P78346 (RPP30_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribonuclease P protein subunit p30
Short name=RNaseP protein p30
EC=3.1.26.5

Alternative name(s):
RNase P subunit 2

Gene names

Name:	RPP30
Synonyms:	RNASEP2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	268 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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.
Catalytic activity	Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Subunit structure	RNase P consists of a RNA moiety and at least 8 protein subunits; POP1, RPP14, RPP20/POP7, RPP25, RPP29/POP4, RPP30, RPP38 and RPP40.
Subcellular location	Nucleus › nucleolus Potential.
Miscellaneous	Autoantibodies against RPP30 are found in sera from scleroderma patients.
Sequence similarities	Belongs to the eukaryotic/archaeal RNase P protein component 3 family.

Ontologies

Keywords
Biological process	tRNA processing
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	tRNA processing Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleolar ribonuclease P complex Traceable author statement PubMed 9630247. Source: ProtInc
Molecular_function	ribonuclease P activity Traceable author statement PubMed 9630247. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P78346-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P78346-2)

The sequence of this isoform differs from the canonical sequence as follows:
     266-268: CEG → WSHSVTQAGVQWHNLGSLQPLPLGLKPSSHLSLPRTRIQQRQLLISHQRDHTPKNRL

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.7
	Chain	2 – 268	267	Ribonuclease P protein subunit p30		PRO_0000140031
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.7
	Modified residue	251	1	Phosphoserine Ref.8 Ref.9 Ref.10
Natural variations
	Alternative sequence	266 – 268	3	CEG → WSHSVTQAGVQWHNLGSLQP LPLGLKPSSHLSLPRTRIQQ RQLLISHQRDHTPKNRL in isoform 2.		VSP_045673
	Natural variant	12	1	G → D. Corresponds to variant rs11544145 [ dbSNP | Ensembl ].		VAR_051870
Experimental info
	Sequence conflict	65	1	Q → R in AK225532. Ref.3
	Sequence conflict	189	1	S → I AA sequence Ref.1
Isoform 2:
	Sequence conflict	291	1	K → R in AK225532. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 2AB492D98ACDCCBB	FASTA	268	29,321
	10 20 30 40 50 60 MAVFADLDLR AGSDLKALRG LVETAAHLGY SVVAINHIVD FKEKKQEIEK PVAVSELFTT 70 80 90 100 110 120 LPIVQGKSRP IKILTRLTII VSDPSHCNVL RATSSRARLY DVVAVFPKTE KLFHIACTHL 130 140 150 160 170 180 DVDLVCITVT EKLPFYFKRP PINVAIDRGL AFELVYSPAI KDSTMRRYTI SSALNLMQIC 190 200 210 220 230 240 KGKNVIISSA AERPLEIRGP YDVANLGLLF GLSESDAKAA VSTNCRAALL HGETRKTAFG 250 260 IISTVKKPRP SEGDEDCLPA SKKAKCEG
	Isoform 2 [UniParc]. Checksum: B6700D9E4A95C181	FASTA	322	35,564
	10 20 30 40 50 60 MAVFADLDLR AGSDLKALRG LVETAAHLGY SVVAINHIVD FKEKKQEIEK PVAVSELFTT 70 80 90 100 110 120 LPIVQGKSRP IKILTRLTII VSDPSHCNVL RATSSRARLY DVVAVFPKTE KLFHIACTHL 130 140 150 160 170 180 DVDLVCITVT EKLPFYFKRP PINVAIDRGL AFELVYSPAI KDSTMRRYTI SSALNLMQIC 190 200 210 220 230 240 KGKNVIISSA AERPLEIRGP YDVANLGLLF GLSESDAKAA VSTNCRAALL HGETRKTAFG 250 260 270 280 290 300 IISTVKKPRP SEGDEDCLPA SKKAKWSHSV TQAGVQWHNL GSLQPLPLGL KPSSHLSLPR 310 320 TRIQQRQLLI SHQRDHTPKN RL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of two scleroderma autoimmune antigens that copurify with human ribonuclease P." Eder P.S., Kekuda R., Stolc V., Altman S. Proc. Natl. Acad. Sci. U.S.A. 94:1101-1106(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 21-30; 140-148 AND 185-198.
[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] (ISOFORM 1). Tissue: Brain.
[3]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Signet-ring cell carcinoma.
[4]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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].
[6]	"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] (ISOFORM 1). Tissue: Kidney.
[7]	Bienvenut W.V., Lao L., Ryan K.M. Submitted (JUN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-10; 99-108; 139-161; 184-198 AND 237-246, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Osteosarcoma.
[8]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"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	U77665 mRNA. Translation: AAC51143.1. AK312900 mRNA. Translation: BAG35746.1. AK225532 mRNA. No translation available. AL590622 Genomic DNA. Translation: CAC70100.1. CH471066 Genomic DNA. Translation: EAW50117.1. BC006991 mRNA. Translation: AAH06991.1.
IPI	IPI00019196. IPI00876864.
RefSeq	NP_001098016.1. NM_001104546.1. NP_006404.1. NM_006413.4.
UniGene	Hs.139120.
3D structure databases
ProteinModelPortal	P78346.
ModBase	Search...
Protein-protein interaction databases
IntAct	P78346. 3 interactions.
STRING	9606.ENSP00000389182.
PTM databases
PhosphoSite	P78346.
Polymorphism databases
DMDM	13124514.
Proteomic databases
PaxDb	P78346.
PRIDE	P78346.
Protocols and materials databases
DNASU	10556.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000371703; ENSP00000360768; ENSG00000148688. ENST00000413330; ENSP00000389182; ENSG00000148688.
GeneID	10556.
KEGG	hsa:10556.
UCSC	uc009xtx.3. human.
Organism-specific databases
CTD	10556.
GeneCards	GC10P092621.
HGNC	HGNC:17688. RPP30.
HPA	HPA037578.
MIM	606115. gene.
neXtProt	NX_P78346.
PharmGKB	PA134876345.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1603.
HOGENOM	HOG000157793.
HOVERGEN	HBG010226.
KO	K03539.
OrthoDB	EOG4D52Z9.
PhylomeDB	P78346.
Gene expression databases
ArrayExpress	P78346.
Bgee	P78346.
CleanEx	HS_RPP30.
Genevestigator	P78346.
GermOnline	ENSG00000148688. Homo sapiens.
Family and domain databases
InterPro	IPR016195. Pol/histidinol_Pase-like. IPR002738. RNase_P_p30. [Graphical view]
PANTHER	PTHR13031. PTHR13031. 1 hit.
Pfam	PF01876. RNase_P_p30. 1 hit. [Graphical view]
SUPFAM	SSF89550. PHP-like. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	10556.
NextBio	40053.
SOURCE	Search...

Entry information

Entry name

RPP30_HUMAN

Accession

Primary (citable) accession number: P78346
Secondary accession number(s): B2R799, E9PB02

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	May 1, 1997
Last modified:	May 1, 2013
This is version 121 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.