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P0CW22

- RS17L_HUMAN

UniProt

P0CW22 - RS17L_HUMAN

Protein

40S ribosomal protein S17-like

Gene

RPS17L

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
  1. Functioni

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. structural constituent of ribosome Source: InterPro

    GO - Biological processi

    1. translation Source: InterPro

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    40S ribosomal protein S17-like
    Gene namesi
    Name:RPS17L
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:40029. RPS17L.

    Subcellular locationi

    GO - Cellular componenti

    1. ribosome Source: UniProtKB-KW

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 13513440S ribosomal protein S17-likePRO_0000410726Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei113 – 1131Phosphoserine4 Publications
    Modified residuei130 – 1301Phosphothreonine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiP0CW22.

    PTM databases

    PhosphoSiteiP0CW22.

    Expressioni

    Gene expression databases

    BgeeiP0CW22.

    Organism-specific databases

    HPAiHPA055060.

    Interactioni

    Protein-protein interaction databases

    BioGridi112132. 68 interactions.
    1527840. 14 interactions.
    IntActiP0CW22. 3 interactions.
    MINTiMINT-8395037.

    Structurei

    3D structure databases

    ProteinModelPortaliP0CW22.
    SMRiP0CW22. Positions 1-126.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein S17e family.Curated

    Phylogenomic databases

    KOiK02962.
    OrthoDBiEOG72C52C.
    PhylomeDBiP0CW22.
    TreeFamiTF317992.

    Family and domain databases

    Gene3Di1.10.60.20. 1 hit.
    HAMAPiMF_00511. Ribosomal_S17e.
    InterProiIPR001210. Ribosomal_S17e.
    IPR018273. Ribosomal_S17e_CS.
    [Graphical view]
    PANTHERiPTHR10732. PTHR10732. 1 hit.
    PfamiPF00833. Ribosomal_S17e. 1 hit.
    [Graphical view]
    SUPFAMiSSF116820. SSF116820. 1 hit.
    PROSITEiPS00712. RIBOSOMAL_S17E. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P0CW22-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGRVRTKTVK KAARVIIEKY YTRLGNDFHT NKRVCEEIAI IPSKKLRNKI    50
    AGYVTHLMKR IQRGPVRGIS IKLQEEERER RDNYVPEVSA LDQEIIEVDP 100
    DTKEMLKLLD FGSLSNLQVT QPTVGMNFKT PRGPV 135
    Length:135
    Mass (Da):15,550
    Last modified:June 28, 2011 - v1
    Checksum:i299AD605C5401325
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC010724 Genomic DNA. No translation available.
    RefSeqiNP_001012.1. NM_001021.4.
    UniGeneiHs.433427.
    Hs.512525.

    Genome annotation databases

    GeneIDi6218.
    KEGGihsa:100505503.
    hsa:6218.
    UCSCiuc002bhr.1. human.

    Polymorphism databases

    DMDMi338819320.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC010724 Genomic DNA. No translation available.
    RefSeqi NP_001012.1. NM_001021.4.
    UniGenei Hs.433427.
    Hs.512525.

    3D structure databases

    ProteinModelPortali P0CW22.
    SMRi P0CW22. Positions 1-126.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112132. 68 interactions.
    1527840. 14 interactions.
    IntActi P0CW22. 3 interactions.
    MINTi MINT-8395037.

    PTM databases

    PhosphoSitei P0CW22.

    Polymorphism databases

    DMDMi 338819320.

    Proteomic databases

    PRIDEi P0CW22.

    Protocols and materials databases

    DNASUi 6218.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 6218.
    KEGGi hsa:100505503.
    hsa:6218.
    UCSCi uc002bhr.1. human.

    Organism-specific databases

    CTDi 6218.
    GeneCardsi GC15M083202.
    HGNCi HGNC:40029. RPS17L.
    HPAi HPA055060.
    neXtProti NX_P0CW22.
    GenAtlasi Search...

    Phylogenomic databases

    KOi K02962.
    OrthoDBi EOG72C52C.
    PhylomeDBi P0CW22.
    TreeFami TF317992.

    Miscellaneous databases

    ChiTaRSi RPS17L. human.
    NextBioi 24145.
    PROi P0CW22.

    Gene expression databases

    Bgeei P0CW22.

    Family and domain databases

    Gene3Di 1.10.60.20. 1 hit.
    HAMAPi MF_00511. Ribosomal_S17e.
    InterProi IPR001210. Ribosomal_S17e.
    IPR018273. Ribosomal_S17e_CS.
    [Graphical view ]
    PANTHERi PTHR10732. PTHR10732. 1 hit.
    Pfami PF00833. Ribosomal_S17e. 1 hit.
    [Graphical view ]
    SUPFAMi SSF116820. SSF116820. 1 hit.
    PROSITEi PS00712. RIBOSOMAL_S17E. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113 AND THR-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    4. "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 SER-113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    5. "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-113 AND THR-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "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-113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRS17L_HUMAN
    AccessioniPrimary (citable) accession number: P0CW22
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 28, 2011
    Last sequence update: June 28, 2011
    Last modified: October 1, 2014
    This is version 31 of the entry and version 1 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    2. Ribosomal proteins
      Ribosomal proteins families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3