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Protein

60S ribosomal protein L27

Gene

Rpl27

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiR-MMU-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-MMU-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-MMU-6791226. Major pathway of rRNA processing in the nucleolus.
R-MMU-72689. Formation of a pool of free 40S subunits.
R-MMU-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-MMU-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-MMU-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L27
Gene namesi
Name:Rpl27
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componentsi: Chromosome 11, Chromosome 18

Organism-specific databases

MGIiMGI:98036. Rpl27.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13613660S ribosomal protein L27PRO_0000126078Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei27 – 271N6-acetyllysineCombined sources
Modified residuei93 – 931N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP61358.
PaxDbiP61358.
PeptideAtlasiP61358.
PRIDEiP61358.
TopDownProteomicsiP61358.

PTM databases

iPTMnetiP61358.
PhosphoSiteiP61358.
SwissPalmiP61358.

Expressioni

Gene expression databases

BgeeiP61358.
CleanExiMM_RPL27.
ExpressionAtlasiP61358. baseline and differential.
GenevisibleiP61358. MM.

Interactioni

Protein-protein interaction databases

BioGridi202974. 6 interactions.
IntActiP61358. 1 interaction.
MINTiMINT-1863099.
STRINGi10090.ENSMUSP00000095287.

Structurei

3D structure databases

ProteinModelPortaliP61358.
SMRiP61358. Positions 2-136.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 4036KOWAdd
BLAST

Sequence similaritiesi

Belongs to the ribosomal protein L27e family.Curated
Contains 1 KOW domain.Curated

Phylogenomic databases

eggNOGiKOG3418. Eukaryota.
COG2163. LUCA.
HOGENOMiHOG000210138.
HOVERGENiHBG050005.
InParanoidiP61358.
KOiK02901.
OMAiKIYKPGK.
OrthoDBiEOG7J181Z.
PhylomeDBiP61358.
TreeFamiTF314648.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
InterProiIPR005824. KOW.
IPR014722. Rib_L2_dom2.
IPR001141. Ribosomal_L27e.
IPR018262. Ribosomal_L27e_CS.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERiPTHR10497. PTHR10497. 1 hit.
PfamiPF00467. KOW. 1 hit.
PF01777. Ribosomal_L27e. 1 hit.
[Graphical view]
ProDomiPD009396. Ribosomal_L27e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00739. KOW. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.
PROSITEiPS01107. RIBOSOMAL_L27E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P61358-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKFMKPGKV VLVLAGRYSG RKAVIVKNID DGTSDRPYSH ALVAGIDRYP
60 70 80 90 100
RKVTAAMGKK KIAKRSKIKS FVKVYNYNHL MPTRYSVDIP LDKTVVNKDV
110 120 130
FRDPALKRKA RREAKVKFEE RYKTGKNKWF FQKLRF
Length:136
Mass (Da):15,798
Last modified:January 23, 2007 - v2
Checksum:i73F4151495029A32
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF214527 mRNA. Translation: AAF25951.1.
AK002945 mRNA. Translation: BAB22471.1.
AK008120 mRNA. Translation: BAB25475.1.
AK088211 mRNA. Translation: BAC40213.1.
AK010627 mRNA. Translation: BAB27073.1.
AK012566 mRNA. Translation: BAB28321.1.
BC024366 mRNA. Translation: AAH24366.1.
BC082284 mRNA. Translation: AAH82284.1.
CCDSiCCDS25470.1.
RefSeqiNP_035419.1. NM_011289.3.
UniGeneiMm.340658.
Mm.439813.

Genome annotation databases

EnsembliENSMUST00000077856; ENSMUSP00000090305; ENSMUSG00000063316.
ENSMUST00000097682; ENSMUSP00000095287; ENSMUSG00000073640.
ENSMUST00000107249; ENSMUSP00000102870; ENSMUSG00000063316.
GeneIDi19942.
KEGGimmu:19942.
UCSCiuc007low.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF214527 mRNA. Translation: AAF25951.1.
AK002945 mRNA. Translation: BAB22471.1.
AK008120 mRNA. Translation: BAB25475.1.
AK088211 mRNA. Translation: BAC40213.1.
AK010627 mRNA. Translation: BAB27073.1.
AK012566 mRNA. Translation: BAB28321.1.
BC024366 mRNA. Translation: AAH24366.1.
BC082284 mRNA. Translation: AAH82284.1.
CCDSiCCDS25470.1.
RefSeqiNP_035419.1. NM_011289.3.
UniGeneiMm.340658.
Mm.439813.

3D structure databases

ProteinModelPortaliP61358.
SMRiP61358. Positions 2-136.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202974. 6 interactions.
IntActiP61358. 1 interaction.
MINTiMINT-1863099.
STRINGi10090.ENSMUSP00000095287.

PTM databases

iPTMnetiP61358.
PhosphoSiteiP61358.
SwissPalmiP61358.

Proteomic databases

EPDiP61358.
PaxDbiP61358.
PeptideAtlasiP61358.
PRIDEiP61358.
TopDownProteomicsiP61358.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000077856; ENSMUSP00000090305; ENSMUSG00000063316.
ENSMUST00000097682; ENSMUSP00000095287; ENSMUSG00000073640.
ENSMUST00000107249; ENSMUSP00000102870; ENSMUSG00000063316.
GeneIDi19942.
KEGGimmu:19942.
UCSCiuc007low.2. mouse.

Organism-specific databases

CTDi6155.
MGIiMGI:98036. Rpl27.

Phylogenomic databases

eggNOGiKOG3418. Eukaryota.
COG2163. LUCA.
HOGENOMiHOG000210138.
HOVERGENiHBG050005.
InParanoidiP61358.
KOiK02901.
OMAiKIYKPGK.
OrthoDBiEOG7J181Z.
PhylomeDBiP61358.
TreeFamiTF314648.

Enzyme and pathway databases

ReactomeiR-MMU-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-MMU-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-MMU-6791226. Major pathway of rRNA processing in the nucleolus.
R-MMU-72689. Formation of a pool of free 40S subunits.
R-MMU-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-MMU-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-MMU-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

ChiTaRSiRpl27. mouse.
PROiP61358.
SOURCEiSearch...

Gene expression databases

BgeeiP61358.
CleanExiMM_RPL27.
ExpressionAtlasiP61358. baseline and differential.
GenevisibleiP61358. MM.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
InterProiIPR005824. KOW.
IPR014722. Rib_L2_dom2.
IPR001141. Ribosomal_L27e.
IPR018262. Ribosomal_L27e_CS.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERiPTHR10497. PTHR10497. 1 hit.
PfamiPF00467. KOW. 1 hit.
PF01777. Ribosomal_L27e. 1 hit.
[Graphical view]
ProDomiPD009396. Ribosomal_L27e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00739. KOW. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.
PROSITEiPS01107. RIBOSOMAL_L27E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of cDNA encoding mouse ribosomal protein L27."
    Jin C.G., Chen W.F., Li Y.
    Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
  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 and NOD.
    Tissue: Brain, Small intestine and Thymus.
  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: 129 and FVB/N.
    Tissue: Colon and Mammary gland.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  5. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiRL27_MOUSE
AccessioniPrimary (citable) accession number: P61358
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 119 of the entry and version 2 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

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 one 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.