ELOV2_HUMAN - dbPTM
ELOV2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ELOV2_HUMAN
UniProt AC Q9NXB9
Protein Name Elongation of very long chain fatty acids protein 2 {ECO:0000255|HAMAP-Rule:MF_03202, ECO:0000305}
Gene Name ELOVL2 {ECO:0000255|HAMAP-Rule:MF_03202}
Organism Homo sapiens (Human).
Sequence Length 296
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. Acts specifically toward polyunsaturated acyl-CoA with the higher activity toward C20:4(n-6) acyl-CoA. Condensing enzyme that catalyzes the synthesis of polyunsaturated very long chain fatty acid (C20- and C22-PUFA). May participate in the production of polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators..
Protein Sequence MEHLKAFDDEINAFLDNMFGPRDSRVRGWFMLDSYLPTFFLTVMYLLSIWLGNKYMKNRPALSLRGILTLYNLGITLLSAYMLAELILSTWEGGYNLQCQDLTSAGEADIRVAKVLWWYYFSKSVEFLDTIFFVLRKKTSQITFLHVYHHASMFNIWWCVLNWIPCGQSFFGPTLNSFIHILMYSYYGLSVFPSMHKYLWWKKYLTQAQLVQFVLTITHTMSAVVKPCGFPFGCLIFQSSYMLTLVILFLNFYVQTYRKKPMKKDMQEPPAGKEVKNGFSKAYFTAANGVMNKKAQ
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 Orthologous
Protein Cluster
34PhosphorylationRGWFMLDSYLPTFFL
CCHHCCCCHHHHHHH
25.3025693802
35PhosphorylationGWFMLDSYLPTFFLT
CHHCCCCHHHHHHHH
19.1725693802
38PhosphorylationMLDSYLPTFFLTVMY
CCCCHHHHHHHHHHH
25.1525693802
42PhosphorylationYLPTFFLTVMYLLSI
HHHHHHHHHHHHHHH
9.7025693802
45PhosphorylationTFFLTVMYLLSIWLG
HHHHHHHHHHHHHHC
10.5225693802
48PhosphorylationLTVMYLLSIWLGNKY
HHHHHHHHHHHCCHH
14.7725693802
55PhosphorylationSIWLGNKYMKNRPAL
HHHHCCHHHCCCCCH
19.8120049867
63PhosphorylationMKNRPALSLRGILTL
HCCCCCHHHHHHHHH
20.3724719451
293AcetylationAANGVMNKKAQ----
HHHCCCCCCCC----
31.2430588479

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 ELOV2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ELOV2_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 ELOV2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ELOV2_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ELOV2_HUMAN

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Related Literatures of Post-Translational Modification

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