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P36578

- RL4_HUMAN

UniProt

P36578 - RL4_HUMAN

Protein

60S ribosomal protein L4

Gene

RPL4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 5 (23 Jan 2007)
      Previous versions | rss
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    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 L4
    Alternative name(s):
    60S ribosomal protein L1
    Gene namesi
    Name:RPL4
    Synonyms:RPL1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:10353. RPL4.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. cytosolic large ribosomal subunit Source: UniProtKB
    4. extracellular vesicular exosome Source: UniProt
    5. membrane Source: UniProtKB
    6. nucleolus Source: HPA
    7. nucleus Source: UniProt
    8. ribonucleoprotein complex Source: MGI

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34749.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 42742660S ribosomal protein L4PRO_0000129350Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei14 – 141N6-acetyllysine1 Publication
    Modified residuei106 – 1061N6-acetyllysine1 Publication
    Modified residuei259 – 2591N6-acetyllysineBy similarity
    Modified residuei295 – 2951Phosphoserine2 Publications
    Modified residuei300 – 3001CitrullineBy similarity
    Modified residuei333 – 3331N6-acetyllysine1 Publication
    Modified residuei353 – 3531N6-acetyllysineBy similarity
    Modified residuei364 – 3641N6-acetyllysineBy similarity
    Modified residuei365 – 3651Phosphoserine2 Publications

    Post-translational modificationi

    Citrullinated by PADI4.By similarity

    Keywords - PTMi

    Acetylation, Citrullination, Phosphoprotein

    Proteomic databases

    MaxQBiP36578.
    PaxDbiP36578.
    PRIDEiP36578.

    2D gel databases

    SWISS-2DPAGEP36578.

    PTM databases

    PhosphoSiteiP36578.

    Miscellaneous databases

    PMAP-CutDBP36578.

    Expressioni

    Gene expression databases

    ArrayExpressiP36578.
    BgeeiP36578.
    CleanExiHS_RPL4.
    GenevestigatoriP36578.

    Organism-specific databases

    HPAiHPA034600.

    Interactioni

    Subunit structurei

    May bind IPO9 with low affinity. Interacts with RBM3 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HTTP428582EBI-348313,EBI-466029

    Protein-protein interaction databases

    BioGridi112044. 139 interactions.
    DIPiDIP-27559N.
    IntActiP36578. 33 interactions.
    MINTiMINT-1034893.
    STRINGi9606.ENSP00000311430.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3J3Belectron microscopy5.00C1-427[»]
    ProteinModelPortaliP36578.
    SMRiP36578. Positions 4-371.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi364 – 42764Lys-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ribosomal protein L4P family.Curated

    Phylogenomic databases

    eggNOGiCOG0088.
    HOVERGENiHBG001453.
    InParanoidiP36578.
    KOiK02930.
    OMAiKAKMLKP.
    OrthoDBiEOG73RBBP.
    PhylomeDBiP36578.
    TreeFamiTF300593.

    Family and domain databases

    Gene3Di3.40.1370.10. 1 hit.
    InterProiIPR025755. Ribos_L4_C_dom.
    IPR002136. Ribosomal_L4/L1e.
    IPR013000. Ribosomal_L4/L1e_euk/arc_CS.
    IPR023574. Ribosomal_L4_dom.
    [Graphical view]
    PfamiPF14374. Ribos_L4_asso_C. 1 hit.
    PF00573. Ribosomal_L4. 1 hit.
    [Graphical view]
    SUPFAMiSSF52166. SSF52166. 1 hit.
    PROSITEiPS00939. RIBOSOMAL_L1E. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P36578-1 [UniParc]FASTAAdd to Basket

    « Hide

    MACARPLISV YSEKGESSGK NVTLPAVFKA PIRPDIVNFV HTNLRKNNRQ    50
    PYAVSELAGH QTSAESWGTG RAVARIPRVR GGGTHRSGQG AFGNMCRGGR 100
    MFAPTKTWRR WHRRVNTTQK RYAICSALAA SALPALVMSK GHRIEEVPEL 150
    PLVVEDKVEG YKKTKEAVLL LKKLKAWNDI KKVYASQRMR AGKGKMRNRR 200
    RIQRRGPCII YNEDNGIIKA FRNIPGITLL NVSKLNILKL APGGHVGRFC 250
    IWTESAFRKL DELYGTWRKA ASLKSNYNLP MHKMINTDLS RILKSPEIQR 300
    ALRAPRKKIH RRVLKKNPLK NLRIMLKLNP YAKTMRRNTI LRQARNHKLR 350
    VDKAAAAAAA LQAKSDEKAA VAGKKPVVGK KGKKAAVGVK KQKKPLVGKK 400
    AAATKKPAPE KKPAEKKPTT EEKKPAA 427
    Length:427
    Mass (Da):47,697
    Last modified:January 23, 2007 - v5
    Checksum:i4785ED31699CD792
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31C → V in AAA60281. (PubMed:8268230)Curated
    Sequence conflicti36 – 361I → M in AAA60281. (PubMed:8268230)Curated
    Sequence conflicti63 – 631S → R in AAA60281. (PubMed:8268230)Curated
    Sequence conflicti147 – 1471V → F in AAA60281. (PubMed:8268230)Curated
    Sequence conflicti201 – 2011Missing in AAA60281. (PubMed:8268230)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L20868 mRNA. Translation: AAA60281.2.
    D23660 mRNA. Translation: BAA04887.1.
    AB061820 Genomic DNA. Translation: BAB79458.1.
    AK291117 mRNA. Translation: BAF83806.1.
    AK291859 mRNA. Translation: BAF84548.1.
    CH471082 Genomic DNA. Translation: EAW77776.1.
    BC001365 mRNA. Translation: AAH01365.1.
    BC005817 mRNA. Translation: AAH05817.1.
    BC007748 mRNA. Translation: AAH07748.1.
    BC007996 mRNA. Translation: AAH07996.1.
    BC009888 mRNA. Translation: AAH09888.1.
    BC010151 mRNA. Translation: AAH10151.1.
    BC014653 mRNA. Translation: AAH14653.1.
    BC066925 mRNA. Translation: AAH66925.1.
    BC095427 mRNA. Translation: AAH95427.1.
    CCDSiCCDS10218.1.
    PIRiT09551.
    RefSeqiNP_000959.2. NM_000968.3.
    UniGeneiHs.186350.
    Hs.644628.

    Genome annotation databases

    EnsembliENST00000307961; ENSP00000311430; ENSG00000174444.
    GeneIDi6124.
    KEGGihsa:6124.
    UCSCiuc002apv.3. human.

    Polymorphism databases

    DMDMi22002063.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L20868 mRNA. Translation: AAA60281.2 .
    D23660 mRNA. Translation: BAA04887.1 .
    AB061820 Genomic DNA. Translation: BAB79458.1 .
    AK291117 mRNA. Translation: BAF83806.1 .
    AK291859 mRNA. Translation: BAF84548.1 .
    CH471082 Genomic DNA. Translation: EAW77776.1 .
    BC001365 mRNA. Translation: AAH01365.1 .
    BC005817 mRNA. Translation: AAH05817.1 .
    BC007748 mRNA. Translation: AAH07748.1 .
    BC007996 mRNA. Translation: AAH07996.1 .
    BC009888 mRNA. Translation: AAH09888.1 .
    BC010151 mRNA. Translation: AAH10151.1 .
    BC014653 mRNA. Translation: AAH14653.1 .
    BC066925 mRNA. Translation: AAH66925.1 .
    BC095427 mRNA. Translation: AAH95427.1 .
    CCDSi CCDS10218.1.
    PIRi T09551.
    RefSeqi NP_000959.2. NM_000968.3.
    UniGenei Hs.186350.
    Hs.644628.

    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 C 1-427 [» ]
    ProteinModelPortali P36578.
    SMRi P36578. Positions 4-371.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112044. 139 interactions.
    DIPi DIP-27559N.
    IntActi P36578. 33 interactions.
    MINTi MINT-1034893.
    STRINGi 9606.ENSP00000311430.

    PTM databases

    PhosphoSitei P36578.

    Polymorphism databases

    DMDMi 22002063.

    2D gel databases

    SWISS-2DPAGE P36578.

    Proteomic databases

    MaxQBi P36578.
    PaxDbi P36578.
    PRIDEi P36578.

    Protocols and materials databases

    DNASUi 6124.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000307961 ; ENSP00000311430 ; ENSG00000174444 .
    GeneIDi 6124.
    KEGGi hsa:6124.
    UCSCi uc002apv.3. human.

    Organism-specific databases

    CTDi 6124.
    GeneCardsi GC15M066790.
    HGNCi HGNC:10353. RPL4.
    HPAi HPA034600.
    MIMi 180479. gene.
    neXtProti NX_P36578.
    PharmGKBi PA34749.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0088.
    HOVERGENi HBG001453.
    InParanoidi P36578.
    KOi K02930.
    OMAi KAKMLKP.
    OrthoDBi EOG73RBBP.
    PhylomeDBi P36578.
    TreeFami TF300593.

    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 RPL4. human.
    GeneWikii Ribosomal_protein_L4.
    GenomeRNAii 6124.
    NextBioi 23787.
    PMAP-CutDB P36578.
    PROi P36578.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P36578.
    Bgeei P36578.
    CleanExi HS_RPL4.
    Genevestigatori P36578.

    Family and domain databases

    Gene3Di 3.40.1370.10. 1 hit.
    InterProi IPR025755. Ribos_L4_C_dom.
    IPR002136. Ribosomal_L4/L1e.
    IPR013000. Ribosomal_L4/L1e_euk/arc_CS.
    IPR023574. Ribosomal_L4_dom.
    [Graphical view ]
    Pfami PF14374. Ribos_L4_asso_C. 1 hit.
    PF00573. Ribosomal_L4. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52166. SSF52166. 1 hit.
    PROSITEi PS00939. RIBOSOMAL_L1E. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human ribosomal protein L4: cloning and sequencing of the cDNA and primary structure of the protein."
      Bagni C., Mariottini P., Annesi F., Amaldi F.
      Biochim. Biophys. Acta 1216:475-478(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. Bagni C.
      Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. Kato S.
      Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lymphoma.
    4. "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].
    5. "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].
      Tissue: Skeletal muscle.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Colon, Embryonic stem cell, Eye, Hippocampus, Muscle, Pancreas and Skin.
    8. Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.
      Submitted (MAY-2006) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-13, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: T-cell.
    9. "Importins fulfill a dual function as nuclear import receptors and cytoplasmic chaperones for exposed basic domains."
      Jaekel S., Mingot J.-M., Schwarzmaier P., Hartmann E., Goerlich D.
      EMBO J. 21:377-386(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IPO9.
    10. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295 AND SER-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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].
    13. "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-14; LYS-106 AND LYS-333, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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-295 AND SER-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

    Entry informationi

    Entry nameiRL4_HUMAN
    AccessioniPrimary (citable) accession number: P36578
    Secondary accession number(s): A8K502
    , P39029, Q4VBR0, Q969Z9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 148 of the entry and version 5 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 15
      Human chromosome 15: 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