Q9Y4X5: E3 ubiquitin-protein ligase ARIH1 (ARIH1)

E3 ubiquitin-protein ligase ARIH1 (ARIH1) is a 557-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9Y4X5.

Gene
ARIH1
Organism
Homo sapiens
Length
557 residues
Mean pLDDT
80.0
Model
AF-Q9Y4X5-F1 v6
Model created
1 Aug 2025
PDB structures
10

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Model confidence (pLDDT)

The mean pLDDT of this model is 80.0 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate58%
70 to 90Confident: backbone generally right20%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions19%

What pLDDT means and how to read it

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…

Subunit structure

Interacts (via the first RING-type zinc finger) with UBE2L3 (PubMed:11278816, PubMed:21532592, PubMed:23707686, PubMed:24076655). Associates with cullin-RING ubiquitin ligase (CRL) complexes containing CUL1, CUL2 and CUL3 (PubMed:24076655, PubMed:27565346). Interacts with neddylated CUL1 (PubMed:24076655, PubMed:27565346). Interacts with neddylated CUL2 (PubMed:24076655, PubMed:27565346).…

Subcellular location

Cytoplasm, Nucleus, Nucleus, Cajal body

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
5UDHX-ray3.24 ÅA/B=90-557
4KBLX-ray3.3 ÅA/B=1-557
5TTEX-ray3.5 ÅB=1-557
4KC9X-ray3.6 ÅA=1-557
7B5NEM3.6 ÅH=1-557
7B5SEM3.6 ÅH=1-557
7B5LEM3.8 ÅH=1-557
7B5MEM3.91 ÅH=1-557
1WD2NMRA=336-394
2M9YNMRA=325-396

More AlphaFold highlights

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