HSFX1_HUMAN
ID HSFX1_HUMAN Reviewed; 423 AA.
AC Q9UBD0;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Heat shock transcription factor, X-linked;
GN Name=HSFX1; Synonyms=LW-1;
GN and
GN Name=HSFX2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Testis;
RA Wang L., Thibodeau S.N.;
RT "Expression of a testis-specific gene LW-1 in cancers.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=15044259; DOI=10.1095/biolreprod.103.023580;
RA Shinka T., Sato Y., Chen G., Naroda T., Kinoshita K., Unemi Y., Tsuji K.,
RA Toida K., Iwamoto T., Nakahori Y.;
RT "Molecular characterization of heat shock-like factor encoded on the human
RT Y chromosome, and implications for male infertility.";
RL Biol. Reprod. 71:297-306(2004).
RN [5]
RP SUMOYLATION AT LYS-215.
RC TISSUE=Cervix carcinoma;
RX PubMed=20388717; DOI=10.1074/jbc.m110.106955;
RA Blomster H.A., Imanishi S.Y., Siimes J., Kastu J., Morrice N.A.,
RA Eriksson J.E., Sistonen L.;
RT "In vivo identification of sumoylation sites by a signature tag and
RT cysteine-targeted affinity purification.";
RL J. Biol. Chem. 285:19324-19329(2010).
CC -!- INTERACTION:
CC Q9UBD0; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-947253, EBI-11522760;
CC Q9UBD0; P54253: ATXN1; NbExp=6; IntAct=EBI-947253, EBI-930964;
CC Q9UBD0; Q9UGQ2: CACFD1; NbExp=3; IntAct=EBI-947253, EBI-8652492;
CC Q9UBD0; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-947253, EBI-10176379;
CC Q9UBD0; Q969L2: MAL2; NbExp=3; IntAct=EBI-947253, EBI-944295;
CC Q9UBD0; Q5XKP0: MICOS13; NbExp=3; IntAct=EBI-947253, EBI-1053887;
CC Q9UBD0; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-947253, EBI-3923617;
CC Q9UBD0; Q8N3Y7: SDR16C5; NbExp=3; IntAct=EBI-947253, EBI-3923480;
CC Q9UBD0; P08247: SYP; NbExp=3; IntAct=EBI-947253, EBI-9071725;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cytoplasm
CC {ECO:0000269|PubMed:15044259}.
CC -!- TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:15044259}.
CC -!- SIMILARITY: Belongs to the HSF family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF139980; AAD45879.1; -; mRNA.
DR EMBL; AF139982; AAD45880.1; -; Genomic_DNA.
DR EMBL; AF139981; AAD45880.1; JOINED; Genomic_DNA.
DR EMBL; CH471169; EAW99371.1; -; Genomic_DNA.
DR EMBL; BC021706; AAH21706.1; -; mRNA.
DR CCDS; CCDS44011.1; -.
DR CCDS; CCDS48179.1; -.
DR RefSeq; NP_001157887.1; NM_001164415.2.
DR RefSeq; NP_057237.1; NM_016153.2.
DR AlphaFoldDB; Q9UBD0; -.
DR SMR; Q9UBD0; -.
DR BioGRID; 325062; 23.
DR BioGRID; 576546; 9.
DR IntAct; Q9UBD0; 14.
DR STRING; 9606.ENSP00000359444; -.
DR iPTMnet; Q9UBD0; -.
DR PhosphoSitePlus; Q9UBD0; -.
DR BioMuta; HSFX1; -.
DR DMDM; 74761890; -.
DR MassIVE; Q9UBD0; -.
DR PaxDb; Q9UBD0; -.
DR PeptideAtlas; Q9UBD0; -.
DR PRIDE; Q9UBD0; -.
DR Antibodypedia; 56729; 160 antibodies from 20 providers.
DR Antibodypedia; 76028; 36 antibodies from 11 providers.
DR DNASU; 100130086; -.
DR Ensembl; ENST00000370416.4; ENSP00000359444.4; ENSG00000171116.7.
DR Ensembl; ENST00000598963.3; ENSP00000469223.1; ENSG00000268738.3.
DR GeneID; 100130086; -.
DR GeneID; 100506164; -.
DR KEGG; hsa:100130086; -.
DR KEGG; hsa:100506164; -.
DR MANE-Select; ENST00000370416.4; ENSP00000359444.4; NM_016153.3; NP_057237.1.
DR MANE-Select; ENST00000598963.3; ENSP00000469223.1; NM_001164415.3; NP_001157887.1.
DR UCSC; uc022cgk.2; human.
DR CTD; 100130086; -.
DR CTD; 100506164; -.
DR GeneCards; HSFX1; -.
DR GeneCards; HSFX2; -.
DR HGNC; HGNC:29603; HSFX1.
DR HGNC; HGNC:32701; HSFX2.
DR HPA; ENSG00000171116; Low tissue specificity.
DR HPA; ENSG00000268738; Tissue enriched (testis).
DR neXtProt; NX_Q9UBD0; -.
DR OpenTargets; ENSG00000171116; -.
DR PharmGKB; PA145008220; -.
DR VEuPathDB; HostDB:ENSG00000171116; -.
DR VEuPathDB; HostDB:ENSG00000268738; -.
DR eggNOG; KOG0627; Eukaryota.
DR GeneTree; ENSGT00940000163633; -.
DR HOGENOM; CLU_053156_1_0_1; -.
DR InParanoid; Q9UBD0; -.
DR OMA; DSEIYHH; -.
DR OrthoDB; 843026at2759; -.
DR PhylomeDB; Q9UBD0; -.
DR TreeFam; TF330401; -.
DR PathwayCommons; Q9UBD0; -.
DR SignaLink; Q9UBD0; -.
DR BioGRID-ORCS; 100130086; 5 hits in 583 CRISPR screens.
DR BioGRID-ORCS; 100506164; 10 hits in 607 CRISPR screens.
DR Pharos; Q9UBD0; Tbio.
DR PRO; PR:Q9UBD0; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9UBD0; protein.
DR Bgee; ENSG00000171116; Expressed in cortical plate and 88 other tissues.
DR ExpressionAtlas; Q9UBD0; baseline.
DR Genevisible; Q9UBD0; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:LIFEdb.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000232; HSF_DNA-bd.
DR InterPro; IPR027725; HSF_fam.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10015; PTHR10015; 1.
DR Pfam; PF00447; HSF_DNA-bind; 1.
DR SMART; SM00415; HSF; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; DNA-binding; Isopeptide bond; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..423
FT /note="Heat shock transcription factor, X-linked"
FT /id="PRO_0000339188"
FT DNA_BIND 98..282
FT /evidence="ECO:0000250"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 215
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
SQ SEQUENCE 423 AA; 46742 MW; EB27C8CD82C1C806 CRC64;
MEDKRSLSMA RCEERNSRGQ DHGLERVPFP PQLQSETYLH PADPSPAWDD PGSTGSPNLR
LLTEEIAFQP LAEEASFRRP HPDGDVPPQG EDNLLSLPFP QKLWRLVSSN QFSSIWWDDS
GACRVINQKL FEKEILKRDV AHKVFATTSI KSFFRQLNLY GFRKRRQCTF RTFTRIFSAK
RLVSILNKLE FYCHPYFQRD SPHLLVRMKR RVGVKSAPRH QEEDKPEAAG SCLAPADTEQ
QDHTSPNEND QVTPQHREPA GPNTQIRSGS APPATPVMVP DSAVASDNSP VTQPAGEWSE
GSQAHVTPVA AVPGPAALPF LYVPGSPTQM NSYGPVVALP TASRSTLAMD TTGLPAPGML
PFCHLWVPVT LVAAGAAQPA ASMVMFPHLP ALHHHCPHSH RTSQYMPASD GPQAYPDYAD
QST