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Q9NQT4

- EXOS5_HUMAN

UniProt

Q9NQT4 - EXOS5_HUMAN

Protein

Exosome complex component RRP46

Gene

EXOSC5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes.2 Publications

    GO - Molecular functioni

    1. 3'-5'-exoribonuclease activity Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. defense response to virus Source: MGI
    2. DNA deamination Source: UniProtKB
    3. exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Source: UniProtKB
    4. gene expression Source: Reactome
    5. mRNA metabolic process Source: Reactome
    6. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
    7. RNA metabolic process Source: Reactome
    8. RNA phosphodiester bond hydrolysis, exonucleolytic Source: GOC
    9. rRNA processing Source: UniProtKB

    Keywords - Biological processi

    rRNA processing

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_18355. ATF4 activates genes.
    REACT_20619. mRNA decay by 3' to 5' exoribonuclease.
    REACT_24915. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
    REACT_25042. KSRP destabilizes mRNA.
    REACT_25064. Tristetraprolin (TTP) destabilizes mRNA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Exosome complex component RRP46
    Alternative name(s):
    Chronic myelogenous leukemia tumor antigen 28
    Exosome component 5
    Ribosomal RNA-processing protein 46
    p12B
    Gene namesi
    Name:EXOSC5
    Synonyms:CML28, RRP46
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:24662. EXOSC5.

    Subcellular locationi

    Nucleusnucleolus 1 Publication. Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. exosome (RNase complex) Source: UniProtKB
    4. nucleolus Source: UniProtKB
    5. transcriptionally active chromatin Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Exosome, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134890468.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 235235Exosome complex component RRP46PRO_0000139975Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei20 – 201Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9NQT4.
    PaxDbiQ9NQT4.
    PRIDEiQ9NQT4.

    PTM databases

    PhosphoSiteiQ9NQT4.

    Expressioni

    Tissue specificityi

    Highly expressed in a variety of hematopoietic and epithelial tumor cell lines, but not in normal hematopoietic tissues or other normal tissue, with the exception of testis.

    Gene expression databases

    ArrayExpressiQ9NQT4.
    BgeeiQ9NQT4.
    CleanExiHS_EXOSC5.
    GenevestigatoriQ9NQT4.

    Organism-specific databases

    HPAiHPA053150.

    Interactioni

    Subunit structurei

    Component of the RNA exosome complex. Specifically part of the catalytically inactive RNA exosome core (Exo-9) complex which is believed to associate with catalytic subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA exosome complex forms. Exo-9 is formed by a hexameric ring of RNase PH domain-containing subunits specifically containing the heterodimers EXOSC4-EXOSC9, EXOSC5-EXOSC8 and EXOSC6-EXOSC7, and peripheral S1 domain-containing components EXOSC1, EXOSC2 and EXOSC3 located on the top of the ring structure. Interacts with EXOSC1. Interacts with GTPBP1. Interacts with ZC3HAV1. Interacts with DDX17 only in the presence of ZC3HAV1 in an RNA-independent manner.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EXOSC1Q9Y3B210EBI-371876,EBI-371892
    EXOSC3Q9NQT57EBI-371876,EBI-371866
    EXOSC8Q96B264EBI-371876,EBI-371922

    Protein-protein interaction databases

    BioGridi121243. 29 interactions.
    DIPiDIP-29846N.
    IntActiQ9NQT4. 21 interactions.
    MINTiMINT-1479651.
    STRINGi9606.ENSP00000221233.

    Structurei

    Secondary structure

    1
    235
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi31 – 366
    Beta strandi39 – 4911
    Beta strandi52 – 6312
    Beta strandi74 – 818
    Beta strandi83 – 853
    Helixi89 – 10517
    Helixi107 – 1093
    Beta strandi111 – 12414
    Helixi129 – 14315
    Beta strandi152 – 1598
    Beta strandi165 – 1684
    Helixi171 – 1766
    Beta strandi178 – 1869
    Turni187 – 1893
    Beta strandi194 – 2007
    Helixi203 – 23129

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2NN6X-ray3.35D1-235[»]
    ProteinModelPortaliQ9NQT4.
    SMRiQ9NQT4. Positions 25-234.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NQT4.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RNase PH family.Curated

    Phylogenomic databases

    eggNOGiCOG0689.
    HOGENOMiHOG000229515.
    HOVERGENiHBG051520.
    InParanoidiQ9NQT4.
    KOiK12590.
    OMAiTCEASLL.
    PhylomeDBiQ9NQT4.
    TreeFamiTF315920.

    Family and domain databases

    Gene3Di3.30.230.70. 1 hit.
    InterProiIPR001247. ExoRNase_PH_dom1.
    IPR015847. ExoRNase_PH_dom2.
    IPR027408. PNPase/RNase_PH_dom.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    [Graphical view]
    PfamiPF01138. RNase_PH. 1 hit.
    PF03725. RNase_PH_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF54211. SSF54211. 1 hit.
    SSF55666. SSF55666. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9NQT4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEEETHTDAK IRAENGTGSS PRGPGCSLRH FACEQNLLSR PDGSASFLQG    50
    DTSVLAGVYG PAEVKVSKEI FNKATLEVIL RPKIGLPGVA EKSRERLIRN 100
    TCEAVVLGTL HPRTSITVVL QVVSDAGSLL ACCLNAACMA LVDAGVPMRA 150
    LFCGVACALD SDGTLVLDPT SKQEKEARAV LTFALDSVER KLLMSSTKGL 200
    YSDTELQQCL AAAQAASQHV FRFYRESLQR RYSKS 235
    Length:235
    Mass (Da):25,249
    Last modified:October 1, 2000 - v1
    Checksum:iC3C1FCB39D85B1EE
    GO

    Sequence cautioni

    The sequence AAM75154.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti5 – 51T → M.1 Publication
    Corresponds to variant rs10853751 [ dbSNP | Ensembl ].
    VAR_030788
    Natural varianti33 – 331C → W.
    Corresponds to variant rs34500671 [ dbSNP | Ensembl ].
    VAR_051868

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF281134 mRNA. Translation: AAF82135.1.
    AF285785 mRNA. Translation: AAM75154.1. Different initiation.
    AC011462 Genomic DNA. No translation available.
    BC007742 mRNA. Translation: AAH07742.1.
    BC107696 mRNA. Translation: AAI07697.1.
    CCDSiCCDS12580.1.
    RefSeqiNP_064543.3. NM_020158.3.
    UniGeneiHs.283741.

    Genome annotation databases

    EnsembliENST00000221233; ENSP00000221233; ENSG00000077348.
    GeneIDi56915.
    KEGGihsa:56915.
    UCSCiuc002oqo.3. human.

    Polymorphism databases

    DMDMi14285757.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF281134 mRNA. Translation: AAF82135.1 .
    AF285785 mRNA. Translation: AAM75154.1 . Different initiation.
    AC011462 Genomic DNA. No translation available.
    BC007742 mRNA. Translation: AAH07742.1 .
    BC107696 mRNA. Translation: AAI07697.1 .
    CCDSi CCDS12580.1.
    RefSeqi NP_064543.3. NM_020158.3.
    UniGenei Hs.283741.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2NN6 X-ray 3.35 D 1-235 [» ]
    ProteinModelPortali Q9NQT4.
    SMRi Q9NQT4. Positions 25-234.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121243. 29 interactions.
    DIPi DIP-29846N.
    IntActi Q9NQT4. 21 interactions.
    MINTi MINT-1479651.
    STRINGi 9606.ENSP00000221233.

    PTM databases

    PhosphoSitei Q9NQT4.

    Polymorphism databases

    DMDMi 14285757.

    Proteomic databases

    MaxQBi Q9NQT4.
    PaxDbi Q9NQT4.
    PRIDEi Q9NQT4.

    Protocols and materials databases

    DNASUi 56915.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000221233 ; ENSP00000221233 ; ENSG00000077348 .
    GeneIDi 56915.
    KEGGi hsa:56915.
    UCSCi uc002oqo.3. human.

    Organism-specific databases

    CTDi 56915.
    GeneCardsi GC19M041892.
    HGNCi HGNC:24662. EXOSC5.
    HPAi HPA053150.
    MIMi 606492. gene.
    neXtProti NX_Q9NQT4.
    PharmGKBi PA134890468.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0689.
    HOGENOMi HOG000229515.
    HOVERGENi HBG051520.
    InParanoidi Q9NQT4.
    KOi K12590.
    OMAi TCEASLL.
    PhylomeDBi Q9NQT4.
    TreeFami TF315920.

    Enzyme and pathway databases

    Reactomei REACT_18355. ATF4 activates genes.
    REACT_20619. mRNA decay by 3' to 5' exoribonuclease.
    REACT_24915. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
    REACT_25042. KSRP destabilizes mRNA.
    REACT_25064. Tristetraprolin (TTP) destabilizes mRNA.

    Miscellaneous databases

    EvolutionaryTracei Q9NQT4.
    GeneWikii Exosome_component_5.
    GenomeRNAii 56915.
    NextBioi 62403.
    PROi Q9NQT4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NQT4.
    Bgeei Q9NQT4.
    CleanExi HS_EXOSC5.
    Genevestigatori Q9NQT4.

    Family and domain databases

    Gene3Di 3.30.230.70. 1 hit.
    InterProi IPR001247. ExoRNase_PH_dom1.
    IPR015847. ExoRNase_PH_dom2.
    IPR027408. PNPase/RNase_PH_dom.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    [Graphical view ]
    Pfami PF01138. RNase_PH. 1 hit.
    PF03725. RNase_PH_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54211. SSF54211. 1 hit.
    SSF55666. SSF55666. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    2. "CML28 is a broadly immunogenic antigen, which is overexpressed in tumor cells."
      Yang X.-F., Wu C.J., Chen L., Alyea E.P., Canning C., Kantoff P., Soiffer R.J., Dranoff G., Ritz J.
      Cancer Res. 62:5517-5522(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "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].
    4. "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], VARIANT MET-5.
      Tissue: B-cell.
    5. "The yeast exosome and human PM-Scl are related complexes of 3'-->5' exonucleases."
      Allmang C., Petfalski E., Podtelejnikov A., Mann M., Tollervey D., Mitchell P.
      Genes Dev. 13:2148-2158(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    6. "AU binding proteins recruit the exosome to degrade ARE-containing mRNAs."
      Chen C.-Y., Gherzi R., Ong S.-E., Chan E.L., Raijmakers R., Pruijn G.J.M., Stoecklin G., Moroni C., Mann M., Karin M.
      Cell 107:451-464(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE RNA EXOSOME CORE COMPLEX.
    7. "The mammalian exosome mediates the efficient degradation of mRNAs that contain AU-rich elements."
      Mukherjee D., Gao M., O'Connor J.P., Raijmakers R., Pruijn G., Lutz C.S., Wilusz J.
      EMBO J. 21:165-174(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CYTOPLASMIC MRNA DEGRADATION.
    8. "Protein-protein interactions of hCsl4p with other human exosome subunits."
      Raijmakers R., Noordman Y.E., van Venrooij W.J., Pruijn G.J.M.
      J. Mol. Biol. 315:809-818(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH EXOSC1.
    9. "The zinc-finger antiviral protein recruits the RNA processing exosome to degrade the target mRNA."
      Guo X., Ma J., Sun J., Gao G.
      Proc. Natl. Acad. Sci. U.S.A. 104:151-156(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZC3HAV1.
    10. "p72 DEAD box RNA helicase is required for optimal function of the zinc-finger antiviral protein."
      Chen G., Guo X., Lv F., Xu Y., Gao G.
      Proc. Natl. Acad. Sci. U.S.A. 105:4352-4357(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DDX17.
    11. "Dis3-like 1: a novel exoribonuclease associated with the human exosome."
      Staals R.H., Bronkhorst A.W., Schilders G., Slomovic S., Schuster G., Heck A.J., Raijmakers R., Pruijn G.J.
      EMBO J. 29:2358-2367(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE RNA EXOSOME COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    12. "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-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "The RNA exosome targets the AID cytidine deaminase to both strands of transcribed duplex DNA substrates."
      Basu U., Meng F.L., Keim C., Grinstein V., Pefanis E., Eccleston J., Zhang T., Myers D., Wasserman C.R., Wesemann D.R., Januszyk K., Gregory R.I., Deng H., Lima C.D., Alt F.W.
      Cell 144:353-363(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DEAMINATION OF TRANSCRIBED DNA SUBSTRATE.
    15. "Modulation of exosome-mediated mRNA turnover by interaction of GTP-binding protein 1 (GTPBP1) with its target mRNAs."
      Woo K.C., Kim T.D., Lee K.H., Kim D.Y., Kim S., Lee H.R., Kang H.J., Chung S.J., Senju S., Nishimura Y., Kim K.T.
      FASEB J. 25:2757-2769(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GTPBP1.
    16. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Reconstitution, activities, and structure of the eukaryotic RNA exosome."
      Liu Q., Greimann J.C., Lima C.D.
      Cell 127:1223-1237(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS), LACK OF CATALYTIC ACTIVITY, RECONSTITUTION OF THE RNA EXOSOME CORE COMPLEX.
    18. Erratum
      Liu Q., Greimann J.C., Lima C.D.
      Cell 131:188-189(2007)

    Entry informationi

    Entry nameiEXOS5_HUMAN
    AccessioniPrimary (citable) accession number: Q9NQT4
    Secondary accession number(s): Q32Q81, Q8NG16, Q96I89
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 2001
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 130 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

    Caution

    The six exosome core subunits containing a RNase PH-domain are not phosphorolytically active.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3