E3 ubiquitin-protein ligase ARIH1 (EC 2.3.2.31) (H7-AP2) (HHARI) (Monocyte protein 6) (MOP-6) (Protein ariadne-1 homolog) (ARI-1) (UbcH7-binding protein) (UbcM4-interacting protein) (Ubiquitin-conjugating enzyme E2-binding protein 1)
1_MDSDE 6_ GYNYE 11_ FDEDE 16_ ECSEE 21_ DSGAE 26_ EEEDE 31_ DDDEP 36_ DDDTL 41_ DLGEV 46_ ELVEP 51_ GLGVG 56_ GERDG 61_ LLCGE 66_ TGGGG 71_ GSALG 76_ PGGGG 81_ GGGGG 86_ GGGGG 91_ PGHEQ 96_ EEDYR 101_ YEVLT 106_ AEQIL 111_ QHMVE 116_ CIREV 121_ NEVIQ 126_ NPATI 131_ TRILL 136_ SHFNW 141_ DKEKL 146_ MERYF 151_ DGNLE 156_ KLFAE 161_ CHVIN 166_ PSKKS 171_ RTRQM 176_ NTRSS 181_ AQDMP 186_ CQICY 191_ LNYPN 196_ SYFTG 201_ LECGH 206_ KFCMQ 211_ CWSEY 216_ LTTKI 221_ MEEGM 226_ GQTIS 231_ CPAHG 236_ CDILV 241_ DDNTV 246_ MRLIT 251_ DSKVK 256_ LKYQH 261_ LITNS 266_ FVECN 271_ RLLKW 276_ CPAPD 281_ CHHVV 286_ KVQYP 291_ DAKPV 296_ RCKCG 301_ RQFCF 306_ NCGEN 311_ WHDPV 316_ KCKWL 321_ KKWIK 326_ KCDDD 331_ SETSN 336_ WIAAN 341_ TKECP 346_ KCHVT 351_ IEKDG 356_ GCNHM 361_ VCRNQ 366_ NCKAE 371_ FCWVC 376_ LGPWE 381_ PHGSA 386_ WYNCN 391_ RYNED 396_ DAKAA 401_ RDAQE 406_ RSRAA 411_ LQRYL 416_ FYCNR 421_ YMNHM 426_ QSLRF 431_ EHKLY 436_ AQVKQ 441_ KMEEM 446_ QQHNM 451_ SWIEV 456_ QFLKK 461_ AVDVL 466_ CQCRA 471_ TLMYT 476_ YVFAF 481_ YLKKN 486_ NQSII 491_ FENNQ 496_ ADLEN 501_ ATEVL 506_ SGYLE 511_ RDISQ 516_ DSLQD 521_ IKQKV 526_ QDKYR 531_ YCESR 536_ RRVLL 541_ QHVHE 546_ GYEKD 551_LWEYI
1: 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)