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Q9DB28

- POP5_MOUSE

UniProt

Q9DB28 - POP5_MOUSE

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Protein
Ribonuclease P/MRP protein subunit POP5
Gene
Pop5
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP By similarity.

Catalytic activityi

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

GO - Molecular functioni

  1. ribonuclease MRP activity Source: MGI
  2. ribonuclease P activity Source: MGI
Complete GO annotation...

GO - Biological processi

  1. RNA phosphodiester bond hydrolysis Source: GOC
  2. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
  3. rRNA processing Source: MGI
  4. tRNA processing Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

tRNA processing

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease P/MRP protein subunit POP5 (EC:3.1.26.5)
Gene namesi
Name:Pop5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:2151221. Pop5.

Subcellular locationi

Nucleusnucleolus By similarity

GO - Cellular componenti

  1. nucleolar ribonuclease P complex Source: MGI
  2. ribonuclease MRP complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 169169Ribonuclease P/MRP protein subunit POP5
PRO_0000239008Add
BLAST

Proteomic databases

PRIDEiQ9DB28.

PTM databases

PhosphoSiteiQ9DB28.

Expressioni

Gene expression databases

ArrayExpressiQ9DB28.
BgeeiQ9DB28.
GenevestigatoriQ9DB28.

Interactioni

Subunit structurei

Component of nuclear RNase P and RNase MRP ribonucleoproteins. 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 By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ9DB28.
SMRiQ9DB28. Positions 1-120.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG284693.
GeneTreeiENSGT00390000012331.
HOGENOMiHOG000293345.
HOVERGENiHBG082157.
InParanoidiQ9DB28.
KOiK03537.
OMAiCEVVSDD.
OrthoDBiEOG7GTT69.
PhylomeDBiQ9DB28.
TreeFamiTF317496.

Family and domain databases

InterProiIPR016819. RNase_P/MRP_POP5.
IPR002759. RNase_P/MRP_subunit.
[Graphical view]
PfamiPF01900. RNase_P_Rpp14. 1 hit.
[Graphical view]
PIRSFiPIRSF023803. Ribonuclease_P_prd. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9DB28-1 [UniParc]FASTAAdd to Basket

« Hide

MVRFKHRYLL CELVSEDARC RLSLDDRVLG GLVRDTIARV HGAFGAAACS    50
VGFAVRYLNA YTGVVLLRCR KDFYQLVWSA LPFITYLENK GHRYPCFFNT 100
LHVGGTIRTC QKFLIQYNRR QLLILLQNCT DEGEREAIKK SVSRSCLLDR 150
EPVEELSDSA GEEVAEAME 169
Length:169
Mass (Da):19,285
Last modified:June 1, 2001 - v1
Checksum:i8334DECD7665A48D
GO

Sequence cautioni

The sequence BAB28294.1 differs from that shown. Reason: Frameshift at position 44.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21V → R in BAB28751. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK005290 mRNA. Translation: BAB23935.1.
AK012523 mRNA. Translation: BAB28294.1. Frameshift.
AK013257 mRNA. Translation: BAB28751.1.
BC022670 mRNA. Translation: AAH22670.1.
CCDSiCCDS19583.1.
RefSeqiNP_080674.1. NM_026398.4.
UniGeneiMm.24636.

Genome annotation databases

EnsembliENSMUST00000081497; ENSMUSP00000080215; ENSMUSG00000060152.
ENSMUST00000135455; ENSMUSP00000118408; ENSMUSG00000060152.
GeneIDi117109.
KEGGimmu:117109.
UCSCiuc008zdi.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK005290 mRNA. Translation: BAB23935.1 .
AK012523 mRNA. Translation: BAB28294.1 . Frameshift.
AK013257 mRNA. Translation: BAB28751.1 .
BC022670 mRNA. Translation: AAH22670.1 .
CCDSi CCDS19583.1.
RefSeqi NP_080674.1. NM_026398.4.
UniGenei Mm.24636.

3D structure databases

ProteinModelPortali Q9DB28.
SMRi Q9DB28. Positions 1-120.
ModBasei Search...

PTM databases

PhosphoSitei Q9DB28.

Proteomic databases

PRIDEi Q9DB28.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000081497 ; ENSMUSP00000080215 ; ENSMUSG00000060152 .
ENSMUST00000135455 ; ENSMUSP00000118408 ; ENSMUSG00000060152 .
GeneIDi 117109.
KEGGi mmu:117109.
UCSCi uc008zdi.1. mouse.

Organism-specific databases

CTDi 51367.
MGIi MGI:2151221. Pop5.

Phylogenomic databases

eggNOGi NOG284693.
GeneTreei ENSGT00390000012331.
HOGENOMi HOG000293345.
HOVERGENi HBG082157.
InParanoidi Q9DB28.
KOi K03537.
OMAi CEVVSDD.
OrthoDBi EOG7GTT69.
PhylomeDBi Q9DB28.
TreeFami TF317496.

Miscellaneous databases

ChiTaRSi POP5. mouse.
NextBioi 369498.
PROi Q9DB28.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9DB28.
Bgeei Q9DB28.
Genevestigatori Q9DB28.

Family and domain databases

InterProi IPR016819. RNase_P/MRP_POP5.
IPR002759. RNase_P/MRP_subunit.
[Graphical view ]
Pfami PF01900. RNase_P_Rpp14. 1 hit.
[Graphical view ]
PIRSFi PIRSF023803. Ribonuclease_P_prd. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "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.
    , 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: Cerebellum and Embryo.
  2. "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.

Entry informationi

Entry nameiPOP5_MOUSE
AccessioniPrimary (citable) accession number: Q9DB28
Secondary accession number(s): Q9CSC3, Q9CSL4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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