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Reviewed, UniProtKB/Swiss-Prot O95059 (RPP14_HUMAN)

Last modified November 24, 2009. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Ribonuclease P protein subunit p14
    EC=3.1.26.5
Gene names
Name: RPP14
OrganismHomo sapiens (Human) [Complete 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 a RNA moiety and at least 8 protein subunits; POP1, RPP14, RPP20/POP7, RPP25, RPP29/POP4, RPP30, RPP38 and RPP40.

Subcellular location

Nucleus Potential.

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
Gene Ontology (GO)
   Biological processtRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentnucleus Ref.1

Traceable author statement. Source: ProtInc

   Molecular functionRNA binding Ref.1

Traceable author statement. Source: ProtInc

identical protein binding

Inferred from physical interaction. Source: IntAct

ribonuclease P activity

Inferred from electronic annotation. Source: 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
O95059-1 [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: 10024167] [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: 14702039] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary gland and Skin.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
IPIIPI00215966.
RefSeqNP_001092253.1.
NP_008973.1.
UniGeneHs.446320
Hs.700016

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActO95059. 7 interactions.
STRINGO95059.

Proteomic databases

PRIDEO95059.

Genome annotation databases

EnsemblENST00000295959; ENSP00000295959; ENSG00000163684; Homo sapiens. [Genome view]
ENST00000445193; ENSP00000412894; ENSG00000163684; Homo sapiens. [Genome view]
ENST00000466547; ENSP00000419909; ENSG00000163684; Homo sapiens. [Genome view]
GeneID11102.
KEGGhsa:11102.
UCSCuc003dju.2. human.

Organism-specific databases

CTD11102.
GeneCardsGC03P058267.
H-InvDBHIX0003400.
HGNCHGNC:30327. RPP14.
MIM606112. gene.
PharmGKBPA134896894.
GenAtlasSearch...

Phylogenomic databases

HOGENOMO95059.
HOVERGENO95059.
OMAAQFKQLI
OrthoDBEOG9ZW7WS

Enzyme and pathway databases

BRENDA3.1.26.5. 247.

Gene expression databases

ArrayExpressO95059.
BgeeO95059.
CleanExHS_RPP14.
GenevestigatorO95059.
GermOnlineENSG00000163684. Homo sapiens.

Family and domain databases

InterProIPR002759. RNase_P_related.
[Graphical view]
PfamPF01900. RNase_P_Rpp14. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio42210.
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: November 24, 2009
This is version 77 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 3

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

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents