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P49207

- RL34_HUMAN

UniProt

P49207 - RL34_HUMAN

Protein

60S ribosomal protein L34

Gene

RPL34

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

    GO - Molecular functioni

    1. RNA binding Source: ProtInc
    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

    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: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:10340. RPL34.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. cytosolic large ribosomal subunit Source: UniProtKB
    4. extracellular vesicular exosome Source: UniProt
    5. nucleolus Source: HPA

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34723.

    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.
    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. 21 interactions.
    IntActiP49207. 7 interactions.
    MINTiMINT-3017141.
    STRINGi9606.ENSP00000378160.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3J3Belectron microscopy5.00g1-117[»]
    ProteinModelPortaliP49207.
    SMRiP49207. Positions 2-115.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L34e family.Curated

    Phylogenomic databases

    eggNOGiCOG2174.
    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

    MVQRLTYRRR LSYNTASNKT RLSRTPGNRI VYLYTKKVGK APKSACGVCP    50
    GRLRGVRAVR PKVLMRLSKT KKHVSRAYGG SMCAKCVRDR IKRAFLIEEQ 100
    KIVVKVLKAQ AQSQKAK 117
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS3680.1.
    PIRi I68524.
    RefSeqi NP_000986.2. NM_000995.3.
    NP_296374.1. NM_033625.2.
    XP_005263229.1. XM_005263172.2.
    XP_006714350.1. XM_006714287.1.
    UniGenei Hs.438227.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3J3B electron microscopy 5.00 g 1-117 [» ]
    ProteinModelPortali P49207.
    SMRi P49207. Positions 2-115.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112083. 21 interactions.
    IntActi P49207. 7 interactions.
    MINTi MINT-3017141.
    STRINGi 9606.ENSP00000378160.

    PTM databases

    PhosphoSitei P49207.

    Proteomic databases

    MaxQBi P49207.
    PaxDbi P49207.
    PeptideAtlasi P49207.
    PRIDEi P49207.

    Protocols and materials databases

    DNASUi 6164.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000394665 ; ENSP00000378160 ; ENSG00000109475 .
    ENST00000394667 ; ENSP00000378162 ; ENSG00000109475 .
    ENST00000394668 ; ENSP00000378163 ; ENSG00000109475 .
    ENST00000502534 ; ENSP00000423983 ; ENSG00000109475 .
    ENST00000506397 ; ENSP00000423316 ; ENSG00000109475 .
    GeneIDi 6164.
    KEGGi hsa:6164.
    UCSCi uc003hyz.3. human.

    Organism-specific databases

    CTDi 6164.
    GeneCardsi GC04P109541.
    H-InvDB HIX0004432.
    HGNCi HGNC:10340. RPL34.
    HPAi HPA035139.
    neXtProti NX_P49207.
    PharmGKBi PA34723.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2174.
    HOGENOMi HOG000216922.
    HOVERGENi HBG024280.
    InParanoidi P49207.
    KOi K02915.
    OMAi RCGDCVK.
    OrthoDBi EOG7QC7Z7.
    PhylomeDBi P49207.
    TreeFami TF314326.

    Enzyme and pathway databases

    Reactomei REACT_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

    ChiTaRSi RPL34. human.
    GeneWikii RPL34.
    GenomeRNAii 6164.
    NextBioi 23943.
    PROi P49207.

    Gene expression databases

    Bgeei P49207.
    CleanExi HS_RPL34.
    Genevestigatori P49207.

    Family and domain databases

    InterProi IPR008195. Ribosomal_L34Ae.
    IPR018065. Ribosomal_L34e_CS.
    [Graphical view ]
    PANTHERi PTHR10759. PTHR10759. 1 hit.
    Pfami PF01199. Ribosomal_L34e. 1 hit.
    [Graphical view ]
    PRINTSi PR01250. RIBOSOMALL34.
    PROSITEi PS01145. RIBOSOMAL_L34E. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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: October 1, 2014
    This is version 128 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