Ubiquitin-conjugating enzyme E2 N - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P61088 (UBE2N_HUMAN)

Last modified November 25, 2008. Version 65. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Ubiquitin-conjugating enzyme E2 N
    EC=6.3.2.19
Alternative name(s):
    Ubiquitin-protein ligase N
    Ubiquitin carrier protein N
    Ubc13
    Bendless-like ubiquitin-conjugating enzyme

Gene names

Name:	UBE2N
Synonyms:	BLU

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	152 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	The UBE2V2/UBE2N heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'. This type of poly-ubiquitination 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 ligase SHPRH in the poly-ubiquitination of PCNA 'Lys-164' upon genotoxic stress, which is required for DNA repair.
Catalytic activity	ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Heterodimer with UBE2V2. Interacts with RNF8 and SHPRH.
Post-translational modification	Conjugation to ISG15 impairs formation of the thioester bond with ubiquitin but not interaction with UBE2V2.
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.

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Ontologies

Keywords
Biological process	DNA damage DNA repair Ubl conjugation pathway
Molecular function	Ligase
PTM	Ubl conjugation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Uncategorized	ubiquitin cycle Ref.5 Traceable author statement. Source: HGNC
Biological process	DNA double-strand break processing Inferred from mutant phenotype. Source: HGNC T cell receptor signaling pathway Inferred from mutant phenotype. Source: UniProtKB double-strand break repair via homologous recombination Inferred from mutant phenotype. Source: HGNC positive regulation of DNA repair Inferred from mutant phenotype. Source: HGNC positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from mutant phenotype. Source: HGNC positive regulation of NF-kappaB transcription factor activity Inferred from mutant phenotype. Source: UniProtKB positive regulation of histone modification Inferred from mutant phenotype. Source: HGNC positive regulation of ubiquitin-protein ligase activity Inferred from mutant phenotype. Source: HGNC postreplication repair Inferred from mutant phenotype. Source: HGNC regulation of histone ubiquitination Inferred from mutant phenotype. Source: HGNC ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	UBC13-MMS2 complex Inferred from direct assay. Source: HGNC cytoplasm Traceable author statement. Source: UniProtKB nucleus Inferred from direct assay. Source: HGNC
Molecular function	ubiquitin binding Ref.5 Inferred from direct assay. Source: HGNC ubiquitin-protein ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
UBE2V2	Q15819	1	EBI-1052908,EBI-714329

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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_0000082502

Sites

Active site

Glycyl thioester intermediate

Amino acid modifications

Cross-link

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)

Experimental info

Mutagenesis

C → A: Impairs interaction with SHPRH

Mutagenesis

K → R: No ISGylation

Mutagenesis

K → R: No effect on ISGylation

Secondary structure

152

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P61088-1 [UniParc].

Last modified April 26, 2004. Version 1.
Checksum: FACD84D883D77407
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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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of cDNA encoding a human ubiquitin-conjugating enzyme similar to the Drosophila bendless gene product." Yamaguchi T., Kim N.-S., Sekine S., Seino H., Osaka F., Yamao F., Kato S. J. Biochem. 120:494-497(1996) [PubMed: 8902611] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung, Placenta and Uterus.
[4]	Lubec G., Vishwanath V. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 34-68, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[5]	"ISG15 modification of ubiquitin E2 Ubc13 disrupts its ability to form thioester bond with ubiquitin." Zou W., Papov V., Malakhova O., Kim K.I., Dao C., Li J., Zhang D.-E. Biochem. Biophys. Res. Commun. 336:61-68(2005) [PubMed: 16122702] [Abstract] Cited for: PROTEIN SEQUENCE OF 86-94, MUTAGENESIS OF LYS-92, ISGYLATION AT LYS-92, MASS SPECTROMETRY.
[6]	"Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair." Hofmann R.M., Pickart C.M. Cell 96:645-653(1999) [PubMed: 10089880] [Abstract] Cited for: FUNCTION, INTERACTION WITH UBE2V2.
[7]	"The Chfr mitotic checkpoint protein functions with Ubc13-Mms2 to form Lys63-linked polyubiquitin chains." Bothos J., Summers M.K., Venere M., Scolnick D.M., Halazonetis T.D. Oncogene 22:7101-7107(2003) [PubMed: 14562038] [Abstract] Cited for: FUNCTION, INTERACTION WITH UBE2V2.
[8]	"ISG15 modification of Ubc13 suppresses its ubiquitin-conjugating activity." Takeuchi T., Yokosawa H. Biochem. Biophys. Res. Commun. 336:9-13(2005) [PubMed: 16112642] [Abstract] Cited for: MUTAGENESIS OF LYS-92 AND LYS-94, ISGYLATION AT LYS-92.
[9]	"Human SHPRH suppresses genomic instability through proliferating cell nuclear antigen polyubiquitination." Motegi A., Sood R., Moinova H., Markowitz S.D., Liu P.P., Myung K. J. Cell Biol. 175:703-708(2006) [PubMed: 17130289] [Abstract] Cited for: INTERACTION WITH SHPRH, MUTAGENESIS OF CYS-87.
[10]	"The RING finger protein RNF8 recruits UBC13 for lysine 63-based self polyubiquitylation." Plans V., Scheper J., Soler M., Loukili N., Okano Y., Thomson T.M. J. Cell. Biochem. 97:572-582(2006) [PubMed: 16215985] [Abstract] Cited for: INTERACTION WITH RNF8.
[11]	"Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependent polyubiquitylation of proliferating cell nuclear antigen." Unk I., Hajdu I., Fatyol K., Szakal B., Blastyak A., Bermudez V., Hurwitz J., Prakash L., Prakash S., Haracska L. Proc. Natl. Acad. Sci. U.S.A. 103:18107-18112(2006) [PubMed: 17108083] [Abstract] Cited for: INTERACTION WITH SHPRH.
[12]	"Crystal structure of the human ubiquitin conjugating enzyme complex, hMms2-hUbc13." Moraes T.F., Edwards R.A., McKenna S., Pastushok L., Xiao W., Glover J.N.M., Ellison M.J. Nat. Struct. Biol. 8:669-673(2001) [PubMed: 11473255] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH UBE2V2.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

D83004 mRNA. Translation: BAA11675.1.
BT006873 mRNA. Translation: AAP35519.1.
BC000396 mRNA. Translation: AAH00396.1.
BC003365 mRNA. Translation: AAH03365.1.
BC108704 mRNA. Translation: AAI08705.1.

PIR

JC4894.

RefSeq

NP_003339.1.

UniGene

Hs.524630

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1J7D	X-ray	1.85	B	1-152	[»]
2C2V	X-ray	2.90	B/E/H/K	2-152	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P61088.

PTM databases

PhosphoSite

P61088.

2-D gel databases

OGP

Q16781.

REPRODUCTION-2DPAGE

IPI00003949.

Proteomic databases

PeptideAtlas

P61088.

Genome annotation databases

Ensembl

ENSG00000177889. Homo sapiens. [Contig view]

GeneID

7334.

KEGG

hsa:7334.

Organism-specific databases

H-InvDB

HIX0010883.
HIX0056502.

HGNC

HGNC:12492. UBE2N.

HPA

HPA003962.

MIM

603679. gene.

PharmGKB

PA37141.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

P61088.

HOVERGEN

P61088.

Gene expression databases

ArrayExpress

P61088.

CleanEx

HS_UBE2N.

GermOnline

ENSG00000177889. Homo sapiens.

Family and domain databases

InterPro

IPR016135. UBQ-conjugat/RWD-like.
IPR000608. UBQ-conjugat_E2.
[Graphical view]

Gene3D

G3DSA:3.10.110.10. UBQ-conjugat_E2. 1 hit.

PANTHER

PTHR11621. UBQ-conjugat_E2. 1 hit.

Pfam

PF00179. UQ_con. 1 hit.
[Graphical view]

ProDom

PD000461. UBQ_conjugat. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00212. UBCc. 1 hit.
[Graphical view]

PROSITE

PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

LinkHub

P61088.

NextBio

28704.

SOURCE

Search...

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Entry information

Entry name

UBE2N_HUMAN

Accession

Primary (citable) accession number: P61088
Secondary accession number(s): Q16781, Q53Y81

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	April 26, 2004
Last modified:	November 25, 2008
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents