HSF2_HUMAN
ID HSF2_HUMAN Reviewed; 536 AA.
AC Q03933; B4DGJ4; Q0VAH9; Q2M1K4; Q9H445;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Heat shock factor protein 2;
DE Short=HSF 2;
DE AltName: Full=Heat shock transcription factor 2;
DE Short=HSTF 2;
GN Name=HSF2; Synonyms=HSTF2;
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 [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 65-71.
RX PubMed=1871106; DOI=10.1073/pnas.88.16.6911;
RA Schuetz T.J., Gallo G.J., Sheldon L., Tempst P., Kingston R.E.;
RT "Isolation of a cDNA for HSF2: evidence for two heat shock factor genes in
RT humans.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:6911-6915(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [7]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS.
RX PubMed=8339932; DOI=10.1101/gad.7.8.1549;
RA Sheldon L., Kingston R.E.;
RT "Hydrophobic coiled-coil domains regulate the subcellular localization of
RT human heat shock factor 2.";
RL Genes Dev. 7:1549-1558(1993).
RN [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-82 AND LYS-139, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-82 AND LYS-139, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-82 AND LYS-139, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-2; LYS-82; LYS-135; LYS-139;
RP LYS-151; LYS-210; LYS-218 AND LYS-237, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: DNA-binding protein that specifically binds heat shock
CC promoter elements (HSE) and activates transcription. In higher
CC eukaryotes, HSF is unable to bind to the HSE unless the cells are heat
CC shocked.
CC -!- SUBUNIT: DNA-binding homotrimer in stressed or heat shocked cells,
CC otherwise found as a homodimer.
CC -!- INTERACTION:
CC Q03933; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-2556750, EBI-742887;
CC Q03933; Q9Y315: DERA; NbExp=3; IntAct=EBI-2556750, EBI-1048152;
CC Q03933; Q00613: HSF1; NbExp=8; IntAct=EBI-2556750, EBI-719620;
CC Q03933; O75031: HSF2BP; NbExp=3; IntAct=EBI-2556750, EBI-7116203;
CC Q03933; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-2556750, EBI-11522433;
CC Q03933; P37198: NUP62; NbExp=5; IntAct=EBI-2556750, EBI-347978;
CC Q03933; Q9NRD5: PICK1; NbExp=6; IntAct=EBI-2556750, EBI-79165;
CC Q03933; P06753: TPM3; NbExp=10; IntAct=EBI-2556750, EBI-355607;
CC Q03933; Q5VU62: TPM3; NbExp=3; IntAct=EBI-2556750, EBI-10184033;
CC Q03933; P61964: WDR5; NbExp=7; IntAct=EBI-2556750, EBI-540834;
CC Q03933-2; Q92993: KAT5; NbExp=3; IntAct=EBI-10223348, EBI-399080;
CC Q03933-2; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-10223348, EBI-11742507;
CC Q03933-2; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-10223348, EBI-742948;
CC Q03933-2; P37198: NUP62; NbExp=3; IntAct=EBI-10223348, EBI-347978;
CC Q03933-2; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-10223348, EBI-9090795;
CC Q03933-2; P61981: YWHAG; NbExp=3; IntAct=EBI-10223348, EBI-359832;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8339932}. Nucleus
CC {ECO:0000269|PubMed:8339932}. Note=Cytoplasmic during normal growth and
CC moves to the nucleus upon activation.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q03933-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q03933-2; Sequence=VSP_041128;
CC -!- SIMILARITY: Belongs to the HSF family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/hsf2/";
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DR EMBL; M65217; AAA36017.1; -; mRNA.
DR EMBL; DQ492684; ABF47087.1; -; Genomic_DNA.
DR EMBL; AK294624; BAG57805.1; -; mRNA.
DR EMBL; AK316377; BAH14748.1; -; mRNA.
DR EMBL; AL121954; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z99129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48176.1; -; Genomic_DNA.
DR EMBL; BC112323; AAI12324.1; -; mRNA.
DR EMBL; BC121050; AAI21051.1; -; mRNA.
DR EMBL; BC121051; AAI21052.1; -; mRNA.
DR EMBL; BC128420; AAI28421.1; -; mRNA.
DR CCDS; CCDS47470.1; -. [Q03933-2]
DR CCDS; CCDS5124.1; -. [Q03933-1]
DR PIR; A41138; A41138.
DR RefSeq; NP_001129036.1; NM_001135564.1. [Q03933-2]
DR RefSeq; NP_004497.1; NM_004506.3. [Q03933-1]
DR PDB; 5D8K; X-ray; 1.73 A; B=8-115.
DR PDB; 5D8L; X-ray; 2.07 A; B/D/F/H=8-115.
DR PDB; 5HDK; X-ray; 1.32 A; A/B/C/D=7-112.
DR PDB; 7DCI; X-ray; 1.70 A; A=7-110.
DR PDB; 7DCU; X-ray; 1.75 A; A/B/C=7-112.
DR PDBsum; 5D8K; -.
DR PDBsum; 5D8L; -.
DR PDBsum; 5HDK; -.
DR PDBsum; 7DCI; -.
DR PDBsum; 7DCU; -.
DR AlphaFoldDB; Q03933; -.
DR SMR; Q03933; -.
DR BioGRID; 109531; 69.
DR CORUM; Q03933; -.
DR DIP; DIP-56593N; -.
DR IntAct; Q03933; 81.
DR STRING; 9606.ENSP00000357440; -.
DR ChEMBL; CHEMBL3988631; -.
DR iPTMnet; Q03933; -.
DR PhosphoSitePlus; Q03933; -.
DR BioMuta; HSF2; -.
DR DMDM; 462334; -.
DR EPD; Q03933; -.
DR jPOST; Q03933; -.
DR MassIVE; Q03933; -.
DR MaxQB; Q03933; -.
DR PaxDb; Q03933; -.
DR PeptideAtlas; Q03933; -.
DR PRIDE; Q03933; -.
DR ProteomicsDB; 58228; -. [Q03933-1]
DR ProteomicsDB; 58229; -. [Q03933-2]
DR Antibodypedia; 4231; 724 antibodies from 40 providers.
DR DNASU; 3298; -.
DR Ensembl; ENST00000368455.9; ENSP00000357440.4; ENSG00000025156.13. [Q03933-1]
DR Ensembl; ENST00000452194.5; ENSP00000400380.1; ENSG00000025156.13. [Q03933-2]
DR GeneID; 3298; -.
DR KEGG; hsa:3298; -.
DR MANE-Select; ENST00000368455.9; ENSP00000357440.4; NM_004506.4; NP_004497.1.
DR UCSC; uc003pyu.3; human. [Q03933-1]
DR CTD; 3298; -.
DR DisGeNET; 3298; -.
DR GeneCards; HSF2; -.
DR HGNC; HGNC:5225; HSF2.
DR HPA; ENSG00000025156; Low tissue specificity.
DR MIM; 140581; gene.
DR neXtProt; NX_Q03933; -.
DR OpenTargets; ENSG00000025156; -.
DR PharmGKB; PA29494; -.
DR VEuPathDB; HostDB:ENSG00000025156; -.
DR eggNOG; KOG0627; Eukaryota.
DR GeneTree; ENSGT00940000155906; -.
DR HOGENOM; CLU_038829_1_0_1; -.
DR InParanoid; Q03933; -.
DR OMA; PTDHDHI; -.
DR OrthoDB; 1154048at2759; -.
DR PhylomeDB; Q03933; -.
DR TreeFam; TF330401; -.
DR PathwayCommons; Q03933; -.
DR SignaLink; Q03933; -.
DR SIGNOR; Q03933; -.
DR BioGRID-ORCS; 3298; 36 hits in 1104 CRISPR screens.
DR ChiTaRS; HSF2; human.
DR GeneWiki; HSF2; -.
DR GenomeRNAi; 3298; -.
DR Pharos; Q03933; Tbio.
DR PRO; PR:Q03933; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q03933; protein.
DR Bgee; ENSG00000025156; Expressed in cortical plate and 199 other tissues.
DR ExpressionAtlas; Q03933; baseline and differential.
DR Genevisible; Q03933; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
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:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:ARUK-UCL.
DR GO; GO:0001162; F:RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR027712; HSF2.
DR InterPro; IPR000232; HSF_DNA-bd.
DR InterPro; IPR027725; HSF_fam.
DR InterPro; IPR010542; Vert_HSTF_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10015; PTHR10015; 1.
DR PANTHER; PTHR10015:SF185; PTHR10015:SF185; 1.
DR Pfam; PF00447; HSF_DNA-bind; 1.
DR Pfam; PF06546; Vert_HS_TF; 1.
DR PRINTS; PR00056; HSFDOMAIN.
DR SMART; SM00415; HSF; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00434; HSF_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; DNA-binding; Isopeptide bond; Nucleus;
KW Reference proteome; Stress response; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..536
FT /note="Heat shock factor protein 2"
FT /id="PRO_0000124569"
FT DNA_BIND 7..112
FT /evidence="ECO:0000250"
FT REGION 119..192
FT /note="Hydrophobic repeat HR-A/B"
FT REGION 300..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..385
FT /note="Hydrophobic repeat HR-C"
FT REGION 407..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 108..122
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 195..210
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 304..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 2
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 82
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 135
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 151
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 210
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 218
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 237
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 393..410
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_041128"
FT MUTAGEN 109
FT /note="R->G: Fails to translocate to nucleus."
FT /evidence="ECO:0000269|PubMed:8339932"
FT MUTAGEN 196..198
FT /note="RKR->ASS: Fails to translocate to nucleus."
FT /evidence="ECO:0000269|PubMed:8339932"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:5HDK"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:5HDK"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:5HDK"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:5HDK"
FT TURN 31..34
FT /evidence="ECO:0007829|PDB:5HDK"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:5HDK"
FT HELIX 41..47
FT /evidence="ECO:0007829|PDB:5HDK"
FT HELIX 49..53
FT /evidence="ECO:0007829|PDB:5HDK"
FT HELIX 58..67
FT /evidence="ECO:0007829|PDB:5HDK"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:5HDK"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:5D8L"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:5D8K"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:5HDK"
FT HELIX 101..106
FT /evidence="ECO:0007829|PDB:5HDK"
SQ SEQUENCE 536 AA; 60348 MW; 00DFD05CFD9DF0D3 CRC64;
MKQSSNVPAF LSKLWTLVEE THTNEFITWS QNGQSFLVLD EQRFAKEILP KYFKHNNMAS
FVRQLNMYGF RKVVHIDSGI VKQERDGPVE FQHPYFKQGQ DDLLENIKRK VSSSKPEENK
IRQEDLTKII SSAQKVQIKQ ETIESRLSEL KSENESLWKE VSELRAKHAQ QQQVIRKIVQ
FIVTLVQNNQ LVSLKRKRPL LLNTNGAQKK NLFQHIVKEP TDNHHHKVPH SRTEGLKPRE
RISDDIIIYD VTDDNADEEN IPVIPETNED VISDPSNCSQ YPDIVIVEDD NEDEYAPVIQ
SGEQNEPARE SLSSGSDGSS PLMSSAVQLN GSSSLTSEDP VTMMDSILND NINLLGKVEL
LDYLDSIDCS LEDFQAMLSG RQFSIDPDLL VDLFTSSVQM NPTDYINNTK SENKGLETTK
NNVVQPVSEE GRKSKSKPDK QLIQYTAFPL LAFLDGNPAS SVEQASTTAS SEVLSSVDKP
IEVDELLDSS LDPEPTQSKL VRLEPLTEAE ASEATLFYLC ELAPAPLDSD MPLLDS
