Q5R7J6 (UBE2N_PONAB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin-conjugating enzyme E2 N
EC=6.3.2.19

Alternative name(s):
Ubiquitin carrier protein N
Ubiquitin-protein ligase N

Gene names

Name:

UBE2N

Organism

Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]

Taxonomic identifier

9601 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Ponginae › Pongo

Protein attributes

Sequence length	152 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	The UBE2V1-UBE2N and UBE2V2-UBE2N heterodimers catalyze the synthesis of non-canonical 'Lys-63'-linked polyubiquitin chains. This type of polyubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. Acts together with the E3 ligases, HLTF and SHPRH, in the 'Lys-63'-linked poly-ubiquitination of PCNA upon genotoxic stress, which is required for DNA repair. Appears to act together with E3 ligase RNF5 in the 'Lys-63'-linked polyubiquitination of JKAMP thereby regulating JKAMP function by decreasing its association with components of the proteasome and ERAD By similarity. Promotes TRIM5 capsid-specific restriction activity and the UBE2V1-UBE2N heterodimer acts in concert with TRIM5 to generate 'Lys-63'-linked polyubiquitin chains which activate the MAP3K7/TAK1 complex which in turn results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes By similarity.
Catalytic activity	ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
Enzyme regulation	Activity is inhibited by binding to OTUB1, which prevents 'Lys-63'-linked polyubiquitination By similarity.
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Heterodimer with UBE2V2. Interacts (UBE2V2-UBE2N heterodimer) with the E3 ligase STUB1 (via the U-box domain); the complex has a specific 'Lys-63'-linked polyubiquitination activity. Interacts with RNF8 and RNF168. Interacts with RNF11. Interacts with the E3 ligases, HLTF and SHPRH; the interactions promote the 'Lys-63'-linked polyubiquitination of PCNA upon genotoxic stress and lead to DNA repair. Interacts with ARIH2 (via RING-type 2). Interacts with OTUB1; leading to inhibit E2-conjugating activity By similarity.
Post-translational modification	Conjugation to ISG15 impairs formation of the thioester bond with ubiquitin but not interaction with UBE2V2 By similarity.
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
Biological process	DNA damage DNA repair Ubl conjugation pathway
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Acetylation Isopeptide bond Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA double-strand break processing Inferred from electronic annotation. Source: Compara T cell receptor signaling pathway Inferred from electronic annotation. Source: Compara double-strand break repair via homologous recombination Inferred from electronic annotation. Source: Compara histone ubiquitination Inferred from electronic annotation. Source: Compara positive regulation of DNA repair Inferred from electronic annotation. Source: Compara positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from electronic annotation. Source: Compara positive regulation of NF-kappaB transcription factor activity Inferred from electronic annotation. Source: Compara positive regulation of histone modification Inferred from electronic annotation. Source: Compara positive regulation of ubiquitin-protein ligase activity Inferred from electronic annotation. Source: Compara postreplication repair Inferred from electronic annotation. Source: Compara protein K63-linked ubiquitination Inferred from sequence or structural similarity. Source: UniProtKB regulation of histone ubiquitination Inferred from electronic annotation. Source: Compara ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: Compara
Cellular_component	UBC13-MMS2 complex Inferred from electronic annotation. Source: Compara UBC13-UEV1A complex Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from electronic annotation. Source: Compara ubiquitin ligase complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-protein ligase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 152	152	Ubiquitin-conjugating enzyme E2 N		PRO_0000082505
Sites
	Active site	87	1	Glycyl thioester intermediate
Amino acid modifications
	Modified residue	82	1	N6-acetyllysine By similarity
	Cross-link	92		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5R7J6 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: FACD84D883D77407	FASTA	152	17,138
	10 20 30 40 50 60 MAGLPRRIIK ETQRLLAEPV PGIKAEPDES NARYFHVVIA GPQDSPFEGG TFKLELFLPE 70 80 90 100 110 120 EYPMAAPKVR FMTKIYHPNV DKLGRICLDI LKDKWSPALQ IRTVLLSIQA LLSAPNPDDP 130 140 150 LANDVAEQWK TNEAQAIETA RAWTRLYAMN NI

References

[1]	The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain cortex.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR860119 mRNA. Translation: CAH92264.1.
RefSeq	NP_001127530.1. NM_001134058.1.
UniGene	Pab.18824.
3D structure databases
ProteinModelPortal	Q5R7J6.
ModBase	Search...
Proteomic databases
PRIDE	Q5R7J6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSPPYT00000005723; ENSPPYP00000005510; ENSPPYG00000004832.
GeneID	100174607.
KEGG	pon:100174607.
Organism-specific databases
CTD	7334.
Phylogenomic databases
GeneTree	ENSGT00540000070023.
HOVERGEN	HBG063308.
InParanoid	Q5R7J6.
KO	K10580.
OMA	DDNLRYF.
Enzyme and pathway databases
UniPathway	UPA00143.
Family and domain databases
Gene3D	3.10.110.10. 1 hit.
InterPro	IPR000608. UBQ-conjugat_E2. IPR023313. UBQ-conjugating_AS. IPR016135. UBQ-conjugating_enzyme/RWD. [Graphical view]
Pfam	PF00179. UQ_con. 1 hit. [Graphical view]
SUPFAM	SSF54495. UBQ-conjugat/RWD-like. 1 hit.
PROSITE	PS00183. UBIQUITIN_CONJUGAT_1. 1 hit. PS50127. UBIQUITIN_CONJUGAT_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q5R7J6.

Entry information

Entry name

UBE2N_PONAB

Accession

Primary (citable) accession number: Q5R7J6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2005
Last sequence update:	December 21, 2004
Last modified:	May 1, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program