ARIH2
entrez
10425
canonical
uniprot
O95376
canonical
ensembl
ENSG00000177479
resolver
ensp
ENSP00000348769
resolver
ensp
ENSP00000403222
resolver
ensp
ENSP00000577566
resolver
ensp
ENSP00000577567
resolver
ensp
ENSP00000577568
resolver
ensp
ENSP00000577569
resolver
ensp
ENSP00000577570
resolver
ensp
ENSP00000577572
resolver
ensp
ENSP00000577574
resolver
ensp
ENSP00000577575
resolver
ensp
ENSP00000577577
resolver
ensp
ENSP00000577578
resolver
ensp
ENSP00000577582
resolver
ensp
ENSP00000577584
resolver
ensp
ENSP00000583637
resolver
ensp
ENSP00000583639
resolver
ensp
ENSP00000583641
resolver
ensp
ENSP00000583642
resolver
ensp
ENSP00000583643
resolver
ensp
ENSP00000583644
resolver
ensp
ENSP00000583645
resolver
ensp
ENSP00000583646
resolver
ensp
ENSP00000583647
resolver
ensp
ENSP00000583648
resolver
ensp
ENSP00000642276
resolver
ensp
ENSP00000642278
resolver
ensp
ENSP00000642283
resolver
ensp
ENSP00000642284
resolver
ensp
ENSP00000642285
resolver
ensp
ENSP00000642287
resolver
ensp
ENSP00000642289
resolver
ensp
ENSP00000642290
resolver
ensp
ENSP00000642291
resolver
ensp
ENSP00000642293
resolver
ensp
ENSP00000642294
resolver
ensp
ENSP00000676254
resolver
ensp
ENSP00000693924
resolver
ensp
ENSP00000780924
resolver
ensp
ENSP00000780927
resolver
ensp
ENSP00000782639
resolver
enst
ENST00000356401
resolver
enst
ENST00000449376
resolver
enst
ENST00000907507
resolver
enst
ENST00000907508
resolver
enst
ENST00000907510
resolver
enst
ENST00000907511
resolver
enst
ENST00000907513
resolver
enst
ENST00000907515
resolver
enst
ENST00000907516
resolver
enst
ENST00000907518
resolver
enst
ENST00000907519
resolver
enst
ENST00000907523
resolver
enst
ENST00000907525
resolver
enst
ENST00000913578
resolver
enst
ENST00000913580
resolver
enst
ENST00000913582
resolver
enst
ENST00000913583
resolver
enst
ENST00000913584
resolver
enst
ENST00000913585
resolver
enst
ENST00000913586
resolver
enst
ENST00000913587
resolver
enst
ENST00000913589
resolver
enst
ENST00000972217
resolver
enst
ENST00000972219
resolver
enst
ENST00000972224
resolver
enst
ENST00000972225
resolver
enst
ENST00000972228
resolver
enst
ENST00000972230
resolver
enst
ENST00000972231
resolver
enst
ENST00000972232
resolver
enst
ENST00000972234
resolver
enst
ENST00000972235
resolver
genesymbol
ARIH2
resolver
genesymbol_syn
ARI2
resolver
genesymbol_syn
TRIAD1
resolver
hgnc
HGNC:690
resolver
uniprot
A0A024R2S5
resolver
uniprot
Q53ET9
resolver
uniprot
Q6IBL8
resolver
uniprot
Q9HBZ6
resolver
uniprot
Q9UEM9
resolver
uniprot_entry
ARI2_HUMAN
resolver
uniprot_entry
Q53ET9_HUMAN
resolver
uniprot_entry
Q6IBL8_HUMAN
resolver
uniprot_sec
A0A024R2S5
resolver
uniprot_sec
Q9HBZ6
resolver
uniprot_sec
Q9UEM9
resolver
activity_regulation
ACTIVITY REGULATION: Autoinhibited by the ariadne domain, which masks the second RING-type zinc finger that contains the active site and inhibits the E3 activity (PubMed:34518685). Inhibition is relieved upon binding to neddylated cullin-RING ubiquitin ligase complexes, which activate the E3 ligase activity of ARIH1 (PubMed:24076655, PubMed:33268465, PubMed:34518685). {ECO:0000269|PubMed:24076655, ECO:0000269|PubMed:33268465, ECO:0000269|PubMed:34518685}.
uniprot
proteins
amino_acid_sequence
MSVDMNSQGSDSNEEDYDPNCEEEEEEEEDDPGDIEDYYVGVASDVEQQGADAFDPEEYQFTCLTYKESEGALNEHMTSLASVLKVSHSVAKLILVNFHWQVSEILDRYKSNSAQLLVEARVQPNPSKHVPTSHPPHHCAVCMQFVRKENLLSLACQHQFCRSCWEQHCSVLVKDGVGVGVSCMAQDCPLRTPEDFVFPLLPNEELREKYRRYLFRDYVESHYQLQLCPGADCPMVIRVQEPRARRVQCNRCNEVFCFKCRQMYHAPTDCATIRKWLTKCADDSETANYISAHTKDCPKCNICIEKNGGCNHMQCSKCKHDFCWMCLGDWKTHGSEYYECSRYKENPDIVNQSQQAQAREALKKYLFYFERWENHNKSLQLEAQTYQRIHEKIQERVMNNLGTWIDWQYLQNAAKLLAKCRYTLQYTYPYAYYMESGPRKKLFEYQQAQLEAEIENLSWKVERADSYDRGDLENQMHIAEQRRRTLLKDFHDT
uniprot
proteins
ec_number
2.3.2.31
uniprot
proteins
function
FUNCTION: E3 ubiquitin-protein ligase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 UBE2L3 (PubMed:16118314, PubMed:17646546, PubMed:19340006, PubMed:24076655, PubMed:33268465, PubMed:34518685, PubMed:38418882). Acts as an atypical E3 ubiquitin-protein ligase by working together with cullin-5-RING ubiquitin ligase complex (ECS complex, also named CRL5 complex) and initiating ubiquitination of ECS substrates: associates with ECS complex and specifically mediates addition of the first ubiquitin on ECS targets (PubMed:33268465, PubMed:34518685, PubMed:38418882). The initial ubiquitin is then elongated (PubMed:33268465). E3 ubiquitin-protein ligase activity is activated upon binding to neddylated form of the cullin-5 (CUL5) component of the ECS complex (PubMed:24076655). Together with the ECS(ASB9) complex, catalyzes ubiquitination of CKB (PubMed:33268465). Promotes ubiquitination of DCUN1D1 (PubMed:30587576). Mediates 'Lys-6', 'Lys-48'- and 'Lys-63'-linked polyubiquitination (PubMed:16118314, PubMed:17646546, PubMed:19340006). May play a role in myelopoiesis (PubMed:19340006). {ECO:0000269|PubMed:16118314, ECO:0000269|PubMed:17646546, ECO:0000269|PubMed:19340006, ECO:0000269|PubMed:24076655, ECO:0000269|PubMed:30587576, ECO:0000269|PubMed:33268465, ECO:0000269|PubMed:34518685, ECO:0000269|PubMed:38418882}.; FUNCTION: (Microbial infection) Following infection by HIV-1 virus, acts together with a cullin-5-RING E3 ubiquitin-protein ligase complex (ECS complex) hijacked by the HIV-1 Vif protein, to catalyze ubiquitination and degradation of APOBEC3F and APOBEC3G. {ECO:0000269|PubMed:31253590, ECO:0000269|PubMed:36754086}.
uniprot
proteins
mass_dalton
57819
uniprot
proteins
mutagenesis
MUTAGEN 38; /note="Y->A: Impaired ability to ubiquitinate proteins."; /evidence="ECO:0000269|PubMed:34518685"; MUTAGEN 39; /note="Y->A: Impaired ability to ubiquitinate proteins."; /evidence="ECO:0000269|PubMed:34518685"; MUTAGEN 84..86; /note="LKV->AKA: Reduced interaction with neddylated CUL5; when associated with A-100."; /evidence="ECO:0000269|PubMed:24076655"; MUTAGEN 100; /note="W->A: Reduced interaction with neddylated CUL5; when associated with 84-A--A-86."; /evidence="ECO:0000269|PubMed:24076655"; MUTAGEN 158; /note="H->A: Loss of effect in myelopoiesis. Abolishes interaction with UBE2L3."; /evidence="ECO:0000269|PubMed:16118314, ECO:0000269|PubMed:24076655"; MUTAGEN 161; /note="C->A: Loss of effect in myelopoiesis."; /evidence="ECO:0000269|PubMed:16118314"; MUTAGEN 257; /note="C->A: Does not affect interaction with UBE2L3."; /evidence="ECO:0000269|PubMed:24076655"; MUTAGEN 300; /note="C->A: Does not affect interaction with UBE2L3."; /evidence="ECO:0000269|PubMed:24076655"; MUTAGEN 310; /note="C->A: Abolishes E3 ubiquitin-protein ligase activity."; /evidence="ECO:0000269|PubMed:24076655, ECO:0000269|PubMed:31253590"; MUTAGEN 381..382; /note="LE->AA: Abolishes autoinhibition; when associated with A-455."; /evidence="ECO:0000269|PubMed:34518685"; MUTAGEN 455; /note="E->A: Abolishes autoinhibition; when associated with 381-A-A-382."; /evidence="ECO:0000269|PubMed:34518685
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:16118314, ECO:0000269|PubMed:17646546, ECO:0000269|PubMed:19340006, ECO:0000269|PubMed:30587576, ECO:0000269|PubMed:33268465, ECO:0000269|PubMed:34518685}.
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated. Ubiquitination promotes proteasomal degradation. {ECO:0000269|PubMed:16118314}.
uniprot
proteins
protein_family
Ariadne subfamily
uniprot
proteins
protein_family
RBR family
uniprot
proteins
pubmed
10422847
uniprot
proteins
pubmed
10880484
uniprot
proteins
pubmed
10931946
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16118314
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
17646546
uniprot
proteins
pubmed
19340006
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24076655
uniprot
proteins
pubmed
30587576
uniprot
proteins
pubmed
31253590
uniprot
proteins
pubmed
33268465
uniprot
proteins
pubmed
34518685
uniprot
proteins
pubmed
36754086
uniprot
proteins
pubmed
38418882
uniprot
proteins
sequence_length
493
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16118314}. Cytoplasm {ECO:0000269|PubMed:19340006}.
uniprot
proteins