dbPTM

HACD2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HACD2_HUMAN
UniProt AC	Q6Y1H2
Protein Name	Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 2 {ECO:0000305}
Gene Name	HACD2 {ECO:0000303\|PubMed:18554506, ECO:0000312\|HGNC:HGNC:9640}
Organism	Homo sapiens (Human).
Sequence Length	254
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..
Protein Sequence	MAAVAATAAAKGNGGGGGRAGAGDASGTRKKKGPGPLATAYLVIYNVVMTAGWLVIAVGLVRAYLAKGSYHSLYYSIEKPLKFFQTGALLEILHCAIGIVPSSVVLTSFQVMSRVFLIWAVTHSVKEVQSEDSVLLFVIAWTITEIIRYSFYTFSLLNHLPYLIKWARYTLFIVLYPMGVSGELLTIYAALPFVRQAGLYSISLPNKYNFSFDYYAFLILIMISYIPIFPQLYFHMIHQRRKILSHTEEHKKFE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAVAATAA ------CCHHHHHHH	15.62	25732826
7	Phosphorylation	-MAAVAATAAAKGNG -CCHHHHHHHHCCCC	13.69	-
11	Ubiquitination	VAATAAAKGNGGGGG HHHHHHHCCCCCCCC	48.45	24816145
140	Ubiquitination	SVLLFVIAWTITEII CCHHHHHHHHHHHHH	7.64	33845483
141	Ubiquitination	VLLFVIAWTITEIIR CHHHHHHHHHHHHHH	4.17	29967540
158	Ubiquitination	FYTFSLLNHLPYLIK HHHHHHHHCHHHHHH	39.69	33845483
159	Ubiquitination	YTFSLLNHLPYLIKW HHHHHHHCHHHHHHH	28.31	29967540
169	Phosphorylation	YLIKWARYTLFIVLY HHHHHHHHHHEEEEE	10.47	24043423
170	Phosphorylation	LIKWARYTLFIVLYP HHHHHHHHHEEEEEC	15.05	24043423
176	Phosphorylation	YTLFIVLYPMGVSGE HHHEEEEECCCCCHH	4.73	24043423
181	Phosphorylation	VLYPMGVSGELLTIY EEECCCCCHHHHHHH	22.33	24043423
186	Phosphorylation	GVSGELLTIYAALPF CCCHHHHHHHHHHHH	25.27	24043423
188	Phosphorylation	SGELLTIYAALPFVR CHHHHHHHHHHHHHH	4.79	24043423
209	N-linked_Glycosylation	ISLPNKYNFSFDYYA EECCCCCCCCCHHHH	27.91	UniProtKB CARBOHYD
245	Phosphorylation	HQRRKILSHTEEHKK HHHHHHHHCCHHHHC	31.66	29496907
247	Phosphorylation	RRKILSHTEEHKKFE HHHHHHCCHHHHCCC	39.43	29496907
251	Ubiquitination	LSHTEEHKKFE---- HHCCHHHHCCC----	63.54	24816145
251	2-Hydroxyisobutyrylation	LSHTEEHKKFE---- HHCCHHHHCCC----	63.54	-
252	Ubiquitination	SHTEEHKKFE----- HCCHHHHCCC-----	57.54	29967540
274	Ubiquitination	--------------------------- ---------------------------		33845483
275	Ubiquitination	---------------------------- ----------------------------		29967540

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of HACD2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of HACD2_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of HACD2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
BAP31_HUMAN	BCAP31	physical	15024066

Drug and Disease Associations

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

Regulatory Network of HACD2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]