CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008339
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Palmitoyl-protein thioesterase 1 
Protein Synonyms/Alias
 PPT-1; Palmitoyl-protein hydrolase 1 
Gene Name
 PPT1 
Gene Synonyms/Alias
 PPT 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
165HICDFIRKTLNAGAYubiquitination[1]
174LNAGAYSKVVQERLVubiquitination[1, 2, 3, 4]
191EYWHDPIKEDVYRNHubiquitination[1, 3]
224KNLMALKKFVMVKFLubiquitination[1]
253FYRSGQAKETIPLQEubiquitination[1, 3, 4]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661
Functional Description
 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. 
Sequence Annotation
 ACT_SITE 115 115 By similarity.
 ACT_SITE 233 233 By similarity.
 ACT_SITE 289 289 By similarity.
 CARBOHYD 197 197 N-linked (GlcNAc...).
 CARBOHYD 212 212 N-linked (GlcNAc...).
 CARBOHYD 232 232 N-linked (GlcNAc...).
 DISULFID 45 46
 DISULFID 96 128
 DISULFID 152 160  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Disease mutation; Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Neurodegeneration; Neuronal ceroid lipofuscinosis; Polymorphism; Reference proteome; Sensory transduction; Signal; Vision. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 306 AA 
Protein Sequence
MASPGCLWLL AVALLPWTCA SRALQHLDPP APLPLVIWHG MGDSCCNPLS MGAIKKMVEK 60
KIPGIYVLSL EIGKTLMEDV ENSFFLNVNS QVTTVCQALA KDPKLQQGYN AMGFSQGGQF 120
LRAVAQRCPS PPMINLISVG GQHQGVFGLP RCPGESSHIC DFIRKTLNAG AYSKVVQERL 180
VQAEYWHDPI KEDVYRNHSI FLADINQERG INESYKKNLM ALKKFVMVKF LNDSIVDPVD 240
SEWFGFYRSG QAKETIPLQE TSLYTQDRLG LKEMDNAGQL VFLATEGDHL QLSEEWFYAH 300
IIPFLG 306 
Gene Ontology
 GO:0030424; C:axon; IDA:UniProtKB.
 GO:0005829; C:cytosol; ISS:UniProtKB.
 GO:0030425; C:dendrite; IEA:Compara.
 GO:0005576; C:extracellular region; IDA:UniProtKB.
 GO:0005615; C:extracellular space; IEA:Compara.
 GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
 GO:0005764; C:lysosome; IDA:UniProtKB.
 GO:0045121; C:membrane raft; IDA:UniProtKB.
 GO:0043025; C:neuronal cell body; IEA:Compara.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0008021; C:synaptic vesicle; IDA:UniProtKB.
 GO:0008474; F:palmitoyl-(protein) hydrolase activity; IDA:UniProtKB.
 GO:0016290; F:palmitoyl-CoA hydrolase activity; IDA:UniProtKB.
 GO:0008344; P:adult locomotory behavior; IEA:Compara.
 GO:0006309; P:apoptotic DNA fragmentation; IDA:UniProtKB.
 GO:0008306; P:associative learning; IEA:Compara.
 GO:0007420; P:brain development; IMP:UniProtKB.
 GO:0044257; P:cellular protein catabolic process; IEA:Compara.
 GO:0051186; P:cofactor metabolic process; IMP:UniProtKB.
 GO:0051181; P:cofactor transport; IMP:UniProtKB.
 GO:0007625; P:grooming behavior; IEA:Compara.
 GO:0007042; P:lysosomal lumen acidification; IMP:UniProtKB.
 GO:0031579; P:membrane raft organization; IMP:UniProtKB.
 GO:0030308; P:negative regulation of cell growth; IMP:UniProtKB.
 GO:0043524; P:negative regulation of neuron apoptotic process; IMP:UniProtKB.
 GO:0048666; P:neuron development; TAS:UniProtKB.
 GO:0007269; P:neurotransmitter secretion; IEA:Compara.
 GO:0006907; P:pinocytosis; IMP:MGI.
 GO:0048549; P:positive regulation of pinocytosis; IMP:UniProtKB.
 GO:0048260; P:positive regulation of receptor-mediated endocytosis; IMP:UniProtKB.
 GO:0002084; P:protein depalmitoylation; IDA:UniProtKB.
 GO:0015031; P:protein transport; IMP:UniProtKB.
 GO:0006898; P:receptor-mediated endocytosis; IMP:MGI.
 GO:0032429; P:regulation of phospholipase A2 activity; IEA:Compara.
 GO:0050803; P:regulation of synapse structure and activity; NAS:UniProtKB.
 GO:0030149; P:sphingolipid catabolic process; TAS:UniProtKB.
 GO:0007601; P:visual perception; IEA:UniProtKB-KW. 
Interpro
 IPR002472; Palm_thioest. 
Pfam
 PF02089; Palm_thioest 
SMART
  
PROSITE
  
PRINTS
 PR00414; PPTHIESTRASE.