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Protein

60S ribosomal protein L34

Gene

RPL34

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

Functioni

GO - Molecular functioni

  • RNA binding Source: ProtInc
  • structural constituent of ribosome Source: UniProtKB

GO - Biological processi

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 L34
Gene namesi
Name:RPL34
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:10340. RPL34.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • cytosolic large ribosomal subunit Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • nucleolus Source: HPA
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34723.

Polymorphism and mutation databases

BioMutaiRPL34.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 11711660S ribosomal protein L34PRO_0000131831Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei12 – 121Phosphoserine2 Publications
Modified residuei36 – 361N6-acetyllysine1 Publication
Modified residuei43 – 431N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP49207.
PaxDbiP49207.
PeptideAtlasiP49207.
PRIDEiP49207.

PTM databases

PhosphoSiteiP49207.

Expressioni

Gene expression databases

BgeeiP49207.
CleanExiHS_RPL34.
ExpressionAtlasiP49207. baseline and differential.
GenevestigatoriP49207.

Organism-specific databases

HPAiHPA035139.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CNBPP626331EBI-1051893,EBI-1047529
DDX56Q9NY931EBI-1051893,EBI-372376
EIF6P565371EBI-1051893,EBI-372243
MAGEB2O154791EBI-1051893,EBI-1057615
PSTPIP1O435861EBI-1051893,EBI-1050964

Protein-protein interaction databases

BioGridi112083. 26 interactions.
IntActiP49207. 7 interactions.
MINTiMINT-3017141.
STRINGi9606.ENSP00000378160.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00Cg1-117[»]
ProteinModelPortaliP49207.
SMRiP49207. Positions 2-115.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L34e family.Curated

Phylogenomic databases

eggNOGiCOG2174.
GeneTreeiENSGT00390000008294.
HOGENOMiHOG000216922.
HOVERGENiHBG024280.
InParanoidiP49207.
KOiK02915.
OMAiRCGDCVK.
OrthoDBiEOG7QC7Z7.
PhylomeDBiP49207.
TreeFamiTF314326.

Family and domain databases

InterProiIPR008195. Ribosomal_L34Ae.
IPR018065. Ribosomal_L34e_CS.
[Graphical view]
PANTHERiPTHR10759. PTHR10759. 1 hit.
PfamiPF01199. Ribosomal_L34e. 1 hit.
[Graphical view]
PRINTSiPR01250. RIBOSOMALL34.
PROSITEiPS01145. RIBOSOMAL_L34E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P49207-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVQRLTYRRR LSYNTASNKT RLSRTPGNRI VYLYTKKVGK APKSACGVCP
60 70 80 90 100
GRLRGVRAVR PKVLMRLSKT KKHVSRAYGG SMCAKCVRDR IKRAFLIEEQ
110
KIVVKVLKAQ AQSQKAK
Length:117
Mass (Da):13,293
Last modified:January 23, 2007 - v3
Checksum:iFC09D00B98CB770C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 521R → K in AAC41916 (PubMed:7490091).Curated
Sequence conflicti58 – 581A → P in AAC41916 (PubMed:7490091).Curated
Sequence conflicti103 – 1031V → I in AAC41916 (PubMed:7490091).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L38941 mRNA. Translation: AAC41916.1.
AB061832 Genomic DNA. Translation: BAB79470.1.
CR542232 mRNA. Translation: CAG47028.1.
CR542242 mRNA. Translation: CAG47038.1.
BC001773 mRNA. Translation: AAH01773.1.
BC070208 mRNA. Translation: AAH70208.1.
BC106009 mRNA. Translation: AAI06010.1.
AB007181 Genomic DNA. Translation: BAA25840.1.
CCDSiCCDS3680.1.
PIRiI68524.
RefSeqiNP_000986.2. NM_000995.3.
NP_296374.1. NM_033625.2.
XP_005263229.1. XM_005263172.2.
XP_006714350.1. XM_006714287.1.
UniGeneiHs.438227.

Genome annotation databases

EnsembliENST00000394665; ENSP00000378160; ENSG00000109475.
ENST00000394667; ENSP00000378162; ENSG00000109475.
ENST00000394668; ENSP00000378163; ENSG00000109475.
ENST00000502534; ENSP00000423983; ENSG00000109475.
ENST00000506397; ENSP00000423316; ENSG00000109475.
GeneIDi6164.
KEGGihsa:6164.
UCSCiuc003hyz.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L38941 mRNA. Translation: AAC41916.1.
AB061832 Genomic DNA. Translation: BAB79470.1.
CR542232 mRNA. Translation: CAG47028.1.
CR542242 mRNA. Translation: CAG47038.1.
BC001773 mRNA. Translation: AAH01773.1.
BC070208 mRNA. Translation: AAH70208.1.
BC106009 mRNA. Translation: AAI06010.1.
AB007181 Genomic DNA. Translation: BAA25840.1.
CCDSiCCDS3680.1.
PIRiI68524.
RefSeqiNP_000986.2. NM_000995.3.
NP_296374.1. NM_033625.2.
XP_005263229.1. XM_005263172.2.
XP_006714350.1. XM_006714287.1.
UniGeneiHs.438227.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00Cg1-117[»]
ProteinModelPortaliP49207.
SMRiP49207. Positions 2-115.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112083. 26 interactions.
IntActiP49207. 7 interactions.
MINTiMINT-3017141.
STRINGi9606.ENSP00000378160.

PTM databases

PhosphoSiteiP49207.

Polymorphism and mutation databases

BioMutaiRPL34.

Proteomic databases

MaxQBiP49207.
PaxDbiP49207.
PeptideAtlasiP49207.
PRIDEiP49207.

Protocols and materials databases

DNASUi6164.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000394665; ENSP00000378160; ENSG00000109475.
ENST00000394667; ENSP00000378162; ENSG00000109475.
ENST00000394668; ENSP00000378163; ENSG00000109475.
ENST00000502534; ENSP00000423983; ENSG00000109475.
ENST00000506397; ENSP00000423316; ENSG00000109475.
GeneIDi6164.
KEGGihsa:6164.
UCSCiuc003hyz.3. human.

Organism-specific databases

CTDi6164.
GeneCardsiGC04P109541.
H-InvDBHIX0004432.
HGNCiHGNC:10340. RPL34.
HPAiHPA035139.
neXtProtiNX_P49207.
PharmGKBiPA34723.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2174.
GeneTreeiENSGT00390000008294.
HOGENOMiHOG000216922.
HOVERGENiHBG024280.
InParanoidiP49207.
KOiK02915.
OMAiRCGDCVK.
OrthoDBiEOG7QC7Z7.
PhylomeDBiP49207.
TreeFamiTF314326.

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

ChiTaRSiRPL34. human.
GeneWikiiRPL34.
GenomeRNAii6164.
NextBioi23943.
PROiP49207.

Gene expression databases

BgeeiP49207.
CleanExiHS_RPL34.
ExpressionAtlasiP49207. baseline and differential.
GenevestigatoriP49207.

Family and domain databases

InterProiIPR008195. Ribosomal_L34Ae.
IPR018065. Ribosomal_L34e_CS.
[Graphical view]
PANTHERiPTHR10759. PTHR10759. 1 hit.
PfamiPF01199. Ribosomal_L34e. 1 hit.
[Graphical view]
PRINTSiPR01250. RIBOSOMALL34.
PROSITEiPS01145. RIBOSOMAL_L34E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Generation of a transcription map at the HSD17B locus centromeric to BRCA1 at 17q21."
    Rommens J.M., Durocher F., McArthur J., Tonin P., Leblanc J.-F., Allen T., Samson C., Ferri L., Narod S., Morgan K., Simard J.
    Genomics 28:530-542(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Ovary.
  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. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "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: Bone and Eye.
  5. "A map of 75 human ribosomal protein genes."
    Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J., Tanaka T., Page D.C.
    Genome Res. 8:509-523(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 4-48.
  6. "Characterization and analysis of posttranslational modifications of the human large cytoplasmic ribosomal subunit proteins by mass spectrometry and Edman sequencing."
    Odintsova T.I., Muller E.C., Ivanov A.V., Egorov T.A., Bienert R., Vladimirov S.N., Kostka S., Otto A., Wittmann-Liebold B., Karpova G.G.
    J. Protein Chem. 22:249-258(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-12, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRL34_HUMAN
AccessioniPrimary (citable) accession number: P49207
Secondary accession number(s): Q6FG66, Q9BUZ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: May 27, 2015
This is version 134 of the entry and version 3 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 4
    Human chromosome 4: 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.