DGAT1_HUMAN - dbPTM
DGAT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DGAT1_HUMAN
UniProt AC O75907
Protein Name Diacylglycerol O-acyltransferase 1
Gene Name DGAT1
Organism Homo sapiens (Human).
Sequence Length 488
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein .
Protein Description Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. In contrast to DGAT2 it is not essential for survival. May be involved in VLDL (very low density lipoprotein) assembly. In liver, plays a role in esterifying exogenous fatty acids to glycerol. Functions as the major acyl-CoA retinol acyltransferase (ARAT) in the skin, where it acts to maintain retinoid homeostasis and prevent retinoid toxicity leading to skin and hair disorders..
Protein Sequence MGDRGSSRRRRTGSRPSSHGGGGPAAAEEEVRDAAAGPDVGAAGDAPAPAPNKDGDAGVGSGHWELRCHRLQDSLFSSDSGFSNYRGILNWCVVMLILSNARLFLENLIKYGILVDPIQVVSLFLKDPYSWPAPCLVIAANVFAVAAFQVEKRLAVGALTEQAGLLLHVANLATILCFPAAVVLLVESITPVGSLLALMAHTILFLKLFSYRDVNSWCRRARAKAASAGKKASSAAAPHTVSYPDNLTYRDLYYFLFAPTLCYELNFPRSPRIRKRFLLRRILEMLFFTQLQVGLIQQWMVPTIQNSMKPFKDMDYSRIIERLLKLAVPNHLIWLIFFYWLFHSCLNAVAELMQFGDREFYRDWWNSESVTYFWQNWNIPVHKWCIRHFYKPMLRRGSSKWMARTGVFLASAFFHEYLVSVPLRMFRLWAFTGMMAQIPLAWFVGRFFQGNYGNAAVWLSLIIGQPIAVLMYVHDYYVLNYEAPAAEA
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
12PhosphorylationGSSRRRRTGSRPSSH
CCCCCCCCCCCCCCC
37.3823401153
14PhosphorylationSRRRRTGSRPSSHGG
CCCCCCCCCCCCCCC
40.1730278072
17PhosphorylationRRTGSRPSSHGGGGP
CCCCCCCCCCCCCCC
33.5830278072
18PhosphorylationRTGSRPSSHGGGGPA
CCCCCCCCCCCCCCC
28.9130278072
61PhosphorylationDGDAGVGSGHWELRC
CCCCCCCCCCEEEEE
25.6923898821
80PhosphorylationDSLFSSDSGFSNYRG
HHHCCCCCCCCCHHH
43.62-
233PhosphorylationASAGKKASSAAAPHT
HHCCCHHHCCCCCCC
29.4123312004
234PhosphorylationSAGKKASSAAAPHTV
HCCCHHHCCCCCCCC
27.1323312004
240PhosphorylationSSAAAPHTVSYPDNL
HCCCCCCCCCCCCCC
15.3023312004
242PhosphorylationAAAPHTVSYPDNLTY
CCCCCCCCCCCCCCH
31.9123312004
243PhosphorylationAAPHTVSYPDNLTYR
CCCCCCCCCCCCCHH
15.4023312004
248PhosphorylationVSYPDNLTYRDLYYF
CCCCCCCCHHHHHHH
23.8223312004
249PhosphorylationSYPDNLTYRDLYYFL
CCCCCCCHHHHHHHH
12.8023312004
316PhosphorylationKPFKDMDYSRIIERL
CCCCCCCHHHHHHHH
8.0022817900
367PhosphorylationFYRDWWNSESVTYFW
HHHHHCCCCCEEEEH
19.9523684312
369PhosphorylationRDWWNSESVTYFWQN
HHHCCCCCEEEEHHC
21.4123684312
371PhosphorylationWWNSESVTYFWQNWN
HCCCCCEEEEHHCCC
23.4523684312
391MalonylationWCIRHFYKPMLRRGS
HHHHHHHHHHHHCCC
24.0226320211
398PhosphorylationKPMLRRGSSKWMART
HHHHHCCCCHHHHHH
27.2524260401

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 DGAT1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DGAT1_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 DGAT1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DGAT1_HUMANDGAT1physical
11672446
GBRA4_HUMANGABRA4physical
21988832

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615863Diarrhea 7 (DIAR7)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DGAT1_HUMAN

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Related Literatures of Post-Translational Modification

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