SRBP2_MOUSE
ID SRBP2_MOUSE Reviewed; 1130 AA.
AC Q3U1N2; Q925C2; Q9ESZ4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Sterol regulatory element-binding protein 2 {ECO:0000303|PubMed:29068315};
DE Short=SREBP-2 {ECO:0000303|PubMed:29068315};
DE AltName: Full=Sterol regulatory element-binding transcription factor 2 {ECO:0000303|PubMed:29068315};
DE Contains:
DE RecName: Full=Processed sterol regulatory element-binding protein 2 {ECO:0000305};
DE AltName: Full=Transcription factor SREBF2 {ECO:0000305};
GN Name=Srebf2 {ECO:0000312|MGI:MGI:107585};
GN Synonyms=Srebp2 {ECO:0000303|PubMed:29068315};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE33463.1}; TISSUE=Dendritic cell;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-1096 (ISOFORM 1), AND INTERACTION WITH
RP LMNA.
RC STRAIN=Swiss albino {ECO:0000269|PubMed:11929849};
RC TISSUE=Adipocyte {ECO:0000269|PubMed:11929849};
RX PubMed=11929849; DOI=10.1093/hmg/11.7.769;
RA Lloyd D.J., Trembath R.C., Shackleton S.;
RT "A novel interaction between lamin A and SREBP1: implications for partial
RT lipodystrophy and other laminopathies.";
RL Hum. Mol. Genet. 11:769-777(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 141-392.
RX PubMed=12668174; DOI=10.1016/s1388-1981(03)00041-6;
RA Salles J., Sargueil F., Knoll-Gellida A., Witters L.A., Cassagne C.,
RA Garbay B.;
RT "Acetyl-CoA carboxylase and SREBP expression during peripheral nervous
RT system myelination.";
RL Biochim. Biophys. Acta 1631:229-238(2003).
RN [5]
RP FUNCTION.
RX PubMed=9616204; DOI=10.1172/jci2961;
RA Horton J.D., Shimomura I., Brown M.S., Hammer R.E., Goldstein J.L.,
RA Shimano H.;
RT "Activation of cholesterol synthesis in preference to fatty acid synthesis
RT in liver and adipose tissue of transgenic mice overproducing sterol
RT regulatory element-binding protein-2.";
RL J. Clin. Invest. 101:2331-2339(1998).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=10397761; DOI=10.1091/mbc.10.7.2221;
RA Nagoshi E., Imamoto N., Sato R., Yoneda Y.;
RT "Nuclear import of sterol regulatory element-binding protein-2, a basic
RT helix-loop-helix-leucine zipper (bHLH-Zip)-containing transcription factor,
RT occurs through the direct interaction of importin beta with HLH-Zip.";
RL Mol. Biol. Cell 10:2221-2233(1999).
RN [7]
RP SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF 369-LEU--LEU-383.
RX PubMed=11283257; DOI=10.1128/mcb.21.8.2779-2789.2001;
RA Nagoshi E., Yoneda Y.;
RT "Dimerization of sterol regulatory element-binding protein 2 via the helix-
RT loop-helix-leucine zipper domain is a prerequisite for its nuclear
RT localization mediated by importin beta.";
RL Mol. Cell. Biol. 21:2779-2789(2001).
RN [8] {ECO:0000305}
RP REVIEW, AND DISRUPTION PHENOTYPE.
RX PubMed=11994399; DOI=10.1172/jci15593;
RA Horton J.D., Goldstein J.L., Brown M.S.;
RT "SREBPs: activators of the complete program of cholesterol and fatty acid
RT synthesis in the liver.";
RL J. Clin. Invest. 109:1125-1131(2002).
RN [9]
RP FUNCTION.
RX PubMed=16100574; DOI=10.1172/jci25614;
RA Engelking L.J., Liang G., Hammer R.E., Takaishi K., Kuriyama H.,
RA Evers B.M., Li W.P., Horton J.D., Goldstein J.L., Brown M.S.;
RT "Schoenheimer effect explained--feedback regulation of cholesterol
RT synthesis in mice mediated by Insig proteins.";
RL J. Clin. Invest. 115:2489-2498(2005).
RN [10]
RP PHOSPHORYLATION BY AMPK.
RX PubMed=21459323; DOI=10.1016/j.cmet.2011.03.009;
RA Li Y., Xu S., Mihaylova M.M., Zheng B., Hou X., Jiang B., Park O., Luo Z.,
RA Lefai E., Shyy J.Y., Gao B., Wierzbicki M., Verbeuren T.J., Shaw R.J.,
RA Cohen R.A., Zang M.;
RT "AMPK phosphorylates and inhibits SREBP activity to attenuate hepatic
RT steatosis and atherosclerosis in diet-induced insulin-resistant mice.";
RL Cell Metab. 13:376-388(2011).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=29068315; DOI=10.7554/elife.28766;
RA Zhang L., Rajbhandari P., Priest C., Sandhu J., Wu X., Temel R.,
RA Castrillo A., de Aguiar Vallim T.Q., Sallam T., Tontonoz P.;
RT "Inhibition of cholesterol biosynthesis through RNF145-dependent
RT ubiquitination of SCAP.";
RL Elife 6:0-0(2017).
RN [12]
RP REVIEW.
RX PubMed=28849786; DOI=10.1038/nrendo.2017.91;
RA Shimano H., Sato R.;
RT "SREBP-regulated lipid metabolism: convergent physiology - divergent
RT pathophysiology.";
RL Nat. Rev. Endocrinol. 13:710-730(2017).
CC -!- FUNCTION: [Sterol regulatory element-binding protein 2]: Precursor of
CC the transcription factor form (Processed sterol regulatory element-
CC binding protein 2), which is embedded in the endoplasmic reticulum
CC membrane (By similarity). Low sterol concentrations promote processing
CC of this form, releasing the transcription factor form that translocates
CC into the nucleus and activates transcription of genes involved in
CC cholesterol biosynthesis (PubMed:9616204, PubMed:16100574).
CC {ECO:0000250|UniProtKB:Q12772, ECO:0000269|PubMed:16100574,
CC ECO:0000269|PubMed:9616204}.
CC -!- FUNCTION: [Processed sterol regulatory element-binding protein 2]: Key
CC transcription factor that regulates expression of genes involved in
CC cholesterol biosynthesis (PubMed:9616204). Binds to the sterol
CC regulatory element 1 (SRE-1) (5'-ATCACCCCAC-3'). Has dual sequence
CC specificity binding to both an E-box motif (5'-ATCACGTGA-3') and to
CC SRE-1 (5'-ATCACCCCAC-3') (By similarity). Regulates transcription of
CC genes related to cholesterol synthesis pathway (PubMed:9616204).
CC {ECO:0000250|UniProtKB:Q12772, ECO:0000269|PubMed:9616204}.
CC -!- SUBUNIT: [Sterol regulatory element-binding protein 2]: Forms a tight
CC complex with SCAP, the SCAP-SREBP complex, in the endoplasmic reticulum
CC membrane. Interacts (via C-terminal domain) with RNF139.
CC {ECO:0000250|UniProtKB:Q12772}.
CC -!- SUBUNIT: [Processed sterol regulatory element-binding protein 2]:
CC Homodimer; efficient DNA binding of the soluble transcription factor
CC fragment requires dimerization with another bHLH protein
CC (PubMed:11283257). Interacts with LMNA (PubMed:11929849).
CC {ECO:0000269|PubMed:11283257, ECO:0000269|PubMed:11929849}.
CC -!- INTERACTION:
CC Q3U1N2; Q9JM73: Srf; NbExp=3; IntAct=EBI-645275, EBI-493266;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q12772}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000303|PubMed:28849786};
CC Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, COPII-
CC coated vesicle membrane {ECO:0000303|PubMed:28849786}; Multi-pass
CC membrane protein {ECO:0000255}. Note=At high sterol concentrations, the
CC SCAP-SREBP is retained in the endoplasmic reticulum (By similarity).
CC Low sterol concentrations promote recruitment into COPII-coated
CC vesicles and transport of the SCAP-SREBP to the Golgi, where it is
CC processed (By similarity). {ECO:0000250|UniProtKB:Q12772}.
CC -!- SUBCELLULAR LOCATION: [Processed sterol regulatory element-binding
CC protein 2]: Nucleus {ECO:0000269|PubMed:10397761,
CC ECO:0000269|PubMed:11283257, ECO:0000269|PubMed:29068315}.
CC Note=Transported into the nucleus with the help of importin-beta
CC (PubMed:10397761, PubMed:11283257). Dimerization of the bHLH domain is
CC a prerequisite for importin beta-dependent nuclear import
CC (PubMed:10397761, PubMed:11283257). {ECO:0000269|PubMed:10397761,
CC ECO:0000269|PubMed:11283257}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3U1N2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3U1N2-2; Sequence=VSP_052658, VSP_052659;
CC -!- PTM: [Sterol regulatory element-binding protein 2]: Processed in the
CC Golgi apparatus, releasing the protein from the membrane. At low
CC cholesterol the SCAP-SREBP complex is recruited into COPII vesicles for
CC export from the endoplasmic reticulum. In the Golgi, complex SREBPs are
CC cleaved sequentially by site-1 (MBTPS1, S1P) and site-2 (MBTPS2, S2P)
CC proteases. The first cleavage by site-1 protease occurs within the
CC luminal loop, the second cleavage by site-2 protease occurs within the
CC first transmembrane domain, releasing the transcription factor from the
CC Golgi membrane. Apoptosis triggers cleavage by the cysteine proteases
CC caspase-3 and caspase-7. Cleavage and activation is induced by mediated
CC cholesterol efflux. {ECO:0000250|UniProtKB:Q12772}.
CC -!- PTM: Phosphorylated by AMPK, leading to suppress protein processing and
CC nuclear translocation, and repress target gene expression.
CC {ECO:0000269|PubMed:21459323}.
CC -!- PTM: [Processed sterol regulatory element-binding protein 2]:
CC Ubiquitinated; the nuclear form has a rapid turnover and is rapidly
CC ubiquitinated and degraded by the proteasome in the nucleus.
CC {ECO:0000250|UniProtKB:Q12772}.
CC -!- DISRUPTION PHENOTYPE: Death around embryonic day 7-8.
CC {ECO:0000269|PubMed:11994399}.
CC -!- SIMILARITY: Belongs to the SREBP family. {ECO:0000305}.
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DR EMBL; AK155857; BAE33463.1; -; mRNA.
DR EMBL; AC105358; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF374267; AAK54763.1; -; mRNA.
DR EMBL; AF289715; AAG01859.2; -; mRNA.
DR CCDS; CCDS27683.1; -. [Q3U1N2-1]
DR RefSeq; NP_150087.1; NM_033218.1. [Q3U1N2-1]
DR AlphaFoldDB; Q3U1N2; -.
DR SMR; Q3U1N2; -.
DR BioGRID; 203496; 8.
DR IntAct; Q3U1N2; 3.
DR STRING; 10090.ENSMUSP00000023100; -.
DR ChEMBL; CHEMBL4630828; -.
DR iPTMnet; Q3U1N2; -.
DR PhosphoSitePlus; Q3U1N2; -.
DR EPD; Q3U1N2; -.
DR MaxQB; Q3U1N2; -.
DR PaxDb; Q3U1N2; -.
DR PeptideAtlas; Q3U1N2; -.
DR PRIDE; Q3U1N2; -.
DR ProteomicsDB; 261655; -. [Q3U1N2-1]
DR ProteomicsDB; 262680; -. [Q3U1N2-2]
DR Antibodypedia; 13093; 370 antibodies from 37 providers.
DR DNASU; 20788; -.
DR Ensembl; ENSMUST00000023100; ENSMUSP00000023100; ENSMUSG00000022463. [Q3U1N2-1]
DR Ensembl; ENSMUST00000229336; ENSMUSP00000155022; ENSMUSG00000022463. [Q3U1N2-2]
DR GeneID; 20788; -.
DR KEGG; mmu:20788; -.
DR UCSC; uc007wyi.1; mouse. [Q3U1N2-1]
DR UCSC; uc011zwr.1; mouse. [Q3U1N2-2]
DR CTD; 6721; -.
DR MGI; MGI:107585; Srebf2.
DR VEuPathDB; HostDB:ENSMUSG00000022463; -.
DR eggNOG; KOG2588; Eukaryota.
DR GeneTree; ENSGT00940000157339; -.
DR HOGENOM; CLU_008042_0_0_1; -.
DR InParanoid; Q3U1N2; -.
DR OMA; VCRWWTS; -.
DR OrthoDB; 330300at2759; -.
DR PhylomeDB; Q3U1N2; -.
DR TreeFam; TF313894; -.
DR Reactome; R-MMU-1655829; Regulation of cholesterol biosynthesis by SREBP (SREBF).
DR Reactome; R-MMU-191273; Cholesterol biosynthesis.
DR BioGRID-ORCS; 20788; 8 hits in 75 CRISPR screens.
DR ChiTaRS; Srebf2; mouse.
DR PRO; PR:Q3U1N2; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q3U1N2; protein.
DR Bgee; ENSMUSG00000022463; Expressed in embryonic brain and 243 other tissues.
DR ExpressionAtlas; Q3U1N2; baseline and differential.
DR Genevisible; Q3U1N2; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0032937; C:SREBP-SCAP-Insig complex; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0070888; F:E-box binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:MGI.
DR GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; IEA:Ensembl.
DR GO; GO:0009267; P:cellular response to starvation; ISO:MGI.
DR GO; GO:0042632; P:cholesterol homeostasis; IGI:MGI.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0090370; P:negative regulation of cholesterol efflux; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045542; P:positive regulation of cholesterol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0010886; P:positive regulation of cholesterol storage; ISO:MGI.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; IDA:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0009725; P:response to hormone; ISO:MGI.
DR GO; GO:0032933; P:SREBP signaling pathway; ISS:UniProtKB.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR003006; Ig/MHC_CS.
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 Activator; Alternative splicing; Cholesterol metabolism;
KW Cytoplasmic vesicle; DNA-binding; Endoplasmic reticulum; Golgi apparatus;
KW Isopeptide bond; Lipid metabolism; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Steroid metabolism; Sterol metabolism; Transcription;
KW Transcription regulation; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT CHAIN 1..1130
FT /note="Sterol regulatory element-binding protein 2"
FT /id="PRO_0000317059"
FT CHAIN 1..473
FT /note="Processed sterol regulatory element-binding protein
FT 2"
FT /evidence="ECO:0000250|UniProtKB:Q12772"
FT /id="PRO_0000317060"
FT TOPO_DOM 1..470
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 471..491
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 492..522
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 523..543
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 544..1130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 319..369
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..50
FT /note="Transcriptional activation (acidic)"
FT /evidence="ECO:0000250|UniProtKB:P36956"
FT REGION 53..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..480
FT /note="Interaction with LMNA"
FT /evidence="ECO:0000269|PubMed:11929849"
FT REGION 369..390
FT /note="Leucine-zipper"
FT COMPBIAS 53..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..131
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 457..458
FT /note="Cleavage; by caspase-3 and caspase-7"
FT /evidence="ECO:0000250|UniProtKB:Q12772"
FT SITE 473..474
FT /note="Cleavage; by MBTPS2"
FT /evidence="ECO:0000250|UniProtKB:Q12772"
FT SITE 511..512
FT /note="Cleavage; by MBTPS1"
FT /evidence="ECO:0000250|UniProtKB:Q12772"
FT MOD_RES 1087
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12772"
FT CROSSLNK 453
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q12772"
FT VAR_SEQ 57..96
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052658"
FT VAR_SEQ 1105..1130
FT /note="VGDRRSCSDCQQMIVKLGGGTAIAAS -> SCEDEGKTDCSELLPAKAFGSF
FT RASRTMGRAP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052659"
FT MUTAGEN 369..383
FT /note="LQQVNHKLRQENMVL->AQQVNHKARQENMVA: In L1.2.3A mutant;
FT reduced affinity for importin-beta."
FT /evidence="ECO:0000269|PubMed:11283257"
FT CONFLICT 334
FT /note="S -> F (in Ref. 3; AAK54763)"
FT /evidence="ECO:0000305"
FT CONFLICT 621
FT /note="R -> H (in Ref. 3; AAK54763)"
FT /evidence="ECO:0000305"
FT CONFLICT 698
FT /note="L -> P (in Ref. 3; AAK54763)"
FT /evidence="ECO:0000305"
FT CONFLICT 899
FT /note="E -> K (in Ref. 3; AAK54763)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1130 AA; 122911 MW; 052E858B0C3945F2 CRC64;
MDESSELGVL ETMETLTELG DELTLGDIDE MLQFVSNQVG EFPDLFSEQL CSSFPGGGSN
GGSGNNSSGR GNNGGATDPA VQRSFSQVPL STFSPSAASP QAPALQVKVS PTPPRATPVL
QPRPQPQPQP PAQLQQQTVM ITPTFSTAPQ TRIIQQPLIY QNAATSFQVL QPQVQSLVTS
PQVQPVTIQQ QVQTVQAQRV LTQTANGTLQ TLAPATVQTV AAPQVQQVPV LVQPQIIKTD
SLVLTTLKTD GSPVMAAVQN PALTALTAPI QTAALQVPTL VGSNGTILTT MPVMMGQEKV
PIKQVPGGVK QLDPPKEGER RTTHNIIEKR YRSSINDKII ELKDLVMGTD AKMHKSGVLR
KAIDYIKYLQ QVNHKLRQEN MVLKLANQKN KLLKGIDLGS LVDSDVDLKI DDFNQNVLLM
SPPASDSGSQ AGFSPYSIDS EPGSPLLDDA KVKDEPDSPP VALGMVDRSR ILLCVLTFLG
LSFNPLTSLL QWGGAHNTDQ HPYSGSGRSV LSLESGAGGW FDWMVPTLLL WLVNGVIVLS
VFVKLLVHGE PVIRPHSRPS VTFWRHRKQA DLDLAKGDFA AAAANLQTCL SVLGRALPTS
RLDLACSLSW NVIRYSLQKL RLVRWLLKKV FQRWRATPAT AAGFEDEAKS SARDAALAYH
RLHQLHITGK LPAGSACSDV HMALCAVNLA ECAEEKILPS TLIEIHLTAA MGLKTRCGGK
LGFLASYFLN RAQSLCGPEH STVPDSLRWL CHPLGQKFFM ERSWSIKSAA KESLYCAQRS
PADPIAQVHQ AFCKNLLERA VESLVKPQAK KKAGDQEEES CEFSSALEYL KLLHSFVDSV
GFVTSPFSSS SVLRSALGPD VICRWWTSAV TMAISWLQGD DAAVRSRFTE VERVPKALEV
TESPLVKAVF YTCRAMHASL SGKADGQQNS FCHCERASGH LWSSLNVSGT TSDPSLNHVI
QLFTCDLLLS LRTALWQKQA SASQLLGETY HASGTELAGF QRDLGSLRRL AHSFRPAYRK
VFLHEATVRL MAGASPTRTH QLLEHSLRRR PTQNTKHGEV DTWPGQRERA TAILLACRHL
PLSFLSSPGQ RAVLLAEAAR TLEKVGDRRS CSDCQQMIVK LGGGTAIAAS
