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Estrogen receptor beta (ER-beta) (Nuclear receptor subfamily 3 group A member 2)

 ESR2_MOUSE              Reviewed;         530 AA.
O08537; B2RUC6; E9QKX7; O35635; O70519; Q8BG65; Q91Z86;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
21-MAR-2012, sequence version 3.
20-JUN-2018, entry version 182.
RecName: Full=Estrogen receptor beta;
Short=ER-beta;
AltName: Full=Nuclear receptor subfamily 3 group A member 2;
Name=Esr2; Synonyms=Estrb, Nr3a2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Ovary;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 46-530, AND MUTAGENESIS.
STRAIN=129/Sv; TISSUE=Ovary;
PubMed=9058381; DOI=10.1210/mend.11.3.9902;
Tremblay G.B., Tremblay A., Copeland N.G., Gilbert D.J., Jenkins N.A.,
Labrie F., Giguere V.;
"Cloning, chromosomal localization, and functional analysis of the
murine estrogen receptor beta.";
Mol. Endocrinol. 11:353-365(1997).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 46-530, AND CHARACTERIZATION.
TISSUE=Ovary;
PubMed=9280064; DOI=10.1210/mend.11.10.9989;
Pettersson K., Grandien K., Kuiper G.G.J.M., Gustafsson J.-A.;
"Mouse estrogen receptor beta forms estrogen response element-binding
heterodimers with estrogen receptor alpha.";
Mol. Endocrinol. 11:1486-1496(1997).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 46-530 (ISOFORM 2), AND INDUCTION.
STRAIN=ddY; TISSUE=Calvaria;
PubMed=11878304; DOI=10.1359/jbmr.2002.17.3.394;
Dang Z.C., van Bezooijen R.L., Karperien M., Papapoulos S.E.,
Lowik C.W.;
"Exposure of KS483 cells to estrogen enhances osteogenesis and
inhibits adipogenesis.";
J. Bone Miner. Res. 17:394-405(2002).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-60.
TISSUE=Ovary;
Leygue E., Lu B., Dotzlaw H., Glor C., Watson P.H., Murphy L.C.;
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-60.
TISSUE=Ovary;
Rosenfeld C.S., Lubahn D.B.;
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[9]
INTERACTION WITH NCOA3.
PubMed=9192892; DOI=10.1038/42652;
Torchia J., Rose D.W., Inostroza J., Kamei Y., Westin S., Glass C.K.,
Rosenfeld M.G.;
"The transcriptional co-activator p/CIP binds CBP and mediates
nuclear-receptor function.";
Nature 387:677-684(1997).
[10]
TISSUE SPECIFICITY.
PubMed=9607809; DOI=10.1210/endo.139.6.6028;
Rosenfeld C.S., Ganjam V.K., Taylor J.A., Yuan X., Stiehr J.R.,
Hardy M.P., Lubahn D.B.;
"Transcription and translation of estrogen receptor-beta in the male
reproductive tract of estrogen receptor-alpha knock-out and wild-type
mice.";
Endocrinology 139:2982-2987(1998).
[11]
ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4 AND 5).
TISSUE=Ovary;
PubMed=9685228; DOI=10.1016/S0303-7207(98)00050-1;
Lu B., Leygue E., Dotzlaw H., Murphy L.J., Murphy L.C., Watson P.H.;
"Estrogen receptor-beta mRNA variants in human and murine tissues.";
Mol. Cell. Endocrinol. 138:199-203(1998).
[12]
PHOSPHORYLATION AT SER-87 AND SER-105.
PubMed=10230404; DOI=10.1016/S1097-2765(00)80479-7;
Tremblay A., Tremblay G.B., Labrie F., Giguere V.;
"Ligand-independent recruitment of SRC-1 to estrogen receptor beta
through phosphorylation of activation function AF-1.";
Mol. Cell 3:513-519(1999).
[13]
GLYCOSYLATION AT SER-61, AND PHOSPHORYLATION AT SER-61.
PubMed=10995228; DOI=10.1021/bi000755i;
Cheng X., Cole R.N., Zaia J., Hart G.W.;
"Alternative O-glycosylation/O-phosphorylation of the murine estrogen
receptor beta.";
Biochemistry 39:11609-11620(2000).
[14]
INTERACTION WITH NCOA6.
PubMed=10788465; DOI=10.1074/jbc.275.18.13510;
Zhu Y.-J., Kan L., Qi C., Kanwar Y.S., Yeldandi A.V., Rao M.S.,
Reddy J.K.;
"Isolation and characterization of peroxisome proliferator-activated
receptor (PPAR) interacting protein (PRIP) as a coactivator for
PPAR.";
J. Biol. Chem. 275:13510-13516(2000).
-!- FUNCTION: Nuclear hormone receptor. Binds estrogens with an
affinity similar to that of ESR1 (ER-alpha), and activates
expression of reporter genes containing estrogen response elements
(ERE) in an estrogen-dependent manner. May play a role in ovarian
follicular growth and maturation.
-!- SUBUNIT: Binds DNA as a homodimer. Can form a heterodimer with
ESR1. Interacts with NCOA1, NCOA3, NCOA5 and NCOA6 coactivators,
leading to a strong increase of transcription of target genes.
Interacts with PELP1, UBE1C and AKAP13. Interacts with DNTTIP2 (By
similarity). Interacts with CCDC62 in the presence of
estradiol/E2; this interaction seems to enhance the transcription
of target genes. Interacts with DNAAF4. Interacts with PRMT2.
Interacts with CCAR2 (via N-terminus) in a ligand-independent
manner (By similarity). {ECO:0000250|UniProtKB:Q62986,
ECO:0000250|UniProtKB:Q92731}.
-!- INTERACTION:
P01101:Fos; NbExp=2; IntAct=EBI-2526214, EBI-4288185;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=Beta-1;
IsoId=O08537-1; Sequence=Displayed;
Name=2; Synonyms=Beta-2;
IsoId=O08537-2; Sequence=VSP_003693;
Name=3; Synonyms=Beta-5A;
IsoId=O08537-4; Sequence=VSP_003696;
Note=Corresponds to exons 5 and 6 deletion.
{ECO:0000305|PubMed:9685228};
Name=4;
IsoId=O08537-6; Sequence=VSP_042429, VSP_042430;
Note=Corresponds to exon 5 deletion (PubMed:9685228). May be
produced at very low levels due to a premature stop codon in the
mRNA, leading to nonsense-mediated mRNA decay. No experimental
confirmation available. {ECO:0000305|PubMed:9685228};
Name=5;
IsoId=O08537-7; Sequence=VSP_042431, VSP_042432;
Note=Corresponds to exon 6 deletion (PubMed:9685228). May be
produced at very low levels due to a premature stop codon in the
mRNA, leading to nonsense-mediated mRNA decay. No experimental
confirmation available. {ECO:0000305|PubMed:9685228};
-!- TISSUE SPECIFICITY: Expressed in prostate, ovary, Leydig cells and
in epithelium of the efferent ductules and of the initial segment
of the epididymis. {ECO:0000269|PubMed:9607809}.
-!- INDUCTION: Isoforms 1 and 2 are down-regulated by 17-beta-
estradiol. {ECO:0000269|PubMed:11878304}.
-!- DOMAIN: Composed of three domains: a modulating N-terminal domain,
a DNA-binding domain and a C-terminal ligand-binding domain.
-!- PTM: Phosphorylation at Ser-87 and Ser-105 recruits NCOA1.
{ECO:0000269|PubMed:10230404, ECO:0000269|PubMed:10995228}.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC17919.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAI41076.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAI45330.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAL15175.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAC35719.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAC35770.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AK054290; BAC35719.1; ALT_INIT; mRNA.
EMBL; AK054413; BAC35770.1; ALT_INIT; mRNA.
EMBL; AC164121; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC141075; AAI41076.1; ALT_INIT; mRNA.
EMBL; BC145329; AAI45330.1; ALT_INIT; mRNA.
EMBL; U81451; AAB51132.1; -; mRNA.
EMBL; AJ000220; CAA03949.1; -; Genomic_DNA.
EMBL; AY054413; AAL15175.1; ALT_INIT; mRNA.
EMBL; AF067422; AAC17919.1; ALT_INIT; mRNA.
EMBL; AF063853; AAC16656.1; -; mRNA.
RefSeq; NP_034287.3; NM_010157.3.
RefSeq; NP_997590.1; NM_207707.1.
UniGene; Mm.2561; -.
ProteinModelPortal; O08537; -.
SMR; O08537; -.
BioGrid; 199522; 3.
IntAct; O08537; 2.
STRING; 10090.ENSMUSP00000098849; -.
BindingDB; O08537; -.
ChEMBL; CHEMBL2995; -.
GuidetoPHARMACOLOGY; 621; -.
GlyConnect; 146; -.
iPTMnet; O08537; -.
PhosphoSitePlus; O08537; -.
UniCarbKB; O08537; -.
PaxDb; O08537; -.
PRIDE; O08537; -.
Ensembl; ENSMUST00000101291; ENSMUSP00000098849; ENSMUSG00000021055. [O08537-2]
Ensembl; ENSMUST00000110421; ENSMUSP00000106051; ENSMUSG00000021055. [O08537-1]
Ensembl; ENSMUST00000133564; ENSMUSP00000138637; ENSMUSG00000021055. [O08537-6]
GeneID; 13983; -.
KEGG; mmu:13983; -.
UCSC; uc007nxu.1; mouse. [O08537-2]
UCSC; uc007nxv.1; mouse. [O08537-1]
CTD; 2100; -.
MGI; MGI:109392; Esr2.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
GeneTree; ENSGT00760000118887; -.
HOGENOM; HOG000233468; -.
HOVERGEN; HBG108344; -.
InParanoid; O08537; -.
KO; K08551; -.
TreeFam; TF323751; -.
Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-MMU-8939211; ESR-mediated signaling.
PRO; PR:O08537; -.
Proteomes; UP000000589; Chromosome 12.
CleanEx; MM_ESR2; -.
ExpressionAtlas; O08537; baseline and differential.
GO; GO:0005929; C:cilium; ISO:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0043005; C:neuron projection; ISO:MGI.
GO; GO:0043025; C:neuronal cell body; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0043204; C:perikaryon; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0032993; C:protein-DNA complex; ISO:MGI.
GO; GO:0001046; F:core promoter sequence-specific DNA binding; ISO:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0008144; F:drug binding; ISO:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:1903924; F:estradiol binding; ISO:MGI.
GO; GO:0030284; F:estrogen receptor activity; ISO:MGI.
GO; GO:0034056; F:estrogen response element binding; ISO:MGI.
GO; GO:0042562; F:hormone binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0042975; F:peroxisome proliferator activated receptor binding; ISO:MGI.
GO; GO:1990841; F:promoter-specific chromatin binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; ISO:MGI.
GO; GO:0038052; F:RNA polymerase II transcription factor activity, estrogen-activated sequence-specific DNA binding; ISO:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
GO; GO:0005496; F:steroid binding; ISS:UniProtKB.
GO; GO:1990239; F:steroid hormone binding; ISO:MGI.
GO; GO:0003707; F:steroid hormone receptor activity; ISO:MGI.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0001662; P:behavioral fear response; ISO:MGI.
GO; GO:0007420; P:brain development; IMP:MGI.
GO; GO:0071392; P:cellular response to estradiol stimulus; ISO:MGI.
GO; GO:0060743; P:epithelial cell maturation involved in prostate gland development; IMP:MGI.
GO; GO:0044849; P:estrous cycle; ISO:MGI.
GO; GO:0008628; P:hormone-mediated apoptotic signaling pathway; IMP:MGI.
GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IMP:MGI.
GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; ISO:MGI.
GO; GO:0007611; P:learning or memory; ISO:MGI.
GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; IMP:MGI.
GO; GO:0048521; P:negative regulation of behavior; ISO:MGI.
GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; IGI:MGI.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:MGI.
GO; GO:2000252; P:negative regulation of feeding behavior; ISO:MGI.
GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; ISO:MGI.
GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0001764; P:neuron migration; IMP:MGI.
GO; GO:0001541; P:ovarian follicle development; IMP:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
GO; GO:0097755; P:positive regulation of blood vessel diameter; ISO:MGI.
GO; GO:0051091; P:positive regulation of DNA binding transcription factor activity; ISS:UniProtKB.
GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; ISO:MGI.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0060740; P:prostate gland epithelium morphogenesis; IMP:MGI.
GO; GO:0042127; P:regulation of cell proliferation; IMP:MGI.
GO; GO:0043523; P:regulation of neuron apoptotic process; ISO:MGI.
GO; GO:0033574; P:response to testosterone; ISO:MGI.
GO; GO:0060011; P:Sertoli cell proliferation; ISO:MGI.
GO; GO:0060065; P:uterus development; IGI:MGI.
GO; GO:0060068; P:vagina development; IGI:MGI.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR028355; ER-beta/gamma.
InterPro; IPR021064; Estrogen_rcpt_beta_N.
InterPro; IPR035500; NHR_like_dom_sf.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR024178; Oest_rcpt/oest-rel_rcp.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF12497; ERbeta_N; 1.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF00105; zf-C4; 1.
PIRSF; PIRSF500102; ER-b; 1.
PIRSF; PIRSF002527; ER-like_NR; 1.
PRINTS; PR00398; STRDHORMONER.
PRINTS; PR00047; STROIDFINGER.
SMART; SM00430; HOLI; 1.
SMART; SM00399; ZnF_C4; 1.
SUPFAM; SSF48508; SSF48508; 2.
PROSITE; PS51843; NR_LBD; 1.
PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
1: Evidence at protein level;
Activator; Alternative splicing; Complete proteome; DNA-binding;
Glycoprotein; Lipid-binding; Metal-binding; Nucleus; Phosphoprotein;
Receptor; Reference proteome; Steroid-binding; Transcription;
Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 530 Estrogen receptor beta.
/FTId=PRO_0000053644.
DOMAIN 264 498 NR LBD. {ECO:0000255|PROSITE-
ProRule:PRU01189}.
DNA_BIND 149 214 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 149 169 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 185 209 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
REGION 1 148 Modulating.
MOD_RES 61 61 Phosphoserine; alternate.
{ECO:0000269|PubMed:10995228}.
MOD_RES 87 87 Phosphoserine; by MAPK.
{ECO:0000269|PubMed:10230404}.
MOD_RES 105 105 Phosphoserine; by MAPK.
{ECO:0000269|PubMed:10230404}.
CARBOHYD 61 61 O-linked (GlcNAc) serine; alternate.
{ECO:0000269|PubMed:10995228}.
/FTId=CAR_000201.
VAR_SEQ 319 409 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_003696.
VAR_SEQ 319 343 FVELSLLDQVRLLESCWMEVLMVGL -> MRGSAWKGFWKS
LTCSWRRRHGSVS (in isoform 4).
{ECO:0000305}.
/FTId=VSP_042429.
VAR_SEQ 344 530 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_042430.
VAR_SEQ 364 364 R -> RSSEDPHWHVAQTKSAVPR (in isoform 2).
{ECO:0000303|PubMed:11878304,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_003693.
VAR_SEQ 365 377 DEGKCVEGILEIF -> YVPLGYRKPGSRE (in
isoform 5). {ECO:0000305}.
/FTId=VSP_042431.
VAR_SEQ 378 530 Missing (in isoform 5). {ECO:0000305}.
/FTId=VSP_042432.
MUTAGEN 105 105 S->A: Abolishes stimulatory effect of
Ras. {ECO:0000269|PubMed:9058381}.
MUTAGEN 139 139 S->A: No loss of the stimulatory effect
of Ras. {ECO:0000269|PubMed:9058381}.
CONFLICT 47 47 T -> A (in Ref. 5; CAA03949).
{ECO:0000305}.
CONFLICT 142 142 A -> T (in Ref. 5; CAA03949).
{ECO:0000305}.
CONFLICT 200 200 S -> N (in Ref. 5; CAA03949).
{ECO:0000305}.
CONFLICT 378 378 D -> G (in Ref. 1; AAB51132 and 6;
AAL15175). {ECO:0000305}.
CONFLICT 412 412 P -> H (in Ref. 5; CAA03949).
{ECO:0000305}.
CONFLICT 445 445 G -> R (in Ref. 5; CAA03949).
{ECO:0000305}.
CONFLICT 511 511 E -> G (in Ref. 5; CAA03949).
{ECO:0000305}.
SEQUENCE 530 AA; 59070 MW; BEFA25F62650A8D4 CRC64;
MEIKNSPSSL TSPASYNCSQ SILPLEHGPI YIPSSYVESR HEYSAMTFYS PAVMNYSVPS
STGNLEGGPV RQTASPNVLW PTSGHLSPLA THCQSSLLYA EPQKSPWCEA RSLEHTLPVN
RETLKRKLGG SGCASPVTSP SAKRDAHFCA VCSDYASGYH YGVWSCEGCK AFFKRSIQGH
NDYICPATNQ CTIDKNRRKS CQACRLRKCY EVGMVKCGSR RERCGYRIVR RQRSASEQVH
CLNKAKRTSG HTPRVKELLL NSLSPEQLVL TLLEAEPPNV LVSRPSMPFT EASMMMSLTK
LADKELVHMI GWAKKIPGFV ELSLLDQVRL LESCWMEVLM VGLMWRSIDH PGKLIFAPDL
VLDRDEGKCV EGILEIFDML LATTARFREL KLQHKEYLCV KAMILLNSSM YPLATASQEA
ESSRKLTHLL NAVTDALVWV ISKSGISSQQ QSVRLANLLM LLSHVRHISN KGMEHLLSMK
CKNVVPVYDL LLEMLNAHTL RGYKSSISGS ECCSTEDSKS KEGSQNLQSQ


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