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P78345

- RPP38_HUMAN

UniProt

P78345 - RPP38_HUMAN

Protein

Ribonuclease P protein subunit p38

Gene

RPP38

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 (06 Dec 2005)
      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. RPP38 may associate transiently with RNase P RNA as a factor involved in the transport of H1 RNA to the putative site of its assembly in the cell, the nucleolus.

    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

    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 p38 (EC:3.1.26.5)
    Short name:
    RNaseP protein p38
    Gene namesi
    Name:RPP38
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:30329. RPP38.

    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

    PharmGKBiPA134957031.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 283282Ribonuclease P protein subunit p38PRO_0000136783Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei226 – 2261Phosphoserine1 Publication
    Modified residuei235 – 2351Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP78345.
    PaxDbiP78345.
    PRIDEiP78345.

    PTM databases

    PhosphoSiteiP78345.

    Expressioni

    Gene expression databases

    ArrayExpressiP78345.
    BgeeiP78345.
    CleanExiHS_RPP38.
    GenevestigatoriP78345.

    Organism-specific databases

    HPAiHPA045128.

    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. RPP38 is probably a dimer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NCK1P163332EBI-366493,EBI-389883
    POP4O957072EBI-366493,EBI-366477

    Protein-protein interaction databases

    BioGridi115808. 18 interactions.
    IntActiP78345. 8 interactions.
    MINTiMINT-5009179.
    STRINGi9606.ENSP00000367439.

    Structurei

    3D structure databases

    ProteinModelPortaliP78345.
    SMRiP78345. Positions 111-197.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi63 – 686Poly-Lys

    Sequence similaritiesi

    Belongs to the ribosomal protein L7Ae family.Curated

    Phylogenomic databases

    eggNOGiNOG308103.
    HOGENOMiHOG000231566.
    HOVERGENiHBG060241.
    InParanoidiP78345.
    KOiK14523.
    OMAiKIRKPPK.
    OrthoDBiEOG74BJT8.
    PhylomeDBiP78345.
    TreeFamiTF332558.

    Family and domain databases

    Gene3Di3.30.1330.30. 1 hit.
    InterProiIPR029064. L30e-like.
    IPR004038. Ribosomal_L7Ae/L30e/S12e/Gad45.
    [Graphical view]
    PfamiPF01248. Ribosomal_L7Ae. 1 hit.
    [Graphical view]
    SUPFAMiSSF55315. SSF55315. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P78345-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAAPQAPGR GSLRKTRPLV VKTSLNNPYI IRWSALESED MHFILQTLED    50
    RLKAIGLQKI EDKKKKNKTP FLKKESREKC SIAVDISENL KEKKTDAKQQ 100
    VSGWTPAHVR KQLAIGVNEV TRALERRELL LVLVCKSVKP AMITSHLIQL 150
    SLSRSVPACQ VPRLSERIAP VIGLKCVLAL AFKKNTTDFV DEVRAIIPRV 200
    PSLSVPWLQD RIEDSGENLE TEPLESQDRE LLDTSFEDLS KPKRKLADGR 250
    QASVTLQPLK IKKLIPNPNK IRKPPKSKKA TPK 283
    Length:283
    Mass (Da):31,834
    Last modified:December 6, 2005 - v2
    Checksum:i233F3397DBDE4F18
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti24 – 241S → A AA sequence (PubMed:9037013)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti86 – 861I → V.
    Corresponds to variant rs3814171 [ dbSNP | Ensembl ].
    VAR_051811
    Natural varianti88 – 881E → D.
    Corresponds to variant rs1052157 [ dbSNP | Ensembl ].
    VAR_023960
    Natural varianti114 – 1141A → V.1 Publication
    Corresponds to variant rs1132078 [ dbSNP | Ensembl ].
    VAR_023961
    Natural varianti181 – 1811A → G.2 Publications
    Corresponds to variant rs15772 [ dbSNP | Ensembl ].
    VAR_023962
    Natural varianti202 – 2021S → R.
    Corresponds to variant rs12249258 [ dbSNP | Ensembl ].
    VAR_051812
    Natural varianti212 – 2121I → T.
    Corresponds to variant rs10242 [ dbSNP | Ensembl ].
    VAR_029298
    Natural varianti250 – 2501R → G.
    Corresponds to variant rs34040166 [ dbSNP | Ensembl ].
    VAR_051813

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U77664 mRNA. Translation: AAC51142.1.
    AK057006 mRNA. Translation: BAG51842.1.
    CR541816 mRNA. Translation: CAG46615.1.
    AK223418 mRNA. Translation: BAD97138.1.
    AL590365 Genomic DNA. Translation: CAH73968.1.
    CH471072 Genomic DNA. Translation: EAW86240.1.
    CH471072 Genomic DNA. Translation: EAW86241.1.
    BC029494 mRNA. Translation: AAH29494.1.
    CCDSiCCDS7108.1.
    RefSeqiNP_001091059.1. NM_001097590.2.
    NP_001252530.1. NM_001265601.1.
    NP_006405.2. NM_006414.4.
    NP_892117.1. NM_183005.4.
    XP_006717426.1. XM_006717363.1.
    XP_006717427.1. XM_006717364.1.
    UniGeneiHs.94986.

    Genome annotation databases

    EnsembliENST00000378197; ENSP00000367439; ENSG00000152464.
    ENST00000378202; ENSP00000367444; ENSG00000152464.
    ENST00000378203; ENSP00000367445; ENSG00000152464.
    GeneIDi10557.
    KEGGihsa:10557.
    UCSCiuc001inx.5. human.

    Polymorphism databases

    DMDMi83305638.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U77664 mRNA. Translation: AAC51142.1 .
    AK057006 mRNA. Translation: BAG51842.1 .
    CR541816 mRNA. Translation: CAG46615.1 .
    AK223418 mRNA. Translation: BAD97138.1 .
    AL590365 Genomic DNA. Translation: CAH73968.1 .
    CH471072 Genomic DNA. Translation: EAW86240.1 .
    CH471072 Genomic DNA. Translation: EAW86241.1 .
    BC029494 mRNA. Translation: AAH29494.1 .
    CCDSi CCDS7108.1.
    RefSeqi NP_001091059.1. NM_001097590.2.
    NP_001252530.1. NM_001265601.1.
    NP_006405.2. NM_006414.4.
    NP_892117.1. NM_183005.4.
    XP_006717426.1. XM_006717363.1.
    XP_006717427.1. XM_006717364.1.
    UniGenei Hs.94986.

    3D structure databases

    ProteinModelPortali P78345.
    SMRi P78345. Positions 111-197.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115808. 18 interactions.
    IntActi P78345. 8 interactions.
    MINTi MINT-5009179.
    STRINGi 9606.ENSP00000367439.

    PTM databases

    PhosphoSitei P78345.

    Polymorphism databases

    DMDMi 83305638.

    Proteomic databases

    MaxQBi P78345.
    PaxDbi P78345.
    PRIDEi P78345.

    Protocols and materials databases

    DNASUi 10557.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000378197 ; ENSP00000367439 ; ENSG00000152464 .
    ENST00000378202 ; ENSP00000367444 ; ENSG00000152464 .
    ENST00000378203 ; ENSP00000367445 ; ENSG00000152464 .
    GeneIDi 10557.
    KEGGi hsa:10557.
    UCSCi uc001inx.5. human.

    Organism-specific databases

    CTDi 10557.
    GeneCardsi GC10P015140.
    HGNCi HGNC:30329. RPP38.
    HPAi HPA045128.
    MIMi 606116. gene.
    neXtProti NX_P78345.
    PharmGKBi PA134957031.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG308103.
    HOGENOMi HOG000231566.
    HOVERGENi HBG060241.
    InParanoidi P78345.
    KOi K14523.
    OMAi KIRKPPK.
    OrthoDBi EOG74BJT8.
    PhylomeDBi P78345.
    TreeFami TF332558.

    Miscellaneous databases

    GeneWikii RPP38.
    GenomeRNAii 10557.
    NextBioi 40059.
    PROi P78345.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P78345.
    Bgeei P78345.
    CleanExi HS_RPP38.
    Genevestigatori P78345.

    Family and domain databases

    Gene3Di 3.30.1330.30. 1 hit.
    InterProi IPR029064. L30e-like.
    IPR004038. Ribosomal_L7Ae/L30e/S12e/Gad45.
    [Graphical view ]
    Pfami PF01248. Ribosomal_L7Ae. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55315. SSF55315. 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], PROTEIN SEQUENCE OF 24-32; 113-122 AND 212-228, VARIANT VAL-114.
    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], VARIANT GLY-181.
      Tissue: Skeletal muscle.
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLY-181.
    5. "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].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Testis.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "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-235, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRPP38_HUMAN
    AccessioniPrimary (citable) accession number: P78345
    Secondary accession number(s): B3KPY0
    , D3DRT8, Q53F71, Q8NHS8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: December 6, 2005
    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

    Miscellaneous

    Autoantibodies against RPP38 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. Ribosomal proteins
      Ribosomal proteins families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3