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Protein

Arginine-glutamic acid dipeptide repeats protein

Gene

Rere

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role as a transcriptional repressor during development. May play a role in the control of cell survival (By similarity). Interacts with FAT1 (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri507 – 53226GATA-typeAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Arginine-glutamic acid dipeptide repeats protein
Alternative name(s):
Atrophin-1-related protein
Gene namesi
Name:Rere
Synonyms:Arp
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi629475. Rere.

Subcellular locationi

  • NucleusPML body By similarity

  • Note: Localized in nuclear bodies of variable size. Colocalized with PML and BAX in nuclear PODs (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15591559Arginine-glutamic acid dipeptide repeats proteinPRO_0000083506Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 531PhosphoserineCombined sources
Modified residuei56 – 561PhosphoserineCombined sources
Modified residuei141 – 1411PhosphoserineBy similarity
Modified residuei303 – 3031PhosphoserineBy similarity
Modified residuei593 – 5931PhosphoserineCombined sources
Modified residuei599 – 5991PhosphoserineCombined sources
Modified residuei612 – 6121PhosphoserineBy similarity
Cross-linki636 – 636Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei641 – 6411PhosphoserineCombined sources
Modified residuei655 – 6551PhosphoserineCombined sources
Modified residuei674 – 6741PhosphoserineCombined sources
Modified residuei678 – 6781PhosphoserineCombined sources
Modified residuei1098 – 10981PhosphoserineBy similarity
Modified residuei1105 – 11051PhosphoserineBy similarity
Modified residuei1107 – 11071PhosphoserineBy similarity
Modified residuei1111 – 11111PhosphothreonineBy similarity
Modified residuei1150 – 11501N6-acetyllysineBy similarity
Modified residuei1252 – 12521PhosphotyrosineBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ62901.

PTM databases

iPTMnetiQ62901.
PhosphoSiteiQ62901.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

ExpressionAtlasiQ62901. baseline and differential.
GenevisibleiQ62901. RN.

Interactioni

Subunit structurei

Interacts with HDAC1 and ATN1. Interaction with ATN1 is improved when the poly-Gln region of ATN1 is extended (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000024443.

Structurei

3D structure databases

ProteinModelPortaliQ62901.
SMRiQ62901. Positions 391-445.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini102 – 282181BAHPROSITE-ProRule annotationAdd
BLAST
Domaini283 – 386104ELM2PROSITE-ProRule annotationAdd
BLAST
Domaini390 – 44253SANTPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1148 – 120558Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi737 – 1110374Pro-richAdd
BLAST
Compositional biasi1180 – 119112Arg/Glu-rich (mixed charge)Add
BLAST
Compositional biasi1292 – 130918Arg/Glu-rich (mixed charge)Add
BLAST
Compositional biasi1418 – 143821His-richAdd
BLAST
Compositional biasi1444 – 150360Pro-richAdd
BLAST

Domaini

The interaction with ATN1 is mediated by the coiled domain.By similarity

Sequence similaritiesi

Contains 1 BAH domain.PROSITE-ProRule annotation
Contains 1 ELM2 domain.PROSITE-ProRule annotation
Contains 1 GATA-type zinc finger.Curated
Contains 1 SANT domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri507 – 53226GATA-typeAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG2133. Eukaryota.
ENOG410ZIND. LUCA.
HOGENOMiHOG000231091.
HOVERGENiHBG079774.
InParanoidiQ62901.
KOiK05628.
OrthoDBiEOG7D59MN.
PhylomeDBiQ62901.
TreeFamiTF328554.

Family and domain databases

InterProiIPR002951. Atrophin-like.
IPR001025. BAH_dom.
IPR000949. ELM2_dom.
IPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR000679. Znf_GATA.
[Graphical view]
PfamiPF03154. Atrophin-1. 1 hit.
PF01426. BAH. 1 hit.
PF01448. ELM2. 1 hit.
PF00320. GATA. 1 hit.
[Graphical view]
SMARTiSM00439. BAH. 1 hit.
SM01189. ELM2. 1 hit.
SM00717. SANT. 1 hit.
SM00401. ZnF_GATA. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
PROSITEiPS51038. BAH. 1 hit.
PS51156. ELM2. 1 hit.
PS51293. SANT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q62901-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTADKDKDKD KEKDRDRDRD RERDKRDKAR ESENARPRRS CTLEGGAKNY
60 70 80 90 100
AESDHSEDED NDNGATTEES ARKSRKKPPK KKSRYERTDT GEITSYITED
110 120 130 140 150
DVVYRPGDCV YIESRRPNTP YFICSIQDFK LVHNSQACCR SPAPALCDPP
160 170 180 190 200
ACSLPVASQP PQHLSEAGRG PVGSKRDHLL MNVKWYYRQS EVPDSVYQHL
210 220 230 240 250
VQDRHNENDS GRELVITDPV IKNRELFISD YVDTYHAAAL RGKCNISHFS
260 270 280 290 300
DIFAAREFKA RVDSFFYILG YNPETRRLNS TQGEIRVGPS HQAKLPDLQP
310 320 330 340 350
FPSPDGDTVT QHEELVWMPG VSDCDLLMYL RAARSMAAFA GMCDGGSTED
360 370 380 390 400
GCVAASRDDT TLNALNTLHE SSYDAGKALQ RLVKKPVPKL IEKCWTEDEV
410 420 430 440 450
KRFVKGLRQY GKNFFRIRKE LLPNKETGEL ITFYYYWKKT PEAASSRAHR
460 470 480 490 500
RHRRQAVFRR IKTRTASTPV NTPSRPPSSE FLDLSSASED DFDSEDSEQE
510 520 530 540 550
LKGYACRHCF TTTSKDWHHG GRENILLCTD CRIHFKKYGE LPPIEKPVDP
560 570 580 590 600
PPFMFKPVKE EDDGLSGKHS MRTRRSRGSM STLRSGRKKQ PASPDGRASP
610 620 630 640 650
VNEDVRSSGR NSPSAASTSS NDSKAEAVKK SAKKVKEEAA SPLKNTKRQR
660 670 680 690 700
EKVASDTEDT DRATSKKTKT QEISRPNSPS EGEGESSDSR SVNDEGSSDP
710 720 730 740 750
KDIDQDNRST SPSIPSPQDN ESDSDSSAQQ QMLQTQPPAL QAPSGAASAP
760 770 780 790 800
STAPPGTTQL PTPGPTPSAT TVPPQGSPAT SQPPNQTQST VAPAAHTLIQ
810 820 830 840 850
QTPTLHPPRL PSPHPPLQPM TAPPSQNSAQ PHPQPSLHGQ GPPGPHSLQT
860 870 880 890 900
GPLLQHPGPP QPFGLTPQSS QGQGPLGPSP AAAHPHSTIQ LPASQSALQP
910 920 930 940 950
QQPPREQPLP PAPLAMPHIK PPPTTPIPQL PAPQAHKHPP HLSGPSPFSM
960 970 980 990 1000
NANLPPPPAL KPLSSLSTHH PPSAHPPPLQ LMPQSQPLPS SPAQPPGLTQ
1010 1020 1030 1040 1050
SQSLPPPAAS HPTTGGLHQV PSQSPFPQHP FVPGGPPPIT PPSCPPTSTP
1060 1070 1080 1090 1100
PAGPSSSSQP PCSAAVSSGG NVPGAPSCPL PAVQIKEEAL DEAEEPESPP
1110 1120 1130 1140 1150
PPPRSPSPEP TVVDTPSHAS QSARFYKHLD RGYNSCARTD LYFMPLAGSK
1160 1170 1180 1190 1200
LAKKREEAIE KAKREAEQKA REEREREKEK EKERERERER EREAERAAQK
1210 1220 1230 1240 1250
ASSSAHEGRL SDPQLSGPGH MRPSFEPPPT TIAAVPPYIG PDTPALRTLS
1260 1270 1280 1290 1300
EYARPHVMSP TNRNHPFYMP LNPTDPLLAY HMPGLYNVDP TIRERELRER
1310 1320 1330 1340 1350
EIREREIRER ELRERMKPGF EVKPPELDPL HPATNPMEHF ARHSALTIPP
1360 1370 1380 1390 1400
AAGPHPFASF HPGLNPLERE RLALAGPQLR PEMSYPDRLA AERIHAERMA
1410 1420 1430 1440 1450
SLTSDPLARL QMFNVTPHHH QHSHIHSHLH LHQQDPLHQG SAGPVHPLVD
1460 1470 1480 1490 1500
PLTAGPHLAR FPYPPGTLPN PLLGQPPHEH EMLRHPVFGT PYPRDLPGAI
1510 1520 1530 1540 1550
PPPMSAAHQL QAMHAQSAEL QRLAMEQQWL HGHPHMHGGH LPSQEDYYSR

LKKEGDKQL
Length:1,559
Mass (Da):171,815
Last modified:January 10, 2006 - v2
Checksum:i2BE2A7A93CAE0600
GO

Sequence cautioni

The sequence AAA98970.1 differs from that shown. Reason: Frameshift at several positions. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti342 – 3432MC → IVV in AAA98970 (PubMed:9173919).Curated
Sequence conflicti355 – 3551A → G in AAA98970 (PubMed:9173919).Curated
Sequence conflicti360 – 3601T → N in AAA98970 (PubMed:9173919).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U44091 mRNA. Translation: AAA98970.1. Frameshift.
AABR03040456 Genomic DNA. No translation available.
AABR03040863 Genomic DNA. No translation available.
AABR03040940 Genomic DNA. No translation available.
AABR03041203 Genomic DNA. No translation available.
PIRiT42731.
RefSeqiNP_446337.2. NM_053885.2.
UniGeneiRn.10277.

Genome annotation databases

EnsembliENSRNOT00000024443; ENSRNOP00000024443; ENSRNOG00000017940.
GeneIDi116665.
KEGGirno:116665.
UCSCiRGD:629475. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U44091 mRNA. Translation: AAA98970.1. Frameshift.
AABR03040456 Genomic DNA. No translation available.
AABR03040863 Genomic DNA. No translation available.
AABR03040940 Genomic DNA. No translation available.
AABR03041203 Genomic DNA. No translation available.
PIRiT42731.
RefSeqiNP_446337.2. NM_053885.2.
UniGeneiRn.10277.

3D structure databases

ProteinModelPortaliQ62901.
SMRiQ62901. Positions 391-445.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000024443.

PTM databases

iPTMnetiQ62901.
PhosphoSiteiQ62901.

Proteomic databases

PaxDbiQ62901.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000024443; ENSRNOP00000024443; ENSRNOG00000017940.
GeneIDi116665.
KEGGirno:116665.
UCSCiRGD:629475. rat.

Organism-specific databases

CTDi473.
RGDi629475. Rere.

Phylogenomic databases

eggNOGiKOG2133. Eukaryota.
ENOG410ZIND. LUCA.
HOGENOMiHOG000231091.
HOVERGENiHBG079774.
InParanoidiQ62901.
KOiK05628.
OrthoDBiEOG7D59MN.
PhylomeDBiQ62901.
TreeFamiTF328554.

Miscellaneous databases

PROiQ62901.

Gene expression databases

ExpressionAtlasiQ62901. baseline and differential.
GenevisibleiQ62901. RN.

Family and domain databases

InterProiIPR002951. Atrophin-like.
IPR001025. BAH_dom.
IPR000949. ELM2_dom.
IPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR000679. Znf_GATA.
[Graphical view]
PfamiPF03154. Atrophin-1. 1 hit.
PF01426. BAH. 1 hit.
PF01448. ELM2. 1 hit.
PF00320. GATA. 1 hit.
[Graphical view]
SMARTiSM00439. BAH. 1 hit.
SM01189. ELM2. 1 hit.
SM00717. SANT. 1 hit.
SM00401. ZnF_GATA. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
PROSITEiPS51038. BAH. 1 hit.
PS51156. ELM2. 1 hit.
PS51293. SANT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning and characterization of an atrophin-1 (DRPLA disease gene)-related protein."
    Khan F.A., Margolis R.L., Loev S.L., Sharp A.H., Li S.-H., Ross C.A.
    Neurobiol. Dis. 3:121-128(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53; SER-56; SER-593; SER-599; SER-641; SER-655; SER-674 AND SER-678, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRERE_RAT
AccessioniPrimary (citable) accession number: Q62901
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: January 10, 2006
Last modified: June 8, 2016
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.