Q9BUL9 (RPP25_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribonuclease P protein subunit p25
Short name=RNase P protein subunit p25
EC=3.1.26.5

Gene names

Name:

RPP25

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	199 AA.
Sequence status	Complete.
Protein existence	Evidence 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 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. Ref.5
Subcellular location	Nucleus Ref.1.
Sequence similarities	Belongs to the histone-like Alba family.

Ontologies

Keywords
Biological process	tRNA processing
Cellular component	Nucleus
Ligand	RNA-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	tRNA processing Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.5. Source: IntAct ribonuclease P activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
POP4	O95707	2	EBI-366570,EBI-366477
POP7	O75817	2	EBI-366570,EBI-366574

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 199	199	Ribonuclease P protein subunit p25		PRO_0000237582
Amino acid modifications
	Modified residue	162	1	Phosphoserine Ref.6
	Modified residue	172	1	Phosphoserine Ref.7
Experimental info
	Sequence conflict	73	1	A → V in BAA91128. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9BUL9 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 9A4494F0297B2A81	FASTA	199	20,632
	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

References

	« Hide 'large scale' referencesShow '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: 12003489] [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: 14702039] [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. , 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: 15489334] [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: 15096576] [Abstract] Cited for: INTERACTION WITH POP7; POP4 AND RMRP.
[6]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[7]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172, MASS SPECTROMETRY. 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: 21269460] [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.
IPI	IPI00306056.
RefSeq	NP_060263.2. NM_017793.2.
UniGene	Hs.8562.
3D structure databases
ProteinModelPortal	Q9BUL9.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9BUL9. 5 interactions.
STRING	Q9BUL9.
PTM databases
PhosphoSite	Q9BUL9.
Polymorphism databases
DMDM	74733233.
Proteomic databases
PeptideAtlas	Q9BUL9.
PRIDE	Q9BUL9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000322177; ENSP00000317691; ENSG00000178718.
GeneID	54913.
KEGG	hsa:54913.
UCSC	uc002azj.1. human.
Organism-specific databases
CTD	54913.
GeneCards	GC15M075247.
H-InvDB	HIX0012434.
HGNC	HGNC:30361. RPP25.
HPA	HPA046900.
neXtProt	NX_Q9BUL9.
PharmGKB	PA134990737.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG17447.
GeneTree	ENSGT00390000002564.
HOGENOM	HBG749867.
HOVERGEN	HBG056729.
InParanoid	Q9BUL9.
OMA	AVHMRVK.
OrthoDB	EOG49ZXQR.
PhylomeDB	Q9BUL9.
Gene expression databases
ArrayExpress	Q9BUL9.
Bgee	Q9BUL9.
CleanEx	HS_RPP25.
Genevestigator	Q9BUL9.
GermOnline	ENSG00000178718. Homo sapiens.
Family and domain databases
InterPro	IPR002775. DNA/RNA-bd_Alba-like. [Graphical view]
KO	K14525.
Pfam	PF01918. Alba. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	57966.

Entry information

Entry name

RPP25_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.