PPT1
entrez
5538
canonical
uniprot
P50897
canonical
ensembl
ENSG00000131238
resolver
ensp
ENSP00000392293
resolver
ensp
ENSP00000403207
resolver
ensp
ENSP00000493153
resolver
enst
ENST00000439754
resolver
genesymbol
PPT1
resolver
genesymbol_syn
CLN1
resolver
genesymbol_syn
PPT
resolver
hgnc
HGNC:9325
resolver
uniprot
B4DY24
resolver
uniprot
Q5T0S4
resolver
uniprot
Q6FGQ4
resolver
uniprot_entry
PPT1_HUMAN
resolver
uniprot_entry
Q5T0S4_HUMAN
resolver
uniprot_sec
B4DY24
resolver
uniprot_sec
Q6FGQ4
resolver
activity_regulation
ACTIVITY REGULATION: Palmitoylation reduces PPT1 enzymatic activity. {ECO:0000269|PubMed:26731412}.
uniprot
proteins
amino_acid_sequence
MASPGCLWLLAVALLPWTCASRALQHLDPPAPLPLVIWHGMGDSCCNPLSMGAIKKMVEKKIPGIYVLSLEIGKTLMEDVENSFFLNVNSQVTTVCQALAKDPKLQQGYNAMGFSQGGQFLRAVAQRCPSPPMINLISVGGQHQGVFGLPRCPGESSHICDFIRKTLNAGAYSKVVQERLVQAEYWHDPIKEDVYRNHSIFLADINQERGINESYKKNLMALKKFVMVKFLNDSIVDPVDSEWFGFYRSGQAKETIPLQETSLYTQDRLGLKEMDNAGQLVFLATEGDHLQLSEEWFYAHIIPFLG
uniprot
proteins
disease_involvement
DISEASE: 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). {ECO:0000269|PubMed:10477428, ECO:0000269|PubMed:11506414, ECO:0000269|PubMed:19201763, ECO:0000269|PubMed:19941651, ECO:0000269|PubMed:21990111, ECO:0000269|PubMed:7637805, ECO:0000269|PubMed:9425237, ECO:0000269|PubMed:9664077}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.1.2.2
uniprot
proteins
ec_number
3.1.2.22
uniprot
proteins
function
FUNCTION: Has thioesterase activity against fatty acid thioesters with 14 -18 carbons, including palmitoyl-CoA, S-palmitoyl-N-acetylcysteamine, and palmitoylated proteins (PubMed:12855696, PubMed:26731412, PubMed:8816748). In contrast to PPT2, PPT1 can hydrolyze palmitoylated proteins and palmitoylcysteine (PubMed:12855696). {ECO:0000269|PubMed:12855696, ECO:0000269|PubMed:26731412, ECO:0000269|PubMed:8816748}.
uniprot
proteins
mass_dalton
34193
uniprot
proteins
mutagenesis
MUTAGEN 6; /note="C->S: Does not affect its subcellular localizations. Increases depalmitoylation activity."; /evidence="ECO:0000269|PubMed:26731412
uniprot
proteins
post_translational_modification
PTM: Glycosylated. {ECO:0000250|UniProtKB:P45478}.
uniprot
proteins
protein_family
Palmitoyl-protein thioesterase family
uniprot
proteins
pubmed
10477428
uniprot
proteins
pubmed
10658183
uniprot
proteins
pubmed
11506414
uniprot
proteins
pubmed
12754519
uniprot
proteins
pubmed
12855696
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19201763
uniprot
proteins
pubmed
19941651
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21990111
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26731412
uniprot
proteins
pubmed
7637805
uniprot
proteins
pubmed
8633062
uniprot
proteins
pubmed
8786130
uniprot
proteins
pubmed
8816748
uniprot
proteins
pubmed
9425237
uniprot
proteins
pubmed
9664077
uniprot
proteins
sequence_length
306
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:19941651, ECO:0000269|PubMed:26731412}. Secreted {ECO:0000269|PubMed:26731412}. Golgi apparatus {ECO:0000269|PubMed:26731412}. Endoplasmic reticulum {ECO:0000269|PubMed:26731412}.
uniprot
proteins