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Q80UU2

- RPP38_MOUSE

UniProt

Q80UU2 - RPP38_MOUSE

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Protein

Ribonuclease P protein subunit p38

Gene

Rpp38

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 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. 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).By similarity

Catalytic activityi

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

GO - Molecular functioni

  1. ribonuclease P activity Source: UniProtKB-EC

GO - Biological processi

  1. tRNA processing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

tRNA processing

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease P protein subunit p38 (EC:3.1.26.5)
Short name:
RNaseP protein p38
Gene namesi
Name:Rpp38
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:2443607. Rpp38.

Subcellular locationi

Nucleusnucleolus Curated

GO - Cellular componenti

  1. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 280279Ribonuclease P protein subunit p38PRO_0000136784Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei221 – 2211PhosphoserineBy similarity
Modified residuei230 – 2301PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ80UU2.
PaxDbiQ80UU2.
PRIDEiQ80UU2.

PTM databases

PhosphoSiteiQ80UU2.

Expressioni

Gene expression databases

CleanExiMM_RPP38.
GenevestigatoriQ80UU2.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000050992.

Structurei

3D structure databases

ProteinModelPortaliQ80UU2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi63 – 686Poly-Lys

Sequence similaritiesi

Belongs to the ribosomal protein L7Ae family.Curated

Phylogenomic databases

eggNOGiNOG308103.
HOGENOMiHOG000231566.
HOVERGENiHBG060241.
InParanoidiQ80UU2.
PhylomeDBiQ80UU2.

Family and domain databases

Gene3Di3.30.1330.30. 1 hit.
InterProiIPR029064. L30e-like.
IPR004038. Ribosomal_L7Ae/L30e/S12e/Gad45.
[Graphical view]
PfamiPF01248. Ribosomal_L7Ae. 1 hit.
[Graphical view]
SUPFAMiSSF55315. SSF55315. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q80UU2-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MAAAPQAPKR GSIRKTRPLV VKTSLNNPYV ISWSTLERED IHFILQTLEA
60 70 80 90 100
KFKLIGLQKI EDKKKRKKTA LMKKQSCRPD IEISEDPKEP DGDVLVSGWT
110 120 130 140 150
PVHVRKQLVI GVNEVTRALE RNELLLVLVC KSVKPAIITS HLIQLSLSRT
160 170 180 190 200
VPACQVPQLS ERIAPVIGLK CVLALGSRKN TRDFADEVEA IIPRVPSLNV
210 220 230 240 250
PWLPDRTQGP TDSLETEPSE SQDNEILDTS FDDLTKLSKR KLAEGGQASA
260 270 280
ATLQPLKIKK LIPNPSKIRK PPKSKKSISK
Length:280
Mass (Da):31,129
Last modified:June 1, 2003 - v1
Checksum:iE0AAF663AEEAB4F3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261N → D in BAE23865. (PubMed:16141072)Curated
Sequence conflicti107 – 1071Q → K in BAE23865. (PubMed:16141072)Curated
Sequence conflicti177 – 1771S → F in BAC40000. (PubMed:16141072)Curated
Sequence conflicti177 – 1771S → F in BAE23865. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC051448 mRNA. Translation: AAH51448.1.
AK087782 mRNA. Translation: BAC40000.1.
AK139023 mRNA. Translation: BAE23865.1.
CCDSiCCDS15645.1.
UniGeneiMm.293948.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC051448 mRNA. Translation: AAH51448.1 .
AK087782 mRNA. Translation: BAC40000.1 .
AK139023 mRNA. Translation: BAE23865.1 .
CCDSi CCDS15645.1.
UniGenei Mm.293948.

3D structure databases

ProteinModelPortali Q80UU2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000050992.

PTM databases

PhosphoSitei Q80UU2.

Proteomic databases

MaxQBi Q80UU2.
PaxDbi Q80UU2.
PRIDEi Q80UU2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

MGIi MGI:2443607. Rpp38.

Phylogenomic databases

eggNOGi NOG308103.
HOGENOMi HOG000231566.
HOVERGENi HBG060241.
InParanoidi Q80UU2.
PhylomeDBi Q80UU2.

Miscellaneous databases

PROi Q80UU2.
SOURCEi Search...

Gene expression databases

CleanExi MM_RPP38.
Genevestigatori Q80UU2.

Family and domain databases

Gene3Di 3.30.1330.30. 1 hit.
InterProi IPR029064. L30e-like.
IPR004038. Ribosomal_L7Ae/L30e/S12e/Gad45.
[Graphical view ]
Pfami PF01248. Ribosomal_L7Ae. 1 hit.
[Graphical view ]
SUPFAMi SSF55315. SSF55315. 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: 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.

Entry informationi

Entry nameiRPP38_MOUSE
AccessioniPrimary (citable) accession number: Q80UU2
Secondary accession number(s): Q3UTW5, Q8BU46
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: June 1, 2003
Last modified: October 29, 2014
This is version 78 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. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3