FADS1_MOUSE - dbPTM
FADS1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FADS1_MOUSE
UniProt AC Q920L1
Protein Name Fatty acid desaturase 1
Gene Name Fads1
Organism Mus musculus (Mouse).
Sequence Length 447
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein . Mitochondrion .
Protein Description Component of a lipid metabolic pathway that catalyzes biosynthesis of highly unsaturated fatty acids (HUFA) from precursor essential polyunsaturated fatty acids (PUFA) linoleic acid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3). Catalyzes the desaturation of dihomo-gamma-linoleic acid (DHGLA) (20:3n-6) and eicosatetraenoic acid (20:4n-3) to generate arachidonic acid (AA) (20:4n-6) and eicosapentaenoic acid (EPA)(20:5n-3) respectively (By similarity)..
Protein Sequence MAPDPVPTPGPASAQLRQTRYFTWEEVAQRSGREKERWLVIDRKVYNISDFSRRHPGGSRVISHYAGQDATDPFVAFHINKGLVRKYMNSLLIGELAPEQPSFEPTKNKALTDEFRELRATVERMGLMKANHLFFLVYLLHILLLDVAAWLTLWIFGTSLVPFILCAVLLSTVQAQAGWLQHDFGHLSVFGTSTWNHLLHHFVIGHLKGAPASWWNHMHFQHHAKPNCFRKDPDINMHPLFFALGKVLPVELGREKKKHMPYNHQHKYFFLIGPPALLPLYFQWYIFYFVVQRKKWVDLAWMLSFYARIFFTYMPLLGLKGFLGLFFIVRFLESNWFVWVTQMNHIPMHIDHDRNVDWVSTQLQATCNVHQSAFNNWFSGHLNFQIEHHLFPTMPRHNYHKVAPLVQSLCAKYGIKYESKPLLTAFADIVYSLKESGQLWLDAYLHQ
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
1Acetylation-------MAPDPVPT
-------CCCCCCCC
12.62-
8PhosphorylationMAPDPVPTPGPASAQ
CCCCCCCCCCCCCHH
40.9029514104
13PhosphorylationVPTPGPASAQLRQTR
CCCCCCCCHHHCHHE
21.4930352176
44UbiquitinationRWLVIDRKVYNISDF
EEEEEEEEEECHHHH
45.3722790023
81UbiquitinationFVAFHINKGLVRKYM
EEEEEECHHHHHHHH
53.6822790023
86UbiquitinationINKGLVRKYMNSLLI
ECHHHHHHHHHHHHH
41.1822790023
107UbiquitinationQPSFEPTKNKALTDE
CCCCCCCCCCCCCHH
68.1422790023
109UbiquitinationSFEPTKNKALTDEFR
CCCCCCCCCCCHHHH
46.4522790023
112PhosphorylationPTKNKALTDEFRELR
CCCCCCCCHHHHHHH
38.0420469934
231UbiquitinationAKPNCFRKDPDINMH
CCCCCCCCCCCCCCC
54.0522790023
246UbiquitinationPLFFALGKVLPVELG
HHHHHHCCCCCHHHC
41.2622790023
262PhosphorylationEKKKHMPYNHQHKYF
CHHCCCCCCCCCCEE
20.0825159016
292UbiquitinationYIFYFVVQRKKWVDL
HHHHHHHHCCCHHHH
46.2927667366
312PhosphorylationFYARIFFTYMPLLGL
HHHHHHHHHHHHHCH
14.2529899451
313PhosphorylationYARIFFTYMPLLGLK
HHHHHHHHHHHHCHH
7.5029899451
401UbiquitinationMPRHNYHKVAPLVQS
CCCCCHHHHHHHHHH
29.7222790023
412UbiquitinationLVQSLCAKYGIKYES
HHHHHHHHHCCCCCC
42.9122790023
416UbiquitinationLCAKYGIKYESKPLL
HHHHHCCCCCCCCHH
38.3127667366

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 FADS1_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FADS1_MOUSE !!

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 FADS1_MOUSE !!

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

Oops, there are no PPI records of FADS1_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FADS1_MOUSE

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Related Literatures of Post-Translational Modification

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