| UniProt ID | AACS_HUMAN | |
|---|---|---|
| UniProt AC | Q86V21 | |
| Protein Name | Acetoacetyl-CoA synthetase | |
| Gene Name | AACS | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 672 | |
| Subcellular Localization | Cytoplasm, cytosol. | |
| Protein Description | Activates acetoacetate to acetoacetyl-CoA. May be involved in utilizing ketone body for the fatty acid-synthesis during adipose tissue development (By similarity).. | |
| Protein Sequence | MSKEERPGREEILECQVMWEPDSKKNTQMDRFRAAVGAACGLALESYDDLYHWSVESYSDFWAEFWKFSGIVFSRVYDEVVDTSKGIADVPEWFKGSRLNYAENLLRHKENDRVALYIAREGKEEIVKVTFEELRQEVALFAAAMRKMGVKKGDRVVGYLPNSEHAVEAMLAAASIGAIWSSTSPDFGVNGVLDRFSQIQPKLIFSVEAVVYNGKEHNHMEKLQQVVKGLPDLKKVVVIPYVSSRENIDLSKIPNSVFLDDFLATGTSEQAPQLEFEQLPFSHPLFIMFSSGTTGAPKCMVHSAGGTLIQHLKEHLLHGNMTSSDILLCYTTVGWMMWNWMVSLLATGAAMVLYDGSPLVPTPNVLWDLVDRIGITVLVTGAKWLSVLEEKAMKPVETHSLQMLHTILSTGSPLKAQSYEYVYRCIKSSILLGSISGGTDIISCFMGHNFSLPVYKGEIQARNLGMAVEAWNEEGKAVWGESGELVCTKPIPCQPTHFWNDENGNKYRKAYFSKFPGIWAHGDYCRINPKTGGIVMLGRSDGTLNPNGVRFGSSEIYNIVESFEEVEDSLCVPQYNKYREERVILFLKMASGHAFQPDLVKRIRDAIRMGLSARHVPSLILETKGIPYTLNGKKVEVAVKQIIAGKAVEQGGAFSNPETLDLYRDIPELQGF | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 7 (in isoform 3) | Phosphorylation | - | 49.85 | 25159151 | |
| 10 (in isoform 3) | Phosphorylation | - | 56.13 | 25159151 | |
| 46 | Phosphorylation | ACGLALESYDDLYHW HHHHHHHCCCCCCCC | 34.41 | 24043423 | |
| 47 | Phosphorylation | CGLALESYDDLYHWS HHHHHHCCCCCCCCC | 12.23 | 24043423 | |
| 51 | Phosphorylation | LESYDDLYHWSVESY HHCCCCCCCCCCCCC | 14.29 | 24043423 | |
| 54 | Phosphorylation | YDDLYHWSVESYSDF CCCCCCCCCCCCHHH | 11.60 | 24043423 | |
| 57 | Phosphorylation | LYHWSVESYSDFWAE CCCCCCCCCHHHHHH | 27.99 | 24043423 | |
| 58 | Phosphorylation | YHWSVESYSDFWAEF CCCCCCCCHHHHHHH | 9.96 | 24043423 | |
| 59 | Phosphorylation | HWSVESYSDFWAEFW CCCCCCCHHHHHHHH | 35.29 | 24043423 | |
| 85 | Ubiquitination | DEVVDTSKGIADVPE HHHHCCCCCCCCCCH | 57.33 | - | |
| 95 | Ubiquitination | ADVPEWFKGSRLNYA CCCCHHHHCCCCHHH | 57.98 | 21890473 | |
| 95 (in isoform 2) | Ubiquitination | - | 57.98 | 21890473 | |
| 95 (in isoform 1) | Ubiquitination | - | 57.98 | 21890473 | |
| 97 | Phosphorylation | VPEWFKGSRLNYAEN CCHHHHCCCCHHHHH | 33.90 | 28857561 | |
| 212 | Phosphorylation | FSVEAVVYNGKEHNH EEEEEEEECCCCCCH | 16.17 | 22817900 | |
| 222 | Ubiquitination | KEHNHMEKLQQVVKG CCCCHHHHHHHHHHC | 43.98 | - | |
| 228 | Ubiquitination | EKLQQVVKGLPDLKK HHHHHHHHCCCCCCE | 56.74 | - | |
| 241 | Phosphorylation | KKVVVIPYVSSRENI CEEEEEEECCCCCCC | 11.22 | 70959849 | |
| 243 | Phosphorylation | VVVIPYVSSRENIDL EEEEEECCCCCCCCH | 20.17 | 70959855 | |
| 244 | Phosphorylation | VVIPYVSSRENIDLS EEEEECCCCCCCCHH | 33.30 | 70959861 | |
| 406 | Phosphorylation | HSLQMLHTILSTGSP HHHHHHHHHHHCCCC | 21.47 | 24043423 | |
| 409 | Phosphorylation | QMLHTILSTGSPLKA HHHHHHHHCCCCCCC | 27.20 | 24114839 | |
| 410 | Phosphorylation | MLHTILSTGSPLKAQ HHHHHHHCCCCCCCC | 37.93 | 24043423 | |
| 412 | Phosphorylation | HTILSTGSPLKAQSY HHHHHCCCCCCCCCH | 27.44 | 72262553 | |
| 418 | Phosphorylation | GSPLKAQSYEYVYRC CCCCCCCCHHHHHHH | 25.45 | 24043423 | |
| 419 | Phosphorylation | SPLKAQSYEYVYRCI CCCCCCCHHHHHHHH | 10.13 | 24043423 | |
| 421 | Phosphorylation | LKAQSYEYVYRCIKS CCCCCHHHHHHHHHH | 8.44 | 24043423 | |
| 423 | Phosphorylation | AQSYEYVYRCIKSSI CCCHHHHHHHHHHHH | 10.00 | 24043423 | |
| 489 | Acetylation | SGELVCTKPIPCQPT CCCEEECCCCCCCCC | 35.50 | 26051181 | |
| 489 | Ubiquitination | SGELVCTKPIPCQPT CCCEEECCCCCCCCC | 35.50 | - | |
| 506 | Ubiquitination | WNDENGNKYRKAYFS EECCCCCEEEHHHHH | 48.07 | - | |
| 524 | Phosphorylation | GIWAHGDYCRINPKT CCEECCCCEEECCCC | 6.55 | 53509 | |
| 530 | Ubiquitination | DYCRINPKTGGIVML CCEEECCCCCCEEEE | 56.14 | - | |
| 531 | Phosphorylation | YCRINPKTGGIVMLG CEEECCCCCCEEEEE | 41.73 | 21406692 | |
| 536 | Sulfoxidation | PKTGGIVMLGRSDGT CCCCCEEEEECCCCC | 2.87 | 21406390 | |
| 540 | Phosphorylation | GIVMLGRSDGTLNPN CEEEEECCCCCCCCC | 38.30 | 28857561 | |
| 543 | Phosphorylation | MLGRSDGTLNPNGVR EEECCCCCCCCCCEE | 28.49 | 28188228 | |
| 578 | Phosphorylation | CVPQYNKYREERVIL CCCCCCCCCHHHHHE | 21.44 | 11197149 | |
| 618 | Phosphorylation | LSARHVPSLILETKG CCCCCCCCEEEEECC | 27.27 | 30108239 | |
| 624 | Ubiquitination | PSLILETKGIPYTLN CCEEEEECCCCEEEC | 45.53 | - | |
| 634 | Malonylation | PYTLNGKKVEVAVKQ CEEECCEEEEEEEEH | 45.05 | 26320211 | |
| 640 | Ubiquitination | KKVEVAVKQIIAGKA EEEEEEEEHHHCCCH | 26.49 | - | |
| 646 | Acetylation | VKQIIAGKAVEQGGA EEHHHCCCHHHCCCC | 39.99 | 23236377 | |
| 646 | Ubiquitination | VKQIIAGKAVEQGGA EEHHHCCCHHHCCCC | 39.99 | - |
| 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 AACS_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AACS_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 AACS_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| CKLF5_HUMAN | CMTM5 | physical | 25416956 | |
| STAT6_HUMAN | STAT6 | physical | 26344197 | |
| UN13D_HUMAN | UNC13D | physical | 26344197 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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