Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9DCH2 (POP7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 p20

Short name=RNaseP protein p20
EC=3.1.26.5
Gene names
Name:Pop7
Synonyms:Rpp20
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length140 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 complex, which cleaves pre-rRNA sequences By similarity.

Catalytic activity

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

Subunit structure

Component of nuclear RNase P and RNase MRP complexes. RNase P consists of an RNA moiety and at least 8 protein subunits; POP1, RPP14, RPP20/POP7, RPP25, RPP29/POP4, RPP30, RPP38 and RPP40. RNase MRP consists of an RNA moiety and at least 9 protein subunits; POP1, RPP14, RPP20/POP7, RPP25, RPP29/POP4, RPP30, RPP38, RPP40, POP5 and RPP21. Interacts with RPP25 and SMN1. RPP20/POP7 is probably a dimer By similarity.

Subcellular location

Nucleusnucleolus By similarity. Cytoplasm By similarity. Cytoplasmic granule By similarity. Note: Under stress conditions colocalizes with SMN1 in punctuated cytoplasmic granules By similarity.

Sequence similarities

Belongs to the histone-like Alba family.

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentCytoplasm
Nucleus
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processtRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionnucleic acid binding

Inferred from electronic annotation. Source: InterPro

ribonuclease P activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 140140Ribonuclease P protein subunit p20
PRO_0000237701

Sequences

Sequence LengthMass (Da)Tools
Q9DCH2 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 0F30841C7F50DFA4

FASTA14015,777
        10         20         30         40         50         60 
MAENREPRCA IEAELDPVEY TLRKRLPHRL PRRPNDIYVN MKTDFKAQLA RCQKLLDGGT 

        70         80         90        100        110        120 
RGQNACTEIY IHGLGLAINR AINIALQLQA GSFGSLQVAA NTSTVELVDE LEPETDSREP 

       130        140 
LTRVRNNSAI HIRVFRVTPK 

« Hide

References

« Hide 'large scale' references
[1]"Comparative analysis of the gene-dense ACHE/TFR2 region on human chromosome 7q22 with the orthologous region on mouse chromosome 5."
Wilson M.D., Riemer C., Martindale D.W., Schnupf P., Boright A.P., Cheung T.L., Hardy D.M., Schwartz S., Scherer S.W., Tsui L.-C., Miller W., Koop B.F.
Nucleic Acids Res. 29:1352-1365(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/Sv.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Egg, Kidney and Visual cortex.
[3]"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].
Strain: FVB/N.
Tissue: Colon.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF312033 Genomic DNA. Translation: AAK28826.1.
AK002782 mRNA. Translation: BAB22355.1.
AK158620 mRNA. Translation: BAE34584.1.
AK162268 mRNA. Translation: BAE36826.1.
BC010780 mRNA. Translation: AAH10780.1.
CCDSCCDS19768.1.
RefSeqNP_083029.1. NM_028753.2.
UniGeneMm.290242.

3D structure databases

ProteinModelPortalQ9DCH2.
SMRQ9DCH2. Positions 35-136.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000106664.

PTM databases

PhosphoSiteQ9DCH2.

Proteomic databases

PaxDbQ9DCH2.
PRIDEQ9DCH2.

Protocols and materials databases

DNASU74097.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031728; ENSMUSP00000031728; ENSMUSG00000029715.
ENSMUST00000111035; ENSMUSP00000106664; ENSMUSG00000029715.
GeneID74097.
KEGGmmu:74097.
UCSCuc009aco.1. mouse.

Organism-specific databases

CTD10248.
MGIMGI:1921347. Pop7.

Phylogenomic databases

eggNOGNOG86230.
GeneTreeENSGT00510000048483.
HOGENOMHOG000253010.
HOVERGENHBG001490.
InParanoidQ9DCH2.
KOK14527.
OMACTEIYIH.
OrthoDBEOG7N37FG.
PhylomeDBQ9DCH2.
TreeFamTF313948.

Gene expression databases

BgeeQ9DCH2.
GenevestigatorQ9DCH2.

Family and domain databases

Gene3D3.30.110.20. 1 hit.
InterProIPR002775. DNA/RNA-bd_Alba-like.
IPR014612. RNase_P/MRP_p20.
[Graphical view]
PANTHERPTHR15314. PTHR15314. 1 hit.
PfamPF01918. Alba. 1 hit.
[Graphical view]
PIRSFPIRSF036572. RPP20. 1 hit.
SUPFAMSSF82704. SSF82704. 1 hit.
ProtoNetSearch...

Other

NextBio339761.
PROQ9DCH2.
SOURCESearch...

Entry information

Entry namePOP7_MOUSE
AccessionPrimary (citable) accession number: Q9DCH2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot