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USF2_RAT
ID   USF2_RAT                Reviewed;         346 AA.
AC   Q63665; Q76MJ1; Q76MU2; Q9EQX1; Q9EQX2; Q9EQX3;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Upstream stimulatory factor 2;
DE   AltName: Full=Major late transcription factor 2;
DE   AltName: Full=Upstream transcription factor 2;
GN   Name=Usf2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5).
RC   TISSUE=Intestine;
RX   PubMed=11272846; DOI=10.1271/bbb.65.56;
RA   Takahashi K., Nishiyama C., Okumura K., Ra C., Ohtake Y., Yokota T.;
RT   "Molecular cloning of rat USF2 cDNA and characterization of splicing
RT   variants.";
RL   Biosci. Biotechnol. Biochem. 65:56-62(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION.
RC   TISSUE=Ovarian granulosa cell;
RX   PubMed=11319134; DOI=10.1095/biolreprod64.5.1315;
RA   Yamada K., Mizutani T., Shou Z., Yazawa T., Sekiguchi T., Yoshino M.,
RA   Inazu T., Miyamoto K.;
RT   "Cloning and functional expression of an E box-binding protein from rat
RT   granulosa cells.";
RL   Biol. Reprod. 64:1315-1319(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 56-346 (ISOFORM 1).
RC   STRAIN=Sprague-Dawley; 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).
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). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC         Comment=At least 2 isoforms are produced.;
CC       Name=1; Synonyms=USF2L, USF2A;
CC         IsoId=Q63665-1; Sequence=Displayed;
CC       Name=2; Synonyms=USF2delta1;
CC         IsoId=Q63665-2; Sequence=VSP_016547;
CC       Name=3; Synonyms=USF2delta2, USF2B;
CC         IsoId=Q63665-3; Sequence=VSP_016546;
CC       Name=4; Synonyms=USF2delta3;
CC         IsoId=Q63665-4; Sequence=VSP_016542, VSP_016545;
CC       Name=5; Synonyms=USF2delta4;
CC         IsoId=Q63665-5; Sequence=VSP_016543, VSP_016544;
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DR   EMBL; AB035647; BAB19964.1; -; mRNA.
DR   EMBL; AB035648; BAB19965.1; -; mRNA.
DR   EMBL; AB035649; BAB19966.1; -; mRNA.
DR   EMBL; AB035650; BAB19967.1; -; mRNA.
DR   EMBL; AB035651; BAB19968.1; -; mRNA.
DR   EMBL; AB047556; BAB20993.1; -; mRNA.
DR   EMBL; X90823; CAA62338.1; -; mRNA.
DR   RefSeq; NP_112401.1; NM_031139.1. [Q63665-1]
DR   AlphaFoldDB; Q63665; -.
DR   STRING; 10116.ENSRNOP00000028550; -.
DR   iPTMnet; Q63665; -.
DR   PhosphoSitePlus; Q63665; -.
DR   PaxDb; Q63665; -.
DR   Ensembl; ENSRNOT00000103509; ENSRNOP00000094253; ENSRNOG00000053725. [Q63665-3]
DR   GeneID; 81817; -.
DR   KEGG; rno:81817; -.
DR   UCSC; RGD:620975; rat. [Q63665-1]
DR   CTD; 7392; -.
DR   RGD; 620975; Usf2.
DR   eggNOG; KOG1318; Eukaryota.
DR   GeneTree; ENSGT00940000160704; -.
DR   InParanoid; Q63665; -.
DR   OrthoDB; 1345445at2759; -.
DR   PhylomeDB; Q63665; -.
DR   TreeFam; TF323338; -.
DR   PRO; PR:Q63665; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   GO; GO:0005634; C:nucleus; IDA:RGD.
DR   GO; GO:0043425; F:bHLH transcription factor binding; ISO:RGD.
DR   GO; GO:0003677; F:DNA binding; ISO:RGD.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:RGD.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:RGD.
DR   GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD.
DR   GO; GO:0042802; F:identical protein binding; IMP:RGD.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR   GO; GO:0044877; F:protein-containing complex binding; IMP:RGD.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:RGD.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR   GO; GO:0007595; P:lactation; ISO:RGD.
DR   GO; GO:0055088; P:lipid homeostasis; ISO:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:RGD.
DR   GO; GO:0000432; P:positive regulation of transcription from RNA polymerase II promoter by glucose; ISO:RGD.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR   Gene3D; 4.10.280.10; -; 1.
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   Alternative splicing; DNA-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..346
FT                   /note="Upstream stimulatory factor 2"
FT                   /id="PRO_0000127502"
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         21..27
FT                   /note="SHDKGPE -> RRGRPGG (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:11272846"
FT                   /id="VSP_016542"
FT   VAR_SEQ         21..22
FT                   /note="SH -> RL (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:11272846"
FT                   /id="VSP_016543"
FT   VAR_SEQ         23..346
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:11272846"
FT                   /id="VSP_016544"
FT   VAR_SEQ         28..346
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:11272846"
FT                   /id="VSP_016545"
FT   VAR_SEQ         77..143
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:11272846"
FT                   /id="VSP_016546"
FT   VAR_SEQ         117..143
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11272846"
FT                   /id="VSP_016547"
FT   CONFLICT        95
FT                   /note="A -> T (in Ref. 3; CAA62338)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   346 AA;  36954 MW;  E9D216BC25F9447B CRC64;
     MDMLDPGLDP ASSATAAAAA SHDKGPEAEE GVELQEGGDG PGAEEQTAVA IASVQQAAFG
     DHNIQYQFRT ESNGGQVTYR VVQVTDGQLD GQGDAAGAVS VVSTAAFAGG QQAVTQVGVD
     GAAQRPGPAA ASVPTGPAAP FPLAVIQNPF SNGGSPAAEA VSGEARFAYF PASSVGDTTA
     VSVQTTDQSL QAGGQFYVMM TPQDVLQTGT QRTIAPRTHP YSPKIDGTRT PRDERRRAQH
     NEVERRRRDK INNWIVQLSK IIPDCHADNS KTGASKGGIL SKACDYIREL RQTNQRMQET
     FKEAERLQMD NELLRQQIEE LKNENALLRA QLQQHNLEMV GESTRQ
 
 
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