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Q9P2R6

- RERE_HUMAN

UniProt

Q9P2R6 - RERE_HUMAN

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Protein

Arginine-glutamic acid dipeptide repeats protein

Gene

RERE

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 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. Overexpression of RERE recruits BAX to the nucleus particularly to POD and triggers caspase-3 activation, leading to cell death.1 Publication

Regions

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

GO - Molecular functioni

  1. chromatin binding Source: InterPro
  2. poly-glutamine tract binding Source: ProtInc
  3. sequence-specific DNA binding Source: InterPro
  4. sequence-specific DNA binding transcription factor activity Source: InterPro
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. chromatin remodeling Source: Ensembl
  2. multicellular organismal development Source: UniProtKB-KW
  3. NLS-bearing protein import into nucleus Source: ProtInc
  4. transcription, DNA-templated Source: UniProtKB-KW
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-like protein
Atrophin-1-related protein
Gene namesi
Name:RERE
Synonyms:ARG, ARP, ATN1L, KIAA0458
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:9965. RERE.

Subcellular locationi

Nucleus 2 PublicationsPROSITE-ProRule annotation
Note: Localized in nuclear bodies of variables size. Colocalized with PML and BAX in nuclear PODs.

GO - Cellular componenti

  1. histone deacetylase complex Source: Ensembl
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving RERE is found in the neuroblastoma cell line NGP. Translocation t(1;15)(p36.2;q24).

Organism-specific databases

PharmGKBiPA34332.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15661566Arginine-glutamic acid dipeptide repeats proteinPRO_0000083504Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 531Phosphoserine2 Publications
Modified residuei56 – 561Phosphoserine2 Publications
Modified residuei304 – 3041Phosphoserine1 Publication
Modified residuei642 – 6421Phosphoserine3 Publications
Modified residuei656 – 6561Phosphoserine1 Publication
Modified residuei675 – 6751Phosphoserine2 Publications
Modified residuei679 – 6791Phosphoserine2 Publications
Modified residuei1106 – 11061Phosphoserine2 Publications
Modified residuei1158 – 11581N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9P2R6.
PaxDbiQ9P2R6.
PRIDEiQ9P2R6.

PTM databases

PhosphoSiteiQ9P2R6.

Expressioni

Tissue specificityi

Widely expressed. Expressed in tumor cell lines.3 Publications

Gene expression databases

BgeeiQ9P2R6.
CleanExiHS_RERE.
ExpressionAtlasiQ9P2R6. baseline and differential.
GenevestigatoriQ9P2R6.

Organism-specific databases

HPAiHPA024093.

Interactioni

Subunit structurei

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.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ATN1P542593EBI-948076,EBI-945980
EHMT2Q96KQ73EBI-948076,EBI-744366

Protein-protein interaction databases

BioGridi106963. 26 interactions.
IntActiQ9P2R6. 23 interactions.
MINTiMINT-2820762.
STRINGi9606.ENSP00000338629.

Structurei

Secondary structure

1
1566
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi398 – 41013Combined sources
Helixi415 – 4217Combined sources
Helixi428 – 43912Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YQKNMR-A392-441[»]
ProteinModelPortaliQ9P2R6.
SMRiQ9P2R6. Positions 284-446.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9P2R6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini103 – 283181BAHPROSITE-ProRule annotationAdd
BLAST
Domaini284 – 387104ELM2PROSITE-ProRule annotationAdd
BLAST
Domaini391 – 44353SANTPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1156 – 121156Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi738 – 1118381Pro-richAdd
BLAST
Compositional biasi1179 – 120426Arg/Glu-rich (mixed charge)Add
BLAST
Compositional biasi1300 – 132223Arg/Glu-rich (mixed charge)Add
BLAST
Compositional biasi1425 – 144521His-richAdd
BLAST
Compositional biasi1451 – 151060Pro-richAdd
BLAST

Domaini

The interaction with ATN1 is mediated by the coiled coil domain.

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

eggNOGiNOG331121.
GeneTreeiENSGT00580000081398.
HOGENOMiHOG000231091.
HOVERGENiHBG079774.
InParanoidiQ9P2R6.
KOiK05628.
OMAiHHPPSAH.
OrthoDBiEOG7D59MN.
PhylomeDBiQ9P2R6.
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.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q9P2R6-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MTADKDKDKD KEKDRDRDRD REREKRDKAR ESENSRPRRS CTLEGGAKNY
60 70 80 90 100
AESDHSEDED NDNNSATAEE STKKNKKKPP KKKSRYERTD TGEITSYITE
110 120 130 140 150
DDVVYRPGDC VYIESRRPNT PYFICSIQDF KLVHNSQACC RSPTPALCDP
160 170 180 190 200
PACSLPVASQ PPQHLSEAGR GPVGSKRDHL LMNVKWYYRQ SEVPDSVYQH
210 220 230 240 250
LVQDRHNEND SGRELVITDP VIKNRELFIS DYVDTYHAAA LRGKCNISHF
260 270 280 290 300
SDIFAAREFK ARVDSFFYIL GYNPETRRLN STQGEIRVGP SHQAKLPDLQ
310 320 330 340 350
PFPSPDGDTV TQHEELVWMP GVNDCDLLMY LRAARSMAAF AGMCDGGSTE
360 370 380 390 400
DGCVAASRDD TTLNALNTLH ESGYDAGKAL QRLVKKPVPK LIEKCWTEDE
410 420 430 440 450
VKRFVKGLRQ YGKNFFRIRK ELLPNKETGE LITFYYYWKK TPEAASSRAH
460 470 480 490 500
RRHRRQAVFR RIKTRTASTP VNTPSRPPSS EFLDLSSASE DDFDSEDSEQ
510 520 530 540 550
ELKGYACRHC FTTTSKDWHH GGRENILLCT DCRIHFKKYG ELPPIEKPVD
560 570 580 590 600
PPPFMFKPVK EEDDGLSGKH SMRTRRSRGS MSTLRSGRKK QPASPDGRTS
610 620 630 640 650
PINEDIRSSG RNSPSAASTS SNDSKAETVK KSAKKVKEEA SSPLKSNKRQ
660 670 680 690 700
REKVASDTEE ADRTSSKKTK TQEISRPNSP SEGEGESSDS RSVNDEGSSD
710 720 730 740 750
PKDIDQDNRS TSPSIPSPQD NESDSDSSAQ QQMLQAQPPA LQAPTGVTPA
760 770 780 790 800
PSSAPPGTPQ LPTPGPTPSA TAVPPQGSPT ASQAPNQPQA PTAPVPHTHI
810 820 830 840 850
QQAPALHPQR PPSPHPPPHP SPHPPLQPLT GSAGQPSAPS HAQPPLHGQG
860 870 880 890 900
PPGPHSLQAG PLLQHPGPPQ PFGLPPQASQ GQAPLGTSPA AAYPHTSLQL
910 920 930 940 950
PASQSALQSQ QPPREQPLPP APLAMPHIKP PPTTPIPQLP APQAHKHPPH
960 970 980 990 1000
LSGPSPFSMN ANLPPPPALK PLSSLSTHHP PSAHPPPLQL MPQSQPLPSS
1010 1020 1030 1040 1050
PAQPPGLTQS QNLPPPPASH PPTGLHQVAP QPPFAQHPFV PGGPPPITPP
1060 1070 1080 1090 1100
TCPSTSTPPA GPGTSAQPPC SGAAASGGSI AGGSSCPLPT VQIKEEALDD
1110 1120 1130 1140 1150
AEEPESPPPP PRSPSPEPTV VDTPSHASQS ARFYKHLDRG YNSCARTDLY
1160 1170 1180 1190 1200
FMPLAGSKLA KKREEAIEKA KREAEQKARE EREREKEKEK ERERERERER
1210 1220 1230 1240 1250
EAERAAKASS SAHEGRLSDP QLSGPGHMRP SFEPPPTTIA AVPPYIGPDT
1260 1270 1280 1290 1300
PALRTLSEYA RPHVMSPTNR NHPFYMPLNP TDPLLAYHMP GLYNVDPTIR
1310 1320 1330 1340 1350
ERELREREIR EREIRERELR ERMKPGFEVK PPELDPLHPA ANPMEHFARH
1360 1370 1380 1390 1400
SALTIPPTAG PHPFASFHPG LNPLERERLA LAGPQLRPEM SYPDRLAAER
1410 1420 1430 1440 1450
IHAERMASLT SDPLARLQMF NVTPHHHQHS HIHSHLHLHQ QDPLHQGSAG
1460 1470 1480 1490 1500
PVHPLVDPLT AGPHLARFPY PPGTLPNPLL GQPPHEHEML RHPVFGTPYP
1510 1520 1530 1540 1550
RDLPGAIPPP MSAAHQLQAM HAQSAELQRL AMEQQWLHGH PHMHGGHLPS
1560
QEDYYSRLKK EGDKQL
Length:1,566
Mass (Da):172,424
Last modified:January 10, 2006 - v2
Checksum:iECA4A22026E3E96F
GO
Isoform 2 (identifier: Q9P2R6-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,012
Mass (Da):109,048
Checksum:i54B60DCBF0FB85FE
GO

Sequence cautioni

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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 651S → G in BAA95898. (PubMed:10814707)Curated
Sequence conflicti68 – 681A → T in BAA95898. (PubMed:10814707)Curated
Sequence conflicti114 – 1152ES → VC in BAA95898. (PubMed:10814707)Curated
Sequence conflicti643 – 6431P → L in AAC31120. 1 PublicationCurated
Sequence conflicti921 – 9211A → G in BAA95898. (PubMed:10814707)Curated
Sequence conflicti940 – 9401P → A in BAA95898. (PubMed:10814707)Curated
Sequence conflicti957 – 9571F → L in AAD27584. (PubMed:10729226)Curated
Sequence conflicti977 – 9771T → K no nucleotide entry (PubMed:11331249)Curated
Sequence conflicti984 – 9841H → N no nucleotide entry (PubMed:11331249)Curated
Sequence conflicti1009 – 10113QSQ → RTR in AAD27584. (PubMed:10729226)Curated
Sequence conflicti1117 – 11171E → D in AAD27584. (PubMed:10729226)Curated
Sequence conflicti1272 – 12721H → Q in AAD27584. (PubMed:10729226)Curated
Sequence conflicti1489 – 14902ML → IV in BAA95898. (PubMed:10814707)Curated
Sequence conflicti1529 – 15291R → K in AAD27584. (PubMed:10729226)Curated
Sequence conflicti1536 – 15361W → C in AAD27584. (PubMed:10729226)Curated
Sequence conflicti1543 – 15431M → R in AAD27584. (PubMed:10729226)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 554554Missing in isoform 2. 1 PublicationVSP_016878Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS41243.1. [Q9P2R6-2]
CCDS95.1. [Q9P2R6-1]
RefSeqiNP_001036146.1. NM_001042681.1. [Q9P2R6-1]
NP_001036147.1. NM_001042682.1. [Q9P2R6-2]
NP_036234.3. NM_012102.3. [Q9P2R6-1]
XP_005263521.1. XM_005263464.1. [Q9P2R6-1]
XP_006710716.1. XM_006710653.1. [Q9P2R6-1]
UniGeneiHs.463041.

Genome annotation databases

EnsembliENST00000337907; ENSP00000338629; ENSG00000142599. [Q9P2R6-1]
ENST00000400908; ENSP00000383700; ENSG00000142599. [Q9P2R6-1]
ENST00000476556; ENSP00000422246; ENSG00000142599. [Q9P2R6-2]
GeneIDi473.
KEGGihsa:473.
UCSCiuc001apd.3. human. [Q9P2R6-1]

Polymorphism databases

DMDMi85540730.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS41243.1. [Q9P2R6-2 ]
CCDS95.1. [Q9P2R6-1 ]
RefSeqi NP_001036146.1. NM_001042681.1. [Q9P2R6-1 ]
NP_001036147.1. NM_001042682.1. [Q9P2R6-2 ]
NP_036234.3. NM_012102.3. [Q9P2R6-1 ]
XP_005263521.1. XM_005263464.1. [Q9P2R6-1 ]
XP_006710716.1. XM_006710653.1. [Q9P2R6-1 ]
UniGenei Hs.463041.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2YQK NMR - A 392-441 [» ]
ProteinModelPortali Q9P2R6.
SMRi Q9P2R6. Positions 284-446.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106963. 26 interactions.
IntActi Q9P2R6. 23 interactions.
MINTi MINT-2820762.
STRINGi 9606.ENSP00000338629.

PTM databases

PhosphoSitei Q9P2R6.

Polymorphism databases

DMDMi 85540730.

Proteomic databases

MaxQBi Q9P2R6.
PaxDbi Q9P2R6.
PRIDEi Q9P2R6.

Protocols and materials databases

DNASUi 473.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000337907 ; ENSP00000338629 ; ENSG00000142599 . [Q9P2R6-1 ]
ENST00000400908 ; ENSP00000383700 ; ENSG00000142599 . [Q9P2R6-1 ]
ENST00000476556 ; ENSP00000422246 ; ENSG00000142599 . [Q9P2R6-2 ]
GeneIDi 473.
KEGGi hsa:473.
UCSCi uc001apd.3. human. [Q9P2R6-1 ]

Organism-specific databases

CTDi 473.
GeneCardsi GC01M008412.
HGNCi HGNC:9965. RERE.
HPAi HPA024093.
MIMi 605226. gene.
neXtProti NX_Q9P2R6.
PharmGKBi PA34332.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG331121.
GeneTreei ENSGT00580000081398.
HOGENOMi HOG000231091.
HOVERGENi HBG079774.
InParanoidi Q9P2R6.
KOi K05628.
OMAi HHPPSAH.
OrthoDBi EOG7D59MN.
PhylomeDBi Q9P2R6.
TreeFami TF328554.

Miscellaneous databases

ChiTaRSi RERE. human.
EvolutionaryTracei Q9P2R6.
GeneWikii RERE.
GenomeRNAii 473.
NextBioi 1955.
PROi Q9P2R6.
SOURCEi Search...

Gene expression databases

Bgeei Q9P2R6.
CleanExi HS_RERE.
ExpressionAtlasi Q9P2R6. baseline and differential.
Genevestigatori Q9P2R6.

Family and domain databases

InterProi IPR002951. Atrophin-like.
IPR001025. BAH_dom.
IPR000949. ELM2_dom.
IPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR000679. Znf_GATA.
[Graphical view ]
Pfami PF03154. Atrophin-1. 1 hit.
PF01426. BAH. 1 hit.
PF01448. ELM2. 1 hit.
PF00320. GATA. 1 hit.
[Graphical view ]
SMARTi SM00439. BAH. 1 hit.
SM00717. SANT. 1 hit.
SM00401. ZnF_GATA. 1 hit.
[Graphical view ]
SUPFAMi SSF46689. SSF46689. 1 hit.
PROSITEi PS51038. BAH. 1 hit.
PS51156. ELM2. 1 hit.
PS51293. SANT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53; SER-56 AND SER-642, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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.

Entry informationi

Entry nameiRERE_HUMAN
AccessioniPrimary (citable) accession number: Q9P2R6
Secondary accession number(s): O43393
, O75046, O75359, Q5VXL9, Q6P6B9, Q9Y2W4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: January 10, 2006
Last modified: October 29, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3