PPT2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PPT2_HUMAN
• UniProt AC: Q9UMR5
• Protein Name: Lysosomal thioesterase PPT2
• Gene Name: PPT2
• Organism: Homo sapiens (Human).
• Sequence Length: 302
• Subcellular Localization: Lysosome .
• Protein Description: Removes thioester-linked fatty acyl groups from various substrates including S-palmitoyl-CoA. Has the highest S-thioesterase activity for the acyl groups palmitic and myristic acid followed by other short- and long-chain acyl substrates. However, because of structural constraints, is unable to remove palmitate from peptides or proteins..
• Protein Sequence: MLGLCGQRLPAAWVLLLLPFLPLLLLAAPAPHRASYKPVIVVHGLFDSSYSFRHLLEYINETHPGTVVTVLDLFDGRESLRPLWEQVQGFREAVVPIMAKAPQGVHLICYSQGGLVCRALLSVMDDHNVDSFISLSSPQMGQYGDTDYLKWLFPTSMRSNLYRICYSPWGQEFSICNYWHDPHHDDLYLNASSFLALINGERDHPNATVWRKNFLRVGHLVLIGGPDDGVITPWQSSFFGFYDANETVLEMEEQLVYLRDSFGLKTLLARGAIVRCPMAGISHTAWHSNRTLYETCIEPWLS

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
60	N-linked_Glycosylation	RHLLEYINETHPGTV HHHHHHHHHCCCCCE	47.41	UniProtKB CARBOHYD
190	N-linked_Glycosylation	HHDDLYLNASSFLAL CCCCCEECHHHHHHH	24.99	12855696
206	N-linked_Glycosylation	NGERDHPNATVWRKN CCCCCCCCCCCCCCC	44.84	UniProtKB CARBOHYD
245	N-linked_Glycosylation	FFGFYDANETVLEME CCCEECCCHHHEHHH	42.44	UniProtKB CARBOHYD
289	N-linked_Glycosylation	SHTAWHSNRTLYETC CCCEECCCCCHHHHH	28.24	UniProtKB CARBOHYD

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of PPT2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PPT2_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of PPT2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RS16_HUMAN	RPS16	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
SPTN1_HUMAN	SPTAN1	physical	22939629
SSRD_HUMAN	SSR4	physical	22939629
RM23_HUMAN	MRPL23	physical	22939629
RL21_HUMAN	RPL21	physical	22939629
RL8_HUMAN	RPL8	physical	22939629
SYSM_HUMAN	SARS2	physical	22939629
SYIM_HUMAN	IARS2	physical	22939629
RL3_HUMAN	RPL3	physical	22939629
RS26_HUMAN	RPS26	physical	22939629
PYC_HUMAN	PC	physical	22939629
SPT5H_HUMAN	SUPT5H	physical	22939629
RM49_HUMAN	MRPL49	physical	22939629

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"The crystal structure of palmitoyl protein thioesterase-2 (PPT2)reveals the basis for divergent substrate specificities of the twolysosomal thioesterases, PPT1 and PPT2.";
Calero G., Gupta P., Nonato M.C., Tandel S., Biehl E.R., Hofmann S.L.,Clardy J.;
J. Biol. Chem. 278:37957-37964(2003).
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), FUNCTION, KINETIC PARAMETERS,MUTAGENESIS OF SER-111; ASP-228; HIS-283 AND HIS-287, GLYCOSYLATION ATASN-190, AND DISULFIDE BONDS.
PubMed: 12855696