Search Results
Overview
| Uniprot ID | Q9H6R3 |
|---|---|
| Protein Name | Acyl-CoA synthetase short-chain family member 3, mitochondrial |
| Gene Name | ACSS3 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 128 | IENGKGDKIAIIYDS |
| 162 | KLAGVLVKHGIKKGD |
| 205 | IFGGFASKELSSRID |
| 411 | DPGAALGKQYSLTRF |
| 493 | ILDDNMQKLKARCLG |
| 524 | WKNQEAFKHLYFEKF |
| 594 | VGKEDPLKGHVPLAL |
| 662 | LSAIVNGKPYKITST |
| 79 | DPERFWGKAAEQISW |
| 92 | SWYKPWTKTLENKHS |
| 97 | WTKTLENKHSPSTRW |
Function
Catalyzes the synthesis of acetyl-CoA from short-chain fatty acids (PubMed:28003429). Propionate is the preferred substrate (PubMed:28003429). Can utilize acetate and butyrate with a much lower affinity (By similarity)
Protein Sequence
10
MKPSWLQCRK
20
VTSAGGLGGP
30
LPGSSPARGA
40
GAALRALVVP
50
GPRGGLGGRG
60
CRALSSGSGS
70
EYKTHFAASV
80
TDPERFWGKA
90
AEQISWYKPW
100
TKTLENKHSP
110
STRWFVEGML
120
NICYNAVDRH
130
IENGKGDKIA
140
IIYDSPVTNT
150
KATFTYKEVL
160
EQVSKLAGVL
170
VKHGIKKGDT
180
VVIYMPMIPQ
190
AMYTMLACAR
200
IGAIHSLIFG
210
GFASKELSSR
220
IDHVKPKVVV
230
TASFGIEPGR
240
RVEYVPLVEE
250
ALKIGQHKPD
260
KILIYNRPNM
270
EAVPLAPGRD
280
LDWDEEMAKA
290
QSHDCVPVLS
300
EHPLYILYTS
310
GTTGLPKGVI
320
RPTGGYAVML
330
HWSMSSIYGL
340
QPGEVWWAAS
350
DLGWVVGHSY
360
ICYGPLLHGN
370
TTVLYEGKPV
380
GTPDAGAYFR
390
VLAEHGVAAL
400
FTAPTAIRAI
410
RQQDPGAALG
420
KQYSLTRFKT
430
LFVAGERCDV
440
ETLEWSKNVF
450
RVPVLDHWWQ
460
TETGSPITAS
470
CVGLGNSKTP
480
PPGQAGKSVP
490
GYNVMILDDN
500
MQKLKARCLG
510
NIVVKLPLPP
520
GAFSGLWKNQ
530
EAFKHLYFEK
540
FPGYYDTMDA
550
GYMDEEGYLY
560
VMSRVDDVIN
570
VAGHRISAGA
580
IEESILSHGT
590
VADCAVVGKE
600
DPLKGHVPLA
610
LCVLRKDINA
620
TEEQVLEEIV
630
KHVRQNIGPV
640
AAFRNAVFVK
650
QLPKTRSGKI
660
PRSALSAIVN
670
GKPYKITSTI
680
EDPSIFGHVE
EMLKQA
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005759 | mitochondrial matrix |
| Cellular Component | GO:0005739 | mitochondrion |
| Molecular Function | GO:0003987 | acetate-CoA ligase activity |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0031956 | medium-chain fatty acid-CoA ligase activity |
| Molecular Function | GO:0050218 | propionate-CoA ligase activity |
| Biological Process | GO:0046951 | ketone body biosynthetic process |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.