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P62899

- RL31_HUMAN

UniProt

P62899 - RL31_HUMAN

Protein

60S ribosomal protein L31

Gene

RPL31

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. RNA binding Source: ProtInc
    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 L31
    Gene namesi
    Name:RPL31
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:10334. RPL31.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. cytosolic large ribosomal subunit Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. membrane Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34715.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12512560S ribosomal protein L31PRO_0000153763Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei55 – 551N6-succinyllysineBy similarity
    Modified residuei70 – 701N6-succinyllysineBy similarity
    Modified residuei75 – 751N6-acetyllysine; alternate1 Publication
    Modified residuei75 – 751N6-succinyllysine; alternateBy similarity
    Modified residuei98 – 981Phosphoserine3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP62899.
    PaxDbiP62899.
    PRIDEiP62899.

    2D gel databases

    SWISS-2DPAGEP62899.

    PTM databases

    PhosphoSiteiP62899.

    Expressioni

    Gene expression databases

    ArrayExpressiP62899.
    BgeeiP62899.
    CleanExiHS_RPL31.
    GenevestigatoriP62899.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ASF1BQ9NVP21EBI-1053664,EBI-1055650
    CNBPP626331EBI-1053664,EBI-1047529
    DDX56Q9NY931EBI-1053664,EBI-372376
    LYARQ9NX581EBI-1053664,EBI-713507
    MAGEB2O154791EBI-1053664,EBI-1057615
    PINX1Q96BK51EBI-1053664,EBI-721782
    PSTPIP1O435861EBI-1053664,EBI-1050964
    WBP5Q9UHQ71EBI-1053664,EBI-1051372
    YWHAZP631041EBI-1053664,EBI-347088

    Protein-protein interaction databases

    BioGridi112079. 120 interactions.
    IntActiP62899. 25 interactions.
    MINTiMINT-5000327.
    STRINGi9606.ENSP00000386717.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3J3Belectron microscopy5.00d1-125[»]
    ProteinModelPortaliP62899.
    SMRiP62899. Positions 12-124.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L31e family.Curated

    Phylogenomic databases

    eggNOGiCOG2097.
    HOGENOMiHOG000216660.
    HOVERGENiHBG001549.
    KOiK02910.
    OMAiHIWSKGI.
    PhylomeDBiP62899.
    TreeFamiTF314858.

    Family and domain databases

    Gene3Di3.10.440.10. 1 hit.
    InterProiIPR000054. Ribosomal_L31e.
    IPR020052. Ribosomal_L31e_CS.
    IPR023621. Ribosomal_L31e_dom.
    [Graphical view]
    PANTHERiPTHR10956. PTHR10956. 1 hit.
    PfamiPF01198. Ribosomal_L31e. 1 hit.
    [Graphical view]
    ProDomiPD006030. Ribosomal_L31e. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF54575. SSF54575. 1 hit.
    PROSITEiPS01144. RIBOSOMAL_L31E. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P62899-1) [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

    MAPAKKGGEK KKGRSAINEV VTREYTINIH KRIHGVGFKK RAPRALKEIR    50
    KFAMKEMGTP DVRIDTRLNK AVWAKGIRNV PYRIRVRLSR KRNEDEDSPN 100
    KLYTLVTYVP VTTFKNLQTV NVDEN 125
    Length:125
    Mass (Da):14,463
    Last modified:August 31, 2004 - v1
    Checksum:iBA9DBE79B9E1C071
    GO
    Isoform 2 (identifier: P62899-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         116-125: NLQTVNVDEN → ISVLNSVTVAKSP

    Note: No experimental confirmation available.

    Show »
    Length:128
    Mass (Da):14,632
    Checksum:i73178D90B1AE79A8
    GO
    Isoform 3 (identifier: P62899-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         116-125: NLQTVNVDEN → SKFSIP

    Note: No experimental confirmation available.

    Show »
    Length:121
    Mass (Da):13,995
    Checksum:iBAD3547E9019CF61
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei116 – 12510NLQTVNVDEN → ISVLNSVTVAKSP in isoform 2. 1 PublicationVSP_042572
    Alternative sequencei116 – 12510NLQTVNVDEN → SKFSIP in isoform 3. 1 PublicationVSP_043224

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15940 mRNA. Translation: CAA34066.1.
    AB061830 Genomic DNA. Translation: BAB79468.1.
    AK297483 mRNA. Translation: BAH12588.1.
    AC016738 Genomic DNA. Translation: AAY14823.1.
    CH471127 Genomic DNA. Translation: EAX01826.1.
    CH471127 Genomic DNA. Translation: EAX01827.1.
    CH471127 Genomic DNA. Translation: EAX01829.1.
    BC017343 mRNA. Translation: AAH17343.1.
    BC070210 mRNA. Translation: AAH70210.1.
    BC070373 mRNA. Translation: AAH70373.1.
    X69181 mRNA. Translation: CAA48925.1.
    CCDSiCCDS2049.1. [P62899-1]
    CCDS46373.1. [P62899-2]
    CCDS46374.1. [P62899-3]
    PIRiS05576. R5HU31.
    RefSeqiNP_000984.1. NM_000993.4. [P62899-1]
    NP_001092047.1. NM_001098577.2. [P62899-2]
    NP_001093163.1. NM_001099693.1. [P62899-3]
    UniGeneiHs.469473.

    Genome annotation databases

    EnsembliENST00000264258; ENSP00000264258; ENSG00000071082. [P62899-1]
    ENST00000409028; ENSP00000386717; ENSG00000071082. [P62899-2]
    ENST00000409320; ENSP00000387163; ENSG00000071082. [P62899-3]
    ENST00000409733; ENSP00000386681; ENSG00000071082. [P62899-1]
    GeneIDi6160.
    KEGGihsa:6160.
    UCSCiuc002taq.4. human. [P62899-1]
    uc002tar.4. human. [P62899-3]
    uc010fiu.1. human. [P62899-2]

    Polymorphism databases

    DMDMi51702807.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15940 mRNA. Translation: CAA34066.1 .
    AB061830 Genomic DNA. Translation: BAB79468.1 .
    AK297483 mRNA. Translation: BAH12588.1 .
    AC016738 Genomic DNA. Translation: AAY14823.1 .
    CH471127 Genomic DNA. Translation: EAX01826.1 .
    CH471127 Genomic DNA. Translation: EAX01827.1 .
    CH471127 Genomic DNA. Translation: EAX01829.1 .
    BC017343 mRNA. Translation: AAH17343.1 .
    BC070210 mRNA. Translation: AAH70210.1 .
    BC070373 mRNA. Translation: AAH70373.1 .
    X69181 mRNA. Translation: CAA48925.1 .
    CCDSi CCDS2049.1. [P62899-1 ]
    CCDS46373.1. [P62899-2 ]
    CCDS46374.1. [P62899-3 ]
    PIRi S05576. R5HU31.
    RefSeqi NP_000984.1. NM_000993.4. [P62899-1 ]
    NP_001092047.1. NM_001098577.2. [P62899-2 ]
    NP_001093163.1. NM_001099693.1. [P62899-3 ]
    UniGenei Hs.469473.

    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 d 1-125 [» ]
    ProteinModelPortali P62899.
    SMRi P62899. Positions 12-124.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112079. 120 interactions.
    IntActi P62899. 25 interactions.
    MINTi MINT-5000327.
    STRINGi 9606.ENSP00000386717.

    PTM databases

    PhosphoSitei P62899.

    Polymorphism databases

    DMDMi 51702807.

    2D gel databases

    SWISS-2DPAGE P62899.

    Proteomic databases

    MaxQBi P62899.
    PaxDbi P62899.
    PRIDEi P62899.

    Protocols and materials databases

    DNASUi 6160.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264258 ; ENSP00000264258 ; ENSG00000071082 . [P62899-1 ]
    ENST00000409028 ; ENSP00000386717 ; ENSG00000071082 . [P62899-2 ]
    ENST00000409320 ; ENSP00000387163 ; ENSG00000071082 . [P62899-3 ]
    ENST00000409733 ; ENSP00000386681 ; ENSG00000071082 . [P62899-1 ]
    GeneIDi 6160.
    KEGGi hsa:6160.
    UCSCi uc002taq.4. human. [P62899-1 ]
    uc002tar.4. human. [P62899-3 ]
    uc010fiu.1. human. [P62899-2 ]

    Organism-specific databases

    CTDi 6160.
    GeneCardsi GC02P101618.
    H-InvDB HIX0017577.
    HGNCi HGNC:10334. RPL31.
    neXtProti NX_P62899.
    PharmGKBi PA34715.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2097.
    HOGENOMi HOG000216660.
    HOVERGENi HBG001549.
    KOi K02910.
    OMAi HIWSKGI.
    PhylomeDBi P62899.
    TreeFami TF314858.

    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 RPL31. human.
    GeneWikii 60S_ribosomal_protein_L31.
    GenomeRNAii 6160.
    NextBioi 23923.
    PROi P62899.

    Gene expression databases

    ArrayExpressi P62899.
    Bgeei P62899.
    CleanExi HS_RPL31.
    Genevestigatori P62899.

    Family and domain databases

    Gene3Di 3.10.440.10. 1 hit.
    InterProi IPR000054. Ribosomal_L31e.
    IPR020052. Ribosomal_L31e_CS.
    IPR023621. Ribosomal_L31e_dom.
    [Graphical view ]
    PANTHERi PTHR10956. PTHR10956. 1 hit.
    Pfami PF01198. Ribosomal_L31e. 1 hit.
    [Graphical view ]
    ProDomi PD006030. Ribosomal_L31e. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF54575. SSF54575. 1 hit.
    PROSITEi PS01144. RIBOSOMAL_L31E. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "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].
    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] (ISOFORM 2).
      Tissue: Brain.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [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: Brain, Liver and Prostate.
    7. "Identification of a human ribosomal protein mRNA with increased expression in colorectal tumours."
      Chester K.A., Robson L., Beyent R.H.J., Talbot I.C., Pringle J.H., Primrose L., Macpherson A.J.S., Boxer G., Southhall P., Malcolm A.D.B.
      Biochim. Biophys. Acta 1009:297-300(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-125 (ISOFORM 1).
    8. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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.
    12. "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-75, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

    Entry informationi

    Entry nameiRL31_HUMAN
    AccessioniPrimary (citable) accession number: P62899
    Secondary accession number(s): B7Z4K2
    , D3DVJ4, P12947, Q53SQ5, Q6IRZ0, Q6LBJ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 31, 2004
    Last sequence update: August 31, 2004
    Last modified: October 1, 2014
    This is version 109 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Ribosomal proteins
      Ribosomal proteins families and list of entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3