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Steroid hormone receptor ERR1 (Estrogen receptor-like 1) (Estrogen-related receptor alpha) (ERR-alpha) (Nuclear receptor subfamily 3 group B member 1)

 ERR1_HUMAN              Reviewed;         423 AA.
P11474; Q14514;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 3.
05-DEC-2018, entry version 208.
RecName: Full=Steroid hormone receptor ERR1;
AltName: Full=Estrogen receptor-like 1;
AltName: Full=Estrogen-related receptor alpha;
Short=ERR-alpha;
AltName: Full=Nuclear receptor subfamily 3 group B member 1;
Name=ESRRA; Synonyms=ERR1, ESRL1, NR3B1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Kidney;
PubMed=3267207; DOI=10.1038/331091a0;
Giguere V., Yang N., Segui P., Evans R.M.;
"Identification of a new class of steroid hormone receptors.";
Nature 331:91-94(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Uterus;
PubMed=8621448; DOI=10.1074/jbc.271.10.5795;
Yang N., Shigeta H., Shi H., Teng C.T.;
"Estrogen-related receptor, hERR1, modulates estrogen receptor-
mediated response of human lactoferrin gene promoter.";
J. Biol. Chem. 271:5795-5804(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[4]
PROTEIN SEQUENCE OF 69-76.
PubMed=8224847; DOI=10.1101/gad.7.11.2206;
Wiley S.R., Kraus R.J., Zuo F., Murray E.E., Loritz K., Mertz J.E.;
"SV40 early-to-late switch involves titration of cellular
transcriptional repressors.";
Genes Dev. 7:2206-2219(1993).
[5]
FUNCTION.
PubMed=9271417; DOI=10.1128/MCB.17.9.5400;
Sladek R., Bader J.-A., Giguere V.;
"The orphan nuclear receptor estrogen-related receptor alpha is a
transcriptional regulator of the human medium-chain acyl coenzyme A
dehydrogenase gene.";
Mol. Cell. Biol. 17:5400-5409(1997).
[6]
INTERACTION WITH PPARGC1A, INDUCTION, AND FUNCTION.
PubMed=12522104; DOI=10.1074/jbc.M212923200;
Schreiber S.N., Knutti D., Brogli K., Uhlmann T., Kralli A.;
"The transcriptional coactivator PGC-1 regulates the expression and
activity of the orphan nuclear receptor estrogen-related receptor
alpha (ERRalpha).";
J. Biol. Chem. 278:9013-9018(2003).
[7]
DNA-BINDING SPECIFICITY, INTERACTION WITH PPARGC1A, HOMODIMERIZATION,
FUNCTION, AND MUTAGENESIS OF SER-118 AND THR-124.
PubMed=16150865; DOI=10.1210/me.2005-0313;
Barry J.B., Laganiere J., Giguere V.;
"A single nucleotide in an estrogen-related receptor alpha site can
dictate mode of binding and peroxisome proliferator-activated receptor
gamma coactivator 1alpha activation of target promoters.";
Mol. Endocrinol. 20:302-310(2006).
[8]
SUMOYLATION AT LYS-14 AND LYS-403, PHOSPHORYLATION AT SER-19 AND
SER-22, FUNCTION, AND MUTAGENESIS OF LYS-14; SER-19; SER-22; LYS-403;
LEU-413 AND LEU-418.
PubMed=17676930; DOI=10.1021/bi700316g;
Vu E.H., Kraus R.J., Mertz J.E.;
"Phosphorylation-dependent sumoylation of estrogen-related receptor
alpha1.";
Biochemistry 46:9795-9804(2007).
[9]
SUMOYLATION AT LYS-14 AND LYS-403, PHOSPHORYLATION AT SER-19 AND
SER-22, INTERACTION WITH PIAS4, FUNCTION, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF LYS-14; SER-19; SER-22 AND LYS-403.
PubMed=18063693; DOI=10.1210/me.2007-0357;
Tremblay A.M., Wilson B.J., Yang X.-J., Giguere V.;
"Phosphorylation-dependent sumoylation regulates estrogen-related
receptor-alpha and -gamma transcriptional activity through a synergy
control motif.";
Mol. Endocrinol. 22:570-584(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-22, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
ACETYLATION AT LYS-129; LYS-138; LYS-160 AND LYS-162 BY PCAF/KAT2B,
MUTAGENESIS OF LYS-129; LYS-138; LYS-160 AND LYS-162, AND
DEACETYLATION BY SIRT1 AND HDAC8.
PubMed=20484414; DOI=10.1210/me.2009-0441;
Wilson B.J., Tremblay A.M., Deblois G., Sylvain-Drolet G., Giguere V.;
"An acetylation switch modulates the transcriptional activity of
estrogen-related receptor alpha.";
Mol. Endocrinol. 24:1349-1358(2010).
[12]
INTERACTION WITH MAPK15, AND SUBCELLULAR LOCATION.
PubMed=21190936; DOI=10.1074/jbc.M110.179523;
Rossi M., Colecchia D., Iavarone C., Strambi A., Piccioni F.,
Verrotti di Pianella A., Chiariello M.;
"Extracellular signal-regulated kinase 8 (ERK8) controls estrogen-
related receptor alpha (ERRalpha) cellular localization and inhibits
its transcriptional activity.";
J. Biol. Chem. 286:8507-8522(2011).
[13]
FUNCTION.
PubMed=23836911; DOI=10.1074/jbc.M113.489674;
Cho Y., Hazen B.C., Russell A.P., Kralli A.;
"Peroxisome proliferator-activated receptor gamma coactivator 1 (PGC-
1)- and estrogen-related receptor (ERR)-induced regulator in muscle 1
(Perm1) is a tissue-specific regulator of oxidative capacity in
skeletal muscle cells.";
J. Biol. Chem. 288:25207-25218(2013).
[14]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-189 AND LYS-403, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[15]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-403, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[16]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-189 AND LYS-403, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[17]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 193-423 IN COMPLEX WITH THE
L3 SITE-CONTAINING PEPTIDE OF COACTIVATOR PPARGC1A, HOMODIMERIZATION,
AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=15337744; DOI=10.1074/jbc.M407999200;
Kallen J., Schlaeppi J.-M., Bitsch F., Filipuzzi I., Schilb A.,
Riou V., Graham A., Strauss A., Geiser M., Fournier B.;
"Evidence for ligand-independent transcriptional activation of the
human estrogen-related receptor alpha (ERRalpha): crystal structure of
ERRalpha ligand binding domain in complex with peroxisome
proliferator-activated receptor coactivator-1alpha.";
J. Biol. Chem. 279:49330-49337(2004).
[18]
X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF 180-423 IN COMPLEX WITH THE
L3 SITE-CONTAINING PEPTIDE OF COACTIVATOR PPARGC1A, INTERACTION WITH
PPARGC1A, AND MUTAGENESIS OF 258-MET--GLN-262; SER-259; ARG-315;
ASP-338; HIS-341; GLU-343 AND 421-MET--ASP-423.
PubMed=18441008; DOI=10.1074/jbc.M801920200;
Greschik H., Althage M., Flaig R., Sato Y., Chavant V.,
Peluso-Iltis C., Choulier L., Cronet P., Rochel N., Schuele R.,
Stroemstedt P.E., Moras D.;
"Communication between the ERRalpha homodimer interface and the PGC-
1alpha binding surface via the helix 8-9 loop.";
J. Biol. Chem. 283:20220-20230(2008).
-!- FUNCTION: Binds to an ERR-alpha response element (ERRE) containing
a single consensus half-site, 5'-TNAAGGTCA-3'. Can bind to the
medium-chain acyl coenzyme A dehydrogenase (MCAD) response element
NRRE-1 and may act as an important regulator of MCAD promoter.
Binds to the C1 region of the lactoferrin gene promoter. Requires
dimerization and the coactivator, PGC-1A, for full activity. The
ERRalpha/PGC1alpha complex is a regulator of energy metabolism.
Induces the expression of PERM1 in the skeletal muscle.
{ECO:0000269|PubMed:12522104, ECO:0000269|PubMed:16150865,
ECO:0000269|PubMed:17676930, ECO:0000269|PubMed:18063693,
ECO:0000269|PubMed:23836911, ECO:0000269|PubMed:9271417}.
-!- SUBUNIT: Binds DNA as a monomer or a homodimer. Interacts (via the
AF2 domain) with coactivator PPARGC1A (via the L3 motif); the
interaction greatly enhances transcriptional activity of genes
involved in energy metabolism. Interacts with PIAS4; the
interaction enhances sumoylation. Interacts with MAPK15; promotes
re-localization of ESRRA to the cytoplasm through a XPO1-dependent
mechanism then inhibits ESRRA transcriptional activity.
{ECO:0000269|PubMed:12522104, ECO:0000269|PubMed:15337744,
ECO:0000269|PubMed:16150865, ECO:0000269|PubMed:18063693,
ECO:0000269|PubMed:18441008}.
-!- INTERACTION:
Q16665:HIF1A; NbExp=3; IntAct=EBI-372412, EBI-447269;
Q8N2W9:PIAS4; NbExp=3; IntAct=EBI-372412, EBI-473160;
Q9UBK2:PPARGC1A; NbExp=19; IntAct=EBI-372412, EBI-765486;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00407, ECO:0000269|PubMed:18063693,
ECO:0000269|PubMed:21190936}. Cytoplasm
{ECO:0000269|PubMed:21190936}. Note=Co-localizes to the cytoplasm
only in presence of MAPK15. {ECO:0000269|PubMed:21190936}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P11474-1; Sequence=Displayed;
Name=2;
IsoId=P11474-2; Sequence=VSP_035756;
Note=No experimental confirmation available.;
-!- INDUCTION: Induced by PGC1alpha in a number of specific cell types
including heart, kidney and muscle. {ECO:0000269|PubMed:12522104}.
-!- PTM: Phosphorylation on Ser-19 enhances sumoylation on Lys-14
increasing repression of transcriptional activity.
{ECO:0000269|PubMed:17676930, ECO:0000269|PubMed:18063693}.
-!- PTM: Sumoylated with SUMO2. Main site is Lys-14 which is enhanced
by phosphorylation on Ser-19, cofactor activation, and by
interaction with PIAS4. Sumoylation enhances repression of
transcriptional activity, but has no effect on subcellular
location nor on DNA binding. {ECO:0000269|PubMed:17676930,
ECO:0000269|PubMed:18063693}.
-!- PTM: Reversibly acetylated. Acetylation by PCAF/KAT2 at Lys-129,
Lys-138, Lys-160 and Lys-162 and PCAF/KAT2 decreases
transcriptional activity probably by inhibiting DNA-binding
activity; deacetylation involves SIRT1 and HDAC8 and increases
DNA-binding. {ECO:0000269|PubMed:20484414}.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB17015.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAA35778.1; Type=Frameshift; Positions=345, 354; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/ESRRAID44408ch11q13.html";
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EMBL; X51416; CAA35778.1; ALT_FRAME; mRNA.
EMBL; L38487; AAB17015.1; ALT_INIT; mRNA.
EMBL; AP001453; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS41667.1; -. [P11474-1]
CCDS; CCDS60830.1; -. [P11474-2]
PIR; A29345; A29345.
RefSeq; NP_001269379.1; NM_001282450.1. [P11474-1]
RefSeq; NP_001269380.1; NM_001282451.1. [P11474-2]
RefSeq; NP_004442.3; NM_004451.4. [P11474-1]
UniGene; Hs.110849; -.
PDB; 1XB7; X-ray; 2.50 A; A=194-423.
PDB; 2PJL; X-ray; 2.30 A; A/B=193-423.
PDB; 3D24; X-ray; 2.11 A; A/C=192-423.
PDB; 3K6P; X-ray; 2.00 A; A=193-423.
PDBsum; 1XB7; -.
PDBsum; 2PJL; -.
PDBsum; 3D24; -.
PDBsum; 3K6P; -.
ProteinModelPortal; P11474; -.
SMR; P11474; -.
BioGrid; 108405; 38.
DIP; DIP-35053N; -.
IntAct; P11474; 28.
MINT; P11474; -.
STRING; 9606.ENSP00000000442; -.
BindingDB; P11474; -.
ChEMBL; CHEMBL3429; -.
DrugBank; DB06833; 1-CYCLOHEXYL-N-{[1-(4-METHYLPHENYL)-1H-INDOL-3-YL]METHYL}METHANAMINE.
DrugBank; DB00197; Troglitazone.
GuidetoPHARMACOLOGY; 622; -.
iPTMnet; P11474; -.
PhosphoSitePlus; P11474; -.
DMDM; 215274146; -.
EPD; P11474; -.
PaxDb; P11474; -.
PeptideAtlas; P11474; -.
PRIDE; P11474; -.
ProteomicsDB; 52781; -.
ProteomicsDB; 52782; -. [P11474-2]
DNASU; 2101; -.
Ensembl; ENST00000000442; ENSP00000000442; ENSG00000173153. [P11474-1]
Ensembl; ENST00000405666; ENSP00000384851; ENSG00000173153. [P11474-1]
Ensembl; ENST00000406310; ENSP00000385971; ENSG00000173153. [P11474-2]
GeneID; 2101; -.
KEGG; hsa:2101; -.
UCSC; uc001nzr.3; human. [P11474-1]
CTD; 2101; -.
DisGeNET; 2101; -.
EuPathDB; HostDB:ENSG00000173153.13; -.
GeneCards; ESRRA; -.
HGNC; HGNC:3471; ESRRA.
HPA; HPA053785; -.
MIM; 601998; gene.
neXtProt; NX_P11474; -.
OpenTargets; ENSG00000173153; -.
PharmGKB; PA27887; -.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
GeneTree; ENSGT00940000160341; -.
HOGENOM; HOG000233467; -.
HOVERGEN; HBG108344; -.
InParanoid; P11474; -.
KO; K08552; -.
OMA; CHSGHKE; -.
OrthoDB; EOG091G0DYP; -.
PhylomeDB; P11474; -.
TreeFam; TF323751; -.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
SignaLink; P11474; -.
SIGNOR; P11474; -.
EvolutionaryTrace; P11474; -.
GeneWiki; Estrogen-related_receptor_alpha; -.
GenomeRNAi; 2101; -.
PRO; PR:P11474; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000173153; Expressed in 207 organ(s), highest expression level in apex of heart.
CleanEx; HS_ESRRA; -.
ExpressionAtlas; P11474; baseline and differential.
Genevisible; P11474; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0001650; C:fibrillar center; IDA:HPA.
GO; GO:0045171; C:intercellular bridge; IDA:HPA.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
GO; GO:0004879; F:nuclear receptor activity; TAS:ProtInc.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0001077; F:proximal promoter DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
GO; GO:0001078; F:proximal promoter DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0005496; F:steroid binding; IEA:InterPro.
GO; GO:0003707; F:steroid hormone receptor activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0051216; P:cartilage development; IEA:Ensembl.
GO; GO:0007005; P:mitochondrion organization; TAS:Reactome.
GO; GO:1900078; P:positive regulation of cellular response to insulin stimulus; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
GO; GO:0042127; P:regulation of cell proliferation; IEA:Ensembl.
GO; GO:0045667; P:regulation of osteoblast differentiation; IEA:Ensembl.
GO; GO:0045670; P:regulation of osteoclast differentiation; IEA:Ensembl.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR035500; NHR_like_dom_sf.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR027289; Oest-rel_rcp.
InterPro; IPR024178; Oest_rcpt/oest-rel_rcp.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF00105; zf-C4; 1.
PIRSF; PIRSF002527; ER-like_NR; 1.
PIRSF; PIRSF500939; ERR1-2-3; 1.
PRINTS; PR00398; STRDHORMONER.
PRINTS; PR00047; STROIDFINGER.
SMART; SM00430; HOLI; 1.
SMART; SM00399; ZnF_C4; 1.
SUPFAM; SSF48508; SSF48508; 1.
PROSITE; PS51843; NR_LBD; 1.
PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; DNA-binding; Isopeptide bond;
Metal-binding; Nucleus; Phosphoprotein; Receptor; Reference proteome;
Transcription; Transcription regulation; Ubl conjugation; Zinc;
Zinc-finger.
CHAIN 1 423 Steroid hormone receptor ERR1.
/FTId=PRO_0000053660.
DOMAIN 193 421 NR LBD. {ECO:0000255|PROSITE-
ProRule:PRU01189}.
DNA_BIND 76 151 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 79 99 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 115 134 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
REGION 1 76 Repressor domain.
REGION 403 423 AF-2 domain.
SITE 124 124 Required for DNA-dependent dimerization.
MOD_RES 19 19 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:17676930,
ECO:0000269|PubMed:18063693}.
MOD_RES 22 22 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:17676930,
ECO:0000269|PubMed:18063693}.
MOD_RES 129 129 N6-acetyllysine; by PCAF/KAT2B.
{ECO:0000269|PubMed:20484414}.
MOD_RES 138 138 N6-acetyllysine; by PCAF/KAT2B.
{ECO:0000269|PubMed:20484414}.
MOD_RES 160 160 N6-acetyllysine; by PCAF/KAT2B.
{ECO:0000269|PubMed:20484414}.
MOD_RES 162 162 N6-acetyllysine; by PCAF/KAT2B.
{ECO:0000269|PubMed:20484414}.
CROSSLNK 14 14 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:17676930,
ECO:0000269|PubMed:18063693}.
CROSSLNK 189 189 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 403 403 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000269|PubMed:17676930,
ECO:0000269|PubMed:18063693}.
CROSSLNK 403 403 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 191 191 Missing (in isoform 2).
{ECO:0000303|PubMed:8621448}.
/FTId=VSP_035756.
MUTAGEN 14 14 K->R: Some loss of sumoylation. Complete
loss of sumoylation; when associated with
R-403. {ECO:0000269|PubMed:17676930,
ECO:0000269|PubMed:18063693}.
MUTAGEN 19 19 S->A: 50% loss of phosphorylation but
represses transactivation activity in the
absence of coactivator. Almost complete
loss of phosphorylation and 2-fold loss
of repression of transactivation activity
in response to coactivator; when
associated with A-22.
{ECO:0000269|PubMed:17676930,
ECO:0000269|PubMed:18063693}.
MUTAGEN 19 19 S->D: Represses transactivation activity
in response to coactivator as for wild
type; when associated with D-22.
{ECO:0000269|PubMed:17676930,
ECO:0000269|PubMed:18063693}.
MUTAGEN 22 22 S->A: 15% loss of phosphorylation but
little transactivating activity. Almost
complete loss of phosphorylation and 2-
fold loss of repression of
transactivation activity in the presence
of coactivator; when associated with A-
19. {ECO:0000269|PubMed:17676930,
ECO:0000269|PubMed:18063693}.
MUTAGEN 22 22 S->D: Represses transactivation activity
in response to coactivator as for wild
type; when associated with D-19.
{ECO:0000269|PubMed:17676930,
ECO:0000269|PubMed:18063693}.
MUTAGEN 118 118 S->A: Binds DNA as a monomer or as a
dimer as for wild type. No effect on
interaction with PPARGC1A.
{ECO:0000269|PubMed:16150865}.
MUTAGEN 124 124 T->A: Binds DNA predominantly as a
monomer. Loss of interaction with
PPARGC1A. {ECO:0000269|PubMed:16150865}.
MUTAGEN 129 129 K->R: Abolishes acetylation by
PCAF/KAT2B; when associated with R-138,
R-160 and R-162.
{ECO:0000269|PubMed:20484414}.
MUTAGEN 138 138 K->R: Abolishes acetylation by
PCAF/KAT2B; when associated with R-129,
R-160 and R-162.
{ECO:0000269|PubMed:20484414}.
MUTAGEN 160 160 K->R: Abolishes acetylation by
PCAF/KAT2B; when associated with R-129,
R-138 and R-162.
{ECO:0000269|PubMed:20484414}.
MUTAGEN 162 162 K->R: Abolishes acetylation by
PCAF/KAT2B; when associated with R-129,
R-138 and R-160.
{ECO:0000269|PubMed:20484414}.
MUTAGEN 258 262 MSVLQ->VSVLE: Almost complete loss of
interaction to L2 or to L3 of PPARGC1A.
{ECO:0000269|PubMed:18441008}.
MUTAGEN 259 259 S->H: Little effect on binding L2 of
PPARGC1A. Greatly reduced binding to L3
of PPARGC1A.
{ECO:0000269|PubMed:18441008}.
MUTAGEN 315 315 R->A: Almost complete loss of interaction
to L2 or to L3 of PPARGC1A.
{ECO:0000269|PubMed:18441008}.
MUTAGEN 338 338 D->A: Almost complete loss of interaction
to L2 or to L3 of PPARGC1A.
{ECO:0000269|PubMed:18441008}.
MUTAGEN 341 341 H->A: Little effect on binding L3 of
PPARGC1A. {ECO:0000269|PubMed:18441008}.
MUTAGEN 343 343 E->A: No effect on binding L3 of
PPARGC1A. {ECO:0000269|PubMed:18441008}.
MUTAGEN 403 403 K->R: Decrease in sumoylation. No effect
on transcriptional activity. Complete
loss of sumoylation; when associated with
R-14. {ECO:0000269|PubMed:17676930,
ECO:0000269|PubMed:18063693}.
MUTAGEN 413 413 L->A: Loss of coactivation activity; when
associated with A-418. Loss of increased
response to coactivator; when associated
with A-19 and A-418.
{ECO:0000269|PubMed:17676930}.
MUTAGEN 418 418 L->A: Loss of coactivation activity; when
associated with A-413. Loss of increased
response to coactivator activity; when
associated with A-19 and A-413.
{ECO:0000269|PubMed:17676930}.
MUTAGEN 421 423 Missing: Greatly reduced interaction with
L3 motif of PPARGC1A. Less effect on
binding to L2 motif of PPARGC1A.
{ECO:0000269|PubMed:18441008}.
MUTAGEN 423 423 D->A: Little effect on binding L3 of
PPARGC1A.
HELIX 195 204 {ECO:0000244|PDB:3K6P}.
HELIX 224 244 {ECO:0000244|PDB:3K6P}.
HELIX 249 251 {ECO:0000244|PDB:3K6P}.
HELIX 254 277 {ECO:0000244|PDB:3K6P}.
STRAND 280 282 {ECO:0000244|PDB:3K6P}.
STRAND 284 287 {ECO:0000244|PDB:3K6P}.
STRAND 290 292 {ECO:0000244|PDB:3K6P}.
HELIX 294 299 {ECO:0000244|PDB:3K6P}.
TURN 300 304 {ECO:0000244|PDB:3K6P}.
HELIX 305 317 {ECO:0000244|PDB:3K6P}.
TURN 318 320 {ECO:0000244|PDB:3K6P}.
HELIX 323 335 {ECO:0000244|PDB:3K6P}.
HELIX 345 364 {ECO:0000244|PDB:3K6P}.
HELIX 377 382 {ECO:0000244|PDB:3K6P}.
HELIX 385 400 {ECO:0000244|PDB:3K6P}.
HELIX 404 406 {ECO:0000244|PDB:2PJL}.
HELIX 410 421 {ECO:0000244|PDB:3K6P}.
SEQUENCE 423 AA; 45510 MW; BAE62DAF0BE6BA96 CRC64;
MSSQVVGIEP LYIKAEPASP DSPKGSSETE TEPPVALAPG PAPTRCLPGH KEEEDGEGAG
PGEQGGGKLV LSSLPKRLCL VCGDVASGYH YGVASCEACK AFFKRTIQGS IEYSCPASNE
CEITKRRRKA CQACRFTKCL RVGMLKEGVR LDRVRGGRQK YKRRPEVDPL PFPGPFPAGP
LAVAGGPRKT AAPVNALVSH LLVVEPEKLY AMPDPAGPDG HLPAVATLCD LFDREIVVTI
SWAKSIPGFS SLSLSDQMSV LQSVWMEVLV LGVAQRSLPL QDELAFAEDL VLDEEGARAA
GLGELGAALL QLVRRLQALR LEREEYVLLK ALALANSDSV HIEDAEAVEQ LREALHEALL
EYEAGRAGPG GGAERRRAGR LLLTLPLLRQ TAGKVLAHFY GVKLEGKVPM HKLFLEMLEA
MMD


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