Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ribonuclease P protein subunit p25

Gene

RPP25

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
  • ribonuclease P activity Source: UniProtKB-EC

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease P protein subunit p25 (EC:3.1.26.5)
Short name:
RNase P protein subunit p25
Gene namesi
Name:RPP25
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:30361. RPP25.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134990737.

Polymorphism and mutation databases

BioMutaiRPP25.
DMDMi74733233.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 199199Ribonuclease P protein subunit p25PRO_0000237582Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei172 – 1721Phosphoserine2 Publications
Modified residuei182 – 1821Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9BUL9.
PaxDbiQ9BUL9.
PeptideAtlasiQ9BUL9.
PRIDEiQ9BUL9.

PTM databases

PhosphoSiteiQ9BUL9.

Expressioni

Gene expression databases

BgeeiQ9BUL9.
CleanExiHS_RPP25.
GenevisibleiQ9BUL9. HS.

Organism-specific databases

HPAiHPA046900.

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. 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 RPP21.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
POP4O957072EBI-366570,EBI-366477
POP7O758172EBI-366570,EBI-366574

Protein-protein interaction databases

BioGridi120255. 17 interactions.
IntActiQ9BUL9. 5 interactions.
MINTiMINT-5009653.
STRINGi9606.ENSP00000317691.

Structurei

3D structure databases

ProteinModelPortaliQ9BUL9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histone-like Alba family.Curated

Phylogenomic databases

eggNOGiNOG247262.
GeneTreeiENSGT00390000002564.
HOGENOMiHOG000231665.
HOVERGENiHBG056729.
InParanoidiQ9BUL9.
KOiK14525.
OMAiMENFRKV.
OrthoDBiEOG7XM309.
PhylomeDBiQ9BUL9.
TreeFamiTF325688.

Family and domain databases

Gene3Di3.30.110.20. 1 hit.
InterProiIPR002775. DNA/RNA-bd_Alba-like.
[Graphical view]
PfamiPF01918. Alba. 1 hit.
[Graphical view]
SUPFAMiSSF82704. SSF82704. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9BUL9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENFRKVRSE EAPAGCGAEG GGPGSGPFAD LAPGAVHMRV KEGSKIRNLM
60 70 80 90 100
AFATASMAQP ATRAIVFSGC GRATTKTVTC AEILKRRLAG LHQVTRLRYR
110 120 130 140 150
SVREVWQSLP PGPTQGQTPG EPAASLSVLK NVPGLAILLS KDALDPRQPG
160 170 180 190
YQPPNPHPGP SSPPAAPASK RSLGEPAAGE GSAKRSQPEP GVADEDQTA
Length:199
Mass (Da):20,632
Last modified:June 1, 2001 - v1
Checksum:i9A4494F0297B2A81
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 731A → V in BAA91128 (PubMed:14702039).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS10274.1.
RefSeqiNP_060263.2. NM_017793.2.
UniGeneiHs.8562.

Genome annotation databases

EnsembliENST00000322177; ENSP00000317691; ENSG00000178718.
GeneIDi54913.
KEGGihsa:54913.
UCSCiuc002azj.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS10274.1.
RefSeqiNP_060263.2. NM_017793.2.
UniGeneiHs.8562.

3D structure databases

ProteinModelPortaliQ9BUL9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120255. 17 interactions.
IntActiQ9BUL9. 5 interactions.
MINTiMINT-5009653.
STRINGi9606.ENSP00000317691.

PTM databases

PhosphoSiteiQ9BUL9.

Polymorphism and mutation databases

BioMutaiRPP25.
DMDMi74733233.

Proteomic databases

MaxQBiQ9BUL9.
PaxDbiQ9BUL9.
PeptideAtlasiQ9BUL9.
PRIDEiQ9BUL9.

Protocols and materials databases

DNASUi54913.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000322177; ENSP00000317691; ENSG00000178718.
GeneIDi54913.
KEGGihsa:54913.
UCSCiuc002azj.1. human.

Organism-specific databases

CTDi54913.
GeneCardsiGC15M075247.
HGNCiHGNC:30361. RPP25.
HPAiHPA046900.
neXtProtiNX_Q9BUL9.
PharmGKBiPA134990737.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG247262.
GeneTreeiENSGT00390000002564.
HOGENOMiHOG000231665.
HOVERGENiHBG056729.
InParanoidiQ9BUL9.
KOiK14525.
OMAiMENFRKV.
OrthoDBiEOG7XM309.
PhylomeDBiQ9BUL9.
TreeFamiTF325688.

Miscellaneous databases

GenomeRNAii54913.
NextBioi57966.
PROiQ9BUL9.

Gene expression databases

BgeeiQ9BUL9.
CleanExiHS_RPP25.
GenevisibleiQ9BUL9. HS.

Family and domain databases

Gene3Di3.30.110.20. 1 hit.
InterProiIPR002775. DNA/RNA-bd_Alba-like.
[Graphical view]
PfamiPF01918. Alba. 1 hit.
[Graphical view]
SUPFAMiSSF82704. SSF82704. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRPP25_HUMAN
AccessioniPrimary (citable) accession number: Q9BUL9
Secondary accession number(s): D3DW70, Q9NX88
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: June 1, 2001
Last modified: June 24, 2015
This is version 98 of the entry and version 1 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, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

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.