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Protein

60S ribosomal protein L32

Gene

Rpl32

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

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

GO - Biological processi

  1. translation Source: MGI
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 L32
Gene namesi
Name:Rpl32
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:98038. Rpl32.

Subcellular locationi

GO - Cellular componenti

  1. cytosolic large ribosomal subunit Source: MGI
  2. membrane Source: Ensembl
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 13513460S ribosomal protein L32PRO_0000131115Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei50 – 501N6-succinyllysine1 Publication

Proteomic databases

MaxQBiP62911.
PaxDbiP62911.
PRIDEiP62911.

PTM databases

PhosphoSiteiP62911.

Expressioni

Gene expression databases

BgeeiP62911.
CleanExiMM_RPL32.
GenevestigatoriP62911.

Interactioni

Protein-protein interaction databases

BioGridi202982. 10 interactions.
IntActiP62911. 2 interactions.
MINTiMINT-1854367.
STRINGi10090.ENSMUSP00000080523.

Structurei

3D structure databases

ProteinModelPortaliP62911.
SMRiP62911. Positions 2-129.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L32e family.Curated

Phylogenomic databases

eggNOGiCOG1717.
GeneTreeiENSGT00390000014729.
HOGENOMiHOG000231288.
HOVERGENiHBG056057.
InParanoidiP62911.
KOiK02912.
OMAiQSDRYDK.
OrthoDBiEOG779P0S.
PhylomeDBiP62911.
TreeFamiTF314947.

Family and domain databases

InterProiIPR001515. Ribosomal_L32e.
IPR018263. Ribosomal_L32e_CS.
[Graphical view]
PfamiPF01655. Ribosomal_L32e. 1 hit.
[Graphical view]
ProDomiPD003823. Ribosomal_L32e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF52042. SSF52042. 1 hit.
PROSITEiPS00580. RIBOSOMAL_L32E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P62911-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAALRPLVKP KIVKKRTKKF IRHQSDRYVK IKRNWRKPRG IDNRVRRRFK
60 70 80 90 100
GQILMPNIGY GSNKKTKHML PSGFRKFLVH NVKELEVLLM CNKSYCAEIA
110 120 130
HNVSSKNRKA IVERAAQLAI RVTNPNARLR SEENE
Length:135
Mass (Da):15,860
Last modified:January 23, 2007 - v2
Checksum:iEDEE48446483966E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02060 Genomic DNA. Translation: AAC28897.1.
AK002353 mRNA. Translation: BAB22032.1.
AK011017 mRNA. Translation: BAB27335.1.
AK012525 mRNA. Translation: BAB28296.1.
AK028204 mRNA. Translation: BAC25812.1.
AK146768 mRNA. Translation: BAE27419.1.
AK148453 mRNA. Translation: BAE28563.1.
AK150705 mRNA. Translation: BAE29784.1.
AK168282 mRNA. Translation: BAE40228.1.
BC046339 mRNA. Translation: AAH46339.1.
CCDSiCCDS20443.1.
PIRiA02829. R5MS32.
RefSeqiNP_742083.1. NM_172086.2.
XP_006544660.1. XM_006544597.1.
UniGeneiMm.104368.

Genome annotation databases

EnsembliENSMUST00000081840; ENSMUSP00000080523; ENSMUSG00000057841.
GeneIDi19951.
652989.
KEGGimmu:102642959.
mmu:19951.
UCSCiuc009djc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02060 Genomic DNA. Translation: AAC28897.1.
AK002353 mRNA. Translation: BAB22032.1.
AK011017 mRNA. Translation: BAB27335.1.
AK012525 mRNA. Translation: BAB28296.1.
AK028204 mRNA. Translation: BAC25812.1.
AK146768 mRNA. Translation: BAE27419.1.
AK148453 mRNA. Translation: BAE28563.1.
AK150705 mRNA. Translation: BAE29784.1.
AK168282 mRNA. Translation: BAE40228.1.
BC046339 mRNA. Translation: AAH46339.1.
CCDSiCCDS20443.1.
PIRiA02829. R5MS32.
RefSeqiNP_742083.1. NM_172086.2.
XP_006544660.1. XM_006544597.1.
UniGeneiMm.104368.

3D structure databases

ProteinModelPortaliP62911.
SMRiP62911. Positions 2-129.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202982. 10 interactions.
IntActiP62911. 2 interactions.
MINTiMINT-1854367.
STRINGi10090.ENSMUSP00000080523.

PTM databases

PhosphoSiteiP62911.

Proteomic databases

MaxQBiP62911.
PaxDbiP62911.
PRIDEiP62911.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000081840; ENSMUSP00000080523; ENSMUSG00000057841.
GeneIDi19951.
652989.
KEGGimmu:102642959.
mmu:19951.
UCSCiuc009djc.1. mouse.

Organism-specific databases

CTDi6161.
MGIiMGI:98038. Rpl32.

Phylogenomic databases

eggNOGiCOG1717.
GeneTreeiENSGT00390000014729.
HOGENOMiHOG000231288.
HOVERGENiHBG056057.
InParanoidiP62911.
KOiK02912.
OMAiQSDRYDK.
OrthoDBiEOG779P0S.
PhylomeDBiP62911.
TreeFamiTF314947.

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.

Miscellaneous databases

ChiTaRSiRpl32. mouse.
NextBioi23931.
PROiP62911.
SOURCEiSearch...

Gene expression databases

BgeeiP62911.
CleanExiMM_RPL32.
GenevestigatoriP62911.

Family and domain databases

InterProiIPR001515. Ribosomal_L32e.
IPR018263. Ribosomal_L32e_CS.
[Graphical view]
PfamiPF01655. Ribosomal_L32e. 1 hit.
[Graphical view]
ProDomiPD003823. Ribosomal_L32e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF52042. SSF52042. 1 hit.
PROSITEiPS00580. RIBOSOMAL_L32E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The gene family encoding the mouse ribosomal protein L32 contains a uniquely expressed intron-containing gene and an unmutated processed gene."
    Dudov K.P., Perry R.P.
    Cell 37:457-468(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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: BALB/c and C57BL/6J.
    Tissue: Bone marrow, Kidney, Liver, Pancreas and Stomach.
  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: FVB/N.
    Tissue: Colon.
  4. "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-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiRL32_MOUSE
AccessioniPrimary (citable) accession number: P62911
Secondary accession number(s): P02433, Q3UFJ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 92 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

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.