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P27635

- RL10_HUMAN

UniProt

P27635 - RL10_HUMAN

Protein

60S ribosomal protein L10

Gene

RPL10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 4 (12 Jun 2007)
      Previous versions | rss
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    Functioni

    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

    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 L10
    Alternative name(s):
    Laminin receptor homolog
    Protein QM
    Tumor suppressor QM
    Gene namesi
    Name:RPL10
    Synonyms:DXS648E, QM
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:10298. RPL10.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. cytosolic large ribosomal subunit Source: UniProtKB
    3. endoplasmic reticulum Source: LIFEdb
    4. membrane Source: UniProtKB

    Pathology & Biotechi

    Involvement in diseasei

    Autism, X-linked 5 (AUTSX5) [MIM:300847]: A complex multifactorial, pervasive developmental disorder characterized by impairments in reciprocal social interaction and communication, restricted and stereotyped patterns of interests and activities, and the presence of developmental abnormalities by 3 years of age. Most individuals with autism also manifest moderate mental retardation.2 Publications
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. RPL10 is involved in autism only in rare cases. Two hypomorphic variants affecting the translation process have been found in families with autism spectrum disorders, suggesting that aberrant translation may play a role in disease mechanisms.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti206 – 2061L → M in AUTSX5. 1 Publication
    VAR_027795
    Natural varianti213 – 2131H → Q in AUTSX5. 2 Publications
    VAR_027796

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi300847. phenotype.
    Orphaneti106. Autism.
    PharmGKBiPA34660.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 21421360S ribosomal protein L10PRO_0000147105Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei32 – 321CitrullineBy similarity
    Cross-linki188 – 188Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

    Post-translational modificationi

    Citrullinated by PADI4.By similarity

    Keywords - PTMi

    Citrullination, Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiP27635.
    PaxDbiP27635.
    PRIDEiP27635.

    PTM databases

    PhosphoSiteiP27635.

    Miscellaneous databases

    PMAP-CutDBP27635.

    Expressioni

    Developmental stagei

    Down-regulated during adipocyte, kidney, and heart differentiation.

    Gene expression databases

    ArrayExpressiP27635.
    BgeeiP27635.
    CleanExiHS_RPL10.
    GenevestigatoriP27635.

    Organism-specific databases

    HPAiCAB010339.
    HPA011311.

    Interactioni

    Subunit structurei

    Component of the large ribosomal subunit. Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains about 33 different proteins and 1 molecule of RNA (18S). The 60S subunit contains about 49 different proteins and 3 molecules of RNA (28S, 5.8S and 5S).

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SRCP129316EBI-352398,EBI-621482

    Protein-protein interaction databases

    BioGridi112054. 80 interactions.
    DIPiDIP-1133N.
    IntActiP27635. 17 interactions.
    MINTiMINT-1153266.
    STRINGi9606.ENSP00000341730.

    Structurei

    Secondary structure

    1
    214
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni43 – 453
    Beta strandi48 – 547
    Beta strandi58 – 614
    Helixi62 – 8019
    Beta strandi84 – 896
    Beta strandi126 – 1294
    Beta strandi133 – 1408
    Helixi142 – 1443
    Helixi145 – 15511
    Helixi156 – 1583
    Beta strandi159 – 1613
    Beta strandi163 – 1697

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2PA2X-ray2.50A/B34-182[»]
    ProteinModelPortaliP27635.
    SMRiP27635. Positions 2-214.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27635.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L10e family.Curated

    Phylogenomic databases

    eggNOGiCOG0197.
    HOVERGENiHBG002287.
    KOiK02866.
    OMAiIMSMRCK.
    PhylomeDBiP27635.
    TreeFamiTF300082.

    Family and domain databases

    Gene3Di3.90.1170.10. 1 hit.
    InterProiIPR001197. Ribosomal_L10e.
    IPR016180. Ribosomal_L10e/L16.
    IPR018255. Ribosomal_L10e_CS.
    [Graphical view]
    PfamiPF00252. Ribosomal_L16. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005590. Ribosomal_L10. 1 hit.
    SUPFAMiSSF54686. SSF54686. 1 hit.
    TIGRFAMsiTIGR00279. L10e. 1 hit.
    PROSITEiPS01257. RIBOSOMAL_L10E. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P27635-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGRRPARCYR YCKNKPYPKS RFCRGVPDAK IRIFDLGRKK AKVDEFPLCG    50
    HMVSDEYEQL SSEALEAARI CANKYMVKSC GKDGFHIRVR LHPFHVIRIN 100
    KMLSCAGADR LQTGMRGAFG KPQGTVARVH IGQVIMSIRT KLQNKEHVIE 150
    ALRRAKFKFP GRQKIHISKK WGFTKFNADE FEDMVAEKRL IPDGCGVKYI 200
    PNRGPLDKWR ALHS 214
    Length:214
    Mass (Da):24,604
    Last modified:June 12, 2007 - v4
    Checksum:i0860CECC91DF74FE
    GO

    Sequence cautioni

    The sequence AAB22173.1 differs from that shown. Reason: Frameshift at position 124.
    The sequence CAM45852.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAM45853.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti23 – 231Missing in AAL88713. (PubMed:12138090)Curated
    Sequence conflicti157 – 1571F → L in BAD97029. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti202 – 2021N → S.10 Publications
    Corresponds to variant rs12012747 [ dbSNP | Ensembl ].
    VAR_006922
    Natural varianti206 – 2061L → M in AUTSX5. 1 Publication
    VAR_027795
    Natural varianti213 – 2131H → Q in AUTSX5. 2 Publications
    VAR_027796

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64241 mRNA. Translation: AAA63253.1.
    M81806 Genomic DNA. Translation: AAA36021.1.
    M73791 mRNA. Translation: AAA36378.1.
    S64169, S64168 Genomic DNA. Translation: AAB27665.1.
    AF486812 mRNA. Translation: AAL88713.1.
    DQ369703 mRNA. Translation: ABC88559.1.
    DQ369704 mRNA. Translation: ABC88560.1.
    DQ369705 mRNA. Translation: ABC88561.1.
    DQ369706 mRNA. Translation: ABC88562.1.
    DQ369707 mRNA. Translation: ABC88563.1.
    DQ369708 mRNA. Translation: ABC88564.1.
    DQ369709 mRNA. Translation: ABC88565.1.
    DQ369710 mRNA. Translation: ABC88566.1.
    DQ369711 mRNA. Translation: ABC88567.1.
    DQ369712 mRNA. Translation: ABC88568.1.
    DQ369713 mRNA. Translation: ABC88569.1.
    DQ369714 mRNA. Translation: ABC88570.1.
    DQ369715 mRNA. Translation: ABC88571.1.
    DQ369716 mRNA. Translation: ABC88572.1.
    CR456797 mRNA. Translation: CAG33078.1.
    CR542069 mRNA. Translation: CAG46866.1.
    AK223309 mRNA. Translation: BAD97029.1.
    L44140 Genomic DNA. Translation: AAA92646.1.
    BX936347, BX936346 Genomic DNA. Translation: CAI43214.1.
    BX936346, BX936347 Genomic DNA. Translation: CAI43230.1.
    BX936347, BX936346 Genomic DNA. Translation: CAM45852.1. Sequence problems.
    BX936346, BX936347 Genomic DNA. Translation: CAM45853.1. Sequence problems.
    CH471172 Genomic DNA. Translation: EAW72737.1.
    CH471172 Genomic DNA. Translation: EAW72739.1.
    BC003358 mRNA. Translation: AAH03358.1.
    BC026276 mRNA. Translation: AAH26276.1.
    BC071918 mRNA. Translation: AAH71918.1.
    S35960 mRNA. Translation: AAB22173.1. Frameshift.
    AB007170 Genomic DNA. Translation: BAA28595.1.
    CCDSiCCDS14746.1.
    PIRiA42735.
    RefSeqiNP_001243506.1. NM_001256577.1.
    NP_001243509.1. NM_001256580.1.
    NP_006004.2. NM_006013.3.
    UniGeneiHs.534404.

    Genome annotation databases

    EnsembliENST00000344746; ENSP00000341730; ENSG00000147403.
    ENST00000369817; ENSP00000358832; ENSG00000147403.
    ENST00000424325; ENSP00000413436; ENSG00000147403.
    GeneIDi6134.
    KEGGihsa:6134.
    UCSCiuc004fkm.2. human.

    Polymorphism databases

    DMDMi148887414.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64241 mRNA. Translation: AAA63253.1 .
    M81806 Genomic DNA. Translation: AAA36021.1 .
    M73791 mRNA. Translation: AAA36378.1 .
    S64169 , S64168 Genomic DNA. Translation: AAB27665.1 .
    AF486812 mRNA. Translation: AAL88713.1 .
    DQ369703 mRNA. Translation: ABC88559.1 .
    DQ369704 mRNA. Translation: ABC88560.1 .
    DQ369705 mRNA. Translation: ABC88561.1 .
    DQ369706 mRNA. Translation: ABC88562.1 .
    DQ369707 mRNA. Translation: ABC88563.1 .
    DQ369708 mRNA. Translation: ABC88564.1 .
    DQ369709 mRNA. Translation: ABC88565.1 .
    DQ369710 mRNA. Translation: ABC88566.1 .
    DQ369711 mRNA. Translation: ABC88567.1 .
    DQ369712 mRNA. Translation: ABC88568.1 .
    DQ369713 mRNA. Translation: ABC88569.1 .
    DQ369714 mRNA. Translation: ABC88570.1 .
    DQ369715 mRNA. Translation: ABC88571.1 .
    DQ369716 mRNA. Translation: ABC88572.1 .
    CR456797 mRNA. Translation: CAG33078.1 .
    CR542069 mRNA. Translation: CAG46866.1 .
    AK223309 mRNA. Translation: BAD97029.1 .
    L44140 Genomic DNA. Translation: AAA92646.1 .
    BX936347 , BX936346 Genomic DNA. Translation: CAI43214.1 .
    BX936346 , BX936347 Genomic DNA. Translation: CAI43230.1 .
    BX936347 , BX936346 Genomic DNA. Translation: CAM45852.1 . Sequence problems.
    BX936346 , BX936347 Genomic DNA. Translation: CAM45853.1 . Sequence problems.
    CH471172 Genomic DNA. Translation: EAW72737.1 .
    CH471172 Genomic DNA. Translation: EAW72739.1 .
    BC003358 mRNA. Translation: AAH03358.1 .
    BC026276 mRNA. Translation: AAH26276.1 .
    BC071918 mRNA. Translation: AAH71918.1 .
    S35960 mRNA. Translation: AAB22173.1 . Frameshift.
    AB007170 Genomic DNA. Translation: BAA28595.1 .
    CCDSi CCDS14746.1.
    PIRi A42735.
    RefSeqi NP_001243506.1. NM_001256577.1.
    NP_001243509.1. NM_001256580.1.
    NP_006004.2. NM_006013.3.
    UniGenei Hs.534404.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2PA2 X-ray 2.50 A/B 34-182 [» ]
    ProteinModelPortali P27635.
    SMRi P27635. Positions 2-214.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112054. 80 interactions.
    DIPi DIP-1133N.
    IntActi P27635. 17 interactions.
    MINTi MINT-1153266.
    STRINGi 9606.ENSP00000341730.

    PTM databases

    PhosphoSitei P27635.

    Polymorphism databases

    DMDMi 148887414.

    Proteomic databases

    MaxQBi P27635.
    PaxDbi P27635.
    PRIDEi P27635.

    Protocols and materials databases

    DNASUi 6134.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000344746 ; ENSP00000341730 ; ENSG00000147403 .
    ENST00000369817 ; ENSP00000358832 ; ENSG00000147403 .
    ENST00000424325 ; ENSP00000413436 ; ENSG00000147403 .
    GeneIDi 6134.
    KEGGi hsa:6134.
    UCSCi uc004fkm.2. human.

    Organism-specific databases

    CTDi 6134.
    GeneCardsi GC0XP153618.
    GeneReviewsi RPL10.
    H-InvDB HIX0017152.
    HIX0202878.
    HGNCi HGNC:10298. RPL10.
    HPAi CAB010339.
    HPA011311.
    MIMi 300847. phenotype.
    312173. gene.
    neXtProti NX_P27635.
    Orphaneti 106. Autism.
    PharmGKBi PA34660.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0197.
    HOVERGENi HBG002287.
    KOi K02866.
    OMAi IMSMRCK.
    PhylomeDBi P27635.
    TreeFami TF300082.

    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 RPL10. human.
    EvolutionaryTracei P27635.
    GeneWikii RPL10.
    GenomeRNAii 6134.
    NextBioi 23827.
    PMAP-CutDB P27635.
    PROi P27635.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P27635.
    Bgeei P27635.
    CleanExi HS_RPL10.
    Genevestigatori P27635.

    Family and domain databases

    Gene3Di 3.90.1170.10. 1 hit.
    InterProi IPR001197. Ribosomal_L10e.
    IPR016180. Ribosomal_L10e/L16.
    IPR018255. Ribosomal_L10e_CS.
    [Graphical view ]
    Pfami PF00252. Ribosomal_L16. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005590. Ribosomal_L10. 1 hit.
    SUPFAMi SSF54686. SSF54686. 1 hit.
    TIGRFAMsi TIGR00279. L10e. 1 hit.
    PROSITEi PS01257. RIBOSOMAL_L10E. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The isolation and characterization of a novel cDNA demonstrating an altered mRNA level in nontumorigenic Wilms' microcell hybrid cells."
      Dowdy S.F., Lai K.M., Weissman B.E., Matsui Y., Hogan B.L.M., Stanbridge E.S.
      Nucleic Acids Res. 19:5763-5769(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-202.
    2. "Identification and characterization of a new gene in the human Xq28 region."
      van den Ouweland A.M.W., Kioschis P., Verdijk M., Tamanini F., Toniolo D., Poustka A., van Oost B.A.
      Hum. Mol. Genet. 1:269-273(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-202.
    3. "Sequence analysis of a novel gene expressed in normal and in tumor-derived tissue."
      Kroepelin M.
      Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-202.
      Tissue: Mammary gland.
    4. "Genomic organization of a cDNA (QM) demonstrating an altered mRNA level in nontumorigenic Wilms' microcell hybrid cells and its localization to Xq28."
      Kaneko K., Kobayashi H., Onodera O., Miyatake T., Tsuji S.
      Hum. Mol. Genet. 1:529-533(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-202.
    5. "QM, a putative tumor suppressor, regulates proto-oncogene c-Yes."
      Oh H.S., Kwon H., Sun S.K., Yang C.-H.
      J. Biol. Chem. 277:36489-36498(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    6. "Loss of heterozygosity and microsatellite instability at the Xq28 and the A/G heterozygosity of the QM gene are associated with ovarian cancer."
      Shen X.J., Ali-Fehmi R., Weng C.R., Sarkar F.H., Grignon D., Liao D.J.
      Cancer Biol. Ther. 5:523-528(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-202.
      Tissue: Mammary cancer, Ovarian carcinoma, Pancreatic cancer and Prostatic carcinoma.
    7. "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], VARIANT SER-202.
    8. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-202.
      Tissue: Thymus.
    9. "Long-range sequence analysis in Xq28: thirteen known and six candidate genes in 219.4 kb of high GC DNA between the RCP/GCP and G6PD loci."
      Chen E.Y., Zollo M., Mazzarella R.A., Ciccodicola A., Chen C.-N., Zuo L., Heiner C., Burough F.W., Ripetto M., Schlessinger D., D'Urso M.
      Hum. Mol. Genet. 5:659-668(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-202.
    11. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    12. "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], VARIANT SER-202.
      Tissue: Brain, Mammary gland and Placenta.
    13. "cDNA cloning and genomic analysis of a new multigene family sharing common phylogenetic and expression profiles with the laminin receptor gene."
      Bignon C., Roux-Dosseto M., Zeigler M.E., Wicha M.S., Martin P.M.
      Biochem. Biophys. Res. Commun. 184:1165-1172(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-147.
    14. "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 135-214, VARIANT SER-202.
    15. "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 2-11, IDENTIFICATION BY MASS SPECTROMETRY.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Crystal structure of human ribosomal protein L10 core domain reveals eukaryote-specific motifs in addition to the conserved fold."
      Nishimura M., Kaminishi T., Takemoto C., Kawazoe M., Yoshida T., Tanaka A., Sugano S., Shirouzu M., Ohkubo T., Yokoyama S., Kobayashi Y.
      J. Mol. Biol. 377:421-430(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 34-182.
    18. Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO AUTISM, VARIANTS AUTSX5 MET-206 AND GLN-213.
    19. "Mutation and expression analyses of the ribosomal protein gene RPL10 in an extended German sample of patients with autism spectrum disorder."
      Chiocchetti A., Pakalapati G., Duketis E., Wiemann S., Poustka A., Poustka F., Klauck S.M.
      Am. J. Med. Genet. A 155:1472-1475(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT AUTSX5 GLN-213.

    Entry informationi

    Entry nameiRL10_HUMAN
    AccessioniPrimary (citable) accession number: P27635
    Secondary accession number(s): A3KQT0
    , D3DWW6, Q16470, Q2HXT7, Q53FH7, Q6FGN8, Q8TDA5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: June 12, 2007
    Last modified: October 1, 2014
    This is version 152 of the entry and version 4 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 X
      Human chromosome X: 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