USF1_HUMAN
ID USF1_HUMAN Reviewed; 310 AA.
AC P22415; B2RBZ4; Q5SY46; Q7Z5Y1;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Upstream stimulatory factor 1;
DE AltName: Full=Class B basic helix-loop-helix protein 11;
DE Short=bHLHb11;
DE AltName: Full=Major late transcription factor 1;
GN Name=USF1; Synonyms=BHLHB11, USF;
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 1-25.
RX PubMed=2249772; DOI=10.1101/gad.4.10.1730;
RA Gregor P.D., Sawadogo M., Roeder R.G.;
RT "The adenovirus major late transcription factor USF is a member of the
RT helix-loop-helix group of regulatory proteins and binds to DNA as a
RT dimer.";
RL Genes Dev. 4:1730-1740(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Fukamizu A.;
RT "Human USF1 genomic sequence.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
RA Saito T., Oishi T., Yanai K., Shimamoto Y., Fukamizu A.;
RT "Cloning and characterization of a novel splicing isoform of USF1.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG SeattleSNPs variation discovery resource;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
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 [10]
RP INTERACTION WITH VARICELLA-ZOSTER VIRUS IE62 PROTEIN.
RX PubMed=14573800; DOI=10.1099/vir.0.19335-0;
RA Rahaus M., Desloges N., Yang M., Ruyechan W.T., Wolff M.H.;
RT "Transcription factor USF, expressed during the entire phase of Varicella-
RT zoster virus infection, interacts physically with the major viral
RT transactivator IE62 and plays a significant role in virus replication.";
RL J. Gen. Virol. 84:2957-2967(2003).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-306, AND IDENTIFICATION BY MASS
RP 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 [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-306, 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).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 197-260.
RX PubMed=8306960; DOI=10.1002/j.1460-2075.1994.tb06247.x;
RA Ferre-D'Amare A.R., Pognonec P., Roeder R.G., Burley S.K.;
RT "Structure and function of the b/HLH/Z domain of USF.";
RL EMBO J. 13:180-189(1994).
RN [14]
RP INVOLVEMENT IN FCHL1.
RX PubMed=14991056; DOI=10.1038/ng1320;
RA Pajukanta P., Lilja H.E., Sinsheimer J.S., Cantor R.M., Lusis A.J.,
RA Gentile M., Duan X.J., Soro-Paavonen A., Naukkarinen J., Saarela J.,
RA Laakso M., Ehnholm C., Taskinen M.-R., Peltonen L.;
RT "Familial combined hyperlipidemia is associated with upstream transcription
RT factor 1 (USF1).";
RL Nat. Genet. 36:371-376(2004).
CC -!- FUNCTION: Transcription factor that binds to a symmetrical DNA sequence
CC (E-boxes) (5'-CACGTG-3') that is found in a variety of viral and
CC cellular promoters.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Binds DNA as a homodimer or a heterodimer (USF1/USF2).
CC Interacts with varicella-zoster virus IE62 protein.
CC {ECO:0000269|PubMed:14573800}.
CC -!- INTERACTION:
CC P22415; P22607: FGFR3; NbExp=3; IntAct=EBI-1054489, EBI-348399;
CC P22415; Q6FG41: FOS; NbExp=3; IntAct=EBI-1054489, EBI-10198738;
CC P22415; P15407: FOSL1; NbExp=6; IntAct=EBI-1054489, EBI-744510;
CC P22415; P01112: HRAS; NbExp=3; IntAct=EBI-1054489, EBI-350145;
CC P22415; Q92831: KAT2B; NbExp=5; IntAct=EBI-1054489, EBI-477430;
CC P22415; P28838: LAP3; NbExp=3; IntAct=EBI-1054489, EBI-2339312;
CC P22415; P57077-4: MAP3K7CL; NbExp=3; IntAct=EBI-1054489, EBI-10215880;
CC P22415; Q13573: SNW1; NbExp=3; IntAct=EBI-1054489, EBI-632715;
CC P22415; Q12933: TRAF2; NbExp=3; IntAct=EBI-1054489, EBI-355744;
CC P22415; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-1054489, EBI-741480;
CC P22415; P22415: USF1; NbExp=4; IntAct=EBI-1054489, EBI-1054489;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P22415-1; Sequence=Displayed;
CC Name=2; Synonyms=usf1-bd;
CC IsoId=P22415-2; Sequence=VSP_047740;
CC -!- DISEASE: Hyperlipidemia, familial combined, 1 (FCHL1) [MIM:602491]: A
CC disorder characterized by a variable pattern of elevated levels of
CC serum total cholesterol, triglycerides or both. It is observed in a
CC percentage of individuals with premature coronary heart disease.
CC {ECO:0000269|PubMed:14991056}. Note=Disease susceptibility is
CC associated with variants affecting the gene represented in this entry.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/usf1/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/USF1ID45856ch1q23.html";
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DR EMBL; X55666; CAA39201.1; -; mRNA.
DR EMBL; AB017568; BAA76541.1; -; Genomic_DNA.
DR EMBL; AB098540; BAC78384.1; -; mRNA.
DR EMBL; AK314876; BAG37391.1; -; mRNA.
DR EMBL; AL832119; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY593992; AAS89301.1; -; Genomic_DNA.
DR EMBL; AL591806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW52675.1; -; Genomic_DNA.
DR EMBL; BC035505; AAH35505.1; -; mRNA.
DR CCDS; CCDS1214.1; -. [P22415-1]
DR PIR; S13525; S13525.
DR RefSeq; NP_001263302.1; NM_001276373.1. [P22415-1]
DR RefSeq; NP_009053.1; NM_007122.4. [P22415-1]
DR RefSeq; NP_996888.1; NM_207005.2. [P22415-2]
DR PDB; 1AN4; X-ray; 2.90 A; A/B=197-260.
DR PDBsum; 1AN4; -.
DR AlphaFoldDB; P22415; -.
DR SASBDB; P22415; -.
DR SMR; P22415; -.
DR BioGRID; 113237; 76.
DR ComplexPortal; CPX-3079; USF1-USF2 upstream stimulatory factor complex.
DR ComplexPortal; CPX-3082; USF1 upstream stimulatory factor complex.
DR CORUM; P22415; -.
DR DIP; DIP-654N; -.
DR IntAct; P22415; 45.
DR MINT; P22415; -.
DR STRING; 9606.ENSP00000357000; -.
DR GlyGen; P22415; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P22415; -.
DR PhosphoSitePlus; P22415; -.
DR BioMuta; USF1; -.
DR DMDM; 137170; -.
DR EPD; P22415; -.
DR jPOST; P22415; -.
DR MassIVE; P22415; -.
DR MaxQB; P22415; -.
DR PaxDb; P22415; -.
DR PeptideAtlas; P22415; -.
DR PRIDE; P22415; -.
DR ProteomicsDB; 53989; -. [P22415-1]
DR ProteomicsDB; 69358; -.
DR Antibodypedia; 3773; 376 antibodies from 36 providers.
DR DNASU; 7391; -.
DR Ensembl; ENST00000368020.5; ENSP00000356999.1; ENSG00000158773.14. [P22415-1]
DR Ensembl; ENST00000368021.7; ENSP00000357000.3; ENSG00000158773.14. [P22415-1]
DR GeneID; 7391; -.
DR KEGG; hsa:7391; -.
DR MANE-Select; ENST00000368021.7; ENSP00000357000.3; NM_007122.5; NP_009053.1.
DR UCSC; uc001fxi.5; human. [P22415-1]
DR CTD; 7391; -.
DR DisGeNET; 7391; -.
DR GeneCards; USF1; -.
DR HGNC; HGNC:12593; USF1.
DR HPA; ENSG00000158773; Low tissue specificity.
DR MalaCards; USF1; -.
DR MIM; 191523; gene.
DR MIM; 602491; phenotype.
DR neXtProt; NX_P22415; -.
DR OpenTargets; ENSG00000158773; -.
DR PharmGKB; PA37223; -.
DR VEuPathDB; HostDB:ENSG00000158773; -.
DR eggNOG; KOG1318; Eukaryota.
DR GeneTree; ENSGT00940000157083; -.
DR InParanoid; P22415; -.
DR OMA; KTIPECN; -.
DR PhylomeDB; P22415; -.
DR TreeFam; TF323338; -.
DR PathwayCommons; P22415; -.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR SignaLink; P22415; -.
DR SIGNOR; P22415; -.
DR BioGRID-ORCS; 7391; 13 hits in 1101 CRISPR screens.
DR ChiTaRS; USF1; human.
DR EvolutionaryTrace; P22415; -.
DR GeneWiki; USF1; -.
DR GenomeRNAi; 7391; -.
DR Pharos; P22415; Tbio.
DR PRO; PR:P22415; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P22415; protein.
DR Bgee; ENSG00000158773; Expressed in granulocyte and 93 other tissues.
DR ExpressionAtlas; P22415; baseline and differential.
DR Genevisible; P22415; HS.
DR GO; GO:0000785; C:chromatin; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:LIFEdb.
DR GO; GO:0005667; C:transcription regulator complex; IDA:BHF-UCL.
DR GO; GO:0043425; F:bHLH transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
DR GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:BHF-UCL.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0045990; P:carbon catabolite regulation of transcription; TAS:BHF-UCL.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IDA:BHF-UCL.
DR GO; GO:0042593; P:glucose homeostasis; TAS:BHF-UCL.
DR GO; GO:0019086; P:late viral transcription; IDA:BHF-UCL.
DR GO; GO:0055088; P:lipid homeostasis; ISS:BHF-UCL.
DR GO; GO:0051918; P:negative regulation of fibrinolysis; IC:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0000432; P:positive regulation of transcription from RNA polymerase II promoter by glucose; IMP:BHF-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0000430; P:regulation of transcription from RNA polymerase II promoter by glucose; IC:BHF-UCL.
DR GO; GO:0001666; P:response to hypoxia; IMP:BHF-UCL.
DR GO; GO:0009411; P:response to UV; ISS:BHF-UCL.
DR Gene3D; 4.10.280.10; -; 1.
DR IDEAL; IID00121; -.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing; DNA-binding;
KW Isopeptide bond; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..310
FT /note="Upstream stimulatory factor 1"
FT /id="PRO_0000127496"
FT DOMAIN 199..254
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..292
FT /note="Leucine-zipper"
FT COMPBIAS 190..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 306
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..59
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_047740"
FT HELIX 205..225
FT /evidence="ECO:0007829|PDB:1AN4"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:1AN4"
FT TURN 240..247
FT /evidence="ECO:0007829|PDB:1AN4"
FT HELIX 248..255
FT /evidence="ECO:0007829|PDB:1AN4"
FT TURN 256..258
FT /evidence="ECO:0007829|PDB:1AN4"
SQ SEQUENCE 310 AA; 33538 MW; BFDA91519B4B80AE CRC64;
MKGQQKTAET EEGTVQIQEG AVATGEDPTS VAIASIQSAA TFPDPNVKYV FRTENGGQVM
YRVIQVSEGQ LDGQTEGTGA ISGYPATQSM TQAVIQGAFT SDDAVDTEGT AAETHYTYFP
STAVGDGAGG TTSGSTAAVV TTQGSEALLG QATPPGTGQF FVMMSPQEVL QGGSQRSIAP
RTHPYSPKSE APRTTRDEKR RAQHNEVERR RRDKINNWIV QLSKIIPDCS MESTKSGQSK
GGILSKACDY IQELRQSNHR LSEELQGLDQ LQLDNDVLRQ QVEDLKNKNL LLRAQLRHHG
LEVVIKNDSN
