EDF1_HUMAN
ID EDF1_HUMAN Reviewed; 148 AA.
AC O60869; Q5T5T2; Q9UIM1;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Endothelial differentiation-related factor 1;
DE Short=EDF-1;
DE AltName: Full=Multiprotein-bridging factor 1;
DE Short=MBF1;
GN Name=EDF1;
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), TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, INDUCTION, AND FUNCTION.
RX PubMed=9813014; DOI=10.1074/jbc.273.47.31119;
RA Dragoni I., Mariotti M., Consalez G.G., Soria M.R., Maier J.A.M.;
RT "EDF-1, a novel gene product down-regulated in human endothelial cell
RT differentiation.";
RL J. Biol. Chem. 273:31119-31124(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY,
RP INTERACTION WITH TBP; NR5A1; FOS; JUN AND ATF1, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RX PubMed=10567391; DOI=10.1074/jbc.274.48.34196;
RA Kabe Y., Goto M., Shima D., Imai T., Wada T., Morohashi K., Shirakawa M.,
RA Hirose S., Handa H.;
RT "The role of human MBF1 as a transcriptional coactivator.";
RL J. Biol. Chem. 274:34196-34202(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pancreas;
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 PROTEIN SEQUENCE OF 2-13 AND 99-113, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [8]
RP INTERACTION WITH CALM AND TBP, MUTAGENESIS OF THR-40; THR-58; THR-91 AND
RP SER-111, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=10816571; DOI=10.1074/jbc.m001928200;
RA Mariotti M., De Benedictis L., Avon E., Maier J.A.M.;
RT "Interaction between endothelial differentiation-related factor-1 and
RT calmodulin in vitro and in vivo.";
RL J. Biol. Chem. 275:24047-24051(2000).
RN [9]
RP INTERACTION WITH NR5A2; NR1H3; PPARG AND TFIID COMPLEX, TISSUE SPECIFICITY,
RP AND FUNCTION.
RX PubMed=12040021; DOI=10.1210/mend.16.6.0843;
RA Brendel C., Gelman L., Auwerx J.;
RT "Multiprotein bridging factor-1 (MBF-1) is a cofactor for nuclear receptors
RT that regulate lipid metabolism.";
RL Mol. Endocrinol. 16:1367-1377(2002).
RN [10]
RP MUTAGENESIS OF THR-65; THR-74 AND SER-87, INTERACTION WITH TBP AND CALM,
RP PHOSPHORYLATION, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=15112053; DOI=10.1007/s00018-004-4016-0;
RA Ballabio E., Mariotti M., De Benedictis L., Maier J.A.M.;
RT "The dual role of endothelial differentiation-related factor-1 in the
RT cytosol and nucleus: modulation by protein kinase A.";
RL Cell. Mol. Life Sci. 61:1069-1074(2004).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND IDENTIFICATION BY MASS
RP 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP METHYLATION [LARGE SCALE ANALYSIS] AT LYS-25, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [18]
RP STRUCTURE BY NMR OF 71-148.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structures of the HTH domain of human EDF-1 protein.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Transcriptional coactivator stimulating NR5A1 and ligand-
CC dependent NR1H3/LXRA and PPARG transcriptional activities. Enhances the
CC DNA-binding activity of ATF1, ATF2, CREB1 and NR5A1. Regulates nitric
CC oxid synthase activity probably by sequestering calmodulin in the
CC cytoplasm. May function in endothelial cells differentiation, hormone-
CC induced cardiomyocytes hypertrophy and lipid metabolism.
CC {ECO:0000269|PubMed:10567391, ECO:0000269|PubMed:12040021,
CC ECO:0000269|PubMed:15112053, ECO:0000269|PubMed:9813014}.
CC -!- SUBUNIT: Interacts with TBP and the transcription factor IID (TFIID)
CC complex, NR5A2, NR1H3 and PPARG. Interaction with TBP is regulated by
CC phosphorylation. Binds NR5A1, ATF1, FOS and JUN via their conserved
CC basic region. Binding to calmodulin is regulated by calcium and
CC phosphorylation of the IQ motif. {ECO:0000269|PubMed:10567391,
CC ECO:0000269|PubMed:10816571, ECO:0000269|PubMed:12040021,
CC ECO:0000269|PubMed:15112053}.
CC -!- INTERACTION:
CC O60869; P03372: ESR1; NbExp=3; IntAct=EBI-781301, EBI-78473;
CC O60869; P42858: HTT; NbExp=6; IntAct=EBI-781301, EBI-466029;
CC O60869; P50222: MEOX2; NbExp=3; IntAct=EBI-781301, EBI-748397;
CC O60869; Q13133: NR1H3; NbExp=4; IntAct=EBI-781301, EBI-781356;
CC O60869; O00482: NR5A2; NbExp=2; IntAct=EBI-781301, EBI-781320;
CC O60869; P37231: PPARG; NbExp=4; IntAct=EBI-781301, EBI-781384;
CC O60869; P03495: NS; Xeno; NbExp=2; IntAct=EBI-781301, EBI-2548993;
CC O60869-1; P20226: TBP; NbExp=2; IntAct=EBI-781310, EBI-355371;
CC O60869-1; Q04752: NR5A1; Xeno; NbExp=4; IntAct=EBI-781310, EBI-850837;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Also nuclear upon
CC binding to NR5A1 and treatment of cells with TPA or forskolin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Alpha;
CC IsoId=O60869-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta;
CC IsoId=O60869-2; Sequence=VSP_013336;
CC Name=3;
CC IsoId=O60869-3; Sequence=VSP_054701;
CC -!- TISSUE SPECIFICITY: Expressed in brain, liver, lung, kidney and heart
CC (at protein level). Ubiquitously expressed. More abundant in heart,
CC pancreas, liver, intestine and adipose tissues.
CC {ECO:0000269|PubMed:10567391, ECO:0000269|PubMed:12040021,
CC ECO:0000269|PubMed:9813014}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal tissues. More abundant in
CC kidney. {ECO:0000269|PubMed:9813014}.
CC -!- INDUCTION: Down-regulated by HIV-1 Tat or phorbol ester (TPA) treatment
CC in endothelial cells (at mRNA and protein levels).
CC {ECO:0000269|PubMed:9813014}.
CC -!- DOMAIN: The IQ motif, which is involved in calmodulin binding, overlaps
CC with the binding domain for nuclear receptors and transcription
CC factors. Its phosphorylation probably allows a switch between the two
CC activities of the protein (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated (by PKA and PKC). {ECO:0000269|PubMed:10816571,
CC ECO:0000269|PubMed:15112053}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ005259; CAA06446.1; -; mRNA.
DR EMBL; AB002282; BAA88073.1; -; mRNA.
DR EMBL; AB002283; BAA88074.1; -; mRNA.
DR EMBL; CR541914; CAG46712.1; -; mRNA.
DR EMBL; BT009863; AAP88865.1; -; mRNA.
DR EMBL; AL355987; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015500; AAH15500.1; -; mRNA.
DR CCDS; CCDS65193.1; -. [O60869-3]
DR CCDS; CCDS7011.1; -. [O60869-1]
DR CCDS; CCDS7012.1; -. [O60869-2]
DR RefSeq; NP_001268226.1; NM_001281297.1. [O60869-3]
DR RefSeq; NP_001268227.1; NM_001281298.1.
DR RefSeq; NP_001268228.1; NM_001281299.1.
DR RefSeq; NP_003783.1; NM_003792.3. [O60869-1]
DR RefSeq; NP_694880.1; NM_153200.2. [O60869-2]
DR PDB; 1X57; NMR; -; A=71-148.
DR PDB; 6ZVH; EM; 2.90 A; i=24-133.
DR PDBsum; 1X57; -.
DR PDBsum; 6ZVH; -.
DR AlphaFoldDB; O60869; -.
DR BMRB; O60869; -.
DR SMR; O60869; -.
DR BioGRID; 114260; 59.
DR IntAct; O60869; 28.
DR MINT; O60869; -.
DR STRING; 9606.ENSP00000224073; -.
DR ChEMBL; CHEMBL4295670; -.
DR GlyGen; O60869; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O60869; -.
DR PhosphoSitePlus; O60869; -.
DR BioMuta; EDF1; -.
DR EPD; O60869; -.
DR jPOST; O60869; -.
DR MassIVE; O60869; -.
DR MaxQB; O60869; -.
DR PaxDb; O60869; -.
DR PeptideAtlas; O60869; -.
DR PRIDE; O60869; -.
DR ProteomicsDB; 49636; -. [O60869-1]
DR ProteomicsDB; 49637; -. [O60869-2]
DR TopDownProteomics; O60869-1; -. [O60869-1]
DR Antibodypedia; 18815; 221 antibodies from 33 providers.
DR DNASU; 8721; -.
DR Ensembl; ENST00000224073.6; ENSP00000224073.1; ENSG00000107223.13. [O60869-1]
DR Ensembl; ENST00000371648.4; ENSP00000360711.4; ENSG00000107223.13. [O60869-2]
DR Ensembl; ENST00000371649.5; ENSP00000360712.1; ENSG00000107223.13. [O60869-3]
DR GeneID; 8721; -.
DR KEGG; hsa:8721; -.
DR MANE-Select; ENST00000224073.6; ENSP00000224073.1; NM_003792.4; NP_003783.1.
DR UCSC; uc004cjt.3; human. [O60869-1]
DR CTD; 8721; -.
DR DisGeNET; 8721; -.
DR GeneCards; EDF1; -.
DR HGNC; HGNC:3164; EDF1.
DR HPA; ENSG00000107223; Low tissue specificity.
DR MIM; 605107; gene.
DR neXtProt; NX_O60869; -.
DR OpenTargets; ENSG00000107223; -.
DR PharmGKB; PA27604; -.
DR VEuPathDB; HostDB:ENSG00000107223; -.
DR eggNOG; KOG3398; Eukaryota.
DR GeneTree; ENSGT00390000008519; -.
DR HOGENOM; CLU_112609_0_1_1; -.
DR InParanoid; O60869; -.
DR OMA; NKAHQGT; -.
DR OrthoDB; 1571466at2759; -.
DR PhylomeDB; O60869; -.
DR TreeFam; TF300064; -.
DR PathwayCommons; O60869; -.
DR SignaLink; O60869; -.
DR SIGNOR; O60869; -.
DR BioGRID-ORCS; 8721; 88 hits in 1107 CRISPR screens.
DR ChiTaRS; EDF1; human.
DR EvolutionaryTrace; O60869; -.
DR GeneWiki; EDF1; -.
DR GenomeRNAi; 8721; -.
DR Pharos; O60869; Tbio.
DR PRO; PR:O60869; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; O60869; protein.
DR Bgee; ENSG00000107223; Expressed in parotid gland and 202 other tissues.
DR Genevisible; O60869; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0001094; F:TFIID-class transcription factor complex binding; IDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IMP:UniProtKB.
DR GO; GO:0045446; P:endothelial cell differentiation; TAS:UniProtKB.
DR GO; GO:0043388; P:positive regulation of DNA binding; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; TAS:UniProtKB.
DR GO; GO:0019216; P:regulation of lipid metabolic process; TAS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:UniProtKB.
DR CDD; cd00093; HTH_XRE; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR013729; MBF1_N.
DR Pfam; PF01381; HTH_3; 1.
DR Pfam; PF08523; MBF1; 1.
DR SMART; SM00530; HTH_XRE; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR PROSITE; PS50943; HTH_CROC1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing;
KW Calmodulin-binding; Cytoplasm; Developmental protein; Differentiation;
KW Direct protein sequencing; DNA-binding; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712"
FT CHAIN 2..148
FT /note="Endothelial differentiation-related factor 1"
FT /id="PRO_0000149795"
FT DOMAIN 81..135
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT DNA_BIND 92..111
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT REGION 33..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 37..113
FT /note="Interaction with NR5A2, PPARG and NR1H3"
FT /evidence="ECO:0000269|PubMed:12040021"
FT REGION 69..108
FT /note="Interaction with TBP and NR5A1"
FT /evidence="ECO:0000269|PubMed:10567391"
FT MOTIF 81..88
FT /note="IQ motif"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 25
FT /note="N6-methyllysine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 129..148
FT /note="GLKLRGKDIGKPIEKGPRAK -> DVGTRSARVLRAQ (in isoform
FT 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_054701"
FT VAR_SEQ 130..148
FT /note="LKLRGKDIGKPIEKGPRAK -> ECPSTLRRVR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10567391"
FT /id="VSP_013336"
FT MUTAGEN 40
FT /note="T->D: Loss of interaction with CALM; when associated
FT with D-58; D-91 and D-111."
FT /evidence="ECO:0000269|PubMed:10816571"
FT MUTAGEN 58
FT /note="T->D: Loss of interaction with CALM; when associated
FT with D-40; D-91 and D-111."
FT /evidence="ECO:0000269|PubMed:10816571"
FT MUTAGEN 65
FT /note="T->D: No effect on CALM-binding. No effect; when
FT associated with D-74."
FT /evidence="ECO:0000269|PubMed:15112053"
FT MUTAGEN 74
FT /note="T->D: No effect on CALM-binding. No effect; when
FT associated with D-65."
FT /evidence="ECO:0000269|PubMed:15112053"
FT MUTAGEN 87
FT /note="S->A: No effect on CALM-binding."
FT /evidence="ECO:0000269|PubMed:15112053"
FT MUTAGEN 87
FT /note="S->D: Loss of interaction with CALM and higher
FT affinity for TBP. Same effect; when associated with D-65
FT and D-74."
FT /evidence="ECO:0000269|PubMed:15112053"
FT MUTAGEN 91
FT /note="T->A: No effect on CALM-binding."
FT /evidence="ECO:0000269|PubMed:10816571"
FT MUTAGEN 91
FT /note="T->D: Partial loss of interaction with CALM.
FT Complete loss of interaction; when associated with D-40; D-
FT 58 and D-111."
FT /evidence="ECO:0000269|PubMed:10816571"
FT MUTAGEN 111
FT /note="S->D: Loss of interaction with CALM; when associated
FT with D-40; D-58 and D-91."
FT /evidence="ECO:0000269|PubMed:10816571"
FT HELIX 25..32
FT /evidence="ECO:0007829|PDB:6ZVH"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:6ZVH"
FT HELIX 75..86
FT /evidence="ECO:0007829|PDB:6ZVH"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:6ZVH"
FT HELIX 92..98
FT /evidence="ECO:0007829|PDB:6ZVH"
FT HELIX 103..110
FT /evidence="ECO:0007829|PDB:6ZVH"
FT HELIX 118..128
FT /evidence="ECO:0007829|PDB:6ZVH"
FT TURN 135..138
FT /evidence="ECO:0007829|PDB:1X57"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:1X57"
SQ SEQUENCE 148 AA; 16369 MW; ADC2C5384BF85C11 CRC64;
MAESDWDTVT VLRKKGPTAA QAKSKQAILA AQRRGEDVET SKKWAAGQNK QHSITKNTAK
LDRETEELHH DRVTLEVGKV IQQGRQSKGL TQKDLATKIN EKPQVIADYE SGRAIPNNQV
LGKIERAIGL KLRGKDIGKP IEKGPRAK
