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O95059 (RPP14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonuclease P protein subunit p14

EC=3.1.26.5
Gene names
Name:RPP14
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length124 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Part 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 an RNA moiety and at least 8 protein subunits; POP1, RPP14, RPP20/POP7, RPP25, RPP29/POP4, RPP30, RPP38 and RPP40.

Subcellular location

Nucleus Potential.

Miscellaneous

This protein is produced by a bicistronic gene which also produces the HTD2 protein from an overlapping reading frame.

Sequence similarities

Belongs to the eukaryotic/archaeal RNase P protein component 2 family.

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentNucleus
   Molecular functionHydrolase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processtRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleus

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionRNA binding

Traceable author statement Ref.1. Source: ProtInc

ribonuclease P activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 124123Ribonuclease P protein subunit p14
PRO_0000140010

Sequences

Sequence LengthMass (Da)Tools
O95059 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 10AF6C947785DD90

FASTA12413,693
        10         20         30         40         50         60 
MPAPAATYER VVYKNPSEYH YMKVCLEFQD CGVGLNAAQF KQLLISAVKD LFGEVDAALP 

        70         80         90        100        110        120 
LDILTYEEKT LSAILRICSS GLVKLWSSLT LLGSYKGKKC AFRVIQVSPF LLALSGNSRE 


LVLD 

« Hide

References

« Hide 'large scale' references
[1]"Rpp14 and Rpp29, two protein subunits of human ribonuclease P."
Jarrous N., Eder P.S., Wesolowski D., Altman S.
RNA 5:153-157(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-14.
Tissue: Liver and Spleen.
[2]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"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].
Tissue: Kidney.
[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: Mammary gland and Skin.
[5]"An ancient genetic link between vertebrate mitochondrial fatty acid synthesis and RNA processing."
Autio K.J., Kastaniotis A.J., Pospiech H., Miinalainen I.J., Schonauer M.S., Dieckmann C.L., Hiltunen J.K.
FASEB J. 22:569-578(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF BICISTRONIC GENE.
[6]"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].
[7]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF001175 mRNA. Translation: AAD00892.1.
CR407611 mRNA. Translation: CAG28539.1.
AK311969 mRNA. Translation: BAG34908.1.
BC002441 mRNA. Translation: AAH02441.1.
BC007342 mRNA. Translation: AAH07342.1.
BC012017 mRNA. Translation: AAH12017.1.
RefSeqNP_001092253.1. NM_001098783.2.
NP_008973.1. NM_007042.4.
UniGeneHs.446320.
Hs.700016.

3D structure databases

ProteinModelPortalO95059.
SMRO95059. Positions 18-115.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116283. 18 interactions.
IntActO95059. 16 interactions.
MINTMINT-1368513.
STRING9606.ENSP00000295959.

Proteomic databases

PaxDbO95059.
PRIDEO95059.

Protocols and materials databases

DNASU11102.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295959; ENSP00000295959; ENSG00000163684.
ENST00000445193; ENSP00000412894; ENSG00000163684.
ENST00000466547; ENSP00000419909; ENSG00000163684.
GeneID11102.
KEGGhsa:11102.
UCSCuc003dju.5. human.

Organism-specific databases

CTD11102.
GeneCardsGC03P058267.
HGNCHGNC:30327. RPP14.
HPAHPA036194.
MIM606112. gene.
neXtProtNX_O95059.
PharmGKBPA134896894.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG77977.
HOGENOMHOG000006985.
HOVERGENHBG079505.
InParanoidO95059.
KOK14529.
OMAHHYMKVC.
PhylomeDBO95059.
TreeFamTF324711.

Gene expression databases

BgeeO95059.
CleanExHS_RPP14.
GenevestigatorO95059.

Family and domain databases

InterProIPR002759. RNase_P/MRP_subunit.
[Graphical view]
PfamPF01900. RNase_P_Rpp14. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRPP14. human.
GeneWikiRPP14.
GenomeRNAi11102.
NextBio42210.
PROO95059.
SOURCESearch...

Entry information

Entry nameRPP14_HUMAN
AccessionPrimary (citable) accession number: O95059
Secondary accession number(s): Q53X97
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 112 of the entry and version 3 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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM