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Q9CR08 (RPP29_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 82. 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
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 p29
EC=3.1.26.5
Gene names
Name:Pop4
Synonyms:Rpp29
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length221 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. May function with RPP38 to coordinate the nucleolar targeting and/or assembly of RNase P By similarity.

Catalytic activity

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

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. Interacts with RPP25 and POP5 By similarity.

Subcellular location

Nucleus › nucleolus By similarity.

Sequence similarities

Belongs to the eukaryotic/archaeal RNase P protein component 1 family.

Ontologies

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

Inferred from electronic annotation. Source: InterPro

rRNA processing

Inferred from electronic annotation. Source: InterPro

tRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleolar ribonuclease P complex

Inferred from electronic annotation. Source: InterPro

ribonuclease MRP complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: InterPro

ribonuclease P activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 221221Ribonuclease P protein subunit p29
PRO_0000128419

Amino acid modifications

Modified residue101Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9CR08 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 372E834DFC46A086

FASTA22125,637
        10         20         30         40         50         60 
MKAAIYHAFS HKEAKDHDVQ ELGSQRAEAF VRAFLKQSIP HMSQEDCESH LQRKAVILEY 

        70         80         90        100        110        120 
FTRLKPRPRP KKKSKGLSAK QRRDMRLFDI KPEQQRYSLF LPLHELWKQY IRDLCNGLKP 

       130        140        150        160        170        180 
DTQPQMIQAK LLKADLHGAI ISVTKSKCPS YVGVTGILLQ ETKHVFKIIT REDHLKVIPK 

       190        200        210        220 
LNCVFTIEID DFISYIYGSK FQLRASERSA KKFKAKGSID L

« Hide

References

[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. 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: Bone marrow and Kidney.
[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: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK002855 mRNA. Translation: BAB22410.1.
AK003293 mRNA. Translation: BAB22696.1.
AK150459 mRNA. Translation: BAE29579.1.
AK152948 mRNA. Translation: BAE31617.1.
BC011465 mRNA. Translation: AAH11465.1.
IPIIPI00132900.
RefSeqNP_079666.1. NM_025390.4.
UniGeneMm.22284.

3D structure databases

ProteinModelPortalQ9CR08.
SMRQ9CR08. Positions 108-214.
ModBaseSearch...

PTM databases

PhosphoSiteQ9CR08.

Proteomic databases

PaxDbQ9CR08.
PRIDEQ9CR08.

Protocols and materials databases

DNASU66161.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000032585; ENSMUSP00000032585; ENSMUSG00000030423.
GeneID66161.
KEGGmmu:66161.
UCSCuc009gkv.1. mouse.

Organism-specific databases

CTD10775.
MGIMGI:1913411. Pop4.

Phylogenomic databases

eggNOGNOG255667.
GeneTreeENSGT00390000010067.
HOGENOMHOG000007746.
HOVERGENHBG002676.
InParanoidQ9CR08.
KOK03538.
OMARSKCPSY.
OrthoDBEOG4TXBT7.

Gene expression databases

BgeeQ9CR08.
GenevestigatorQ9CR08.
GermOnlineENSMUSG00000030423. Mus musculus.

Family and domain databases

Gene3D2.30.30.210. 1 hit.
InterProIPR002730. RNase_P/MRP_p29.
IPR016848. RNase_P/MRP_p29-subunit.
IPR023534. Rof/RNase_P-like.
[Graphical view]
PfamPF01868. UPF0086. 1 hit.
[Graphical view]
PIRSFPIRSF027081. RNase_P/MRP_p29_subunit. 1 hit.
SMARTSM00538. POP4. 1 hit.
[Graphical view]
SUPFAMSSF101744. RNase_P_Rpp29. 1 hit.
ProtoNetSearch...

Other

NextBio320810.
SOURCESearch...

Entry information

Entry nameRPP29_MOUSE
AccessionPrimary (citable) accession number: Q9CR08
Secondary accession number(s): Q3U6V7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: June 1, 2001
Last modified: May 1, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

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