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Reviewed, UniProtKB/Swiss-Prot Q969H6 (POP5_HUMAN)

Last modified November 3, 2009. Version 57. 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/MRP protein subunit POP5
      Short name=hPop5
    EC=3.1.26.5
Gene names
Name: POP5
ORF Names: AD-008, HSPC004, x0003
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length163 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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. Ref.1

Catalytic activity

Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. Ref.1

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. 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.1

Subcellular location

Nucleusnucleolus.

Miscellaneous

The last C-terminal 19 amino acids are not required for complex association and RNase activity.

Sequence similarities

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

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentNucleus
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processtRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentnucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionprotein binding Ref.6

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

Chain1 – 163163Ribonuclease P/MRP protein subunit POP5
PRO_0000239007

Amino acid modifications

Modified residue1541Phosphoserine Ref.7 Ref.8 Ref.9

Experimental info

Sequence conflict47 – 482AA → P in AAF17213. Ref.2
Sequence conflict47 – 482AA → P in AAD20966. Ref.3
Sequence conflict991N → D in BAD96926. Ref.4
Sequence conflict1021H → R in BAD96926. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q969H6-1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: DF436E60B3DD50C1

FASTA16318,820
        10         20         30         40         50         60 
MVRFKHRYLL CELVSDDPRC RLSLDDRVLS SLVRDTIARV HGTFGAAACS IGFAVRYLNA 

        70         80         90        100        110        120 
YTGIVLLRCR KEFYQLVWSA LPFITYLENK GHRYPCFFNT LHVGGTIRTC QKFLIQYNRR 

       130        140        150        160 
QLLILLQNCT DEGEREAIQK SVTRSCLLEE EEESGEEAAE AME 

« Hide

References

« Hide 'large scale' references
[1]"hPop5, a protein subunit of the human RNase MRP and RNase P endoribonucleases."
van Eenennaam H., Lugtenberg D., Vogelzangs J.H.P., van Venrooij W.J., Pruijn G.J.M.
J. Biol. Chem. 276:31635-31641(2001) [PubMed: 11413139] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
[2]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed: 10931946] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Adrenal gland.
[3]"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. expand/collapse author list , Gu J., Chen S.-J., Chen Z.
Genome Res. 10:1546-1560(2000) [PubMed: 11042152] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Umbilical cord blood.
[4]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney proximal tubule.
[5]"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.
[6]"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 POP4 AND RPP14.
[7]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, MASS SPECTROMETRY.
Tissue: Epithelium.
[8]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, MASS SPECTROMETRY.
[9]"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-154, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

AJ306296 mRNA. Translation: CAC59822.1.
AF117232 mRNA. Translation: AAF17213.1.
AF070660 mRNA. Translation: AAD20966.1.
AK223206 mRNA. Translation: BAD96926.1.
BC012505 mRNA. Translation: AAH12505.1.
IPIIPI00107563.
RefSeqNP_057002.2.
NP_937845.1.
UniGeneHs.279913

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ969H6. 4 interactions.
STRINGQ969H6.

PTM databases

PhosphoSiteQ969H6.

Genome annotation databases

EnsemblENST00000341039; ENSP00000341791; ENSG00000167272; Homo sapiens. [Genome view]
ENST00000357500; ENSP00000350098; ENSG00000167272; Homo sapiens. [Genome view]
GeneID51367.
KEGGhsa:51367.
UCSCuc001tys.1. human.

Organism-specific databases

CTD51367.
GeneCardsGC12M119479.
H-InvDBHIX0011067.
HGNCHGNC:17689. POP5.
MIM609992. gene.
PharmGKBPA128394660.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ969H6.
HOVERGENQ969H6.
OMACEVVSDD.

Enzyme and pathway databases

BRENDA3.1.26.5. 247.

Gene expression databases

ArrayExpressQ969H6.
BgeeQ969H6.
CleanExHS_POP5.
GenevestigatorQ969H6.
GermOnlineENSG00000167272. Homo sapiens.

Family and domain databases

InterProIPR016819. RNase_P/MRP_POP5.
IPR002759. RNase_P_related.
[Graphical view]
PfamPF01900. RNase_P_Rpp14. 1 hit.
[Graphical view]
PIRSFPIRSF023803. Ribonuclease_P_prd. 1 hit.
ProtoNetSearch...

Other Resources

NextBio54841.
SOURCESearch...

Entry information

Entry namePOP5_HUMAN
AccessionPrimary (citable) accession number: Q969H6
Secondary accession number(s): Q53FS5, Q9Y2Q6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: December 1, 2001
Last modified: November 3, 2009
This is version 57 of the entry and version 1 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 12

Human chromosome 12: 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