THTM_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: THTM_HUMAN
• UniProt AC: P25325
• Protein Name: 3-mercaptopyruvate sulfurtransferase
• Gene Name: MPST
• Organism: Homo sapiens (Human).
• Sequence Length: 297
• Subcellular Localization: Cytoplasm . Mitochondrion . Cell junction, synapse, synaptosome .
• Protein Description: Transfer of a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity. Detoxifies cyanide and is required for thiosulfate biosynthesis. Acts as an antioxidant. In combination with cysteine aminotransferase (CAT), contributes to the catabolism of cysteine and is an important producer of hydrogen sulfide in the brain, retina and vascular endothelial cells. Hydrogen sulfide H(2)S is an important synaptic modulator, signaling molecule, smooth muscle contractor and neuroprotectant. Its production by the 3MST/CAT pathway is regulated by calcium ions..
• Protein Sequence: MASPQLCRALVSAQWVAEALRAPRAGQPLQLLDASWYLPKLGRDARREFEERHIPGAAFFDIDQCSDRTSPYDHMLPGAEHFAEYAGRLGVGAATHVVIYDASDQGLYSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQNLPLSSGKSQPAPAEFRAQLDPAFIKTYEDIKENLESRRFQVVDSRATGRFRGTEPEPRDGIEPGHIPGTVNIPFTDFLSQEGLEKSPEEIRHLFQEKKVDLSKPLVATCGSGVTACHVALGAYLCGKPDVPIYDGSWVEWYMRARPEDVISEGRGKTH

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
2	Acetylation	------MASPQLCRA ------CCCHHHHHH	29.89	25944712
3	Phosphorylation	-----MASPQLCRAL -----CCCHHHHHHH	16.33	20068231
12	Phosphorylation	QLCRALVSAQWVAEA HHHHHHHHHHHHHHH	18.65	24670416
15 (in isoform 2)	Phosphorylation	-	7.33	20201521
15	Phosphorylation	RALVSAQWVAEALRA HHHHHHHHHHHHHCC	7.33	24719451
17	Phosphorylation	LVSAQWVAEALRAPR HHHHHHHHHHHCCCC	8.06	24719451
17 (in isoform 2)	Phosphorylation	-	8.06	30266825
23	Phosphorylation	VAEALRAPRAGQPLQ HHHHHCCCCCCCCEE	21.88	-
23 (in isoform 2)	Phosphorylation	-	21.88	25159151
35	Phosphorylation	PLQLLDASWYLPKLG CEEEECHHHHHHHCC	18.87	20068231
37	Phosphorylation	QLLDASWYLPKLGRD EEECHHHHHHHCCHH	15.61	20068231
40	Acetylation	DASWYLPKLGRDARR CHHHHHHHCCHHHHH	62.06	-
40	Succinylation	DASWYLPKLGRDARR CHHHHHHHCCHHHHH	62.06	-
40	Ubiquitination	DASWYLPKLGRDARR CHHHHHHHCCHHHHH	62.06	-
40	Succinylation	DASWYLPKLGRDARR CHHHHHHHCCHHHHH	62.06	-
40	Ubiquitination	DASWYLPKLGRDARR CHHHHHHHCCHHHHH	62.06	-
55	Phosphorylation	EFEERHIPGAAFFDI HHHHCCCCCCEEECH	21.90	-
65	Glutathionylation	AFFDIDQCSDRTSPY EEECHHHCCCCCCCC	3.97	22555962
72	Phosphorylation	CSDRTSPYDHMLPGA CCCCCCCCCCCCCCH	20.46	-
85	Phosphorylation	GAEHFAEYAGRLGVG CHHHHHHHHHHHCCC	15.78	-
108	Phosphorylation	DASDQGLYSAPRVWW ECCCCCCCHHHHHHH	15.04	-
144	Phosphorylation	RQNLPLSSGKSQPAP HHCCCCCCCCCCCCC	58.90	26437602
146	Ubiquitination	NLPLSSGKSQPAPAE CCCCCCCCCCCCCHH	48.11	-
146	Succinylation	NLPLSSGKSQPAPAE CCCCCCCCCCCCCHH	48.11	-
146	Succinylation	NLPLSSGKSQPAPAE CCCCCCCCCCCCCHH	48.11	-
164	Ubiquitination	QLDPAFIKTYEDIKE HCCHHHHHHHHHHHH	38.30	-
164	Succinylation	QLDPAFIKTYEDIKE HCCHHHHHHHHHHHH	38.30	21906983
164	Ubiquitination	QLDPAFIKTYEDIKE HCCHHHHHHHHHHHH	38.30	21906983
164	Succinylation	QLDPAFIKTYEDIKE HCCHHHHHHHHHHHH	38.30	-
164	Ubiquitination	QLDPAFIKTYEDIKE HCCHHHHHHHHHHHH	38.30	-
165	Phosphorylation	LDPAFIKTYEDIKEN CCHHHHHHHHHHHHH	27.59	28796482
166	Phosphorylation	DPAFIKTYEDIKENL CHHHHHHHHHHHHHH	13.45	28796482
170	Sumoylation	IKTYEDIKENLESRR HHHHHHHHHHHHHCC	53.52	-
170	Acetylation	IKTYEDIKENLESRR HHHHHHHHHHHHHCC	53.52	25038526
170	Ubiquitination	IKTYEDIKENLESRR HHHHHHHHHHHHHCC	53.52	-
184	Ubiquitination	RFQVVDSRATGRFRG CEEEECCCCCCCCCC	31.53	21906983
214	Phosphorylation	GTVNIPFTDFLSQEG CCEECCHHHHCCHHH	22.08	26552605
218	Phosphorylation	IPFTDFLSQEGLEKS CCHHHHCCHHHHCCC	26.61	26657352
224	Ubiquitination	LSQEGLEKSPEEIRH CCHHHHCCCHHHHHH	76.09	-
225	Phosphorylation	SQEGLEKSPEEIRHL CHHHHCCCHHHHHHH	28.33	20068231
234	Phosphorylation	EEIRHLFQEKKVDLS HHHHHHHHHCCCCCC	68.88	27251275
236	2-Hydroxyisobutyrylation	IRHLFQEKKVDLSKP HHHHHHHCCCCCCCC	47.52	-
236	Ubiquitination	IRHLFQEKKVDLSKP HHHHHHHCCCCCCCC	47.52	-
236	Acetylation	IRHLFQEKKVDLSKP HHHHHHHCCCCCCCC	47.52	25953088
241	Phosphorylation	QEKKVDLSKPLVATC HHCCCCCCCCCCCCC	27.97	24719451
245	Phosphorylation	VDLSKPLVATCGSGV CCCCCCCCCCCCCCH	5.86	24719451
247	Phosphorylation	LSKPLVATCGSGVTA CCCCCCCCCCCCHHH	15.21	20068231
250	Phosphorylation	PLVATCGSGVTACHV CCCCCCCCCHHHHHH	32.03	20068231
253	Phosphorylation	ATCGSGVTACHVALG CCCCCCHHHHHHHHH	27.39	20068231
262	Phosphorylation	CHVALGAYLCGKPDV HHHHHHHHHCCCCCC	10.75	20068231
270	Phosphorylation	LCGKPDVPIYDGSWV HCCCCCCCCCCCCHH	27.14	-
272	Phosphorylation	GKPDVPIYDGSWVEW CCCCCCCCCCCHHHH	14.26	-

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of THTM_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 THTM_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UCRI_HUMAN	UQCRFS1	physical	22939629
TIM9_HUMAN	TIMM9	physical	22939629
VAPB_HUMAN	VAPB	physical	22939629
YKT6_HUMAN	YKT6	physical	22939629
TPIS_HUMAN	TPI1	physical	22939629
UPP1_HUMAN	UPP1	physical	22939629
TM189_HUMAN	TMEM189	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.