TECR_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TECR_HUMAN
• UniProt AC: Q9NZ01
• Protein Name: Very-long-chain enoyl-CoA reductase {ECO:0000305}
• Gene Name: TECR
• Organism: Homo sapiens (Human).
• 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: MKHYEVEILDAKTREKLCFLDKVEPHATIAEIKNLFTKTHPQWYPARQSLRLDPKGKSLKDEDVLQKLPVGTTATLYFRDLGAQISWVTVFLTEYAGPLFIYLLFYFRVPFIYGHKYDFTSSRHTVVHLACICHSFHYIKRLLETLFVHRFSHGTMPLRNIFKNCTYYWGFAAWMAYYINHPLYTPPTYGAQQVKLALAIFVICQLGNFSIHMALRDLRPAGSKTRKIPYPTKNPFTWLFLLVSCPNYTYEVGSWIGFAIMTQCLPVALFSLVGFTQMTIWAKGKHRSYLKEFRDYPPLRMPIIPFLL

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	------MKHYEVEIL ------CCCEEEEEE	55.69	21890473
2	Acetylation	------MKHYEVEIL ------CCCEEEEEE	55.69	25825284
2 (in isoform 2)	Ubiquitination	-	55.69	21890473
2	Malonylation	------MKHYEVEIL ------CCCEEEEEE	55.69	26320211
2 (in isoform 1)	Ubiquitination	-	55.69	21890473
4	Phosphorylation	----MKHYEVEILDA ----CCCEEEEEEEH	19.02	28152594
12 (in isoform 1)	Ubiquitination	-	48.02	21890473
12 (in isoform 2)	Ubiquitination	-	48.02	21890473
12	Malonylation	EVEILDAKTREKLCF EEEEEEHHCCHHEEC	48.02	26320211
12	Acetylation	EVEILDAKTREKLCF EEEEEEHHCCHHEEC	48.02	25953088
12	Ubiquitination	EVEILDAKTREKLCF EEEEEEHHCCHHEEC	48.02	21890473
13	Phosphorylation	VEILDAKTREKLCFL EEEEEHHCCHHEECC	45.86	22210691
16	Ubiquitination	LDAKTREKLCFLDKV EEHHCCHHEECCCCC	47.46	-
16	Acetylation	LDAKTREKLCFLDKV EEHHCCHHEECCCCC	47.46	25953088
16	2-Hydroxyisobutyrylation	LDAKTREKLCFLDKV EEHHCCHHEECCCCC	47.46	-
22	Ubiquitination	EKLCFLDKVEPHATI HHEECCCCCCCCCCH	51.12	21890473
22	Acetylation	EKLCFLDKVEPHATI HHEECCCCCCCCCCH	51.12	19608861
28	Phosphorylation	DKVEPHATIAEIKNL CCCCCCCCHHHHHHH	20.07	20068231
33	Ubiquitination	HATIAEIKNLFTKTH CCCHHHHHHHHHCCC	38.82	21890473
33 (in isoform 1)	Ubiquitination	-	38.82	21890473
38	Acetylation	EIKNLFTKTHPQWYP HHHHHHHCCCCCCCC	37.19	25825284
38	Malonylation	EIKNLFTKTHPQWYP HHHHHHHCCCCCCCC	37.19	26320211
38	2-Hydroxyisobutyrylation	EIKNLFTKTHPQWYP HHHHHHHCCCCCCCC	37.19	-
38 (in isoform 1)	Ubiquitination	-	37.19	21890473
38	Ubiquitination	EIKNLFTKTHPQWYP HHHHHHHCCCCCCCC	37.19	21890473
39	Phosphorylation	IKNLFTKTHPQWYPA HHHHHHCCCCCCCCC	35.41	27080861
44	Phosphorylation	TKTHPQWYPARQSLR HCCCCCCCCCCHHCC	5.03	28152594
49	Phosphorylation	QWYPARQSLRLDPKG CCCCCCHHCCCCCCC	15.20	27251275
57 (in isoform 1)	Ubiquitination	-	59.76	21890473
57	Malonylation	LRLDPKGKSLKDEDV CCCCCCCCCCCCHHH	59.76	26320211
57	Ubiquitination	LRLDPKGKSLKDEDV CCCCCCCCCCCCHHH	59.76	-
58	Phosphorylation	RLDPKGKSLKDEDVL CCCCCCCCCCCHHHH	49.69	25159151
60	2-Hydroxyisobutyrylation	DPKGKSLKDEDVLQK CCCCCCCCCHHHHHH	67.19	-
60	Acetylation	DPKGKSLKDEDVLQK CCCCCCCCCHHHHHH	67.19	23954790
60 (in isoform 1)	Ubiquitination	-	67.19	21890473
60	Malonylation	DPKGKSLKDEDVLQK CCCCCCCCCHHHHHH	67.19	26320211
60	Ubiquitination	DPKGKSLKDEDVLQK CCCCCCCCCHHHHHH	67.19	-
67 (in isoform 1)	Ubiquitination	-	51.07	21890473
67	Ubiquitination	KDEDVLQKLPVGTTA CCHHHHHHCCCCCEE	51.07	21890473
67	Acetylation	KDEDVLQKLPVGTTA CCHHHHHHCCCCCEE	51.07	26051181
72	Phosphorylation	LQKLPVGTTATLYFR HHHCCCCCEEEEEEH	17.31	28152594
73 (in isoform 2)	Ubiquitination	-	16.24	21890473
73	Phosphorylation	QKLPVGTTATLYFRD HHCCCCCEEEEEEHH	16.24	28152594
75	Phosphorylation	LPVGTTATLYFRDLG CCCCCEEEEEEHHHC	21.65	28152594
77	Phosphorylation	VGTTATLYFRDLGAQ CCCEEEEEEHHHCCC	7.69	28152594
116 (in isoform 1)	Ubiquitination	-	42.00	21890473
116	Ubiquitination	VPFIYGHKYDFTSSR CCCCCCCCCCCCCCC	42.00	21890473
117	Phosphorylation	PFIYGHKYDFTSSRH CCCCCCCCCCCCCCH	15.60	26437602
140 (in isoform 2)	Ubiquitination	-	29.81	21890473
145	Phosphorylation	YIKRLLETLFVHRFS HHHHHHHHHHHHHCC	26.01	21406692
164	N-linked_Glycosylation	PLRNIFKNCTYYWGF CHHHHHCCCCHHHHH	16.77	UniProtKB CARBOHYD
224	Ubiquitination	DLRPAGSKTRKIPYP HCCCCCCCCCCCCCC	51.97	21906983
224 (in isoform 1)	Ubiquitination	-	51.97	21890473
227	Ubiquitination	PAGSKTRKIPYPTKN CCCCCCCCCCCCCCC	53.95	-
247	N-linked_Glycosylation	FLLVSCPNYTYEVGS EEEECCCCCCCCCCC	46.21	UniProtKB CARBOHYD
291	Acetylation	GKHRSYLKEFRDYPP CCCHHHHHHHCCCCC	46.72	25953088
291	Malonylation	GKHRSYLKEFRDYPP CCCHHHHHHHCCCCC	46.72	26320211
291	Ubiquitination	GKHRSYLKEFRDYPP CCCHHHHHHHCCCCC	46.72	21890473
291 (in isoform 1)	Ubiquitination	-	46.72	21890473

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

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

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HACD2_HUMAN	PTPLB	physical	25416956
ACADM_HUMAN	ACADM	physical	26344197
ATPG_HUMAN	ATP5C1	physical	26344197
CALX_HUMAN	CANX	physical	26344197
TCPZ_HUMAN	CCT6A	physical	26344197
CISD1_HUMAN	CISD1	physical	26344197
CLH1_HUMAN	CLTC	physical	26344197
OST48_HUMAN	DDOST	physical	26344197
DX39B_HUMAN	DDX39B	physical	26344197
EHD1_HUMAN	EHD1	physical	26344197
GORS2_HUMAN	GORASP2	physical	26344197
DHB12_HUMAN	HSD17B12	physical	26344197
HSP7C_HUMAN	HSPA8	physical	26344197
JAGN1_HUMAN	JAGN1	physical	26344197
RAB1A_HUMAN	RAB1A	physical	26344197
RAB1B_HUMAN	RAB1B	physical	26344197
RPN1_HUMAN	RPN1	physical	26344197
SCAM3_HUMAN	SCAMP3	physical	26344197
S61A1_HUMAN	SEC61A1	physical	26344197
SGPL1_HUMAN	SGPL1	physical	26344197
MPCP_HUMAN	SLC25A3	physical	26344197
SSRA_HUMAN	SSR1	physical	26344197
SSRD_HUMAN	SSR4	physical	26344197
TOM22_HUMAN	TOMM22	physical	26344197
QCR2_HUMAN	UQCRC2	physical	26344197
VDAC1_HUMAN	VDAC1	physical	26344197
VDAC2_HUMAN	VDAC2	physical	26344197

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 614020: Mental retardation, autosomal recessive 14 (MRT14)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Acetylation

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-22, AND MASS SPECTROMETRY.
PubMed: 19608861