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Protein

60S acidic ribosomal protein P1

Gene

Rplp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Plays an important role in the elongation step of protein synthesis.

GO - Molecular functioni

GO - Biological processi

  • regulation of translation Source: MGI
  • translational elongation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_279505. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_292264. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_302277. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_308559. Formation of a pool of free 40S subunits.
REACT_311765. Peptide chain elongation.
REACT_319670. Eukaryotic Translation Termination.
REACT_331340. SRP-dependent cotranslational protein targeting to membrane.
REACT_340387. L13a-mediated translational silencing of Ceruloplasmin expression.

Names & Taxonomyi

Protein namesi
Recommended name:
60S acidic ribosomal protein P1
Gene namesi
Name:Rplp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1927099. Rplp1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 11411360S acidic ribosomal protein P1PRO_0000157687Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei101 – 1011PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP47955.
PaxDbiP47955.
PRIDEiP47955.

PTM databases

PhosphoSiteiP47955.

Expressioni

Gene expression databases

BgeeiP47955.
CleanExiMM_RPLP1.
ExpressionAtlasiP47955. baseline and differential.
GenevisibleiP47955. MM.

Interactioni

Subunit structurei

Heterodimer with RPLP2 at the lateral ribosomal stalk of the large ribosomal subunit.By similarity

Protein-protein interaction databases

BioGridi207787. 11 interactions.
IntActiP47955. 5 interactions.
MINTiMINT-4132672.
STRINGi10090.ENSMUSP00000008036.

Structurei

3D structure databases

ProteinModelPortaliP47955.
SMRiP47955. Positions 1-114.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L12P family.Curated

Phylogenomic databases

eggNOGiCOG2058.
HOGENOMiHOG000229898.
HOVERGENiHBG002291.
InParanoidiP47955.
KOiK02942.
OMAiICNIGVG.
OrthoDBiEOG7M0NVC.
PhylomeDBiP47955.
TreeFamiTF312932.

Family and domain databases

HAMAPiMF_01478. Ribosomal_L12_arch.
InterProiIPR027534. Ribosomal_L12.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P47955-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASVSELACI YSALILHDDE VTVTEDKINA LIKAAGVSVE PFWPGLFAKA
60 70 80 90 100
LANVNIGSLI CNVGAGGPAP AAGAAPAGGA APSTAAAPAE EKKVEAKKEE
110
SEESEDDMGF GLFD
Length:114
Mass (Da):11,475
Last modified:February 1, 1996 - v1
Checksum:i63C344A2772350D2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29402 mRNA. Translation: AAA70106.1.
AK007832 mRNA. Translation: BAB25292.1.
AK010656 mRNA. Translation: BAB27095.1.
AK088070 mRNA. Translation: BAC40128.1.
BC058685 mRNA. Translation: AAH58685.1.
CCDSiCCDS23260.1.
RefSeqiNP_061341.1. NM_018853.3.
UniGeneiMm.3158.

Genome annotation databases

EnsembliENSMUST00000008036; ENSMUSP00000008036; ENSMUSG00000007892.
GeneIDi56040.
KEGGimmu:56040.
UCSCiuc009pzt.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29402 mRNA. Translation: AAA70106.1.
AK007832 mRNA. Translation: BAB25292.1.
AK010656 mRNA. Translation: BAB27095.1.
AK088070 mRNA. Translation: BAC40128.1.
BC058685 mRNA. Translation: AAH58685.1.
CCDSiCCDS23260.1.
RefSeqiNP_061341.1. NM_018853.3.
UniGeneiMm.3158.

3D structure databases

ProteinModelPortaliP47955.
SMRiP47955. Positions 1-114.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207787. 11 interactions.
IntActiP47955. 5 interactions.
MINTiMINT-4132672.
STRINGi10090.ENSMUSP00000008036.

PTM databases

PhosphoSiteiP47955.

Proteomic databases

MaxQBiP47955.
PaxDbiP47955.
PRIDEiP47955.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000008036; ENSMUSP00000008036; ENSMUSG00000007892.
GeneIDi56040.
KEGGimmu:56040.
UCSCiuc009pzt.1. mouse.

Organism-specific databases

CTDi6176.
MGIiMGI:1927099. Rplp1.

Phylogenomic databases

eggNOGiCOG2058.
HOGENOMiHOG000229898.
HOVERGENiHBG002291.
InParanoidiP47955.
KOiK02942.
OMAiICNIGVG.
OrthoDBiEOG7M0NVC.
PhylomeDBiP47955.
TreeFamiTF312932.

Enzyme and pathway databases

ReactomeiREACT_279505. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_292264. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_302277. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_308559. Formation of a pool of free 40S subunits.
REACT_311765. Peptide chain elongation.
REACT_319670. Eukaryotic Translation Termination.
REACT_331340. SRP-dependent cotranslational protein targeting to membrane.
REACT_340387. L13a-mediated translational silencing of Ceruloplasmin expression.

Miscellaneous databases

NextBioi311800.
PROiP47955.
SOURCEiSearch...

Gene expression databases

BgeeiP47955.
CleanExiMM_RPLP1.
ExpressionAtlasiP47955. baseline and differential.
GenevisibleiP47955. MM.

Family and domain databases

HAMAPiMF_01478. Ribosomal_L12_arch.
InterProiIPR027534. Ribosomal_L12.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Crowe D.L., Cui X.M., Shuler C.F.
    Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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.
    , 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: Head and Pancreas.
  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: C57BL/6.
    Tissue: Brain.

Entry informationi

Entry nameiRLA1_MOUSE
AccessioniPrimary (citable) accession number: P47955
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: June 24, 2015
This is version 113 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.