Overview
| Uniprot ID | Q9Y4X5 |
|---|
| Protein Name | E3 ubiquitin-protein ligase ARIH1 |
|---|
| Gene Name | ARIH1 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 168 |
CHVINPSKKSRTRQM |
Function
E3 ubiquitin-protein ligase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 UBE2L3 (PubMed:15236971, PubMed:21532592, PubMed:23707686, PubMed:24076655, PubMed:27565346). Acts as an atypical E3 ubiquitin-protein ligase by working together with cullin-RING ubiquitin ligase (CRL) complexes and initiating ubiquitination of CRL substrates: associates with CRL complexes and specifically mediates addition of the first ubiquitin on CRLs targets (PubMed:27565346). The initial ubiquitin is then elongated by CDC34/UBE2R1 and UBE2R2 (PubMed:27565346). E3 ubiquitin-protein ligase activity is activated upon binding to neddylated cullin-RING ubiquitin ligase complexes (PubMed:24076655, PubMed:27565346). Plays a role in protein translation in response to DNA damage by mediating ubiquitination of EIF4E2, the consequences of EIF4E2 ubiquitination are however unclear (PubMed:25624349). According to a report, EIF4E2 ubiquitination leads to promote EIF4E2 cap-binding and protein translation arrest (PubMed:25624349). According to another report EIF4E2 ubiquitination leads to its subsequent degradation (PubMed:14623119). Acts as the ligase involved in ISGylation of EIF4E2 (PubMed:17289916). In vitro, controls the degradation of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex member SUN2 and may therefore have a role in the formation and localization of the LINC complex, and as a consequence, nuclear subcellular localization and nuclear morphology (PubMed:29689197)
Protein Sequence
10
MDSDEGYNYE
20
FDEDEECSEE
30
DSGAEEEEDE
40
DDDEPDDDTL
50
DLGEVELVEP
60
GLGVGGERDG
70
LLCGETGGGG
80
GSALGPGGGG
90
GGGGGGGGGG
100
PGHEQEEDYR
110
YEVLTAEQIL
120
QHMVECIREV
130
NEVIQNPATI
140
TRILLSHFNW
150
DKEKLMERYF
160
DGNLEKLFAE
170
CHVINPSKKS
180
RTRQMNTRSS
190
AQDMPCQICY
200
LNYPNSYFTG
210
LECGHKFCMQ
220
CWSEYLTTKI
230
MEEGMGQTIS
240
CPAHGCDILV
250
DDNTVMRLIT
260
DSKVKLKYQH
270
LITNSFVECN
280
RLLKWCPAPD
290
CHHVVKVQYP
300
DAKPVRCKCG
310
RQFCFNCGEN
320
WHDPVKCKWL
330
KKWIKKCDDD
340
SETSNWIAAN
350
TKECPKCHVT
360
IEKDGGCNHM
370
VCRNQNCKAE
380
FCWVCLGPWE
390
PHGSAWYNCN
400
RYNEDDAKAA
410
RDAQERSRAA
420
LQRYLFYCNR
430
YMNHMQSLRF
440
EHKLYAQVKQ
450
KMEEMQQHNM
460
SWIEVQFLKK
470
AVDVLCQCRA
480
TLMYTYVFAF
490
YLKKNNQSII
500
FENNQADLEN
510
ATEVLSGYLE
520
RDISQDSLQD
530
IKQKVQDKYR
540
YCESRRRVLL
550
QHVHEGYEKD
LWEYIED
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0015030 |
Cajal body |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0097413 |
Lewy body |
| Cellular Component |
GO:0016604 |
nuclear body |
| Cellular Component |
GO:0005654 |
nucleoplasm |
| Cellular Component |
GO:0005634 |
nucleus |
| Cellular Component |
GO:0000151 |
ubiquitin ligase complex |
| Molecular Function |
GO:0031624 |
ubiquitin conjugating enzyme binding |
| Molecular Function |
GO:0061630 |
ubiquitin protein ligase activity |
| Molecular Function |
GO:0031625 |
ubiquitin protein ligase binding |
| Molecular Function |
GO:0019787 |
ubiquitin-like protein transferase activity |
| Molecular Function |
GO:0004842 |
ubiquitin-protein transferase activity |
| Molecular Function |
GO:0008270 |
zinc ion binding |
| Biological Process |
GO:0039585 |
PKR/eIFalpha signaling |
| Biological Process |
GO:0016567 |
protein ubiquitination |
| Biological Process |
GO:0006511 |
ubiquitin-dependent protein catabolic process |
Reference
[1] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.