P61089 (UBE2N_MOUSE) 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
Ubc13
Ubiquitin carrier protein N
Ubiquitin-protein ligase N

Gene names

Name:	Ube2n
Synonyms:	Blu

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [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 › Mus › Mus

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. Ref.6
Subcellular location	Nucleus By similarity. Cytoplasm 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.
Sequence caution	The sequence BAE36659.1 differs from that shown. Reason: Frameshift at position 105.

Ontologies

Keywords
Biological process	DNA damage DNA repair Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
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 double-strand break processing Inferred from sequence or structural similarity. Source: HGNC T cell receptor signaling pathway Inferred from sequence or structural similarity PubMed 15125833. Source: HGNC double-strand break repair via homologous recombination Inferred from sequence or structural similarity. Source: HGNC histone ubiquitination Inferred from sequence or structural similarity. Source: HGNC positive regulation of DNA repair Inferred from sequence or structural similarity. Source: HGNC positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from sequence or structural similarity. Source: HGNC positive regulation of NF-kappaB transcription factor activity Inferred from sequence or structural similarity PubMed 14695475. Source: HGNC positive regulation of histone modification Inferred from sequence or structural similarity. Source: HGNC positive regulation of ubiquitin-protein ligase activity Inferred from sequence or structural similarity. Source: HGNC postreplication repair Inferred from sequence or structural similarity. Source: HGNC protein K63-linked ubiquitination Inferred from sequence or structural similarity. Source: UniProtKB regulation of histone ubiquitination Inferred from sequence or structural similarity. Source: HGNC ubiquitin-dependent protein catabolic process Inferred from direct assay Ref.2. Source: MGI
Cellular_component	UBC13-MMS2 complex Inferred from sequence or structural similarity. Source: HGNC UBC13-UEV1A complex Inferred from sequence or structural similarity. Source: UniProtKB cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB nucleus 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 binding Inferred from sequence or structural similarity. Source: HGNC 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_0000082504
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
Experimental info
	Sequence conflict	114	1	A → D in BAB24239. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P61089 [UniParc]. Last modified April 26, 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

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Rugarli E.I., Valsecchi V., Ballabio A. Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: ICR X Swiss Webster.
[2]	"Roles of mouse UBC13 in DNA postreplication repair and Lys63-linked ubiquitination." Ashley C., Pastushok L., McKenna S., Ellison M.J., Xiao W. Gene 285:183-191(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: B-cell.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Cerebellum, Olfactory bulb and Testis.
[4]	"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]. Strain: C57BL/6. Tissue: Eye and Mammary gland.
[5]	Lubec G., Klug S., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 15-24; 34-68; 95-102 AND 131-141, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain and Hippocampus.
[6]	"Chaperoned ubiquitylation -- crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex." Zhang M., Windheim M., Roe S.M., Peggie M., Cohen P., Prodromou C., Pearl L.H. Mol. Cell 20:525-538(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH STUB1 AND UBE2V1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y09873 mRNA. Translation: CAA71001.1. AY039837 mRNA. Translation: AAK74128.1. AK005302 mRNA. Translation: BAB23941.1. AK005788 mRNA. Translation: BAB24239.1. AK161968 mRNA. Translation: BAE36659.1. Frameshift. BC034898 mRNA. Translation: AAH34898.3. BC067069 mRNA. Translation: AAH67069.1.
IPI	IPI00165854.
RefSeq	NP_542127.1. NM_080560.3.
UniGene	Mm.371667. Mm.440187. Mm.486592.
3D structure databases
ProteinModelPortal	P61089.
ModBase	Search...
Protein-protein interaction databases
IntAct	P61089. 5 interactions.
PTM databases
PhosphoSite	P61089.
2D gel databases
REPRODUCTION-2DPAGE	IPI00165854. P61089.
Proteomic databases
PaxDb	P61089.
PRIDE	P61089.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000099329; ENSMUSP00000096932; ENSMUSG00000074781.
GeneID	93765.
KEGG	mmu:93765.
Organism-specific databases
CTD	7334.
MGI	MGI:1934835. Ube2n.
Phylogenomic databases
eggNOG	COG5078.
GeneTree	ENSGT00540000070023.
HOGENOM	HOG000233455.
HOVERGEN	HBG063308.
InParanoid	P61089.
KO	K10580.
OMA	DDNLRYF.
OrthoDB	EOG4MCX1K.
Enzyme and pathway databases
UniPathway	UPA00143.
Gene expression databases
ArrayExpress	P61089.
Bgee	P61089.
CleanEx	MM_UBE2N.
Genevestigator	P61089.
GermOnline	ENSMUSG00000047099. Mus musculus.
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	P61089.
NextBio	28704.
SOURCE	Search...

Entry information

Entry name

UBE2N_MOUSE

Accession

Primary (citable) accession number: P61089
Secondary accession number(s): Q16781 , Q3TSL6, Q6ZWZ0, Q9DAJ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	April 26, 2004
Last modified:	May 1, 2013
This is version 109 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program