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P62911

- RL32_MOUSE

UniProt

P62911 - RL32_MOUSE

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Protein

60S ribosomal protein L32

Gene

Rpl32

Organism
Mus musculus (Mouse)
Status
Reviewed - 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
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.
OMAiTRHMLPT.
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 .
CCDSi CCDS20443.1.
PIRi A02829. R5MS32.
RefSeqi NP_742083.1. NM_172086.2.
XP_006544660.1. XM_006544597.1.
UniGenei Mm.104368.

3D structure databases

ProteinModelPortali P62911.
SMRi P62911. Positions 2-129.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202982. 10 interactions.
IntActi P62911. 2 interactions.
MINTi MINT-1854367.
STRINGi 10090.ENSMUSP00000080523.

PTM databases

PhosphoSitei P62911.

Proteomic databases

MaxQBi P62911.
PaxDbi P62911.
PRIDEi P62911.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000081840 ; ENSMUSP00000080523 ; ENSMUSG00000057841 .
GeneIDi 19951.
652989.
KEGGi mmu:102642959.
mmu:19951.
UCSCi uc009djc.1. mouse.

Organism-specific databases

CTDi 6161.
MGIi MGI:98038. Rpl32.

Phylogenomic databases

eggNOGi COG1717.
GeneTreei ENSGT00390000014729.
HOGENOMi HOG000231288.
HOVERGENi HBG056057.
InParanoidi P62911.
KOi K02912.
OMAi TRHMLPT.
OrthoDBi EOG779P0S.
PhylomeDBi P62911.
TreeFami TF314947.

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

ChiTaRSi Rpl32. mouse.
NextBioi 23931.
PROi P62911.
SOURCEi Search...

Gene expression databases

Bgeei P62911.
CleanExi MM_RPL32.
Genevestigatori P62911.

Family and domain databases

InterProi IPR001515. Ribosomal_L32e.
IPR018263. Ribosomal_L32e_CS.
[Graphical view ]
Pfami PF01655. Ribosomal_L32e. 1 hit.
[Graphical view ]
ProDomi PD003823. Ribosomal_L32e. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF52042. SSF52042. 1 hit.
PROSITEi PS00580. RIBOSOMAL_L32E. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: November 26, 2014
This is version 91 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