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P34914

- HYES_MOUSE

UniProt

P34914 - HYES_MOUSE

Protein

Bifunctional epoxide hydrolase 2

Gene

Ephx2

Organism
Mus musculus (Mouse)
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 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides. Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides. Also determines steady-state levels of physiological mediators. The N-terminal domain has lipid phosphatase activity, with the highest activity towards threo-9,10-phosphonooxy-hydroxy-octadecanoic acid, followed by erythro-9,10-phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy-octadec-9Z-enoic acid, 12-phosphonooxy-octadec-9E-enoic acid, and p-nitrophenyl phospate By similarity.By similarity

    Catalytic activityi

    An epoxide + H2O = a glycol.
    (9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate + H2O = (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate.

    Cofactori

    Magnesium.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi9 – 91MagnesiumBy similarity
    Metal bindingi11 – 111MagnesiumBy similarity
    Metal bindingi185 – 1851MagnesiumBy similarity
    Active sitei333 – 3331Nucleophile
    Binding sitei381 – 3811SubstrateBy similarity
    Active sitei465 – 4651Proton donor
    Active sitei523 – 5231Proton acceptor

    GO - Molecular functioni

    1. 10-hydroxy-9-(phosphonooxy)octadecanoate phosphatase activity Source: UniProtKB-EC
    2. epoxide hydrolase activity Source: UniProtKB-EC
    3. lipid phosphatase activity Source: UniProtKB
    4. magnesium ion binding Source: UniProtKB
    5. toxic substance binding Source: Ensembl

    GO - Biological processi

    1. cholesterol homeostasis Source: UniProtKB
    2. phospholipid dephosphorylation Source: UniProtKB
    3. positive regulation of gene expression Source: UniProtKB
    4. regulation of cholesterol metabolic process Source: UniProtKB
    5. response to toxic substance Source: UniProtKB-KW
    6. stilbene catabolic process Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Aromatic hydrocarbons catabolism, Detoxification, Lipid metabolism

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BRENDAi3.3.2.10. 3474.
    ReactomeiREACT_196570. Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET).

    Protein family/group databases

    MEROPSiS33.973.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional epoxide hydrolase 2
    Including the following 2 domains:
    Cytosolic epoxide hydrolase 2 (EC:3.3.2.10)
    Short name:
    CEH
    Alternative name(s):
    Epoxide hydratase
    Soluble epoxide hydrolase
    Short name:
    SEH
    Lipid-phosphate phosphatase (EC:3.1.3.76)
    Gene namesi
    Name:Ephx2
    Synonyms:Eph2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:99500. Ephx2.

    Subcellular locationi

    GO - Cellular componenti

    1. focal adhesion Source: Ensembl
    2. Golgi apparatus Source: Ensembl
    3. nucleolus Source: Ensembl
    4. peroxisome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 554554Bifunctional epoxide hydrolase 2PRO_0000084112Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei55 – 551N6-succinyllysine1 Publication
    Modified residuei176 – 1761N6-acetyllysine; alternate1 Publication
    Modified residuei176 – 1761N6-succinyllysine; alternate1 Publication
    Modified residuei191 – 1911N6-acetyllysine1 Publication
    Modified residuei215 – 2151N6-acetyllysine1 Publication
    Modified residuei368 – 3681Phosphoserine1 Publication
    Modified residuei371 – 3711N6-succinyllysine1 Publication
    Modified residuei420 – 4201N6-succinyllysine1 Publication
    Modified residuei454 – 4541N6-succinyllysine1 Publication
    Modified residuei504 – 5041N6-succinyllysine1 Publication
    Modified residuei508 – 5081N6-acetyllysine; alternate1 Publication
    Modified residuei508 – 5081N6-succinyllysine; alternate1 Publication
    Lipidationi521 – 5211S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteineBy similarity
    Modified residuei553 – 5531N6-succinyllysine1 Publication

    Post-translational modificationi

    The N-terminus is blocked.
    The covalent modification of cysteine by 15-deoxy-Delta12,14-prostaglandin-J2 is autocatalytic and reversible. It may occur as an alternative to other cysteine modifications, such as S-nitrosylation and S-palmitoylation By similarity.By similarity

    Keywords - PTMi

    Acetylation, Lipoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP34914.
    PaxDbiP34914.
    PRIDEiP34914.

    2D gel databases

    SWISS-2DPAGEP34914.

    PTM databases

    PhosphoSiteiP34914.

    Expressioni

    Tissue specificityi

    Detected in liver, intestine, ovary and kidney. Detected at low levels in heart and muscle.2 Publications

    Inductioni

    Up-regulated during the luteal phase of the stimulated estrus cycle and by compounds that cause peroxisome proliferation, such as clofibrate, tiadenol and fenofibrate.3 Publications

    Gene expression databases

    ArrayExpressiP34914.
    BgeeiP34914.
    CleanExiMM_EPHX2.
    GenevestigatoriP34914.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    IntActiP34914. 5 interactions.
    MINTiMINT-1859181.

    Structurei

    Secondary structure

    1
    554
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 84
    Helixi10 – 123
    Beta strandi13 – 175
    Turni51 – 566
    Beta strandi57 – 626
    Helixi94 – 974
    Helixi103 – 11412
    Beta strandi118 – 1236
    Beta strandi130 – 1323
    Helixi134 – 14310
    Helixi144 – 1463
    Beta strandi148 – 1525
    Helixi153 – 1564
    Helixi163 – 17311
    Beta strandi177 – 18711
    Turni188 – 1903
    Helixi191 – 1955
    Beta strandi199 – 2024
    Beta strandi205 – 2073
    Helixi208 – 2158
    Beta strandi216 – 2183
    Beta strandi232 – 24110
    Beta strandi243 – 2453
    Beta strandi247 – 2548
    Beta strandi256 – 2627
    Helixi269 – 2746
    Helixi275 – 2817
    Beta strandi285 – 2906
    Helixi304 – 3063
    Helixi308 – 32215
    Beta strandi327 – 3326
    Helixi334 – 34512
    Turni347 – 3493
    Beta strandi350 – 3578
    Helixi369 – 3757
    Helixi377 – 3793
    Helixi380 – 3856
    Helixi390 – 3978
    Helixi399 – 4068
    Turni418 – 4203
    Helixi421 – 4244
    Turni427 – 4304
    Beta strandi439 – 4413
    Helixi443 – 45614
    Helixi459 – 4624
    Helixi463 – 4675
    Helixi468 – 4758
    Helixi476 – 4783
    Beta strandi487 – 4926
    Beta strandi496 – 4983
    Helixi500 – 5034
    Helixi506 – 5083
    Beta strandi514 – 5185
    Helixi525 – 5284
    Helixi530 – 54314

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CQZX-ray2.80A/B1-554[»]
    1CR6X-ray2.80A/B1-554[»]
    1EK1X-ray3.10A/B1-554[»]
    1EK2X-ray3.00A/B1-554[»]
    ProteinModelPortaliP34914.
    SMRiP34914. Positions 4-544.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP34914.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 224224PhosphataseAdd
    BLAST
    Regioni123 – 1242Phosphate bindingBy similarity
    Regioni233 – 554322Epoxide hydrolaseAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi552 – 5543Microbody targeting signalSequence Analysis

    Domaini

    The N-terminal domain has phosphatase activity. The C-terminal domain has epoxide hydrolase activity.

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0596.
    GeneTreeiENSGT00530000063213.
    HOGENOMiHOG000028073.
    HOVERGENiHBG006095.
    InParanoidiP34914.
    KOiK08726.
    OMAiGHWTQMD.
    OrthoDBiEOG72VH5T.
    PhylomeDBiP34914.
    TreeFamiTF315395.

    Family and domain databases

    Gene3Di1.10.150.240. 1 hit.
    3.40.50.1000. 1 hit.
    3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR000073. AB_hydrolase_1.
    IPR000639. Epox_hydrolase-like.
    IPR023214. HAD-like_dom.
    IPR006439. HAD-SF_hydro_IA.
    IPR023198. PGP_dom2.
    [Graphical view]
    PfamiPF00561. Abhydrolase_1. 1 hit.
    PF13419. HAD_2. 1 hit.
    [Graphical view]
    PRINTSiPR00111. ABHYDROLASE.
    PR00412. EPOXHYDRLASE.
    SUPFAMiSSF53474. SSF53474. 1 hit.
    SSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01509. HAD-SF-IA-v3. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P34914-1) [UniParc]FASTAAdd to Basket

    Also known as: Ephx2A

    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

    MALRVAAFDL DGVLALPSIA GAFRRSEEAL ALPRDFLLGA YQTEFPEGPT    50
    EQLMKGKITF SQWVPLMDES YRKSSKACGA NLPENFSISQ IFSQAMAARS 100
    INRPMLQAAI ALKKKGFTTC IVTNNWLDDG DKRDSLAQMM CELSQHFDFL 150
    IESCQVGMIK PEPQIYNFLL DTLKAKPNEV VFLDDFGSNL KPARDMGMVT 200
    ILVHNTASAL RELEKVTGTQ FPEAPLPVPC NPNDVSHGYV TVKPGIRLHF 250
    VEMGSGPALC LCHGFPESWF SWRYQIPALA QAGFRVLAID MKGYGDSSSP 300
    PEIEEYAMEL LCKEMVTFLD KLGIPQAVFI GHDWAGVMVW NMALFYPERV 350
    RAVASLNTPF MPPDPDVSPM KVIRSIPVFN YQLYFQEPGV AEAELEKNMS 400
    RTFKSFFRAS DETGFIAVHK ATEIGGILVN TPEDPNLSKI TTEEEIEFYI 450
    QQFKKTGFRG PLNWYRNTER NWKWSCKGLG RKILVPALMV TAEKDIVLRP 500
    EMSKNMEKWI PFLKRGHIED CGHWTQIEKP TEVNQILIKW LQTEVQNPSV 550
    TSKI 554
    Length:554
    Mass (Da):62,515
    Last modified:October 1, 1996 - v2
    Checksum:i2F3A3F7DACE47C93
    GO
    Isoform 2 (identifier: P34914-2) [UniParc]FASTAAdd to Basket

    Also known as: Ephx2B

    The sequence of this isoform differs from the canonical sequence as follows:
         1-62: MALRVAAFDL...LMKGKITFSQ → MRFAAMAAFS...EDTDTIHTSE

    Show »
    Length:536
    Mass (Da):60,613
    Checksum:iD9BD995CB9347551
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti77 – 771A → T in CAA85471. (PubMed:8750907)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6262MALRV…ITFSQ → MRFAAMAAFSVFFVSKGLLM NSNIWCVGQEGPSQEDTDTI HTSE in isoform 2. 1 PublicationVSP_013904Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L05781 mRNA. Translation: AAA37555.1.
    Z37107 mRNA. Translation: CAA85471.1.
    AY098585 mRNA. Translation: AAM28238.1.
    BC015087 mRNA. Translation: AAH15087.1.
    CCDSiCCDS27218.1. [P34914-1]
    PIRiA47504.
    RefSeqiNP_001258332.1. NM_001271403.1. [P34914-2]
    NP_031966.2. NM_007940.4. [P34914-1]
    UniGeneiMm.15295.

    Genome annotation databases

    EnsembliENSMUST00000070515; ENSMUSP00000069209; ENSMUSG00000022040. [P34914-1]
    GeneIDi13850.
    KEGGimmu:13850.
    UCSCiuc007ujv.1. mouse. [P34914-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L05781 mRNA. Translation: AAA37555.1 .
    Z37107 mRNA. Translation: CAA85471.1 .
    AY098585 mRNA. Translation: AAM28238.1 .
    BC015087 mRNA. Translation: AAH15087.1 .
    CCDSi CCDS27218.1. [P34914-1 ]
    PIRi A47504.
    RefSeqi NP_001258332.1. NM_001271403.1. [P34914-2 ]
    NP_031966.2. NM_007940.4. [P34914-1 ]
    UniGenei Mm.15295.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CQZ X-ray 2.80 A/B 1-554 [» ]
    1CR6 X-ray 2.80 A/B 1-554 [» ]
    1EK1 X-ray 3.10 A/B 1-554 [» ]
    1EK2 X-ray 3.00 A/B 1-554 [» ]
    ProteinModelPortali P34914.
    SMRi P34914. Positions 4-544.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P34914. 5 interactions.
    MINTi MINT-1859181.

    Chemistry

    BindingDBi P34914.
    ChEMBLi CHEMBL4140.

    Protein family/group databases

    MEROPSi S33.973.

    PTM databases

    PhosphoSitei P34914.

    2D gel databases

    SWISS-2DPAGE P34914.

    Proteomic databases

    MaxQBi P34914.
    PaxDbi P34914.
    PRIDEi P34914.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000070515 ; ENSMUSP00000069209 ; ENSMUSG00000022040 . [P34914-1 ]
    GeneIDi 13850.
    KEGGi mmu:13850.
    UCSCi uc007ujv.1. mouse. [P34914-1 ]

    Organism-specific databases

    CTDi 2053.
    MGIi MGI:99500. Ephx2.

    Phylogenomic databases

    eggNOGi COG0596.
    GeneTreei ENSGT00530000063213.
    HOGENOMi HOG000028073.
    HOVERGENi HBG006095.
    InParanoidi P34914.
    KOi K08726.
    OMAi GHWTQMD.
    OrthoDBi EOG72VH5T.
    PhylomeDBi P34914.
    TreeFami TF315395.

    Enzyme and pathway databases

    BRENDAi 3.3.2.10. 3474.
    Reactomei REACT_196570. Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET).

    Miscellaneous databases

    EvolutionaryTracei P34914.
    NextBioi 284704.
    PROi P34914.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P34914.
    Bgeei P34914.
    CleanExi MM_EPHX2.
    Genevestigatori P34914.

    Family and domain databases

    Gene3Di 1.10.150.240. 1 hit.
    3.40.50.1000. 1 hit.
    3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR000073. AB_hydrolase_1.
    IPR000639. Epox_hydrolase-like.
    IPR023214. HAD-like_dom.
    IPR006439. HAD-SF_hydro_IA.
    IPR023198. PGP_dom2.
    [Graphical view ]
    Pfami PF00561. Abhydrolase_1. 1 hit.
    PF13419. HAD_2. 1 hit.
    [Graphical view ]
    PRINTSi PR00111. ABHYDROLASE.
    PR00412. EPOXHYDRLASE.
    SUPFAMi SSF53474. SSF53474. 1 hit.
    SSF56784. SSF56784. 1 hit.
    TIGRFAMsi TIGR01509. HAD-SF-IA-v3. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and expression of murine liver soluble epoxide hydrolase."
      Grant D.F., Storms D.H., Hammock B.D.
      J. Biol. Chem. 268:17628-17633(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, INDUCTION.
      Tissue: Liver.
    2. "Tissue specific basal expression of soluble murine epoxide hydrolase and effects of clofibrate on the mRNA levels in extrahepatic tissues and liver."
      Johansson C., Stark A., Sandberg M., Ek B., Rask L., Meijer J.
      Arch. Toxicol. 70:61-63(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INDUCTION.
      Strain: NMRI.
    3. "Identification and characterization of an ovary-selective isoform of epoxide hydrolase."
      Hennebold J.D., Mah K., Perez W., Vance J.E., Stouffer R.L., Morisseau C., Hammock B.D., Adashi E.Y.
      Biol. Reprod. 72:968-975(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, INDUCTION.
      Strain: C57BL/6.
    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).
      Strain: FVB/N.
      Tissue: Colon.
    5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    6. "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: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-55; LYS-176; LYS-371; LYS-420; LYS-454; LYS-504; LYS-508 AND LYS-553, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    7. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
      Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
      Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-176; LYS-191; LYS-215 AND LYS-508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    8. "Detoxification of environmental mutagens and carcinogens: structure, mechanism, and evolution of liver epoxide hydrolase."
      Argiriadi M.A., Morisseau C., Hammock B.D., Christianson D.W.
      Proc. Natl. Acad. Sci. U.S.A. 96:10637-10642(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
      Tissue: Liver.
    9. "Binding of alkylurea inhibitors to epoxide hydrolase implicates active site tyrosines in substrate activation."
      Argiriadi M.A., Morisseau C., Goodrow M.H., Dowdy D.L., Hammock B.D., Christianson D.W.
      J. Biol. Chem. 275:15265-15270(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH EPOXIDE HYDROLASE INHIBITOR.

    Entry informationi

    Entry nameiHYES_MOUSE
    AccessioniPrimary (citable) accession number: P34914
    Secondary accession number(s): Q8CGV0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: October 1, 1996
    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

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

    Documents

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

    External Data

    Dasty 3