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P50897

- PPT1_HUMAN

UniProt

P50897 - PPT1_HUMAN

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Protein
Palmitoyl-protein thioesterase 1
Gene
PPT1, PPT
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 1151 By similarity
Active sitei233 – 2331 By similarity
Active sitei289 – 2891 By 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
Complete GO annotation...

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

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).
Note: The disease is caused by mutations affecting the gene represented in this entry.6 Publications
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 – 2727 By similarity
Add
BLAST
Chaini28 – 306279Palmitoyl-protein thioesterase 1
PRO_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

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.

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.
VSP_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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 147 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

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