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Q91WE3 (RPP25_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ribonuclease P protein subunit p25
Short name=RNase P protein subunit p25
EC=3.1.26.5
Gene names
Name:Rpp25
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length199 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 By similarity.

Catalytic activity

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

Subunit structure

Component of nuclear RNase P and RNase MRP ribonucleoproteins. RNase P consists of a 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 a RNA moiety and at least 9 protein subunits; POP1, RPP14, RPP20/POP7, RPP25, RPP29/POP4, RPP30, RPP38, RPP40, POP5 and RPP21 By similarity.

Subcellular location

Nucleus By similarity.

Sequence similarities

Belongs to the histone-like Alba family.

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentNucleus
   LigandRNA-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processtRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcentrosome

Inferred from electronic annotation. Source: Compara

mitochondrion

Inferred from electronic annotation. Source: Compara

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

ribonuclease P activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 199199Ribonuclease P protein subunit p25
PRO_0000237583

Amino acid modifications

Modified residue1721Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q91WE3 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: B9DE105BE3293D64

FASTA19921,038
        10         20         30         40         50         60 
MENFRKVRSE EAPAGDGDEG GSPNSGPFAD LAPGAVHMRV KEGSKIRNLL AFATASMAQP 

        70         80         90        100        110        120 
ATRAIVFSGC GRATTKTVTC AEILKRRLAG LHQVTRLRYR SVREVWQSLP PGPTPGQTPS 

       130        140        150        160        170        180 
DPAASLSVLK NVPSLAILLS KDALDPRQLG YQPPNLSPGP SSPPTVSTSK RSLGESAAEE 

       190 
GTAKRSQPEP EAENEDRTA

« Hide

References

[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. expand/collapse author list , 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.
[2]"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: Eye.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK082822 mRNA. Translation: BAC38636.1.
BC016085 mRNA. Translation: AAH16085.1.
BC083064 mRNA. Translation: AAH83064.1.
IPIIPI00128066.
RefSeqNP_598743.1. NM_133982.1.
UniGeneMm.274421.

3D structure databases

ProteinModelPortalQ91WE3.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000079358.

PTM databases

PhosphoSiteQ91WE3.

Proteomic databases

PRIDEQ91WE3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000080514; ENSMUSP00000079358; ENSMUSG00000062309.
GeneID102614.
KEGGmmu:102614.
UCSCuc009puy.1. mouse.

Organism-specific databases

CTD54913.
MGIMGI:2143151. Rpp25.

Phylogenomic databases

eggNOGNOG247262.
GeneTreeENSGT00390000002564.
HOGENOMHOG000231665.
HOVERGENHBG056729.
InParanoidQ91WE3.
KOK14525.
OMAAVHMRVK.
OrthoDBEOG49ZXQR.

Gene expression databases

BgeeQ91WE3.
CleanExMM_RPP25.
GenevestigatorQ91WE3.
GermOnlineENSMUSG00000062309. Mus musculus.

Family and domain databases

InterProIPR002775. DNA/RNA-bd_Alba-like.
[Graphical view]
PfamPF01918. Alba. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio355562.
SOURCESearch...

Entry information

Entry nameRPP25_MOUSE
AccessionPrimary (citable) accession number: Q91WE3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: December 1, 2001
Last modified: April 3, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

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