Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9BUL9

- RPP25_HUMAN

UniProt

Q9BUL9 - RPP25_HUMAN

Protein

Ribonuclease P protein subunit p25

Gene

RPP25

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP. This subunit binds to RNA.

    Catalytic activityi

    Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. ribonuclease P activity Source: UniProtKB-EC

    GO - Biological processi

    1. tRNA processing Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    tRNA processing

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribonuclease P protein subunit p25 (EC:3.1.26.5)
    Short name:
    RNase P protein subunit p25
    Gene namesi
    Name:RPP25
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:30361. RPP25.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134990737.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 199199Ribonuclease P protein subunit p25PRO_0000237582Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei172 – 1721Phosphoserine2 Publications
    Modified residuei182 – 1821Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9BUL9.
    PaxDbiQ9BUL9.
    PeptideAtlasiQ9BUL9.
    PRIDEiQ9BUL9.

    PTM databases

    PhosphoSiteiQ9BUL9.

    Expressioni

    Gene expression databases

    BgeeiQ9BUL9.
    CleanExiHS_RPP25.
    GenevestigatoriQ9BUL9.

    Organism-specific databases

    HPAiHPA046900.

    Interactioni

    Subunit structurei

    Component of nuclear RNase P and RNase MRP ribonucleoproteins. RNase P consists of an RNA moiety and at least 8 protein subunits; POP1, RPP14, RPP20/POP7, RPP25, RPP29/POP4, RPP30, RPP38 and RPP40. Interacts with the P3 domain of RNase MRP complex. RNase MRP consists of an RNA moiety and at least 9 protein subunits; POP1, RPP14, RPP20/POP7, RPP25, RPP29/POP4, RPP30, RPP38, RPP40, POP5 and RPP21.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    POP4O957072EBI-366570,EBI-366477
    POP7O758172EBI-366570,EBI-366574

    Protein-protein interaction databases

    BioGridi120255. 8 interactions.
    IntActiQ9BUL9. 5 interactions.
    MINTiMINT-5009653.
    STRINGi9606.ENSP00000317691.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BUL9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histone-like Alba family.Curated

    Phylogenomic databases

    eggNOGiNOG247262.
    HOGENOMiHOG000231665.
    HOVERGENiHBG056729.
    InParanoidiQ9BUL9.
    KOiK14525.
    OMAiMENFRKV.
    OrthoDBiEOG7XM309.
    PhylomeDBiQ9BUL9.
    TreeFamiTF325688.

    Family and domain databases

    Gene3Di3.30.110.20. 1 hit.
    InterProiIPR002775. DNA/RNA-bd_Alba-like.
    [Graphical view]
    PfamiPF01918. Alba. 1 hit.
    [Graphical view]
    SUPFAMiSSF82704. SSF82704. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9BUL9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MENFRKVRSE EAPAGCGAEG GGPGSGPFAD LAPGAVHMRV KEGSKIRNLM    50
    AFATASMAQP ATRAIVFSGC GRATTKTVTC AEILKRRLAG LHQVTRLRYR 100
    SVREVWQSLP PGPTQGQTPG EPAASLSVLK NVPGLAILLS KDALDPRQPG 150
    YQPPNPHPGP SSPPAAPASK RSLGEPAAGE GSAKRSQPEP GVADEDQTA 199
    Length:199
    Mass (Da):20,632
    Last modified:June 1, 2001 - v1
    Checksum:i9A4494F0297B2A81
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti73 – 731A → V in BAA91128. (PubMed:14702039)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY034074 mRNA. Translation: AAK54443.1.
    AK000381 mRNA. Translation: BAA91128.1.
    CH471136 Genomic DNA. Translation: EAW99285.1.
    CH471136 Genomic DNA. Translation: EAW99286.1.
    BC002497 mRNA. Translation: AAH02497.1.
    BC007270 mRNA. Translation: AAH07270.1.
    CCDSiCCDS10274.1.
    RefSeqiNP_060263.2. NM_017793.2.
    UniGeneiHs.8562.

    Genome annotation databases

    EnsembliENST00000322177; ENSP00000317691; ENSG00000178718.
    GeneIDi54913.
    KEGGihsa:54913.
    UCSCiuc002azj.1. human.

    Polymorphism databases

    DMDMi74733233.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY034074 mRNA. Translation: AAK54443.1 .
    AK000381 mRNA. Translation: BAA91128.1 .
    CH471136 Genomic DNA. Translation: EAW99285.1 .
    CH471136 Genomic DNA. Translation: EAW99286.1 .
    BC002497 mRNA. Translation: AAH02497.1 .
    BC007270 mRNA. Translation: AAH07270.1 .
    CCDSi CCDS10274.1.
    RefSeqi NP_060263.2. NM_017793.2.
    UniGenei Hs.8562.

    3D structure databases

    ProteinModelPortali Q9BUL9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120255. 8 interactions.
    IntActi Q9BUL9. 5 interactions.
    MINTi MINT-5009653.
    STRINGi 9606.ENSP00000317691.

    PTM databases

    PhosphoSitei Q9BUL9.

    Polymorphism databases

    DMDMi 74733233.

    Proteomic databases

    MaxQBi Q9BUL9.
    PaxDbi Q9BUL9.
    PeptideAtlasi Q9BUL9.
    PRIDEi Q9BUL9.

    Protocols and materials databases

    DNASUi 54913.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000322177 ; ENSP00000317691 ; ENSG00000178718 .
    GeneIDi 54913.
    KEGGi hsa:54913.
    UCSCi uc002azj.1. human.

    Organism-specific databases

    CTDi 54913.
    GeneCardsi GC15M075247.
    HGNCi HGNC:30361. RPP25.
    HPAi HPA046900.
    neXtProti NX_Q9BUL9.
    PharmGKBi PA134990737.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG247262.
    HOGENOMi HOG000231665.
    HOVERGENi HBG056729.
    InParanoidi Q9BUL9.
    KOi K14525.
    OMAi MENFRKV.
    OrthoDBi EOG7XM309.
    PhylomeDBi Q9BUL9.
    TreeFami TF325688.

    Miscellaneous databases

    GenomeRNAii 54913.
    NextBioi 57966.
    PROi Q9BUL9.

    Gene expression databases

    Bgeei Q9BUL9.
    CleanExi HS_RPP25.
    Genevestigatori Q9BUL9.

    Family and domain databases

    Gene3Di 3.30.110.20. 1 hit.
    InterProi IPR002775. DNA/RNA-bd_Alba-like.
    [Graphical view ]
    Pfami PF01918. Alba. 1 hit.
    [Graphical view ]
    SUPFAMi SSF82704. SSF82704. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Purification and characterization of Rpp25, an RNA-binding protein subunit of human ribonuclease P."
      Guerrier-Takada C., Eder P.S., Gopalan V., Altman S.
      RNA 8:290-295(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], RNA-BINDING, SUBCELLULAR LOCATION.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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].
      Tissue: Brain and Skin.
    5. "Mutual interactions between subunits of the human RNase MRP ribonucleoprotein complex."
      Welting T.J., van Venrooij W.J., Pruijn G.J.
      Nucleic Acids Res. 32:2138-2146(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH POP7; POP4 AND RMRP.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "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-172 AND SER-182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRPP25_HUMAN
    AccessioniPrimary (citable) accession number: Q9BUL9
    Secondary accession number(s): D3DW70, Q9NX88
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2006
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 93 of the entry and version 1 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 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3