ID   ERR1_MOUSE              Reviewed;         422 AA.
AC   O08580; B2RRU9; Q3U110;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 4.
DT   24-JAN-2024, entry version 192.
DE   RecName: Full=Steroid hormone receptor ERR1;
DE   AltName: Full=Estrogen receptor-like 1;
DE   AltName: Full=Estrogen-related receptor alpha;
DE            Short=ERR-alpha;
DE   AltName: Full=Nuclear receptor subfamily 3 group B member 1;
GN   Name=Esrra; Synonyms=Err1, Estrra, Nr3b1;
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 [MRNA].
RC   STRAIN=BALB/cJ;
RX   PubMed=9271417; DOI=10.1128/mcb.17.9.5400;
RA   Sladek R., Bader J.-A., Giguere V.;
RT   "The orphan nuclear receptor estrogen-related receptor alpha is a
RT   transcriptional regulator of the human medium-chain acyl coenzyme A
RT   dehydrogenase gene.";
RL   Mol. Cell. Biol. 17:5400-5409(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain, and Kidney;
RX   PubMed=9460651; DOI=10.1677/jme.0.0190299;
RA   Shigeta H., Zuo W., Yang N., DiAugustine R., Teng C.T.;
RT   "The mouse estrogen receptor-related orphan receptor alpha 1: molecular
RT   cloning and estrogen responsiveness.";
RL   J. Mol. Endocrinol. 19:299-309(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Spleen;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [5]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=14585956; DOI=10.1128/mcb.23.22.7947-7956.2003;
RA   Luo J., Sladek R., Carrier J., Bader J.A., Richard D., Giguere V.;
RT   "Reduced fat mass in mice lacking orphan nuclear receptor estrogen-related
RT   receptor alpha.";
RL   Mol. Cell. Biol. 23:7947-7956(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   SUMOYLATION, AND PHOSPHORYLATION AT SER-19.
RX   PubMed=18063693; DOI=10.1210/me.2007-0357;
RA   Tremblay A.M., Wilson B.J., Yang X.-J., Giguere V.;
RT   "Phosphorylation-dependent sumoylation regulates estrogen-related receptor-
RT   alpha and -gamma transcriptional activity through a synergy control
RT   motif.";
RL   Mol. Endocrinol. 22:570-584(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-22, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [9]
RP   ACETYLATION BY PCAF/KAT2B, AND DEACETYLATION BY SIRT1 AND HDAC8.
RX   PubMed=20484414; DOI=10.1210/me.2009-0441;
RA   Wilson B.J., Tremblay A.M., Deblois G., Sylvain-Drolet G., Giguere V.;
RT   "An acetylation switch modulates the transcriptional activity of estrogen-
RT   related receptor alpha.";
RL   Mol. Endocrinol. 24:1349-1358(2010).
RN   [10]
RP   INTERACTION WITH MAPK15.
RX   PubMed=21190936; DOI=10.1074/jbc.m110.179523;
RA   Rossi M., Colecchia D., Iavarone C., Strambi A., Piccioni F.,
RA   Verrotti di Pianella A., Chiariello M.;
RT   "Extracellular signal-regulated kinase 8 (ERK8) controls estrogen-related
RT   receptor alpha (ERRalpha) cellular localization and inhibits its
RT   transcriptional activity.";
RL   J. Biol. Chem. 286:8507-8522(2011).
RN   [11]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=28572090; DOI=10.15252/emmm.201707604;
RA   Wang T., Liu J., McDonald C., Lupino K., Zhai X., Wilkins B.J.,
RA   Hakonarson H., Pei L.;
RT   "GDF15 is a heart-derived hormone that regulates body growth.";
RL   EMBO Mol. Med. 9:1150-1164(2017).
CC   -!- FUNCTION: Binds to an ERR-alpha response element (ERRE) containing a
CC       single consensus half-site, 5'-TNAAGGTCA-3'. Can bind to the medium-
CC       chain acyl coenzyme A dehydrogenase (MCAD) response element NRRE-1 and
CC       may act as an important regulator of MCAD promoter. Binds to the C1
CC       region of the lactoferrin gene promoter. Requires dimerization and the
CC       coactivator, PGC-1A, for full activity. The ERRalpha/PGC1alpha complex
CC       is a regulator of energy metabolism. Induces the expression of PERM1 in
CC       the skeletal muscle (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds DNA as a monomer or a homodimer. Interacts (via the AF2
CC       domain) with coactivator PPARGC1A (via the L3 motif); the interaction
CC       greatly enhances transcriptional activity of genes involved in energy
CC       metabolism. Interacts with PIAS4; the interaction enhances sumoylation
CC       (By similarity). Interacts with MAPK15; promotes re-localization of
CC       ESRRA to the cytoplasm through a XPO1-dependent mechanism then inhibits
CC       ESRRA transcriptional activity (PubMed:21190936). {ECO:0000250,
CC       ECO:0000269|PubMed:21190936}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P11474,
CC       ECO:0000255|PROSITE-ProRule:PRU00407}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P11474}. Note=Co-localizes to the cytoplasm only
CC       in presence of MAPK15. {ECO:0000250|UniProtKB:P11474}.
CC   -!- TISSUE SPECIFICITY: Most highly expressed in kidney, heart, and brown
CC       adipocytes. Also found in uterus, cervix and vagina.
CC   -!- DEVELOPMENTAL STAGE: Expressed in an organ specific manner through
CC       mid- to late embryonic development with persistent high-level
CC       expression in brown adipose tissue and intestinal mucosa.
CC   -!- INDUCTION: Activated by diethylstilbestrol (DES) and estradiol in the
CC       uterus.
CC   -!- PTM: Phosphorylation on Ser-19 enhances sumoylation on Lys-14
CC       increasing repression of transcriptional activity. {ECO:0000250}.
CC   -!- PTM: Sumoylated with SUMO2. Main site is Lys-14 which is enhanced by
CC       phosphorylation on Ser-19, cofactor activation, and by interaction with
CC       PIAS4. Sumoylation enhances repression of transcriptional activity, but
CC       has no effect on subcellular location nor on DNA binding (By
CC       similarity). {ECO:0000250}.
CC   -!- PTM: Reversibly acetylated. Acetylation by PCAF/KAT2 at Lys-129, Lys-
CC       138, Lys-160 and Lys-162 and PCAF/KAT2 decreases transcriptional
CC       activity probably by inhibiting DNA-binding activity; deacetylation
CC       involves SIRT1 and HDAC8 and increases DNA-binding (By similarity).
CC       {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype; mice are viable, fertile
CC       and display no gross anatomical alterations, with the exception of
CC       reduced body weight and peripheral fat deposits. Mice are resistant to
CC       a high-fat diet-induced obesity. Cardiomyocyte-specific double konckout
CC       for ESRRA and ESRRG are slower at gaining weight, smaller and shorter
CC       from 5 to 7 days of age compared to controls. They show decreased
CC       absolute weight of most internal organs except the heart. They have
CC       about 70% decreased plasma IGF1 levels but normal plasma growth hormone
CC       levels. At 14-15 days, mutants develop lethal dilated cardiomyopathy
CC       and heart failure (PubMed:28572090). {ECO:0000269|PubMed:14585956,
CC       ECO:0000269|PubMed:28572090}.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC       subfamily. {ECO:0000305}.
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DR   EMBL; U85259; AAB51250.1; -; mRNA.
DR   EMBL; AK156371; BAE33690.1; -; mRNA.
DR   EMBL; BC138586; AAI38587.1; -; mRNA.
DR   EMBL; BC171958; AAI71958.1; -; mRNA.
DR   CCDS; CCDS29509.1; -.
DR   RefSeq; NP_031979.2; NM_007953.2.
DR   AlphaFoldDB; O08580; -.
DR   SMR; O08580; -.
DR   BioGRID; 204937; 8.
DR   IntAct; O08580; 2.
DR   STRING; 10090.ENSMUSP00000025906; -.
DR   ChEMBL; CHEMBL1914280; -.
DR   DrugCentral; O08580; -.
DR   GuidetoPHARMACOLOGY; 622; -.
DR   iPTMnet; O08580; -.
DR   PhosphoSitePlus; O08580; -.
DR   EPD; O08580; -.
DR   jPOST; O08580; -.
DR   MaxQB; O08580; -.
DR   PaxDb; 10090-ENSMUSP00000025906; -.
DR   PeptideAtlas; O08580; -.
DR   ProteomicsDB; 275675; -.
DR   Antibodypedia; 7260; 648 antibodies from 40 providers.
DR   DNASU; 26379; -.
DR   Ensembl; ENSMUST00000025906.12; ENSMUSP00000025906.4; ENSMUSG00000024955.16.
DR   GeneID; 26379; -.
DR   KEGG; mmu:26379; -.
DR   UCSC; uc008gjg.1; mouse.
DR   AGR; MGI:1346831; -.
DR   CTD; 2101; -.
DR   MGI; MGI:1346831; Esrra.
DR   VEuPathDB; HostDB:ENSMUSG00000024955; -.
DR   eggNOG; KOG3575; Eukaryota.
DR   GeneTree; ENSGT00940000160341; -.
DR   HOGENOM; CLU_007368_11_0_1; -.
DR   InParanoid; O08580; -.
DR   OMA; ASNVCEI; -.
DR   OrthoDB; 5387678at2759; -.
DR   PhylomeDB; O08580; -.
DR   TreeFam; TF323751; -.
DR   Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
DR   BioGRID-ORCS; 26379; 7 hits in 83 CRISPR screens.
DR   ChiTaRS; Esrra; mouse.
DR   PRO; PR:O08580; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; O08580; Protein.
DR   Bgee; ENSMUSG00000024955; Expressed in small intestine Peyer's patch and 289 other cell types or tissues.
DR   ExpressionAtlas; O08580; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR   GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR   GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR   GO; GO:0034056; F:estrogen response element binding; IBA:GO_Central.
DR   GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
DR   GO; GO:0003707; F:nuclear steroid receptor activity; IEA:InterPro.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0005496; F:steroid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0051216; P:cartilage development; ISO:MGI.
DR   GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:1900078; P:positive regulation of cellular response to insulin stimulus; ISO:MGI.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:0042127; P:regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; ISS:UniProtKB.
DR   GO; GO:0030278; P:regulation of ossification; ISO:MGI.
DR   GO; GO:0045667; P:regulation of osteoblast differentiation; ISO:MGI.
DR   GO; GO:0045670; P:regulation of osteoclast differentiation; ISO:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd07170; NR_DBD_ERR; 1.
DR   CDD; cd06946; NR_LBD_ERR; 1.
DR   Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR   Gene3D; 1.10.565.10; Retinoid X Receptor; 1.
DR   InterPro; IPR024178; Est_rcpt/est-rel_rcp.
DR   InterPro; IPR035500; NHR-like_dom_sf.
DR   InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR   InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR   InterPro; IPR027289; Oest-rel_rcp.
DR   InterPro; IPR001628; Znf_hrmn_rcpt.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   PANTHER; PTHR48092; KNIRPS-RELATED PROTEIN-RELATED; 1.
DR   PANTHER; PTHR48092:SF15; STEROID HORMONE RECEPTOR ERR1; 1.
DR   Pfam; PF00104; Hormone_recep; 1.
DR   Pfam; PF00105; zf-C4; 1.
DR   PIRSF; PIRSF002527; ER-like_NR; 1.
DR   PIRSF; PIRSF500939; ERR1-2-3; 1.
DR   PRINTS; PR00398; STRDHORMONER.
DR   PRINTS; PR00047; STROIDFINGER.
DR   SMART; SM00430; HOLI; 1.
DR   SMART; SM00399; ZnF_C4; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 1.
DR   PROSITE; PS51843; NR_LBD; 1.
DR   PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR   PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
DR   Genevisible; O08580; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; DNA-binding; Isopeptide bond; Metal-binding;
KW   Nucleus; Phosphoprotein; Receptor; Reference proteome; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..422
FT                   /note="Steroid hormone receptor ERR1"
FT                   /id="PRO_0000053661"
FT   DOMAIN          192..420
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        76..151
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         79..99
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         115..134
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          1..76
FT                   /note="Repressor domain"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          402..422
FT                   /note="AF-2 domain"
FT                   /evidence="ECO:0000250"
FT   SITE            124
FT                   /note="Required for DNA-dependent dimerization"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         19
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18063693,
FT                   ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT   MOD_RES         22
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         129
FT                   /note="N6-acetyllysine; by PCAF/KAT2B"
FT                   /evidence="ECO:0000250|UniProtKB:P11474"
FT   MOD_RES         138
FT                   /note="N6-acetyllysine; by PCAF/KAT2B"
FT                   /evidence="ECO:0000250|UniProtKB:P11474"
FT   MOD_RES         160
FT                   /note="N6-acetyllysine; by PCAF/KAT2B"
FT                   /evidence="ECO:0000250|UniProtKB:P11474"
FT   MOD_RES         162
FT                   /note="N6-acetyllysine; by PCAF/KAT2B"
FT                   /evidence="ECO:0000250|UniProtKB:P11474"
FT   CROSSLNK        14
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        189
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P11474"
FT   CROSSLNK        402
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO); alternate"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        402
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P11474"
FT   CONFLICT        275
FT                   /note="R -> G (in Ref. 1; AAB51250)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        308
FT                   /note="Missing (in Ref. 1; AAB51250)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        408..412
FT                   /note="PMHKL -> HAQV (in Ref. 1; AAB51250)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   422 AA;  45464 MW;  2F54EEA1BD3B511D CRC64;
     MSSQVVGIEP LYIKAEPASP DSPKGSSETE TEPPVTLASG PAPARCLPGH KEEEDGEGAG
     SGEQGSGKLV LSSLPKRLCL VCGDVASGYH YGVASCEACK AFFKRTIQGS IEYSCPASNE
     CEITKRRRKA CQACRFTKCL RVGMLKEGVR LDRVRGGRQK YKRRPEVDPL PFPGPFPAGP
     LAVAGGPRKT APVNALVSHL LVVEPEKLYA MPDPASPDGH LPAVATLCDL FDREIVVTIS
     WAKSIPGFSS LSLSDQMSVL QSVWMEVLVL GVAQRSLPLQ DELAFAEDLV LDEEGARAAG
     LGDLGAALLQ LVRRLQALRL EREEYVLLKA LALANSDSVH IEDAEAVEQL REALHEALLE
     YEAGRAGPGG GAERRRAGRL LLTLPLLRQT AGKVLAHFYG VKLEGKVPMH KLFLEMLEAM
     MD
//