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P30050

- RL12_HUMAN

UniProt

P30050 - RL12_HUMAN

Protein

60S ribosomal protein L12

Gene

RPL12

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

    Binds directly to 26S ribosomal RNA.By similarity

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. 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

    Keywords - Ligandi

    RNA-binding

    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 L12
    Gene namesi
    Name:RPL12
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:10302. RPL12.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. cytosolic large ribosomal subunit Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. membrane Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34665.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 16516560S ribosomal protein L12PRO_0000104456Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei38 – 381Phosphoserine4 Publications
    Modified residuei54 – 541N6-acetyllysine1 Publication
    Modified residuei83 – 831N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP30050.
    PaxDbiP30050.
    PRIDEiP30050.

    2D gel databases

    SWISS-2DPAGEP30050.

    PTM databases

    PhosphoSiteiP30050.

    Expressioni

    Gene expression databases

    BgeeiP30050.
    CleanExiHS_RPL12.
    GenevestigatoriP30050.

    Organism-specific databases

    HPAiHPA003403.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CANXP278243EBI-352743,EBI-355947

    Protein-protein interaction databases

    BioGridi112056. 106 interactions.
    IntActiP30050. 31 interactions.
    MINTiMINT-2802291.
    STRINGi9606.ENSP00000354739.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3J3Belectron microscopy5.00K1-165[»]
    ProteinModelPortaliP30050.
    SMRiP30050. Positions 1-163.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L11P family.Curated

    Phylogenomic databases

    eggNOGiCOG0080.
    HOVERGENiHBG007231.
    InParanoidiP30050.
    KOiK02870.
    OMAiGCTIDGR.
    OrthoDBiEOG7JMGG9.
    PhylomeDBiP30050.
    TreeFamiTF300123.

    Family and domain databases

    Gene3Di1.10.10.250. 1 hit.
    3.30.1550.10. 1 hit.
    HAMAPiMF_00736. Ribosomal_L11.
    InterProiIPR000911. Ribosomal_L11/L12.
    IPR020783. Ribosomal_L11_C.
    IPR020785. Ribosomal_L11_CS.
    IPR020784. Ribosomal_L11_N.
    [Graphical view]
    PANTHERiPTHR11661. PTHR11661. 1 hit.
    PfamiPF00298. Ribosomal_L11. 1 hit.
    PF03946. Ribosomal_L11_N. 1 hit.
    [Graphical view]
    SMARTiSM00649. RL11. 1 hit.
    [Graphical view]
    SUPFAMiSSF46906. SSF46906. 1 hit.
    SSF54747. SSF54747. 1 hit.
    PROSITEiPS00359. RIBOSOMAL_L11. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P30050-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MPPKFDPNEI KVVYLRCTGG EVGATSALAP KIGPLGLSPK KVGDDIAKAT    50
    GDWKGLRITV KLTIQNRQAQ IEVVPSASAL IIKALKEPPR DRKKQKNIKH 100
    SGNITFDEIV NIARQMRHRS LARELSGTIK EILGTAQSVG CNVDGRHPHD 150
    IIDDINSGAV ECPAS 165
    Length:165
    Mass (Da):17,819
    Last modified:April 1, 1993 - v1
    Checksum:i7EFD783A8ED350F9
    GO
    Isoform 2 (identifier: P30050-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         38-70: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:132
    Mass (Da):14,199
    Checksum:i1FDF4BEF878AD5D5
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei38 – 7033Missing in isoform 2. 1 PublicationVSP_034695Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L06505 mRNA. Translation: AAA36157.1.
    AL445222 Genomic DNA. Translation: CAH72929.1.
    CH471090 Genomic DNA. Translation: EAW87669.1.
    BC050644 mRNA. Translation: AAH50644.1.
    BC059950 mRNA. Translation: AAH59950.1.
    BC094831 mRNA. Translation: AAH94831.1.
    BC105603 mRNA. Translation: AAI05604.1.
    CCDSiCCDS6872.1. [P30050-1]
    PIRiS35531.
    RefSeqiNP_000967.1. NM_000976.3. [P30050-1]
    UniGeneiHs.408054.

    Genome annotation databases

    EnsembliENST00000361436; ENSP00000354739; ENSG00000197958. [P30050-1]
    ENST00000536368; ENSP00000441179; ENSG00000197958. [P30050-2]
    GeneIDi6136.
    KEGGihsa:6136.
    UCSCiuc004bqy.2. human. [P30050-1]
    uc004bqz.2. human. [P30050-2]

    Polymorphism databases

    DMDMi266921.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L06505 mRNA. Translation: AAA36157.1 .
    AL445222 Genomic DNA. Translation: CAH72929.1 .
    CH471090 Genomic DNA. Translation: EAW87669.1 .
    BC050644 mRNA. Translation: AAH50644.1 .
    BC059950 mRNA. Translation: AAH59950.1 .
    BC094831 mRNA. Translation: AAH94831.1 .
    BC105603 mRNA. Translation: AAI05604.1 .
    CCDSi CCDS6872.1. [P30050-1 ]
    PIRi S35531.
    RefSeqi NP_000967.1. NM_000976.3. [P30050-1 ]
    UniGenei Hs.408054.

    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 K 1-165 [» ]
    ProteinModelPortali P30050.
    SMRi P30050. Positions 1-163.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112056. 106 interactions.
    IntActi P30050. 31 interactions.
    MINTi MINT-2802291.
    STRINGi 9606.ENSP00000354739.

    PTM databases

    PhosphoSitei P30050.

    Polymorphism databases

    DMDMi 266921.

    2D gel databases

    SWISS-2DPAGE P30050.

    Proteomic databases

    MaxQBi P30050.
    PaxDbi P30050.
    PRIDEi P30050.

    Protocols and materials databases

    DNASUi 6136.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361436 ; ENSP00000354739 ; ENSG00000197958 . [P30050-1 ]
    ENST00000536368 ; ENSP00000441179 ; ENSG00000197958 . [P30050-2 ]
    GeneIDi 6136.
    KEGGi hsa:6136.
    UCSCi uc004bqy.2. human. [P30050-1 ]
    uc004bqz.2. human. [P30050-2 ]

    Organism-specific databases

    CTDi 6136.
    GeneCardsi GC09M130209.
    H-InvDB HIX0170298.
    HGNCi HGNC:10302. RPL12.
    HPAi HPA003403.
    MIMi 180475. gene.
    neXtProti NX_P30050.
    PharmGKBi PA34665.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0080.
    HOVERGENi HBG007231.
    InParanoidi P30050.
    KOi K02870.
    OMAi GCTIDGR.
    OrthoDBi EOG7JMGG9.
    PhylomeDBi P30050.
    TreeFami TF300123.

    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 RPL12. human.
    GeneWikii RPL12.
    GenomeRNAii 6136.
    NextBioi 23835.
    PROi P30050.
    SOURCEi Search...

    Gene expression databases

    Bgeei P30050.
    CleanExi HS_RPL12.
    Genevestigatori P30050.

    Family and domain databases

    Gene3Di 1.10.10.250. 1 hit.
    3.30.1550.10. 1 hit.
    HAMAPi MF_00736. Ribosomal_L11.
    InterProi IPR000911. Ribosomal_L11/L12.
    IPR020783. Ribosomal_L11_C.
    IPR020785. Ribosomal_L11_CS.
    IPR020784. Ribosomal_L11_N.
    [Graphical view ]
    PANTHERi PTHR11661. PTHR11661. 1 hit.
    Pfami PF00298. Ribosomal_L11. 1 hit.
    PF03946. Ribosomal_L11_N. 1 hit.
    [Graphical view ]
    SMARTi SM00649. RL11. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46906. SSF46906. 1 hit.
    SSF54747. SSF54747. 1 hit.
    PROSITEi PS00359. RIBOSOMAL_L11. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The primary structure of human ribosomal protein L12."
      Chu W., Presky D.H., Swerlisk R.A., Burns D.K.
      Nucleic Acids Res. 21:749-749(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORMS 1 AND 2).
      Tissue: Ovary.
    5. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      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-54 AND LYS-83, 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-38, 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-38, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.

    Entry informationi

    Entry nameiRL12_HUMAN
    AccessioniPrimary (citable) accession number: P30050
    Secondary accession number(s): Q5VVV2, Q6PB27
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 141 of the entry and version 1 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, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Ribosomal proteins
      Ribosomal proteins families and list of entries
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3