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P47914

- RL29_HUMAN

UniProt

P47914 - RL29_HUMAN

Protein

60S ribosomal protein L29

Gene

RPL29

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

    GO - Molecular functioni

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

    GO - Biological processi

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

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Ligandi

    Heparin-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.
    SignaLinkiP47914.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    60S ribosomal protein L29
    Alternative name(s):
    Cell surface heparin-binding protein HIP
    Gene namesi
    Name:RPL29
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:10331. RPL29.

    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

    PharmGKBiPA34711.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 15915860S ribosomal protein L29PRO_0000219134Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei5 – 51N6-methyllysine1 Publication
    Modified residuei33 – 331N6-acetyllysine1 Publication
    Cross-linki56 – 56Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki73 – 73Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei142 – 1421Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP47914.
    PaxDbiP47914.
    PRIDEiP47914.

    PTM databases

    PhosphoSiteiP47914.

    Expressioni

    Gene expression databases

    ArrayExpressiP47914.
    BgeeiP47914.
    CleanExiHS_RPL29.
    GenevestigatoriP47914.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DDX56Q9NY931EBI-714039,EBI-372376
    PSTPIP1O435861EBI-714039,EBI-1050964

    Protein-protein interaction databases

    BioGridi112078. 52 interactions.
    IntActiP47914. 12 interactions.
    MINTiMINT-1375294.
    STRINGi9606.ENSP00000294189.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3J3Belectron microscopy5.00b1-159[»]
    ProteinModelPortaliP47914.
    SMRiP47914. Positions 2-79.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L29e family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG249125.
    HOVERGENiHBG000386.
    InParanoidiP47914.
    KOiK02905.
    OMAiCRPKSQA.
    OrthoDBiEOG7JT70C.
    PhylomeDBiP47914.
    TreeFamiTF313858.

    Family and domain databases

    InterProiIPR002673. Ribosomal_L29e.
    [Graphical view]
    PANTHERiPTHR12884. PTHR12884. 1 hit.
    PfamiPF01779. Ribosomal_L29e. 1 hit.
    [Graphical view]
    ProDomiPD010314. Ribosomal_L29e. 1 hit.
    [Graphical view] [Entries sharing at least one domain]

    Sequencei

    Sequence statusi: Complete.

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

    P47914-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKSKNHTTH NQSRKWHRNG IKKPRSQRYE SLKGVDPKFL RNMRFAKKHN    50
    KKGLKKMQAN NAKAMSARAE AIKALVKPKE VKPKIPKGVS RKLDRLAYIA 100
    HPKLGKRARA RIAKGLRLCR PKAKAKAKAK DQTKAQAAAP ASVPAQAPKR 150
    TQAPTKASE 159
    Length:159
    Mass (Da):17,752
    Last modified:January 23, 2007 - v2
    Checksum:i2A0C31984EF4FF95
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti5 – 51K → R in BAF82227. (PubMed:14702039)Curated
    Sequence conflicti120 – 1201R → A in CAA89008. (PubMed:8597591)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U10248 mRNA. Translation: AAC50499.1.
    Z49148 mRNA. Translation: CAA89008.1.
    U49083 mRNA. Translation: AAC50647.1.
    AK289538 mRNA. Translation: BAF82227.1.
    AK311884 mRNA. Translation: BAG34825.1.
    BC008926 mRNA. Translation: AAH08926.1.
    BC070190 mRNA. Translation: AAH70190.1.
    BC070481 mRNA. Translation: AAH70481.1.
    BC071663 mRNA. Translation: AAH71663.1.
    CCDSiCCDS2845.1.
    PIRiS65784.
    RefSeqiNP_000983.1. NM_000992.2.
    UniGeneiHs.425125.

    Genome annotation databases

    EnsembliENST00000294189; ENSP00000294189; ENSG00000162244.
    ENST00000466397; ENSP00000418868; ENSG00000162244.
    ENST00000475248; ENSP00000417048; ENSG00000162244.
    ENST00000479017; ENSP00000418153; ENSG00000162244.
    ENST00000492277; ENSP00000418346; ENSG00000162244.
    ENST00000495383; ENSP00000420673; ENSG00000162244.
    GeneIDi6159.
    KEGGihsa:6159.
    UCSCiuc003dcs.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U10248 mRNA. Translation: AAC50499.1 .
    Z49148 mRNA. Translation: CAA89008.1 .
    U49083 mRNA. Translation: AAC50647.1 .
    AK289538 mRNA. Translation: BAF82227.1 .
    AK311884 mRNA. Translation: BAG34825.1 .
    BC008926 mRNA. Translation: AAH08926.1 .
    BC070190 mRNA. Translation: AAH70190.1 .
    BC070481 mRNA. Translation: AAH70481.1 .
    BC071663 mRNA. Translation: AAH71663.1 .
    CCDSi CCDS2845.1.
    PIRi S65784.
    RefSeqi NP_000983.1. NM_000992.2.
    UniGenei Hs.425125.

    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 b 1-159 [» ]
    ProteinModelPortali P47914.
    SMRi P47914. Positions 2-79.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112078. 52 interactions.
    IntActi P47914. 12 interactions.
    MINTi MINT-1375294.
    STRINGi 9606.ENSP00000294189.

    PTM databases

    PhosphoSitei P47914.

    Proteomic databases

    MaxQBi P47914.
    PaxDbi P47914.
    PRIDEi P47914.

    Protocols and materials databases

    DNASUi 6159.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000294189 ; ENSP00000294189 ; ENSG00000162244 .
    ENST00000466397 ; ENSP00000418868 ; ENSG00000162244 .
    ENST00000475248 ; ENSP00000417048 ; ENSG00000162244 .
    ENST00000479017 ; ENSP00000418153 ; ENSG00000162244 .
    ENST00000492277 ; ENSP00000418346 ; ENSG00000162244 .
    ENST00000495383 ; ENSP00000420673 ; ENSG00000162244 .
    GeneIDi 6159.
    KEGGi hsa:6159.
    UCSCi uc003dcs.3. human.

    Organism-specific databases

    CTDi 6159.
    GeneCardsi GC03M052029.
    H-InvDB HIX0031209.
    HGNCi HGNC:10331. RPL29.
    MIMi 601832. gene.
    neXtProti NX_P47914.
    PharmGKBi PA34711.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG249125.
    HOVERGENi HBG000386.
    InParanoidi P47914.
    KOi K02905.
    OMAi CRPKSQA.
    OrthoDBi EOG7JT70C.
    PhylomeDBi P47914.
    TreeFami TF313858.

    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.
    SignaLinki P47914.

    Miscellaneous databases

    ChiTaRSi RPL29. human.
    GeneWikii RPL29.
    GenomeRNAii 6159.
    NextBioi 23919.
    PROi P47914.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P47914.
    Bgeei P47914.
    CleanExi HS_RPL29.
    Genevestigatori P47914.

    Family and domain databases

    InterProi IPR002673. Ribosomal_L29e.
    [Graphical view ]
    PANTHERi PTHR12884. PTHR12884. 1 hit.
    Pfami PF01779. Ribosomal_L29e. 1 hit.
    [Graphical view ]
    ProDomi PD010314. Ribosomal_L29e. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    ProtoNeti Search...

    Publicationsi

    1. Law P.T., Tsui S.K., Lee C.Y., Waye M.M.
      Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "cDNA cloning and expression of HIP, a novel cell surface heparan sulfate/heparin-binding protein of human uterine epithelial cells and cell lines."
      Liu S., Smith S.E., Julian J., Rohde L.H., Karin N.J., Carson D.D.
      J. Biol. Chem. 271:11817-11823(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [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: Brain and Cerebellum.
    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: Ovary and Pancreas.
    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 2-15, IDENTIFICATION BY MASS SPECTROMETRY, METHYLATION AT LYS-5.
    7. "Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
      Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
      Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-56 AND LYS-73.
      Tissue: Mammary cancer.
    8. "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-33, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "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-142, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

    Entry informationi

    Entry nameiRL29_HUMAN
    AccessioniPrimary (citable) accession number: P47914
    Secondary accession number(s): A8K0H3, B2R4M8, Q6IPY3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 132 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. 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