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P46776

- RL27A_HUMAN

UniProt

P46776 - RL27A_HUMAN

Protein

60S ribosomal protein L27a

Gene

RPL27A

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

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. RNA binding Source: ProtInc
    4. 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 L27a
    Gene namesi
    Name:RPL27A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:10329. RPL27A.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. cytosolic large ribosomal subunit Source: UniProtKB
    3. membrane Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34708.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 14814760S ribosomal protein L27aPRO_0000104879Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei39 – 391(3S)-3-hydroxyhistidine1 Publication
    Modified residuei47 – 471N6-acetyllysine1 Publication
    Modified residuei55 – 551N6-acetyllysine1 Publication
    Modified residuei68 – 681Phosphoserine2 Publications
    Modified residuei110 – 1101N6-acetyllysine1 Publication

    Post-translational modificationi

    Hydroxylated on His-39 by MINA.1 Publication

    Keywords - PTMi

    Acetylation, Hydroxylation, Phosphoprotein

    Proteomic databases

    MaxQBiP46776.
    PaxDbiP46776.
    PRIDEiP46776.

    2D gel databases

    SWISS-2DPAGEP46776.

    PTM databases

    PhosphoSiteiP46776.

    Expressioni

    Gene expression databases

    ArrayExpressiP46776.
    BgeeiP46776.
    CleanExiHS_RPL27A.
    GenevestigatoriP46776.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GTF2F2P139842EBI-350581,EBI-1030560

    Protein-protein interaction databases

    BioGridi112076. 84 interactions.
    DIPiDIP-33121N.
    IntActiP46776. 15 interactions.
    MINTiMINT-1150308.
    STRINGi9606.ENSP00000346015.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3J3Belectron microscopy5.00a1-148[»]
    4BXFX-ray2.05C/D32-50[»]
    ProteinModelPortaliP46776.
    SMRiP46776. Positions 2-148.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L15P family.Curated

    Phylogenomic databases

    eggNOGiCOG0200.
    HOGENOMiHOG000231263.
    HOVERGENiHBG054587.
    InParanoidiP46776.
    KOiK02900.
    OMAiDKAPVID.
    OrthoDBiEOG78SQKP.
    PhylomeDBiP46776.
    TreeFamiTF313742.

    Family and domain databases

    HAMAPiMF_01341. Ribosomal_L15.
    InterProiIPR001196. Ribosomal_L15_CS.
    IPR021131. Ribosomal_L18e/L15P.
    [Graphical view]
    PfamiPF00828. Ribosomal_L18e. 1 hit.
    [Graphical view]
    SUPFAMiSSF52080. SSF52080. 1 hit.
    PROSITEiPS00475. RIBOSOMAL_L15. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P46776-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPSRLRKTRK LRGHVSHGHG RIGKHRKHPG GRGNAGGLHH HRINFDKYHP    50
    GYFGKVGMKH YHLKRNQSFC PTVNLDKLWT LVSEQTRVNA AKNKTGAAPI 100
    IDVVRSGYYK VLGKGKLPKQ PVIVKAKFFS RRAEEKIKSV GGACVLVA 148
    Length:148
    Mass (Da):16,561
    Last modified:January 23, 2007 - v2
    Checksum:iCB5E09C91507798F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U14968 mRNA. Translation: AAA85656.1.
    AB020236 Genomic DNA. Translation: BAA77361.1.
    AK311767 mRNA. Translation: BAG34710.1.
    CH471064 Genomic DNA. Translation: EAW68619.1.
    BC005326 mRNA. Translation: AAH05326.1.
    BC020169 mRNA. Translation: AAH20169.1.
    AB007178 Genomic DNA. Translation: BAA25837.1.
    CCDSiCCDS7790.1.
    PIRiS55914.
    RefSeqiNP_000981.1. NM_000990.4.
    UniGeneiHs.523463.

    Genome annotation databases

    EnsembliENST00000314138; ENSP00000346015; ENSG00000166441.
    GeneIDi6157.
    KEGGihsa:6157.
    UCSCiuc001mgs.4. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U14968 mRNA. Translation: AAA85656.1 .
    AB020236 Genomic DNA. Translation: BAA77361.1 .
    AK311767 mRNA. Translation: BAG34710.1 .
    CH471064 Genomic DNA. Translation: EAW68619.1 .
    BC005326 mRNA. Translation: AAH05326.1 .
    BC020169 mRNA. Translation: AAH20169.1 .
    AB007178 Genomic DNA. Translation: BAA25837.1 .
    CCDSi CCDS7790.1.
    PIRi S55914.
    RefSeqi NP_000981.1. NM_000990.4.
    UniGenei Hs.523463.

    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 a 1-148 [» ]
    4BXF X-ray 2.05 C/D 32-50 [» ]
    ProteinModelPortali P46776.
    SMRi P46776. Positions 2-148.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112076. 84 interactions.
    DIPi DIP-33121N.
    IntActi P46776. 15 interactions.
    MINTi MINT-1150308.
    STRINGi 9606.ENSP00000346015.

    PTM databases

    PhosphoSitei P46776.

    2D gel databases

    SWISS-2DPAGE P46776.

    Proteomic databases

    MaxQBi P46776.
    PaxDbi P46776.
    PRIDEi P46776.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000314138 ; ENSP00000346015 ; ENSG00000166441 .
    GeneIDi 6157.
    KEGGi hsa:6157.
    UCSCi uc001mgs.4. human.

    Organism-specific databases

    CTDi 6157.
    GeneCardsi GC11P008703.
    HGNCi HGNC:10329. RPL27A.
    MIMi 603637. gene.
    neXtProti NX_P46776.
    PharmGKBi PA34708.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0200.
    HOGENOMi HOG000231263.
    HOVERGENi HBG054587.
    InParanoidi P46776.
    KOi K02900.
    OMAi DKAPVID.
    OrthoDBi EOG78SQKP.
    PhylomeDBi P46776.
    TreeFami TF313742.

    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

    GeneWikii RPL27A.
    GenomeRNAii 6157.
    NextBioi 23911.
    PROi P46776.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P46776.
    Bgeei P46776.
    CleanExi HS_RPL27A.
    Genevestigatori P46776.

    Family and domain databases

    HAMAPi MF_01341. Ribosomal_L15.
    InterProi IPR001196. Ribosomal_L15_CS.
    IPR021131. Ribosomal_L18e/L15P.
    [Graphical view ]
    Pfami PF00828. Ribosomal_L18e. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52080. SSF52080. 1 hit.
    PROSITEi PS00475. RIBOSOMAL_L15. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9, S10 and S29 human ribosomal protein mRNAs."
      Frigerio J.-M., Dagorn J.-C., Iovanna J.L.
      Biochim. Biophys. Acta 1262:64-68(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Colon.
    2. "Genomic structure and chromosome location of RPL27A/Rpl27a, the genes encoding human and mouse ribosomal protein L27A."
      Kusuda J., Hirai M., Tanuma R., Hirata M., Hashimoto K.
      Cytogenet. Cell Genet. 85:248-251(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "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: Tongue.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Kidney and Lymph.
    6. "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 73-106.
    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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, 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-47; LYS-55 AND LYS-110, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: HYDROXYLATION AT HIS-39 BY MINA.
    12. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

    Entry informationi

    Entry nameiRL27A_HUMAN
    AccessioniPrimary (citable) accession number: P46776
    Secondary accession number(s): B2R4B3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 127 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, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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