P20D1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: P20D1_HUMAN
• UniProt AC: Q6GTS8
• Protein Name: N-fatty-acyl-amino acid synthase/hydrolase PM20D1 {ECO:0000305|PubMed:27374330}
• Gene Name: PM20D1 {ECO:0000312|HGNC:HGNC:26518}
• Organism: Homo sapiens (Human).
• Sequence Length: 502
• Subcellular Localization: Secreted .
• Protein Description: Bidirectional N-fatty-acyl amino acid synthase/hydrolase that regulates the production of N-fatty-acyl amino acids. These metabolites are endogenous chemical uncouplers of mitochondrial respiration. In an UCP1-independent manner, maybe through interaction with mitochondrial transporters, they promote proton leakage into the mitochondrial matrix. Thereby, this secreted protein may indirectly regulate the bodily dissipation of chemical energy as heat through thermogenic respiration..
• Protein Sequence: MAQRCVCVLALVAMLLLVFPTVSRSMGPRSGEHQRASRIPSQFSKEERVAMKEALKGAIQIPTVTFSSEKSNTTALAEFGKYIHKVFPTVVSTSFIQHEVVEEYSHLFTIQGSDPSLQPYLLMAHFDVVPAPEEGWEVPPFSGLERDGIIYGRGTLDDKNSVMALLQALELLLIRKYIPRRSFFISLGHDEESSGTGAQRISALLQSRGVQLAFIVDEGGFILDDFIPNFKKPIALIAVSEKGSMNLMLQVNMTSGHSSAPPKETSIGILAAAVSRLEQTPMPIIFGSGTVVTVLQQLANEFPFPVNIILSNPWLFEPLISRFMERNPLTNAIIRTTTALTIFKAGVKFNVIPPVAQATVNFRIHPGQTVQEVLELTKNIVADNRVQFHVLSAFDPLPVSPSDDKALGYQLLRQTVQSVFPEVNITAPVTSIGNTDSRFFTNLTTGIYRFYPIYIQPEDFKRIHGVNEKISVQAYETQVKFIFELIQNADTDQEPVSHLHKL

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
25	Phosphorylation	VFPTVSRSMGPRSGE HHHHHHHHCCCCCCC	22.15	28509920
37	Phosphorylation	SGEHQRASRIPSQFS CCCCCHHHCCCCCCC	32.69	28509920
44	Phosphorylation	SRIPSQFSKEERVAM HCCCCCCCHHHHHHH	31.36	23403867
63	Phosphorylation	KGAIQIPTVTFSSEK CCCEECCEEEECCCC	33.53	30301811
65	Phosphorylation	AIQIPTVTFSSEKSN CEECCEEEECCCCCC	21.93	30301811
67	Phosphorylation	QIPTVTFSSEKSNTT ECCEEEECCCCCCCH	28.37	30301811
68	Phosphorylation	IPTVTFSSEKSNTTA CCEEEECCCCCCCHH	44.87	30301811
252	N-linked_Glycosylation	MNLMLQVNMTSGHSS EEEEEEEECCCCCCC	18.30	UniProtKB CARBOHYD
258	Phosphorylation	VNMTSGHSSAPPKET EECCCCCCCCCCCCC	31.55	20068231
259	Phosphorylation	NMTSGHSSAPPKETS ECCCCCCCCCCCCCH	38.84	20068231
265	Phosphorylation	SSAPPKETSIGILAA CCCCCCCCHHHHHHH	31.60	26657352
266	Phosphorylation	SAPPKETSIGILAAA CCCCCCCHHHHHHHH	21.65	26657352
275	Phosphorylation	GILAAAVSRLEQTPM HHHHHHHHHHHCCCC	26.82	26657352
280 (in isoform 2)	Phosphorylation	-	16.51	24043423
288 (in isoform 2)	Phosphorylation	-	22.12	24043423
290 (in isoform 2)	Phosphorylation	-	17.32	24043423
293 (in isoform 2)	Phosphorylation	-	15.91	24043423
303 (in isoform 2)	Phosphorylation	-	26.84	24043423
377	Phosphorylation	VQEVLELTKNIVADN HHHHHHHHHHHHCCC	16.81	26074081
392	Phosphorylation	RVQFHVLSAFDPLPV CEEEEEEECCCCCCC	26.29	26074081
400	Phosphorylation	AFDPLPVSPSDDKAL CCCCCCCCCCCCHHH	19.42	26074081
402	Phosphorylation	DPLPVSPSDDKALGY CCCCCCCCCCHHHHH	51.43	26074081
471	Phosphorylation	HGVNEKISVQAYETQ CCCCCCEEEEEHHHH	21.17	29396449

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

Oops, there are no upstream regulatory protein records of P20D1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of P20D1_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 P20D1_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of P20D1_HUMAN !!

Drug and Disease Associations

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