Search Results
Overview
| Uniprot ID | Q9UDR5 |
|---|---|
| Protein Name | Alpha-aminoadipic semialdehyde synthase, mitochondrial |
| Gene Name | AASS |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 104 | EEKLMSRKTYAFFSH |
| 259 | SQTGDLRKVYGTVLS |
| 274 | RHHHLVRKTDAVYDP |
| 286 | YDPAEYDKHPERYIS |
| 458 | SNGTLPDKYKYIQTL |
| 460 | GTLPDKYKYIQTLRE |
| 48 | PLAPKHIKGITNLGY |
| 522 | NQIEQLGKKYNINPV |
| 535 | PVSMDICKQEEKLGF |
| 539 | DICKQEEKLGFLVAK |
Function
Bifunctional enzyme that catalyzes the first two steps in lysine degradation
Protein Sequence
10
MLQVHRTGLG
20
RLGVSLSKGL
30
HHKAVLAVRR
40
EDVNAWERRA
50
PLAPKHIKGI
60
TNLGYKVLIQ
70
PSNRRAIHDK
80
DYVKAGGILQ
90
EDISEACLIL
100
GVKRPPEEKL
110
MSRKTYAFFS
120
HTIKAQEANM
130
GLLDEILKQE
140
IRLIDYEKMV
150
DHRGVRVVAF
160
GQWAGVAGMI
170
NILHGMGLRL
180
LALGHHTPFM
190
HIGMAHNYRN
200
SSQAVQAVRD
210
AGYEISLGLM
220
PKSIGPLTFV
230
FTGTGNVSKG
240
AQAIFNELPC
250
EYVEPHELKE
260
VSQTGDLRKV
270
YGTVLSRHHH
280
LVRKTDAVYD
290
PAEYDKHPER
300
YISRFNTDIA
310
PYTTCLINGI
320
YWEQNTPRLL
330
TRQDAQSLLA
340
PGKFSPAGVE
350
GCPALPHKLV
360
AICDISADTG
370
GSIEFMTECT
380
TIEHPFCMYD
390
ADQHIIHDSV
400
EGSGILMCSI
410
DNLPAQLPIE
420
ATECFGDMLY
430
PYVEEMILSD
440
ATQPLESQNF
450
SPVVRDAVIT
460
SNGTLPDKYK
470
YIQTLRESRE
480
RAQSLSMGTR
490
RKVLVLGSGY
500
ISEPVLEYLS
510
RDGNIEITVG
520
SDMKNQIEQL
530
GKKYNINPVS
540
MDICKQEEKL
550
GFLVAKQDLV
560
ISLLPYVLHP
570
LVAKACITNK
580
VNMVTASYIT
590
PALKELEKSV
600
EDAGITIIGE
610
LGLDPGLDHM
620
LAMETIDKAK
630
EVGATIESYI
640
SYCGGLPAPE
650
HSNNPLRYKF
660
SWSPVGVLMN
670
VMQSATYLLD
680
GKVVNVAGGI
690
SFLDAVTSMD
700
FFPGLNLEGY
710
PNRDSTKYAE
720
IYGISSAHTL
730
LRGTLRYKGY
740
MKALNGFVKL
750
GLINREALPA
760
FRPEANPLTW
770
KQLLCDLVGI
780
SPSSEHDVLK
790
EAVLKKLGGD
800
NTQLEAAEWL
810
GLLGDEQVPQ
820
AESILDALSK
830
HLVMKLSYGP
840
EEKDMIVMRD
850
SFGIRHPSGH
860
LEHKTIDLVA
870
YGDINGFSAM
880
AKTVGLPTAM
890
AAKMLLDGEI
900
GAKGLMGPFS
910
KEIYGPILER
920
IKAEGIIYTT
QSTIKP
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005759 | mitochondrial matrix |
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0042393 | histone binding |
| Molecular Function | GO:0047131 | saccharopine dehydrogenase (NAD+, L-glutamate-forming) activity |
| Molecular Function | GO:0004754 | saccharopine dehydrogenase (NAD+, L-lysine-forming) activity |
| Molecular Function | GO:0047130 | saccharopine dehydrogenase (NADP+, L-lysine-forming) activity |
| Molecular Function | GO:0004753 | saccharopine dehydrogenase activity |
| Molecular Function | GO:0003714 | transcription corepressor activity |
| Biological Process | GO:0019878 | L-lysine biosynthetic process via aminoadipic acid |
| Biological Process | GO:0033512 | L-lysine catabolic process to acetyl-CoA via L-saccharopine |
| Biological Process | GO:0006554 | lysine catabolic process |
| Biological Process | GO:0000122 | negative regulation of transcription by RNA polymerase II |
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] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.