UniProt ID | ACBG2_HUMAN | |
---|---|---|
UniProt AC | Q5FVE4 | |
Protein Name | Long-chain-fatty-acid--CoA ligase ACSBG2 | |
Gene Name | ACSBG2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 666 | |
Subcellular Localization |
Cytoplasm. Membrane Peripheral membrane protein. |
|
Protein Description | Mediates activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Able to activate long-chain fatty acids. Also able to activate very long-chain fatty acids; however, the relevance of such activity is unclear in vivo. Has increased ability to activate oleic and linoleic acid. May play a role in spermatogenesis.. | |
Protein Sequence | MTGTPKTQEGAKDLEVDMNKTEVTPRLWTTCRDGEVLLRLSKHGPGHETPMTIPEFFRESVNRFGTYPALASKNGKKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVENDQQLQKILSIPQSSLEPLKAIIQYRLPMKKNNNLYSWDDFMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALKGTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWARNIGFKVNSKKMLGKYNTPVSYRMAKTLVFSKVKTSLGLDHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQNKDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETLVKKKIPIISNAMLVGDKLKFLSMLLTLKCEMNQMSGEPLDKLNFEAINFCRGLGSQASTVTEIVKQQDPLVYKAIQQGINAVNQEAMNNAQRIEKWVILEKDFSIYGGELGPMMKLKRHFVAQKYKKQIDHMYH | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
66 | Phosphorylation | ESVNRFGTYPALASK HHHHHHCCHHHHHCC | 24.50 | 24409183 | |
86 | Phosphorylation | EILNFNQYYEACRKA EEECHHHHHHHHHHH | 12.36 | 22144111 | |
87 | Phosphorylation | ILNFNQYYEACRKAA EECHHHHHHHHHHHH | 6.31 | 22144111 | |
96 | Phosphorylation | ACRKAAKSLIKLGLE HHHHHHHHHHHHCHH | 30.51 | 24719451 | |
169 | Phosphorylation | QQLQKILSIPQSSLE HHHHHHHCCCHHHCH | 35.38 | 24719451 | |
184 | Phosphorylation | PLKAIIQYRLPMKKN HHHHHHHCCCCCCCC | 12.05 | 24719451 | |
266 | Phosphorylation | KLTDKHETVVSYLPL CCCCCCHHHHHHCCH | 26.40 | 46158025 | |
308 | Phosphorylation | LKGTLVSTLKEVKPT HCCCHHHHHCHHCCE | 34.08 | 23403867 | |
358 | Phosphorylation | NIGFKVNSKKMLGKY HCCEEECCCHHHCCC | 36.32 | 23898821 | |
370 | Phosphorylation | GKYNTPVSYRMAKTL CCCCCCCHHHHHHHH | 14.28 | 30631047 | |
380 | Phosphorylation | MAKTLVFSKVKTSLG HHHHHHHHHHCCCCC | 29.12 | 30631047 | |
541 | Phosphorylation | KKKIPIISNAMLVGD CCCCCEECCCEECCH | 21.18 | 23532336 | |
587 | Phosphorylation | NFCRGLGSQASTVTE HHHCCCCCCHHHHHH | 27.84 | 25693802 | |
590 | Phosphorylation | RGLGSQASTVTEIVK CCCCCCHHHHHHHHH | 18.77 | 25693802 | |
591 | Phosphorylation | GLGSQASTVTEIVKQ CCCCCHHHHHHHHHC | 34.17 | 25693802 | |
593 | Phosphorylation | GSQASTVTEIVKQQD CCCHHHHHHHHHCCC | 21.78 | 25693802 | |
636 | Phosphorylation | VILEKDFSIYGGELG EEEECCCEEECCCCH | 25.65 | 30622161 | |
657 | Phosphorylation | RHFVAQKYKKQIDHM HHHHHHHHHHHHHHC | 16.02 | 7479569 | |
665 | Phosphorylation | KKQIDHMYH------ HHHHHHCCC------ | 10.85 | 7479579 |
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 ACBG2_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ACBG2_HUMAN !! |
* 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 ACBG2_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
ZZEF1_HUMAN | ZZEF1 | physical | 28514442 | |
CMS1_HUMAN | CMSS1 | physical | 28514442 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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