ELOV5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ELOV5_HUMAN
• UniProt AC: Q9NYP7
• Protein Name: Elongation of very long chain fatty acids protein 5 {ECO:0000255|HAMAP-Rule:MF_03205, ECO:0000305}
• Gene Name: ELOVL5 {ECO:0000255|HAMAP-Rule:MF_03205}
• Organism: Homo sapiens (Human).
• Sequence Length: 299
• Subcellular Localization: Endoplasmic reticulum membrane ; Multi-pass membrane protein . Cell projection, dendrite . In Purkinje cells, the protein localizes to the soma and proximal portion of the dendritic tree.
• Protein Description: Catalyzes the first and rate-limiting reaction of the four that constitute 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. Condensing enzyme that acts specifically toward polyunsaturated acyl-CoA with the higher activity toward C18:3(n-6) acyl-CoA. May participate in the production of monounsaturated and of polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators..
• Protein Sequence: MEHFDASLSTYFKALLGPRDTRVKGWFLLDNYIPTFICSVIYLLIVWLGPKYMRNKQPFSCRGILVVYNLGLTLLSLYMFCELVTGVWEGKYNFFCQGTRTAGESDMKIIRVLWWYYFSKLIEFMDTFFFILRKNNHQITVLHVYHHASMLNIWWFVMNWVPCGHSYFGATLNSFIHVLMYSYYGLSSVPSMRPYLWWKKYITQGQLLQFVLTIIQTSCGVIWPCTFPLGWLYFQIGYMISLIALFTNFYIQTYNKKGASRRKDHLKDHQNGSMAAVNGHTNSFSPLENNVKPRKLRKD

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	-------MEHFDASL -------CCCCHHHH	9.01	25944712
7	Phosphorylation	-MEHFDASLSTYFKA -CCCCHHHHHHHHHH	25.38	20068231
9	Phosphorylation	EHFDASLSTYFKALL CCCHHHHHHHHHHHH	20.68	20068231
10	Phosphorylation	HFDASLSTYFKALLG CCHHHHHHHHHHHHC	37.97	20068231
11	Phosphorylation	FDASLSTYFKALLGP CHHHHHHHHHHHHCC	10.33	20068231
13	Ubiquitination	ASLSTYFKALLGPRD HHHHHHHHHHHCCCC	27.93	-
21	Phosphorylation	ALLGPRDTRVKGWFL HHHCCCCCCCCCEEH	38.35	20068231
56	Ubiquitination	GPKYMRNKQPFSCRG CHHHHCCCCCCCCCC	49.32	-
108	Ubiquitination	TAGESDMKIIRVLWW CCCHHHHHHHHHHHH	39.72	-
199	2-Hydroxyisobutyrylation	MRPYLWWKKYITQGQ CCCCHHHHHHCCHHH	24.90	-
199	Ubiquitination	MRPYLWWKKYITQGQ CCCCHHHHHHCCHHH	24.90	21890473
226	Ubiquitination	CGVIWPCTFPLGWLY CCCHHCCCCCHHHHH	24.98	21890473
267	Ubiquitination	SRRKDHLKDHQNGSM CCCCHHHHHCCCCCC	50.15	21890473
273	Phosphorylation	LKDHQNGSMAAVNGH HHHCCCCCCEECCCC	16.88	23927012
281	Phosphorylation	MAAVNGHTNSFSPLE CEECCCCCCCCCCCC	33.68	25159151
283	Phosphorylation	AVNGHTNSFSPLENN ECCCCCCCCCCCCCC	28.40	23927012
285	Phosphorylation	NGHTNSFSPLENNVK CCCCCCCCCCCCCCC	28.53	23927012
294	Ubiquitination	LENNVKPRKLRKD-- CCCCCCCCCCCCC--	44.94	21890473
300	Phosphorylation	PRKLRKD-------- CCCCCCC--------		27251275
310	Phosphorylation	------------------ ------------------		24719451

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

Oops, there are no upstream regulatory protein records of ELOV5_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ELOV5_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 ELOV5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ROMO1_HUMAN	ROMO1	physical	27173435

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 615957: Spinocerebellar ataxia 38 (SCA38)
• 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

"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, AND MASSSPECTROMETRY.
PubMed: 18691976