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P78346

- RPP30_HUMAN

UniProt

P78346 - RPP30_HUMAN

Protein

Ribonuclease P protein subunit p30

Gene

RPP30

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 1 (01 May 1997)
      Previous versions | rss
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    Functioni

    Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.

    Catalytic activityi

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

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. ribonuclease P activity Source: ProtInc

    GO - Biological processi

    1. RNA phosphodiester bond hydrolysis Source: GOC
    2. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
    3. tRNA processing Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    tRNA processing

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribonuclease P protein subunit p30 (EC:3.1.26.5)
    Short name:
    RNaseP protein p30
    Alternative name(s):
    RNase P subunit 2
    Gene namesi
    Name:RPP30
    Synonyms:RNASEP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:17688. RPP30.

    Subcellular locationi

    Nucleusnucleolus Curated

    GO - Cellular componenti

    1. nucleolar ribonuclease P complex Source: ProtInc
    2. nucleus Source: ProtInc

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134876345.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 268267Ribonuclease P protein subunit p30PRO_0000140031Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei251 – 2511Phosphoserine3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP78346.
    PaxDbiP78346.
    PRIDEiP78346.

    PTM databases

    PhosphoSiteiP78346.

    Expressioni

    Gene expression databases

    ArrayExpressiP78346.
    BgeeiP78346.
    CleanExiHS_RPP30.
    GenevestigatoriP78346.

    Organism-specific databases

    HPAiHPA037578.

    Interactioni

    Subunit structurei

    RNase P consists of an RNA moiety and at least 8 protein subunits; POP1, RPP14, RPP20/POP7, RPP25, RPP29/POP4, RPP30, RPP38 and RPP40.

    Protein-protein interaction databases

    BioGridi115807. 21 interactions.
    IntActiP78346. 3 interactions.
    MINTiMINT-3023090.
    STRINGi9606.ENSP00000389182.

    Structurei

    3D structure databases

    ProteinModelPortaliP78346.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1603.
    HOGENOMiHOG000157793.
    HOVERGENiHBG010226.
    KOiK03539.
    OMAiGVCFELV.
    OrthoDBiEOG73FQNP.
    PhylomeDBiP78346.
    TreeFamiTF106113.

    Family and domain databases

    InterProiIPR016195. Pol/histidinol_Pase-like.
    IPR002738. RNase_P_p30.
    [Graphical view]
    PANTHERiPTHR13031. PTHR13031. 1 hit.
    PfamiPF01876. RNase_P_p30. 1 hit.
    [Graphical view]
    SUPFAMiSSF89550. SSF89550. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P78346-1) [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

    MAVFADLDLR AGSDLKALRG LVETAAHLGY SVVAINHIVD FKEKKQEIEK    50
    PVAVSELFTT LPIVQGKSRP IKILTRLTII VSDPSHCNVL RATSSRARLY 100
    DVVAVFPKTE KLFHIACTHL DVDLVCITVT EKLPFYFKRP PINVAIDRGL 150
    AFELVYSPAI KDSTMRRYTI SSALNLMQIC KGKNVIISSA AERPLEIRGP 200
    YDVANLGLLF GLSESDAKAA VSTNCRAALL HGETRKTAFG IISTVKKPRP 250
    SEGDEDCLPA SKKAKCEG 268
    Length:268
    Mass (Da):29,321
    Last modified:May 1, 1997 - v1
    Checksum:i2AB492D98ACDCCBB
    GO
    Isoform 2 (identifier: P78346-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         266-268: CEG → WSHSVTQAGVQWHNLGSLQPLPLGLKPSSHLSLPRTRIQQRQLLISHQRDHTPKNRL

    Note: No experimental confirmation available.Curated

    Show »
    Length:322
    Mass (Da):35,564
    Checksum:iB6700D9E4A95C181
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti65 – 651Q → R in AK225532. 1 PublicationCurated
    Sequence conflicti189 – 1891S → I AA sequence (PubMed:9037013)Curated
    Isoform 2 (identifier: P78346-2)
    Sequence conflicti291 – 2911K → R in AK225532. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti12 – 121G → D.
    Corresponds to variant rs11544145 [ dbSNP | Ensembl ].
    VAR_051870

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei266 – 2683CEG → WSHSVTQAGVQWHNLGSLQP LPLGLKPSSHLSLPRTRIQQ RQLLISHQRDHTPKNRL in isoform 2. 1 PublicationVSP_045673

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U77665 mRNA. Translation: AAC51143.1.
    AK312900 mRNA. Translation: BAG35746.1.
    AK225532 mRNA. No translation available.
    AL590622 Genomic DNA. Translation: CAC70100.1.
    CH471066 Genomic DNA. Translation: EAW50117.1.
    BC006991 mRNA. Translation: AAH06991.1.
    CCDSiCCDS44458.1. [P78346-2]
    CCDS7411.1. [P78346-1]
    RefSeqiNP_001098016.1. NM_001104546.1. [P78346-2]
    NP_006404.1. NM_006413.4. [P78346-1]
    UniGeneiHs.139120.

    Genome annotation databases

    EnsembliENST00000371703; ENSP00000360768; ENSG00000148688. [P78346-1]
    ENST00000413330; ENSP00000389182; ENSG00000148688. [P78346-2]
    GeneIDi10556.
    KEGGihsa:10556.
    UCSCiuc001khd.2. human.
    uc009xtx.3. human. [P78346-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U77665 mRNA. Translation: AAC51143.1 .
    AK312900 mRNA. Translation: BAG35746.1 .
    AK225532 mRNA. No translation available.
    AL590622 Genomic DNA. Translation: CAC70100.1 .
    CH471066 Genomic DNA. Translation: EAW50117.1 .
    BC006991 mRNA. Translation: AAH06991.1 .
    CCDSi CCDS44458.1. [P78346-2 ]
    CCDS7411.1. [P78346-1 ]
    RefSeqi NP_001098016.1. NM_001104546.1. [P78346-2 ]
    NP_006404.1. NM_006413.4. [P78346-1 ]
    UniGenei Hs.139120.

    3D structure databases

    ProteinModelPortali P78346.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115807. 21 interactions.
    IntActi P78346. 3 interactions.
    MINTi MINT-3023090.
    STRINGi 9606.ENSP00000389182.

    PTM databases

    PhosphoSitei P78346.

    Proteomic databases

    MaxQBi P78346.
    PaxDbi P78346.
    PRIDEi P78346.

    Protocols and materials databases

    DNASUi 10556.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371703 ; ENSP00000360768 ; ENSG00000148688 . [P78346-1 ]
    ENST00000413330 ; ENSP00000389182 ; ENSG00000148688 . [P78346-2 ]
    GeneIDi 10556.
    KEGGi hsa:10556.
    UCSCi uc001khd.2. human.
    uc009xtx.3. human. [P78346-1 ]

    Organism-specific databases

    CTDi 10556.
    GeneCardsi GC10P092621.
    HGNCi HGNC:17688. RPP30.
    HPAi HPA037578.
    MIMi 606115. gene.
    neXtProti NX_P78346.
    PharmGKBi PA134876345.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1603.
    HOGENOMi HOG000157793.
    HOVERGENi HBG010226.
    KOi K03539.
    OMAi GVCFELV.
    OrthoDBi EOG73FQNP.
    PhylomeDBi P78346.
    TreeFami TF106113.

    Miscellaneous databases

    GeneWikii RPP30.
    GenomeRNAii 10556.
    NextBioi 40053.
    PROi P78346.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P78346.
    Bgeei P78346.
    CleanExi HS_RPP30.
    Genevestigatori P78346.

    Family and domain databases

    InterProi IPR016195. Pol/histidinol_Pase-like.
    IPR002738. RNase_P_p30.
    [Graphical view ]
    PANTHERi PTHR13031. PTHR13031. 1 hit.
    Pfami PF01876. RNase_P_p30. 1 hit.
    [Graphical view ]
    SUPFAMi SSF89550. SSF89550. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of two scleroderma autoimmune antigens that copurify with human ribonuclease P."
      Eder P.S., Kekuda R., Stolc V., Altman S.
      Proc. Natl. Acad. Sci. U.S.A. 94:1101-1106(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 21-30; 140-148 AND 185-198.
    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] (ISOFORM 1).
      Tissue: Brain.
    3. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Signet-ring cell carcinoma.
    4. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Kidney.
    7. Bienvenut W.V., Lao L., Ryan K.M.
      Submitted (JUN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-10; 99-108; 139-161; 184-198 AND 237-246, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Osteosarcoma.
    8. "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-251, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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-251, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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-251, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRPP30_HUMAN
    AccessioniPrimary (citable) accession number: P78346
    Secondary accession number(s): B2R799, E9PB02
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 132 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

    Miscellaneous

    Autoantibodies against RPP30 are found in sera from scleroderma patients.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3