ESRRA
entrez
2101
canonical
uniprot
P11474
canonical
ensembl
ENSG00000173153
resolver
ensp
ENSP00000000442
resolver
ensp
ENSP00000384851
resolver
ensp
ENSP00000503245
resolver
ensp
ENSP00000574967
resolver
ensp
ENSP00000574968
resolver
genesymbol
ESRRA
resolver
genesymbol_syn
ERR1
resolver
genesymbol_syn
ESRL1
resolver
genesymbol_syn
NR3B1
resolver
hgnc
HGNC:3471
resolver
uniprot
Q14514
resolver
uniprot
Q569H8
resolver
uniprot
Q6P3W9
resolver
uniprot_entry
ERR1_HUMAN
resolver
uniprot_entry
Q569H8_HUMAN
resolver
uniprot_sec
Q14514
resolver
uniprot_sec
Q6P3W9
resolver
amino_acid_sequence
MSSQVVGIEPLYIKAEPASPDSPKGSSETETEPPVALAPGPAPTRCLPGHKEEEDGEGAGPGEQGGGKLVLSSLPKRLCLVCGDVASGYHYGVASCEACKAFFKRTIQGSIEYSCPASNECEITKRRRKACQACRFTKCLRVGMLKEGVRLDRVRGGRQKYKRRPEVDPLPFPGPFPAGPLAVAGGPRKTAAPVNALVSHLLVVEPEKLYAMPDPAGPDGHLPAVATLCDLFDREIVVTISWAKSIPGFSSLSLSDQMSVLQSVWMEVLVLGVAQRSLPLQDELAFAEDLVLDEEGARAAGLGELGAALLQLVRRLQALRLEREEYVLLKALALANSDSVHIEDAEAVEQLREALHEALLEYEAGRAGPGGGAERRRAGRLLLTLPLLRQTAGKVLAHFYGVKLEGKVPMHKLFLEMLEAMMD
uniprot
proteins
function
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}.
uniprot
proteins
mass_dalton
45510
uniprot
proteins
mutagenesis
MUTAGEN 14; /note="K->R: Some loss of sumoylation. Complete loss of sumoylation; when associated with R-403."; /evidence="ECO:0000269|PubMed:17676930, ECO:0000269|PubMed:18063693"; MUTAGEN 19; /note="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."; /evidence="ECO:0000269|PubMed:17676930, ECO:0000269|PubMed:18063693"; MUTAGEN 19; /note="S->D: Represses transactivation activity in response to coactivator as for wild type; when associated with D-22."; /evidence="ECO:0000269|PubMed:17676930, ECO:0000269|PubMed:18063693"; MUTAGEN 22; /note="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."; /evidence="ECO:0000269|PubMed:17676930, ECO:0000269|PubMed:18063693"; MUTAGEN 22; /note="S->D: Represses transactivation activity in response to coactivator as for wild type; when associated with D-19."; /evidence="ECO:0000269|PubMed:17676930, ECO:0000269|PubMed:18063693"; MUTAGEN 118; /note="S->A: Binds DNA as a monomer or as a dimer as for wild type. No effect on interaction with PPARGC1A."; /evidence="ECO:0000269|PubMed:16150865"; MUTAGEN 124; /note="T->A: Binds DNA predominantly as a monomer. Loss of interaction with PPARGC1A."; /evidence="ECO:0000269|PubMed:16150865"; MUTAGEN 129; /note="K->R: Abolishes acetylation by PCAF/KAT2B; when associated with R-138, R-160 and R-162."; /evidence="ECO:0000269|PubMed:20484414"; MUTAGEN 138; /note="K->R: Abolishes acetylation by PCAF/KAT2B; when associated with R-129, R-160 and R-162."; /evidence="ECO:0000269|PubMed:20484414"; MUTAGEN 160; /note="K->R: Abolishes acetylation by PCAF/KAT2B; when associated with R-129, R-138 and R-162."; /evidence="ECO:0000269|PubMed:20484414"; MUTAGEN 162; /note="K->R: Abolishes acetylation by PCAF/KAT2B; when associated with R-129, R-138 and R-160."; /evidence="ECO:0000269|PubMed:20484414"; MUTAGEN 258..262; /note="MSVLQ->VSVLE: Almost complete loss of interaction to L2 or to L3 of PPARGC1A."; /evidence="ECO:0000269|PubMed:18441008"; MUTAGEN 259; /note="S->H: Little effect on binding L2 of PPARGC1A. Greatly reduced binding to L3 of PPARGC1A."; /evidence="ECO:0000269|PubMed:18441008"; MUTAGEN 315; /note="R->A: Almost complete loss of interaction to L2 or to L3 of PPARGC1A."; /evidence="ECO:0000269|PubMed:18441008"; MUTAGEN 338; /note="D->A: Almost complete loss of interaction to L2 or to L3 of PPARGC1A."; /evidence="ECO:0000269|PubMed:18441008"; MUTAGEN 341; /note="H->A: Little effect on binding L3 of PPARGC1A."; /evidence="ECO:0000269|PubMed:18441008"; MUTAGEN 343; /note="E->A: No effect on binding L3 of PPARGC1A."; /evidence="ECO:0000269|PubMed:18441008"; MUTAGEN 403; /note="K->R: Decrease in sumoylation. No effect on transcriptional activity. Complete loss of sumoylation; when associated with R-14."; /evidence="ECO:0000269|PubMed:17676930, ECO:0000269|PubMed:18063693"; MUTAGEN 413; /note="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."; /evidence="ECO:0000269|PubMed:17676930"; MUTAGEN 418; /note="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."; /evidence="ECO:0000269|PubMed:17676930"; MUTAGEN 421..423; /note="Missing: Greatly reduced interaction with L3 motif of PPARGC1A. Less effect on binding to L2 motif of PPARGC1A."; /evidence="ECO:0000269|PubMed:18441008"; MUTAGEN 423; /note="D->A: Little effect on binding L3 of PPARGC1A.
uniprot
proteins
post_translational_modification
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}.
uniprot
proteins
protein_family
NR3 subfamily
uniprot
proteins
protein_family
Nuclear hormone receptor family
uniprot
proteins
pubmed
12522104
uniprot
proteins
pubmed
15337744
uniprot
proteins
pubmed
16150865
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
17676930
uniprot
proteins
pubmed
18063693
uniprot
proteins
pubmed
18441008
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
20484414
uniprot
proteins
pubmed
21190936
uniprot
proteins
pubmed
23836911
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
3267207
uniprot
proteins
pubmed
8224847
uniprot
proteins
pubmed
8621448
uniprot
proteins
pubmed
9271417
uniprot
proteins
sequence_length
423
uniprot
proteins
subcellular_location
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}.
uniprot
proteins