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Arginine-glutamic acid dipeptide repeats protein (Atrophin-2)

 RERE_MOUSE              Reviewed;        1558 AA.
Q80TZ9; A2A7T4;
10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
28-MAR-2018, entry version 119.
RecName: Full=Arginine-glutamic acid dipeptide repeats protein;
AltName: Full=Atrophin-2;
Name=Rere; Synonyms=Atr2, Kiaa0458;
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 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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 673-1558.
TISSUE=Brain;
PubMed=12693553; DOI=10.1093/dnares/10.1.35;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
Nakajima D., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
II. The complete nucleotide sequences of 400 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:35-48(2003).
[3]
FUNCTION, INTERACTION WITH ATN1 AND HDAC1, DEVELOPMENTAL STAGE, AND
DISRUPTION PHENOTYPE.
PubMed=14645126; DOI=10.1242/dev.00908;
Zoltewicz J.S., Stewart N.J., Leung R., Peterson A.S.;
"Atrophin 2 recruits histone deacetylase and is required for the
function of multiple signaling centers during mouse embryogenesis.";
Development 131:3-14(2004).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675 AND SER-679, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53; SER-56; SER-142;
THR-593; SER-594; SER-600; SER-675; SER-679; SER-1098; SER-1105 AND
SER-1107, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1150, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: Plays a role as a transcriptional repressor during
development. May play a role in the control of cell survival.
{ECO:0000269|PubMed:14645126}.
-!- SUBUNIT: Interacts with HDAC1 and ATN1. Interaction with ATN1 is
improved when the poly-Gln region of ATN1 is extended. Interacts
with FAT1 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus, PML body {ECO:0000250}.
Note=Localized in nuclear bodies of variables size. Colocalized
with PML and BAX in nuclear PODs (By similarity). {ECO:0000250}.
-!- DEVELOPMENTAL STAGE: At E8.25 expression is strongly elevated in
the anterior midline. At E8.5 expression is elevated throughout
the anteroposterior extent of the notochord and is down-regulated
in the heart. At E8.75 expression is increased in the ventral
brain. At E9.5 strong expression appears besides the notochord
including the apical ectodermal ridge (AER), the isthmus and the
ventral diencephalon. At E10.5 expression increases in the
notochord, the AER and spinal and brain neurons.
{ECO:0000269|PubMed:14645126}.
-!- DOMAIN: The interaction with ATN1 is mediated by the coiled
domain. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice embryos exhibit a variety of patterning
defects that first appear at E8.0. Defects include a specific
failure in ventralization of the anterior neural plate, loss of
heart looping and irregular partitioning of somites. In mutant
embryos, Shh expression fails to initiate along the anterior
midline at E8.0, and Fgf8 is delocalized from the anterior neural
ridge at E8.5. {ECO:0000269|PubMed:14645126}.
-----------------------------------------------------------------------
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EMBL; AL691453; CAM16595.1; -; Genomic_DNA.
EMBL; AL606982; CAM16595.1; JOINED; Genomic_DNA.
EMBL; AL606988; CAM16595.1; JOINED; Genomic_DNA.
EMBL; AL606982; CAM21921.1; -; Genomic_DNA.
EMBL; AL606988; CAM21921.1; JOINED; Genomic_DNA.
EMBL; AL691453; CAM21921.1; JOINED; Genomic_DNA.
EMBL; AL606988; CAM22173.1; -; Genomic_DNA.
EMBL; AL606982; CAM22173.1; JOINED; Genomic_DNA.
EMBL; AL691453; CAM22173.1; JOINED; Genomic_DNA.
EMBL; CU210934; CAQ51525.1; -; Genomic_DNA.
EMBL; CU210933; CAQ51525.1; JOINED; Genomic_DNA.
EMBL; CU210933; CAQ51728.1; -; Genomic_DNA.
EMBL; CU210934; CAQ51728.1; JOINED; Genomic_DNA.
EMBL; AK122287; BAC65569.1; -; Transcribed_RNA.
CCDS; CCDS38979.1; -.
RefSeq; NP_001078961.1; NM_001085492.1.
UniGene; Mm.291274; -.
ProteinModelPortal; Q80TZ9; -.
SMR; Q80TZ9; -.
BioGrid; 213002; 2.
IntAct; Q80TZ9; 3.
STRING; 10090.ENSMUSP00000101307; -.
iPTMnet; Q80TZ9; -.
PhosphoSitePlus; Q80TZ9; -.
MaxQB; Q80TZ9; -.
PaxDb; Q80TZ9; -.
PeptideAtlas; Q80TZ9; -.
PRIDE; Q80TZ9; -.
DNASU; 68703; -.
Ensembl; ENSMUST00000105682; ENSMUSP00000101307; ENSMUSG00000039852.
GeneID; 68703; -.
KEGG; mmu:68703; -.
UCSC; uc008vxr.1; mouse.
CTD; 473; -.
MGI; MGI:2683486; Rere.
eggNOG; KOG2133; Eukaryota.
eggNOG; ENOG410ZIND; LUCA.
GeneTree; ENSGT00580000081398; -.
HOGENOM; HOG000231091; -.
HOVERGEN; HBG079774; -.
InParanoid; Q80TZ9; -.
KO; K05628; -.
OMA; FMPLAGS; -.
OrthoDB; EOG091G0O1H; -.
TreeFam; TF328554; -.
ChiTaRS; Rere; mouse.
PRO; PR:Q80TZ9; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000039852; -.
CleanEx; MM_RERE; -.
ExpressionAtlas; Q80TZ9; baseline and differential.
Genevisible; Q80TZ9; MM.
GO; GO:0000118; C:histone deacetylase complex; IPI:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
GO; GO:0003682; F:chromatin binding; IEA:InterPro.
GO; GO:0003700; F:DNA binding transcription factor activity; IEA:InterPro.
GO; GO:0001105; F:RNA polymerase II transcription coactivator activity; IDA:MGI.
GO; GO:0001106; F:RNA polymerase II transcription corepressor activity; IMP:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0048755; P:branching morphogenesis of a nerve; IMP:MGI.
GO; GO:0021930; P:cerebellar granule cell precursor proliferation; IMP:MGI.
GO; GO:0021691; P:cerebellar Purkinje cell layer maturation; IMP:MGI.
GO; GO:0021549; P:cerebellum development; IMP:MGI.
GO; GO:0006338; P:chromatin remodeling; IPI:MGI.
GO; GO:0048813; P:dendrite morphogenesis; IMP:MGI.
GO; GO:0021942; P:radial glia guided migration of Purkinje cell; IMP:MGI.
InterPro; IPR002951; Atrophin-like.
InterPro; IPR001025; BAH_dom.
InterPro; IPR000949; ELM2_dom.
InterPro; IPR009057; Homeobox-like_sf.
InterPro; IPR001005; SANT/Myb.
InterPro; IPR017884; SANT_dom.
InterPro; IPR000679; Znf_GATA.
Pfam; PF03154; Atrophin-1; 1.
Pfam; PF01426; BAH; 1.
Pfam; PF01448; ELM2; 1.
Pfam; PF00320; GATA; 1.
SMART; SM00439; BAH; 1.
SMART; SM01189; ELM2; 1.
SMART; SM00717; SANT; 1.
SMART; SM00401; ZnF_GATA; 1.
SUPFAM; SSF46689; SSF46689; 1.
PROSITE; PS51038; BAH; 1.
PROSITE; PS51156; ELM2; 1.
PROSITE; PS51293; SANT; 1.
1: Evidence at protein level;
Acetylation; Coiled coil; Complete proteome; Developmental protein;
Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
Reference proteome; Repressor; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 1558 Arginine-glutamic acid dipeptide repeats
protein.
/FTId=PRO_0000083505.
DOMAIN 103 283 BAH. {ECO:0000255|PROSITE-
ProRule:PRU00370}.
DOMAIN 284 387 ELM2. {ECO:0000255|PROSITE-
ProRule:PRU00512}.
DOMAIN 391 443 SANT. {ECO:0000255|PROSITE-
ProRule:PRU00624}.
ZN_FING 507 532 GATA-type.
COILED 1148 1203 {ECO:0000255}.
COMPBIAS 738 1110 Pro-rich.
COMPBIAS 1171 1196 Arg/Glu-rich (mixed charge).
COMPBIAS 1292 1314 Arg/Glu-rich (mixed charge).
COMPBIAS 1417 1437 His-rich.
COMPBIAS 1443 1502 Pro-rich.
MOD_RES 53 53 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 56 56 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 120 120 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9P2R6}.
MOD_RES 142 142 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 304 304 Phosphoserine.
{ECO:0000250|UniProtKB:Q9P2R6}.
MOD_RES 593 593 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 594 594 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 600 600 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 613 613 Phosphoserine.
{ECO:0000250|UniProtKB:Q9P2R6}.
MOD_RES 642 642 Phosphoserine.
{ECO:0000250|UniProtKB:Q9P2R6}.
MOD_RES 656 656 Phosphoserine.
{ECO:0000250|UniProtKB:Q9P2R6}.
MOD_RES 675 675 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 679 679 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 1098 1098 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1105 1105 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1107 1107 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1111 1111 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9P2R6}.
MOD_RES 1150 1150 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 1251 1251 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9P2R6}.
MOD_RES 1258 1258 Phosphoserine.
{ECO:0000250|UniProtKB:Q9P2R6}.
CROSSLNK 560 560 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9P2R6}.
CROSSLNK 637 637 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9P2R6}.
CONFLICT 840 840 S -> G (in Ref. 2; BAC65569).
{ECO:0000305}.
CONFLICT 1236 1239 Missing (in Ref. 2; BAC65569).
{ECO:0000305}.
SEQUENCE 1558 AA; 171755 MW; 723A76184971CAA3 CRC64;
MTADKDKDKD KEKDRDRDRD RERDKRDKAR ESENARPRRS CTLEGGAKNY AESDHSEDED
NDNNSATTEE SNKKSRKKPP KKKSRYERTD TGEITSYITE DDVVYRPGDC VYIESRRPNT
PYFICSIQDF KLVHSSQACC RSPAPAFCDP PACSLPVAPQ PPQHLSEAGR GPGGSKRDHL
LMNVKWYYRQ SEVPDSVYQH LVQDRHNEND SGRELVITDP VIKNRELFIS DYVDTYHAAA
LRGKCNISHF SDIFAAREFK ARVDSFFYIL GYNPETRRLN STQGEIRVGP SHQAKLPDLQ
PFPSPDGDTV TQHEELVWMP GVSDCDLLMY LRAARSMAAF AGMCDGGSTE DGCVAASRDD
TTLNALNTLH ESSYDAGKAL QRLVKKPVPK LIEKCWTEDE VKRFVKGLRQ YGKNFFRIRK
ELLPSKETGE LITFYYYWKK TPEAASSRAH RRHRRQAVFR RIKTRTASTP VNTPSRPPSS
EFLDLSSASE DDFDSEDSEQ ELKGYACRHC FTTTSKDWHH GGRENILLCT DCRIHFKKYG
ELPPIEKPVD PPPFMFKPVK EEDDGLSGKH SMRTRRSRGS MSTLRSGRKK QPTSPDGRAS
PINEDIRSSG RNSPSAASTS SNDSKAETVK KSAKKVKEEA ASPLKSTKRQ REKVASDTED
TDRITSKKTK TQEISRPNSP SEGEGESSDS RSVNDEGSSD PKDIDQDNRS TSPSIPSPQD
NESDSDSSAQ QQMLQAQPPA LQAPSGAASA PSTAPPGTPQ LPTQGPTPSA TAVPPQGSPA
TSQPPNQTQS TVAPAAHTHI QQAPTLHPPR LPSPHPPLQP MTAPPSQSSA QPHPQPSLHS
QGPPGPHSLQ TGPLLQHPGP PQPFGLPSQP SQGQGPLGPS PAAAHPHSTI QLPASQSALQ
PQQPPREQPL PPAPLAMPHI KPPPTTPIPQ LPAPQAHKHP PHLSGPSPFS LNANLPPPPA
LKPLSSLSTH HPPSAHPPPL QLMPQSQPLP SSPAQPPGLT QSQSLPPPAA SHPTTGLHQV
PSQSPFPQHP FVPGGPPPIT PPSCPPTSTP PAGPSSSSQP PCSAAVSSGG SVPGAPSCPL
PAVQIKEEAL DEAEEPESPP PPPRSPSPEP TVVDTPSHAS QSARFYKHLD RGYNSCARTD
LYFMPLAGSK LAKKREEAIE KAKREAEQKA REEREREKEK EKERERERER EREAERAAKA
SSSAHEGRLS DPQLSGPGHM RPSFEPPPTT IAAVPPYIGP DTPALRTLSE YARPHVMSPT
NRNHPFYMPL NPTDPLLAYH MPGLYNVDPT IRERELRERE IREREIRERE LRERMKPGFE
VKPPELDPLH PATNPMEHFA RHSALTIPPA AGPHPFASFH PGLNPLERER LALAGPQLRP
EMSYPDRLAA ERIHAERMAS LTSDPLARLQ MFNVTPHHHQ HSHIHSHLHL HQQDPLHQGS
AGPVHPLVDP LTAGPHLARF PYPPGTLPNP LLGQPPHEHE MLRHPVFGTP YPRDLPGAIP
PPMSAAHQLQ AMHAQSAELQ RLAMEQQWLH GHPHMHGGHL PSQEDYYSRL KKEGDKQL


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