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Protein

60S ribosomal protein L31

Gene

Rpl31

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-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 L31
Gene namesi
Name:Rpl31
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:2149632. Rpl31.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12512560S ribosomal protein L31PRO_0000153764Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei15 – 151PhosphoserineCombined sources
Modified residuei55 – 551N6-succinyllysineCombined sources
Modified residuei70 – 701N6-succinyllysineCombined sources
Modified residuei75 – 751N6-acetyllysine; alternateBy similarity
Modified residuei75 – 751N6-succinyllysine; alternateCombined sources
Modified residuei98 – 981PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP62900.
PaxDbiP62900.
PRIDEiP62900.

PTM databases

iPTMnetiP62900.
PhosphoSiteiP62900.

Expressioni

Gene expression databases

BgeeiP62900.
CleanExiMM_RPL31.
ExpressionAtlasiP62900. baseline and differential.
GenevisibleiP62900. MM.

Interactioni

Protein-protein interaction databases

BioGridi227776. 3 interactions.
IntActiP62900. 6 interactions.
MINTiMINT-1857573.
STRINGi10090.ENSMUSP00000083722.

Structurei

3D structure databases

ProteinModelPortaliP62900.
SMRiP62900. Positions 22-102.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L31e family.Curated

Phylogenomic databases

eggNOGiKOG0893. Eukaryota.
COG2097. LUCA.
HOGENOMiHOG000216660.
HOVERGENiHBG001549.
InParanoidiP62900.
KOiK02910.
OrthoDBiEOG7V768M.
PhylomeDBiP62900.
TreeFamiTF314858.

Family and domain databases

Gene3Di3.10.440.10. 1 hit.
InterProiIPR000054. Ribosomal_L31e.
IPR020052. Ribosomal_L31e_CS.
IPR023621. Ribosomal_L31e_dom.
[Graphical view]
PANTHERiPTHR10956. PTHR10956. 1 hit.
PfamiPF01198. Ribosomal_L31e. 1 hit.
[Graphical view]
ProDomiPD006030. Ribosomal_L31e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM01380. Ribosomal_L31e. 1 hit.
[Graphical view]
SUPFAMiSSF54575. SSF54575. 1 hit.
PROSITEiPS01144. RIBOSOMAL_L31E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P62900-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPAKKGGEK KKGRSAINEV VTREYTINIH KRIHGVGFKK RAPRALKEIR
60 70 80 90 100
KFAMKEMGTP DVRIDTRLNK AVWAKGIRNV PYRIRVRLSR KRNEDEDSPN
110 120
KLYTLVTYVP VTTFKNLQTV NVDEN
Length:125
Mass (Da):14,463
Last modified:August 31, 2004 - v1
Checksum:iBA9DBE79B9E1C071
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF362574 mRNA. Translation: AAK70404.1.
AK011236 mRNA. Translation: BAB27484.1.
AK014295 mRNA. Translation: BAB29251.1.
AK020627 mRNA. Translation: BAB32156.1.
BC008223 mRNA. No translation available.
BC050113 mRNA. Translation: AAH50113.1.
BC055720 mRNA. Translation: AAH55720.1.
CCDSiCCDS14904.1.
RefSeqiNP_001239147.1. NM_001252218.1.
NP_001239148.1. NM_001252219.1.
NP_444487.1. NM_053257.3.
UniGeneiMm.379302.
Mm.443000.

Genome annotation databases

EnsembliENSMUST00000086535; ENSMUSP00000083722; ENSMUSG00000073702.
ENSMUST00000178079; ENSMUSP00000136354; ENSMUSG00000073702.
ENSMUST00000179954; ENSMUSP00000137631; ENSMUSG00000073702.
GeneIDi114641.
KEGGimmu:114641.
UCSCiuc007ate.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF362574 mRNA. Translation: AAK70404.1.
AK011236 mRNA. Translation: BAB27484.1.
AK014295 mRNA. Translation: BAB29251.1.
AK020627 mRNA. Translation: BAB32156.1.
BC008223 mRNA. No translation available.
BC050113 mRNA. Translation: AAH50113.1.
BC055720 mRNA. Translation: AAH55720.1.
CCDSiCCDS14904.1.
RefSeqiNP_001239147.1. NM_001252218.1.
NP_001239148.1. NM_001252219.1.
NP_444487.1. NM_053257.3.
UniGeneiMm.379302.
Mm.443000.

3D structure databases

ProteinModelPortaliP62900.
SMRiP62900. Positions 22-102.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi227776. 3 interactions.
IntActiP62900. 6 interactions.
MINTiMINT-1857573.
STRINGi10090.ENSMUSP00000083722.

PTM databases

iPTMnetiP62900.
PhosphoSiteiP62900.

Proteomic databases

EPDiP62900.
PaxDbiP62900.
PRIDEiP62900.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000086535; ENSMUSP00000083722; ENSMUSG00000073702.
ENSMUST00000178079; ENSMUSP00000136354; ENSMUSG00000073702.
ENSMUST00000179954; ENSMUSP00000137631; ENSMUSG00000073702.
GeneIDi114641.
KEGGimmu:114641.
UCSCiuc007ate.2. mouse.

Organism-specific databases

CTDi6160.
MGIiMGI:2149632. Rpl31.

Phylogenomic databases

eggNOGiKOG0893. Eukaryota.
COG2097. LUCA.
HOGENOMiHOG000216660.
HOVERGENiHBG001549.
InParanoidiP62900.
KOiK02910.
OrthoDBiEOG7V768M.
PhylomeDBiP62900.
TreeFamiTF314858.

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-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

NextBioi368590.
PROiP62900.
SOURCEiSearch...

Gene expression databases

BgeeiP62900.
CleanExiMM_RPL31.
ExpressionAtlasiP62900. baseline and differential.
GenevisibleiP62900. MM.

Family and domain databases

Gene3Di3.10.440.10. 1 hit.
InterProiIPR000054. Ribosomal_L31e.
IPR020052. Ribosomal_L31e_CS.
IPR023621. Ribosomal_L31e_dom.
[Graphical view]
PANTHERiPTHR10956. PTHR10956. 1 hit.
PfamiPF01198. Ribosomal_L31e. 1 hit.
[Graphical view]
ProDomiPD006030. Ribosomal_L31e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM01380. Ribosomal_L31e. 1 hit.
[Graphical view]
SUPFAMiSSF54575. SSF54575. 1 hit.
PROSITEiPS01144. RIBOSOMAL_L31E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identifying different gene expression using subtraction suppression hybridization."
    Zhao S., Zhang Y., Yu Y., Yang T., Ge S., Geng Y., Cui C.
    Submitted (MAR-2001) 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.
    Tissue: Urinary bladder.
  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/6J.
    Tissue: Brain and Pancreas.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-55; LYS-70 AND LYS-75, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.

Entry informationi

Entry nameiRL31_MOUSE
AccessioniPrimary (citable) accession number: P62900
Secondary accession number(s): P12947
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: May 11, 2016
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

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.