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Q80UU2 (RPP38_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 p38

Short name=RNaseP protein p38
EC=3.1.26.5
Gene names
Name:Rpp38
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length280 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. RPP38 may associate transiently with RNase P RNA as a factor involved in the transport of H1 RNA to the putative site of its assembly in the cell, the nucleolus By similarity.

Catalytic activity

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

Subunit structure

RNase P consists of an RNA moiety and at least 8 protein subunits; POP1, RPP14, RPP20/POP7, RPP25, RPP29/POP4, RPP30, RPP38 and RPP40. RPP38 is probably a dimer By similarity.

Subcellular location

Nucleusnucleolus Potential.

Sequence similarities

Belongs to the ribosomal protein L7Ae family.

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentNucleus
   Molecular functionHydrolase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processtRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionribonuclease P activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 280279Ribonuclease P protein subunit p38
PRO_0000136784

Regions

Compositional bias63 – 686Poly-Lys

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue2211Phosphoserine By similarity
Modified residue2301Phosphoserine By similarity

Experimental info

Sequence conflict261N → D in BAE23865. Ref.1
Sequence conflict1071Q → K in BAE23865. Ref.1
Sequence conflict1771S → F in BAC40000. Ref.1
Sequence conflict1771S → F in BAE23865. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q80UU2 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: E0AAF663AEEAB4F3

FASTA28031,129
        10         20         30         40         50         60 
MAAAPQAPKR GSIRKTRPLV VKTSLNNPYV ISWSTLERED IHFILQTLEA KFKLIGLQKI 

        70         80         90        100        110        120 
EDKKKRKKTA LMKKQSCRPD IEISEDPKEP DGDVLVSGWT PVHVRKQLVI GVNEVTRALE 

       130        140        150        160        170        180 
RNELLLVLVC KSVKPAIITS HLIQLSLSRT VPACQVPQLS ERIAPVIGLK CVLALGSRKN 

       190        200        210        220        230        240 
TRDFADEVEA IIPRVPSLNV PWLPDRTQGP TDSLETEPSE SQDNEILDTS FDDLTKLSKR 

       250        260        270        280 
KLAEGGQASA ATLQPLKIKK LIPNPSKIRK PPKSKKSISK 

« 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: Aorta and Ovary.
[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: C3H/He.
Tissue: Mesenchymal stem cell.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC051448 mRNA. Translation: AAH51448.1.
AK087782 mRNA. Translation: BAC40000.1.
AK139023 mRNA. Translation: BAE23865.1.
CCDSCCDS15645.1.
UniGeneMm.293948.

3D structure databases

ProteinModelPortalQ80UU2.
SMRQ80UU2. Positions 105-192.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000050992.

PTM databases

PhosphoSiteQ80UU2.

Proteomic databases

PaxDbQ80UU2.
PRIDEQ80UU2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

MGIMGI:2443607. Rpp38.

Phylogenomic databases

eggNOGNOG308103.
HOGENOMHOG000231566.
HOVERGENHBG060241.
InParanoidQ80UU2.
PhylomeDBQ80UU2.

Gene expression databases

CleanExMM_RPP38.
GenevestigatorQ80UU2.

Family and domain databases

Gene3D3.30.1330.30. 1 hit.
InterProIPR029064. L30e-like.
IPR004038. Ribosomal_L7Ae/L30e/S12e/Gad45.
[Graphical view]
PfamPF01248. Ribosomal_L7Ae. 1 hit.
[Graphical view]
SUPFAMSSF55315. SSF55315. 1 hit.
ProtoNetSearch...

Other

PROQ80UU2.
SOURCESearch...

Entry information

Entry nameRPP38_MOUSE
AccessionPrimary (citable) accession number: Q80UU2
Secondary accession number(s): Q3UTW5, Q8BU46
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 76 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

Ribosomal proteins

Ribosomal proteins families and list of entries

MGD cross-references

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