PPT1_HUMAN - dbPTM
PPT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PPT1_HUMAN
UniProt AC P50897
Protein Name Palmitoyl-protein thioesterase 1
Gene Name PPT1
Organism Homo sapiens (Human).
Sequence Length 306
Subcellular Localization Lysosome . Secreted .
Protein 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. [PubMed: 8816748]
Protein Sequence MASPGCLWLLAVALLPWTCASRALQHLDPPAPLPLVIWHGMGDSCCNPLSMGAIKKMVEKKIPGIYVLSLEIGKTLMEDVENSFFLNVNSQVTTVCQALAKDPKLQQGYNAMGFSQGGQFLRAVAQRCPSPPMINLISVGGQHQGVFGLPRCPGESSHICDFIRKTLNAGAYSKVVQERLVQAEYWHDPIKEDVYRNHSIFLADINQERGINESYKKNLMALKKFVMVKFLNDSIVDPVDSEWFGFYRSGQAKETIPLQETSLYTQDRLGLKEMDNAGQLVFLATEGDHLQLSEEWFYAHIIPFLG
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
6S-palmitoylation--MASPGCLWLLAVA
--CCCHHHHHHHHHH		2.5326731412
18PhosphorylationAVALLPWTCASRALQ
HHHHHHHHHHHHHHH		9.0329083192
21PhosphorylationLLPWTCASRALQHLD
HHHHHHHHHHHHCCC		21.8930631047
62UbiquitinationKKMVEKKIPGIYVLS
HHHHHHCCCCEEEEE		5.8321963094
66PhosphorylationEKKIPGIYVLSLEIG
HHCCCCEEEEEECCC		10.97-
69PhosphorylationIPGIYVLSLEIGKTL
CCCEEEEEECCCCHH		17.57-
71UbiquitinationGIYVLSLEIGKTLME
CEEEEEECCCCHHHH		46.4421890473
71UbiquitinationGIYVLSLEIGKTLME
CEEEEEECCCCHHHH		46.4427667366
75PhosphorylationLSLEIGKTLMEDVEN
EEECCCCHHHHHHHH		26.5624043423
83PhosphorylationLMEDVENSFFLNVNS
HHHHHHHCEECCCHH		12.1324043423
88UbiquitinationENSFFLNVNSQVTTV
HHCEECCCHHHHHHH		8.7429967540
90PhosphorylationSFFLNVNSQVTTVCQ
CEECCCHHHHHHHHH		23.0324043423
93PhosphorylationLNVNSQVTTVCQALA
CCCHHHHHHHHHHHH		13.0824043423
94PhosphorylationNVNSQVTTVCQALAK
CCHHHHHHHHHHHHC		22.0424043423
113UbiquitinationQQGYNAMGFSQGGQF
HCCCCCCCCCHHHHH		19.3529967540
150UbiquitinationHQGVFGLPRCPGESS
CCCCCCCCCCCCCHH		35.8921963094
165UbiquitinationHICDFIRKTLNAGAY
HHHHHHHHHCCCCHH		53.1821963094
172PhosphorylationKTLNAGAYSKVVQER
HHCCCCHHHHHHHHH		14.22-
174UbiquitinationLNAGAYSKVVQERLV
CCCCHHHHHHHHHHH		33.4821906983
174UbiquitinationLNAGAYSKVVQERLV
CCCCHHHHHHHHHHH		33.4821890473
185PhosphorylationERLVQAEYWHDPIKE
HHHHHHHHCCCCCCH		15.85-
191UbiquitinationEYWHDPIKEDVYRNH
HHCCCCCCHHHHHCC		53.9329967540
191AcetylationEYWHDPIKEDVYRNH
HHCCCCCCHHHHHCC		53.9326822725
197N-linked_GlycosylationIKEDVYRNHSIFLAD
CCHHHHHCCCEEEHH		18.6416399764
197N-linked_GlycosylationIKEDVYRNHSIFLAD
CCHHHHHCCCEEEHH		18.6416399764
199O-linked_GlycosylationEDVYRNHSIFLADIN
HHHHHCCCEEEHHCC		20.7030059200
212N-linked_GlycosylationINQERGINESYKKNL
CCHHCCCCHHHHHHH		34.6819159218
216UbiquitinationRGINESYKKNLMALK
CCCCHHHHHHHHHHH		44.4529967540
224AcetylationKNLMALKKFVMVKFL
HHHHHHHHHHHHHHC		44.0019811655
224UbiquitinationKNLMALKKFVMVKFL
HHHHHHHHHHHHHHC		44.00-
232N-linked_GlycosylationFVMVKFLNDSIVDPV
HHHHHHCCCCCCCCC		44.0812754519
232N-linked_GlycosylationFVMVKFLNDSIVDPV
HHHHHHCCCCCCCCC		44.0812754519
253UbiquitinationFYRSGQAKETIPLQE
EECCCCCCCEECCCC		47.7221963094
261PhosphorylationETIPLQETSLYTQDR
CEECCCCCCCCCCCC		15.8628152594
262PhosphorylationTIPLQETSLYTQDRL
EECCCCCCCCCCCCC		20.7328152594
264PhosphorylationPLQETSLYTQDRLGL
CCCCCCCCCCCCCCC		11.3428152594
265PhosphorylationLQETSLYTQDRLGLK
CCCCCCCCCCCCCCE		29.3228152594
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of PPT1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PPT1_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PPT1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XRCC1_HUMANXRCC1physical
22939629
SPHM_HUMANSGSHphysical
22939629
TMEM9_HUMANTMEM9physical
22939629
RIF1_HUMANRIF1physical
22939629
TCOF_HUMANTCOF1physical
22939629
TERA_HUMANVCPphysical
25865307
ODB2_HUMANDBTphysical
25865307
MAP1B_HUMANMAP1Bphysical
25865307
VAPB_HUMANVAPBphysical
25865307
AT1A1_HUMANATP1A1physical
25865307
PRDX1_HUMANPRDX1physical
25865307
TXTP_HUMANSLC25A1physical
25865307
ATPB_HUMANATP5Bphysical
25865307
DPYL1_HUMANCRMP1physical
25865307
ODP2_HUMANDLATphysical
25865307
CRIP2_HUMANCRIP2physical
25865307
ATPA_HUMANATP5A1physical
25865307
DOPO_HUMANDBHphysical
25865307
VGF_HUMANVGFphysical
25865307
PRDX2_HUMANPRDX2physical
25865307
ODPB_HUMANPDHBphysical
25865307
PRDX5_HUMANPRDX5physical
25865307
ODPA_HUMANPDHA1physical
25865307
ATPO_HUMANATP5Ophysical
25865307
CALX_HUMANCANXphysical
25865307
CATD_HUMANCTSDphysical
25865307
CMC2_HUMANSLC25A13physical
25865307
VDAC2_HUMANVDAC2physical
25865307
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
256730Ceroid lipofuscinosis, neuronal, 1 (CLN1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PPT1_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple 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).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-197; ASN-212 AND ASN-232,AND MASS SPECTROMETRY.
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry.";
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
Nat. Biotechnol. 21:660-666(2003).
Cited for: GLYCOSYLATION AT ASN-232.

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