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Q9UMR5

- PPT2_HUMAN

UniProt

Q9UMR5 - PPT2_HUMAN

Protein

Lysosomal thioesterase PPT2

Gene

PPT2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 4 (18 May 2010)
      Previous versions | rss
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    Functioni

    Removes thioester-linked fatty acyl groups from various substrates including S-palmitoyl-CoA. Has the highest S-thioesterase activity for the acyl groups palmitic and myristic acid followed by other short- and long-chain acyl substrates. However, because of structural constraints, is unable to remove palmitate from peptides or proteins.3 Publications

    Kineticsi

    1. KM=67 µM for S-palmitoyl-CoA1 Publication
    2. KM=37 µM for S-palmitoyl-N-acetylcysteamine1 Publication
    3. KM=117 µM for 4-methylumbelliferyl-6-S-palmitoyl-beta-D-glucopyranoside1 Publication

    Vmax=1.7 µmol/min/mg enzyme toward S-palmitoyl-CoA1 Publication

    Vmax=3.3 µmol/min/mg enzyme toward S-palmitoyl-N-acetylcysteamine1 Publication

    Vmax=0.43 µmol/min/mg enzyme toward 4-methylumbelliferyl-6-S-palmitoyl-beta-D-glucopyranoside1 Publication

    pH dependencei

    Optimum pH is 7.0.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei111 – 1111Nucleophile
    Active sitei228 – 2281
    Active sitei283 – 2831

    GO - Molecular functioni

    1. palmitoyl-(protein) hydrolase activity Source: UniProtKB
    2. thiolester hydrolase activity Source: UniProtKB

    GO - Biological processi

    1. cellular protein modification process Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysosomal thioesterase PPT2 (EC:3.1.2.-)
    Short name:
    PPT-2
    Alternative name(s):
    S-thioesterase G14
    Gene namesi
    Name:PPT2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:9326. PPT2.

    Subcellular locationi

    Lysosome 1 Publication

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. lysosome Source: UniProtKB

    Keywords - Cellular componenti

    Lysosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi111 – 1111S → A: Abolishes enzymatic activity. 1 Publication
    Mutagenesisi228 – 2281D → A: Abolishes enzymatic activity. 1 Publication
    Mutagenesisi283 – 2831H → A: Abolishes enzymatic activity. 1 Publication
    Mutagenesisi287 – 2871H → A: No effect on enzymatic activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA33689.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Sequence AnalysisAdd
    BLAST
    Chaini28 – 302275Lysosomal thioesterase PPT2PRO_0000025554Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi60 – 601N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi109 ↔ 1171 Publication
    Disulfide bondi165 ↔ 1761 Publication
    Glycosylationi190 – 1901N-linked (GlcNAc...)1 Publication
    Glycosylationi206 – 2061N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi245 – 2451N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi276 ↔ 2961 Publication
    Glycosylationi289 – 2891N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ9UMR5.
    PaxDbiQ9UMR5.
    PRIDEiQ9UMR5.

    Expressioni

    Tissue specificityi

    Broadly expressed, with highest levels in skeletal muscle.1 Publication

    Gene expression databases

    ArrayExpressiQ9UMR5.
    BgeeiQ9UMR5.
    GenevestigatoriQ9UMR5.

    Organism-specific databases

    HPAiHPA000414.

    Interactioni

    Protein-protein interaction databases

    BioGridi114775. 27 interactions.
    MINTiMINT-4721124.

    Structurei

    Secondary structure

    1
    302
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi39 – 424
    Helixi49 – 524
    Helixi53 – 6210
    Beta strandi68 – 703
    Helixi77 – 804
    Helixi83 – 10018
    Beta strandi105 – 1106
    Helixi112 – 12312
    Beta strandi129 – 1368
    Helixi147 – 1526
    Helixi158 – 1658
    Helixi170 – 1723
    Helixi175 – 1784
    Helixi185 – 1917
    Helixi195 – 1984
    Helixi207 – 2148
    Beta strandi218 – 2247
    Beta strandi229 – 2335
    Helixi234 – 2385
    Helixi251 – 2533
    Helixi255 – 2584
    Turni259 – 2624
    Helixi264 – 2696
    Beta strandi273 – 2775
    Turni283 – 2875
    Helixi290 – 2967
    Helixi298 – 3003

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PJAX-ray2.70A1-302[»]
    ProteinModelPortaliQ9UMR5.
    SMRiQ9UMR5. Positions 35-302.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UMR5.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG1075.
    HOVERGENiHBG019159.
    InParanoidiQ9UMR5.
    KOiK01074.
    OMAiVPWISEL.
    PhylomeDBiQ9UMR5.
    TreeFamiTF323926.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR002472. Palm_thioest.
    [Graphical view]
    PfamiPF02089. Palm_thioest. 1 hit.
    [Graphical view]
    PRINTSiPR00414. PPTHIESTRASE.
    SUPFAMiSSF53474. SSF53474. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UMR5-1) [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

    MLGLCGQRLP AAWVLLLLPF LPLLLLAAPA PHRASYKPVI VVHGLFDSSY    50
    SFRHLLEYIN ETHPGTVVTV LDLFDGRESL RPLWEQVQGF REAVVPIMAK 100
    APQGVHLICY SQGGLVCRAL LSVMDDHNVD SFISLSSPQM GQYGDTDYLK 150
    WLFPTSMRSN LYRICYSPWG QEFSICNYWH DPHHDDLYLN ASSFLALING 200
    ERDHPNATVW RKNFLRVGHL VLIGGPDDGV ITPWQSSFFG FYDANETVLE 250
    MEEQLVYLRD SFGLKTLLAR GAIVRCPMAG ISHTAWHSNR TLYETCIEPW 300
    LS 302
    Length:302
    Mass (Da):34,225
    Last modified:May 18, 2010 - v4
    Checksum:iE242D677970B4BEA
    GO
    Isoform 2 (identifier: Q9UMR5-2) [UniParc]FASTAAdd to Basket

    Also known as: I

    The sequence of this isoform differs from the canonical sequence as follows:
         256-300: VYLRDSFGLK...TLYETCIEPW → PARPTHQSEL...ESWGPGLSCA

    Note: Catalytically inactive due to lack of His-283. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:301
    Mass (Da):34,055
    Checksum:i37EC25978B3FE96E
    GO
    Isoform 3 (identifier: Q9UMR5-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MKSCGSM

    Note: No experimental confirmation available.

    Show »
    Length:308
    Mass (Da):34,819
    Checksum:iE83460052465B3A4
    GO

    Sequence cautioni

    The sequence CAG38577.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti189 – 1891L → P in CAG38577. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti5 – 51C → W.10 Publications
    Corresponds to variant rs3134604 [ dbSNP | Ensembl ].
    VAR_027107
    Natural varianti34 – 341A → E.3 Publications
    Corresponds to variant rs3096696 [ dbSNP | Ensembl ].
    VAR_027108

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MKSCGSM in isoform 3. 1 PublicationVSP_054027
    Alternative sequencei256 – 30045VYLRD…CIEPW → PARPTHQSELLLLRLVCLKP PRRKKPACRVQRQSESWGPG LSCA in isoform 2. 2 PublicationsVSP_005188Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF020543 mRNA. Translation: AAB80730.1.
    AF020544 mRNA. Translation: AAB80731.1.
    Y17958 mRNA. Translation: CAB46981.1.
    AL110128 mRNA. Translation: CAB53659.1.
    CR533546 mRNA. Translation: CAG38577.1. Different initiation.
    AK292729 mRNA. Translation: BAF85418.1.
    U89336 Genomic DNA. Translation: AAB47495.1.
    AL662828 Genomic DNA. Translation: CAI17424.1.
    AL662828 Genomic DNA. Translation: CAI17426.2.
    AL662828 Genomic DNA. Translation: CAM24823.1.
    AL662828 Genomic DNA. Translation: CAM24825.1.
    AL662884 Genomic DNA. Translation: CAI18342.1.
    AL662884 Genomic DNA. Translation: CAI18344.1.
    AL662884 Genomic DNA. Translation: CAI41763.1.
    AL845464 Genomic DNA. Translation: CAI41797.1.
    AL845464 Genomic DNA. Translation: CAI41798.1.
    AL845464 Genomic DNA. Translation: CAI41799.1.
    AL845464 Genomic DNA. Translation: CAM25714.1.
    BX284686 Genomic DNA. Translation: CAM26213.1.
    BX284686 Genomic DNA. Translation: CAM26215.1.
    BX284686 Genomic DNA. Translation: CAM26216.1.
    BX284686 Genomic DNA. Translation: CAM26218.1.
    BX927239 Genomic DNA. Translation: CAQ06588.1.
    BX927239 Genomic DNA. Translation: CAQ06590.1.
    CR753803 Genomic DNA. Translation: CAQ09561.1.
    CR933878 Genomic DNA. Translation: CAQ09617.1.
    CR933878 Genomic DNA. Translation: CAQ09619.1.
    CR812478 Genomic DNA. Translation: CAQ10692.1.
    CR812478 Genomic DNA. Translation: CAQ10694.1.
    CH471081 Genomic DNA. Translation: EAX03597.1.
    CH471081 Genomic DNA. Translation: EAX03591.1.
    BC001355 mRNA. Translation: AAH01355.1.
    CCDSiCCDS4740.1. [Q9UMR5-3]
    CCDS4742.1. [Q9UMR5-1]
    RefSeqiNP_001191032.1. NM_001204103.1. [Q9UMR5-1]
    NP_005146.4. NM_005155.6. [Q9UMR5-1]
    NP_619731.2. NM_138717.2. [Q9UMR5-3]
    UniGeneiHs.332138.
    Hs.731888.

    Genome annotation databases

    EnsembliENST00000324816; ENSP00000320528; ENSG00000221988. [Q9UMR5-1]
    ENST00000361568; ENSP00000354608; ENSG00000221988. [Q9UMR5-3]
    ENST00000375137; ENSP00000364279; ENSG00000221988. [Q9UMR5-1]
    ENST00000375143; ENSP00000364285; ENSG00000221988. [Q9UMR5-1]
    ENST00000383301; ENSP00000372789; ENSG00000206329.
    ENST00000395523; ENSP00000378894; ENSG00000221988. [Q9UMR5-1]
    ENST00000412651; ENSP00000416505; ENSG00000236649.
    ENST00000414356; ENSP00000398462; ENSG00000168452.
    ENST00000415972; ENSP00000408333; ENSG00000228116.
    ENST00000423347; ENSP00000406219; ENSG00000231618.
    ENST00000433748; ENSP00000410001; ENSG00000206256.
    ENST00000476214; ENSP00000432308; ENSG00000168452.
    ENST00000480383; ENSP00000432502; ENSG00000236649.
    ENST00000483565; ENSP00000431928; ENSG00000231618.
    ENST00000488579; ENSP00000434992; ENSG00000236649.
    ENST00000490624; ENSP00000433323; ENSG00000168452.
    ENST00000493809; ENSP00000436963; ENSG00000227600.
    ENST00000496937; ENSP00000432964; ENSG00000231618.
    ENST00000527704; ENSP00000433061; ENSG00000227600.
    GeneIDi9374.
    KEGGihsa:9374.
    UCSCiuc003nzx.3. human. [Q9UMR5-1]
    uc010jtu.1. human. [Q9UMR5-2]

    Polymorphism databases

    DMDMi296453016.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF020543 mRNA. Translation: AAB80730.1 .
    AF020544 mRNA. Translation: AAB80731.1 .
    Y17958 mRNA. Translation: CAB46981.1 .
    AL110128 mRNA. Translation: CAB53659.1 .
    CR533546 mRNA. Translation: CAG38577.1 . Different initiation.
    AK292729 mRNA. Translation: BAF85418.1 .
    U89336 Genomic DNA. Translation: AAB47495.1 .
    AL662828 Genomic DNA. Translation: CAI17424.1 .
    AL662828 Genomic DNA. Translation: CAI17426.2 .
    AL662828 Genomic DNA. Translation: CAM24823.1 .
    AL662828 Genomic DNA. Translation: CAM24825.1 .
    AL662884 Genomic DNA. Translation: CAI18342.1 .
    AL662884 Genomic DNA. Translation: CAI18344.1 .
    AL662884 Genomic DNA. Translation: CAI41763.1 .
    AL845464 Genomic DNA. Translation: CAI41797.1 .
    AL845464 Genomic DNA. Translation: CAI41798.1 .
    AL845464 Genomic DNA. Translation: CAI41799.1 .
    AL845464 Genomic DNA. Translation: CAM25714.1 .
    BX284686 Genomic DNA. Translation: CAM26213.1 .
    BX284686 Genomic DNA. Translation: CAM26215.1 .
    BX284686 Genomic DNA. Translation: CAM26216.1 .
    BX284686 Genomic DNA. Translation: CAM26218.1 .
    BX927239 Genomic DNA. Translation: CAQ06588.1 .
    BX927239 Genomic DNA. Translation: CAQ06590.1 .
    CR753803 Genomic DNA. Translation: CAQ09561.1 .
    CR933878 Genomic DNA. Translation: CAQ09617.1 .
    CR933878 Genomic DNA. Translation: CAQ09619.1 .
    CR812478 Genomic DNA. Translation: CAQ10692.1 .
    CR812478 Genomic DNA. Translation: CAQ10694.1 .
    CH471081 Genomic DNA. Translation: EAX03597.1 .
    CH471081 Genomic DNA. Translation: EAX03591.1 .
    BC001355 mRNA. Translation: AAH01355.1 .
    CCDSi CCDS4740.1. [Q9UMR5-3 ]
    CCDS4742.1. [Q9UMR5-1 ]
    RefSeqi NP_001191032.1. NM_001204103.1. [Q9UMR5-1 ]
    NP_005146.4. NM_005155.6. [Q9UMR5-1 ]
    NP_619731.2. NM_138717.2. [Q9UMR5-3 ]
    UniGenei Hs.332138.
    Hs.731888.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PJA X-ray 2.70 A 1-302 [» ]
    ProteinModelPortali Q9UMR5.
    SMRi Q9UMR5. Positions 35-302.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114775. 27 interactions.
    MINTi MINT-4721124.

    Chemistry

    ChEMBLi CHEMBL2189137.

    Polymorphism databases

    DMDMi 296453016.

    Proteomic databases

    MaxQBi Q9UMR5.
    PaxDbi Q9UMR5.
    PRIDEi Q9UMR5.

    Protocols and materials databases

    DNASUi 9374.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000324816 ; ENSP00000320528 ; ENSG00000221988 . [Q9UMR5-1 ]
    ENST00000361568 ; ENSP00000354608 ; ENSG00000221988 . [Q9UMR5-3 ]
    ENST00000375137 ; ENSP00000364279 ; ENSG00000221988 . [Q9UMR5-1 ]
    ENST00000375143 ; ENSP00000364285 ; ENSG00000221988 . [Q9UMR5-1 ]
    ENST00000383301 ; ENSP00000372789 ; ENSG00000206329 .
    ENST00000395523 ; ENSP00000378894 ; ENSG00000221988 . [Q9UMR5-1 ]
    ENST00000412651 ; ENSP00000416505 ; ENSG00000236649 .
    ENST00000414356 ; ENSP00000398462 ; ENSG00000168452 .
    ENST00000415972 ; ENSP00000408333 ; ENSG00000228116 .
    ENST00000423347 ; ENSP00000406219 ; ENSG00000231618 .
    ENST00000433748 ; ENSP00000410001 ; ENSG00000206256 .
    ENST00000476214 ; ENSP00000432308 ; ENSG00000168452 .
    ENST00000480383 ; ENSP00000432502 ; ENSG00000236649 .
    ENST00000483565 ; ENSP00000431928 ; ENSG00000231618 .
    ENST00000488579 ; ENSP00000434992 ; ENSG00000236649 .
    ENST00000490624 ; ENSP00000433323 ; ENSG00000168452 .
    ENST00000493809 ; ENSP00000436963 ; ENSG00000227600 .
    ENST00000496937 ; ENSP00000432964 ; ENSG00000231618 .
    ENST00000527704 ; ENSP00000433061 ; ENSG00000227600 .
    GeneIDi 9374.
    KEGGi hsa:9374.
    UCSCi uc003nzx.3. human. [Q9UMR5-1 ]
    uc010jtu.1. human. [Q9UMR5-2 ]

    Organism-specific databases

    CTDi 9374.
    GeneCardsi GC06P032122.
    GC06Pi32132.
    GC06Pj32069.
    GC06Pk32096.
    GC06Pl32160.
    GC06Pm32197.
    GC06Pn32078.
    GC06Po32128.
    HGNCi HGNC:9326. PPT2.
    HPAi HPA000414.
    MIMi 603298. gene.
    neXtProti NX_Q9UMR5.
    PharmGKBi PA33689.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1075.
    HOVERGENi HBG019159.
    InParanoidi Q9UMR5.
    KOi K01074.
    OMAi VPWISEL.
    PhylomeDBi Q9UMR5.
    TreeFami TF323926.

    Miscellaneous databases

    EvolutionaryTracei Q9UMR5.
    GeneWikii PPT2.
    GenomeRNAii 9374.
    NextBioi 35116.
    PROi Q9UMR5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UMR5.
    Bgeei Q9UMR5.
    Genevestigatori Q9UMR5.

    Family and domain databases

    Gene3Di 3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR002472. Palm_thioest.
    [Graphical view ]
    Pfami PF02089. Palm_thioest. 1 hit.
    [Graphical view ]
    PRINTSi PR00414. PPTHIESTRASE.
    SUPFAMi SSF53474. SSF53474. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and expression of palmitoyl-protein thioesterase 2 (PPT2), a homolog of lysosomal palmitoyl-protein thioesterase with a distinct substrate specificity."
      Soyombo A.A., Hofmann S.L.
      J. Biol. Chem. 272:27456-27463(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, GLYCOSYLATION, PH DEPENDENCE, VARIANT TRP-5.
    2. "Characterization of a human MHC class III region gene product with S-thioesterase activity."
      Aguado B., Campbell R.D.
      Biochem. J. 341:679-689(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), GLYCOSYLATION, FUNCTION, VARIANT TRP-5.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT TRP-5.
      Tissue: Brain.
    4. "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), VARIANT TRP-5.
    5. "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 2), VARIANT TRP-5.
      Tissue: Kidney.
    6. "Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
      Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
      Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS TRP-5 AND GLU-34.
    7. "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], VARIANTS TRP-5 AND GLU-34.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT TRP-5.
    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), VARIANT TRP-5.
      Tissue: Skin.
    10. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "The crystal structure of palmitoyl protein thioesterase-2 (PPT2) reveals the basis for divergent substrate specificities of the two lysosomal thioesterases, PPT1 and PPT2."
      Calero G., Gupta P., Nonato M.C., Tandel S., Biehl E.R., Hofmann S.L., Clardy J.
      J. Biol. Chem. 278:37957-37964(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), FUNCTION, KINETIC PARAMETERS, MUTAGENESIS OF SER-111; ASP-228; HIS-283 AND HIS-287, GLYCOSYLATION AT ASN-190, DISULFIDE BONDS.
    13. "Structure of the human palmitoyl-protein thioesterase-2 gene (PPT2) in the major histocompatibility complex on chromosome 6p21.3."
      Soyombo A.A., Yi W., Hofmann S.L.
      Genomics 56:208-216(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TRP-5 AND GLU-34.

    Entry informationi

    Entry nameiPPT2_HUMAN
    AccessioniPrimary (citable) accession number: Q9UMR5
    Secondary accession number(s): A2ABC9
    , A2ABD1, A2ARM7, A2BFH7, A2BFH9, A2BFI2, A8K9L4, B0S868, G8JLE1, O14799, Q0P6K0, Q5JP13, Q5JP14, Q5JQF0, Q5SSX4, Q5SSX5, Q5SSX6, Q5STJ4, Q5STJ5, Q5STJ6, Q6FI80, Q99945
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 5, 2002
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 125 of the entry and version 4 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, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3