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P61088

- UBE2N_HUMAN

UniProt

P61088 - UBE2N_HUMAN

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Protein

Ubiquitin-conjugating enzyme E2 N

Gene

UBE2N

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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. 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).By similarity

Catalytic activityi

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.PROSITE-ProRule annotation

Enzyme regulationi

Activity is inhibited by binding to OTUB1, which prevents 'Lys-63'-linked polyubiquitination.3 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei87 – 871Glycyl thioester intermediate

GO - Molecular functioni

  1. acid-amino acid ligase activity Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. poly(A) RNA binding Source: UniProtKB
  4. ubiquitin binding Source: HGNC
  5. ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

  1. cellular protein modification process Source: ProtInc
  2. cytokine-mediated signaling pathway Source: Reactome
  3. DNA double-strand break processing Source: HGNC
  4. double-strand break repair via homologous recombination Source: HGNC
  5. Fc-epsilon receptor signaling pathway Source: Reactome
  6. histone ubiquitination Source: HGNC
  7. innate immune response Source: Reactome
  8. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
  9. nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Source: Reactome
  10. nucleotide-binding oligomerization domain containing signaling pathway Source: Reactome
  11. positive regulation of DNA repair Source: HGNC
  12. positive regulation of histone modification Source: HGNC
  13. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: HGNC
  14. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  15. positive regulation of ubiquitin-protein transferase activity Source: HGNC
  16. postreplication repair Source: HGNC
  17. protein K63-linked ubiquitination Source: UniProtKB
  18. protein ubiquitination Source: HGNC
  19. proteolysis Source: ProtInc
  20. regulation of DNA repair Source: ProtInc
  21. regulation of histone ubiquitination Source: HGNC
  22. T cell receptor signaling pathway Source: UniProtKB
  23. toll-like receptor 10 signaling pathway Source: Reactome
  24. toll-like receptor 2 signaling pathway Source: Reactome
  25. toll-like receptor 4 signaling pathway Source: Reactome
  26. toll-like receptor 5 signaling pathway Source: Reactome
  27. toll-like receptor 9 signaling pathway Source: Reactome
  28. toll-like receptor signaling pathway Source: Reactome
  29. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
  30. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
  31. ubiquitin-dependent protein catabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_115831. ISG15 antiviral mechanism.
REACT_12555. Downstream TCR signaling.
REACT_163994. FCERI mediated NF-kB activation.
REACT_22442. Interleukin-1 signaling.
REACT_24918. IRAK1 recruits IKK complex.
REACT_25120. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
REACT_25354. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
REACT_25374. IKK complex recruitment mediated by RIP1.
REACT_75776. NOD1/2 Signaling Pathway.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiP61088.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2 N (EC:6.3.2.19)
Alternative name(s):
Bendless-like ubiquitin-conjugating enzyme
Ubc13
UbcH13
Ubiquitin carrier protein N
Ubiquitin-protein ligase N
Gene namesi
Name:UBE2N
Synonyms:BLU
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:12492. UBE2N.

Subcellular locationi

Nucleus 1 Publication. Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProtKB
  4. nucleus Source: UniProtKB
  5. protein complex Source: MGI
  6. UBC13-MMS2 complex Source: HGNC
  7. UBC13-UEV1A complex Source: UniProtKB
  8. ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi87 – 871C → A: Loss of polyubiquitination of PCNA. Impairs interaction with SHPRH. 2 Publications
Mutagenesisi92 – 921K → R: No ISGylation. 2 Publications
Mutagenesisi94 – 941K → R: No effect on ISGylation. 1 Publication

Organism-specific databases

PharmGKBiPA37141.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 152152Ubiquitin-conjugating enzyme E2 NPRO_0000082502Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei82 – 821N6-acetyllysine1 Publication
Disulfide bondi87 – 87Interchain (with C-78 in ISG15)1 Publication
Cross-linki92 – 92Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)

Post-translational modificationi

Conjugation to ISG15 impairs formation of the thioester bond with ubiquitin but not interaction with UBE2V2.

Keywords - PTMi

Acetylation, Disulfide bond, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP61088.
PaxDbiP61088.
PeptideAtlasiP61088.
PRIDEiP61088.

2D gel databases

OGPiQ16781.
REPRODUCTION-2DPAGEIPI00003949.

PTM databases

PhosphoSiteiP61088.

Expressioni

Gene expression databases

BgeeiP61088.
CleanExiHS_UBE2N.
ExpressionAtlasiP61088. baseline and differential.
GenevestigatoriP61088.

Organism-specific databases

HPAiHPA003962.
HPA044976.

Interactioni

Subunit structurei

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.16 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RNF11Q9Y3C54EBI-1052908,EBI-396669
RNF168Q8IYW52EBI-1052908,EBI-914207
STUB1Q9UNE74EBI-1052908,EBI-357085
Stub1Q9WUD12EBI-1052908,EBI-773027From a different organism.
TRAF6Q9Y4K33EBI-1052908,EBI-359276
UBE2V1Q134049EBI-1052908,EBI-1050671
UBE2V2Q158193EBI-1052908,EBI-714329
XIAPP981702EBI-1052908,EBI-517127
ZNRF1Q8ND253EBI-1052908,EBI-2129250

Protein-protein interaction databases

BioGridi113182. 127 interactions.
DIPiDIP-29829N.
IntActiP61088. 58 interactions.
MINTiMINT-5001139.
STRINGi9606.ENSP00000316176.

Structurei

Secondary structure

1
152
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 1712Combined sources
Beta strandi23 – 275Combined sources
Beta strandi34 – 407Combined sources
Turni46 – 494Combined sources
Beta strandi51 – 577Combined sources
Turni60 – 634Combined sources
Beta strandi68 – 736Combined sources
Helixi89 – 913Combined sources
Turni92 – 943Combined sources
Helixi101 – 11313Combined sources
Helixi124 – 1318Combined sources
Helixi133 – 14715Combined sources
Beta strandi148 – 1503Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J7DX-ray1.85B1-152[»]
2C2VX-ray2.90B/E/H/K2-152[»]
3HCTX-ray2.10B1-152[»]
3HCUX-ray2.60B/D1-152[»]
3VONX-ray3.15C/E/G/J/L/N/Q/S/U/X/Z/b/e/g/i/l/n/p3-150[»]
3W31X-ray2.96B1-152[»]
4DHIX-ray1.80D1-152[»]
4DHJX-ray2.35C/G/K/N1-152[»]
4DHZX-ray3.11F1-152[»]
4IP3X-ray2.30B1-152[»]
4ORHX-ray4.80B/F/J1-152[»]
ProteinModelPortaliP61088.
SMRiP61088. Positions 3-152.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61088.

Family & Domainsi

Sequence similaritiesi

Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5078.
HOGENOMiHOG000233455.
HOVERGENiHBG063308.
InParanoidiP61088.
KOiK10580.
OMAiYSTHTHI.
OrthoDBiEOG7XWPQB.
PhylomeDBiP61088.
TreeFamiTF101126.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P61088-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGLPRRIIK ETQRLLAEPV PGIKAEPDES NARYFHVVIA GPQDSPFEGG
60 70 80 90 100
TFKLELFLPE EYPMAAPKVR FMTKIYHPNV DKLGRICLDI LKDKWSPALQ
110 120 130 140 150
IRTVLLSIQA LLSAPNPDDP LANDVAEQWK TNEAQAIETA RAWTRLYAMN

NI
Length:152
Mass (Da):17,138
Last modified:April 26, 2004 - v1
Checksum:iFACD84D883D77407
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS31875.1.
PIRiJC4894.
RefSeqiNP_003339.1. NM_003348.3.
UniGeneiHs.524630.

Genome annotation databases

EnsembliENST00000318066; ENSP00000316176; ENSG00000177889.
GeneIDi7334.
KEGGihsa:7334.
UCSCiuc001tcp.3. human.

Polymorphism databases

DMDMi46577660.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS31875.1.
PIRi JC4894.
RefSeqi NP_003339.1. NM_003348.3.
UniGenei Hs.524630.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
3HCT X-ray 2.10 B 1-152 [» ]
3HCU X-ray 2.60 B/D 1-152 [» ]
3VON X-ray 3.15 C/E/G/J/L/N/Q/S/U/X/Z/b/e/g/i/l/n/p 3-150 [» ]
3W31 X-ray 2.96 B 1-152 [» ]
4DHI X-ray 1.80 D 1-152 [» ]
4DHJ X-ray 2.35 C/G/K/N 1-152 [» ]
4DHZ X-ray 3.11 F 1-152 [» ]
4IP3 X-ray 2.30 B 1-152 [» ]
4ORH X-ray 4.80 B/F/J 1-152 [» ]
ProteinModelPortali P61088.
SMRi P61088. Positions 3-152.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113182. 127 interactions.
DIPi DIP-29829N.
IntActi P61088. 58 interactions.
MINTi MINT-5001139.
STRINGi 9606.ENSP00000316176.

Chemistry

BindingDBi P61088.
ChEMBLi CHEMBL6089.

PTM databases

PhosphoSitei P61088.

Polymorphism databases

DMDMi 46577660.

2D gel databases

OGPi Q16781.
REPRODUCTION-2DPAGE IPI00003949.

Proteomic databases

MaxQBi P61088.
PaxDbi P61088.
PeptideAtlasi P61088.
PRIDEi P61088.

Protocols and materials databases

DNASUi 7334.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000318066 ; ENSP00000316176 ; ENSG00000177889 .
GeneIDi 7334.
KEGGi hsa:7334.
UCSCi uc001tcp.3. human.

Organism-specific databases

CTDi 7334.
GeneCardsi GC12M093735.
HGNCi HGNC:12492. UBE2N.
HPAi HPA003962.
HPA044976.
MIMi 603679. gene.
neXtProti NX_P61088.
PharmGKBi PA37141.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5078.
HOGENOMi HOG000233455.
HOVERGENi HBG063308.
InParanoidi P61088.
KOi K10580.
OMAi YSTHTHI.
OrthoDBi EOG7XWPQB.
PhylomeDBi P61088.
TreeFami TF101126.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_115831. ISG15 antiviral mechanism.
REACT_12555. Downstream TCR signaling.
REACT_163994. FCERI mediated NF-kB activation.
REACT_22442. Interleukin-1 signaling.
REACT_24918. IRAK1 recruits IKK complex.
REACT_25120. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
REACT_25354. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
REACT_25374. IKK complex recruitment mediated by RIP1.
REACT_75776. NOD1/2 Signaling Pathway.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinki P61088.

Miscellaneous databases

ChiTaRSi UBE2N. human.
EvolutionaryTracei P61088.
GeneWikii UBE2N.
GenomeRNAii 7334.
NextBioi 28704.
PROi P61088.
SOURCEi Search...

Gene expression databases

Bgeei P61088.
CleanExi HS_UBE2N.
ExpressionAtlasi P61088. baseline and differential.
Genevestigatori P61088.

Family and domain databases

Gene3Di 3.10.110.10. 1 hit.
InterProi IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view ]
Pfami PF00179. UQ_con. 1 hit.
[Graphical view ]
SUPFAMi SSF54495. SSF54495. 1 hit.
PROSITEi PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung, Placenta and Uterus.
  4. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 15-24; 34-68; 86-92 AND 95-102, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 86-94, MUTAGENESIS OF LYS-92, ISGYLATION AT LYS-92, IDENTIFICATION BY 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SHPRH.
  12. "Site-specific Lys-63-linked tumor necrosis factor receptor-associated factor 6 auto-ubiquitination is a critical determinant of I kappa B kinase activation."
    Lamothe B., Besse A., Campos A.D., Webster W.K., Wu H., Darnay B.G.
    J. Biol. Chem. 282:4102-4112(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-87.
  13. "Human HLTF functions as a ubiquitin ligase for proliferating cell nuclear antigen polyubiquitination."
    Unk I., Hajdu I., Fatyol K., Hurwitz J., Yoon J.-H., Prakash L., Prakash S., Haracska L.
    Proc. Natl. Acad. Sci. U.S.A. 105:3768-3773(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HLTF.
  14. "Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH prevents genomic instability from stalled replication forks."
    Motegi A., Liaw H.-J., Lee K.-Y., Roest H.P., Maas A., Wu X., Moinova H., Markowitz S.D., Ding H., Hoeijmakers J.H.J., Myung K.
    Proc. Natl. Acad. Sci. U.S.A. 105:12411-12416(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HLTF.
  15. Cited for: INTERACTION WITH RNF168.
  16. "Regulation of endoplasmic reticulum-associated degradation by RNF5-dependent ubiquitination of JNK-associated membrane protein (JAMP)."
    Tcherpakov M., Delaunay A., Toth J., Kadoya T., Petroski M.D., Ronai Z.A.
    J. Biol. Chem. 284:12099-12109(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN UBIQUITINATION OF JKAMP.
  17. Cited for: INTERACTION WITH ARIH2, SUBCELLULAR LOCATION.
  18. "Analysis of electrostatic contributions to the selectivity of interactions between RING-finger domains and ubiquitin-conjugating enzymes."
    Scheper J., Oliva B., Villa-Freixa J., Thomson T.M.
    Proteins 74:92-103(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNF11.
  19. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-82, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines."
    David Y., Ziv T., Admon A., Navon A.
    J. Biol. Chem. 285:8595-8604(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  21. Cited for: ENZYME REGULATION, INTERACTION WITH OTUB1.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. Cited for: FUNCTION.
  24. "A DNA damage response screen identifies RHINO, a 9-1-1 and TopBP1 interacting protein required for ATR signaling."
    Cotta-Ramusino C., McDonald E.R. III, Hurov K., Sowa M.E., Harper J.W., Elledge S.J.
    Science 332:1313-1317(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
  25. "Covalent protein modification with ISG15 via a conserved cysteine in the hinge region."
    Bade V.N., Nickels J., Keusekotten K., Praefcke G.J.
    PLoS ONE 7:E38294-E38294(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ISGYLATION, DISULFIDE BOND.
  26. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH UBE2V2.
  27. "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: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 2-152 IN COMPLEX WITH STUB1 AND UBE2V1.
  28. "Molecular insights into the function of RING Finger (RNF)-containing proteins hRNF8 and hRNF168 in Ubc13/Mms2-dependent ubiquitylation."
    Campbell S.J., Edwards R.A., Leung C.C., Neculai D., Hodge C.D., Dhe-Paganon S., Glover J.N.
    J. Biol. Chem. 287:23900-23910(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (4.8 ANGSTROMS) OF 1-150 IN COMPLEX WITH RNF8 AND UBE2V2.
  29. Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 25-271 IN COMPLEX WITH UBE2V2 AND OTUB1, ENZYME REGULATION, INTERACTION WITH OTUB1.
  30. "The mechanism of OTUB1-mediated inhibition of ubiquitination."
    Wiener R., Zhang X., Wang T., Wolberger C.
    Nature 483:618-622(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.11 ANGSTROMS) IN COMPLEX WITH OUTB1 AND UBIQUITIN, ENZYME REGULATION, INTERACTION WITH OTUB1.

Entry informationi

Entry nameiUBE2N_HUMAN
AccessioniPrimary (citable) accession number: P61088
Secondary accession number(s): Q16781, Q53Y81
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: November 26, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3