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Q62167

- DDX3X_MOUSE

UniProt

Q62167 - DDX3X_MOUSE

Protein

ATP-dependent RNA helicase DDX3X

Gene

Ddx3x

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Multifunctional ATP-dependent RNA helicase. The ATPase activity can be stimulated by various ribo- and deoxynucleic acids indicative for a relaxed substrate specificity. In vitro can unwind partially double-stranded DNA with a preference for 5'-single-stranded DNA overhangs. Is involved in several steps of gene expression, such as transcription, mRNA maturation, mRNA export and translation. However, the exact mechanisms are not known and some functions may be specific for a subset of mRNAs. Involved in transcriptional regulation. Can enhance transcription from the CDKN1A/WAF1 promoter in a SP1-dependent manner. Found associated with the E-cadherin promoter and can down-regulate transcription from the promoter. Involved in regulation of translation initiation. Proposed to be involved in positive regulation of translation such as of cyclin E1/CCNE1 mRNA and specifically of mRNAs containing complex secondary structures in their 5'UTRs; these functions seem to require RNA helicase activity. Specifically promotes translation of a subset of viral and cellular mRNAs carrying a 5'proximal stem-loop structure in their 5'UTRs and cooperates with the eIF4F complex. Proposed to act prior to 43S ribosomal scanning and to locally destabilize these RNA structures to allow recognition of the mRNA cap or loading onto the 40S subunit. After association with 40S ribosomal subunits seems to be involved in the functional assembly of 80S ribosomes; the function seems to cover translation of mRNAs with structured and non-structured 5'UTRs and is independent of RNA helicase activity. Also proposed to inhibit cap-dependent translation by competetive interaction with EIF4E which can block the EIF4E:EIF4G complex formation. Proposed to be involved in stress response and stress granule assembly; the function is independent of RNA helicase activity and seems to involve association with EIF4E. May be involved in nuclear export of specific mRNAs but not in bulk mRNA export via interactions with XPO1 and NXF1. Also associates with polyadenylated mRNAs independently of NXF1. Associates with spliced mRNAs in an exon junction complex (EJC)-dependent manner and seems not to be directly involved in splicing. May be involved in nuclear mRNA export by association with DDX5 and regulating its nuclear location. Involved in innate immune signaling promoting the production of type I interferon (IFN-alpha and IFN-beta); proposed to act as viral RNA sensor, signaling intermediate and transcriptional coactivator. Involved in TBK1 and IKBKE-dependent IRF3 activation leading to IFNB induction, plays a role of scaffolding adapter that links IKBKE and IRF3 and coordinates their activation. Also found associated with IFNB promoters; the function is independent of IRF3. Can bind to viral RNAs and via association with MAVS/IPS1 and DDX58/RIG-I is thought to induce signaling in early stages of infection. Involved in regulation of apoptosis. May be required for activation of the intrinsic but inhibit activation of the extrinsic apoptotic pathway. Acts as an antiapoptotic protein through association with GSK3A/B and BIRC2 in an apoptosis antagonizing signaling complex; activation of death receptors promotes caspase-dependent cleavage of BIRC2 and DDX3X and relieves the inhibition. May be involved in mitotic chromosome segregation By similarity.By similarity

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi200 – 2078ATPPROSITE-ProRule annotation
    Nucleotide bindingi224 – 2318ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATPase activity Source: UniProtKB
    2. ATP binding Source: UniProtKB-KW
    3. ATP-dependent DNA helicase activity Source: UniProtKB
    4. ATP-dependent RNA helicase activity Source: UniProtKB
    5. DNA binding Source: UniProtKB
    6. eukaryotic initiation factor 4E binding Source: UniProtKB
    7. mRNA 5'-UTR binding Source: UniProtKB
    8. poly(A) binding Source: UniProtKB
    9. protein binding Source: IntAct
    10. ribosomal small subunit binding Source: UniProtKB
    11. RNA binding Source: UniProtKB
    12. RNA stem-loop binding Source: UniProtKB
    13. transcription factor binding Source: UniProtKB
    14. translation initiation factor binding Source: UniProtKB

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. cellular response to arsenic-containing substance Source: UniProtKB
    3. cellular response to osmotic stress Source: UniProtKB
    4. chromosome segregation Source: UniProtKB
    5. DNA duplex unwinding Source: GOC
    6. extrinsic apoptotic signaling pathway via death domain receptors Source: UniProtKB
    7. innate immune response Source: UniProtKB
    8. intracellular signal transduction Source: UniProtKB
    9. intrinsic apoptotic signaling pathway Source: UniProtKB
    10. mature ribosome assembly Source: UniProtKB
    11. negative regulation of apoptotic process Source: UniProtKB
    12. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    13. negative regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
    14. negative regulation of protein complex assembly Source: UniProtKB
    15. negative regulation of translation Source: UniProtKB
    16. positive regulation of apoptotic process Source: UniProtKB
    17. positive regulation of cell growth Source: UniProtKB
    18. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    19. positive regulation of G1/S transition of mitotic cell cycle Source: UniProtKB
    20. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    21. positive regulation of translation Source: UniProtKB
    22. positive regulation of translational initiation Source: UniProtKB
    23. response to virus Source: UniProtKB
    24. RNA secondary structure unwinding Source: UniProtKB
    25. stress granule assembly Source: UniProtKB
    26. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    Apoptosis, Chromosome partition, Immunity, Innate immunity, Ribosome biogenesis, Transcription, Transcription regulation, Translation regulation

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-dependent RNA helicase DDX3X (EC:3.6.4.13)
    Alternative name(s):
    D1Pas1-related sequence 2
    DEAD box RNA helicase DEAD3
    Short name:
    mDEAD3
    DEAD box protein 3, X-chromosomal
    Embryonic RNA helicase
    Gene namesi
    Name:Ddx3x
    Synonyms:D1Pas1-rs2, Ddx3, Dead3, Erh
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:103064. Ddx3x.

    Subcellular locationi

    Nucleus speckle By similarity. Cytoplasm By similarity. Mitochondrion outer membrane By similarity
    Note: Located predominantly in nuclear speckles and, at low levels, throughout the cytoplasm. Located to the outer side of nuclear pore complexes (NPC). Shuttles between the nucleus and the cytoplasm in a XPO1 and may be also in a NFX1-dependent manner. Associated with polyadenylated mRNAs in the cytoplasm and the nucleus. Predominantly located in nucleus during G0 phase and in the cytoplasm during G1/S phase By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoplasmic stress granule Source: UniProtKB
    3. mitochondrial outer membrane Source: UniProtKB-SubCell
    4. nuclear speck Source: UniProtKB-SubCell
    5. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 662661ATP-dependent RNA helicase DDX3XPRO_0000055010Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei55 – 551N6-acetyllysine1 Publication
    Modified residuei69 – 691PhosphotyrosineBy similarity
    Modified residuei74 – 741PhosphoserineBy similarity
    Modified residuei78 – 781PhosphoserineBy similarity
    Modified residuei104 – 1041Phosphotyrosine1 Publication
    Modified residuei118 – 1181N6-acetyllysineBy similarity
    Modified residuei125 – 1251PhosphoserineBy similarity
    Modified residuei131 – 1311Phosphoserine1 Publication
    Modified residuei343 – 3431PhosphotyrosineBy similarity
    Modified residuei590 – 5901PhosphoserineBy similarity
    Modified residuei594 – 5941PhosphoserineBy similarity
    Modified residuei612 – 6121PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated by TBK1; the phosphorylation is required to synergize with TBK1 in IFN-beta induction. Probably also phosphorylated by IKBKE By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ62167.
    PaxDbiQ62167.
    PRIDEiQ62167.

    2D gel databases

    REPRODUCTION-2DPAGEQ62167.

    PTM databases

    PhosphoSiteiQ62167.

    Expressioni

    Tissue specificityi

    Developmentally regulated.

    Developmental stagei

    Expressed in oocytes. Ubiquitously found in 9 days post-conception embryo, at later stages it is restricted to brain and kidney.

    Gene expression databases

    ArrayExpressiQ62167.
    BgeeiQ62167.
    CleanExiMM_ERH.
    GenevestigatoriQ62167.

    Interactioni

    Subunit structurei

    Interacts with XPO1, TDRD3, PABPC1, NXF1, EIF3C, MAVS, DDX58 and NCAPH. Interacts with DDX5; the interaction is regulated by the phosphorylation status of both proteins. Interacts with EIF4E; DDX3X competes with EIF4G1/EIF4G3 for interaction with EIF4E. Interacts with IKBKE; the interaction is direct. Interacts with IRF3; the interaction allows the phosphorylation and activation of IRF3 by IKBKE. Interacts with TBK1. Associates with the eukaryotic translation initiation factor 3 (eIF-3) complex. Associates with the 40S ribosome. Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TBK1Q9UHD28EBI-773173,EBI-356402From a different organism.

    Protein-protein interaction databases

    BioGridi199084. 2 interactions.
    IntActiQ62167. 7 interactions.
    MINTiMINT-1870173.

    Structurei

    3D structure databases

    ProteinModelPortaliQ62167.
    SMRiQ62167. Positions 139-580.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini211 – 403193Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini414 – 575162Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 139138Required for TBK1 and IKBKE-dependent IFN-beta activationBy similarityAdd
    BLAST
    Regioni2 – 10099Interaction with EIF4EBy similarityAdd
    BLAST
    Regioni100 – 662563Interaction with GSK3BBy similarityAdd
    BLAST
    Regioni100 – 11011Required for interaction with IKBKEBy similarityAdd
    BLAST
    Regioni250 – 25910Involved in stimulation of ATPase activity by DNA and RNA, nucleic acid binding and unwindingBy similarity
    Regioni260 – 517258Necessary for interaction with XPO1By similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi180 – 20829Q motifAdd
    BLAST
    Motifi347 – 3504DEAD box

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi582 – 66281Gly/Ser-richAdd
    BLAST
    Compositional biasi609 – 6168Poly-Ser
    Compositional biasi624 – 6307Poly-Gly
    Compositional biasi633 – 6419Poly-Gly

    Sequence similaritiesi

    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0513.
    GeneTreeiENSGT00740000115030.
    HOGENOMiHOG000268804.
    HOVERGENiHBG015893.
    InParanoidiQ62167.
    KOiK11594.
    OMAiSFGSRND.
    OrthoDBiEOG7B5WV8.
    PhylomeDBiQ62167.
    TreeFamiTF300332.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR000629. RNA-helicase_DEAD-box_CS.
    IPR014014. RNA_helicase_DEAD_Q_motif.
    [Graphical view]
    PfamiPF00270. DEAD. 1 hit.
    PF00271. Helicase_C. 1 hit.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51195. Q_MOTIF. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q62167-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSHVAVENAL GLDQQFAGLD LNSSDNQSGG STASKGRYIP PHLRNREATK    50
    GFYDKDSSGW SSSKDKDAYS SFGSRGDSRG KSSFFGDRGS GSRGRFDDRG 100
    RGDYDGIGGR GDRSGFGKFE RGGNSRWCDK SDEDDWSKPL PPSERLEQEL 150
    FSGGNTGINF EKYDDIPVEA TGNNCPPHIE SFSDVEMGEI IMGNIELTRY 200
    TRPTPVQKHA IPIIKEKRDL MACAQTGSGK TAAFLLPILS QIYADGPGEA 250
    LRAMKENGRY GRRKQYPISL VLAPTRELAV QIYEEARKFS YRSRVRPCVV 300
    YGGAEIGQQI RDLERGCHLL VATPGRLVDM MERGKIGLDF CKYLVLDEAD 350
    RMLDMGFEPQ IRRIVEQDTM PPKGVRHTMM FSATFPKEIQ MLARDFLDEY 400
    IFLAVGRVGS TSENITQKVV WVEEIDKRSF LLDLLNATGK DSLTLVFVET 450
    KKGADSLEDF LYHEGYACTS IHGDRSQRDR EEALHQFRSG KSPILVATAV 500
    AARGLDISNV KHVINFDLPS DIEEYVHRIG RTGRVGNLGL ATSFFNERNI 550
    NITKDLLDLL VEAKQEVPSW LENMAFEHHY KGSSRGRSKS SRFSGGFGAR 600
    DYRQSSGASS SSFSSSRASS SRSGGGGHGG SRGFGGGGYG GFYNSDGYGG 650
    NYNSQGVDWW GN 662
    Length:662
    Mass (Da):73,101
    Last modified:January 23, 2007 - v3
    Checksum:i216515CB00324017
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z38117 mRNA. Translation: CAA86261.1.
    L25126 mRNA. Translation: AAA53630.1.
    CCDSiCCDS30027.1.
    PIRiI84741.
    RefSeqiNP_034158.1. NM_010028.3.
    UniGeneiMm.289662.

    Genome annotation databases

    EnsembliENSMUST00000000804; ENSMUSP00000000804; ENSMUSG00000000787.
    GeneIDi13205.
    KEGGimmu:13205.
    UCSCiuc009srl.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z38117 mRNA. Translation: CAA86261.1 .
    L25126 mRNA. Translation: AAA53630.1 .
    CCDSi CCDS30027.1.
    PIRi I84741.
    RefSeqi NP_034158.1. NM_010028.3.
    UniGenei Mm.289662.

    3D structure databases

    ProteinModelPortali Q62167.
    SMRi Q62167. Positions 139-580.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199084. 2 interactions.
    IntActi Q62167. 7 interactions.
    MINTi MINT-1870173.

    PTM databases

    PhosphoSitei Q62167.

    2D gel databases

    REPRODUCTION-2DPAGE Q62167.

    Proteomic databases

    MaxQBi Q62167.
    PaxDbi Q62167.
    PRIDEi Q62167.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000000804 ; ENSMUSP00000000804 ; ENSMUSG00000000787 .
    GeneIDi 13205.
    KEGGi mmu:13205.
    UCSCi uc009srl.2. mouse.

    Organism-specific databases

    CTDi 1654.
    MGIi MGI:103064. Ddx3x.

    Phylogenomic databases

    eggNOGi COG0513.
    GeneTreei ENSGT00740000115030.
    HOGENOMi HOG000268804.
    HOVERGENi HBG015893.
    InParanoidi Q62167.
    KOi K11594.
    OMAi SFGSRND.
    OrthoDBi EOG7B5WV8.
    PhylomeDBi Q62167.
    TreeFami TF300332.

    Miscellaneous databases

    ChiTaRSi DDX3X. mouse.
    NextBioi 283364.
    PROi Q62167.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q62167.
    Bgeei Q62167.
    CleanExi MM_ERH.
    Genevestigatori Q62167.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR000629. RNA-helicase_DEAD-box_CS.
    IPR014014. RNA_helicase_DEAD_Q_motif.
    [Graphical view ]
    Pfami PF00270. DEAD. 1 hit.
    PF00271. Helicase_C. 1 hit.
    [Graphical view ]
    SMARTi SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    PROSITEi PS00039. DEAD_ATP_HELICASE. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51195. Q_MOTIF. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The embryonic RNA helicase gene (ERH): a new member of the DEAD box family of RNA helicases."
      Sowden J.C., Putt W., Morrison K., Beddington R., Edwards Y.
      Biochem. J. 308:839-846(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6 and DBA.
    2. "Mouse erythroid cells express multiple putative RNA helicase genes exhibiting high sequence conservation from yeast to mammals."
      Gee S.L., Conboy J.G.
      Gene 140:171-177(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Erythroleukemia.
    3. "An N-acetylated natural ligand of human histocompatibility leukocyte antigen (HLA)-B39. Classical major histocompatibility complex class I proteins bind peptides with a blocked NH(2) terminus in vivo."
      Yaguee J., Alvarez I., Rognan D., Ramos M., Vazquez J., Lopez de Castro J.A.
      J. Exp. Med. 191:2083-2092(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-10, ACETYLATION AT SER-2.
    4. Lubec G., Klug S.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 535-548, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Hippocampus.
    5. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-104, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    7. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiDDX3X_MOUSE
    AccessioniPrimary (citable) accession number: Q62167
    Secondary accession number(s): O09060, O09143
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 133 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3