Uniprot ID:Q9Y4X5	Protein name: E3 ubiquitin-protein ligase ARIH1	Gene : ARIH1 ARI MOP6 UBCH7BP HUSSY-27
Protein Family:"RBR family, Ariadne subfamily"	Squence Length : 557

Sequnce	>Q9Y4X5 558 MDSDEGYNYEFDEDEECSEEDSGAEEEEDEDDDEPDDDTLDLGEVELVEPGLGVGGERDGLLCGETGGGGGSALGPGGGGGGGGGGGGGGPGHEQEEDYRYEVLTAEQILQHMVECIREVNEVIQNPATITRILLSHFNWDKEKLMERYFDGNLEKLFAECHVINPSKKSRTRQMNTRSSAQDMPCQICYLNYPNSYFTGLECGHKFCMQCWSEYLTTKIMEEGMGQTISCPAHGCDILVDDNTVMRLITDSKVKLKYQHLITNSFVECNRLLKWCPAPDCHHVVKVQYPDAKPVRCKCGRQFCFNCGENWHDPVKCKWLKKWIKKCDDDSETSNWIAANTKECPKCHVTIEKDGGCNHMVCRNQNCKAEFCWVCLGPWEPHGSAWYNCNRYNEDDAKAARDAQERSRAALQRYLFYCNRYMNHMQSLRFEHKLYAQVKQKMEEMQQHNMSWIEVQFLKKAVDVLCQCRATLMYTYVFAFYLKKNNQSIIFENNQADLENATEVLSGYLERDISQDSLQDIKQKVQDKYRYCESRRRVLLQHVHEGYEKDLWEYIED
RING-type domains repeats	ZN_FING 186 236 RING-type 1 ZN_FING 256 317 IBR-type ZN_FING 344 375 RING-type 2
Domin repeated regions	186 - 236 CQICYLNYPNSYFTGLECGHKFCMQCWSEYLTTKIMEEGMGQTISCPAHGC 344 - 375 CPKCHVTIEKDGGCNHMVCRNQNCKAEFCWVC
Function	"E3 ubiquitin-protein ligase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 UBE2L3 (PubMed:15236971, PubMed:21532592, PubMed:24076655, PubMed:27565346, PubMed:23707686). 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)"
Active Site	ACT_SITE 357 357
Mutation	"123 123 V->A: Strongly decreased ability to initiate ubiquitination of cullin-RING complexes 150 150 F->A: Strongly decreased ability to initiate ubiquitination of cullin-RING complexes 156 158 KLF->AAA: Strongly decreased ability to initiate ubiquitination of cullin-RING complexes 187 188 QI->HV: No loss of interaction with UBE2L3 188 188 I->A: Loss of interaction with UBE2L3 205 205 H->A: Impaired interaction with UBE2L3 without affecting interaction with neddylated cullin-RING complexes 208 208 C->A,H: Loss of interaction with UBE2L3 257 258 KY->AAA: Strongly decreased ability to initiate ubiquitination of cullin-RING complexes 258 258 Y->A: No loss of interaction with UBE2L3 265 267 SFV->AAA: Strongly decreased ability to initiate ubiquitination of cullin-RING complexes 340 341 NT->AA: Strongly decreased ability to initiate ubiquitination of cullin-RING complexes 342 343 KE->AA: Strongly decreased ability to initiate ubiquitination of cullin-RING complexes 347 347 C->A: Impairs zinc-binding and folding 351 352 IE->AA: Strongly decreased ability to initiate ubiquitination of cullin-RING complexes 351 351 I->A: Disrupts the hydrophobic network 357 357 C->A,S: Does not affect zinc binding and folding 358 358 N->A: Defects in ligation 359 359 H->A: Defects in ligation 367 367 C->A: Impairs zinc-binding and folding 371 371 F->A: Disrupts the hydrophobic network 372 372 C->A: Impairs E3 ubiquitin-protein ligase activity 373 373 W->A: Abolishes E3 ubiquitin-protein ligase activity 378 379 PW->AA: Defects in ligation 379 379 W->A: Does not affect E3 ubiquitin-protein ligase activity 383 385 GSA->AAD: Defects in ligation 386 386 W->A: Does not affect E3 ubiquitin-protein ligase activity 416 416 F->A: Slightly relieves autoinhibition of the E3 ligase activity by the ariadne domain 417 417 Y->A: Hyperactive 'open' mutant that displays enhanced E3 ubiquitin-protein ligase activity 420 423 RYMN->AYMA: Slightly relieves autoinhibition of the E3 ligase activity by the ariadne domain when associated with A-503 427 427 S->A: Slightly relieves autoinhibition of the E3 ligase activity by the ariadne domain 430 431 FE->AA: Relieves autoinhibition of the E3 ligase activity by the ariadne domain when associated with A-503 when associated with A-503 476 476 Y->A: Hyperactive 'open' mutant that displays enhanced E3 ubiquitin-protein ligase activity 492 492 E->A: Hyperactive 'open' mutant that displays enhanced E3 ubiquitin-protein ligase activity 493 493 N->A: Hyperactive 'open' mutant that displays enhanced E3 ubiquitin-protein ligase activity 495 495 Q->A: Hyperactive 'open' mutant that displays enhanced E3 ubiquitin-protein ligase activity 499 499 E->A: Hyperactive 'open' mutant that displays enhanced E3 ubiquitin-protein ligase activity 503 503 E->A: Relieves autoinhibition of the E3 ligase activity by the ariadne domain when associated with 430-A-A-431 when associated with 430-A-A-431 when associated with 420-A--A-423 531 531 Y->A: Strongly decreased ability to initiate ubiquitination of cullin-RING complexes"

Q9Y4X5 of Proteins RING-type domain repeats