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P27659

- RL3_MOUSE

UniProt

P27659 - RL3_MOUSE

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Protein

60S ribosomal protein L3

Gene

Rpl3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

The L3 protein is a component of the large subunit of cytoplasmic ribosomes.

GO - Molecular functioni

  1. poly(A) RNA binding Source: Ensembl
  2. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. cellular response to interleukin-4 Source: MGI
  2. translation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_196445. SRP-dependent cotranslational protein targeting to membrane.
REACT_198524. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_198528. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_231519. Eukaryotic Translation Termination.
REACT_249044. Formation of a pool of free 40S subunits.
REACT_253640. Peptide chain elongation.
REACT_259469. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_262078. GTP hydrolysis and joining of the 60S ribosomal subunit.

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L3
Alternative name(s):
J1 protein
Gene namesi
Name:Rpl3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:1351605. Rpl3.

Subcellular locationi

Nucleusnucleolus By similarity. Cytoplasm

GO - Cellular componenti

  1. cytosolic large ribosomal subunit Source: Ensembl
  2. extracellular vesicular exosome Source: Ensembl
  3. nucleolus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 40340260S ribosomal protein L3PRO_0000077229Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei13 – 131PhosphoserineBy similarity
Modified residuei136 – 1361N6-acetyllysine1 Publication
Modified residuei286 – 2861N6-acetyllysine1 Publication
Modified residuei294 – 2941N6-acetyllysineBy similarity
Modified residuei304 – 3041PhosphoserineBy similarity
Modified residuei366 – 3661N6-acetyllysineBy similarity
Modified residuei373 – 3731N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP27659.
PaxDbiP27659.
PRIDEiP27659.

PTM databases

PhosphoSiteiP27659.

Expressioni

Gene expression databases

BgeeiP27659.
CleanExiMM_RPL3.
ExpressionAtlasiP27659. baseline and differential.
GenevestigatoriP27659.

Interactioni

Subunit structurei

Interacts with METTL18.By similarity

Protein-protein interaction databases

BioGridi205174. 10 interactions.
IntActiP27659. 5 interactions.
MINTiMINT-4120935.

Structurei

3D structure databases

ProteinModelPortaliP27659.
SMRiP27659. Positions 2-398.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L3P family.Curated

Phylogenomic databases

eggNOGiCOG0087.
GeneTreeiENSGT00390000017606.
HOGENOMiHOG000107319.
HOVERGENiHBG001864.
InParanoidiP27659.
KOiK02925.
OMAiFQTFEEK.
OrthoDBiEOG7HF1JK.
TreeFamiTF300555.

Family and domain databases

InterProiIPR000597. Ribosomal_L3.
IPR019926. Ribosomal_L3_CS.
IPR009000. Transl_B-barrel.
[Graphical view]
PfamiPF00297. Ribosomal_L3. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
PROSITEiPS00474. RIBOSOMAL_L3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P27659-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSHRKFSAPR HGSLGFLPRK RSSRHRGKVK SFPKDDASKP VHLTAFLGYK
60 70 80 90 100
AGMTHIVREV DRPGSKVNKK EVVEAVTIVE TPPMVVVGIV GYVETPRGLR
110 120 130 140 150
TFKTVFAEHI SDECKRRFYK NWHKSKKKAF TKYCKKWQDD TGKKQLEKDF
160 170 180 190 200
NSMKKYCQVI RIIAHTQMRL LPLRQKKAHL MEIQVNGGTV AEKLDWARER
210 220 230 240 250
LEQQVPVNQV FGQDEMIDVI GVTKGKGYKG VTSRWHTKKL PRKTHRGLRK
260 270 280 290 300
VACIGAWHPA RVAFSVARAG QKGYHHRTEI NKKIYKIGQG YLIKDGKLIK
310 320 330 340 350
NNASTDYDLS DKSINPLGGF VHYGEVTNDF IMLKGCVVGT KKRVLTLRKS
360 370 380 390 400
LLVQTKRRAL EKIDLKFIDT TSKFGHGRFQ TMEEKKAFMG PLKKDRIAKE

EGA
Length:403
Mass (Da):46,110
Last modified:July 27, 2011 - v3
Checksum:i87AA82D9B2A8481E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti265 – 2651S → T in CAA68370. (PubMed:2628163)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00225 mRNA. Translation: CAA68370.1.
U89417 mRNA. Translation: AAC36524.1.
AK088993 mRNA. Translation: BAC40691.1.
AK144518 mRNA. Translation: BAE25922.1.
AK144816 mRNA. Translation: BAE26078.1.
AK146502 mRNA. Translation: BAE27217.1.
AK149494 mRNA. Translation: BAE28917.1.
AK151596 mRNA. Translation: BAE30536.1.
AK166433 mRNA. Translation: BAE38773.1.
AK166825 mRNA. Translation: BAE39049.1.
AK167787 mRNA. Translation: BAE39818.1.
AK167947 mRNA. Translation: BAE39950.1.
AK168040 mRNA. Translation: BAE40022.1.
AK168059 mRNA. Translation: BAE40037.1.
AK168126 mRNA. Translation: BAE40095.1.
AK168128 mRNA. Translation: BAE40097.1.
AK168224 mRNA. Translation: BAE40178.1.
AK168744 mRNA. Translation: BAE40585.1.
AK169060 mRNA. Translation: BAE40848.1.
AK169235 mRNA. Translation: BAE41003.1.
AK169321 mRNA. Translation: BAE41075.1.
AK170819 mRNA. Translation: BAE42051.1.
CH466550 Genomic DNA. Translation: EDL04616.1.
BC009655 mRNA. Translation: AAH09655.1.
BC083134 mRNA. Translation: AAH83134.1.
BC094059 mRNA. Translation: AAH94059.1.
BC158039 mRNA. Translation: AAI58040.1.
CCDSiCCDS37144.1.
RefSeqiNP_038790.2. NM_013762.2.
UniGeneiMm.290771.
Mm.321484.
Mm.396243.
Mm.474802.

Genome annotation databases

EnsembliENSMUST00000081650; ENSMUSP00000080354; ENSMUSG00000060036.
GeneIDi27367.
KEGGimmu:27367.
UCSCiuc007wvb.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00225 mRNA. Translation: CAA68370.1 .
U89417 mRNA. Translation: AAC36524.1 .
AK088993 mRNA. Translation: BAC40691.1 .
AK144518 mRNA. Translation: BAE25922.1 .
AK144816 mRNA. Translation: BAE26078.1 .
AK146502 mRNA. Translation: BAE27217.1 .
AK149494 mRNA. Translation: BAE28917.1 .
AK151596 mRNA. Translation: BAE30536.1 .
AK166433 mRNA. Translation: BAE38773.1 .
AK166825 mRNA. Translation: BAE39049.1 .
AK167787 mRNA. Translation: BAE39818.1 .
AK167947 mRNA. Translation: BAE39950.1 .
AK168040 mRNA. Translation: BAE40022.1 .
AK168059 mRNA. Translation: BAE40037.1 .
AK168126 mRNA. Translation: BAE40095.1 .
AK168128 mRNA. Translation: BAE40097.1 .
AK168224 mRNA. Translation: BAE40178.1 .
AK168744 mRNA. Translation: BAE40585.1 .
AK169060 mRNA. Translation: BAE40848.1 .
AK169235 mRNA. Translation: BAE41003.1 .
AK169321 mRNA. Translation: BAE41075.1 .
AK170819 mRNA. Translation: BAE42051.1 .
CH466550 Genomic DNA. Translation: EDL04616.1 .
BC009655 mRNA. Translation: AAH09655.1 .
BC083134 mRNA. Translation: AAH83134.1 .
BC094059 mRNA. Translation: AAH94059.1 .
BC158039 mRNA. Translation: AAI58040.1 .
CCDSi CCDS37144.1.
RefSeqi NP_038790.2. NM_013762.2.
UniGenei Mm.290771.
Mm.321484.
Mm.396243.
Mm.474802.

3D structure databases

ProteinModelPortali P27659.
SMRi P27659. Positions 2-398.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 205174. 10 interactions.
IntActi P27659. 5 interactions.
MINTi MINT-4120935.

PTM databases

PhosphoSitei P27659.

Proteomic databases

MaxQBi P27659.
PaxDbi P27659.
PRIDEi P27659.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000081650 ; ENSMUSP00000080354 ; ENSMUSG00000060036 .
GeneIDi 27367.
KEGGi mmu:27367.
UCSCi uc007wvb.2. mouse.

Organism-specific databases

CTDi 6122.
MGIi MGI:1351605. Rpl3.

Phylogenomic databases

eggNOGi COG0087.
GeneTreei ENSGT00390000017606.
HOGENOMi HOG000107319.
HOVERGENi HBG001864.
InParanoidi P27659.
KOi K02925.
OMAi FQTFEEK.
OrthoDBi EOG7HF1JK.
TreeFami TF300555.

Enzyme and pathway databases

Reactomei REACT_196445. SRP-dependent cotranslational protein targeting to membrane.
REACT_198524. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_198528. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_231519. Eukaryotic Translation Termination.
REACT_249044. Formation of a pool of free 40S subunits.
REACT_253640. Peptide chain elongation.
REACT_259469. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_262078. GTP hydrolysis and joining of the 60S ribosomal subunit.

Miscellaneous databases

NextBioi 305258.
PROi P27659.
SOURCEi Search...

Gene expression databases

Bgeei P27659.
CleanExi MM_RPL3.
ExpressionAtlasi P27659. baseline and differential.
Genevestigatori P27659.

Family and domain databases

InterProi IPR000597. Ribosomal_L3.
IPR019926. Ribosomal_L3_CS.
IPR009000. Transl_B-barrel.
[Graphical view ]
Pfami PF00297. Ribosomal_L3. 1 hit.
[Graphical view ]
SUPFAMi SSF50447. SSF50447. 1 hit.
PROSITEi PS00474. RIBOSOMAL_L3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Retrovirus activation in embryonal carcinoma cells by cellular promoters."
    Peckham I., Sobel S., Comer J., Jaenisch R., Barklis E.
    Genes Dev. 3:2062-2071(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cellular transcripts encoded at a locus which permits retrovirus expression in mouse embryonic cells."
    Petersen R., Sobel S., Wang C.T., Jaenisch R., Barklis E.
    Gene 101:177-183(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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: BALB/c, C57BL/6J, DBA/2 and NOD.
    Tissue: Bone marrow, Brain cortex, Heart, Kidney, Liver, Lung, Mammary gland and Thymus.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Limb and Mammary tumor.
  6. "Expressed genes in interleukin-4 treated B cells identified by cDNA representational difference analysis."
    Chu C.C., Paul W.E.
    Mol. Immunol. 35:487-502(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 183-299.
    Strain: BALB/c.
    Tissue: Spleen.
  7. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-136; LYS-286 AND LYS-373, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiRL3_MOUSE
AccessioniPrimary (citable) accession number: P27659
Secondary accession number(s): O89071, Q91VJ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 112 of the entry and version 3 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