Q9EQX9 (UBE2N_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Bendless-like ubiquitin-conjugating enzyme
Ubiquitin carrier protein N
Ubiquitin-protein ligase N

Gene names

Name:

Ube2n

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	152 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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 Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW protein K63-linked ubiquitination Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin-dependent protein catabolic process Traceable author statement PubMed 11882492. Source: RGD
Cellular_component	UBC13-UEV1A complex Inferred from sequence or structural similarity. Source: UniProtKB 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_0000082506
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)
	Q9EQX9 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: FACD84D883D27457	FASTA	152	17,124
	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 SNEAQAIETA RAWTRLYAMN NI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Expression of rat Bendless gene in the developing brain." Takahashi H., Yamamoto M., Saito Y. Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[3]	Lubec G., Afjehi-Sadat L., Diao W. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 34-68, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Hippocampus and Spinal cord.
[4]	Maurya D.K., Bhargava P. Submitted (DEC-2008) to UniProtKB Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB032739 mRNA. Translation: BAB20414.1. BC090072 mRNA. Translation: AAH90072.1.
IPI	IPI00190559.
RefSeq	NP_446380.1. NM_053928.2.
UniGene	Rn.230134.
3D structure databases
ProteinModelPortal	Q9EQX9.
SMR	Q9EQX9. Positions 2-150.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9EQX9. 1 interaction.
MINT	MINT-1775821.
STRING	10116.ENSRNOP00000055805.
PTM databases
PhosphoSite	Q9EQX9.
Proteomic databases
PaxDb	Q9EQX9.
PRIDE	Q9EQX9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	116725.
KEGG	rno:116725.
UCSC	RGD:621096. rat.
Organism-specific databases
CTD	7334.
RGD	621096. Ube2n.
Phylogenomic databases
eggNOG	COG5078.
HOGENOM	HOG000233455.
HOVERGEN	HBG063308.
KO	K10580.
OrthoDB	EOG4MCX1K.
Enzyme and pathway databases
UniPathway	UPA00143.
Gene expression databases
Genevestigator	Q9EQX9.
GermOnline	ENSRNOG00000009038. Rattus norvegicus.
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
NextBio	619648.

Entry information

Entry name

UBE2N_RAT

Accession

Primary (citable) accession number: Q9EQX9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2005
Last sequence update:	March 1, 2001
Last modified:	April 3, 2013
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program