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P23396

- RS3_HUMAN

UniProt

P23396 - RS3_HUMAN

Protein

40S ribosomal protein S3

Gene

RPS3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 168 (01 Oct 2014)
      Sequence version 2 (01 Oct 1993)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

    1. damaged DNA binding Source: UniProtKB
    2. DNA-(apurinic or apyrimidinic site) lyase activity Source: UniProtKB
    3. endonuclease activity Source: UniProtKB
    4. enzyme binding Source: UniProtKB
    5. iron-sulfur cluster binding Source: UniProtKB
    6. mRNA binding Source: UniProtKB
    7. NF-kappaB binding Source: UniProtKB
    8. poly(A) RNA binding Source: UniProtKB
    9. protein binding Source: UniProtKB
    10. protein kinase A binding Source: UniProtKB
    11. protein kinase binding Source: UniProtKB
    12. structural constituent of ribosome Source: UniProtKB

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. cellular response to DNA damage stimulus Source: UniProtKB
    3. cytoplasmic translation Source: RefGenome
    4. DNA catabolic process, endonucleolytic Source: GOC
    5. gene expression Source: Reactome
    6. mRNA metabolic process Source: Reactome
    7. negative regulation of DNA repair Source: UniProtKB
    8. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
    9. nucleic acid phosphodiester bond hydrolysis Source: GOC
    10. positive regulation of apoptotic signaling pathway Source: UniProtKB
    11. positive regulation of DNA N-glycosylase activity Source: UniProtKB
    12. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    13. RNA metabolic process Source: Reactome
    14. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
    15. translation Source: UniProtKB
    16. translational elongation Source: Reactome
    17. translational initiation Source: UniProtKB
    18. translational termination Source: Reactome
    19. viral life cycle Source: Reactome
    20. viral process Source: Reactome
    21. viral transcription Source: Reactome

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
    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_1979. Translation initiation complex formation.
    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_931. Ribosomal scanning and start codon recognition.
    REACT_9491. Viral mRNA Translation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    40S ribosomal protein S3
    Gene namesi
    Name:RPS3
    ORF Names:OK/SW-cl.26
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:10420. RPS3.

    Subcellular locationi

    Cytoplasm 1 Publication
    Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. cytosolic small ribosomal subunit Source: UniProtKB
    4. extracellular vesicular exosome Source: UniProt
    5. membrane Source: UniProtKB
    6. nucleus Source: UniProtKB
    7. ribonucleoprotein complex Source: UniProtKB
    8. ruffle membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34829.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 24324240S ribosomal protein S3PRO_0000130320Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei62 – 621N6-acetyllysine1 Publication
    Cross-linki90 – 90Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
    Modified residuei132 – 1321N6-succinyllysineBy similarity
    Cross-linki202 – 202Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
    Modified residuei221 – 2211Phosphothreonine6 Publications
    Modified residuei224 – 2241Phosphoserine1 Publication
    Modified residuei242 – 2421Phosphothreonine1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP23396.
    PaxDbiP23396.
    PeptideAtlasiP23396.
    PRIDEiP23396.

    PTM databases

    PhosphoSiteiP23396.

    Expressioni

    Gene expression databases

    ArrayExpressiP23396.
    BgeeiP23396.
    CleanExiHS_RPS3.
    GenevestigatoriP23396.

    Interactioni

    Subunit structurei

    Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with HNRPD. Identified in a HCV IRES-mediated translation complex, at least composed of EIF3C, IGF2BP1, RPS3 and HCV RNA-replicon.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    IKBKBO149204EBI-351193,EBI-81266
    LRRK2Q5S0072EBI-351193,EBI-5323863
    NEDD8Q158432EBI-351193,EBI-716247
    NFKB1P198382EBI-351193,EBI-300010
    NFKBIAP259636EBI-351193,EBI-307386
    PPIDQ087524EBI-351193,EBI-716596
    RELAQ042067EBI-351193,EBI-73886
    YWHAZP631042EBI-351193,EBI-347088

    Protein-protein interaction databases

    BioGridi112102. 178 interactions.
    IntActiP23396. 44 interactions.
    MINTiMINT-4999144.
    STRINGi9606.ENSP00000278572.

    Structurei

    Secondary structure

    1
    243
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi17 – 2812
    Turni29 – 335
    Beta strandi34 – 418
    Beta strandi46 – 538
    Helixi55 – 595
    Helixi61 – 633
    Helixi64 – 7714
    Beta strandi83 – 908

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WH9NMR-A17-95[»]
    3J3Aelectron microscopy5.00D1-243[»]
    ProteinModelPortaliP23396.
    SMRiP23396. Positions 1-227.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23396.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini21 – 9272KH type-2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ribosomal protein S3P family.Curated
    Contains 1 KH type-2 domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0092.
    HOGENOMiHOG000210611.
    HOVERGENiHBG002195.
    InParanoidiP23396.
    KOiK02985.
    OMAiVDYPEMI.
    OrthoDBiEOG7F7W9M.
    PhylomeDBiP23396.
    TreeFamiTF300901.

    Family and domain databases

    Gene3Di3.30.1140.32. 1 hit.
    3.30.300.20. 1 hit.
    InterProiIPR004087. KH_dom.
    IPR015946. KH_dom-like_a/b.
    IPR004044. KH_dom_type_2.
    IPR009019. KH_prok-type.
    IPR001351. Ribosomal_S3_C.
    IPR018280. Ribosomal_S3_CS.
    IPR005703. Ribosomal_S3_euk/arc.
    [Graphical view]
    PfamiPF07650. KH_2. 1 hit.
    PF00189. Ribosomal_S3_C. 1 hit.
    [Graphical view]
    SMARTiSM00322. KH. 1 hit.
    [Graphical view]
    SUPFAMiSSF54814. SSF54814. 1 hit.
    SSF54821. SSF54821. 1 hit.
    TIGRFAMsiTIGR01008. rpsC_E_A. 1 hit.
    PROSITEiPS50823. KH_TYPE_2. 1 hit.
    PS00548. RIBOSOMAL_S3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P23396-1) [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

    MAVQISKKRK FVADGIFKAE LNEFLTRELA EDGYSGVEVR VTPTRTEIII    50
    LATRTQNVLG EKGRRIRELT AVVQKRFGFP EGSVELYAEK VATRGLCAIA 100
    QAESLRYKLL GGLAVRRACY GVLRFIMESG AKGCEVVVSG KLRGQRAKSM 150
    KFVDGLMIHS GDPVNYYVDT AVRHVLLRQG VLGIKVKIML PWDPTGKIGP 200
    KKPLPDHVSI VEPKDEILPT TPISEQKGGK PEPPAMPQPV PTA 243
    Length:243
    Mass (Da):26,688
    Last modified:October 1, 1993 - v2
    Checksum:i6ECBB34A8EE04AAF
    GO
    Isoform 2 (identifier: P23396-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         85-85: E → ELKIMVMVTGYPLLPLK

    Note: No experimental confirmation available. Gene prediction based on EST data.

    Show »
    Length:259
    Mass (Da):28,487
    Checksum:i68FF5C2DF8769693
    GO

    Sequence cautioni

    The sequence BAB93471.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti8 – 81K → R in AAB19349. (PubMed:1712897)Curated
    Sequence conflicti104 – 1041S → C in CAA39248. (PubMed:2129557)Curated
    Sequence conflicti233 – 2331P → L in CAA39248. (PubMed:2129557)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei85 – 851E → ELKIMVMVTGYPLLPLK in isoform 2. CuratedVSP_046667

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U14990 mRNA. Translation: AAB60336.1.
    U14991 mRNA. Translation: AAB60337.1.
    U14992 mRNA. Translation: AAB60338.1.
    X55715 mRNA. Translation: CAA39248.1.
    S42658 mRNA. Translation: AAB19349.2.
    AB061838 Genomic DNA. Translation: BAB79476.1.
    AY791291 Genomic DNA. Translation: AAV40835.1.
    AK313051 mRNA. Translation: BAG35882.1.
    AP000744 Genomic DNA. No translation available.
    CH471076 Genomic DNA. Translation: EAW74963.1.
    BC003137 mRNA. Translation: AAH03137.1.
    BC003577 mRNA. Translation: AAH03577.1.
    BC013196 mRNA. Translation: AAH13196.1.
    BC034149 mRNA. Translation: AAH34149.1.
    BC071917 mRNA. Translation: AAH71917.1.
    BC100284 mRNA. Translation: AAI00285.1.
    L16016 Genomic DNA. Translation: AAA18095.1.
    AB062288 mRNA. Translation: BAB93471.1. Different initiation.
    CCDSiCCDS58161.1. [P23396-2]
    CCDS8236.1. [P23396-1]
    PIRiA41247. R3HUS3.
    RefSeqiNP_000996.2. NM_001005.4. [P23396-1]
    NP_001243731.1. NM_001256802.1. [P23396-1]
    NP_001247435.1. NM_001260506.1. [P23396-2]
    NP_001247436.1. NM_001260507.1.
    UniGeneiHs.546286.
    Hs.740358.

    Genome annotation databases

    EnsembliENST00000278572; ENSP00000278572; ENSG00000149273. [P23396-2]
    ENST00000524851; ENSP00000433821; ENSG00000149273. [P23396-1]
    ENST00000527446; ENSP00000436971; ENSG00000149273. [P23396-1]
    ENST00000531188; ENSP00000434643; ENSG00000149273. [P23396-1]
    GeneIDi6188.
    KEGGihsa:6188.
    UCSCiuc001owh.4. human. [P23396-1]

    Polymorphism databases

    DMDMi417719.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U14990 mRNA. Translation: AAB60336.1 .
    U14991 mRNA. Translation: AAB60337.1 .
    U14992 mRNA. Translation: AAB60338.1 .
    X55715 mRNA. Translation: CAA39248.1 .
    S42658 mRNA. Translation: AAB19349.2 .
    AB061838 Genomic DNA. Translation: BAB79476.1 .
    AY791291 Genomic DNA. Translation: AAV40835.1 .
    AK313051 mRNA. Translation: BAG35882.1 .
    AP000744 Genomic DNA. No translation available.
    CH471076 Genomic DNA. Translation: EAW74963.1 .
    BC003137 mRNA. Translation: AAH03137.1 .
    BC003577 mRNA. Translation: AAH03577.1 .
    BC013196 mRNA. Translation: AAH13196.1 .
    BC034149 mRNA. Translation: AAH34149.1 .
    BC071917 mRNA. Translation: AAH71917.1 .
    BC100284 mRNA. Translation: AAI00285.1 .
    L16016 Genomic DNA. Translation: AAA18095.1 .
    AB062288 mRNA. Translation: BAB93471.1 . Different initiation.
    CCDSi CCDS58161.1. [P23396-2 ]
    CCDS8236.1. [P23396-1 ]
    PIRi A41247. R3HUS3.
    RefSeqi NP_000996.2. NM_001005.4. [P23396-1 ]
    NP_001243731.1. NM_001256802.1. [P23396-1 ]
    NP_001247435.1. NM_001260506.1. [P23396-2 ]
    NP_001247436.1. NM_001260507.1.
    UniGenei Hs.546286.
    Hs.740358.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WH9 NMR - A 17-95 [» ]
    3J3A electron microscopy 5.00 D 1-243 [» ]
    ProteinModelPortali P23396.
    SMRi P23396. Positions 1-227.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112102. 178 interactions.
    IntActi P23396. 44 interactions.
    MINTi MINT-4999144.
    STRINGi 9606.ENSP00000278572.

    PTM databases

    PhosphoSitei P23396.

    Polymorphism databases

    DMDMi 417719.

    Proteomic databases

    MaxQBi P23396.
    PaxDbi P23396.
    PeptideAtlasi P23396.
    PRIDEi P23396.

    Protocols and materials databases

    DNASUi 6188.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000278572 ; ENSP00000278572 ; ENSG00000149273 . [P23396-2 ]
    ENST00000524851 ; ENSP00000433821 ; ENSG00000149273 . [P23396-1 ]
    ENST00000527446 ; ENSP00000436971 ; ENSG00000149273 . [P23396-1 ]
    ENST00000531188 ; ENSP00000434643 ; ENSG00000149273 . [P23396-1 ]
    GeneIDi 6188.
    KEGGi hsa:6188.
    UCSCi uc001owh.4. human. [P23396-1 ]

    Organism-specific databases

    CTDi 6188.
    GeneCardsi GC11P075110.
    HGNCi HGNC:10420. RPS3.
    MIMi 600454. gene.
    neXtProti NX_P23396.
    PharmGKBi PA34829.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0092.
    HOGENOMi HOG000210611.
    HOVERGENi HBG002195.
    InParanoidi P23396.
    KOi K02985.
    OMAi VDYPEMI.
    OrthoDBi EOG7F7W9M.
    PhylomeDBi P23396.
    TreeFami TF300901.

    Enzyme and pathway databases

    Reactomei REACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
    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_1979. Translation initiation complex formation.
    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_931. Ribosomal scanning and start codon recognition.
    REACT_9491. Viral mRNA Translation.

    Miscellaneous databases

    ChiTaRSi RpS3. human.
    EvolutionaryTracei P23396.
    GeneWikii RPS3.
    GenomeRNAii 6188.
    NextBioi 24029.
    PROi P23396.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P23396.
    Bgeei P23396.
    CleanExi HS_RPS3.
    Genevestigatori P23396.

    Family and domain databases

    Gene3Di 3.30.1140.32. 1 hit.
    3.30.300.20. 1 hit.
    InterProi IPR004087. KH_dom.
    IPR015946. KH_dom-like_a/b.
    IPR004044. KH_dom_type_2.
    IPR009019. KH_prok-type.
    IPR001351. Ribosomal_S3_C.
    IPR018280. Ribosomal_S3_CS.
    IPR005703. Ribosomal_S3_euk/arc.
    [Graphical view ]
    Pfami PF07650. KH_2. 1 hit.
    PF00189. Ribosomal_S3_C. 1 hit.
    [Graphical view ]
    SMARTi SM00322. KH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54814. SSF54814. 1 hit.
    SSF54821. SSF54821. 1 hit.
    TIGRFAMsi TIGR01008. rpsC_E_A. 1 hit.
    PROSITEi PS50823. KH_TYPE_2. 1 hit.
    PS00548. RIBOSOMAL_S3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation of a cDNA encoding human 40S ribosomal protein s3."
      Zhang X.T., Tan Y.M., Tan Y.H.
      Nucleic Acids Res. 18:6689-6689(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Ribosomal protein genes are overexpressed in colorectal cancer: isolation of a cDNA clone encoding the human S3 ribosomal protein."
      Pogue-Geile K., Geiser J.R., Shu M., Miller C., Wool I.G., Meisler A.I., Pipas J.M.
      Mol. Cell. Biol. 11:3842-3849(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "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].
    4. NIEHS SNPs program
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "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] (ISOFORM 1).
      Tissue: Brain.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORM 1).
      Tissue: Adrenal cortex, Liver, Lymph, Skin and Testis.
    9. "A small nucleolar RNA is processed from an intron of the human gene encoding ribosomal protein S3."
      Tycowski K.T., Shu M.D., Steitz J.A.
      Genes Dev. 7:1176-1190(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 1-94 (ISOFORM 1).
    10. Bienvenut W.V., Murray L., Brunton V.G., Frame M.C., Calvo F., Kolch W.
      Submitted (FEB-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-8; 10-64; 68-116; 118-141; 152-173; 186-197 AND 202-243, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Cervix carcinoma and Colon adenocarcinoma.
    11. "Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
      Shichijo S., Itoh K.
      Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-243 (ISOFORM 1).
      Tissue: Colon adenocarcinoma.
    12. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 10-40; 46-54; 76-90; 95-106; 109-116; 118-132; 152-173; 179-185; 188-197 AND 202-243, PHOSPHORYLATION AT THR-221, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Cervix carcinoma.
    13. "Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry."
      Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A.
      Eur. J. Biochem. 239:144-149(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 188-197.
      Tissue: Placenta.
    14. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "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 THR-221, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Pituitary.
    17. Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    18. "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 THR-242, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "IGF2BP1 enhances HCV IRES-mediated translation initiation via the 3'UTR."
      Weinlich S., Huettelmaier S., Schierhorn A., Behrens S.-E., Ostareck-Lederer A., Ostareck D.H.
      RNA 15:1528-1542(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A HCV IRES-MEDIATED TRANSLATION COMPLEX.
    23. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    24. "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-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "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 THR-221, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "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 THR-221, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "AUF1 contributes to Cryptochrome1 mRNA degradation and rhythmic translation."
      Lee K.H., Kim S.H., Kim H.J., Kim W., Lee H.R., Jung Y., Choi J.H., Hong K.Y., Jang S.K., Kim K.T.
      Nucleic Acids Res. 42:3590-3606(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HNRPD.
    30. "Solution structure of the KH domain of human ribosomal protein S3."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2004) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 17-95.
    31. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.

    Entry informationi

    Entry nameiRS3_HUMAN
    AccessioniPrimary (citable) accession number: P23396
    Secondary accession number(s): B2R7N5
    , J3KN86, Q498B5, Q8NI95
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 168 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 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