DHB12_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DHB12_RAT
• UniProt AC: Q6P7R8
• Protein Name: Very-long-chain 3-oxoacyl-CoA reductase {ECO:0000305}
• Gene Name: Hsd17b12 {ECO:0000312|RGD:708367}
• Organism: Rattus norvegicus (Rat).
• 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: MERALPAAGFLYWVGASTIAYLTLRASYSLFRAFQVWCVGNQAFVGPRLGEWAVVTGGTDGIGKSYAEELAKRGMKIVLISRSQDKLKEVSNNIKEKFNVETRTIAVDFSLDDIYDKIKTGLSGLEIGVLVNNVGMSYEYPEYFLEIPDLDNTIKKLININVLSICKVTRLVLPGMVERSKGVILNISSASGMLPVPLLTVYSATKAFVDFFSQCLHEEYKSKGIFVQSVLPFFVATKLAKIRKPTLDKPSAETFVKSAIKTVGLQTRTTGYVIHAIMGSINSILPRWIYFKTIMGFNKSLRNRYLKKTKKN

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
88	Acetylation	SRSQDKLKEVSNNIK ECCHHHHHHHHHHHH	62.91	22902405
97	Acetylation	VSNNIKEKFNVETRT HHHHHHHHHCCCCCE	36.92	22902405
155	"N6,N6-dimethyllysine"	PDLDNTIKKLININV CCCCHHHHHHHCCCH	39.22	-
155	Methylation	PDLDNTIKKLININV CCCCHHHHHHHCCCH	39.22	12692561
156	"N6,N6-dimethyllysine"	DLDNTIKKLININVL CCCHHHHHHHCCCHH	51.23	-
156	Methylation	DLDNTIKKLININVL CCCHHHHHHHCCCHH	51.23	12692561
290	Phosphorylation	SILPRWIYFKTIMGF HHHHHHHHHHHHHCC	7.64	-
299	Acetylation	KTIMGFNKSLRNRYL HHHHCCCHHHHHHHH	48.91	22902405

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

Oops, there are no upstream regulatory protein records of DHB12_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of DHB12_RAT !!

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_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of DHB12_RAT !!

Drug and Disease Associations

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