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P50897

- PPT1_HUMAN

UniProt

P50897 - PPT1_HUMAN

Protein

Palmitoyl-protein thioesterase 1

Gene

PPT1

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 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Removes thioester-linked fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides during lysosomal degradation. Prefers acyl chain lengths of 14 to 18 carbons.

    Catalytic activityi

    Palmitoyl-[protein] + H2O = palmitate + [protein].

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei115 – 1151By similarity
    Active sitei233 – 2331By similarity
    Active sitei289 – 2891By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. adult locomotory behavior Source: Ensembl
    2. apoptotic DNA fragmentation Source: UniProtKB
    3. associative learning Source: Ensembl
    4. brain development Source: UniProtKB
    5. cellular protein catabolic process Source: Ensembl
    6. cofactor metabolic process Source: UniProtKB
    7. cofactor transport Source: UniProtKB
    8. grooming behavior Source: Ensembl
    9. lipid catabolic process Source: UniProtKB
    10. lysosomal lumen acidification Source: UniProtKB
    11. membrane raft organization Source: UniProtKB
    12. negative regulation of apoptotic process Source: UniProtKB
    13. negative regulation of cell growth Source: UniProtKB
    14. negative regulation of neuron apoptotic process Source: UniProtKB
    15. nervous system development Source: UniProtKB
    16. neuron development Source: UniProtKB
    17. neurotransmitter secretion Source: Ensembl
    18. pinocytosis Source: MGI
    19. positive regulation of pinocytosis Source: UniProtKB
    20. positive regulation of receptor-mediated endocytosis Source: UniProtKB
    21. protein catabolic process Source: UniProtKB
    22. protein depalmitoylation Source: UniProtKB
    23. protein transport Source: UniProtKB
    24. receptor-mediated endocytosis Source: MGI
    25. regulation of phospholipase A2 activity Source: Ensembl
    26. regulation of synapse structure and activity Source: UniProtKB
    27. sphingolipid catabolic process Source: UniProtKB
    28. visual perception Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Sensory transduction, Vision

    Enzyme and pathway databases

    BRENDAi3.1.2.22. 2681.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Palmitoyl-protein thioesterase 1 (EC:3.1.2.22)
    Short name:
    PPT-1
    Alternative name(s):
    Palmitoyl-protein hydrolase 1
    Gene namesi
    Name:PPT1
    Synonyms:PPT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9325. PPT1.

    Subcellular locationi

    GO - Cellular componenti

    1. axon Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. dendrite Source: Ensembl
    4. extracellular region Source: UniProtKB
    5. extracellular space Source: Ensembl
    6. extracellular vesicular exosome Source: UniProt
    7. Golgi apparatus Source: UniProtKB
    8. lysosome Source: UniProtKB
    9. membrane Source: UniProtKB
    10. membrane raft Source: UniProtKB
    11. neuronal cell body Source: Ensembl
    12. nucleus Source: UniProtKB
    13. synaptic vesicle Source: UniProtKB

    Keywords - Cellular componenti

    Lysosome

    Pathology & Biotechi

    Involvement in diseasei

    Ceroid lipofuscinosis, neuronal, 1 (CLN1) [MIM:256730]: A form of neuronal ceroid lipofuscinosis with variable age at onset. Infantile, late-infantile, juvenile, and adult onset have been reported. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material, and clinically by seizures, dementia, visual loss, and/or cerebral atrophy. The lipopigment pattern seen most often in CLN1 is referred to as granular osmiophilic deposits (GROD).6 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti38 – 381W → C in CLN1. 1 Publication
    VAR_058434
    Natural varianti39 – 391H → Q in CLN1.
    VAR_005548
    Natural varianti42 – 421G → E in CLN1.
    VAR_005549
    Natural varianti45 – 451C → Y in CLN1. 1 Publication
    VAR_066874
    Natural varianti75 – 751T → P in CLN1; juvenile onset. 2 Publications
    VAR_005550
    Natural varianti79 – 791D → G in CLN1; juvenile onset. 2 Publications
    VAR_005551
    Natural varianti108 – 1081G → R in CLN1; onset in adulthood. 2 Publications
    VAR_018511
    Natural varianti109 – 1091Y → D in CLN1; late infantile form. 1 Publication
    VAR_005552
    Natural varianti122 – 1221R → W in CLN1; seems to result in intracellular accumulation of the enzyme. 1 Publication
    Corresponds to variant rs137852695 [ dbSNP | Ensembl ].
    VAR_005553
    Natural varianti138 – 1381S → L in CLN1. 1 Publication
    VAR_066875
    Natural varianti152 – 1521C → Y in CLN1. 1 Publication
    VAR_066876
    Natural varianti177 – 1771Q → E in CLN1; late infantile form. 1 Publication
    VAR_005555
    Natural varianti181 – 1811V → L in CLN1.
    VAR_005556
    Natural varianti181 – 1811V → M in CLN1; late infantile form. 1 Publication
    VAR_005557
    Natural varianti187 – 1871H → R in CLN1. 1 Publication
    VAR_066877
    Natural varianti189 – 1891P → R in CLN1. 1 Publication
    VAR_066878
    Natural varianti219 – 2191L → Q in CLN1; juvenile onset. 2 Publications
    VAR_005558
    Natural varianti222 – 2221L → P in CLN1; late infantile form. 1 Publication
    VAR_066879
    Natural varianti228 – 2281V → G in CLN1. 1 Publication
    VAR_066880
    Natural varianti247 – 2471Y → H in CLN1. 1 Publication
    VAR_005559
    Natural varianti250 – 2501G → V in CLN1. 1 Publication
    VAR_005560
    Natural varianti296 – 2961W → R in CLN1. 1 Publication
    VAR_066881
    Natural varianti305 – 3051L → P in CLN1. 1 Publication
    VAR_066882

    Keywords - Diseasei

    Disease mutation, Neurodegeneration, Neuronal ceroid lipofuscinosis

    Organism-specific databases

    MIMi256730. phenotype.
    Orphaneti228329. CLN1 disease.
    PharmGKBiPA33688.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727By similarityAdd
    BLAST
    Chaini28 – 306279Palmitoyl-protein thioesterase 1PRO_0000025550Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi45 ↔ 461 Publication
    Disulfide bondi96 ↔ 1281 Publication
    Disulfide bondi152 ↔ 1601 Publication
    Glycosylationi197 – 1971N-linked (GlcNAc...)1 Publication
    Glycosylationi212 – 2121N-linked (GlcNAc...)1 Publication
    Glycosylationi232 – 2321N-linked (GlcNAc...)2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP50897.
    PaxDbiP50897.
    PRIDEiP50897.

    PTM databases

    PhosphoSiteiP50897.

    Expressioni

    Gene expression databases

    ArrayExpressiP50897.
    BgeeiP50897.
    CleanExiHS_PPT1.
    GenevestigatoriP50897.

    Organism-specific databases

    HPAiHPA021546.

    Interactioni

    Protein-protein interaction databases

    BioGridi111530. 13 interactions.
    IntActiP50897. 6 interactions.
    MINTiMINT-3018663.
    STRINGi9606.ENSP00000394863.

    Structurei

    Secondary structure

    1
    306
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi35 – 384
    Turni48 – 503
    Helixi51 – 6111
    Beta strandi67 – 693
    Beta strandi73 – 753
    Helixi76 – 8510
    Helixi88 – 10114
    Helixi103 – 1053
    Beta strandi109 – 1146
    Helixi116 – 12712
    Beta strandi133 – 1408
    Beta strandi153 – 1553
    Helixi157 – 17014
    Helixi174 – 1774
    Helixi181 – 1855
    Beta strandi189 – 1913
    Helixi192 – 1987
    Helixi202 – 2054
    Beta strandi208 – 2103
    Helixi213 – 2208
    Beta strandi223 – 2308
    Beta strandi234 – 2385
    Helixi239 – 2435
    Helixi258 – 2603
    Helixi262 – 2654
    Beta strandi268 – 2703
    Helixi271 – 2766
    Beta strandi280 – 2889
    Helixi294 – 3007
    Helixi302 – 3054

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3GROX-ray2.53A/B22-306[»]
    ProteinModelPortaliP50897.
    SMRiP50897. Positions 30-306.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP50897.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG1075.
    HOGENOMiHOG000199232.
    HOVERGENiHBG018186.
    InParanoidiP50897.
    KOiK01074.
    OMAiLQETTLY.
    OrthoDBiEOG776SQJ.
    PhylomeDBiP50897.
    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 (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P50897-1) [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

    MASPGCLWLL AVALLPWTCA SRALQHLDPP APLPLVIWHG MGDSCCNPLS    50
    MGAIKKMVEK KIPGIYVLSL EIGKTLMEDV ENSFFLNVNS QVTTVCQALA 100
    KDPKLQQGYN AMGFSQGGQF LRAVAQRCPS PPMINLISVG GQHQGVFGLP 150
    RCPGESSHIC DFIRKTLNAG AYSKVVQERL VQAEYWHDPI KEDVYRNHSI 200
    FLADINQERG INESYKKNLM ALKKFVMVKF LNDSIVDPVD SEWFGFYRSG 250
    QAKETIPLQE TSLYTQDRLG LKEMDNAGQL VFLATEGDHL QLSEEWFYAH 300
    IIPFLG 306
    Length:306
    Mass (Da):34,193
    Last modified:October 1, 1996 - v1
    Checksum:i69F8083FD1C15E92
    GO
    Isoform 2 (identifier: P50897-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         42-144: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:203
    Mass (Da):23,094
    Checksum:iC73DB3FEBDEC8F32
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti38 – 381W → C in CLN1. 1 Publication
    VAR_058434
    Natural varianti39 – 391H → Q in CLN1.
    VAR_005548
    Natural varianti42 – 421G → E in CLN1.
    VAR_005549
    Natural varianti45 – 451C → Y in CLN1. 1 Publication
    VAR_066874
    Natural varianti75 – 751T → P in CLN1; juvenile onset. 2 Publications
    VAR_005550
    Natural varianti79 – 791D → G in CLN1; juvenile onset. 2 Publications
    VAR_005551
    Natural varianti108 – 1081G → R in CLN1; onset in adulthood. 2 Publications
    VAR_018511
    Natural varianti109 – 1091Y → D in CLN1; late infantile form. 1 Publication
    VAR_005552
    Natural varianti122 – 1221R → W in CLN1; seems to result in intracellular accumulation of the enzyme. 1 Publication
    Corresponds to variant rs137852695 [ dbSNP | Ensembl ].
    VAR_005553
    Natural varianti134 – 1341I → T.1 Publication
    Corresponds to variant rs1800205 [ dbSNP | Ensembl ].
    VAR_005554
    Natural varianti138 – 1381S → L in CLN1. 1 Publication
    VAR_066875
    Natural varianti152 – 1521C → Y in CLN1. 1 Publication
    VAR_066876
    Natural varianti177 – 1771Q → E in CLN1; late infantile form. 1 Publication
    VAR_005555
    Natural varianti181 – 1811V → L in CLN1.
    VAR_005556
    Natural varianti181 – 1811V → M in CLN1; late infantile form. 1 Publication
    VAR_005557
    Natural varianti187 – 1871H → R in CLN1. 1 Publication
    VAR_066877
    Natural varianti189 – 1891P → R in CLN1. 1 Publication
    VAR_066878
    Natural varianti219 – 2191L → Q in CLN1; juvenile onset. 2 Publications
    VAR_005558
    Natural varianti222 – 2221L → P in CLN1; late infantile form. 1 Publication
    VAR_066879
    Natural varianti228 – 2281V → G in CLN1. 1 Publication
    VAR_066880
    Natural varianti247 – 2471Y → H in CLN1. 1 Publication
    VAR_005559
    Natural varianti250 – 2501G → V in CLN1. 1 Publication
    VAR_005560
    Natural varianti296 – 2961W → R in CLN1. 1 Publication
    VAR_066881
    Natural varianti305 – 3051L → P in CLN1. 1 Publication
    VAR_066882

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei42 – 144103Missing in isoform 2. 1 PublicationVSP_042033Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42809 Genomic DNA. Translation: AAA85337.1.
    U44772 mRNA. Translation: AAB06236.1.
    AF022211
    , AF022203, AF022204, AF022205, AF022206, AF022207, AF022208, AF022209, AF022210 Genomic DNA. Translation: AAB72224.1.
    AK302232 mRNA. Translation: BAG63586.1.
    AK312287 mRNA. Translation: BAG35214.1.
    CR542053 mRNA. Translation: CAG46850.1.
    AL512599 Genomic DNA. Translation: CAI11025.1.
    CH471059 Genomic DNA. Translation: EAX07237.1.
    CH471059 Genomic DNA. Translation: EAX07238.1.
    BC008426 mRNA. Translation: AAH08426.1.
    CCDSiCCDS44119.1. [P50897-2]
    CCDS447.1. [P50897-1]
    PIRiI58097.
    RefSeqiNP_000301.1. NM_000310.3. [P50897-1]
    NP_001136076.1. NM_001142604.1. [P50897-2]
    UniGeneiHs.3873.

    Genome annotation databases

    EnsembliENST00000433473; ENSP00000394863; ENSG00000131238. [P50897-1]
    ENST00000449045; ENSP00000392293; ENSG00000131238. [P50897-2]
    ENST00000529905; ENSP00000432053; ENSG00000131238. [P50897-1]
    GeneIDi5538.
    KEGGihsa:5538.
    UCSCiuc001cfb.2. human. [P50897-1]
    uc010ojg.1. human. [P50897-2]

    Polymorphism databases

    DMDMi1709747.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NCL CLN1

    Neural Ceroid Lipofuscinoses mutation db

    Mutations of the PPT1 gene

    Retina International's Scientific Newsletter

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42809 Genomic DNA. Translation: AAA85337.1 .
    U44772 mRNA. Translation: AAB06236.1 .
    AF022211
    , AF022203 , AF022204 , AF022205 , AF022206 , AF022207 , AF022208 , AF022209 , AF022210 Genomic DNA. Translation: AAB72224.1 .
    AK302232 mRNA. Translation: BAG63586.1 .
    AK312287 mRNA. Translation: BAG35214.1 .
    CR542053 mRNA. Translation: CAG46850.1 .
    AL512599 Genomic DNA. Translation: CAI11025.1 .
    CH471059 Genomic DNA. Translation: EAX07237.1 .
    CH471059 Genomic DNA. Translation: EAX07238.1 .
    BC008426 mRNA. Translation: AAH08426.1 .
    CCDSi CCDS44119.1. [P50897-2 ]
    CCDS447.1. [P50897-1 ]
    PIRi I58097.
    RefSeqi NP_000301.1. NM_000310.3. [P50897-1 ]
    NP_001136076.1. NM_001142604.1. [P50897-2 ]
    UniGenei Hs.3873.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3GRO X-ray 2.53 A/B 22-306 [» ]
    ProteinModelPortali P50897.
    SMRi P50897. Positions 30-306.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111530. 13 interactions.
    IntActi P50897. 6 interactions.
    MINTi MINT-3018663.
    STRINGi 9606.ENSP00000394863.

    Chemistry

    ChEMBLi CHEMBL2331051.

    PTM databases

    PhosphoSitei P50897.

    Polymorphism databases

    DMDMi 1709747.

    Proteomic databases

    MaxQBi P50897.
    PaxDbi P50897.
    PRIDEi P50897.

    Protocols and materials databases

    DNASUi 5538.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000433473 ; ENSP00000394863 ; ENSG00000131238 . [P50897-1 ]
    ENST00000449045 ; ENSP00000392293 ; ENSG00000131238 . [P50897-2 ]
    ENST00000529905 ; ENSP00000432053 ; ENSG00000131238 . [P50897-1 ]
    GeneIDi 5538.
    KEGGi hsa:5538.
    UCSCi uc001cfb.2. human. [P50897-1 ]
    uc010ojg.1. human. [P50897-2 ]

    Organism-specific databases

    CTDi 5538.
    GeneCardsi GC01M040567.
    GeneReviewsi PPT1.
    HGNCi HGNC:9325. PPT1.
    HPAi HPA021546.
    MIMi 256730. phenotype.
    600722. gene.
    neXtProti NX_P50897.
    Orphaneti 228329. CLN1 disease.
    PharmGKBi PA33688.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1075.
    HOGENOMi HOG000199232.
    HOVERGENi HBG018186.
    InParanoidi P50897.
    KOi K01074.
    OMAi LQETTLY.
    OrthoDBi EOG776SQJ.
    PhylomeDBi P50897.
    TreeFami TF323926.

    Enzyme and pathway databases

    BRENDAi 3.1.2.22. 2681.

    Miscellaneous databases

    ChiTaRSi PPT1. human.
    EvolutionaryTracei P50897.
    GeneWikii PPT1.
    GenomeRNAii 5538.
    NextBioi 21454.
    PROi P50897.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P50897.
    Bgeei P50897.
    CleanExi HS_PPT1.
    Genevestigatori P50897.

    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. "Mutations in the palmitoyl protein thioesterase gene causing infantile neuronal ceroid lipofuscinosis."
      Vesa J., Hellsten E., Verkruyse L.A., Camp L.A., Rapola J., Santavuori P., Hofmann S.L., Peltonen L.
      Nature 376:584-587(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANT CLN1 TRP-122.
      Tissue: Brain.
    2. "Didemnin binds to the protein palmitoyl thioesterase responsible for infantile neuronal ceroid lipofuscinosis."
      Crews C.M., Lane W.S., Schreiber S.L.
      Proc. Natl. Acad. Sci. U.S.A. 93:4316-4319(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "cDNA and genomic cloning of human palmitoyl-protein thioesterase (PPT), the enzyme defective in infantile neuronal ceroid lipofuscinosis."
      Schriner J.E., Yi W., Hofmann S.L.
      Genomics 34:317-322(1996) [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] (ISOFORMS 1 AND 2).
      Tissue: Cerebellum and Testis.
    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. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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: Prostate.
    9. "Lipid thioesters derived from acylated proteins accumulate in infantile neuronal ceroid lipofuscinosis: correction of the defect in lymphoblasts by recombinant palmitoyl-protein thioesterase."
      Lu J.-Y., Verkruyse L.A., Hofmann S.L.
      Proc. Natl. Acad. Sci. U.S.A. 93:10046-10050(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    10. "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
      Zhang H., Li X.-J., Martin D.B., Aebersold R.
      Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-232.
    11. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-197; ASN-212 AND ASN-232.
      Tissue: Liver.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Human palmitoyl-protein thioesterase 1."
      Structural genomics consortium (SGC)
      Submitted (APR-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.53 ANGSTROMS) OF 22-306, DISULFIDE BONDS.
    14. "Mutations in the palmitoyl-protein thioesterase gene (PPT; CLN1) causing juvenile neuronal ceroid lipofuscinosis with granular osmiophilic deposits."
      Mitchison H.M., Hofmann S.L., Becerra C.H.R., Munroe P.B., Lake B.D., Crow Y.J., Stephenson J.B.P., Williams R.E., Hofman I.L., Taschner P.E.M., Martin J.-J., Philippart M., Andermann E., Andermann F., Mole S.E., Gardiner R.M., O'Rawe A.M.
      Hum. Mol. Genet. 7:291-297(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CLN1 PRO-75; GLY-79 AND GLN-219.
    15. "Molecular genetics of palmitoyl-protein thioesterase deficiency in the U.S."
      Das A.K., Becerra C.H.R., Yi W., Lu J.-Y., Siakotos A.N., Wisniewski K.E., Hofmann S.L.
      J. Clin. Invest. 102:361-370(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CLN1, VARIANT THR-134.
    16. "Adult neuronal ceroid lipofuscinosis with palmitoyl-protein thioesterase deficiency: first adult-onset patients of a childhood disease."
      van Diggelen O.P., Thobois S., Tilikete C., Zabot M.-T., Keulemans J.L.M., van Bunderen P.A., Taschner P.E.M., Losekoot M., Voznyi Y.V.
      Ann. Neurol. 50:269-272(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CLN1 ARG-108.
    17. "Mutations in CLN7/MFSD8 are a common cause of variant late-infantile neuronal ceroid lipofuscinosis."
      Kousi M., Siintola E., Dvorakova L., Vlaskova H., Turnbull J., Topcu M., Yuksel D., Gokben S., Minassian B.A., Elleder M., Mole S.E., Lehesjoki A.-E.
      Brain 132:810-819(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CLN1 CYS-38.
    18. "Update of the mutation spectrum and clinical correlations of over 360 mutations in eight genes that underlie the neuronal ceroid lipofuscinoses."
      Kousi M., Lehesjoki A.E., Mole S.E.
      Hum. Mutat. 33:42-63(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CLN1 TYR-45; PRO-75; GLY-79; ARG-108; ASP-109; LEU-138; TYR-152; GLU-177; MET-181; ARG-187; ARG-189; GLN-219; PRO-222; GLY-228; HIS-247; VAL-250; ARG-296 AND PRO-305.

    Entry informationi

    Entry nameiPPT1_HUMAN
    AccessioniPrimary (citable) accession number: P50897
    Secondary accession number(s): B4DY24, Q6FGQ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 148 of the entry and version 1 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 1
      Human chromosome 1: 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