ID   USF2_HUMAN              Reviewed;         346 AA.
AC   Q15853; O00671; O00709; Q05750; Q07952; Q15851; Q15852; Q6FI33; Q6YI47;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 201.
DE   RecName: Full=Upstream stimulatory factor 2;
DE   AltName: Full=Class B basic helix-loop-helix protein 12;
DE            Short=bHLHb12;
DE   AltName: Full=FOS-interacting protein;
DE            Short=FIP;
DE   AltName: Full=Major late transcription factor 2;
DE   AltName: Full=Upstream transcription factor 2;
GN   Name=USF2; Synonyms=BHLHB12;
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] (ISOFORMS USF2A; USF2B AND USF2A-DELTA-H).
RC   TISSUE=Liver;
RX   PubMed=8576131; DOI=10.1074/jbc.271.3.1405;
RA   Viollet B., Lefrancois-Martinez A.-M., Henrion A., Kahn A., Raymondjean M.,
RA   Martinez A.;
RT   "Immunochemical characterization and transacting properties of upstream
RT   stimulatory factor isoforms.";
RL   J. Biol. Chem. 271:1405-1415(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=8954795; DOI=10.1006/geno.1996.0609;
RA   Groenen P.M.A., Garcia E., Debeer P., Devriendt K., Fryns J.-P.,
RA   van de Ven W.J.M.;
RT   "Structure, sequence, and chromosome 19 localization of human USF2 and its
RT   rearrangement in a patient with multicystic renal dysplasia.";
RL   Genomics 38:141-148(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM USF2C).
RX   PubMed=15276216; DOI=10.1016/j.gene.2004.05.005;
RA   Yan S., Sloane B.F.;
RT   "Isolation of a novel USF2 isoform: repressor of cathepsin B expression.";
RL   Gene 337:199-206(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM USF2A).
RA   Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA   Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA   LaBaer J.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM USF2A).
RC   TISSUE=Blood;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 46-346.
RC   TISSUE=B-cell;
RX   PubMed=1450663;
RA   Sirito M., Walker S., Lin Q., Kozlowski M.T., Klein W.H., Sawadogo M.;
RT   "Members of the USF family of helix-loop-helix proteins bind DNA as
RT   homo- as well as heterodimers.";
RL   Gene Expr. 2:231-240(1992).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 93-346.
RX   PubMed=1589769; DOI=10.1126/science.1589769;
RA   Blanar M.A., Rutter W.J.;
RT   "Interaction cloning: identification of a helix-loop-helix zipper protein
RT   that interacts with c-Fos.";
RL   Science 256:1014-1018(1992).
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: Interacts with MAF (By similarity). Efficient DNA binding
CC       requires dimerization with another bHLH protein. Binds DNA as a
CC       homodimer or a heterodimer (USF1/USF2). In vivo, the USF1/USF2A
CC       heterodimer represents over 66% of the usf binding activity whereas the
CC       USF1 and USF2A homodimers represent less than 10%. The USF1/USF2B
CC       heterodimer accounted for almost 15% in some cell. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q15853; Q6FG41: FOS; NbExp=3; IntAct=EBI-1055994, EBI-10198738;
CC       Q15853; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-1055994, EBI-741037;
CC       Q15853; Q15562: TEAD2; NbExp=3; IntAct=EBI-1055994, EBI-6427252;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=USF2A;
CC         IsoId=Q15853-1; Sequence=Displayed;
CC       Name=USF2A-delta-H;
CC         IsoId=Q15853-2; Sequence=VSP_002165;
CC       Name=USF2B;
CC         IsoId=Q15853-3; Sequence=VSP_002164;
CC       Name=USF2c;
CC         IsoId=Q15853-4; Sequence=VSP_047804;
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- MISCELLANEOUS: [Isoform USF2c]: Can bind as a homodimer to the E-box of
CC       the cathepsin B (CTSB) promoter. {ECO:0000305}.
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DR   EMBL; X90824; CAA62339.1; -; mRNA.
DR   EMBL; X90825; CAA62340.1; -; mRNA.
DR   EMBL; X90826; CAA62341.1; -; mRNA.
DR   EMBL; Y07661; CAA68942.1; -; Genomic_DNA.
DR   EMBL; AY147880; AAN63092.1; -; mRNA.
DR   EMBL; CR536504; CAG38742.1; -; mRNA.
DR   EMBL; AD000684; AAB51179.1; -; Genomic_DNA.
DR   EMBL; BC049821; AAH49821.1; -; mRNA.
DR   EMBL; S50537; AAB24368.1; -; mRNA.
DR   EMBL; M77476; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS12452.1; -. [Q15853-1]
DR   CCDS; CCDS12453.1; -. [Q15853-3]
DR   CCDS; CCDS82329.1; -. [Q15853-4]
DR   PIR; I54074; I54074.
DR   RefSeq; NP_001308079.1; NM_001321150.1. [Q15853-4]
DR   RefSeq; NP_003358.1; NM_003367.3. [Q15853-1]
DR   RefSeq; NP_997174.1; NM_207291.2. [Q15853-3]
DR   PDB; 8IA3; X-ray; 3.50 A; A/B/E/F=235-346.
DR   PDBsum; 8IA3; -.
DR   AlphaFoldDB; Q15853; -.
DR   SMR; Q15853; -.
DR   BioGRID; 113238; 38.
DR   ComplexPortal; CPX-3079; USF1-USF2 upstream stimulatory factor complex.
DR   ComplexPortal; CPX-3083; USF2 upstream stimulatory factor complex.
DR   CORUM; Q15853; -.
DR   IntAct; Q15853; 20.
DR   MINT; Q15853; -.
DR   STRING; 9606.ENSP00000222305; -.
DR   GlyCosmos; Q15853; 3 sites, 1 glycan.
DR   GlyGen; Q15853; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; Q15853; -.
DR   MetOSite; Q15853; -.
DR   PhosphoSitePlus; Q15853; -.
DR   BioMuta; USF2; -.
DR   DMDM; 2833271; -.
DR   EPD; Q15853; -.
DR   jPOST; Q15853; -.
DR   MassIVE; Q15853; -.
DR   MaxQB; Q15853; -.
DR   PaxDb; 9606-ENSP00000222305; -.
DR   PeptideAtlas; Q15853; -.
DR   ProteomicsDB; 60794; -. [Q15853-1]
DR   ProteomicsDB; 60795; -. [Q15853-2]
DR   ProteomicsDB; 60796; -. [Q15853-3]
DR   ProteomicsDB; 67853; -.
DR   Pumba; Q15853; -.
DR   Antibodypedia; 15859; 414 antibodies from 34 providers.
DR   DNASU; 7392; -.
DR   Ensembl; ENST00000222305.8; ENSP00000222305.2; ENSG00000105698.16. [Q15853-1]
DR   Ensembl; ENST00000343550.9; ENSP00000340633.4; ENSG00000105698.16. [Q15853-3]
DR   Ensembl; ENST00000379134.7; ENSP00000368429.3; ENSG00000105698.16. [Q15853-4]
DR   Ensembl; ENST00000595068.5; ENSP00000471099.1; ENSG00000105698.16. [Q15853-2]
DR   GeneID; 7392; -.
DR   KEGG; hsa:7392; -.
DR   MANE-Select; ENST00000222305.8; ENSP00000222305.2; NM_003367.4; NP_003358.1.
DR   UCSC; uc002nyq.2; human. [Q15853-1]
DR   AGR; HGNC:12594; -.
DR   CTD; 7392; -.
DR   DisGeNET; 7392; -.
DR   GeneCards; USF2; -.
DR   HGNC; HGNC:12594; USF2.
DR   HPA; ENSG00000105698; Low tissue specificity.
DR   MIM; 600390; gene.
DR   neXtProt; NX_Q15853; -.
DR   OpenTargets; ENSG00000105698; -.
DR   PharmGKB; PA37224; -.
DR   VEuPathDB; HostDB:ENSG00000105698; -.
DR   eggNOG; KOG1318; Eukaryota.
DR   GeneTree; ENSGT00940000160704; -.
DR   HOGENOM; CLU_070485_2_0_1; -.
DR   InParanoid; Q15853; -.
DR   OMA; HEKSQEG; -.
DR   OrthoDB; 2911834at2759; -.
DR   PhylomeDB; Q15853; -.
DR   TreeFam; TF323338; -.
DR   PathwayCommons; Q15853; -.
DR   Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR   SignaLink; Q15853; -.
DR   SIGNOR; Q15853; -.
DR   BioGRID-ORCS; 7392; 208 hits in 1186 CRISPR screens.
DR   ChiTaRS; USF2; human.
DR   GeneWiki; USF2; -.
DR   GenomeRNAi; 7392; -.
DR   Pharos; Q15853; Tbio.
DR   PRO; PR:Q15853; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q15853; Protein.
DR   Bgee; ENSG00000105698; Expressed in right hemisphere of cerebellum and 209 other cell types or tissues.
DR   ExpressionAtlas; Q15853; baseline and differential.
DR   GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR   GO; GO:0043425; F:bHLH transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IMP:BHF-UCL.
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: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:0007595; P:lactation; IEA:Ensembl.
DR   GO; GO:0019086; P:late viral transcription; IC:BHF-UCL.
DR   GO; GO:0055088; P:lipid homeostasis; ISS: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; IBA:GO_Central.
DR   GO; GO:0000430; P:regulation of transcription from RNA polymerase II promoter by glucose; IC:BHF-UCL.
DR   CDD; cd18923; bHLHzip_USF2; 1.
DR   Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   PANTHER; PTHR46117; FI24210P1; 1.
DR   PANTHER; PTHR46117:SF2; UPSTREAM STIMULATORY FACTOR 2; 1.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR   PROSITE; PS50888; BHLH; 1.
DR   Genevisible; Q15853; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; DNA-binding; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..346
FT                   /note="Upstream stimulatory factor 2"
FT                   /id="PRO_0000127500"
FT   DOMAIN          235..290
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          215..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          307..328
FT                   /note="Leucine-zipper"
FT   COMPBIAS        226..244
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         76..206
FT                   /note="Missing (in isoform USF2c)"
FT                   /evidence="ECO:0000303|PubMed:15276216"
FT                   /id="VSP_047804"
FT   VAR_SEQ         77..143
FT                   /note="Missing (in isoform USF2B)"
FT                   /evidence="ECO:0000303|PubMed:8576131"
FT                   /id="VSP_002164"
FT   VAR_SEQ         275..282
FT                   /note="Missing (in isoform USF2A-delta-H)"
FT                   /evidence="ECO:0000303|PubMed:8576131"
FT                   /id="VSP_002165"
FT   CONFLICT        46..64
FT                   /note="QTAVAITSVQQAAFGDHNI -> GGGTSGGRGSGIQTRVQHV (in Ref.
FT                   7)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        93..100
FT                   /note="GDTAGAVS -> EFHSWRRH (in Ref. 8; M77476)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        122
FT                   /note="A -> V (in Ref. 8; M77476)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        308
FT                   /note="Q -> R (in Ref. 4; CAG38742)"
FT                   /evidence="ECO:0000305"
FT   TURN            237..239
FT                   /evidence="ECO:0007829|PDB:8IA3"
FT   HELIX           240..261
FT                   /evidence="ECO:0007829|PDB:8IA3"
FT   TURN            263..267
FT                   /evidence="ECO:0007829|PDB:8IA3"
FT   TURN            271..274
FT                   /evidence="ECO:0007829|PDB:8IA3"
FT   HELIX           276..302
FT                   /evidence="ECO:0007829|PDB:8IA3"
FT   HELIX           304..333
FT                   /evidence="ECO:0007829|PDB:8IA3"
FT   TURN            337..340
FT                   /evidence="ECO:0007829|PDB:8IA3"
SQ   SEQUENCE   346 AA;  36955 MW;  78CEFE97AC4C10CF CRC64;
     MDMLDPGLDP AASATAAAAA SHDKGPEAEE GVELQEGGDG PGAEEQTAVA ITSVQQAAFG
     DHNIQYQFRT ETNGGQVTYR VVQVTDGQLD GQGDTAGAVS VVSTAAFAGG QQAVTQVGVD
     GAAQRPGPAA ASVPPGPAAP FPLAVIQNPF SNGGSPAAEA VSGEARFAYF PASSVGDTTA
     VSVQTTDQSL QAGGQFYVMM TPQDVLQTGT QRTIAPRTHP YSPKIDGTRT PRDERRRAQH
     NEVERRRRDK INNWIVQLSK IIPDCNADNS KTGASKGGIL SKACDYIREL RQTNQRMQET
     FKEAERLQMD NELLRQQIEE LKNENALLRA QLQQHNLEMV GEGTRQ
//