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P61927

- RL37_HUMAN

UniProt

P61927 - RL37_HUMAN

Protein

60S ribosomal protein L37

Gene

RPL37

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

    Binds to the 23S rRNA.By similarity

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi19 – 191ZincBy similarity
    Metal bindingi22 – 221ZincBy similarity
    Metal bindingi34 – 341ZincBy similarity
    Metal bindingi37 – 371ZincBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri19 – 3719C4-typeSequence AnalysisAdd
    BLAST

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. RNA binding Source: UniProtKB
    3. rRNA binding Source: UniProtKB-KW
    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

    Keywords - Ligandi

    Metal-binding, RNA-binding, rRNA-binding, Zinc

    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 L37
    Alternative name(s):
    G1.16
    Gene namesi
    Name:RPL37
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:10347. RPL37.

    Subcellular locationi

    GO - Cellular componenti

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

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34736.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 979660S ribosomal protein L37PRO_0000139705Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei10 – 101N6-acetyllysine1 Publication
    Modified residuei96 – 961Phosphoserine1 Publication
    Modified residuei97 – 971Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP61927.
    PaxDbiP61927.
    PRIDEiP61927.

    PTM databases

    PhosphoSiteiP61927.

    Expressioni

    Gene expression databases

    ArrayExpressiP61927.
    BgeeiP61927.
    CleanExiHS_RPL37.
    GenevestigatoriP61927.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DDX56Q9NY931EBI-2105843,EBI-372376

    Protein-protein interaction databases

    BioGridi112086. 14 interactions.
    IntActiP61927. 5 interactions.
    MINTiMINT-3022842.
    STRINGi9606.ENSP00000274242.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3J3Belectron microscopy5.00j1-97[»]
    ProteinModelPortaliP61927.
    SMRiP61927. Positions 2-91.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L37e family.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri19 – 3719C4-typeSequence AnalysisAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG2126.
    HOGENOMiHOG000111076.
    HOVERGENiHBG004454.
    KOiK02922.
    OMAiYLANIRV.
    OrthoDBiEOG7RJPTP.
    PhylomeDBiP61927.
    TreeFamiTF300260.

    Family and domain databases

    Gene3Di2.20.25.30. 1 hit.
    HAMAPiMF_00547. Ribosomal_L37e.
    InterProiIPR011331. Ribosomal_L37ae/L37e.
    IPR001569. Ribosomal_L37e.
    IPR018267. Ribosomal_L37e_CS.
    IPR011332. Ribosomal_zn-bd.
    [Graphical view]
    PANTHERiPTHR10768. PTHR10768. 1 hit.
    PfamiPF01907. Ribosomal_L37e. 1 hit.
    [Graphical view]
    ProDomiPD005132. Ribosomal_L37e. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF57829. SSF57829. 1 hit.
    PROSITEiPS01077. RIBOSOMAL_L37E. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P61927-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTKGTSSFGK RRNKTHTLCR RCGSKAYHLQ KSTCGKCGYP AKRKRKYNWS   50
    AKAKRRNTTG TGRMRHLKIV YRRFRHGFRE GTTPKPKRAA VAASSSS 97
    Length:97
    Mass (Da):11,078
    Last modified:January 23, 2007 - v2
    Checksum:iF565A11E983027C9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti65 – 651R → S in AAB47039. (PubMed:7588717)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti81 – 811G → E.
    Corresponds to variant rs14898 [ dbSNP | Ensembl ].
    VAR_014606

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D23661 mRNA. Translation: BAA04888.1.
    L11567 mRNA. Translation: AAA62148.1.
    S79979 mRNA. Translation: AAB47039.2.
    AB061834 Genomic DNA. Translation: BAB79472.1.
    CR456890 mRNA. Translation: CAG33171.1.
    AK311827 mRNA. Translation: BAG34769.1.
    BC079477 mRNA. Translation: AAH79477.1.
    BC084576 mRNA. Translation: AAH84576.1.
    AB007184 Genomic DNA. Translation: BAA25843.1.
    AB007183 Genomic DNA. Translation: BAA25842.1.
    CCDSiCCDS3934.1.
    PIRiS47646.
    RefSeqiNP_000988.1. NM_000997.4.
    UniGeneiHs.447582.
    Hs.558601.
    Hs.731513.

    Genome annotation databases

    EnsembliENST00000274242; ENSP00000274242; ENSG00000145592.
    GeneIDi6167.
    KEGGihsa:6167.
    UCSCiuc003jme.1. human.

    Polymorphism databases

    DMDMi48429090.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D23661 mRNA. Translation: BAA04888.1 .
    L11567 mRNA. Translation: AAA62148.1 .
    S79979 mRNA. Translation: AAB47039.2 .
    AB061834 Genomic DNA. Translation: BAB79472.1 .
    CR456890 mRNA. Translation: CAG33171.1 .
    AK311827 mRNA. Translation: BAG34769.1 .
    BC079477 mRNA. Translation: AAH79477.1 .
    BC084576 mRNA. Translation: AAH84576.1 .
    AB007184 Genomic DNA. Translation: BAA25843.1 .
    AB007183 Genomic DNA. Translation: BAA25842.1 .
    CCDSi CCDS3934.1.
    PIRi S47646.
    RefSeqi NP_000988.1. NM_000997.4.
    UniGenei Hs.447582.
    Hs.558601.
    Hs.731513.

    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 j 1-97 [» ]
    ProteinModelPortali P61927.
    SMRi P61927. Positions 2-91.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112086. 14 interactions.
    IntActi P61927. 5 interactions.
    MINTi MINT-3022842.
    STRINGi 9606.ENSP00000274242.

    PTM databases

    PhosphoSitei P61927.

    Polymorphism databases

    DMDMi 48429090.

    Proteomic databases

    MaxQBi P61927.
    PaxDbi P61927.
    PRIDEi P61927.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000274242 ; ENSP00000274242 ; ENSG00000145592 .
    GeneIDi 6167.
    KEGGi hsa:6167.
    UCSCi uc003jme.1. human.

    Organism-specific databases

    CTDi 6167.
    GeneCardsi GC05M040825.
    HGNCi HGNC:10347. RPL37.
    MIMi 604181. gene.
    neXtProti NX_P61927.
    PharmGKBi PA34736.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2126.
    HOGENOMi HOG000111076.
    HOVERGENi HBG004454.
    KOi K02922.
    OMAi YLANIRV.
    OrthoDBi EOG7RJPTP.
    PhylomeDBi P61927.
    TreeFami TF300260.

    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 RPL37. human.
    GeneWikii RPL37.
    GenomeRNAii 6167.
    NextBioi 23957.
    PROi P61927.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P61927.
    Bgeei P61927.
    CleanExi HS_RPL37.
    Genevestigatori P61927.

    Family and domain databases

    Gene3Di 2.20.25.30. 1 hit.
    HAMAPi MF_00547. Ribosomal_L37e.
    InterProi IPR011331. Ribosomal_L37ae/L37e.
    IPR001569. Ribosomal_L37e.
    IPR018267. Ribosomal_L37e_CS.
    IPR011332. Ribosomal_zn-bd.
    [Graphical view ]
    PANTHERi PTHR10768. PTHR10768. 1 hit.
    Pfami PF01907. Ribosomal_L37e. 1 hit.
    [Graphical view ]
    ProDomi PD005132. Ribosomal_L37e. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF57829. SSF57829. 1 hit.
    PROSITEi PS01077. RIBOSOMAL_L37E. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of human ribosomal protein L37 cDNA."
      Kato S.
      Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lymphoma.
    2. "Human ribosomal protein L37 has motifs predicting serine/threonine phosphorylation and a zinc-finger domain."
      Barnard G.F., Staniunas R.J., Puder M., Steele G.D. Jr., Chen L.B.
      Biochim. Biophys. Acta 1218:425-428(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Colon.
    3. "Cell cycle, differentiation and tissue-independent expression of ribosomal protein L37."
      Su S., Bird R.C.
      Eur. J. Biochem. 232:789-797(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "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].
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "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: Trachea.
    7. "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: Lung and Ovary.
    8. "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 48-74 AND 76-97.
    9. "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.
    10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "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-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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-97, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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-96 AND SER-97, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.

    Entry informationi

    Entry nameiRL37_HUMAN
    AccessioniPrimary (citable) accession number: P61927
    Secondary accession number(s): B2R4H2
    , P02403, Q6IBB4, Q99883
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 100 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 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Ribosomal proteins
      Ribosomal proteins families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3