ELOV4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ELOV4_HUMAN
• UniProt AC: Q9GZR5
• Protein Name: Elongation of very long chain fatty acids protein 4 {ECO:0000255|HAMAP-Rule:MF_03204, ECO:0000305}
• Gene Name: ELOVL4 {ECO:0000255|HAMAP-Rule:MF_03204}
• Organism: Homo sapiens (Human).
• Sequence Length: 314
• Subcellular Localization: Endoplasmic reticulum membrane ; Multi-pass membrane protein .
• 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 specifically elongates C24:0 and C26:0 acyl-CoAs. May participate in the production of saturated and monounsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. May play a critical role in early brain and skin development..
• Protein Sequence: MGLLDSEPGSVLNVVSTALNDTVEFYRWTWSIADKRVENWPLMQSPWPTLSISTLYLLFVWLGPKWMKDREPFQMRLVLIIYNFGMVLLNLFIFRELFMGSYNAGYSYICQSVDYSNNVHEVRIAAALWWYFVSKGVEYLDTVFFILRKKNNQVSFLHVYHHCTMFTLWWIGIKWVAGGQAFFGAQLNSFIHVIMYSYYGLTAFGPWIQKYLWWKRYLTMLQLIQFHVTIGHTALSLYTDCPFPKWMHWALIAYAISFIFLFLNFYIRTYKEPKKPKAGKTAMNGISANGVSKSEKQLMIENGKKQKNGKAKGD

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
20	N-linked_Glycosylation	NVVSTALNDTVEFYR HHHHHHHCCHHHHHH	40.21	16036915
35	Ubiquitination	WTWSIADKRVENWPL EEEECCCCCHHCCCC	49.69	21890473
270	Phosphorylation	LNFYIRTYKEPKKPK HHHHHHHCCCCCCCC	11.96	33259812
280	Ubiquitination	PKKPKAGKTAMNGIS CCCCCCCCCCCCCCC	37.66	-
292	Phosphorylation	GISANGVSKSEKQLM CCCCCCCCHHHHHHH	31.68	-
293	Ubiquitination	ISANGVSKSEKQLMI CCCCCCCHHHHHHHC	61.29	32015554
294	Phosphorylation	SANGVSKSEKQLMIE CCCCCCHHHHHHHCC	42.38	-
296	Ubiquitination	NGVSKSEKQLMIENG CCCCHHHHHHHCCCC	56.68	32142685

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

Oops, there are no upstream regulatory protein records of ELOV4_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ELOV4_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 ELOV4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ELOV4_HUMAN	ELOVL4	physical	16036915

Drug and Disease Associations

• Kegg Disease
• H00819: Stargardt disease (STGD); Fundus flavimaculatus
• OMIM Disease
• 600110: Stargardt disease 3 (STGD3)
• 614457: Ichthyosis, spastic quadriplegia, and mental retardation (ISQMR)
• 133190: Spinocerebellar ataxia 34 (SCA34)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• DB00132: Alpha-Linolenic Acid

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Dominant negative mechanism underlies autosomal dominant Stargardt-like macular dystrophy linked to mutations in ELOVL4.";
Grayson C., Molday R.S.;
J. Biol. Chem. 280:32521-32530(2005).
Cited for: SUBCELLULAR LOCATION, OLIGOMERIZATION, AND GLYCOSYLATION AT ASN-20.
PubMed: 16036915