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Protein

60S ribosomal protein L32

Gene

RPL32

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

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

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. gene expression Source: Reactome
  3. mRNA metabolic process Source: Reactome
  4. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  5. RNA metabolic process Source: Reactome
  6. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  7. translation Source: UniProtKB
  8. translational elongation Source: Reactome
  9. translational initiation Source: Reactome
  10. translational termination Source: Reactome
  11. viral life cycle Source: Reactome
  12. viral process Source: Reactome
  13. viral transcription Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_9491. Viral mRNA Translation.

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L32
Gene namesi
Name:RPL32
ORF Names:PP9932
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:10336. RPL32.

Subcellular locationi

GO - Cellular componenti

  1. centrosome Source: HPA
  2. cytoplasm Source: HPA
  3. cytosol Source: Reactome
  4. cytosolic large ribosomal subunit Source: UniProtKB
  5. membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34719.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 13513460S ribosomal protein L32PRO_0000131113Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei50 – 501N6-succinyllysineBy similarity

Proteomic databases

MaxQBiP62910.
PaxDbiP62910.
PRIDEiP62910.

PTM databases

PhosphoSiteiP62910.

Expressioni

Gene expression databases

BgeeiP62910.
CleanExiHS_RPL32.
ExpressionAtlasiP62910. baseline.
GenevestigatoriP62910.

Organism-specific databases

HPAiHPA047501.
HPA051994.

Interactioni

Protein-protein interaction databases

BioGridi112080. 58 interactions.
IntActiP62910. 6 interactions.
MINTiMINT-1149317.
STRINGi9606.ENSP00000380156.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00e1-135[»]
ProteinModelPortaliP62910.
SMRiP62910. Positions 2-129.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L32e family.Curated

Phylogenomic databases

eggNOGiCOG1717.
GeneTreeiENSGT00390000014729.
HOGENOMiHOG000231288.
HOVERGENiHBG056057.
InParanoidiP62910.
KOiK02912.
OrthoDBiEOG779P0S.
PhylomeDBiP62910.
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.

P62910-1 [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
X03342 mRNA. Translation: CAA27048.1.
AB061831 Genomic DNA. Translation: BAB79469.1.
AF370435 mRNA. Translation: AAQ15271.1.
AK311909 mRNA. Translation: BAG34850.1.
CH471055 Genomic DNA. Translation: EAW64144.1.
BC011514 mRNA. Translation: AAH11514.1.
BC070209 mRNA. Translation: AAH70209.1.
CCDSiCCDS2614.1.
PIRiS11393. R5HU32.
RefSeqiNP_000985.1. NM_000994.3.
NP_001007074.1. NM_001007073.1.
NP_001007075.1. NM_001007074.1.
UniGeneiHs.265174.

Genome annotation databases

EnsembliENST00000396953; ENSP00000380156; ENSG00000144713.
ENST00000396957; ENSP00000380158; ENSG00000144713.
ENST00000429711; ENSP00000416429; ENSG00000144713.
ENST00000435983; ENSP00000388674; ENSG00000144713.
GeneIDi6161.
KEGGihsa:6161.
UCSCiuc003bxl.3. human.

Polymorphism databases

DMDMi51702809.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03342 mRNA. Translation: CAA27048.1.
AB061831 Genomic DNA. Translation: BAB79469.1.
AF370435 mRNA. Translation: AAQ15271.1.
AK311909 mRNA. Translation: BAG34850.1.
CH471055 Genomic DNA. Translation: EAW64144.1.
BC011514 mRNA. Translation: AAH11514.1.
BC070209 mRNA. Translation: AAH70209.1.
CCDSiCCDS2614.1.
PIRiS11393. R5HU32.
RefSeqiNP_000985.1. NM_000994.3.
NP_001007074.1. NM_001007073.1.
NP_001007075.1. NM_001007074.1.
UniGeneiHs.265174.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00e1-135[»]
ProteinModelPortaliP62910.
SMRiP62910. Positions 2-129.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112080. 58 interactions.
IntActiP62910. 6 interactions.
MINTiMINT-1149317.
STRINGi9606.ENSP00000380156.

PTM databases

PhosphoSiteiP62910.

Polymorphism databases

DMDMi51702809.

Proteomic databases

MaxQBiP62910.
PaxDbiP62910.
PRIDEiP62910.

Protocols and materials databases

DNASUi6161.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000396953; ENSP00000380156; ENSG00000144713.
ENST00000396957; ENSP00000380158; ENSG00000144713.
ENST00000429711; ENSP00000416429; ENSG00000144713.
ENST00000435983; ENSP00000388674; ENSG00000144713.
GeneIDi6161.
KEGGihsa:6161.
UCSCiuc003bxl.3. human.

Organism-specific databases

CTDi6161.
GeneCardsiGC03M012877.
HGNCiHGNC:10336. RPL32.
HPAiHPA047501.
HPA051994.
neXtProtiNX_P62910.
PharmGKBiPA34719.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1717.
GeneTreeiENSGT00390000014729.
HOGENOMiHOG000231288.
HOVERGENiHBG056057.
InParanoidiP62910.
KOiK02912.
OrthoDBiEOG779P0S.
PhylomeDBiP62910.
TreeFamiTF314947.

Enzyme and pathway databases

ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_9491. Viral mRNA Translation.

Miscellaneous databases

ChiTaRSiRPL32. human.
GeneWikiiRPL32.
GenomeRNAii6161.
NextBioi23931.
PROiP62910.

Gene expression databases

BgeeiP62910.
CleanExiHS_RPL32.
ExpressionAtlasiP62910. baseline.
GenevestigatoriP62910.

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. "A processed pseudogene in an intron of the HLA-DP beta 1 chain gene is a member of the ribosomal protein L32 gene family."
    Young J.A.T., Trowsdale J.
    Nucleic Acids Res. 13:8883-8891(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The human ribosomal protein genes: sequencing and comparative analysis of 73 genes."
    Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S., Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.
    Genome Res. 12:379-390(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
    Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
    , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
    Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Thymus.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Placenta.
  7. Bienvenut W.V., Vousden K.H., Lukashchuk N.
    Submitted (MAR-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-11; 84-93 AND 115-121, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Lung carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRL32_HUMAN
AccessioniPrimary (citable) accession number: P62910
Secondary accession number(s): B2R4Q3, P02433
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: February 4, 2015
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. 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.