DHB12_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DHB12_MOUSE
• UniProt AC: O70503
• Protein Name: Very-long-chain 3-oxoacyl-CoA reductase {ECO:0000305}
• Gene Name: Hsd17b12 {ECO:0000312|MGI:MGI:1926967}
• Organism: Mus musculus (Mouse).
• Sequence Length: 312
• Subcellular Localization: Endoplasmic reticulum membrane ; Multi-pass membrane protein .
• Protein Description: Catalyzes the second of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme has a 3-ketoacyl-CoA reductase activity, reducing 3-ketoacyl-CoA to 3-hydroxyacyl-CoA, within each cycle of fatty acid elongation. Thereby, it may participate in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. May also catalyze the transformation of estrone (E1) into estradiol (E2) and play a role in estrogen formation..
• Protein Sequence: MECAPPAAGFLYWVGASTIAYLALRASYSLFRAFQVWCVGNEALVGPRLGEWAVVTGGTDGIGKAYAEELAKRGMKIVLISRSQDKLNQVSNNIKEKFNVETRTIAVDFSLDDIYDKIKTGLSGLEIGVLVNNVGMSYEYPEYFLEIPDLDNTIKKLININVLSVCKVTRLVLPGMVERSKGVILNISSASGMLPVPLLTIYSATKAFVDFFSQCLHEEYKSKGIFVQSVMPYLVATKLAKIQKPTLDKPSAETFVKSAIKTVGLQTRTTGYVIHSLMGSINSIMPRWMYFKIIMGFSKSLRNRYLKKRKKN

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
38	S-palmitoylation	FRAFQVWCVGNEALV HHHHEEEEECCCCCC	2.70	28526873
72	Acetylation	AYAEELAKRGMKIVL HHHHHHHHCCCEEEE	63.21	2387991
72	Ubiquitination	AYAEELAKRGMKIVL HHHHHHHHCCCEEEE	63.21	22790023
81	Phosphorylation	GMKIVLISRSQDKLN CCEEEEEECCHHHHH	23.01	25338131
83	Phosphorylation	KIVLISRSQDKLNQV EEEEEECCHHHHHHH	35.62	30352176
86	Acetylation	LISRSQDKLNQVSNN EEECCHHHHHHHHHH	41.52	23864654
86	Malonylation	LISRSQDKLNQVSNN EEECCHHHHHHHHHH	41.52	26320211
95	Succinylation	NQVSNNIKEKFNVET HHHHHHHHHHHCCCC	57.90	23954790
95	Acetylation	NQVSNNIKEKFNVET HHHHHHHHHHHCCCC	57.90	2389501
95	Ubiquitination	NQVSNNIKEKFNVET HHHHHHHHHHHCCCC	57.90	-
97	Malonylation	VSNNIKEKFNVETRT HHHHHHHHHCCCCCE	36.92	26320211
97	Acetylation	VSNNIKEKFNVETRT HHHHHHHHHCCCCCE	36.92	23201123
117	Acetylation	SLDDIYDKIKTGLSG CHHHHHHHHHHCCCC	29.18	23954790
117	Ubiquitination	SLDDIYDKIKTGLSG CHHHHHHHHHHCCCC	29.18	22790023
119	Acetylation	DDIYDKIKTGLSGLE HHHHHHHHHCCCCCC	42.13	2389517
166	S-palmitoylation	NINVLSVCKVTRLVL CCCHHHHCHHHHHHC	2.36	28526873
215	S-palmitoylation	FVDFFSQCLHEEYKS HHHHHHHHHCHHHHH	3.97	28526873
221	Ubiquitination	QCLHEEYKSKGIFVQ HHHCHHHHHCCCCHH	49.31	22790023
223	Ubiquitination	LHEEYKSKGIFVQSV HCHHHHHCCCCHHHH	52.45	22790023
238	Ubiquitination	MPYLVATKLAKIQKP HHHHHHHHHHHCCCC	36.39	22790023
244	Malonylation	TKLAKIQKPTLDKPS HHHHHCCCCCCCCCC	43.36	26320211
244	Acetylation	TKLAKIQKPTLDKPS HHHHHCCCCCCCCCC	43.36	23864654
249	Acetylation	IQKPTLDKPSAETFV CCCCCCCCCCHHHHH	43.94	23806337
261	Ubiquitination	TFVKSAIKTVGLQTR HHHHHHHHHCCCCCC	36.55	22790023
299	Malonylation	KIIMGFSKSLRNRYL HHHHCCCHHHHHHHH	51.77	26320211

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

Oops, there are no upstream regulatory protein records of DHB12_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of DHB12_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of DHB12_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of DHB12_MOUSE !!

Drug and Disease Associations

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