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P18621

- RL17_HUMAN

UniProt

P18621 - RL17_HUMAN

Protein

60S ribosomal protein L17

Gene

RPL17

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. 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 L17
    Alternative name(s):
    60S ribosomal protein L23
    PD-1
    Gene namesi
    Name:RPL17
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:10307. RPL17.

    Subcellular locationi

    GO - Cellular componenti

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

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34676.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 18418360S ribosomal protein L17PRO_0000125331Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei5 – 51Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP18621.
    PaxDbiP18621.
    PRIDEiP18621.

    PTM databases

    PhosphoSiteiP18621.

    Expressioni

    Tissue specificityi

    Expressed in pancreas, lung, colon, cystic duct, gall bladder, kidney and liver. Expressed at high levels in the well differentiated pancreatic tumor cell lines HPAF, COLO 357 and Capan-1, the moderately differentiated pancreatic tumor cell lines T3M-4, AsPc-1 and BxPc-3, the poorly differentiated pancreatic tumor cell line MIA PaCa-2, and the pancreatic tumor cell lines of undefined differentiation status such as SW979. Expressed at lower levels in the poorly differentiated pancreatic tumor cell lines HCG-25 and PANC-1.1 Publication

    Gene expression databases

    BgeeiP18621.
    CleanExiHS_RPL17.
    GenevestigatoriP18621.

    Organism-specific databases

    HPAiHPA043724.
    HPA046385.

    Interactioni

    Protein-protein interaction databases

    BioGridi112059. 101 interactions.
    IntActiP18621. 30 interactions.
    MINTiMINT-1393841.
    STRINGi9606.ENSP00000389465.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3J3Belectron microscopy5.00P1-184[»]
    ProteinModelPortaliP18621.
    SMRiP18621. Positions 2-179.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L22P family.Curated

    Phylogenomic databases

    eggNOGiCOG0091.
    HOGENOMiHOG000205045.
    HOVERGENiHBG000955.
    InParanoidiP18621.
    KOiK02880.
    OMAiYSREPTN.
    OrthoDBiEOG70GMHF.
    PhylomeDBiP18621.
    TreeFamiTF300042.

    Family and domain databases

    Gene3Di3.90.470.10. 1 hit.
    HAMAPiMF_01331_A. Ribosomal_L22_A.
    InterProiIPR001063. Ribosomal_L22.
    IPR018260. Ribosomal_L22/L17_CS.
    IPR005721. Ribosomal_L22/L17_euk/arc.
    [Graphical view]
    PANTHERiPTHR11593. PTHR11593. 1 hit.
    PfamiPF00237. Ribosomal_L22. 1 hit.
    [Graphical view]
    SUPFAMiSSF54843. SSF54843. 1 hit.
    TIGRFAMsiTIGR01038. L22_arch. 1 hit.
    PROSITEiPS00464. RIBOSOMAL_L22. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P18621-1) [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

    MVRYSLDPEN PTKSCKSRGS NLRVHFKNTR ETAQAIKGMH IRKATKYLKD    50
    VTLQKQCVPF RRYNGGVGRC AQAKQWGWTQ GRWPKKSAEF LLHMLKNAES 100
    NAELKGLDVD SLVIEHIQVN KAPKMRRRTY RAHGRINPYM SSPCHIEMIL 150
    TEKEQIVPKP EEEVAQKKKI SQKKLKKQKL MARE 184
    Length:184
    Mass (Da):21,397
    Last modified:January 23, 2007 - v3
    Checksum:i2FC595DD74ED1CA0
    GO
    Isoform 2 (identifier: P18621-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-38: Missing.

    Show »
    Length:146
    Mass (Da):17,094
    Checksum:iF29AFEFE03D5CA59
    GO
    Isoform 3 (identifier: P18621-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         170-184: ISQKKLKKQKLMARE → LRSSSLGKWCAFLVSSFQFCSGSTKNSWSHIYTLWFPPSLVVYGLRKQYKNPMIQTKAK

    Show »
    Length:228
    Mass (Da):26,373
    Checksum:iDF45454F21504C77
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti133 – 1331H → R in AAH66324. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3838Missing in isoform 2. 1 PublicationVSP_045445Add
    BLAST
    Alternative sequencei170 – 18415ISQKK…LMARE → LRSSSLGKWCAFLVSSFQFC SGSTKNSWSHIYTLWFPPSL VVYGLRKQYKNPMIQTKAK in isoform 3. 1 PublicationVSP_046965Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53777 mRNA. Translation: CAA37793.1.
    AB061824 Genomic DNA. Translation: BAB79462.1.
    AC100778 Genomic DNA. No translation available.
    AK304659 mRNA. Translation: BAG65434.1.
    AK311828 mRNA. Translation: BAG34770.1.
    BX393840 mRNA. No translation available.
    CH471096 Genomic DNA. Translation: EAW62940.1.
    BC000502 mRNA. Translation: AAH00502.1.
    BC017831 mRNA. Translation: AAH17831.1.
    BC066323 mRNA. Translation: AAH66323.1.
    BC066324 mRNA. Translation: AAH66324.1.
    BC106031 mRNA. Translation: AAI06032.1.
    AB007174 Genomic DNA. Translation: BAA25834.1.
    CCDSiCCDS45865.1. [P18621-1]
    CCDS56070.1. [P18621-2]
    PIRiA61192.
    S11218. R5HU22.
    RefSeqiNP_000976.1. NM_000985.4. [P18621-1]
    NP_001030178.1. NM_001035006.2. [P18621-1]
    NP_001186269.1. NM_001199340.1. [P18621-1]
    NP_001186270.1. NM_001199341.1. [P18621-1]
    NP_001186271.1. NM_001199342.1. [P18621-1]
    NP_001186272.1. NM_001199343.1. [P18621-1]
    NP_001186273.1. NM_001199344.1. [P18621-1]
    NP_001186274.1. NM_001199345.1. [P18621-2]
    NP_001186284.1. NM_001199355.1. [P18621-3]
    UniGeneiHs.293653.
    Hs.374588.
    Hs.485081.
    Hs.603040.

    Genome annotation databases

    EnsembliENST00000418495; ENSP00000397798; ENSG00000265681. [P18621-1]
    ENST00000579248; ENSP00000462023; ENSG00000265681. [P18621-1]
    ENST00000579408; ENSP00000463842; ENSG00000265681. [P18621-1]
    ENST00000580261; ENSP00000462385; ENSG00000265681. [P18621-1]
    ENST00000581373; ENSP00000462944; ENSG00000265681. [P18621-2]
    GeneIDi100526842.
    6139.
    KEGGihsa:100526842.
    hsa:6139.
    UCSCiuc002ldp.3. human. [P18621-1]

    Polymorphism databases

    DMDMi132799.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53777 mRNA. Translation: CAA37793.1 .
    AB061824 Genomic DNA. Translation: BAB79462.1 .
    AC100778 Genomic DNA. No translation available.
    AK304659 mRNA. Translation: BAG65434.1 .
    AK311828 mRNA. Translation: BAG34770.1 .
    BX393840 mRNA. No translation available.
    CH471096 Genomic DNA. Translation: EAW62940.1 .
    BC000502 mRNA. Translation: AAH00502.1 .
    BC017831 mRNA. Translation: AAH17831.1 .
    BC066323 mRNA. Translation: AAH66323.1 .
    BC066324 mRNA. Translation: AAH66324.1 .
    BC106031 mRNA. Translation: AAI06032.1 .
    AB007174 Genomic DNA. Translation: BAA25834.1 .
    CCDSi CCDS45865.1. [P18621-1 ]
    CCDS56070.1. [P18621-2 ]
    PIRi A61192.
    S11218. R5HU22.
    RefSeqi NP_000976.1. NM_000985.4. [P18621-1 ]
    NP_001030178.1. NM_001035006.2. [P18621-1 ]
    NP_001186269.1. NM_001199340.1. [P18621-1 ]
    NP_001186270.1. NM_001199341.1. [P18621-1 ]
    NP_001186271.1. NM_001199342.1. [P18621-1 ]
    NP_001186272.1. NM_001199343.1. [P18621-1 ]
    NP_001186273.1. NM_001199344.1. [P18621-1 ]
    NP_001186274.1. NM_001199345.1. [P18621-2 ]
    NP_001186284.1. NM_001199355.1. [P18621-3 ]
    UniGenei Hs.293653.
    Hs.374588.
    Hs.485081.
    Hs.603040.

    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 P 1-184 [» ]
    ProteinModelPortali P18621.
    SMRi P18621. Positions 2-179.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112059. 101 interactions.
    IntActi P18621. 30 interactions.
    MINTi MINT-1393841.
    STRINGi 9606.ENSP00000389465.

    PTM databases

    PhosphoSitei P18621.

    Polymorphism databases

    DMDMi 132799.

    Proteomic databases

    MaxQBi P18621.
    PaxDbi P18621.
    PRIDEi P18621.

    Protocols and materials databases

    DNASUi 6139.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000418495 ; ENSP00000397798 ; ENSG00000265681 . [P18621-1 ]
    ENST00000579248 ; ENSP00000462023 ; ENSG00000265681 . [P18621-1 ]
    ENST00000579408 ; ENSP00000463842 ; ENSG00000265681 . [P18621-1 ]
    ENST00000580261 ; ENSP00000462385 ; ENSG00000265681 . [P18621-1 ]
    ENST00000581373 ; ENSP00000462944 ; ENSG00000265681 . [P18621-2 ]
    GeneIDi 100526842.
    6139.
    KEGGi hsa:100526842.
    hsa:6139.
    UCSCi uc002ldp.3. human. [P18621-1 ]

    Organism-specific databases

    CTDi 100526842.
    6139.
    GeneCardsi GC18M047009.
    GC18M047014.
    HGNCi HGNC:10307. RPL17.
    HPAi HPA043724.
    HPA046385.
    MIMi 603661. gene.
    neXtProti NX_P18621.
    PharmGKBi PA34676.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0091.
    HOGENOMi HOG000205045.
    HOVERGENi HBG000955.
    InParanoidi P18621.
    KOi K02880.
    OMAi YSREPTN.
    OrthoDBi EOG70GMHF.
    PhylomeDBi P18621.
    TreeFami TF300042.

    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

    GeneWikii RPL17.
    NextBioi 23849.
    PROi P18621.
    SOURCEi Search...

    Gene expression databases

    Bgeei P18621.
    CleanExi HS_RPL17.
    Genevestigatori P18621.

    Family and domain databases

    Gene3Di 3.90.470.10. 1 hit.
    HAMAPi MF_01331_A. Ribosomal_L22_A.
    InterProi IPR001063. Ribosomal_L22.
    IPR018260. Ribosomal_L22/L17_CS.
    IPR005721. Ribosomal_L22/L17_euk/arc.
    [Graphical view ]
    PANTHERi PTHR11593. PTHR11593. 1 hit.
    Pfami PF00237. Ribosomal_L22. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54843. SSF54843. 1 hit.
    TIGRFAMsi TIGR01038. L22_arch. 1 hit.
    PROSITEi PS00464. RIBOSOMAL_L22. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A human gene related to the ribosomal protein L23 gene of Halobacterium marismortui."
      Mager D.L., Freeman J.D.
      Nucleic Acids Res. 18:5301-5301(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Blood.
    2. "Isolation and characterization of a complementary DNA (PD-1) differentially expressed by human pancreatic ductal cell tumors."
      Batra S.K., Metzgar R.S., Hollingsworth M.A.
      Cell Growth Differ. 2:385-390(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Pancreatic tumor.
    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. "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] (ISOFORMS 1 AND 2).
      Tissue: Uterus.
    5. Li W.B., Gruber C., Jessee J., Polayes D.
      Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Neuroblastoma.
    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: Hypothalamus, Lung, Prostate and Testis.
    9. "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 2-10, IDENTIFICATION BY MASS SPECTROMETRY.
    10. Bienvenut W.V., Calvo F., Kolch W.
      Submitted (FEB-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-13; 31-42; 47-55; 75-82; 86-96 AND 106-124, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Cervix carcinoma.
    11. "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 170-183.
    12. "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.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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.
    15. "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-5, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

    Entry informationi

    Entry nameiRL17_HUMAN
    AccessioniPrimary (citable) accession number: P18621
    Secondary accession number(s): B2R4H3
    , B4E3C2, B5ME31, J3QL51, Q3KQW2, Q6NZ54, Q7M4M5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 153 of the entry and version 3 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 18
      Human chromosome 18: 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