NRBF2_HUMAN
ID NRBF2_HUMAN Reviewed; 287 AA.
AC Q96F24; A6PW36; B4DWS0; Q86UR2; Q96NP6; Q9H0S9; Q9H2I2;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Nuclear receptor-binding factor 2;
DE Short=NRBF-2;
DE AltName: Full=Comodulator of PPAR and RXR;
GN Name=NRBF2; Synonyms=COPR;
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 1 AND 2), FUNCTION, MUTAGENESIS OF
RP 144-LEU-LEU-145, INTERACTION WITH PPARA; PPARD; PPARG; RARA; RARG AND RXRA,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Keratinocyte;
RX PubMed=15610520; DOI=10.1111/j.0022-202x.2004.23424.x;
RA Flores A.M., Li L., Aneskievich B.J.;
RT "Isolation and functional analysis of a keratinocyte-derived, ligand-
RT regulated nuclear receptor comodulator.";
RL J. Invest. Dermatol. 123:1092-1101(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Dendritic cell;
RA Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Cerebellum, and Esophagus;
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 GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph;
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=18619852; DOI=10.1016/j.mcn.2008.05.013;
RA Larsson J., Forsberg M., Brannvall K., Zhang X.Q., Enarsson M., Hedborg F.,
RA Forsberg-Nilsson K.;
RT "Nuclear receptor binding protein 2 is induced during neural progenitor
RT differentiation and affects cell survival.";
RL Mol. Cell. Neurosci. 39:32-39(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP INTERACTION WITH SCOC.
RX PubMed=22354037; DOI=10.1038/emboj.2012.36;
RA McKnight N.C., Jefferies H.B., Alemu E.A., Saunders R.E., Howell M.,
RA Johansen T., Tooze S.A.;
RT "Genome-wide siRNA screen reveals amino acid starvation-induced autophagy
RT requires SCOC and WAC.";
RL EMBO J. 31:1931-1946(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP FUNCTION, INTERACTION WITH PIK3R4, AND SUBUNIT.
RX PubMed=24785657; DOI=10.1042/bj20140515;
RA Cao Y., Wang Y., Abi Saab W.F., Yang F., Pessin J.E., Backer J.M.;
RT "NRBF2 regulates macroautophagy as a component of Vps34 Complex I.";
RL Biochem. J. 461:315-322(2014).
RN [16]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=25086043; DOI=10.1074/jbc.m114.561134;
RA Zhong Y., Morris D.H., Jin L., Patel M.S., Karunakaran S.K., Fu Y.J.,
RA Matuszak E.A., Weiss H.L., Chait B.T., Wang Q.J.;
RT "Nrbf2 protein suppresses autophagy by modulating Atg14L protein-containing
RT Beclin 1-Vps34 complex architecture and reducing intracellular
RT phosphatidylinositol-3 phosphate levels.";
RL J. Biol. Chem. 289:26021-26037(2014).
CC -!- FUNCTION: May modulate transcriptional activation by target nuclear
CC receptors. Can act as transcriptional activator (in vitro).
CC {ECO:0000269|PubMed:15610520}.
CC -!- FUNCTION: Involved in starvation-induced autophagy probably by its
CC association with PI3K complex I (PI3KC3-C1). However, effects has been
CC described variably. Involved in the induction of starvation-induced
CC autophagy (PubMed:24785657). Stabilzes PI3KC3-C1 assembly and enhances
CC ATG14-linked lipid kinase activity of PIK3C3 (By similarity). Proposed
CC to negatively regulate basal and starvation-induced autophagy and to
CC inhibit PIK3C3 activity by modulating interactions in PI3KC3-C1
CC (PubMed:25086043). May be involved in autophagosome biogenesis
CC (PubMed:25086043). May play a role in neural progenitor cell survival
CC during differentiation (By similarity). {ECO:0000250|UniProtKB:Q8VCQ3,
CC ECO:0000269|PubMed:24785657, ECO:0000269|PubMed:25086043}.
CC -!- SUBUNIT: Interacts with PPARA, PPARD and PPARG. Interacts with RARA,
CC RARG and RXRA in the presence of bound ligand (PubMed:15610520).
CC Interacts with SCOC (PubMed:22354037). Associates with the PI3K complex
CC I (PI3KC3-C1); the direct binding partner in the complex is reported
CC variably as PIK3R4 or ATG14 (PubMed:24785657).
CC {ECO:0000269|PubMed:15610520, ECO:0000269|PubMed:22354037,
CC ECO:0000269|PubMed:24785657, ECO:0000269|PubMed:25086043}.
CC -!- INTERACTION:
CC Q96F24; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-2362014, EBI-747505;
CC Q96F24; P24863: CCNC; NbExp=3; IntAct=EBI-2362014, EBI-395261;
CC Q96F24; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-2362014, EBI-396137;
CC Q96F24; O60341: KDM1A; NbExp=3; IntAct=EBI-2362014, EBI-710124;
CC Q96F24; Q8NEB9: PIK3C3; NbExp=12; IntAct=EBI-2362014, EBI-1056470;
CC Q96F24; Q99570: PIK3R4; NbExp=13; IntAct=EBI-2362014, EBI-1046979;
CC Q96F24; P54646: PRKAA2; NbExp=3; IntAct=EBI-2362014, EBI-1383852;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9QYK3}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9QYK3}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:25086043}. Cytoplasmic vesicle, autophagosome
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=COPR2, Comodulator of PPAR and RXR 2;
CC IsoId=Q96F24-1; Sequence=Displayed;
CC Name=2; Synonyms=COPR1, Comodulator of PPAR and RXR 1;
CC IsoId=Q96F24-2; Sequence=VSP_018488;
CC Name=3;
CC IsoId=Q96F24-3; Sequence=VSP_054555;
CC -!- TISSUE SPECIFICITY: Detected in keratinocytes, liver and placenta
CC (PubMed:15610520). Expressed in a subset of cells in pediatric
CC medulloblastoma (PubMed:18619852). {ECO:0000269|PubMed:15610520,
CC ECO:0000269|PubMed:18619852}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG44735.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY267839; AAP03081.1; -; mRNA.
DR EMBL; AY267840; AAP03082.1; -; mRNA.
DR EMBL; AF267866; AAG44735.1; ALT_FRAME; mRNA.
DR EMBL; AL136656; CAB66591.1; -; mRNA.
DR EMBL; AK054957; BAB70833.1; -; mRNA.
DR EMBL; AK301656; BAG63132.1; -; mRNA.
DR EMBL; AL590502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471083; EAW54241.1; -; Genomic_DNA.
DR EMBL; BC011707; AAH11707.1; -; mRNA.
DR CCDS; CCDS60537.1; -. [Q96F24-3]
DR CCDS; CCDS7268.1; -. [Q96F24-1]
DR RefSeq; NP_001269334.1; NM_001282405.1. [Q96F24-3]
DR RefSeq; NP_110386.2; NM_030759.4. [Q96F24-1]
DR PDB; 4ZEY; X-ray; 1.50 A; A=4-86.
DR PDBsum; 4ZEY; -.
DR AlphaFoldDB; Q96F24; -.
DR SMR; Q96F24; -.
DR BioGRID; 119009; 63.
DR IntAct; Q96F24; 29.
DR MINT; Q96F24; -.
DR STRING; 9606.ENSP00000277746; -.
DR ChEMBL; CHEMBL4295924; -.
DR GlyGen; Q96F24; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96F24; -.
DR PhosphoSitePlus; Q96F24; -.
DR BioMuta; NRBF2; -.
DR DMDM; 74731648; -.
DR EPD; Q96F24; -.
DR jPOST; Q96F24; -.
DR MassIVE; Q96F24; -.
DR MaxQB; Q96F24; -.
DR PaxDb; Q96F24; -.
DR PeptideAtlas; Q96F24; -.
DR PRIDE; Q96F24; -.
DR ProteomicsDB; 5374; -.
DR ProteomicsDB; 76486; -. [Q96F24-1]
DR ProteomicsDB; 76487; -. [Q96F24-2]
DR Antibodypedia; 28311; 331 antibodies from 30 providers.
DR DNASU; 29982; -.
DR Ensembl; ENST00000277746.11; ENSP00000277746.6; ENSG00000148572.16. [Q96F24-1]
DR Ensembl; ENST00000435510.6; ENSP00000397502.2; ENSG00000148572.16. [Q96F24-3]
DR GeneID; 29982; -.
DR KEGG; hsa:29982; -.
DR MANE-Select; ENST00000277746.11; ENSP00000277746.6; NM_030759.5; NP_110386.2.
DR UCSC; uc001jmj.6; human. [Q96F24-1]
DR CTD; 29982; -.
DR DisGeNET; 29982; -.
DR GeneCards; NRBF2; -.
DR HGNC; HGNC:19692; NRBF2.
DR HPA; ENSG00000148572; Low tissue specificity.
DR MIM; 616477; gene.
DR neXtProt; NX_Q96F24; -.
DR OpenTargets; ENSG00000148572; -.
DR PharmGKB; PA134946285; -.
DR VEuPathDB; HostDB:ENSG00000148572; -.
DR eggNOG; ENOG502QRE0; Eukaryota.
DR GeneTree; ENSGT00390000000984; -.
DR HOGENOM; CLU_098323_0_0_1; -.
DR InParanoid; Q96F24; -.
DR OMA; CEAMKLT; -.
DR OrthoDB; 1613014at2759; -.
DR PhylomeDB; Q96F24; -.
DR TreeFam; TF328627; -.
DR PathwayCommons; Q96F24; -.
DR Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
DR SignaLink; Q96F24; -.
DR SIGNOR; Q96F24; -.
DR BioGRID-ORCS; 29982; 112 hits in 1014 CRISPR screens.
DR ChiTaRS; NRBF2; human.
DR GeneWiki; NRBF2; -.
DR GenomeRNAi; 29982; -.
DR Pharos; Q96F24; Tbio.
DR PRO; PR:Q96F24; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q96F24; protein.
DR Bgee; ENSG00000148572; Expressed in buccal mucosa cell and 190 other tissues.
DR Genevisible; Q96F24; HS.
DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0035032; C:phosphatidylinositol 3-kinase complex, class III; IEA:Ensembl.
DR GO; GO:0006914; P:autophagy; IMP:GO_Central.
DR GO; GO:0043550; P:regulation of lipid kinase activity; IEA:Ensembl.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:Ensembl.
DR IDEAL; IID00676; -.
DR InterPro; IPR039679; NRBF2.
DR InterPro; IPR015056; NRBF2_C.
DR InterPro; IPR033393; NRBF2_MIT.
DR PANTHER; PTHR14964; PTHR14964; 1.
DR Pfam; PF08961; NRBF2; 1.
DR Pfam; PF17169; NRBF2_MIT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Autophagy; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..287
FT /note="Nuclear receptor-binding factor 2"
FT /id="PRO_0000235816"
FT REGION 83..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 168..209
FT /evidence="ECO:0000255"
FT MOTIF 141..145
FT /note="Nuclear receptor interaction motif"
FT COMPBIAS 105..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195"
FT VAR_SEQ 1..38
FT /note="MEVMEGPLNLAHQQSRRADRLLAAGKYEEAISCHKKAA -> MFPGATTPLP
FT KAAAYPGVYGSNGRTPQP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054555"
FT VAR_SEQ 90..139
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15610520"
FT /id="VSP_018488"
FT MUTAGEN 144..145
FT /note="LL->AA: Decreased interaction with nuclear
FT receptors."
FT /evidence="ECO:0000269|PubMed:15610520"
FT CONFLICT 150
FT /note="E -> G (in Ref. 4; BAB70833)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="F -> L (in Ref. 3; CAB66591)"
FT /evidence="ECO:0000305"
FT HELIX 7..23
FT /evidence="ECO:0007829|PDB:4ZEY"
FT HELIX 27..45
FT /evidence="ECO:0007829|PDB:4ZEY"
FT HELIX 51..85
FT /evidence="ECO:0007829|PDB:4ZEY"
SQ SEQUENCE 287 AA; 32378 MW; 91EC0407F5108806 CRC64;
MEVMEGPLNL AHQQSRRADR LLAAGKYEEA ISCHKKAAAY LSEAMKLTQS EQAHLSLELQ
RDSHMKQLLL IQERWKRAQR EERLKAQQNT DKDAAAHLQT SHKPSAEDAE GQSPLSQKYS
PSTEKCLPEI QGIFDRDPDT LLYLLQQKSE PAEPCIGSKA PKDDKTIIEE QATKIADLKR
HVEFLVAENE RLRKENKQLK AEKARLLKGP IEKELDVDAD FVETSELWSL PPHAETATAS
STWQKFAANT GKAKDIPIPN LPPLDFPSPE LPLMELSEDI LKGFMNN
