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Q9BUL9 (RPP25_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length199 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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.

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 an 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 an RNA moiety and at least 9 protein subunits; POP1, RPP14, RPP20/POP7, RPP25, RPP29/POP4, RPP30, RPP38, RPP40, POP5 and RPP21. Ref.5

Subcellular location

Nucleus Ref.1.

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_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

ribonuclease P activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 199199Ribonuclease P protein subunit p25
PRO_0000237582

Amino acid modifications

Modified residue1721Phosphoserine Ref.6 Ref.7
Modified residue1821Phosphoserine Ref.7

Experimental info

Sequence conflict731A → V in BAA91128. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9BUL9 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 9A4494F0297B2A81

FASTA19920,632
        10         20         30         40         50         60 
MENFRKVRSE EAPAGCGAEG GGPGSGPFAD LAPGAVHMRV KEGSKIRNLM AFATASMAQP 

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

       130        140        150        160        170        180 
EPAASLSVLK NVPGLAILLS KDALDPRQPG YQPPNPHPGP SSPPAAPASK RSLGEPAAGE 

       190 
GSAKRSQPEP GVADEDQTA 

« Hide

References

« Hide 'large scale' references
[1]"Purification and characterization of Rpp25, an RNA-binding protein subunit of human ribonuclease P."
Guerrier-Takada C., Eder P.S., Gopalan V., Altman S.
RNA 8:290-295(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], RNA-BINDING, SUBCELLULAR LOCATION.
[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. expand/collapse author list , 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].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: Brain and Skin.
[5]"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 POP7; POP4 AND RMRP.
[6]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"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-172 AND SER-182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY034074 mRNA. Translation: AAK54443.1.
AK000381 mRNA. Translation: BAA91128.1.
CH471136 Genomic DNA. Translation: EAW99285.1.
CH471136 Genomic DNA. Translation: EAW99286.1.
BC002497 mRNA. Translation: AAH02497.1.
BC007270 mRNA. Translation: AAH07270.1.
RefSeqNP_060263.2. NM_017793.2.
UniGeneHs.8562.

3D structure databases

ProteinModelPortalQ9BUL9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120255. 8 interactions.
IntActQ9BUL9. 5 interactions.
MINTMINT-5009653.
STRING9606.ENSP00000317691.

PTM databases

PhosphoSiteQ9BUL9.

Polymorphism databases

DMDM74733233.

Proteomic databases

PaxDbQ9BUL9.
PeptideAtlasQ9BUL9.
PRIDEQ9BUL9.

Protocols and materials databases

DNASU54913.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000322177; ENSP00000317691; ENSG00000178718.
ENST00000499788; ENSP00000446246; ENSG00000178718.
GeneID54913.
KEGGhsa:54913.
UCSCuc002azj.1. human.

Organism-specific databases

CTD54913.
GeneCardsGC15M075247.
HGNCHGNC:30361. RPP25.
HPAHPA046900.
neXtProtNX_Q9BUL9.
PharmGKBPA134990737.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG247262.
HOGENOMHOG000231665.
HOVERGENHBG056729.
InParanoidQ9BUL9.
KOK14525.
OMAAVHMRVK.
OrthoDBEOG7XM309.
PhylomeDBQ9BUL9.
TreeFamTF325688.

Gene expression databases

BgeeQ9BUL9.
CleanExHS_RPP25.
GenevestigatorQ9BUL9.

Family and domain databases

Gene3D3.30.110.20. 1 hit.
InterProIPR002775. DNA/RNA-bd_Alba-like.
[Graphical view]
PfamPF01918. Alba. 1 hit.
[Graphical view]
SUPFAMSSF82704. SSF82704. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi54913.
NextBio57966.
PROQ9BUL9.

Entry information

Entry nameRPP25_HUMAN
AccessionPrimary (citable) accession number: Q9BUL9
Secondary accession number(s): D3DW70, Q9NX88
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM