HACD3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: HACD3_MOUSE
• UniProt AC: Q8K2C9
• Protein Name: Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 3 {ECO:0000305}
• Gene Name: Hacd3 {ECO:0000312|MGI:MGI:1889341}
• Organism: Mus musculus (Mouse).
• Sequence Length: 362
• Subcellular Localization: Endoplasmic reticulum membrane ; Multi-pass membrane protein .
• Protein Description: Catalyzes the third 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 catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid 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. Involved in Rac1-signaling pathways leading to the modulation of gene expression. Promotes insulin receptor/INSR autophosphorylation and is involved in INSR internalization (By similarity)..
• Protein Sequence: METQVLTPHVYWAQRHRELYLRVELSDVQNPAISITDNVLHFKAQGHGAKGDNVYEFHLEFLDLVKPEPAYRLTQRQVNITVQKKGSHWWERLTKQEKRPLFLAPDFDRWLDESDAEMELRAKEEERLNKLRLEREGSPETLTNLKKGYLFMYNLVQLLGFSWIFVNLTVRFFILGKESFYDTFHNVADMMYFCQMLALVETLNAAIGVTSTPVLPALIQFLGRNFILFLVFGTMEEMQNKAVVFFVFYSWSAIEIFRYPFYMLSCIDMDWKVLTWLRYTMWIPLYPLGCLSEAVAVIQSIPVFNESGRFSFTLPYPVKMKVRFSFFLQVYLVMLFLGLYINFRHLYKQRRRRYGQKKKKLH

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
1	Acetylation	-------METQVLTP -------CCCCCCCC	13.03	-
7	Phosphorylation	-METQVLTPHVYWAQ -CCCCCCCCCHHHHH	16.70	-
43	Ubiquitination	TDNVLHFKAQGHGAK ECCEEEEEEECCCCC	29.11	22790023
71	Phosphorylation	LVKPEPAYRLTQRQV HCCCCHHEEEEEEEE	19.51	-
85	Malonylation	VNITVQKKGSHWWER EEEEEEECCCHHHHH	48.86	26320211
98	Ubiquitination	ERLTKQEKRPLFLAP HHCCHHCCCCCEECC	57.74	-
98	Malonylation	ERLTKQEKRPLFLAP HHCCHHCCCCCEECC	57.74	26320211
114	Phosphorylation	FDRWLDESDAEMELR HHHHCCCCHHHHHHH	41.61	24925903
138	Phosphorylation	LRLEREGSPETLTNL HHHHCCCCHHHHHHH	18.14	25521595
141	Phosphorylation	EREGSPETLTNLKKG HCCCCHHHHHHHHHH	42.12	25521595
143	Phosphorylation	EGSPETLTNLKKGYL CCCHHHHHHHHHHHH	46.02	22324799
146	Ubiquitination	PETLTNLKKGYLFMY HHHHHHHHHHHHHHH	46.34	27667366
202	Phosphorylation	QMLALVETLNAAIGV HHHHHHHHHHHHHCC	20.17	22802335
210	Phosphorylation	LNAAIGVTSTPVLPA HHHHHCCCCCCHHHH	22.97	22802335
211	Phosphorylation	NAAIGVTSTPVLPAL HHHHCCCCCCHHHHH	28.45	22802335
212	Phosphorylation	AAIGVTSTPVLPALI HHHCCCCCCHHHHHH	14.19	22802335

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

Oops, there are no upstream regulatory protein records of HACD3_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of HACD3_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 HACD3_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of HACD3_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASSSPECTROMETRY.
PubMed: 19144319

"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASSSPECTROMETRY.
PubMed: 18630941

"Mitochondrial phosphoproteome revealed by an improved IMAC method andMS/MS/MS.";
Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
Mol. Cell. Proteomics 6:669-676(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASSSPECTROMETRY.
PubMed: 17208939

"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASSSPECTROMETRY.
PubMed: 17114649

"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASSSPECTROMETRY.
PubMed: 17203969

"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASSSPECTROMETRY.
PubMed: 15345747