UBE1C

UBE1C

Identifiers Symbols UBA3; UBE1C; hUBA3 External IDs OMIM: 603172 MGI: 1341217 HomoloGene: 2951 GeneCards: UBA3 Gene

Gene Ontology
Molecular function	• protein binding • ATP binding • acid-amino acid ligase activity • ligand-dependent nuclear receptor binding • NEDD8 activating enzyme activity • protein heterodimerization activity
Cellular component	• nucleus
Biological process	• cellular protein modification process • proteolysis • endomitotic cell cycle • protein neddylation • negative regulation of transcription, DNA-dependent • regulation of cell cycle
Sources: Amigo / QuickGO

RNA expression pattern More reference expression data Orthologs Species Human Mouse Entrez 9039 22200 Ensembl ENSG00000144744 ENSMUSG00000030061 UniProt Q8TBC4 Q8C878 RefSeq (mRNA) NM_003968 NM_001111106 RefSeq (protein) NP_003959 NP_001104576 Location (UCSC) Chr 3:
69.1 – 69.13 Mb Chr 6:
97.18 – 97.21 Mb PubMed search

E2 binding domain

appbp1-uba3-nedd8, an e1-ubiquitin-like protein complex with atp

Identifiers

Symbol

E2_bind

Pfam

PF08825

InterPro

IPR014929

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe
PDBsum	structure summary

NEDD8-activating enzyme E1 catalytic subunit is a protein that in humans is encoded by the UBA3 gene.

The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E1 ubiquitin-activating enzyme family. The encoded enzyme associates with AppBp1, an amyloid beta precursor protein binding protein, to form a heterodimer, and then the enzyme complex activates NEDD8, a ubiquitin-like protein, which regulates cell division, signaling and embryogenesis. Multiple alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.

This enzyme contains an E2 binding domain, which resembles ubiquitin, and recruits the catalytic core of the E2 enzyme UBE2M (Ubc12) in a similar manner to that in which ubiquitin interacts with ubiquitin binding domains.