263-7 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 ^10.4 ^10.5 Baler, R et al. (1993) Activation of human heat shock genes is accompanied by oligomerization, modification, and rapid translocation of heat shock transcription factor HSF1. Mol. Cell. Biol. 13 2486-96 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 ^11.3 ^11.4 Shamovsky, I et al. (2006) RNA-mediated response to heat shock in mammalian cells. Nature 440 556-60 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 ^12.3 Mercier, PA et al. (1999) Human heat shock factor 1 is predominantly a nuclear protein before and after heat stress. J. Cell. Sci. 112 ( Pt 16) 2765-74 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 ^13.3 Hietakangas, V et al. (2003) Phosphorylation of serine 303 is a prerequisite for the stress-inducible SUMO modification of heat shock factor 1. Mol. Cell. Biol. 23 2953-68 PubMed GONUTS page
↑ ^14.0 ^14.1 ^14.2 ^14.3 Baler, R et al. (1996) Evidence for a role of Hsp70 in the regulation of the heat shock response in mammalian cells. Cell Stress Chaperones 1 33-9 PubMed GONUTS page
↑ ^15.0 ^15.1 ^15.2 ^15.3 Zuo, J et al. (1994) Activation of the DNA-binding ability of human heat shock transcription factor 1 may involve the transition from an intramolecular to an intermolecular triple-stranded coiled-coil structure. Mol. Cell. Biol. 14 7557-68 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 ^16.3 Lee, YJ et al. (2008) HSF1 as a mitotic regulator: phosphorylation of HSF1 by Plk1 is essential for mitotic progression. Cancer Res. 68 7550-60 PubMed GONUTS page
↑ ^17.0 ^17.1 ^17.2 ^17.3 ^17.4 ^17.5 Murshid, A et al. (2010) Protein kinase A binds and activates heat shock factor 1. PLoS ONE 5 e13830 PubMed GONUTS page
↑ ^18.0 ^18.1 ^18.2 ^18.3 Xing, H et al. (2004) HSF1 modulation of Hsp70 mRNA polyadenylation via interaction with symplekin. J. Biol. Chem. 279 10551-5 PubMed GONUTS page
↑ ^19.0 ^19.1 ^19.2 ^19.3 ^19.4 Chen, C et al. (1997) Heat shock factor 1 represses Ras-induced transcriptional activation of the c-fos gene. J. Biol. Chem. 272 26803-6 PubMed GONUTS page
↑ ^20.0 ^20.1 ^20.2 ^20.3 ^20.4 Jolly, C et al. (1999) Rapid and reversible relocalization of heat shock factor 1 within seconds to nuclear stress granules. Proc. Natl. Acad. Sci. U.S.A. 96 6769-74 PubMed GONUTS page
↑ ^21.0 ^21.1 ^21.2 ^21.3 Zou, J et al. (1998) Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. Cell 94 471-80 PubMed GONUTS page
↑ ^22.0 ^22.1 ^22.2 ^22.3 ^22.4 ^22.5 Boellmann, F et al. (2004) DAXX interacts with heat shock factor 1 during stress activation and enhances its transcriptional activity. Proc. Natl. Acad. Sci. U.S.A. 101 4100-5 PubMed GONUTS page
↑ ^23.0 ^23.1 ^23.2 ^23.3 ^23.4 ^23.5 Budzyński, MA et al. (2015) Uncoupling Stress-Inducible Phosphorylation of Heat Shock Factor 1 from Its Activation. Mol. Cell. Biol. 35 2530-40 PubMed GONUTS page
↑ ^24.0 ^24.1 ^24.2 Jin, YH et al. (2015) BAG3 affects the nucleocytoplasmic shuttling of HSF1 upon heat stress. Biochem. Biophys. Res. Commun. 464 561-7 PubMed GONUTS page
↑ Kaitsuka, T et al. (2011) Transformation of eEF1Bδ into heat-shock response transcription factor by alternative splicing. EMBO Rep. 12 673-81 PubMed GONUTS page
↑ ^26.0 ^26.1 Shi, Y et al. (1998) Molecular chaperones as HSF1-specific transcriptional repressors. Genes Dev. 12 654-66 PubMed GONUTS page
↑ ^27.0 ^27.1 Green, M et al. (1995) A heat shock-responsive domain of human HSF1 that regulates transcription activation domain function. Mol. Cell. Biol. 15 3354-62 PubMed GONUTS page
↑ ^28.0 ^28.1 ^28.2 ^28.3 Kang, GY et al. (2015) Heat shock factor 1, an inhibitor of non-homologous end joining repair. Oncotarget 6 29712-24 PubMed GONUTS page
↑ ^29.0 ^29.1 ^29.2 Cahill, CM et al. (1996) Transcriptional repression of the prointerleukin 1beta gene by heat shock factor 1. J. Biol. Chem. 271 24874-9 PubMed GONUTS page
↑ Skaggs, HS et al. (2007) HSF1-TPR interaction facilitates export of stress-induced HSP70 mRNA. J. Biol. Chem. 282 33902-7 PubMed GONUTS page
↑ ^31.0 ^31.1 ^31.2 ^31.3 ^31.4 ^31.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^32.0 ^32.1 Kubota, H et al. (1999) Transcriptional activation of mouse cytosolic chaperonin CCT subunit genes by heat shock factors HSF1 and HSF2. FEBS Lett. 461 125-9 PubMed GONUTS page
↑ Trepte, P et al. (2018) LuTHy: a double-readout bioluminescence-based two-hybrid technology for quantitative mapping of protein-protein interactions in mammalian cells. Mol. Syst. Biol. 14 e8071 PubMed GONUTS page
↑ Jaeger, AM et al. (2016) Structures of HSF2 reveal mechanisms for differential regulation of human heat-shock factors. Nat. Struct. Mol. Biol. 23 147-54 PubMed GONUTS page
↑ Rabindran, SK et al. (1991) Molecular cloning and expression of a human heat shock factor, HSF1. Proc. Natl. Acad. Sci. U.S.A. 88 6906-10 PubMed GONUTS page
↑ Choi, Y et al. (2000) Divergent hTAFII31-binding motifs hidden in activation domains. J. Biol. Chem. 275 15912-6 PubMed GONUTS page

[PMID:19274049-1] 1.0 ^1.1 Vaquerizas, JM et al. (2009) A census of human transcription factors: function, expression and evolution. Nat. Rev. Genet. 10 252-63 PubMed GONUTS page

[PMID:26344102-2] Ma, X et al. (2015) Celastrol Protects against Obesity and Metabolic Dysfunction through Activation of a HSF1-PGC1α Transcriptional Axis. Cell Metab. 22 695-708 PubMed GONUTS page

[PMID:12917326-3] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 Wang, X et al. (2003) Regulation of molecular chaperone gene transcription involves the serine phosphorylation, 14-3-3 epsilon binding, and cytoplasmic sequestration of heat shock factor 1. Mol. Cell. Biol. 23 6013-26 PubMed GONUTS page

[PMID:10747973-4] 4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 Dai, R et al. (2000) c-Jun NH2-terminal kinase targeting and phosphorylation of heat shock factor-1 suppress its transcriptional activity. J. Biol. Chem. 275 18210-8 PubMed GONUTS page

[PMID:11583998-5] 5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 ^5.6 Guo, Y et al. (2001) Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex. J. Biol. Chem. 276 45791-9 PubMed GONUTS page

[PMID:26754925-6] 6.0 ^6.1 ^6.2 ^6.3 Asano, Y et al. (2016) IER5 generates a novel hypo-phosphorylated active form of HSF1 and contributes to tumorigenesis. Sci Rep 6 19174 PubMed GONUTS page

[PMID:16278218-7] 7.0 ^7.1 ^7.2 ^7.3 Wang, X et al. (2006) Phosphorylation of HSF1 by MAPK-activated protein kinase 2 on serine 121, inhibits transcriptional activity and promotes HSP90 binding. J. Biol. Chem. 281 782-91 PubMed GONUTS page

[PMID:12659875-8] 8.0 ^8.1 Soncin, F et al. (2003) Transcriptional activity and DNA binding of heat shock factor-1 involve phosphorylation on threonine 142 by CK2. Biochem. Biophys. Res. Commun. 303 700-6 PubMed GONUTS page

[PMID:11514557-9] 9.0 ^9.1 ^9.2 ^9.3 ^9.4 ^9.5 Hong, Y et al. (2001) Regulation of heat shock transcription factor 1 by stress-induced SUMO-1 modification. J. Biol. Chem. 276 40263-7 PubMed GONUTS page

[PMID:8455624-10] 10.0 ^10.1 ^10.2 ^10.3 ^10.4 ^10.5 Baler, R et al. (1993) Activation of human heat shock genes is accompanied by oligomerization, modification, and rapid translocation of heat shock transcription factor HSF1. Mol. Cell. Biol. 13 2486-96 PubMed GONUTS page

[PMID:16554823-11] 11.0 ^11.1 ^11.2 ^11.3 ^11.4 Shamovsky, I et al. (2006) RNA-mediated response to heat shock in mammalian cells. Nature 440 556-60 PubMed GONUTS page

[PMID:10413683-12] 12.0 ^12.1 ^12.2 ^12.3 Mercier, PA et al. (1999) Human heat shock factor 1 is predominantly a nuclear protein before and after heat stress. J. Cell. Sci. 112 ( Pt 16) 2765-74 PubMed GONUTS page

[PMID:12665592-13] 13.0 ^13.1 ^13.2 ^13.3 Hietakangas, V et al. (2003) Phosphorylation of serine 303 is a prerequisite for the stress-inducible SUMO modification of heat shock factor 1. Mol. Cell. Biol. 23 2953-68 PubMed GONUTS page

[PMID:9222587-14] 14.0 ^14.1 ^14.2 ^14.3 Baler, R et al. (1996) Evidence for a role of Hsp70 in the regulation of the heat shock response in mammalian cells. Cell Stress Chaperones 1 33-9 PubMed GONUTS page

[PMID:7935471-15] 15.0 ^15.1 ^15.2 ^15.3 Zuo, J et al. (1994) Activation of the DNA-binding ability of human heat shock transcription factor 1 may involve the transition from an intramolecular to an intermolecular triple-stranded coiled-coil structure. Mol. Cell. Biol. 14 7557-68 PubMed GONUTS page

[PMID:18794143-16] 16.0 ^16.1 ^16.2 ^16.3 Lee, YJ et al. (2008) HSF1 as a mitotic regulator: phosphorylation of HSF1 by Plk1 is essential for mitotic progression. Cancer Res. 68 7550-60 PubMed GONUTS page

[PMID:21085490-17] 17.0 ^17.1 ^17.2 ^17.3 ^17.4 ^17.5 Murshid, A et al. (2010) Protein kinase A binds and activates heat shock factor 1. PLoS ONE 5 e13830 PubMed GONUTS page

[PMID:14707147-18] 18.0 ^18.1 ^18.2 ^18.3 Xing, H et al. (2004) HSF1 modulation of Hsp70 mRNA polyadenylation via interaction with symplekin. J. Biol. Chem. 279 10551-5 PubMed GONUTS page

[PMID:9341107-19] 19.0 ^19.1 ^19.2 ^19.3 ^19.4 Chen, C et al. (1997) Heat shock factor 1 represses Ras-induced transcriptional activation of the c-fos gene. J. Biol. Chem. 272 26803-6 PubMed GONUTS page

[PMID:10359787-20] 20.0 ^20.1 ^20.2 ^20.3 ^20.4 Jolly, C et al. (1999) Rapid and reversible relocalization of heat shock factor 1 within seconds to nuclear stress granules. Proc. Natl. Acad. Sci. U.S.A. 96 6769-74 PubMed GONUTS page

[PMID:9727490-21] 21.0 ^21.1 ^21.2 ^21.3 Zou, J et al. (1998) Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. Cell 94 471-80 PubMed GONUTS page

[PMID:15016915-22] 22.0 ^22.1 ^22.2 ^22.3 ^22.4 ^22.5 Boellmann, F et al. (2004) DAXX interacts with heat shock factor 1 during stress activation and enhances its transcriptional activity. Proc. Natl. Acad. Sci. U.S.A. 101 4100-5 PubMed GONUTS page

[PMID:25963659-23] 23.0 ^23.1 ^23.2 ^23.3 ^23.4 ^23.5 Budzyński, MA et al. (2015) Uncoupling Stress-Inducible Phosphorylation of Heat Shock Factor 1 from Its Activation. Mol. Cell. Biol. 35 2530-40 PubMed GONUTS page

[PMID:26159920-24] 24.0 ^24.1 ^24.2 Jin, YH et al. (2015) BAG3 affects the nucleocytoplasmic shuttling of HSF1 upon heat stress. Biochem. Biophys. Res. Commun. 464 561-7 PubMed GONUTS page

[PMID:21597468-25] Kaitsuka, T et al. (2011) Transformation of eEF1Bδ into heat-shock response transcription factor by alternative splicing. EMBO Rep. 12 673-81 PubMed GONUTS page

[PMID:9499401-26] 26.0 ^26.1 Shi, Y et al. (1998) Molecular chaperones as HSF1-specific transcriptional repressors. Genes Dev. 12 654-66 PubMed GONUTS page

[PMID:7760831-27] 27.0 ^27.1 Green, M et al. (1995) A heat shock-responsive domain of human HSF1 that regulates transcription activation domain function. Mol. Cell. Biol. 15 3354-62 PubMed GONUTS page

[PMID:26359349-28] 28.0 ^28.1 ^28.2 ^28.3 Kang, GY et al. (2015) Heat shock factor 1, an inhibitor of non-homologous end joining repair. Oncotarget 6 29712-24 PubMed GONUTS page

[PMID:8926278-29] 29.0 ^29.1 ^29.2 Cahill, CM et al. (1996) Transcriptional repression of the prointerleukin 1beta gene by heat shock factor 1. J. Biol. Chem. 271 24874-9 PubMed GONUTS page

[PMID:17897941-30] Skaggs, HS et al. (2007) HSF1-TPR interaction facilitates export of stress-induced HSP70 mRNA. J. Biol. Chem. 282 33902-7 PubMed GONUTS page

[PMID:21873635-31] 31.0 ^31.1 ^31.2 ^31.3 ^31.4 ^31.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:10561509-32] 32.0 ^32.1 Kubota, H et al. (1999) Transcriptional activation of mouse cytosolic chaperonin CCT subunit genes by heat shock factors HSF1 and HSF2. FEBS Lett. 461 125-9 PubMed GONUTS page

[PMID:29997244-33] Trepte, P et al. (2018) LuTHy: a double-readout bioluminescence-based two-hybrid technology for quantitative mapping of protein-protein interactions in mammalian cells. Mol. Syst. Biol. 14 e8071 PubMed GONUTS page

[PMID:26727490-34] Jaeger, AM et al. (2016) Structures of HSF2 reveal mechanisms for differential regulation of human heat-shock factors. Nat. Struct. Mol. Biol. 23 147-54 PubMed GONUTS page

[PMID:1871105-35] Rabindran, SK et al. (1991) Molecular cloning and expression of a human heat shock factor, HSF1. Proc. Natl. Acad. Sci. U.S.A. 88 6906-10 PubMed GONUTS page

[PMID:10821850-36] Choi, Y et al. (2000) Divergent hTAFII31-binding motifs hidden in activation domains. J. Biol. Chem. 275 15912-6 PubMed GONUTS page

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