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O43159

- RRP8_HUMAN

UniProt

O43159 - RRP8_HUMAN

Protein

Ribosomal RNA-processing protein 8

Gene

RRP8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (26 Apr 2005)
      Previous versions | rss
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    Functioni

    Essential component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD+/NADP+ ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. In the complex, RRP8 binds to H3K9me2 and probably acts as a methyltransferase. Its substrates are however unknown.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei281 – 2811S-adenosyl-L-methionine
    Binding sitei316 – 3161S-adenosyl-L-methionine; via carbonyl oxygen
    Binding sitei334 – 3341S-adenosyl-L-methionine
    Binding sitei346 – 3461S-adenosyl-L-methionine
    Binding sitei347 – 3471S-adenosyl-L-methionine
    Binding sitei363 – 3631S-adenosyl-L-methionine; via carbonyl oxygen

    GO - Molecular functioni

    1. methylated histone binding Source: UniProtKB
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. S-adenosylmethionine-dependent methyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. cellular response to glucose starvation Source: UniProtKB
    2. chromatin modification Source: UniProtKB-KW
    3. chromatin silencing at rDNA Source: UniProtKB
    4. intrinsic apoptotic signaling pathway by p53 class mediator Source: UniProtKB
    5. positive regulation of cell cycle arrest Source: UniProtKB
    6. regulation of transcription by glucose Source: UniProtKB
    7. rRNA processing Source: UniProtKB-KW
    8. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Methyltransferase, Repressor, Transferase

    Keywords - Biological processi

    rRNA processing, Transcription, Transcription regulation

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Enzyme and pathway databases

    ReactomeiREACT_200827. SIRT1 negatively regulates rRNA Expression.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribosomal RNA-processing protein 8 (EC:2.1.1.-)
    Alternative name(s):
    Cerebral protein 1
    Nucleomethylin
    Gene namesi
    Name:RRP8
    Synonyms:KIAA0409, NML
    ORF Names:hucep-1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:29030. RRP8.

    Subcellular locationi

    Nucleusnucleolus 3 Publications
    Note: Localizes at rDNA locus.

    GO - Cellular componenti

    1. chromatin silencing complex Source: UniProtKB
    2. cytoplasm Source: HPA
    3. nucleolus Source: UniProtKB
    4. nucleus Source: HPA
    5. plasma membrane Source: HPA
    6. rDNA heterochromatin Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA164725550.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 456456Ribosomal RNA-processing protein 8PRO_0000084090Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei62 – 621Phosphoserine2 Publications
    Modified residuei64 – 641Phosphoserine2 Publications
    Modified residuei171 – 1711Phosphoserine1 Publication
    Modified residuei223 – 2231Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO43159.
    PaxDbiO43159.
    PeptideAtlasiO43159.
    PRIDEiO43159.

    2D gel databases

    SWISS-2DPAGEO43159.

    PTM databases

    PhosphoSiteiO43159.

    Expressioni

    Gene expression databases

    ArrayExpressiO43159.
    BgeeiO43159.
    CleanExiHS_KIAA0409.
    GenevestigatoriO43159.

    Organism-specific databases

    HPAiHPA038487.

    Interactioni

    Subunit structurei

    Component of the eNoSC complex, composed of SIRT1, SUV39H1 and RRP8.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SIRT1Q96EB63EBI-2008793,EBI-1802965
    SUV39H1O434633EBI-2008793,EBI-349968

    Protein-protein interaction databases

    BioGridi116954. 5 interactions.
    DIPiDIP-46686N.
    IntActiO43159. 4 interactions.
    MINTiMINT-4526401.
    STRINGi9606.ENSP00000254605.

    Structurei

    Secondary structure

    1
    456
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi244 – 26017
    Helixi263 – 27210
    Helixi274 – 28815
    Beta strandi291 – 2933
    Helixi295 – 30410
    Beta strandi312 – 3165
    Helixi321 – 3255
    Beta strandi330 – 3367
    Beta strandi342 – 3454
    Beta strandi357 – 3648
    Helixi371 – 38111
    Beta strandi382 – 39211
    Helixi394 – 3963
    Helixi400 – 40910
    Beta strandi412 – 4187
    Beta strandi425 – 4317
    Helixi444 – 4463

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ZFUX-ray2.00A/B242-456[»]
    ProteinModelPortaliO43159.
    SMRiO43159. Positions 243-454.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO43159.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi65 – 706Poly-Glu

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0500.
    HOGENOMiHOG000164004.
    InParanoidiO43159.
    KOiK14850.
    OMAiLMGTNIR.
    OrthoDBiEOG7PGDRQ.
    PhylomeDBiO43159.
    TreeFamiTF313749.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR007823. Methyltransferase-rel.
    IPR029063. SAM-dependent_MTases-like.
    IPR023576. UbiE/COQ5_MeTrFase_CS.
    [Graphical view]
    PANTHERiPTHR12787. PTHR12787. 1 hit.
    PfamiPF05148. Methyltransf_8. 1 hit.
    [Graphical view]
    SUPFAMiSSF53335. SSF53335. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O43159-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFEEPEWAEA APVAAGLGPV ISRPPPAASS QNKGSKRRQL LATLRALEAA    50
    SLSQHPPSLC ISDSEEEEEE RKKKCPKKAS FASASAEVGK KGKKKCQKQG 100
    PPCSDSEEEV ERKKKCHKQA LVGSDSAEDE KRKRKCQKHA PINSAQHLDN 150
    VDQTGPKAWK GSTTNDPPKQ SPGSTSPKPP HTLSRKQWRN RQKNKRRCKN 200
    KFQPPQVPDQ APAEAPTEKT EVSPVPRTDS HEARAGALRA RMAQRLDGAR 250
    FRYLNEQLYS GPSSAAQRLF QEDPEAFLLY HRGFQSQVKK WPLQPVDRIA 300
    RDLRQRPASL VVADFGCGDC RLASSIRNPV HCFDLASLDP RVTVCDMAQV 350
    PLEDESVDVA VFCLSLMGTN IRDFLEEANR VLKPGGLLKV AEVSSRFEDV 400
    RTFLRAVTKL GFKIVSKDLT NSHFFLFDFQ KTGPPLVGPK AQLSGLQLQP 450
    CLYKRR 456
    Length:456
    Mass (Da):50,715
    Last modified:April 26, 2005 - v2
    Checksum:i49251E2A488DA1C4
    GO

    Sequence cautioni

    The sequence BAA23705.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti145 – 1451A → P.
    Corresponds to variant rs11040934 [ dbSNP | Ensembl ].
    VAR_051034
    Natural varianti329 – 3291P → S.
    Corresponds to variant rs17834692 [ dbSNP | Ensembl ].
    VAR_051035

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D87060 mRNA. Translation: BAB46916.1.
    AB007869 mRNA. Translation: BAA23705.1. Different initiation.
    BC001071 mRNA. Translation: AAH01071.1.
    CCDSiCCDS31411.1.
    RefSeqiNP_056139.1. NM_015324.3.
    UniGeneiHs.652255.

    Genome annotation databases

    EnsembliENST00000254605; ENSP00000254605; ENSG00000132275.
    GeneIDi23378.
    KEGGihsa:23378.
    UCSCiuc001med.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D87060 mRNA. Translation: BAB46916.1 .
    AB007869 mRNA. Translation: BAA23705.1 . Different initiation.
    BC001071 mRNA. Translation: AAH01071.1 .
    CCDSi CCDS31411.1.
    RefSeqi NP_056139.1. NM_015324.3.
    UniGenei Hs.652255.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ZFU X-ray 2.00 A/B 242-456 [» ]
    ProteinModelPortali O43159.
    SMRi O43159. Positions 243-454.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116954. 5 interactions.
    DIPi DIP-46686N.
    IntActi O43159. 4 interactions.
    MINTi MINT-4526401.
    STRINGi 9606.ENSP00000254605.

    PTM databases

    PhosphoSitei O43159.

    2D gel databases

    SWISS-2DPAGE O43159.

    Proteomic databases

    MaxQBi O43159.
    PaxDbi O43159.
    PeptideAtlasi O43159.
    PRIDEi O43159.

    Protocols and materials databases

    DNASUi 23378.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000254605 ; ENSP00000254605 ; ENSG00000132275 .
    GeneIDi 23378.
    KEGGi hsa:23378.
    UCSCi uc001med.3. human.

    Organism-specific databases

    CTDi 23378.
    GeneCardsi GC11M006577.
    HGNCi HGNC:29030. RRP8.
    HPAi HPA038487.
    neXtProti NX_O43159.
    PharmGKBi PA164725550.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0500.
    HOGENOMi HOG000164004.
    InParanoidi O43159.
    KOi K14850.
    OMAi LMGTNIR.
    OrthoDBi EOG7PGDRQ.
    PhylomeDBi O43159.
    TreeFami TF313749.

    Enzyme and pathway databases

    Reactomei REACT_200827. SIRT1 negatively regulates rRNA Expression.

    Miscellaneous databases

    EvolutionaryTracei O43159.
    GeneWikii KIAA0409.
    GenomeRNAii 23378.
    NextBioi 45466.
    PROi O43159.

    Gene expression databases

    ArrayExpressi O43159.
    Bgeei O43159.
    CleanExi HS_KIAA0409.
    Genevestigatori O43159.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    InterProi IPR007823. Methyltransferase-rel.
    IPR029063. SAM-dependent_MTases-like.
    IPR023576. UbiE/COQ5_MeTrFase_CS.
    [Graphical view ]
    PANTHERi PTHR12787. PTHR12787. 1 hit.
    Pfami PF05148. Methyltransf_8. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53335. SSF53335. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of a novel gene which is expressed in the human brain."
      Yazaki M., Takayama K., Matsumoto K., Yoshimoto M.
      Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro."
      Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 4:307-313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-64; SER-171 AND SER-223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "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-62 AND SER-64, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 242-456 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE, IDENTIFICATION IN THE ENOSC COMPLEX, FUNCTION, SUBCELLULAR LOCATION, H3K9ME2-BINDING.

    Entry informationi

    Entry nameiRRP8_HUMAN
    AccessioniPrimary (citable) accession number: O43159
    Secondary accession number(s): Q7KZ78, Q9BVM6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2005
    Last sequence update: April 26, 2005
    Last modified: October 1, 2014
    This is version 120 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 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3