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P19484

- TFEB_HUMAN

UniProt

P19484 - TFEB_HUMAN

Protein

Transcription factor EB

Gene

TFEB

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 3 (29 Aug 2001)
      Previous versions | rss
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    Functioni

    Transcription factor that specifically recognizes and binds E-box sequences (5'-CANNTG-3'). Efficient DNA-binding requires dimerization with itself or with another MiT/TFE family member such as TFE3 or MITF. In association with TFE3, activates the expression of CD40L in T-cells, thereby playing a role in T-cell-dependent antibody responses in activated CD4+ T-cells and thymus-dependent humoral immunity. Specifically recognizes and binds the CLEAR-box sequence (5'-GTCACGTGAC-3') present in the regulatory region of many lysosomal genes, leading to activate their expression. It thereby plays a central role in expression of lysosomal genes. Acts as a positive regulator of autophagy by promoting expression of genes involved in autophagy. Specifically recognizes the gamma-E3 box, a subset of E-boxes, present in the heavy-chain immunoglobulin enhancer. Plays a role in the signal transduction processes required for normal vascularization of the placenta.2 Publications

    GO - Molecular functioni

    1. sequence-specific DNA binding transcription factor activity Source: UniProtKB
    2. transcription regulatory region DNA binding Source: UniProtKB

    GO - Biological processi

    1. autophagy Source: UniProtKB-KW
    2. embryonic placenta development Source: UniProtKB
    3. humoral immune response Source: UniProtKB
    4. lysosome organization Source: UniProtKB
    5. positive regulation of autophagy Source: UniProtKB
    6. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    7. regulation of transcription, DNA-templated Source: UniProtKB
    8. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Adaptive immunity, Autophagy, Immunity, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription factor EB
    Alternative name(s):
    Class E basic helix-loop-helix protein 35
    Short name:
    bHLHe35
    Gene namesi
    Name:TFEB
    Synonyms:BHLHE35
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:11753. TFEB.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Mainly present in the cytoplasm. Under aberrant lysosomal storage conditions, it translocates from the cytoplasm to the nucleus.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: UniProtKB
    3. transcription factor complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti319308. Translocation renal cell carcinoma.
    PharmGKBiPA36468.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 476476Transcription factor EBPRO_0000127473Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei122 – 1221Phosphoserine1 Publication
    Modified residuei138 – 1381Phosphoserine2 Publications
    Modified residuei142 – 1421Phosphoserine2 Publications
    Modified residuei183 – 1831Phosphothreonine1 Publication
    Modified residuei441 – 4411Phosphoserine1 Publication
    Modified residuei467 – 4671Phosphoserine1 Publication

    Post-translational modificationi

    Sumoylated; does not affect dimerization with MITF.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP19484.
    PaxDbiP19484.
    PRIDEiP19484.

    PTM databases

    PhosphoSiteiP19484.

    Expressioni

    Gene expression databases

    ArrayExpressiP19484.
    BgeeiP19484.
    CleanExiHS_TFEB.
    GenevestigatoriP19484.

    Organism-specific databases

    HPAiHPA049532.

    Interactioni

    Subunit structurei

    Homodimer and heterodimer; with TFE3 or MITF.

    Protein-protein interaction databases

    BioGridi113668. 2 interactions.
    IntActiP19484. 2 interactions.
    STRINGi9606.ENSP00000230323.

    Structurei

    3D structure databases

    ProteinModelPortaliP19484.
    SMRiP19484. Positions 236-326.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini235 – 28854bHLHPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni156 – 16510Strong transcription activation domainSequence Analysis
    Regioni298 – 31922Leucine-zipperAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi10 – 4435Gln-richAdd
    BLAST
    Compositional biasi35 – 4410Poly-Gln
    Compositional biasi366 – 41449Pro-richAdd
    BLAST

    Domaini

    The leucin zipper region is essential for homo- or heterodimerization and high-affinity DNA binding. DNA binding is mediated by the basic region.1 Publication

    Sequence similaritiesi

    Belongs to the MiT/TFE family.Curated
    Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG251286.
    HOGENOMiHOG000231368.
    HOVERGENiHBG006768.
    InParanoidiP19484.
    KOiK15590.
    PhylomeDBiP19484.
    TreeFamiTF317174.

    Family and domain databases

    Gene3Di4.10.280.10. 1 hit.
    InterProiIPR011598. bHLH_dom.
    IPR021802. bHLH_ZIP_TF_MiT/TFE.
    IPR024098. TFEB.
    [Graphical view]
    PANTHERiPTHR10014:SF9. PTHR10014:SF9. 1 hit.
    PfamiPF11851. DUF3371. 1 hit.
    PF00010. HLH. 1 hit.
    [Graphical view]
    SMARTiSM00353. HLH. 1 hit.
    [Graphical view]
    SUPFAMiSSF47459. SSF47459. 1 hit.
    PROSITEiPS50888. BHLH. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P19484-1) [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

    MASRIGLRMQ LMREQAQQEE QRERMQQQAV MHYMQQQQQQ QQQQLGGPPT    50
    PAINTPVHFQ SPPPVPGEVL KVQSYLENPT SYHLQQSQHQ KVREYLSETY 100
    GNKFAAHISP AQGSPKPPPA ASPGVRAGHV LSSSAGNSAP NSPMAMLHIG 150
    SNPERELDDV IDNIMRLDDV LGYINPEMQM PNTLPLSSSH LNVYSSDPQV 200
    TASLVGVTSS SCPADLTQKR ELTDAESRAL AKERQKKDNH NLIERRRRFN 250
    INDRIKELGM LIPKANDLDV RWNKGTILKA SVDYIRRMQK DLQKSRELEN 300
    HSRRLEMTNK QLWLRIQELE MQARVHGLPT TSPSGMNMAE LAQQVVKQEL 350
    PSEEGPGEAL MLGAEVPDPE PLPALPPQAP LPLPTQPPSP FHHLDFSHSL 400
    SFGGREDEGP PGYPEPLAPG HGSPFPSLSK KDLDLMLLDD SLLPLASDPL 450
    LSTMSPEASK ASSRRSSFSM EEGDVL 476
    Length:476
    Mass (Da):52,865
    Last modified:August 29, 2001 - v3
    Checksum:i093AE3B79C760D99
    GO
    Isoform 2 (identifier: P19484-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         72-156: Missing.

    Show »
    Length:391
    Mass (Da):43,803
    Checksum:i9B43BAA84C5517B2
    GO

    Sequence cautioni

    The sequence AAA36730.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAE77681.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti106 – 1061A → AA in AAA36730. (PubMed:2115126)Curated
    Sequence conflicti113 – 14129GSPKP…NSAPN → ALRNPHQPPPQGCELDTCCP PPLATVLPI in AAA36730. (PubMed:2115126)CuratedAdd
    BLAST
    Sequence conflicti168 – 1703DDV → TMS in AAA36730. (PubMed:2115126)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei72 – 15685Missing in isoform 2. 2 PublicationsVSP_002159Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M33782 mRNA. Translation: AAA36730.1. Different initiation.
    AJ608786 mRNA. Translation: CAE77681.1. Different initiation.
    AL035588 Genomic DNA. Translation: CAD92604.1.
    BC006225 mRNA. Translation: AAH06225.2.
    BC032448 mRNA. Translation: AAH32448.1.
    CCDSiCCDS4858.1. [P19484-1]
    CCDS64424.1. [P19484-2]
    PIRiA35658.
    RefSeqiNP_001161299.2. NM_001167827.2.
    NP_001258872.1. NM_001271943.1. [P19484-2]
    NP_001258873.1. NM_001271944.1. [P19484-1]
    NP_001258874.1. NM_001271945.1. [P19484-1]
    NP_009093.1. NM_007162.2. [P19484-1]
    XP_005249468.1. XM_005249411.1. [P19484-1]
    XP_005249469.1. XM_005249412.1. [P19484-1]
    XP_006715275.1. XM_006715212.1. [P19484-1]
    XP_006715276.1. XM_006715213.1. [P19484-1]
    UniGeneiHs.485360.

    Genome annotation databases

    EnsembliENST00000230323; ENSP00000230323; ENSG00000112561. [P19484-1]
    ENST00000373033; ENSP00000362124; ENSG00000112561. [P19484-1]
    ENST00000403298; ENSP00000384203; ENSG00000112561. [P19484-1]
    ENST00000420312; ENSP00000412551; ENSG00000112561. [P19484-2]
    GeneIDi7942.
    KEGGihsa:7942.
    UCSCiuc003oqr.2. human. [P19484-2]
    uc003oqs.1. human. [P19484-1]

    Polymorphism databases

    DMDMi19856774.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M33782 mRNA. Translation: AAA36730.1 . Different initiation.
    AJ608786 mRNA. Translation: CAE77681.1 . Different initiation.
    AL035588 Genomic DNA. Translation: CAD92604.1 .
    BC006225 mRNA. Translation: AAH06225.2 .
    BC032448 mRNA. Translation: AAH32448.1 .
    CCDSi CCDS4858.1. [P19484-1 ]
    CCDS64424.1. [P19484-2 ]
    PIRi A35658.
    RefSeqi NP_001161299.2. NM_001167827.2.
    NP_001258872.1. NM_001271943.1. [P19484-2 ]
    NP_001258873.1. NM_001271944.1. [P19484-1 ]
    NP_001258874.1. NM_001271945.1. [P19484-1 ]
    NP_009093.1. NM_007162.2. [P19484-1 ]
    XP_005249468.1. XM_005249411.1. [P19484-1 ]
    XP_005249469.1. XM_005249412.1. [P19484-1 ]
    XP_006715275.1. XM_006715212.1. [P19484-1 ]
    XP_006715276.1. XM_006715213.1. [P19484-1 ]
    UniGenei Hs.485360.

    3D structure databases

    ProteinModelPortali P19484.
    SMRi P19484. Positions 236-326.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113668. 2 interactions.
    IntActi P19484. 2 interactions.
    STRINGi 9606.ENSP00000230323.

    PTM databases

    PhosphoSitei P19484.

    Polymorphism databases

    DMDMi 19856774.

    Proteomic databases

    MaxQBi P19484.
    PaxDbi P19484.
    PRIDEi P19484.

    Protocols and materials databases

    DNASUi 7942.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000230323 ; ENSP00000230323 ; ENSG00000112561 . [P19484-1 ]
    ENST00000373033 ; ENSP00000362124 ; ENSG00000112561 . [P19484-1 ]
    ENST00000403298 ; ENSP00000384203 ; ENSG00000112561 . [P19484-1 ]
    ENST00000420312 ; ENSP00000412551 ; ENSG00000112561 . [P19484-2 ]
    GeneIDi 7942.
    KEGGi hsa:7942.
    UCSCi uc003oqr.2. human. [P19484-2 ]
    uc003oqs.1. human. [P19484-1 ]

    Organism-specific databases

    CTDi 7942.
    GeneCardsi GC06M041651.
    HGNCi HGNC:11753. TFEB.
    HPAi HPA049532.
    MIMi 600744. gene.
    neXtProti NX_P19484.
    Orphaneti 319308. Translocation renal cell carcinoma.
    PharmGKBi PA36468.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG251286.
    HOGENOMi HOG000231368.
    HOVERGENi HBG006768.
    InParanoidi P19484.
    KOi K15590.
    PhylomeDBi P19484.
    TreeFami TF317174.

    Miscellaneous databases

    ChiTaRSi TFEB. human.
    GeneWikii TFEB.
    GenomeRNAii 7942.
    NextBioi 30462.
    PROi P19484.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P19484.
    Bgeei P19484.
    CleanExi HS_TFEB.
    Genevestigatori P19484.

    Family and domain databases

    Gene3Di 4.10.280.10. 1 hit.
    InterProi IPR011598. bHLH_dom.
    IPR021802. bHLH_ZIP_TF_MiT/TFE.
    IPR024098. TFEB.
    [Graphical view ]
    PANTHERi PTHR10014:SF9. PTHR10014:SF9. 1 hit.
    Pfami PF11851. DUF3371. 1 hit.
    PF00010. HLH. 1 hit.
    [Graphical view ]
    SMARTi SM00353. HLH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47459. SSF47459. 1 hit.
    PROSITEi PS50888. BHLH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A helix-loop-helix protein related to the immunoglobulin E box-binding proteins."
      Carr C.S., Sharp P.A.
      Mol. Cell. Biol. 10:4384-4388(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
      Tissue: B-cell.
    2. "Regulation of the MiTF/TFE bHLH-LZ transcription factors through restricted spatial expression and alternative splicing of functional domains."
      Kuiper R.P., Schepens M., Thijssen J., Schoenmakers E.F.P.M., Geurts van Kessel A.
      Nucleic Acids Res. 32:2315-2322(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Kidney.
    3. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 58-476 (ISOFORM 2).
      Tissue: Brain and Lung.
    5. "TFEB has DNA-binding and oligomerization properties of a unique helix-loop-helix/leucine-zipper family."
      Fisher D.E., Carr C.S., Parent L.A., Sharp P.A.
      Genes Dev. 5:2342-2352(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA-BINDING, INTERACTION WITH TFE3, DOMAIN.
    6. "Sumoylation of MITF and its related family members TFE3 and TFEB."
      Miller A.J., Levy C., Davis I.J., Razin E., Fisher D.E.
      J. Biol. Chem. 280:146-155(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION, INTERACTION WITH MITF.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138 AND SER-142, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    9. Cited for: FUNCTION, DNA-BINDING.
    10. "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-122; SER-138; SER-142; THR-183 AND SER-441, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "ZKSCAN3 is a master transcriptional repressor of autophagy."
      Chauhan S., Goodwin J.G., Chauhan S., Manyam G., Wang J., Kamat A.M., Boyd D.D.
      Mol. Cell 50:16-28(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiTFEB_HUMAN
    AccessioniPrimary (citable) accession number: P19484
    Secondary accession number(s): Q709B3
    , Q7Z6P9, Q9BRJ5, Q9UJD8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: August 29, 2001
    Last modified: October 1, 2014
    This is version 148 of the entry and version 3 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3