Search Results
Overview
| Uniprot ID | Q6PI48 |
|---|---|
| Protein Name | Aspartate--tRNA ligase, mitochondrial |
| Gene Name | DARS2 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 105 | ESAASVKKILCEAPV |
| 382 | GAKYLKRKDIESIRN |
Function
Catalyzes the attachment of aspartate to tRNA(Asp) in a two-step reaction: aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp)
Protein Sequence
10
MYFPSWLSQL
20
YRGLSRPIRR
30
TTQPIWGSLY
40
RSLLQSSQRR
50
IPEFSSFVVR
60
TNTCGELRSS
70
HLGQEVTLCG
80
WIQYRRQNTF
90
LVLRDFDGLV
100
QVIIPQDESA
110
ASVKKILCEA
120
PVESVVQVSG
130
TVISRPAGQE
140
NPKMPTGEIE
150
IKVKTAELLN
160
ACKKLPFEIK
170
NFVKKTEALR
180
LQYRYLDLRS
190
FQMQYNLRLR
200
SQMVMKMREY
210
LCNLHGFVDI
220
ETPTLFKRTP
230
GGAKEFLVPS
240
REPGKFYSLP
250
QSPQQFKQLL
260
MVGGLDRYFQ
270
VARCYRDEGS
280
RPDRQPEFTQ
290
IDIEMSFVDQ
300
TGIQSLIEGL
310
LQYSWPNDKD
320
PVVVPFPTMT
330
FAEVLATYGT
340
DKPDTRFGMK
350
IIDISDVFRN
360
TEIGFLQDAL
370
SKPHGTVKAI
380
CIPEGAKYLK
390
RKDIESIRNF
400
AADHFNQEIL
410
PVFLNANRNW
420
NSPVANFIME
430
SQRLELIRLM
440
ETQEEDVVLL
450
TAGEHNKACS
460
LLGKLRLECA
470
DLLETRGVVL
480
RDPTLFSFLW
490
VVDFPLFLPK
500
EENPRELESA
510
HHPFTAPHPS
520
DIHLLYTEPK
530
KARSQHYDLV
540
LNGNEIGGGS
550
IRIHNAELQR
560
YILATLLKED
570
VKMLSHLLQA
580
LDYGAPPHGG
590
IALGLDRLIC
600
LVTGSPSIRD
610
VIAFPKSFRG
620
HDLMSNTPDS
630
VPPEELKPYH
640
IRVSKPTDSK
AERAH
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Biological Process | GO:0070145 | mitochondrial asparaginyl-tRNA aminoacylation |
| Cellular Component | GO:0005759 | mitochondrial matrix |
| Cellular Component | GO:0031966 | mitochondrial membrane |
| Cellular Component | GO:0005739 | mitochondrion |
| Molecular Function | GO:0004815 | aspartate-tRNA ligase activity |
| Molecular Function | GO:0050560 | aspartate-tRNA(Asn) ligase activity |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0042803 | protein homodimerization activity |
| Molecular Function | GO:0000049 | tRNA binding |
| Biological Process | GO:0006422 | aspartyl-tRNA aminoacylation |
| Biological Process | GO:0043039 | tRNA aminoacylation |
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.