TECR_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TECR_MOUSE
• UniProt AC: Q9CY27
• Protein Name: Very-long-chain enoyl-CoA reductase {ECO:0000305}
• Gene Name: Tecr
• Organism: Mus musculus (Mouse).
• Sequence Length: 308
• Subcellular Localization: Endoplasmic reticulum membrane ; Multi-pass membrane protein .
• Protein Description: Catalyzes the last of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme reduces the trans-2,3-enoyl-CoA fatty acid intermediate to an acyl-CoA that can be further elongated by entering a new cycle of elongation. Thereby, it participates in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators..
• Protein Sequence: MKHYEVEIRDAKTREKLCFLDKVEPQATISEIKTLFTKTHPQWYPARQSLRLDPKGKSLKDEDVLQKLPVGTTATLYFRDLGAQISWVTVFLTEYAGPLFIYLLFYFRVPFIYGRKYDFTSSRHTVVHLACMCHSFHYIKRLLETLFVHRFSHGTMPLRNIFKNCTYYWGFAAWMAYYINHPLYTPPTYGVQQVKLALAVFVICQLGNFSIHMALRDLRPAGSKTRKIPYPTKNPFTWLFLLVSCPNYTYEVGSWIGFAILTQCVPVALFSLVGFTQMTIWAKGKHRSYLKEFRDYPPLRMPIIPFLL

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	Ubiquitination	------MKHYEVEIR ------CCCEEEEEE	55.69	-
2	Malonylation	------MKHYEVEIR ------CCCEEEEEE	55.69	26320211
16	Ubiquitination	RDAKTREKLCFLDKV ECCCCHHHEECCCCC	47.46	-
16	Malonylation	RDAKTREKLCFLDKV ECCCCHHHEECCCCC	47.46	26320211
18	S-palmitoylation	AKTREKLCFLDKVEP CCCHHHEECCCCCCC	4.76	28526873
18	S-nitrosylation	AKTREKLCFLDKVEP CCCHHHEECCCCCCC	4.76	22178444
18	S-nitrosocysteine	AKTREKLCFLDKVEP CCCHHHEECCCCCCC	4.76	-
22	Acetylation	EKLCFLDKVEPQATI HHEECCCCCCCCCCH	51.12	-
22	Methylation	EKLCFLDKVEPQATI HHEECCCCCCCCCCH	51.12	-
22	Malonylation	EKLCFLDKVEPQATI HHEECCCCCCCCCCH	51.12	26073543
22	Ubiquitination	EKLCFLDKVEPQATI HHEECCCCCCCCCCH	51.12	-
38	Ubiquitination	EIKTLFTKTHPQWYP HHHHHHHCCCCCCCC	37.19	22790023
38	Malonylation	EIKTLFTKTHPQWYP HHHHHHHCCCCCCCC	37.19	30639696
49	Phosphorylation	QWYPARQSLRLDPKG CCCCCCHHCCCCCCC	15.20	25159016
57	Malonylation	LRLDPKGKSLKDEDV CCCCCCCCCCCCHHH	59.76	26320211
57	Ubiquitination	LRLDPKGKSLKDEDV CCCCCCCCCCCCHHH	59.76	-
58	Phosphorylation	RLDPKGKSLKDEDVL CCCCCCCCCCCHHHH	49.69	27742792
60	Ubiquitination	DPKGKSLKDEDVLQK CCCCCCCCCHHHHHH	67.19	-
60	Acetylation	DPKGKSLKDEDVLQK CCCCCCCCCHHHHHH	67.19	23806337
60	Malonylation	DPKGKSLKDEDVLQK CCCCCCCCCHHHHHH	67.19	26320211
67	Ubiquitination	KDEDVLQKLPVGTTA CCHHHHHHCCCCCEE	51.07	22790023
116	Acetylation	VPFIYGRKYDFTSSR CCCCCCCCCCCCCCC	44.82	92221
164	N-linked_Glycosylation	PLRNIFKNCTYYWGF CHHHHHCCCCHHHHH	16.77	-
227	Malonylation	PAGSKTRKIPYPTKN CCCCCCCCCCCCCCC	53.95	26320211
247	N-linked_Glycosylation	FLLVSCPNYTYEVGS EEEECCCCCCCCCCC	46.21	-
291	Ubiquitination	GKHRSYLKEFRDYPP CCCHHHHHHHCCCCC	46.72	-
291	Malonylation	GKHRSYLKEFRDYPP CCCHHHHHHHCCCCC	46.72	26320211

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TECR_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 TECR_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of TECR_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Acetylation

"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-116, AND MASS SPECTROMETRY.
PubMed: 16916647