HACD1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: HACD1_HUMAN
• UniProt AC: B0YJ81
• Protein Name: Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 1 {ECO:0000305}
• Gene Name: HACD1 {ECO:0000303|PubMed:15164054, ECO:0000312|HGNC:HGNC:9639}
• Organism: Homo sapiens (Human).
• Sequence Length: 288
• Subcellular Localization: Isoform 1: Endoplasmic reticulum membrane ; Multi-pass membrane protein .
• Protein Description: Isoform 1: 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.; Isoform 2: In tooth development, may play a role in the recruitment and the differentiation of cells that contribute to cementum formation. May also bind hydroxyapatite and regulate its crystal nucleation to form cementum..
• Protein Sequence: MGRLTEAAAAGSGSRAAGWAGSPPTLLPLSPTSPRCAATMASSDEDGTNGGASEAGEDREAPGERRRLGVLATAWLTFYDIAMTAGWLVLAIAMVRFYMEKGTHRGLYKSIQKTLKFFQTFALLEIVHCLIGIVPTSVIVTGVQVSSRIFMVWLITHSIKPIQNEESVVLFLVAWTVTEITRYSFYTFSLLDHLPYFIKWARYNFFIILYPVGVAGELLTIYAALPHVKKTGMFSIRLPNKYNVSFDYYYFLLITMASYIPLFPQLYFHMLRQRRKVLHGEVIVEKDD

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
5	Phosphorylation	---MGRLTEAAAAGS ---CCHHHHHHHCCC	23.40	20068231
12	Phosphorylation	TEAAAAGSGSRAAGW HHHHHCCCCCCCCCC	28.95	20068231
14	Phosphorylation	AAAAGSGSRAAGWAG HHHCCCCCCCCCCCC	22.05	20068231
22	Phosphorylation	RAAGWAGSPPTLLPL CCCCCCCCCCCEEEC	21.69	11054553
25	Phosphorylation	GWAGSPPTLLPLSPT CCCCCCCCEEECCCC	44.29	20068231
30	Phosphorylation	PPTLLPLSPTSPRCA CCCEEECCCCCCCHH	24.96	20068231
32	Phosphorylation	TLLPLSPTSPRCAAT CEEECCCCCCCHHHH	48.24	20068231
33	Phosphorylation	LLPLSPTSPRCAATM EEECCCCCCCHHHHC	17.46	20068231
39	Phosphorylation	TSPRCAATMASSDED CCCCHHHHCCCCCCC	8.51	23879269
43	Phosphorylation	CAATMASSDEDGTNG HHHHCCCCCCCCCCC	35.17	28787133
109	Ubiquitination	GTHRGLYKSIQKTLK CCCHHHHHHHHHHHH	46.23	-
235	Phosphorylation	VKKTGMFSIRLPNKY CCCCCCEEEECCCCC	9.63	-
243	N-linked_Glycosylation	IRLPNKYNVSFDYYY EECCCCCCCCCCHHH	25.27	UniProtKB CARBOHYD

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

Oops, there are no upstream regulatory protein records of HACD1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of HACD1_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 HACD1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SEMG2_HUMAN	SEMG2	physical	26186194
SEMG1_HUMAN	SEMG1	physical	26186194
SEMG1_HUMAN	SEMG1	physical	28514442
SEMG2_HUMAN	SEMG2	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 255310: Myopathy, congenital, with fiber-type disproportion (CFTD)
• 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

Phosphorylation

"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-30 AND THR-32,AND MASS SPECTROMETRY.
PubMed: 18669648