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P09960

- LKHA4_HUMAN

UniProt

P09960 - LKHA4_HUMAN

Protein

Leukotriene A-4 hydrolase

Gene

LTA4H

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 180 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Epoxide hydrolase that catalyzes the final step in the biosynthesis of the proinflammatory mediator leukotriene B4. Has also aminopeptidase activity.7 Publications

    Catalytic activityi

    (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O = (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate.6 Publications

    Cofactori

    Binds 1 zinc ion per subunit.3 Publications

    Enzyme regulationi

    Inhibited by bestatin. Subject to suicide inhibition by leukotriene A4, due to the formation of a covalent adduct at Tyr-379.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi296 – 2961Zinc; catalytic
    Active sitei297 – 2971Proton acceptor1 Publication
    Metal bindingi300 – 3001Zinc; catalytic
    Metal bindingi319 – 3191Zinc; catalytic
    Sitei376 – 3761Essential for epoxide hydrolase activity, but not for aminopeptidase activity
    Sitei379 – 3791Covalently modified during suicide inhibition by leukotrienes
    Active sitei384 – 3841Proton donor1 Publication

    GO - Molecular functioni

    1. aminopeptidase activity Source: UniProtKB
    2. epoxide hydrolase activity Source: UniProtKB
    3. leukotriene-A4 hydrolase activity Source: UniProtKB
    4. metallopeptidase activity Source: UniProtKB-KW
    5. peptidase activity Source: ProtInc
    6. poly(A) RNA binding Source: UniProtKB
    7. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. arachidonic acid metabolic process Source: Reactome
    2. inflammatory response Source: ProtInc
    3. leukotriene biosynthetic process Source: UniProtKB
    4. leukotriene metabolic process Source: Reactome
    5. peptide catabolic process Source: UniProtKB
    6. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Leukotriene biosynthesis

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03372-MONOMER.
    BRENDAi3.3.2.6. 2681.
    ReactomeiREACT_150420. Synthesis of Leukotrienes (LT) and Eoxins (EX).
    UniPathwayiUPA00878.

    Protein family/group databases

    MEROPSiM01.004.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Leukotriene A-4 hydrolase (EC:3.3.2.6)
    Short name:
    LTA-4 hydrolase
    Alternative name(s):
    Leukotriene A(4) hydrolase
    Gene namesi
    Name:LTA4H
    Synonyms:LTA4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:6710. LTA4H.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi135 – 1351Q → A or L: Srongly increased epoxide hydrolase activity. 2 Publications
    Mutagenesisi135 – 1351Q → A: Strongly reduced aminopeptidase activity. Strongly decreased affinity for leukotriene. Abolishes epoxide hydrolase activity. 2 Publications
    Mutagenesisi137 – 1371Q → A: No loss of activity. 2 Publications
    Mutagenesisi137 – 1371Q → L: Aminopeptidase activity strongly impaired, but keeps LTA4 activity. 2 Publications
    Mutagenesisi137 – 1371Q → N: Aminopeptidase activity almost absent, but keeps LTA4 activity. 2 Publications
    Mutagenesisi140 – 1401H → Q: Aminopeptidase activity almost absent, but keeps LTA4 activity. 2 Publications
    Mutagenesisi269 – 2691G → A: No loss of activity. 1 Publication
    Mutagenesisi270 – 2701G → A: No loss of activity. 2 Publications
    Mutagenesisi271 – 2711M → L: No loss of activity. 2 Publications
    Mutagenesisi272 – 2721E → A or D: Complete loss of activity. 2 Publications
    Mutagenesisi272 – 2721E → Q: Loss of LTA4 activity, and aminopeptidase activity strongly impaired. 2 Publications
    Mutagenesisi273 – 2731N → A: No loss of activity. 2 Publications
    Mutagenesisi296 – 2961H → Y: Complete loss of activity. 1 Publication
    Mutagenesisi297 – 2971E → A: Loss of both activities. 4 Publications
    Mutagenesisi297 – 2971E → K: Loss of both activities. 4 Publications
    Mutagenesisi297 – 2971E → Q: Loss of aminopeptidase activity, but keeps LTA4 activity. 4 Publications
    Mutagenesisi300 – 3001H → L: Complete loss of activity. 1 Publication
    Mutagenesisi319 – 3191E → A: Complete loss of activity. 1 Publication
    Mutagenesisi372 – 3721D → N: No loss of activity. 2 Publications
    Mutagenesisi374 – 3741D → N: No loss of activity. 2 Publications
    Mutagenesisi376 – 3761D → A: Strongly reduced hydrolysis of peptides starting with Arg. Small effect on hydrolysis of peptides starting with Ala. Strongly reduced epoxide hydrolase activity. 3 Publications
    Mutagenesisi376 – 3761D → E: Strongly reduced aminopeptidase activity. Abolishes epoxide hydrolase activity. 3 Publications
    Mutagenesisi376 – 3761D → N: Abolishes aminopeptidase and epoxide hydrolase activity. 3 Publications
    Mutagenesisi385 – 3851E → Q: Reduced aminopeptidase activity. Minor effect on epoxide hydrolase activity. 2 Publications
    Mutagenesisi564 – 5641R → A, K or M: Abolishes epoxide hydrolase activity. Reduced aminopeptidase activity. 2 Publications
    Mutagenesisi566 – 5661K → A or M: Strongly reduced affinity for peptide substrates. Reduced epoxide hydrolase and aminopeptidase activity. 2 Publications
    Mutagenesisi566 – 5661K → R: No effect on epoxide hydrolase and aminopeptidase activity. 2 Publications

    Organism-specific databases

    PharmGKBiPA24345.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 611610Leukotriene A-4 hydrolasePRO_0000095124Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei73 – 731N6-acetyllysine1 Publication
    Modified residuei337 – 3371N6-acetyllysine1 Publication
    Modified residuei414 – 4141N6-acetyllysine1 Publication
    Modified residuei416 – 4161Phosphoserine1 Publication
    Modified residuei573 – 5731N6-acetyllysine1 Publication

    Post-translational modificationi

    Phosphorylation at Ser-416 inhibits enzymatic activity.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP09960.
    PaxDbiP09960.
    PRIDEiP09960.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00219077.

    PTM databases

    PhosphoSiteiP09960.

    Expressioni

    Tissue specificityi

    Isoform 1 and isoform 2 are expressed in monocytes, lymphocytes, neutrophils, reticulocytes, platelets and fibroblasts.

    Gene expression databases

    ArrayExpressiP09960.
    BgeeiP09960.
    CleanExiHS_LTA4H.
    GenevestigatoriP09960.

    Organism-specific databases

    HPAiCAB015221.
    HPA008399.
    HPA017017.

    Interactioni

    Subunit structurei

    Monomer.3 Publications

    Protein-protein interaction databases

    BioGridi110226. 12 interactions.
    IntActiP09960. 5 interactions.
    MINTiMINT-1388946.
    STRINGi9606.ENSP00000228740.

    Structurei

    Secondary structure

    1
    611
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni14 – 163
    Beta strandi17 – 2913
    Turni30 – 334
    Beta strandi34 – 4512
    Beta strandi50 – 5910
    Beta strandi61 – 677
    Beta strandi74 – 763
    Helixi81 – 833
    Beta strandi85 – 9511
    Beta strandi100 – 1089
    Beta strandi116 – 1194
    Helixi121 – 1233
    Beta strandi124 – 1296
    Beta strandi131 – 1344
    Turni137 – 1404
    Helixi141 – 1433
    Beta strandi155 – 16410
    Beta strandi167 – 18014
    Beta strandi182 – 1843
    Beta strandi187 – 19812
    Helixi200 – 2023
    Beta strandi205 – 2095
    Beta strandi211 – 2166
    Beta strandi219 – 2235
    Helixi225 – 2273
    Helixi228 – 2347
    Turni235 – 2373
    Helixi238 – 24912
    Beta strandi258 – 2614
    Beta strandi267 – 2715
    Beta strandi276 – 2794
    Helixi281 – 2833
    Beta strandi286 – 2883
    Turni289 – 2913
    Helixi292 – 2998
    Turni300 – 3023
    Turni304 – 3063
    Beta strandi307 – 3115
    Helixi312 – 3143
    Helixi315 – 33420
    Helixi336 – 35722
    Helixi362 – 3643
    Beta strandi365 – 3673
    Helixi375 – 3784
    Helixi382 – 39817
    Helixi401 – 41515
    Beta strandi418 – 4203
    Helixi422 – 43211
    Helixi434 – 4363
    Helixi437 – 4415
    Helixi445 – 4506
    Turni464 – 4663
    Helixi467 – 47812
    Helixi481 – 4866
    Helixi489 – 4924
    Helixi497 – 50812
    Helixi515 – 52511
    Helixi527 – 5293
    Helixi533 – 54513
    Helixi551 – 56111
    Helixi565 – 57713
    Helixi579 – 59214
    Helixi593 – 5953
    Helixi598 – 60811

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GW6X-ray2.20A2-611[»]
    1H19X-ray2.10A2-611[»]
    1HS6X-ray1.95A1-611[»]
    1SQMX-ray2.30A2-611[»]
    2R59X-ray1.89A2-611[»]
    2VJ8X-ray1.80A1-611[»]
    3B7RX-ray1.81L2-611[»]
    3B7SX-ray1.47A2-611[»]
    3B7TX-ray2.30A2-611[»]
    3B7UX-ray1.90X2-611[»]
    3CHOX-ray1.80A2-611[»]
    3CHPX-ray2.10A2-611[»]
    3CHQX-ray2.09A2-611[»]
    3CHRX-ray2.20A2-611[»]
    3CHSX-ray2.55A2-611[»]
    3FH5X-ray1.63A1-611[»]
    3FH7X-ray2.05A1-611[»]
    3FH8X-ray1.67A1-611[»]
    3FHEX-ray2.16A1-611[»]
    3FTSX-ray2.33A1-611[»]
    3FTUX-ray1.90A1-611[»]
    3FTVX-ray1.70A1-611[»]
    3FTWX-ray1.85A1-611[»]
    3FTXX-ray1.96A1-611[»]
    3FTYX-ray2.15A1-611[»]
    3FTZX-ray2.00A1-611[»]
    3FU0X-ray1.80A1-611[»]
    3FU3X-ray2.00A1-611[»]
    3FU5X-ray2.30A1-611[»]
    3FU6X-ray2.05A1-611[»]
    3FUDX-ray2.20A1-611[»]
    3FUEX-ray2.38A1-611[»]
    3FUFX-ray2.60A1-611[»]
    3FUHX-ray1.80A1-611[»]
    3FUIX-ray2.20A1-611[»]
    3FUJX-ray1.90A1-611[»]
    3FUKX-ray1.95A1-611[»]
    3FULX-ray2.39A1-611[»]
    3FUMX-ray2.15A1-611[»]
    3FUNX-ray1.58A1-611[»]
    3U9WX-ray1.25A4-611[»]
    4DPRX-ray2.02A1-611[»]
    4L2LX-ray1.65A1-611[»]
    4MKTX-ray1.62A1-611[»]
    4MS6X-ray1.72A1-611[»]
    ProteinModelPortaliP09960.
    SMRiP09960. Positions 4-611.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09960.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni135 – 1373Substrate binding
    Regioni267 – 2726Substrate binding
    Regioni564 – 5663Substrate binding

    Sequence similaritiesi

    Belongs to the peptidase M1 family.Curated

    Phylogenomic databases

    eggNOGiCOG0308.
    HOGENOMiHOG000293296.
    HOVERGENiHBG001274.
    InParanoidiP09960.
    KOiK01254.
    OMAiSPASVCQ.
    OrthoDBiEOG7SJD42.
    PhylomeDBiP09960.
    TreeFamiTF300758.

    Family and domain databases

    InterProiIPR016024. ARM-type_fold.
    IPR012777. Leukotriene_A4_hydrolase.
    IPR001930. Peptidase_M1.
    IPR015211. Peptidase_M1_C.
    IPR014782. Peptidase_M1_N.
    [Graphical view]
    PANTHERiPTHR11533. PTHR11533. 1 hit.
    PfamiPF09127. Leuk-A4-hydro_C. 1 hit.
    PF01433. Peptidase_M1. 1 hit.
    [Graphical view]
    PRINTSiPR00756. ALADIPTASE.
    SUPFAMiSSF48371. SSF48371. 1 hit.
    TIGRFAMsiTIGR02411. leuko_A4_hydro. 1 hit.
    PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P09960-1) [UniParc]FASTAAdd to Basket

    Also known as: L-LTA4

    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

    MPEIVDTCSL ASPASVCRTK HLHLRCSVDF TRRTLTGTAA LTVQSQEDNL    50
    RSLVLDTKDL TIEKVVINGQ EVKYALGERQ SYKGSPMEIS LPIALSKNQE 100
    IVIEISFETS PKSSALQWLT PEQTSGKEHP YLFSQCQAIH CRAILPCQDT 150
    PSVKLTYTAE VSVPKELVAL MSAIRDGETP DPEDPSRKIY KFIQKVPIPC 200
    YLIALVVGAL ESRQIGPRTL VWSEKEQVEK SAYEFSETES MLKIAEDLGG 250
    PYVWGQYDLL VLPPSFPYGG MENPCLTFVT PTLLAGDKSL SNVIAHEISH 300
    SWTGNLVTNK TWDHFWLNEG HTVYLERHIC GRLFGEKFRH FNALGGWGEL 350
    QNSVKTFGET HPFTKLVVDL TDIDPDVAYS SVPYEKGFAL LFYLEQLLGG 400
    PEIFLGFLKA YVEKFSYKSI TTDDWKDFLY SYFKDKVDVL NQVDWNAWLY 450
    SPGLPPIKPN YDMTLTNACI ALSQRWITAK EDDLNSFNAT DLKDLSSHQL 500
    NEFLAQTLQR APLPLGHIKR MQEVYNFNAI NNSEIRFRWL RLCIQSKWED 550
    AIPLALKMAT EQGRMKFTRP LFKDLAAFDK SHDQAVRTYQ EHKASMHPVT 600
    AMLVGKDLKV D 611
    Length:611
    Mass (Da):69,285
    Last modified:January 23, 2007 - v2
    Checksum:i329BF6D04D4A06E1
    GO
    Isoform 2 (identifier: P09960-2) [UniParc]FASTAAdd to Basket

    Also known as: S-LTA4

    The sequence of this isoform differs from the canonical sequence as follows:
         511-532: APLPLGHIKRMQEVYNFNAINN → MAAALHSIQVGGRNSFGAKDGN
         533-611: Missing.

    Show »
    Length:532
    Mass (Da):59,733
    Checksum:i474891F08B0215A8
    GO
    Isoform 3 (identifier: P09960-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-53: MPEIVDTCSL...QSQEDNLRSL → MLPQRNLSKRQVPTMHIPVKTRRLLAALK
         511-532: APLPLGHIKRMQEVYNFNAINN → MAAALHSIQVGGRNSFGAKDGN
         533-611: Missing.

    Show »
    Length:508
    Mass (Da):57,300
    Checksum:iA1CDA72AF83A875C
    GO
    Isoform 4 (identifier: P09960-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-53: MPEIVDTCSL...QSQEDNLRSL → MLPQRNLSKRQVPTMHIPVKTRRLLAALK

    Note: No experimental confirmation available.

    Show »
    Length:587
    Mass (Da):66,852
    Checksum:iA70BF2792A0427C7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti115 – 1151A → T in BX647158. (PubMed:17974005)Curated
    Sequence conflicti123 – 1231Q → R in BX647158. (PubMed:17974005)Curated
    Sequence conflicti297 – 2971E → G in BAG60321. (PubMed:14702039)Curated
    Sequence conflicti309 – 3091N → S in BX647158. (PubMed:17974005)Curated
    Sequence conflicti378 – 3781A → V in BX647158. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti131 – 1311Y → H.
    Corresponds to variant rs45630737 [ dbSNP | Ensembl ].
    VAR_051570

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5353MPEIV…NLRSL → MLPQRNLSKRQVPTMHIPVK TRRLLAALK in isoform 3 and isoform 4. 2 PublicationsVSP_041107Add
    BLAST
    Alternative sequencei511 – 53222APLPL…NAINN → MAAALHSIQVGGRNSFGAKD GN in isoform 2 and isoform 3. 1 PublicationVSP_041108Add
    BLAST
    Alternative sequencei533 – 61179Missing in isoform 2 and isoform 3. 1 PublicationVSP_041109Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03459 mRNA. Translation: AAA36176.1.
    J02959 mRNA. Translation: AAA36177.1.
    U27293
    , U27275, U27276, U27277, U27278, U27279, U27280, U27281, U27282, U27283, U27284, U27285, U27286, U27287, U27288, U27289, U27290, U27291, U27292 Genomic DNA. Translation: AAA89077.1.
    AK298017 mRNA. Translation: BAG60321.1.
    CR457068 mRNA. Translation: CAG33349.1.
    BX647158 mRNA. No translation available.
    AC007298 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW97559.1.
    BC032528 mRNA. Translation: AAH32528.1.
    U43410 Genomic DNA. No translation available.
    U43411 Genomic DNA. No translation available.
    CCDSiCCDS58266.1. [P09960-3]
    CCDS58267.1. [P09960-4]
    CCDS9059.1. [P09960-1]
    PIRiS65947.
    RefSeqiNP_000886.1. NM_000895.2. [P09960-1]
    NP_001243572.1. NM_001256643.1. [P09960-4]
    NP_001243573.1. NM_001256644.1. [P09960-3]
    XP_005268928.1. XM_005268871.1. [P09960-2]
    UniGeneiHs.524648.

    Genome annotation databases

    EnsembliENST00000228740; ENSP00000228740; ENSG00000111144. [P09960-1]
    ENST00000413268; ENSP00000395051; ENSG00000111144. [P09960-3]
    ENST00000552789; ENSP00000449958; ENSG00000111144. [P09960-4]
    GeneIDi4048.
    KEGGihsa:4048.
    UCSCiuc001ten.2. human. [P09960-1]
    uc010suz.2. human. [P09960-3]

    Polymorphism databases

    DMDMi126353.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03459 mRNA. Translation: AAA36176.1 .
    J02959 mRNA. Translation: AAA36177.1 .
    U27293
    , U27275 , U27276 , U27277 , U27278 , U27279 , U27280 , U27281 , U27282 , U27283 , U27284 , U27285 , U27286 , U27287 , U27288 , U27289 , U27290 , U27291 , U27292 Genomic DNA. Translation: AAA89077.1 .
    AK298017 mRNA. Translation: BAG60321.1 .
    CR457068 mRNA. Translation: CAG33349.1 .
    BX647158 mRNA. No translation available.
    AC007298 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW97559.1 .
    BC032528 mRNA. Translation: AAH32528.1 .
    U43410 Genomic DNA. No translation available.
    U43411 Genomic DNA. No translation available.
    CCDSi CCDS58266.1. [P09960-3 ]
    CCDS58267.1. [P09960-4 ]
    CCDS9059.1. [P09960-1 ]
    PIRi S65947.
    RefSeqi NP_000886.1. NM_000895.2. [P09960-1 ]
    NP_001243572.1. NM_001256643.1. [P09960-4 ]
    NP_001243573.1. NM_001256644.1. [P09960-3 ]
    XP_005268928.1. XM_005268871.1. [P09960-2 ]
    UniGenei Hs.524648.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GW6 X-ray 2.20 A 2-611 [» ]
    1H19 X-ray 2.10 A 2-611 [» ]
    1HS6 X-ray 1.95 A 1-611 [» ]
    1SQM X-ray 2.30 A 2-611 [» ]
    2R59 X-ray 1.89 A 2-611 [» ]
    2VJ8 X-ray 1.80 A 1-611 [» ]
    3B7R X-ray 1.81 L 2-611 [» ]
    3B7S X-ray 1.47 A 2-611 [» ]
    3B7T X-ray 2.30 A 2-611 [» ]
    3B7U X-ray 1.90 X 2-611 [» ]
    3CHO X-ray 1.80 A 2-611 [» ]
    3CHP X-ray 2.10 A 2-611 [» ]
    3CHQ X-ray 2.09 A 2-611 [» ]
    3CHR X-ray 2.20 A 2-611 [» ]
    3CHS X-ray 2.55 A 2-611 [» ]
    3FH5 X-ray 1.63 A 1-611 [» ]
    3FH7 X-ray 2.05 A 1-611 [» ]
    3FH8 X-ray 1.67 A 1-611 [» ]
    3FHE X-ray 2.16 A 1-611 [» ]
    3FTS X-ray 2.33 A 1-611 [» ]
    3FTU X-ray 1.90 A 1-611 [» ]
    3FTV X-ray 1.70 A 1-611 [» ]
    3FTW X-ray 1.85 A 1-611 [» ]
    3FTX X-ray 1.96 A 1-611 [» ]
    3FTY X-ray 2.15 A 1-611 [» ]
    3FTZ X-ray 2.00 A 1-611 [» ]
    3FU0 X-ray 1.80 A 1-611 [» ]
    3FU3 X-ray 2.00 A 1-611 [» ]
    3FU5 X-ray 2.30 A 1-611 [» ]
    3FU6 X-ray 2.05 A 1-611 [» ]
    3FUD X-ray 2.20 A 1-611 [» ]
    3FUE X-ray 2.38 A 1-611 [» ]
    3FUF X-ray 2.60 A 1-611 [» ]
    3FUH X-ray 1.80 A 1-611 [» ]
    3FUI X-ray 2.20 A 1-611 [» ]
    3FUJ X-ray 1.90 A 1-611 [» ]
    3FUK X-ray 1.95 A 1-611 [» ]
    3FUL X-ray 2.39 A 1-611 [» ]
    3FUM X-ray 2.15 A 1-611 [» ]
    3FUN X-ray 1.58 A 1-611 [» ]
    3U9W X-ray 1.25 A 4-611 [» ]
    4DPR X-ray 2.02 A 1-611 [» ]
    4L2L X-ray 1.65 A 1-611 [» ]
    4MKT X-ray 1.62 A 1-611 [» ]
    4MS6 X-ray 1.72 A 1-611 [» ]
    ProteinModelPortali P09960.
    SMRi P09960. Positions 4-611.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110226. 12 interactions.
    IntActi P09960. 5 interactions.
    MINTi MINT-1388946.
    STRINGi 9606.ENSP00000228740.

    Chemistry

    BindingDBi P09960.
    ChEMBLi CHEMBL4618.
    GuidetoPHARMACOLOGYi 1395.

    Protein family/group databases

    MEROPSi M01.004.

    PTM databases

    PhosphoSitei P09960.

    Polymorphism databases

    DMDMi 126353.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00219077.

    Proteomic databases

    MaxQBi P09960.
    PaxDbi P09960.
    PRIDEi P09960.

    Protocols and materials databases

    DNASUi 4048.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000228740 ; ENSP00000228740 ; ENSG00000111144 . [P09960-1 ]
    ENST00000413268 ; ENSP00000395051 ; ENSG00000111144 . [P09960-3 ]
    ENST00000552789 ; ENSP00000449958 ; ENSG00000111144 . [P09960-4 ]
    GeneIDi 4048.
    KEGGi hsa:4048.
    UCSCi uc001ten.2. human. [P09960-1 ]
    uc010suz.2. human. [P09960-3 ]

    Organism-specific databases

    CTDi 4048.
    GeneCardsi GC12M096394.
    HGNCi HGNC:6710. LTA4H.
    HPAi CAB015221.
    HPA008399.
    HPA017017.
    MIMi 151570. gene.
    neXtProti NX_P09960.
    PharmGKBi PA24345.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0308.
    HOGENOMi HOG000293296.
    HOVERGENi HBG001274.
    InParanoidi P09960.
    KOi K01254.
    OMAi SPASVCQ.
    OrthoDBi EOG7SJD42.
    PhylomeDBi P09960.
    TreeFami TF300758.

    Enzyme and pathway databases

    UniPathwayi UPA00878 .
    BioCyci MetaCyc:HS03372-MONOMER.
    BRENDAi 3.3.2.6. 2681.
    Reactomei REACT_150420. Synthesis of Leukotrienes (LT) and Eoxins (EX).

    Miscellaneous databases

    ChiTaRSi LTA4H. human.
    EvolutionaryTracei P09960.
    GenomeRNAii 4048.
    NextBioi 15856.
    PROi P09960.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P09960.
    Bgeei P09960.
    CleanExi HS_LTA4H.
    Genevestigatori P09960.

    Family and domain databases

    InterProi IPR016024. ARM-type_fold.
    IPR012777. Leukotriene_A4_hydrolase.
    IPR001930. Peptidase_M1.
    IPR015211. Peptidase_M1_C.
    IPR014782. Peptidase_M1_N.
    [Graphical view ]
    PANTHERi PTHR11533. PTHR11533. 1 hit.
    Pfami PF09127. Leuk-A4-hydro_C. 1 hit.
    PF01433. Peptidase_M1. 1 hit.
    [Graphical view ]
    PRINTSi PR00756. ALADIPTASE.
    SUPFAMi SSF48371. SSF48371. 1 hit.
    TIGRFAMsi TIGR02411. leuko_A4_hydro. 1 hit.
    PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of a cDNA coding for human leukotriene A4 hydrolase. Complete primary structure of an enzyme involved in eicosanoid synthesis."
      Minami M., Ohno S., Kawasaki H., Raedmark O., Samuelsson B., Joernvall H., Shimizu T., Seyama Y., Suzuki K.
      J. Biol. Chem. 262:13873-13876(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    3. "Cloning and characterization of the human leukotriene A4 hydrolase gene."
      Mancini J.A., Evans J.F.
      Eur. J. Biochem. 231:65-71(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "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] (ISOFORM 3).
      Tissue: Lung.
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Esophageal carcinoma.
    7. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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).
      Tissue: Eye.
    10. "Leukotriene A4 hydrolase in the human B-lymphocytic cell line Raji: indications of catalytically divergent forms of the enzyme."
      Odlander B., Claesson H.E., Bergman T., Radmark O., Joernvall H., Haeggstrom J.Z.
      Arch. Biochem. Biophys. 287:167-174(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-22, FUNCTION, CATALYTIC ACTIVITY.
      Tissue: B-cell.
    11. "Leukotriene A4 hydrolase in human leukocytes. Purification and properties."
      Radmark O., Shimizu T., Joernvall H., Samuelsson B.
      J. Biol. Chem. 259:12339-12345(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-16.
    12. "Leukotriene A4 hydrolase: mapping of a henicosapeptide involved in mechanism-based inactivation."
      Mueller M.J., Wetterholm A., Blomster M., Jornvall H., Samuelsson B., Haeggstrom J.Z.
      Proc. Natl. Acad. Sci. U.S.A. 92:8383-8387(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 366-386, ENZYME REGULATION, COVALENT MODIFICATION AT TYR-379, CATALYTIC ACTIVITY.
    13. "The human leukotriene A4 hydrolase gene is expressed in two alternatively spliced mRNA forms."
      Jendraschak E., Kaminski W.E., Kiefl R., von Schacky C.
      Biochem. J. 314:733-737(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 511-611, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
    14. "Molecular evolution and zinc ion binding motif of leukotriene A4 hydrolase."
      Toh H., Minami M., Shimizu T.
      Biochem. Biophys. Res. Commun. 171:216-221(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: ZINC-BINDING, FUNCTION AS A PEPTIDASE, SIMILARITY TO ZINC PROTEASES.
    15. Cited for: ZINC-BINDING, FUNCTION AS A PEPTIDASE.
    16. "Leukotriene A4 hydrolase: determination of the three zinc-binding ligands by site-directed mutagenesis and zinc analysis."
      Medina J.F., Wetterholm A., Raadmark O., Shapiro R., Haeggstroem J.Z., Vallee B.L., Samuelsson B.
      Proc. Natl. Acad. Sci. U.S.A. 88:7620-7624(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ZINC LIGANDS.
    17. "Leukotriene A4 hydrolase, a bifunctional enzyme. Distinction of leukotriene A4 hydrolase and aminopeptidase activities by site-directed mutagenesis at Glu-297."
      Minami M., Bito H., Ohishi N., Tsuge H., Miyano M., Mori M., Wada H., Mutoh H., Shimada S., Izumi T., Abe K., Shimuzu T.
      FEBS Lett. 309:353-357(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLU-297.
    18. "Leukotriene A4 hydrolase: abrogation of the peptidase activity by mutation of glutamic acid-296."
      Wetterholm A., Medina J.F., Raadmark O., Shapiro R., Haeggstroem J.Z., Vallee B.L., Samuelsson B.
      Proc. Natl. Acad. Sci. U.S.A. 89:9141-9145(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLU-297.
    19. "Regulation of leukotriene A4 hydrolase activity in endothelial cells by phosphorylation."
      Rybina I.V., Liu H., Gor Y., Feinmark S.J.
      J. Biol. Chem. 272:31865-31871(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-416.
    20. "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-73; LYS-337; LYS-414 AND LYS-573, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Crystal structure of human leukotriene A(4) hydrolase, a bifunctional enzyme in inflammation."
      Thunnissen M.M.G.M., Nordlund P., Haeggstroem J.Z.
      Nat. Struct. Biol. 8:131-135(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
    24. "Crystal structures of leukotriene A4 hydrolase in complex with captopril and two competitive tight-binding inhibitors."
      Thunnissen M.M., Andersson B., Samuelsson B., Wong C.H., Haeggstrom J.Z.
      FASEB J. 16:1648-1650(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH CAPTOPRIL AND ZINC IONS, FUNCTION, COFACTOR, CATALYTIC ACTIVITY, ACTIVE SITE.
    25. "Leukotriene A4 hydrolase/aminopeptidase. Glutamate 271 is a catalytic residue with specific roles in two distinct enzyme mechanisms."
      Rudberg P.C., Tholander F., Thunnissen M.M.G.M., Haeggstroem J.Z.
      J. Biol. Chem. 277:1398-1404(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT GLN-272, MUTAGENESIS OF GLN-137; GLY-270; MET-271; GLU-272 AND ASN-273.
    26. "Leukotriene A4 hydrolase: selective abrogation of leukotriene B4 formation by mutation of aspartic acid 375."
      Rudberg P.C., Tholander F., Thunnissen M.M., Samuelsson B., Haeggstrom J.Z.
      Proc. Natl. Acad. Sci. U.S.A. 99:4215-4220(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT ASN-376 IN COMPLEX WITH BESTATIN AND ZINC IONS, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLN-135; HIS-140; ASP-372; ASP-374; ASP-376 AND GLU-385.
    27. "Leukotriene A4 hydrolase: identification of a common carboxylate recognition site for the epoxide hydrolase and aminopeptidase substrates."
      Rudberg P.C., Tholander F., Andberg M., Thunnissen M.M., Haeggstrom J.Z.
      J. Biol. Chem. 279:27376-27382(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT ALA-564 IN COMPLEX WITH ZINC IONS, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, MUTAGENESIS OF ARG-564 AND LYS-566.
    28. "Structure-based dissection of the active site chemistry of leukotriene A4 hydrolase: implications for M1 aminopeptidases and inhibitor design."
      Tholander F., Muroya A., Roques B.P., Fournie-Zaluski M.C., Thunnissen M.M., Haeggstrom J.Z.
      Chem. Biol. 15:920-929(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) OF MUTANT GLN-297 IN COMPLEXES WITH SUBSTRATE TRIPEPTIDES AND ZINC IONS, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, MUTAGENESIS OF GLU-297 AND ASP-376.
    29. Cited for: X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) IN COMPLEXES WITH INHIBITORS AND ZINC IONS.

    Entry informationi

    Entry nameiLKHA4_HUMAN
    AccessioniPrimary (citable) accession number: P09960
    Secondary accession number(s): B4DNQ9
    , F8VV40, Q6IAT6, Q9UCT7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 180 of the entry and version 2 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 12
      Human chromosome 12: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. Peptidase families
      Classification of peptidase families and list of entries
    8. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3