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Q14684

- RRP1B_HUMAN

UniProt

Q14684 - RRP1B_HUMAN

Protein

Ribosomal RNA processing protein 1 homolog B

Gene

RRP1B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 3 (18 May 2010)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB

    GO - Biological processi

    1. negative regulation of phosphatase activity Source: UniProtKB
    2. rRNA processing Source: InterPro

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribosomal RNA processing protein 1 homolog B
    Alternative name(s):
    RRP1-like protein B
    Gene namesi
    Name:RRP1B
    Synonyms:KIAA0179
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 21

    Organism-specific databases

    HGNCiHGNC:23818. RRP1B.

    Subcellular locationi

    Nucleusnucleolus 1 Publication

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. euchromatin Source: Ensembl
    3. heterochromatin Source: Ensembl
    4. nucleolus Source: HPA
    5. nucleus Source: UniProtKB
    6. preribosome, small subunit precursor Source: InterPro

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162402138.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 758758Ribosomal RNA processing protein 1 homolog BPRO_0000050729Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei245 – 2451Phosphoserine7 Publications
    Modified residuei350 – 3501Phosphoserine3 Publications
    Modified residuei392 – 3921Phosphoserine2 Publications
    Modified residuei394 – 3941Phosphoserine1 Publication
    Modified residuei395 – 3951Phosphoserine1 Publication
    Modified residuei452 – 4521Phosphoserine1 Publication
    Modified residuei458 – 4581Phosphoserine1 Publication
    Modified residuei513 – 5131Phosphoserine3 Publications
    Modified residuei652 – 6521N6-acetyllysine1 Publication
    Modified residuei702 – 7021Phosphoserine2 Publications
    Modified residuei706 – 7061Phosphoserine3 Publications
    Modified residuei712 – 7121CitrullineBy similarity
    Modified residuei728 – 7281Phosphothreonine1 Publication
    Modified residuei732 – 7321Phosphoserine4 Publications
    Modified residuei735 – 7351Phosphoserine2 Publications
    Modified residuei736 – 7361Phosphoserine1 Publication

    Post-translational modificationi

    Citrullinated by PADI4.By similarity

    Keywords - PTMi

    Acetylation, Citrullination, Phosphoprotein

    Proteomic databases

    MaxQBiQ14684.
    PaxDbiQ14684.
    PRIDEiQ14684.

    2D gel databases

    SWISS-2DPAGEQ14684.

    PTM databases

    PhosphoSiteiQ14684.

    Expressioni

    Gene expression databases

    BgeeiQ14684.
    CleanExiHS_RRP1B.
    GenevestigatoriQ14684.

    Organism-specific databases

    HPAiHPA017893.
    HPA020324.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LSM1O151161EBI-372051,EBI-347619

    Protein-protein interaction databases

    BioGridi116708. 48 interactions.
    IntActiQ14684. 12 interactions.
    MINTiMINT-3029999.
    STRINGi9606.ENSP00000339145.

    Structurei

    3D structure databases

    ProteinModelPortaliQ14684.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi402 – 4065Poly-Lys

    Sequence similaritiesi

    Belongs to the RRP1 family.Curated

    Phylogenomic databases

    eggNOGiNOG299406.
    HOGENOMiHOG000070179.
    HOVERGENiHBG098014.
    InParanoidiQ14684.
    KOiK14849.
    OMAiMTAEFKK.
    OrthoDBiEOG718KC8.
    PhylomeDBiQ14684.
    TreeFamiTF315294.

    Family and domain databases

    InterProiIPR010301. Nop52.
    [Graphical view]
    PANTHERiPTHR13026. PTHR13026. 1 hit.
    PfamiPF05997. Nop52. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q14684-1) [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

    MAPAMQPAEI QFAQRLASSE KGIRDRAVKK LRQYISVKTQ RETGGFSQEE    50
    LLKIWKGLFY CMWVQDEPLL QEELANTIAQ LVHAVNNSAA QHLFIQTFWQ 100
    TMNREWKGID RLRLDKYYML IRLVLRQSFE VLKRNGWEES RIKVFLDVLM 150
    KEVLCPESQS PNGVRFHFID IYLDELSKVG GKELLADQNL KFIDPFCKIA 200
    AKTKDHTLVQ TIARGVFEAI VDQSPFVPEE TMEEQKTKVG DGDLSAEEIP 250
    ENEVSLRRAV SKKKTALGKN HSRKDGLSDE RGRDDCGTFE DTGPLLQFDY 300
    KAVADRLLEM TSRKNTPHFN RKRLSKLIKK FQDLSEGSSI SQLSFAEDIS 350
    ADEDDQILSQ GKHKKKGNKL LEKTNLEKEK GSRVFCVEEE DSESSLQKRR 400
    RKKKKKHHLQ PENPGPGGAA PSLEQNRGRE PEASGLKALK ARVAEPGAEA 450
    TSSTGEESGS EHPPAVPMHN KRKRPRKKSP RAHREMLESA VLPPEDMSQS 500
    GPSGSHPQGP RGSPTGGAQL LKRKRKLGVV PVNGSGLSTP AWPPLQQEGP 550
    PTGPAEGANS HTTLPQRRRL QKKKAGPGSL ELCGLPSQKT ASLKKRKKMR 600
    VMSNLVEHNG VLESEAGQPQ ALGSSGTCSS LKKQKLRAES DFVKFDTPFL 650
    PKPLFFRRAK SSTATHPPGP AVQLNKTPSS SKKVTFGLNR NMTAEFKKTD 700
    KSILVSPTGP SRVAFDPEQK PLHGVLKTPT SSPASSPLVA KKPLTTTPRR 750
    RPRAMDFF 758
    Length:758
    Mass (Da):84,428
    Last modified:May 18, 2010 - v3
    Checksum:i738117A7062054F2
    GO
    Isoform 2 (identifier: Q14684-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         51-68: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:740
    Mass (Da):82,176
    Checksum:i7D39CB77AA4BE255
    GO

    Sequence cautioni

    The sequence BAA11496.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti436 – 4361L → P in BAA11496. (PubMed:8724849)Curated
    Sequence conflicti436 – 4361L → P in AAH28386. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei51 – 6818Missing in isoform 2. 1 PublicationVSP_007801Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D80001 mRNA. Translation: BAA11496.1. Different initiation.
    AP001052 Genomic DNA. No translation available.
    BC028386 mRNA. Translation: AAH28386.1.
    CCDSiCCDS33577.1. [Q14684-1]
    RefSeqiNP_055871.1. NM_015056.2. [Q14684-1]
    UniGeneiHs.565725.

    Genome annotation databases

    EnsembliENST00000340648; ENSP00000339145; ENSG00000160208. [Q14684-1]
    GeneIDi23076.
    KEGGihsa:23076.
    UCSCiuc002zdk.3. human. [Q14684-1]

    Polymorphism databases

    DMDMi296452976.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D80001 mRNA. Translation: BAA11496.1 . Different initiation.
    AP001052 Genomic DNA. No translation available.
    BC028386 mRNA. Translation: AAH28386.1 .
    CCDSi CCDS33577.1. [Q14684-1 ]
    RefSeqi NP_055871.1. NM_015056.2. [Q14684-1 ]
    UniGenei Hs.565725.

    3D structure databases

    ProteinModelPortali Q14684.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116708. 48 interactions.
    IntActi Q14684. 12 interactions.
    MINTi MINT-3029999.
    STRINGi 9606.ENSP00000339145.

    PTM databases

    PhosphoSitei Q14684.

    Polymorphism databases

    DMDMi 296452976.

    2D gel databases

    SWISS-2DPAGE Q14684.

    Proteomic databases

    MaxQBi Q14684.
    PaxDbi Q14684.
    PRIDEi Q14684.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000340648 ; ENSP00000339145 ; ENSG00000160208 . [Q14684-1 ]
    GeneIDi 23076.
    KEGGi hsa:23076.
    UCSCi uc002zdk.3. human. [Q14684-1 ]

    Organism-specific databases

    CTDi 23076.
    GeneCardsi GC21P045079.
    H-InvDB HIX0016154.
    HGNCi HGNC:23818. RRP1B.
    HPAi HPA017893.
    HPA020324.
    MIMi 610654. gene.
    neXtProti NX_Q14684.
    PharmGKBi PA162402138.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG299406.
    HOGENOMi HOG000070179.
    HOVERGENi HBG098014.
    InParanoidi Q14684.
    KOi K14849.
    OMAi MTAEFKK.
    OrthoDBi EOG718KC8.
    PhylomeDBi Q14684.
    TreeFami TF315294.

    Miscellaneous databases

    GeneWikii RRP1B.
    GenomeRNAii 23076.
    NextBioi 44187.
    PROi Q14684.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q14684.
    CleanExi HS_RRP1B.
    Genevestigatori Q14684.

    Family and domain databases

    InterProi IPR010301. Nop52.
    [Graphical view ]
    PANTHERi PTHR13026. PTHR13026. 1 hit.
    Pfami PF05997. Nop52. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1."
      Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.
      DNA Res. 3:17-24(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Bone marrow.
    2. "The DNA sequence of human chromosome 21."
      Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
      , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
      Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORM 1).
      Tissue: Testis.
    4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    5. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392 AND SER-513, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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-245, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245; SER-350; SER-392; SER-394; SER-395; SER-452; SER-458; SER-702; SER-706; SER-732 AND SER-736, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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].
    11. "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-245; SER-350; SER-732 AND SER-735, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-652, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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-245; SER-350; SER-513; SER-702; SER-706; SER-732 AND SER-735, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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-245; SER-513; SER-706; THR-728 AND SER-732, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRRP1B_HUMAN
    AccessioniPrimary (citable) accession number: Q14684
    Secondary accession number(s): Q8TBZ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 132 of the entry and version 3 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 21
      Human chromosome 21: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3