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O95707

- RPP29_HUMAN

UniProt

O95707 - RPP29_HUMAN

Protein

Ribonuclease P protein subunit p29

Gene

POP4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (03 Apr 2002)
      Previous versions | rss
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    Functioni

    Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. May function with RPP38 to coordinate the nucleolar targeting and/or assembly of RNase P.

    Catalytic activityi

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

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. ribonuclease P activity Source: ProtInc
    3. RNA binding Source: ProtInc

    GO - Biological processi

    1. mRNA cleavage Source: InterPro
    2. RNA phosphodiester bond hydrolysis Source: GOC
    3. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
    4. rRNA processing Source: ProtInc
    5. tRNA processing Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    tRNA processing

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribonuclease P protein subunit p29 (EC:3.1.26.5)
    Short name:
    hPOP4
    Gene namesi
    Name:POP4
    Synonyms:RPP29
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:30081. POP4.

    Subcellular locationi

    Nucleusnucleolus 1 Publication

    GO - Cellular componenti

    1. nucleolar ribonuclease P complex Source: InterPro
    2. ribonuclease MRP complex Source: ProtInc

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134987921.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 220220Ribonuclease P protein subunit p29PRO_0000128418Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei10 – 101Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO95707.
    PaxDbiO95707.
    PRIDEiO95707.

    PTM databases

    PhosphoSiteiO95707.

    Expressioni

    Gene expression databases

    ArrayExpressiO95707.
    BgeeiO95707.
    CleanExiHS_POP4.
    GenevestigatoriO95707.

    Organism-specific databases

    HPAiHPA042748.

    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. 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. Interacts with RPP25 and POP5.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    POP1Q995752EBI-366477,EBI-366741
    POP5Q969H62EBI-366477,EBI-366525
    RPP25Q9BUL92EBI-366477,EBI-366570
    RPP38P783452EBI-366477,EBI-366493

    Protein-protein interaction databases

    BioGridi115993. 8 interactions.
    IntActiO95707. 7 interactions.
    MINTiMINT-2799029.
    STRINGi9606.ENSP00000221770.

    Structurei

    3D structure databases

    ProteinModelPortaliO95707.
    SMRiO95707. Positions 107-213.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi65 – 7410Poly-Lys

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG255667.
    HOGENOMiHOG000007746.
    HOVERGENiHBG002676.
    InParanoidiO95707.
    KOiK03538.
    OMAiMSQQACE.
    OrthoDBiEOG786H4B.
    PhylomeDBiO95707.

    Family and domain databases

    Gene3Di2.30.30.210. 1 hit.
    InterProiIPR002730. RNase_P/MRP_p29.
    IPR016848. RNase_P/MRP_p29-subunit.
    IPR023534. Rof/RNase_P-like.
    [Graphical view]
    PfamiPF01868. UPF0086. 1 hit.
    [Graphical view]
    PIRSFiPIRSF027081. RNase_P/MRP_p29_subunit. 1 hit.
    SMARTiSM00538. POP4. 1 hit.
    [Graphical view]
    SUPFAMiSSF101744. SSF101744. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O95707-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKSVIYHALS QKEANDSDVQ PSGAQRAEAF VRAFLKRSTP RMSPQAREDQ    50
    LQRKAVVLEY FTRHKRKEKK KKAKGLSARQ RRELRLFDIK PEQQRYSLFL 100
    PLHELWKQYI RDLCSGLKPD TQPQMIQAKL LKADLHGAII SVTKSKCPSY 150
    VGITGILLQE TKHIFKIITK EDRLKVIPKL NCVFTVETDG FISYIYGSKF 200
    QLRSSERSAK KFKAKGTIDL 220
    Length:220
    Mass (Da):25,425
    Last modified:April 3, 2002 - v2
    Checksum:i26141947E9F5C61E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti38 – 392ST → TS in AAD00893. (PubMed:10024167)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF001176 mRNA. Translation: AAD00893.2.
    Y18863 mRNA. Translation: CAB39167.1.
    CR536569 mRNA. Translation: CAG38806.1.
    AK314790 mRNA. Translation: BAG37321.1.
    BC004438 mRNA. Translation: AAH04438.1.
    BC006098 mRNA. Translation: AAH06098.1.
    CCDSiCCDS12416.1.
    RefSeqiNP_006618.1. NM_006627.2.
    UniGeneiHs.412870.

    Genome annotation databases

    EnsembliENST00000585603; ENSP00000465213; ENSG00000105171.
    GeneIDi10775.
    KEGGihsa:10775.
    UCSCiuc002nsf.2. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF001176 mRNA. Translation: AAD00893.2 .
    Y18863 mRNA. Translation: CAB39167.1 .
    CR536569 mRNA. Translation: CAG38806.1 .
    AK314790 mRNA. Translation: BAG37321.1 .
    BC004438 mRNA. Translation: AAH04438.1 .
    BC006098 mRNA. Translation: AAH06098.1 .
    CCDSi CCDS12416.1.
    RefSeqi NP_006618.1. NM_006627.2.
    UniGenei Hs.412870.

    3D structure databases

    ProteinModelPortali O95707.
    SMRi O95707. Positions 107-213.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115993. 8 interactions.
    IntActi O95707. 7 interactions.
    MINTi MINT-2799029.
    STRINGi 9606.ENSP00000221770.

    PTM databases

    PhosphoSitei O95707.

    Proteomic databases

    MaxQBi O95707.
    PaxDbi O95707.
    PRIDEi O95707.

    Protocols and materials databases

    DNASUi 10775.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000585603 ; ENSP00000465213 ; ENSG00000105171 .
    GeneIDi 10775.
    KEGGi hsa:10775.
    UCSCi uc002nsf.2. human.

    Organism-specific databases

    CTDi 10775.
    GeneCardsi GC19P030097.
    HGNCi HGNC:30081. POP4.
    HPAi HPA042748.
    MIMi 606114. gene.
    neXtProti NX_O95707.
    PharmGKBi PA134987921.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG255667.
    HOGENOMi HOG000007746.
    HOVERGENi HBG002676.
    InParanoidi O95707.
    KOi K03538.
    OMAi MSQQACE.
    OrthoDBi EOG786H4B.
    PhylomeDBi O95707.

    Miscellaneous databases

    GenomeRNAii 10775.
    NextBioi 40914.
    PROi O95707.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95707.
    Bgeei O95707.
    CleanExi HS_POP4.
    Genevestigatori O95707.

    Family and domain databases

    Gene3Di 2.30.30.210. 1 hit.
    InterProi IPR002730. RNase_P/MRP_p29.
    IPR016848. RNase_P/MRP_p29-subunit.
    IPR023534. Rof/RNase_P-like.
    [Graphical view ]
    Pfami PF01868. UPF0086. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF027081. RNase_P/MRP_p29_subunit. 1 hit.
    SMARTi SM00538. POP4. 1 hit.
    [Graphical view ]
    SUPFAMi SSF101744. SSF101744. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Rpp14 and Rpp29, two protein subunits of human ribonuclease P."
      Jarrous N., Eder P.S., Wesolowski D., Altman S.
      RNA 5:153-157(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 86-95.
    2. "hPop4: a new protein subunit of the human RNase MRP and RNase P ribonucleoprotein complexes."
      van Eenennaam H., Pruijn G.J.M., van Venrooij W.J.
      Nucleic Acids Res. 27:2465-2472(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "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].
      Tissue: Brain.
    5. "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: Lung and Lymph.
    6. "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 RPP25 AND POP5.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRPP29_HUMAN
    AccessioniPrimary (citable) accession number: O95707
    Secondary accession number(s): Q5XKL7, Q6FHW9, Q9UQQ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: April 3, 2002
    Last modified: October 1, 2014
    This is version 129 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: 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