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P46779

- RL28_HUMAN

UniProt

P46779 - RL28_HUMAN

Protein

60S ribosomal protein L28

Gene

RPL28

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

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. RNA binding Source: ProtInc
    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

    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 L28
    Gene namesi
    Name:RPL28
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:10330. RPL28.

    Subcellular locationi

    GO - Cellular componenti

    1. cell body Source: ParkinsonsUK-UCL
    2. cytoplasm Source: HPA
    3. cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
    4. cytosol Source: Reactome
    5. cytosolic large ribosomal subunit Source: UniProtKB
    6. dendrite Source: ParkinsonsUK-UCL
    7. extracellular vesicular exosome Source: UniProt
    8. membrane Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34710.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 13713660S ribosomal protein L28PRO_0000122389Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine4 Publications
    Modified residuei115 – 1151Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP46779.
    PaxDbiP46779.
    PeptideAtlasiP46779.
    PRIDEiP46779.

    PTM databases

    PhosphoSiteiP46779.

    Miscellaneous databases

    PMAP-CutDBP46779.

    Expressioni

    Gene expression databases

    ArrayExpressiP46779.
    BgeeiP46779.
    CleanExiHS_RPL28.
    GenevestigatoriP46779.

    Organism-specific databases

    HPAiHPA050459.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DCCP431463EBI-366357,EBI-1222919

    Protein-protein interaction databases

    BioGridi112077. 34 interactions.
    IntActiP46779. 23 interactions.
    MINTiMINT-5004261.
    STRINGi9606.ENSP00000401450.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3J3Belectron microscopy5.00r1-137[»]
    ProteinModelPortaliP46779.
    SMRiP46779. Positions 1-137.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L28e family.Curated

    Phylogenomic databases

    eggNOGiNOG148062.
    HOGENOMiHOG000200513.
    HOVERGENiHBG000701.
    InParanoidiP46779.
    KOiK02903.
    OMAiWLIIRNN.
    OrthoDBiEOG74N5JT.
    PhylomeDBiP46779.
    TreeFamiTF300173.

    Family and domain databases

    InterProiIPR029004. L28e/Mak16.
    IPR002672. Ribosomal_L28e.
    [Graphical view]
    PANTHERiPTHR10544. PTHR10544. 1 hit.
    PfamiPF01778. Ribosomal_L28e. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

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

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P46779-1) [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

    MSAHLQWMVV RNCSSFLIKR NKQTYSTEPN NLKARNSFRY NGLIHRKTVG    50
    VEPAADGKGV VVVIKRRSGQ RKPATSYVRT TINKNARATL SSIRHMIRKN 100
    KYRPDLRMAA IRRASAILRS QKPVMVKRKR TRPTKSS 137
    Length:137
    Mass (Da):15,748
    Last modified:January 23, 2007 - v3
    Checksum:i44DCDE45473D7C7B
    GO
    Isoform 2 (identifier: P46779-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         109-137: AAIRRASAILRSQKPVMVKRKRTRPTKSS → VSWGLGIRLG...PRGRLVECMG

    Note: No experimental confirmation available.

    Show »
    Length:163
    Mass (Da):18,430
    Checksum:i1C9BD1FA0A0E14EE
    GO
    Isoform 3 (identifier: P46779-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         109-137: AAIRRASAILRSQKPVMVKRKRTRPTKSS → DMLASTGSGL...QNLLDCAHKS

    Note: No experimental confirmation available.

    Show »
    Length:169
    Mass (Da):19,148
    Checksum:iD4D6E5C7F4116D16
    GO
    Isoform 4 (identifier: P46779-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         69-137: GQRKPATSYVRTTINKNARATLSSIRHMIRKNKYRPDLRMAAIRRASAILRSQKPVMVKRKRTRPTKSS → E

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

    Show »
    Length:69
    Mass (Da):7,888
    Checksum:iEDE20EE54DFE31FE
    GO
    Isoform 5 (identifier: P46779-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         70-137: QRKPATSYVR...RKRTRPTKSS → EFCLVWARERPLSRVWEL

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

    Show »
    Length:87
    Mass (Da):10,088
    Checksum:i791604CE95F509E2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti84 – 841K → R in AAH10182. (PubMed:15489334)Curated
    Sequence conflicti120 – 1201S → T in AAA85657. (PubMed:7772601)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti66 – 661R → L.
    Corresponds to variant rs13502 [ dbSNP | Ensembl ].
    VAR_034460

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei69 – 13769GQRKP…PTKSS → E in isoform 4. CuratedVSP_047026Add
    BLAST
    Alternative sequencei70 – 13768QRKPA…PTKSS → EFCLVWARERPLSRVWEL in isoform 5. CuratedVSP_047027Add
    BLAST
    Alternative sequencei109 – 13729AAIRR…PTKSS → VSWGLGIRLGETGQCCGEGP PTTGCNMGWRGMDSCFQPTP HTQHWPRGRLVECMG in isoform 2. 1 PublicationVSP_043026Add
    BLAST
    Alternative sequencei109 – 13729AAIRR…PTKSS → DMLASTGSGLCCSVAVQPWA SSSTSLCLRTLICNMRVDRP YYSGLMRRLNVQNLLDCAHK S in isoform 3. 1 PublicationVSP_046173Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U14969 mRNA. Translation: AAA85657.1.
    CR457024 mRNA. Translation: CAG33305.1.
    AK311760 mRNA. Translation: BAG34703.1.
    AK293736 mRNA. Translation: BAG57160.1.
    AC020922 Genomic DNA. No translation available.
    CH471135 Genomic DNA. Translation: EAW72374.1.
    CH471135 Genomic DNA. Translation: EAW72375.1.
    CH471135 Genomic DNA. Translation: EAW72376.1.
    BC010173 mRNA. Translation: AAH10173.1.
    BC010182 mRNA. Translation: AAH10182.1.
    BC011582 mRNA. Translation: AAH11582.1.
    BG777550 mRNA. No translation available.
    CCDSiCCDS12924.1. [P46779-1]
    CCDS46189.1. [P46779-3]
    CCDS46190.1. [P46779-2]
    CCDS46191.1. [P46779-4]
    CCDS46192.1. [P46779-5]
    PIRiS55915.
    RefSeqiNP_000982.2. NM_000991.4. [P46779-1]
    NP_001129606.1. NM_001136134.1. [P46779-2]
    NP_001129607.1. NM_001136135.1. [P46779-3]
    NP_001129608.1. NM_001136136.1. [P46779-5]
    NP_001129609.1. NM_001136137.1. [P46779-4]
    UniGeneiHs.652114.

    Genome annotation databases

    EnsembliENST00000344063; ENSP00000342787; ENSG00000108107. [P46779-1]
    ENST00000428193; ENSP00000391665; ENSG00000108107. [P46779-4]
    ENST00000431533; ENSP00000400596; ENSG00000108107. [P46779-5]
    ENST00000558815; ENSP00000452909; ENSG00000108107. [P46779-3]
    ENST00000559463; ENSP00000453319; ENSG00000108107. [P46779-1]
    ENST00000560583; ENSP00000453029; ENSG00000108107. [P46779-2]
    GeneIDi6158.
    KEGGihsa:6158.
    UCSCiuc002qkv.3. human. [P46779-1]
    uc010yfy.1. human.
    uc010yfz.2. human.
    uc010yga.2. human.
    uc010ygb.2. human. [P46779-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U14969 mRNA. Translation: AAA85657.1 .
    CR457024 mRNA. Translation: CAG33305.1 .
    AK311760 mRNA. Translation: BAG34703.1 .
    AK293736 mRNA. Translation: BAG57160.1 .
    AC020922 Genomic DNA. No translation available.
    CH471135 Genomic DNA. Translation: EAW72374.1 .
    CH471135 Genomic DNA. Translation: EAW72375.1 .
    CH471135 Genomic DNA. Translation: EAW72376.1 .
    BC010173 mRNA. Translation: AAH10173.1 .
    BC010182 mRNA. Translation: AAH10182.1 .
    BC011582 mRNA. Translation: AAH11582.1 .
    BG777550 mRNA. No translation available.
    CCDSi CCDS12924.1. [P46779-1 ]
    CCDS46189.1. [P46779-3 ]
    CCDS46190.1. [P46779-2 ]
    CCDS46191.1. [P46779-4 ]
    CCDS46192.1. [P46779-5 ]
    PIRi S55915.
    RefSeqi NP_000982.2. NM_000991.4. [P46779-1 ]
    NP_001129606.1. NM_001136134.1. [P46779-2 ]
    NP_001129607.1. NM_001136135.1. [P46779-3 ]
    NP_001129608.1. NM_001136136.1. [P46779-5 ]
    NP_001129609.1. NM_001136137.1. [P46779-4 ]
    UniGenei Hs.652114.

    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 r 1-137 [» ]
    ProteinModelPortali P46779.
    SMRi P46779. Positions 1-137.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112077. 34 interactions.
    IntActi P46779. 23 interactions.
    MINTi MINT-5004261.
    STRINGi 9606.ENSP00000401450.

    PTM databases

    PhosphoSitei P46779.

    Proteomic databases

    MaxQBi P46779.
    PaxDbi P46779.
    PeptideAtlasi P46779.
    PRIDEi P46779.

    Protocols and materials databases

    DNASUi 6158.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000344063 ; ENSP00000342787 ; ENSG00000108107 . [P46779-1 ]
    ENST00000428193 ; ENSP00000391665 ; ENSG00000108107 . [P46779-4 ]
    ENST00000431533 ; ENSP00000400596 ; ENSG00000108107 . [P46779-5 ]
    ENST00000558815 ; ENSP00000452909 ; ENSG00000108107 . [P46779-3 ]
    ENST00000559463 ; ENSP00000453319 ; ENSG00000108107 . [P46779-1 ]
    ENST00000560583 ; ENSP00000453029 ; ENSG00000108107 . [P46779-2 ]
    GeneIDi 6158.
    KEGGi hsa:6158.
    UCSCi uc002qkv.3. human. [P46779-1 ]
    uc010yfy.1. human.
    uc010yfz.2. human.
    uc010yga.2. human.
    uc010ygb.2. human. [P46779-2 ]

    Organism-specific databases

    CTDi 6158.
    GeneCardsi GC19P055897.
    HGNCi HGNC:10330. RPL28.
    HPAi HPA050459.
    MIMi 603638. gene.
    neXtProti NX_P46779.
    PharmGKBi PA34710.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG148062.
    HOGENOMi HOG000200513.
    HOVERGENi HBG000701.
    InParanoidi P46779.
    KOi K02903.
    OMAi WLIIRNN.
    OrthoDBi EOG74N5JT.
    PhylomeDBi P46779.
    TreeFami TF300173.

    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 RPL28. human.
    GeneWikii 60S_ribosomal_protein_L28.
    GenomeRNAii 6158.
    NextBioi 23915.
    PMAP-CutDB P46779.
    PROi P46779.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P46779.
    Bgeei P46779.
    CleanExi HS_RPL28.
    Genevestigatori P46779.

    Family and domain databases

    InterProi IPR029004. L28e/Mak16.
    IPR002672. Ribosomal_L28e.
    [Graphical view ]
    PANTHERi PTHR10544. PTHR10544. 1 hit.
    Pfami PF01778. Ribosomal_L28e. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9, S10 and S29 human ribosomal protein mRNAs."
      Frigerio J.-M., Dagorn J.-C., Iovanna J.L.
      Biochim. Biophys. Acta 1262:64-68(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Colon.
    2. "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] (ISOFORM 1).
    3. "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: Cerebellum and Hippocampus.
    4. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORMS 1 AND 3).
      Tissue: B-cell, Kidney, Prostatic adenocarcinoma and Uterus.
    7. Cited for: PROTEIN SEQUENCE OF 2-11; 23-33; 40-58; 72-79 AND 120-127, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Hepatoma and Ovarian carcinoma.
    8. "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: ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    9. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "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-115, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

    Entry informationi

    Entry nameiRL28_HUMAN
    AccessioniPrimary (citable) accession number: P46779
    Secondary accession number(s): B2R4A6
    , B4DEP9, C9JB50, E9PB24, G5E9L2, Q6IAY0, Q96FX1, Q9BWQ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 136 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 19
      Human chromosome 19: 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