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P40429

- RL13A_HUMAN

UniProt

P40429 - RL13A_HUMAN

Protein

60S ribosomal protein L13a

Gene

RPL13A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Associated with ribosomes but is not required for canonical ribosome function and has extra-ribosomal functions. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the ribosome and assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation. In the GAIT complex interacts with m7G cap-bound eIF4G at or near the eIF3-binding site and blocks the recruitment of the 43S ribosomal complex. Involved in methylation of rRNA.4 Publications

    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. cellular response to interferon-gamma Source: UniProtKB
    3. gene expression Source: Reactome
    4. mRNA metabolic process Source: Reactome
    5. negative regulation of formation of translation preinitiation complex Source: UniProtKB
    6. negative regulation of translation Source: UniProtKB
    7. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
    8. RNA metabolic process Source: Reactome
    9. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
    10. translation Source: UniProtKB
    11. translational elongation Source: Reactome
    12. translational initiation Source: Reactome
    13. translational termination Source: Reactome
    14. viral life cycle Source: Reactome
    15. viral process Source: Reactome
    16. viral transcription Source: Reactome

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Biological processi

    Translation regulation

    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 L13a
    Alternative name(s):
    23 kDa highly basic protein
    Gene namesi
    Name:RPL13A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:10304. RPL13A.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. cytosolic large ribosomal subunit Source: UniProtKB
    3. GAIT complex Source: UniProtKB
    4. large ribosomal subunit Source: ProtInc
    5. membrane Source: UniProtKB
    6. nucleus Source: UniProt
    7. ribonucleoprotein complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi77 – 771S → A: Loss of interferon-gamma induced phosphorylation. 1 Publication

    Organism-specific databases

    PharmGKBiPA38122.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed5 Publications
    Chaini2 – 20320260S ribosomal protein L13aPRO_0000133769Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine5 Publications
    Modified residuei59 – 591CitrullineBy similarity
    Modified residuei77 – 771Phosphoserine; by ZIPK/DAPK32 Publications
    Modified residuei140 – 1401CitrullineBy similarity
    Modified residuei191 – 1911N6-acetyllysine1 Publication

    Post-translational modificationi

    Phosphorylation at Ser-77 upon interferon-gamma treatment in monocytes involves a DAPK1-DAPK3 kinase cascade and is causing release from the ribosome, association with the GAIT complex and subsequent involvement in transcript-selective translation inhibition.2 Publications
    Citrullinated by PADI4.By similarity

    Keywords - PTMi

    Acetylation, Citrullination, Phosphoprotein

    Proteomic databases

    MaxQBiP40429.
    PaxDbiP40429.
    PRIDEiP40429.

    PTM databases

    PhosphoSiteiP40429.

    Expressioni

    Gene expression databases

    BgeeiP40429.
    CleanExiHS_RPL13A.
    GenevestigatoriP40429.

    Organism-specific databases

    HPAiHPA038751.

    Interactioni

    Subunit structurei

    Component of the 60S ribosome. Component of the GAIT complex. Interacts with EIF4G1.3 Publications

    Protein-protein interaction databases

    BioGridi117068. 39 interactions.
    IntActiP40429. 24 interactions.
    MINTiMINT-1417412.
    STRINGi9606.ENSP00000375730.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3J3Belectron microscopy5.00O1-203[»]
    ProteinModelPortaliP40429.
    SMRiP40429. Positions 2-203.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L13P family.Curated

    Phylogenomic databases

    eggNOGiCOG0102.
    HOGENOMiHOG000225289.
    HOVERGENiHBG062176.
    InParanoidiP40429.
    KOiK02872.
    OrthoDBiEOG7H1JMP.
    PhylomeDBiP40429.
    TreeFamiTF300159.

    Family and domain databases

    Gene3Di3.90.1180.10. 1 hit.
    HAMAPiMF_01366. Ribosomal_L13.
    InterProiIPR005822. Ribosomal_L13.
    IPR023563. Ribosomal_L13_CS.
    IPR023564. Ribosomal_L13_dom.
    IPR005755. Ribosomal_L13_euk/arc.
    [Graphical view]
    PANTHERiPTHR11545. PTHR11545. 1 hit.
    PTHR11545:SF3. PTHR11545:SF3. 1 hit.
    PfamiPF00572. Ribosomal_L13. 1 hit.
    [Graphical view]
    SUPFAMiSSF52161. SSF52161. 1 hit.
    TIGRFAMsiTIGR01077. L13_A_E. 1 hit.
    PROSITEiPS00783. RIBOSOMAL_L13. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P40429-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEVQVLVLD GRGHLLGRLA AIVAKQVLLG RKVVVVRCEG INISGNFYRN    50
    KLKYLAFLRK RMNTNPSRGP YHFRAPSRIF WRTVRGMLPH KTKRGQAALD 100
    RLKVFDGIPP PYDKKKRMVV PAALKVVRLK PTRKFAYLGR LAHEVGWKYQ 150
    AVTATLEEKR KEKAKIHYRK KKQLMRLRKQ AEKNVEKKID KYTEVLKTHG 200
    LLV 203
    Length:203
    Mass (Da):23,577
    Last modified:January 23, 2007 - v2
    Checksum:i3E80D0AB77A0D406
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56932 mRNA. Translation: CAA40254.1.
    AB028893 Genomic DNA. Translation: BAA88214.1.
    AK291120 mRNA. Translation: BAF83809.1.
    CH471177 Genomic DNA. Translation: EAW52495.1.
    BC000514 mRNA. Translation: AAH00514.1.
    BC001675 mRNA. Translation: AAH01675.1.
    BC001836 mRNA. Translation: AAH01836.1.
    BC062537 mRNA. Translation: AAH62537.1.
    BC065236 mRNA. Translation: AAH65236.1.
    BC070223 mRNA. Translation: AAH70223.1.
    BC071929 mRNA. Translation: AAH71929.1.
    CCDSiCCDS12768.1.
    PIRiS29539.
    RefSeqiNP_001257420.1. NM_001270491.1.
    NP_036555.1. NM_012423.3.
    UniGeneiHs.523185.

    Genome annotation databases

    EnsembliENST00000391857; ENSP00000375730; ENSG00000142541.
    GeneIDi23521.
    KEGGihsa:23521.
    UCSCiuc002pny.4. human.

    Polymorphism databases

    DMDMi730451.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56932 mRNA. Translation: CAA40254.1 .
    AB028893 Genomic DNA. Translation: BAA88214.1 .
    AK291120 mRNA. Translation: BAF83809.1 .
    CH471177 Genomic DNA. Translation: EAW52495.1 .
    BC000514 mRNA. Translation: AAH00514.1 .
    BC001675 mRNA. Translation: AAH01675.1 .
    BC001836 mRNA. Translation: AAH01836.1 .
    BC062537 mRNA. Translation: AAH62537.1 .
    BC065236 mRNA. Translation: AAH65236.1 .
    BC070223 mRNA. Translation: AAH70223.1 .
    BC071929 mRNA. Translation: AAH71929.1 .
    CCDSi CCDS12768.1.
    PIRi S29539.
    RefSeqi NP_001257420.1. NM_001270491.1.
    NP_036555.1. NM_012423.3.
    UniGenei Hs.523185.

    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 O 1-203 [» ]
    ProteinModelPortali P40429.
    SMRi P40429. Positions 2-203.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117068. 39 interactions.
    IntActi P40429. 24 interactions.
    MINTi MINT-1417412.
    STRINGi 9606.ENSP00000375730.

    PTM databases

    PhosphoSitei P40429.

    Polymorphism databases

    DMDMi 730451.

    Proteomic databases

    MaxQBi P40429.
    PaxDbi P40429.
    PRIDEi P40429.

    Protocols and materials databases

    DNASUi 23521.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000391857 ; ENSP00000375730 ; ENSG00000142541 .
    GeneIDi 23521.
    KEGGi hsa:23521.
    UCSCi uc002pny.4. human.

    Organism-specific databases

    CTDi 23521.
    GeneCardsi GC19P049991.
    H-InvDB HIX0027968.
    HIX0158081.
    HGNCi HGNC:10304. RPL13A.
    HPAi HPA038751.
    neXtProti NX_P40429.
    PharmGKBi PA38122.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0102.
    HOGENOMi HOG000225289.
    HOVERGENi HBG062176.
    InParanoidi P40429.
    KOi K02872.
    OrthoDBi EOG7H1JMP.
    PhylomeDBi P40429.
    TreeFami TF300159.

    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 RPL13A. human.
    GeneWikii RPL13A.
    GenomeRNAii 23521.
    NextBioi 45973.
    PROi P40429.

    Gene expression databases

    Bgeei P40429.
    CleanExi HS_RPL13A.
    Genevestigatori P40429.

    Family and domain databases

    Gene3Di 3.90.1180.10. 1 hit.
    HAMAPi MF_01366. Ribosomal_L13.
    InterProi IPR005822. Ribosomal_L13.
    IPR023563. Ribosomal_L13_CS.
    IPR023564. Ribosomal_L13_dom.
    IPR005755. Ribosomal_L13_euk/arc.
    [Graphical view ]
    PANTHERi PTHR11545. PTHR11545. 1 hit.
    PTHR11545:SF3. PTHR11545:SF3. 1 hit.
    Pfami PF00572. Ribosomal_L13. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52161. SSF52161. 1 hit.
    TIGRFAMsi TIGR01077. L13_A_E. 1 hit.
    PROSITEi PS00783. RIBOSOMAL_L13. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Conservation of a 23-kDa human transplantation antigen in mammalian species."
      Price S.R., Nightingale M.S., Bobak D.A., Tsuchiya M., Moss J., Vaughan M.
      Genomics 14:959-964(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Gene organization and sequence of the region containing the ribosomal protein genes RPL13A and RPS11 in the human genome and conserved features in the mouse genome."
      Higa S., Yoshihama M., Tanaka T., Kenmochi N.
      Gene 240:371-377(1999) [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].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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].
      Tissue: Lung, Lymph, Muscle, Pancreas and Skin.
    6. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-12; 38-49; 104-115 AND 135-159, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Cervix carcinoma.
    7. "Regulated release of L13a from the 60S ribosomal subunit as a mechanism of transcript-specific translational control."
      Mazumder B., Sampath P., Seshadri V., Maitra R.K., DiCorleto P.E., Fox P.L.
      Cell 115:187-198(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, PHOSPHORYLATION.
    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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    9. "Noncanonical function of glutamyl-prolyl-tRNA synthetase: gene-specific silencing of translation."
      Sampath P., Mazumder B., Seshadri V., Gerber C.A., Chavatte L., Kinter M., Ting S.M., Dignam J.D., Kim S., Driscoll D.M., Fox P.L.
      Cell 119:195-208(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE GAIT COMPLEX.
    10. "L13a blocks 48S assembly: role of a general initiation factor in mRNA-specific translational control."
      Kapasi P., Chaudhuri S., Vyas K., Baus D., Komar A.A., Fox P.L., Merrick W.C., Mazumder B.
      Mol. Cell 25:113-126(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EIF4G1.
    11. "Human ribosomal protein L13a is dispensable for canonical ribosome function but indispensable for efficient rRNA methylation."
      Chaudhuri S., Vyas K., Kapasi P., Komar A.A., Dinman J.D., Barik S., Mazumder B.
      RNA 13:2224-2237(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "DAPK-ZIPK-L13a axis constitutes a negative-feedback module regulating inflammatory gene expression."
      Mukhopadhyay R., Ray P.S., Arif A., Brady A.K., Kinter M., Fox P.L.
      Mol. Cell 32:371-382(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-77, MUTAGENESIS OF SER-77.
    13. "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].
    14. "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-191, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Heterotrimeric GAIT complex drives transcript-selective translation inhibition in murine macrophages."
      Arif A., Chatterjee P., Moodt R.A., Fox P.L.
      Mol. Cell. Biol. 32:5046-5055(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, RECONSTITUTION OF THE GAIT COMPLEX.
    17. "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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.

    Entry informationi

    Entry nameiRL13A_HUMAN
    AccessioniPrimary (citable) accession number: P40429
    Secondary accession number(s): A8K505
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 137 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 19
      Human chromosome 19: 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