Q9P2R6 (RERE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Arginine-glutamic acid dipeptide repeats protein

Alternative name(s):
Atrophin-1-like protein
Atrophin-1-related protein

Gene names

Name:	RERE
Synonyms:	ARG, ARP, ATN1L, KIAA0458

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1566 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.2
Subunit structure	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. Ref.1 Ref.9
Subcellular location	Nucleus. Note: Localized in nuclear bodies of variables size. Colocalized with PML and BAX in nuclear PODs. Ref.1 Ref.2
Tissue specificity	Widely expressed. Expressed in tumor cell lines. Ref.1 Ref.2 Ref.6
Domain	The interaction with ATN1 is mediated by the coiled coil domain.
Involvement in disease	A chromosomal aberration involving RERE is found in the neuroblastoma cell line NGP. Translocation t(1;15)(p36.2;q24).
Sequence similarities	Contains 1 BAH domain. Contains 1 ELM2 domain. Contains 1 GATA-type zinc finger. Contains 1 SANT domain.
Sequence caution	The sequence AAC31120.1 differs from that shown. Reason: Frameshift at positions 588 and 596. The sequence AAD27584.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement
Domain	Coiled coil Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Developmental protein Repressor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	NLS-bearing substrate import into nucleus Traceable author statement Ref.1. Source: ProtInc chromatin remodeling Inferred from electronic annotation. Source: Compara multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	histone deacetylase complex Inferred from electronic annotation. Source: Compara mitochondrion Inferred from direct assay. Source: HPA nucleus Non-traceable author statement Ref.1. Source: UniProtKB
Molecular_function	chromatin binding Inferred from electronic annotation. Source: InterPro poly-glutamine tract binding Traceable author statement Ref.1. Source: ProtInc sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ATN1	P54259	3	EBI-948076,EBI-945980

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q9P2R6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9P2R6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-554: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1566

1566

Arginine-glutamic acid dipeptide repeats protein

PRO_0000083504

Regions

Domain

103 – 283

181

BAH

Domain

284 – 387

104

ELM2

Domain

391 – 443

53

SANT

Zinc finger

507 – 532

26

GATA-type

Coiled coil

1156 – 1211

56

Potential

Compositional bias

738 – 1118

381

Pro-rich

Compositional bias

1179 – 1204

26

Arg/Glu-rich (mixed charge)

Compositional bias

1300 – 1322

23

Arg/Glu-rich (mixed charge)

Compositional bias

1425 – 1445

21

His-rich

Compositional bias

1451 – 1510

60

Pro-rich

Amino acid modifications

Modified residue

53

1

Phosphoserine Ref.8 Ref.12

Modified residue

56

1

Phosphoserine Ref.8 Ref.12

Modified residue

304

1

Phosphoserine Ref.7

Modified residue

600

1

Phosphoserine By similarity

Modified residue

642

1

Phosphoserine Ref.8 Ref.11 Ref.12

Modified residue

656

1

Phosphoserine Ref.12

Modified residue

675

1

Phosphoserine Ref.10 Ref.12

Modified residue

679

1

Phosphoserine Ref.10 Ref.12

Modified residue

1106

1

Phosphoserine Ref.7 Ref.12

Natural variations

Alternative sequence

1 – 554

554

Missing in isoform 2.

VSP_016878

Experimental info

Sequence conflict

65

1

S → G in BAA95898. Ref.1

Sequence conflict

68

1

A → T in BAA95898. Ref.1

Sequence conflict

114 – 115

2

ES → VC in BAA95898. Ref.1

Sequence conflict

643

1

P → L in AAC31120. Ref.3

Sequence conflict

921

1

A → G in BAA95898. Ref.1

Sequence conflict

940

1

P → A in BAA95898. Ref.1

Sequence conflict

957

1

F → L in AAD27584. Ref.6

Sequence conflict

977

1

T → K no nucleotide entry Ref.2

Sequence conflict

984

1

H → N no nucleotide entry Ref.2

Sequence conflict

1009 – 1011

3

QSQ → RTR in AAD27584. Ref.6

Sequence conflict

1117

1

E → D in AAD27584. Ref.6

Sequence conflict

1272

1

H → Q in AAD27584. Ref.6

Sequence conflict

1489 – 1490

2

ML → IV in BAA95898. Ref.1

Sequence conflict

1529

1

R → K in AAD27584. Ref.6

Sequence conflict

1536

1

W → C in AAD27584. Ref.6

Sequence conflict

1543

1

M → R in AAD27584. Ref.6

Secondary structure

1

.

.

.

.

.

.

.

1566

Helix Strand Turn

Details...

Helix

398 – 410

13

Helix

415 – 421

7

Helix

428 – 439

12

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 10, 2006. Version 2. Checksum: ECA4A22026E3E96F	FASTA	1,566	172,424
	10 20 30 40 50 60 MTADKDKDKD KEKDRDRDRD REREKRDKAR ESENSRPRRS CTLEGGAKNY AESDHSEDED 70 80 90 100 110 120 NDNNSATAEE STKKNKKKPP KKKSRYERTD TGEITSYITE DDVVYRPGDC VYIESRRPNT 130 140 150 160 170 180 PYFICSIQDF KLVHNSQACC RSPTPALCDP PACSLPVASQ PPQHLSEAGR GPVGSKRDHL 190 200 210 220 230 240 LMNVKWYYRQ SEVPDSVYQH LVQDRHNEND SGRELVITDP VIKNRELFIS DYVDTYHAAA 250 260 270 280 290 300 LRGKCNISHF SDIFAAREFK ARVDSFFYIL GYNPETRRLN STQGEIRVGP SHQAKLPDLQ 310 320 330 340 350 360 PFPSPDGDTV TQHEELVWMP GVNDCDLLMY LRAARSMAAF AGMCDGGSTE DGCVAASRDD 370 380 390 400 410 420 TTLNALNTLH ESGYDAGKAL QRLVKKPVPK LIEKCWTEDE VKRFVKGLRQ YGKNFFRIRK 430 440 450 460 470 480 ELLPNKETGE LITFYYYWKK TPEAASSRAH RRHRRQAVFR RIKTRTASTP VNTPSRPPSS 490 500 510 520 530 540 EFLDLSSASE DDFDSEDSEQ ELKGYACRHC FTTTSKDWHH GGRENILLCT DCRIHFKKYG 550 560 570 580 590 600 ELPPIEKPVD PPPFMFKPVK EEDDGLSGKH SMRTRRSRGS MSTLRSGRKK QPASPDGRTS 610 620 630 640 650 660 PINEDIRSSG RNSPSAASTS SNDSKAETVK KSAKKVKEEA SSPLKSNKRQ REKVASDTEE 670 680 690 700 710 720 ADRTSSKKTK TQEISRPNSP SEGEGESSDS RSVNDEGSSD PKDIDQDNRS TSPSIPSPQD 730 740 750 760 770 780 NESDSDSSAQ QQMLQAQPPA LQAPTGVTPA PSSAPPGTPQ LPTPGPTPSA TAVPPQGSPT 790 800 810 820 830 840 ASQAPNQPQA PTAPVPHTHI QQAPALHPQR PPSPHPPPHP SPHPPLQPLT GSAGQPSAPS 850 860 870 880 890 900 HAQPPLHGQG PPGPHSLQAG PLLQHPGPPQ PFGLPPQASQ GQAPLGTSPA AAYPHTSLQL 910 920 930 940 950 960 PASQSALQSQ QPPREQPLPP APLAMPHIKP PPTTPIPQLP APQAHKHPPH LSGPSPFSMN 970 980 990 1000 1010 1020 ANLPPPPALK PLSSLSTHHP PSAHPPPLQL MPQSQPLPSS PAQPPGLTQS QNLPPPPASH 1030 1040 1050 1060 1070 1080 PPTGLHQVAP QPPFAQHPFV PGGPPPITPP TCPSTSTPPA GPGTSAQPPC SGAAASGGSI 1090 1100 1110 1120 1130 1140 AGGSSCPLPT VQIKEEALDD AEEPESPPPP PRSPSPEPTV VDTPSHASQS ARFYKHLDRG 1150 1160 1170 1180 1190 1200 YNSCARTDLY FMPLAGSKLA KKREEAIEKA KREAEQKARE EREREKEKEK ERERERERER 1210 1220 1230 1240 1250 1260 EAERAAKASS SAHEGRLSDP QLSGPGHMRP SFEPPPTTIA AVPPYIGPDT PALRTLSEYA 1270 1280 1290 1300 1310 1320 RPHVMSPTNR NHPFYMPLNP TDPLLAYHMP GLYNVDPTIR ERELREREIR EREIRERELR 1330 1340 1350 1360 1370 1380 ERMKPGFEVK PPELDPLHPA ANPMEHFARH SALTIPPTAG PHPFASFHPG LNPLERERLA 1390 1400 1410 1420 1430 1440 LAGPQLRPEM SYPDRLAAER IHAERMASLT SDPLARLQMF NVTPHHHQHS HIHSHLHLHQ 1450 1460 1470 1480 1490 1500 QDPLHQGSAG PVHPLVDPLT AGPHLARFPY PPGTLPNPLL GQPPHEHEML RHPVFGTPYP 1510 1520 1530 1540 1550 1560 RDLPGAIPPP MSAAHQLQAM HAQSAELQRL AMEQQWLHGH PHMHGGHLPS QEDYYSRLKK EGDKQL
	Isoform 2 [UniParc]. Checksum: 54B60DCBF0FB85FE	FASTA	1,012	109,048
	10 20 30 40 50 60 MFKPVKEEDD GLSGKHSMRT RRSRGSMSTL RSGRKKQPAS PDGRTSPINE DIRSSGRNSP 70 80 90 100 110 120 SAASTSSNDS KAETVKKSAK KVKEEASSPL KSNKRQREKV ASDTEEADRT SSKKTKTQEI 130 140 150 160 170 180 SRPNSPSEGE GESSDSRSVN DEGSSDPKDI DQDNRSTSPS IPSPQDNESD SDSSAQQQML 190 200 210 220 230 240 QAQPPALQAP TGVTPAPSSA PPGTPQLPTP GPTPSATAVP PQGSPTASQA PNQPQAPTAP 250 260 270 280 290 300 VPHTHIQQAP ALHPQRPPSP HPPPHPSPHP PLQPLTGSAG QPSAPSHAQP PLHGQGPPGP 310 320 330 340 350 360 HSLQAGPLLQ HPGPPQPFGL PPQASQGQAP LGTSPAAAYP HTSLQLPASQ SALQSQQPPR 370 380 390 400 410 420 EQPLPPAPLA MPHIKPPPTT PIPQLPAPQA HKHPPHLSGP SPFSMNANLP PPPALKPLSS 430 440 450 460 470 480 LSTHHPPSAH PPPLQLMPQS QPLPSSPAQP PGLTQSQNLP PPPASHPPTG LHQVAPQPPF 490 500 510 520 530 540 AQHPFVPGGP PPITPPTCPS TSTPPAGPGT SAQPPCSGAA ASGGSIAGGS SCPLPTVQIK 550 560 570 580 590 600 EEALDDAEEP ESPPPPPRSP SPEPTVVDTP SHASQSARFY KHLDRGYNSC ARTDLYFMPL 610 620 630 640 650 660 AGSKLAKKRE EAIEKAKREA EQKAREERER EKEKEKERER EREREREAER AAKASSSAHE 670 680 690 700 710 720 GRLSDPQLSG PGHMRPSFEP PPTTIAAVPP YIGPDTPALR TLSEYARPHV MSPTNRNHPF 730 740 750 760 770 780 YMPLNPTDPL LAYHMPGLYN VDPTIREREL REREIREREI RERELRERMK PGFEVKPPEL 790 800 810 820 830 840 DPLHPAANPM EHFARHSALT IPPTAGPHPF ASFHPGLNPL ERERLALAGP QLRPEMSYPD 850 860 870 880 890 900 RLAAERIHAE RMASLTSDPL ARLQMFNVTP HHHQHSHIHS HLHLHQQDPL HQGSAGPVHP 910 920 930 940 950 960 LVDPLTAGPH LARFPYPPGT LPNPLLGQPP HEHEMLRHPV FGTPYPRDLP GAIPPPMSAA 970 980 990 1000 1010 HQLQAMHAQS AELQRLAMEQ QWLHGHPHMH GGHLPSQEDY YSRLKKEGDK QL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Protein binding of a DRPLA family through arginine-glutamic acid dipeptide repeats is enhanced by extended polyglutamine." Yanagisawa H., Bundo M., Miyashita T., Okamura-Oho Y., Tadokoro K., Tokunaga K., Yamada M. Hum. Mol. Genet. 9:1433-1442(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH ATN1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]	"Human RERE is localized to nuclear promyelocytic leukemia oncogenic domains and enhances apoptosis." Waerner T., Gardellin P., Pfizenmaier K., Weith A., Kraut N. Cell Growth Differ. 12:201-210(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[3]	"Cloning and localization of human atrophin-1 (DRPLA) related gene." Xia J.-H., Liu C.-Y., Ruan Q.-G., Wang D.-A., Deng H.-X. Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2).
[4]	"The DNA sequence and biological annotation of human chromosome 1." 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. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"Characterization of cDNA clones in size-fractionated cDNA libraries from human brain." Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., Nomura N., Ohara O. DNA Res. 4:345-349(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-1566 (ISOFORM 1). Tissue: Brain.
[6]	"Identification and characterization of novel genes located at the t(1;15)(p36.2;q24) translocation breakpoint in the neuroblastoma cell line NGP." Amler L.C., Bauer A., Corvi R., Dihlmann S., Praml C., Cavenee W.K., Schwab M., Hampton G.M. Genomics 64:195-202(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 555-1566, TISSUE SPECIFICITY, CHROMOSOMAL TRANSLOCATION.
[7]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-1106, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53; SER-56 AND SER-642, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Atrophin proteins interact with the Fat1 cadherin and regulate migration and orientation in vascular smooth muscle cells." Hou R., Sibinga N.E. J. Biol. Chem. 284:6955-6965(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FAT1.
[10]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675 AND SER-679, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." 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. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-642, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53; SER-56; SER-642; SER-656; SER-675; SER-679 AND SER-1106, MASS SPECTROMETRY.
[13]	"Solution structure of the SANT domain in arginine-glutamic acid dipeptide (RE) repeats." RIKEN structural genomics initiative (RSGI) Submitted (OCT-2007) to the PDB data bank Cited for: STRUCTURE BY NMR OF 392-446.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB036737 mRNA. Translation: BAA95898.1.
AF016005 mRNA. Translation: AAC31120.1. Frameshift.
AF041104 , AF041096, AF041097, AF041098, AF041099, AF041100, AF041101, AF041102, AF041103 Genomic DNA. Translation: AAC28264.1.
AL356072, AL096855, AL357713 Genomic DNA. Translation: CAH70516.1.
AL357713, AL096855, AL356072 Genomic DNA. Translation: CAH73433.1.
AL096855, AL356072, AL357713 Genomic DNA. Translation: CAI19208.1.
AB007927 mRNA. Translation: BAA32303.3.
AF118275 mRNA. Translation: AAD27584.1. Different initiation.

IPI

IPI00185027.
IPI01009383.

RefSeq

NP_001036146.1. NM_001042681.1.
NP_001036147.1. NM_001042682.1.
NP_036234.3. NM_012102.3.

UniGene

Hs.463041.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2YQK	NMR	-	A	392-441	[»]

ProteinModelPortal

Q9P2R6.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9P2R6. 20 interactions.

MINT

MINT-2820762.

STRING

9606.ENSP00000338629.

PTM databases

PhosphoSite

Q9P2R6.

Polymorphism databases

DMDM

85540730.

Proteomic databases

PaxDb

Q9P2R6.

PRIDE

Q9P2R6.

Protocols and materials databases

DNASU

473.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000337907; ENSP00000338629; ENSG00000142599.
ENST00000400908; ENSP00000383700; ENSG00000142599.
ENST00000476556; ENSP00000422246; ENSG00000142599.

GeneID

473.

KEGG

hsa:473.

UCSC

uc001apd.3. human.

Organism-specific databases

CTD

473.

GeneCards

GC01M008412.

HGNC

HGNC:9965. RERE.

HPA

HPA024093.

MIM

605226. gene.

neXtProt

NX_Q9P2R6.

PharmGKB

PA34332.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG331121.

HOGENOM

HOG000231091.

HOVERGEN

HBG079774.

InParanoid

Q9P2R6.

KO

K05628.

OMA

HHPPSAH.

OrthoDB

EOG4XGZZB.

PhylomeDB

Q9P2R6.

Gene expression databases

ArrayExpress

Q9P2R6.

Bgee

Q9P2R6.

CleanEx

HS_RERE.

Genevestigator

Q9P2R6.

GermOnline

ENSG00000142599. Homo sapiens.

Family and domain databases

InterPro

IPR002951. Atrophin-like.
IPR001025. BAH_dom.
IPR000949. ELM2_dom.
IPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR000679. Znf_GATA.
[Graphical view]

Pfam

PF03154. Atrophin-1. 1 hit.
PF01426. BAH. 1 hit.
PF01448. ELM2. 1 hit.
PF00320. GATA. 1 hit.
[Graphical view]

SMART

SM00439. BAH. 1 hit.
SM00717. SANT. 1 hit.
SM00401. ZnF_GATA. 1 hit.
[Graphical view]

SUPFAM

SSF46689. Homeodomain_like. 1 hit.

PROSITE

PS51038. BAH. 1 hit.
PS51156. ELM2. 1 hit.
PS00344. GATA_ZN_FINGER_1. False negative.
PS50114. GATA_ZN_FINGER_2. False negative.
PS51293. SANT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

RERE. human.

EvolutionaryTrace

Q9P2R6.

GenomeRNAi

473.

NextBio

1955.

SOURCE

Search...

Entry information

Entry name

RERE_HUMAN

Accession

Primary (citable) accession number: Q9P2R6
Secondary accession number(s): O43393 , O75046, O75359, Q5VXL9, Q6P6B9, Q9Y2W4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	January 10, 2006
Last modified:	May 1, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.