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Arginine-glutamic acid dipeptide repeats protein (Atrophin-1-like protein) (Atrophin-1-related protein)

 RERE_HUMAN              Reviewed;        1566 AA.
Q9P2R6; O43393; O75046; O75359; Q5VXL9; Q6P6B9; Q9Y2W4;
10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
10-JAN-2006, sequence version 2.
20-JUN-2018, entry version 166.
RecName: Full=Arginine-glutamic acid dipeptide repeats protein;
AltName: Full=Atrophin-1-like protein;
AltName: Full=Atrophin-1-related protein;
Name=RERE; Synonyms=ARG, ARP, ATN1L, KIAA0458;
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), INTERACTION WITH ATN1,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=10814707; DOI=10.1093/hmg/9.9.1433;
Yanagisawa H., Bundo M., Miyashita T., Okamura-Oho Y., Tadokoro K.,
Tokunaga K., Yamada M.;
"Protein binding of a DRPLA family through arginine-glutamic acid
dipeptide repeats is enhanced by extended polyglutamine.";
Hum. Mol. Genet. 9:1433-1442(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
AND SUBCELLULAR LOCATION.
PubMed=11331249;
Waerner T., Gardellin P., Pfizenmaier K., Weith A., Kraut N.;
"Human RERE is localized to nuclear promyelocytic leukemia oncogenic
domains and enhances apoptosis.";
Cell Growth Differ. 12:201-210(2001).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2).
Xia J.-H., Liu C.-Y., Ruan Q.-G., Wang D.-A., Deng H.-X.;
"Cloning and localization of human atrophin-1 (DRPLA) related gene.";
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-1566 (ISOFORM 1).
TISSUE=Brain;
PubMed=9455484; DOI=10.1093/dnares/4.5.345;
Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D.,
Nomura N., Ohara O.;
"Characterization of cDNA clones in size-fractionated cDNA libraries
from human brain.";
DNA Res. 4:345-349(1997).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 555-1566, TISSUE SPECIFICITY, AND
CHROMOSOMAL TRANSLOCATION.
PubMed=10729226; DOI=10.1006/geno.1999.6097;
Amler L.C., Bauer A., Corvi R., Dihlmann S., Praml C., Cavenee W.K.,
Schwab M., Hampton G.M.;
"Identification and characterization of novel genes located at the
t(1;15)(p36.2;q24) translocation breakpoint in the neuroblastoma cell
line NGP.";
Genomics 64:195-202(2000).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-1106, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53; SER-56 AND SER-642,
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).
[9]
INTERACTION WITH FAT1.
PubMed=19131340; DOI=10.1074/jbc.M809333200;
Hou R., Sibinga N.E.;
"Atrophin proteins interact with the Fat1 cadherin and regulate
migration and orientation in vascular smooth muscle cells.";
J. Biol. Chem. 284:6955-6965(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675 AND SER-679, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-642, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53; SER-56; SER-642;
SER-656; SER-675; SER-679 AND SER-1106, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-120; SER-594; SER-600;
SER-675; SER-679 AND SER-1266, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304; SER-613; SER-1106;
SER-1113; THR-1119 AND TYR-1259, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[15]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-637, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[16]
INVOLVEMENT IN NEDBEH, VARIANTS NEDBEH ILE-471; ARG-1156; ARG-1262 AND
GLN-1431, AND CHARACTERIZATION OF VARIANT NEDBEH ARG-1156.
PubMed=27087320; DOI=10.1016/j.ajhg.2016.03.002;
Fregeau B., Kim B.J., Hernandez-Garcia A., Jordan V.K., Cho M.T.,
Schnur R.E., Monaghan K.G., Juusola J., Rosenfeld J.A., Bhoj E.,
Zackai E.H., Sacharow S., Baranano K., Bosch D.G., de Vries B.B.,
Lindstrom K., Schroeder A., James P., Kulch P., Lalani S.R.,
van Haelst M.M., van Gassen K.L., van Binsbergen E., Barkovich A.J.,
Scott D.A., Sherr E.H.;
"De novo mutations of RERE cause a genetic syndrome with features that
overlap those associated with proximal 1p36 deletions.";
Am. J. Hum. Genet. 98:963-970(2016).
[17]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-560 AND LYS-637, 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).
[18]
STRUCTURE BY NMR OF 392-446.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the SANT domain in arginine-glutamic acid
dipeptide (RE) repeats.";
Submitted (OCT-2007) to the PDB data bank.
-!- FUNCTION: Plays a role as a transcriptional repressor during
development. May play a role in the control of cell survival.
Overexpression of RERE recruits BAX to the nucleus particularly to
POD and triggers caspase-3 activation, leading to cell death.
{ECO:0000269|PubMed:11331249}.
-!- SUBUNIT: Interacts with HDAC1 (By similarity). Interacts with
ATN1. Interaction with ATN1 is improved when the poly-Gln region
of ATN1 is extended. Interacts with FAT1. {ECO:0000250,
ECO:0000269|PubMed:10814707, ECO:0000269|PubMed:19131340}.
-!- INTERACTION:
P54259:ATN1; NbExp=3; IntAct=EBI-948076, EBI-945980;
Q96KQ7:EHMT2; NbExp=3; IntAct=EBI-948076, EBI-744366;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00512, ECO:0000255|PROSITE-ProRule:PRU00624,
ECO:0000269|PubMed:10814707, ECO:0000269|PubMed:11331249}.
Note=Localized in nuclear bodies of variables size. Colocalized
with PML and BAX in nuclear PODs.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=Q9P2R6-1; Sequence=Displayed;
Name=2;
IsoId=Q9P2R6-2; Sequence=VSP_016878;
-!- TISSUE SPECIFICITY: Widely expressed. Expressed in tumor cell
lines. {ECO:0000269|PubMed:10729226, ECO:0000269|PubMed:10814707,
ECO:0000269|PubMed:11331249}.
-!- DOMAIN: The interaction with ATN1 is mediated by the coiled coil
domain.
-!- DISEASE: Note=A chromosomal aberration involving RERE is found in
the neuroblastoma cell line NGP. Translocation t(1;15)(p36.2;q24).
-!- DISEASE: Neurodevelopmental disorder with or without anomalies of
the brain, eye, or heart (NEDBEH) [MIM:616975]: An autosomal
dominant syndrome characterized by developmental delay,
intellectual disability, brain anomalies, and neurological
abnormalities including seizures, hypotonia, and behavioral
problems such as autism spectrum disorders. Brain anomalies
include abnormalities and/or thinning of the corpus callosum,
diminished white matter volume, abnormal cerebellar vermis, and
ventriculomegaly. Congenital defects of the eye, heart and
genitourinary system are present in half of the patients.
{ECO:0000269|PubMed:27087320}. Note=The disease may be caused by
mutations affecting the gene represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=AAC31120.1; Type=Frameshift; Positions=588, 596; Evidence={ECO:0000305};
Sequence=AAD27584.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AB036737; BAA95898.1; -; mRNA.
EMBL; AF016005; AAC31120.1; ALT_FRAME; mRNA.
EMBL; AF041104; AAC28264.1; -; Genomic_DNA.
EMBL; AF041096; AAC28264.1; JOINED; Genomic_DNA.
EMBL; AF041097; AAC28264.1; JOINED; Genomic_DNA.
EMBL; AF041098; AAC28264.1; JOINED; Genomic_DNA.
EMBL; AF041099; AAC28264.1; JOINED; Genomic_DNA.
EMBL; AF041100; AAC28264.1; JOINED; Genomic_DNA.
EMBL; AF041101; AAC28264.1; JOINED; Genomic_DNA.
EMBL; AF041102; AAC28264.1; JOINED; Genomic_DNA.
EMBL; AF041103; AAC28264.1; JOINED; Genomic_DNA.
EMBL; AL356072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL357713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL096855; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AB007927; BAA32303.3; -; mRNA.
EMBL; AF118275; AAD27584.1; ALT_INIT; mRNA.
CCDS; CCDS41243.1; -. [Q9P2R6-2]
CCDS; CCDS95.1; -. [Q9P2R6-1]
RefSeq; NP_001036146.1; NM_001042681.1. [Q9P2R6-1]
RefSeq; NP_001036147.1; NM_001042682.1. [Q9P2R6-2]
RefSeq; NP_036234.3; NM_012102.3. [Q9P2R6-1]
RefSeq; XP_005263521.1; XM_005263464.2. [Q9P2R6-1]
RefSeq; XP_016856847.1; XM_017001358.1. [Q9P2R6-1]
RefSeq; XP_016856848.1; XM_017001359.1. [Q9P2R6-1]
UniGene; Hs.463041; -.
PDB; 2YQK; NMR; -; A=392-441.
PDBsum; 2YQK; -.
ProteinModelPortal; Q9P2R6; -.
SMR; Q9P2R6; -.
BioGrid; 106963; 31.
DIP; DIP-47606N; -.
IntAct; Q9P2R6; 30.
MINT; Q9P2R6; -.
STRING; 9606.ENSP00000338629; -.
CarbonylDB; Q9P2R6; -.
iPTMnet; Q9P2R6; -.
PhosphoSitePlus; Q9P2R6; -.
BioMuta; RERE; -.
DMDM; 85540730; -.
EPD; Q9P2R6; -.
MaxQB; Q9P2R6; -.
PaxDb; Q9P2R6; -.
PeptideAtlas; Q9P2R6; -.
PRIDE; Q9P2R6; -.
ProteomicsDB; 83883; -.
ProteomicsDB; 83884; -. [Q9P2R6-2]
DNASU; 473; -.
Ensembl; ENST00000337907; ENSP00000338629; ENSG00000142599. [Q9P2R6-1]
Ensembl; ENST00000400908; ENSP00000383700; ENSG00000142599. [Q9P2R6-1]
Ensembl; ENST00000476556; ENSP00000422246; ENSG00000142599. [Q9P2R6-2]
GeneID; 473; -.
KEGG; hsa:473; -.
UCSC; uc001apd.4; human. [Q9P2R6-1]
CTD; 473; -.
DisGeNET; 473; -.
EuPathDB; HostDB:ENSG00000142599.17; -.
GeneCards; RERE; -.
HGNC; HGNC:9965; RERE.
HPA; HPA024093; -.
MalaCards; RERE; -.
MIM; 605226; gene.
MIM; 616975; phenotype.
neXtProt; NX_Q9P2R6; -.
OpenTargets; ENSG00000142599; -.
PharmGKB; PA34332; -.
eggNOG; KOG2133; Eukaryota.
eggNOG; ENOG410ZIND; LUCA.
GeneTree; ENSGT00580000081398; -.
HOGENOM; HOG000231091; -.
HOVERGEN; HBG079774; -.
InParanoid; Q9P2R6; -.
KO; K05628; -.
OMA; FMPLAGS; -.
OrthoDB; EOG091G0O1H; -.
PhylomeDB; Q9P2R6; -.
TreeFam; TF328554; -.
ChiTaRS; RERE; human.
EvolutionaryTrace; Q9P2R6; -.
GeneWiki; RERE; -.
GenomeRNAi; 473; -.
PRO; PR:Q9P2R6; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000142599; -.
CleanEx; HS_RERE; -.
ExpressionAtlas; Q9P2R6; baseline and differential.
Genevisible; Q9P2R6; HS.
GO; GO:0000118; C:histone deacetylase complex; IEA:Ensembl.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0003682; F:chromatin binding; IEA:InterPro.
GO; GO:0008267; F:poly-glutamine tract binding; TAS:ProtInc.
GO; GO:0001105; F:RNA polymerase II transcription coactivator activity; IEA:Ensembl.
GO; GO:0001106; F:RNA polymerase II transcription corepressor activity; IEA:Ensembl.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
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; IEA:Ensembl.
GO; GO:0021930; P:cerebellar granule cell precursor proliferation; IEA:Ensembl.
GO; GO:0021691; P:cerebellar Purkinje cell layer maturation; IEA:Ensembl.
GO; GO:0006338; P:chromatin remodeling; IEA:Ensembl.
GO; GO:0048813; P:dendrite morphogenesis; IEA:Ensembl.
GO; GO:0006607; P:NLS-bearing protein import into nucleus; TAS:ProtInc.
GO; GO:0021942; P:radial glia guided migration of Purkinje cell; IEA:Ensembl.
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;
3D-structure; Acetylation; Alternative splicing;
Chromosomal rearrangement; Coiled coil; Complete proteome;
Developmental protein; Disease mutation; Isopeptide bond;
Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repressor; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 1566 Arginine-glutamic acid dipeptide repeats
protein.
/FTId=PRO_0000083504.
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 1156 1211 {ECO:0000255}.
COMPBIAS 738 1118 Pro-rich.
COMPBIAS 1179 1204 Arg/Glu-rich (mixed charge).
COMPBIAS 1300 1322 Arg/Glu-rich (mixed charge).
COMPBIAS 1425 1445 His-rich.
COMPBIAS 1451 1510 Pro-rich.
MOD_RES 53 53 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
MOD_RES 56 56 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
MOD_RES 120 120 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 142 142 Phosphoserine.
{ECO:0000250|UniProtKB:Q80TZ9}.
MOD_RES 304 304 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:24275569}.
MOD_RES 594 594 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 600 600 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 613 613 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 642 642 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 656 656 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 675 675 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 679 679 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1106 1106 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 1113 1113 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1115 1115 Phosphoserine.
{ECO:0000250|UniProtKB:Q80TZ9}.
MOD_RES 1119 1119 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1158 1158 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q80TZ9}.
MOD_RES 1259 1259 Phosphotyrosine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1266 1266 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 560 560 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 637 637 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 554 Missing (in isoform 2).
{ECO:0000303|Ref.3}.
/FTId=VSP_016878.
VARIANT 471 471 V -> I (in NEDBEH; unknown pathological
significance; dbSNP:rs765016528).
{ECO:0000269|PubMed:27087320}.
/FTId=VAR_077007.
VARIANT 1156 1156 G -> R (in NEDBEH; unknown pathological
significance; dbSNP:rs766951273).
{ECO:0000269|PubMed:27087320}.
/FTId=VAR_077008.
VARIANT 1262 1262 P -> R (in NEDBEH; unknown pathological
significance; dbSNP:rs878853270).
{ECO:0000269|PubMed:27087320}.
/FTId=VAR_077009.
VARIANT 1431 1431 H -> Q (in NEDBEH; unknown pathological
significance; dbSNP:rs869312871).
{ECO:0000269|PubMed:27087320}.
/FTId=VAR_077010.
CONFLICT 65 65 S -> G (in Ref. 1; BAA95898).
{ECO:0000305}.
CONFLICT 68 68 A -> T (in Ref. 1; BAA95898).
{ECO:0000305}.
CONFLICT 114 115 ES -> VC (in Ref. 1; BAA95898).
{ECO:0000305}.
CONFLICT 643 643 P -> L (in Ref. 3; AAC31120).
{ECO:0000305}.
CONFLICT 921 921 A -> G (in Ref. 1; BAA95898).
{ECO:0000305}.
CONFLICT 940 940 P -> A (in Ref. 1; BAA95898).
{ECO:0000305}.
CONFLICT 957 957 F -> L (in Ref. 6; AAD27584).
{ECO:0000305}.
CONFLICT 977 977 T -> K (in Ref. 2; no nucleotide entry).
{ECO:0000305}.
CONFLICT 984 984 H -> N (in Ref. 2; no nucleotide entry).
{ECO:0000305}.
CONFLICT 1009 1011 QSQ -> RTR (in Ref. 6; AAD27584).
{ECO:0000305}.
CONFLICT 1117 1117 E -> D (in Ref. 6; AAD27584).
{ECO:0000305}.
CONFLICT 1272 1272 H -> Q (in Ref. 6; AAD27584).
{ECO:0000305}.
CONFLICT 1489 1490 ML -> IV (in Ref. 1; BAA95898).
{ECO:0000305}.
CONFLICT 1529 1529 R -> K (in Ref. 6; AAD27584).
{ECO:0000305}.
CONFLICT 1536 1536 W -> C (in Ref. 6; AAD27584).
{ECO:0000305}.
CONFLICT 1543 1543 M -> R (in Ref. 6; AAD27584).
{ECO:0000305}.
HELIX 398 410 {ECO:0000244|PDB:2YQK}.
HELIX 415 421 {ECO:0000244|PDB:2YQK}.
HELIX 428 439 {ECO:0000244|PDB:2YQK}.
SEQUENCE 1566 AA; 172424 MW; ECA4A22026E3E96F CRC64;
MTADKDKDKD KEKDRDRDRD REREKRDKAR ESENSRPRRS CTLEGGAKNY AESDHSEDED
NDNNSATAEE STKKNKKKPP KKKSRYERTD TGEITSYITE DDVVYRPGDC VYIESRRPNT
PYFICSIQDF KLVHNSQACC RSPTPALCDP PACSLPVASQ PPQHLSEAGR GPVGSKRDHL
LMNVKWYYRQ SEVPDSVYQH LVQDRHNEND SGRELVITDP VIKNRELFIS DYVDTYHAAA
LRGKCNISHF SDIFAAREFK ARVDSFFYIL GYNPETRRLN STQGEIRVGP SHQAKLPDLQ
PFPSPDGDTV TQHEELVWMP GVNDCDLLMY LRAARSMAAF AGMCDGGSTE DGCVAASRDD
TTLNALNTLH ESGYDAGKAL QRLVKKPVPK LIEKCWTEDE VKRFVKGLRQ YGKNFFRIRK
ELLPNKETGE LITFYYYWKK TPEAASSRAH RRHRRQAVFR RIKTRTASTP VNTPSRPPSS
EFLDLSSASE DDFDSEDSEQ ELKGYACRHC FTTTSKDWHH GGRENILLCT DCRIHFKKYG
ELPPIEKPVD PPPFMFKPVK EEDDGLSGKH SMRTRRSRGS MSTLRSGRKK QPASPDGRTS
PINEDIRSSG RNSPSAASTS SNDSKAETVK KSAKKVKEEA SSPLKSNKRQ REKVASDTEE
ADRTSSKKTK TQEISRPNSP SEGEGESSDS RSVNDEGSSD PKDIDQDNRS TSPSIPSPQD
NESDSDSSAQ QQMLQAQPPA LQAPTGVTPA PSSAPPGTPQ LPTPGPTPSA TAVPPQGSPT
ASQAPNQPQA PTAPVPHTHI QQAPALHPQR PPSPHPPPHP SPHPPLQPLT GSAGQPSAPS
HAQPPLHGQG PPGPHSLQAG PLLQHPGPPQ PFGLPPQASQ GQAPLGTSPA AAYPHTSLQL
PASQSALQSQ QPPREQPLPP APLAMPHIKP PPTTPIPQLP APQAHKHPPH LSGPSPFSMN
ANLPPPPALK PLSSLSTHHP PSAHPPPLQL MPQSQPLPSS PAQPPGLTQS QNLPPPPASH
PPTGLHQVAP QPPFAQHPFV PGGPPPITPP TCPSTSTPPA GPGTSAQPPC SGAAASGGSI
AGGSSCPLPT VQIKEEALDD AEEPESPPPP PRSPSPEPTV VDTPSHASQS ARFYKHLDRG
YNSCARTDLY FMPLAGSKLA KKREEAIEKA KREAEQKARE EREREKEKEK ERERERERER
EAERAAKASS SAHEGRLSDP QLSGPGHMRP SFEPPPTTIA AVPPYIGPDT PALRTLSEYA
RPHVMSPTNR NHPFYMPLNP TDPLLAYHMP GLYNVDPTIR ERELREREIR EREIRERELR
ERMKPGFEVK PPELDPLHPA ANPMEHFARH SALTIPPTAG PHPFASFHPG LNPLERERLA
LAGPQLRPEM SYPDRLAAER IHAERMASLT SDPLARLQMF NVTPHHHQHS HIHSHLHLHQ
QDPLHQGSAG PVHPLVDPLT AGPHLARFPY PPGTLPNPLL GQPPHEHEML RHPVFGTPYP
RDLPGAIPPP MSAAHQLQAM HAQSAELQRL AMEQQWLHGH PHMHGGHLPS QEDYYSRLKK
EGDKQL


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