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Protein

Ribonuclease P protein subunit p40

Gene

Rpp40

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

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

GO - Molecular functioni

  1. ribonuclease P activity Source: MGI

GO - Biological processi

  1. RNA phosphodiester bond hydrolysis Source: GOC
  2. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
  3. tRNA 5'-leader removal Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

tRNA processing

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease P protein subunit p40 (EC:3.1.26.5)
Short name:
RNaseP protein p40
Gene namesi
Name:Rpp40
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13

Organism-specific databases

MGIiMGI:1346084. Rpp40.

Subcellular locationi

Nucleusnucleolus Curated

GO - Cellular componenti

  1. nucleolar ribonuclease P complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 363363Ribonuclease P protein subunit p40PRO_0000354076Add
BLAST

Proteomic databases

MaxQBiQ8R1F9.
PaxDbiQ8R1F9.
PRIDEiQ8R1F9.

PTM databases

PhosphoSiteiQ8R1F9.

Expressioni

Gene expression databases

BgeeiQ8R1F9.
ExpressionAtlasiQ8R1F9. baseline and differential.
GenevestigatoriQ8R1F9.

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.By similarity

Protein-protein interaction databases

IntActiQ8R1F9. 1 interaction.
MINTiMINT-4118578.

Family & Domainsi

Phylogenomic databases

eggNOGiNOG42164.
GeneTreeiENSGT00390000014167.
HOGENOMiHOG000006875.
HOVERGENiHBG055018.
InParanoidiQ8R1F9.
KOiK14530.
OMAiKGSCYAL.
OrthoDBiEOG7ZPNK2.
PhylomeDBiQ8R1F9.
TreeFamiTF330967.

Family and domain databases

InterProiIPR013893. RNase_P_Rpp40.
[Graphical view]
PfamiPF08584. Ribonuc_P_40. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8R1F9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATLRRLQEA PRHLLVCEKS NFGHDKSRHK HLVETHYHNY RVSFLIPECG
60 70 80 90 100
LLSKELKSLV MDIGPYYSVK NLPLHELITH EFINTFVKKG SFSALTYNTS
110 120 130 140 150
IDEDNTVALL PNGKLILSLD KDTYEETGLQ GRPSRYSGRK SMKFVISIDL
160 170 180 190 200
MDLSLNLDSK KYRRISWSFK EKKPLKFDFL LAWHPTGTEE STMMSYFSKY
210 220 230 240 250
QIQEHQPKVA LSTVRELQCP VLRSSGLAGE PEEACSALEF FDWLGAVFCS
260 270 280 290 300
ADLNNEPYNF ISTYCCPQPS AVVAQAFLCT ITGFILPEKI HVLLEQLCHY
310 320 330 340 350
FDEPKLAPWV TLTVQGFADS PVAWREKEHG FHKGGEHLYN FVVFNNQDYW
360
LQMAVGANDD CPP
Length:363
Mass (Da):41,547
Last modified:May 26, 2009 - v2
Checksum:iB62F8025633C2B8E
GO

Sequence cautioni

The sequence AAH24607.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC33465.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence EDL40907.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti75 – 751H → Y in BAC33465 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK048810 mRNA. Translation: BAC33465.1. Different initiation.
CH466546 Genomic DNA. Translation: EDL40907.1. Different initiation.
BC024607 mRNA. Translation: AAH24607.1. Different initiation.
CCDSiCCDS26451.2.
RefSeqiNP_666050.3. NM_145938.4.
UniGeneiMm.35545.

Genome annotation databases

EnsembliENSMUST00000171686; ENSMUSP00000130290; ENSMUSG00000021418.
GeneIDi208366.
KEGGimmu:208366.
UCSCiuc011yyj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK048810 mRNA. Translation: BAC33465.1. Different initiation.
CH466546 Genomic DNA. Translation: EDL40907.1. Different initiation.
BC024607 mRNA. Translation: AAH24607.1. Different initiation.
CCDSiCCDS26451.2.
RefSeqiNP_666050.3. NM_145938.4.
UniGeneiMm.35545.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8R1F9. 1 interaction.
MINTiMINT-4118578.

PTM databases

PhosphoSiteiQ8R1F9.

Proteomic databases

MaxQBiQ8R1F9.
PaxDbiQ8R1F9.
PRIDEiQ8R1F9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000171686; ENSMUSP00000130290; ENSMUSG00000021418.
GeneIDi208366.
KEGGimmu:208366.
UCSCiuc011yyj.1. mouse.

Organism-specific databases

CTDi10799.
MGIiMGI:1346084. Rpp40.

Phylogenomic databases

eggNOGiNOG42164.
GeneTreeiENSGT00390000014167.
HOGENOMiHOG000006875.
HOVERGENiHBG055018.
InParanoidiQ8R1F9.
KOiK14530.
OMAiKGSCYAL.
OrthoDBiEOG7ZPNK2.
PhylomeDBiQ8R1F9.
TreeFamiTF330967.

Miscellaneous databases

NextBioi372258.
PROiQ8R1F9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R1F9.
ExpressionAtlasiQ8R1F9. baseline and differential.
GenevestigatoriQ8R1F9.

Family and domain databases

InterProiIPR013893. RNase_P_Rpp40.
[Graphical view]
PfamiPF08584. Ribonuc_P_40. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cerebellum.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    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] OF 13-363.
    Strain: FVB/N.
    Tissue: Kidney.

Entry informationi

Entry nameiRPP40_MOUSE
AccessioniPrimary (citable) accession number: Q8R1F9
Secondary accession number(s): Q8BX66
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: May 26, 2009
Last modified: January 7, 2015
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.