ARIH2

ARIH2 is an E3 ubiquitin-protein ligase that polyubiquitinates some proteins, tagging them for degradation. The encoded protein upregulates p53 in some cancer cells and may inhibit myelopoiesis. Several transcript variants encoding different isoforms have

Full Name

Ariadne RBR E3 Ubiquitin Protein Ligase 2

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).
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 (By similarity).
The initial ubiquitin is then elongated (By similarity).
E3 ubiquitin-protein ligase activity is activated upon binding to neddylated form of the ECS complex (PubMed:24076655).
Mediates 'Lys-6', 'Lys-48'- and 'Lys-63'-linked polyubiquitination (PubMed:16118314, PubMed:17646546, PubMed:19340006).
May play a role in myelopoiesis (PubMed:19340006).

Biological Process

Developmental cell growth Source: UniProtKB
Hematopoietic stem cell proliferation Source: UniProtKB
Multicellular organism development Source: ProtInc
Positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: GO_Central
Positive regulation of protein targeting to mitochondrion Source: ParkinsonsUK-UCL
Protein K48-linked ubiquitination Source: UniProtKB
Protein K63-linked ubiquitination Source: UniProtKB
Protein polyubiquitination Source: UniProtKB
Protein ubiquitination Source: UniProtKB
Ubiquitin-dependent protein catabolic process Source: UniProtKB

Cellular Location

Cytoplasm; Nucleus

PTM

Ubiquitinated. Ubiquitination promotes proteasomal degradation.