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Q9P2R6

- RERE_HUMAN

UniProt

Q9P2R6 - RERE_HUMAN

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
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 2 (10 Jan 2006)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    4. sequence-specific DNA binding Source: InterPro
    5. sequence-specific DNA binding transcription factor activity Source: InterPro
    6. 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

    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

    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

    ArrayExpressiQ9P2R6.
    BgeeiQ9P2R6.
    CleanExiHS_RERE.
    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. 25 interactions.
    IntActiQ9P2R6. 22 interactions.
    MINTiMINT-2820762.
    STRINGi9606.ENSP00000338629.

    Structurei

    Secondary structure

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

    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.
    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

    MTADKDKDKD KEKDRDRDRD REREKRDKAR ESENSRPRRS CTLEGGAKNY     50
    AESDHSEDED NDNNSATAEE STKKNKKKPP KKKSRYERTD TGEITSYITE 100
    DDVVYRPGDC VYIESRRPNT PYFICSIQDF KLVHNSQACC RSPTPALCDP 150
    PACSLPVASQ PPQHLSEAGR GPVGSKRDHL LMNVKWYYRQ SEVPDSVYQH 200
    LVQDRHNEND SGRELVITDP VIKNRELFIS DYVDTYHAAA LRGKCNISHF 250
    SDIFAAREFK ARVDSFFYIL GYNPETRRLN STQGEIRVGP SHQAKLPDLQ 300
    PFPSPDGDTV TQHEELVWMP GVNDCDLLMY LRAARSMAAF AGMCDGGSTE 350
    DGCVAASRDD TTLNALNTLH ESGYDAGKAL QRLVKKPVPK LIEKCWTEDE 400
    VKRFVKGLRQ YGKNFFRIRK ELLPNKETGE LITFYYYWKK TPEAASSRAH 450
    RRHRRQAVFR RIKTRTASTP VNTPSRPPSS EFLDLSSASE DDFDSEDSEQ 500
    ELKGYACRHC FTTTSKDWHH GGRENILLCT DCRIHFKKYG ELPPIEKPVD 550
    PPPFMFKPVK EEDDGLSGKH SMRTRRSRGS MSTLRSGRKK QPASPDGRTS 600
    PINEDIRSSG RNSPSAASTS SNDSKAETVK KSAKKVKEEA SSPLKSNKRQ 650
    REKVASDTEE ADRTSSKKTK TQEISRPNSP SEGEGESSDS RSVNDEGSSD 700
    PKDIDQDNRS TSPSIPSPQD NESDSDSSAQ QQMLQAQPPA LQAPTGVTPA 750
    PSSAPPGTPQ LPTPGPTPSA TAVPPQGSPT ASQAPNQPQA PTAPVPHTHI 800
    QQAPALHPQR PPSPHPPPHP SPHPPLQPLT GSAGQPSAPS HAQPPLHGQG 850
    PPGPHSLQAG PLLQHPGPPQ PFGLPPQASQ GQAPLGTSPA AAYPHTSLQL 900
    PASQSALQSQ QPPREQPLPP APLAMPHIKP PPTTPIPQLP APQAHKHPPH 950
    LSGPSPFSMN ANLPPPPALK PLSSLSTHHP PSAHPPPLQL MPQSQPLPSS 1000
    PAQPPGLTQS QNLPPPPASH PPTGLHQVAP QPPFAQHPFV PGGPPPITPP 1050
    TCPSTSTPPA GPGTSAQPPC SGAAASGGSI AGGSSCPLPT VQIKEEALDD 1100
    AEEPESPPPP PRSPSPEPTV VDTPSHASQS ARFYKHLDRG YNSCARTDLY 1150
    FMPLAGSKLA KKREEAIEKA KREAEQKARE EREREKEKEK ERERERERER 1200
    EAERAAKASS SAHEGRLSDP QLSGPGHMRP SFEPPPTTIA AVPPYIGPDT 1250
    PALRTLSEYA RPHVMSPTNR NHPFYMPLNP TDPLLAYHMP GLYNVDPTIR 1300
    ERELREREIR EREIRERELR ERMKPGFEVK PPELDPLHPA ANPMEHFARH 1350
    SALTIPPTAG PHPFASFHPG LNPLERERLA LAGPQLRPEM SYPDRLAAER 1400
    IHAERMASLT SDPLARLQMF NVTPHHHQHS HIHSHLHLHQ QDPLHQGSAG 1450
    PVHPLVDPLT AGPHLARFPY PPGTLPNPLL GQPPHEHEML RHPVFGTPYP 1500
    RDLPGAIPPP MSAAHQLQAM HAQSAELQRL AMEQQWLHGH PHMHGGHLPS 1550
    QEDYYSRLKK EGDKQL 1566
    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. 25 interactions.
    IntActi Q9P2R6. 22 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.
    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

    ArrayExpressi Q9P2R6.
    Bgeei Q9P2R6.
    CleanExi HS_RERE.
    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

    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 1, 2014
    This is version 130 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