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Ubiquitin-conjugating enzyme E2 N (EC 2.3.2.23) (Bendless-like ubiquitin-conjugating enzyme) (E2 ubiquitin-conjugating enzyme N) (Ubc13) (UbcH13) (Ubiquitin carrier protein N) (Ubiquitin-protein ligase N)

 UBE2N_HUMAN             Reviewed;         152 AA.
P61088; Q16781; Q53Y81;
26-APR-2004, integrated into UniProtKB/Swiss-Prot.
26-APR-2004, sequence version 1.
22-NOV-2017, entry version 169.
RecName: Full=Ubiquitin-conjugating enzyme E2 N;
EC=2.3.2.23 {ECO:0000269|PubMed:20061386};
AltName: Full=Bendless-like ubiquitin-conjugating enzyme;
AltName: Full=E2 ubiquitin-conjugating enzyme N;
AltName: Full=Ubc13;
AltName: Full=UbcH13;
AltName: Full=Ubiquitin carrier protein N;
AltName: Full=Ubiquitin-protein ligase N;
Name=UBE2N; Synonyms=BLU;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8902611; DOI=10.1093/oxfordjournals.jbchem.a021440;
Yamaguchi T., Kim N.-S., Sekine S., Seino H., Osaka F., Yamao F.,
Kato S.;
"Cloning and expression of cDNA encoding a human ubiquitin-conjugating
enzyme similar to the Drosophila bendless gene product.";
J. Biochem. 120:494-497(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, Placenta, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 15-24; 34-68; 86-92 AND 95-102, AND IDENTIFICATION
BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[5]
PROTEIN SEQUENCE OF 86-94, MUTAGENESIS OF LYS-92, ISGYLATION AT
LYS-92, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16122702; DOI=10.1016/j.bbrc.2005.08.038;
Zou W., Papov V., Malakhova O., Kim K.I., Dao C., Li J., Zhang D.-E.;
"ISG15 modification of ubiquitin E2 Ubc13 disrupts its ability to form
thioester bond with ubiquitin.";
Biochem. Biophys. Res. Commun. 336:61-68(2005).
[6]
FUNCTION, AND INTERACTION WITH UBE2V2.
PubMed=10089880; DOI=10.1016/S0092-8674(00)80575-9;
Hofmann R.M., Pickart C.M.;
"Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in
assembly of novel polyubiquitin chains for DNA repair.";
Cell 96:645-653(1999).
[7]
FUNCTION, AND INTERACTION WITH UBE2V2.
PubMed=14562038; DOI=10.1038/sj.onc.1206831;
Bothos J., Summers M.K., Venere M., Scolnick D.M., Halazonetis T.D.;
"The Chfr mitotic checkpoint protein functions with Ubc13-Mms2 to form
Lys63-linked polyubiquitin chains.";
Oncogene 22:7101-7107(2003).
[8]
MUTAGENESIS OF LYS-92 AND LYS-94, AND ISGYLATION AT LYS-92.
PubMed=16112642; DOI=10.1016/j.bbrc.2005.08.034;
Takeuchi T., Yokosawa H.;
"ISG15 modification of Ubc13 suppresses its ubiquitin-conjugating
activity.";
Biochem. Biophys. Res. Commun. 336:9-13(2005).
[9]
INTERACTION WITH SHPRH, AND MUTAGENESIS OF CYS-87.
PubMed=17130289; DOI=10.1083/jcb.200606145;
Motegi A., Sood R., Moinova H., Markowitz S.D., Liu P.P., Myung K.;
"Human SHPRH suppresses genomic instability through proliferating cell
nuclear antigen polyubiquitination.";
J. Cell Biol. 175:703-708(2006).
[10]
INTERACTION WITH RNF8.
PubMed=16215985; DOI=10.1002/jcb.20587;
Plans V., Scheper J., Soler M., Loukili N., Okano Y., Thomson T.M.;
"The RING finger protein RNF8 recruits UBC13 for lysine 63-based self
polyubiquitylation.";
J. Cell. Biochem. 97:572-582(2006).
[11]
INTERACTION WITH SHPRH.
PubMed=17108083; DOI=10.1073/pnas.0608595103;
Unk I., Hajdu I., Fatyol K., Szakal B., Blastyak A., Bermudez V.,
Hurwitz J., Prakash L., Prakash S., Haracska L.;
"Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependent
polyubiquitylation of proliferating cell nuclear antigen.";
Proc. Natl. Acad. Sci. U.S.A. 103:18107-18112(2006).
[12]
MUTAGENESIS OF CYS-87.
PubMed=17135271; DOI=10.1074/jbc.M609503200;
Lamothe B., Besse A., Campos A.D., Webster W.K., Wu H., Darnay B.G.;
"Site-specific Lys-63-linked tumor necrosis factor receptor-associated
factor 6 auto-ubiquitination is a critical determinant of I kappa B
kinase activation.";
J. Biol. Chem. 282:4102-4112(2007).
[13]
INTERACTION WITH HLTF.
PubMed=18316726; DOI=10.1073/pnas.0800563105;
Unk I., Hajdu I., Fatyol K., Hurwitz J., Yoon J.-H., Prakash L.,
Prakash S., Haracska L.;
"Human HLTF functions as a ubiquitin ligase for proliferating cell
nuclear antigen polyubiquitination.";
Proc. Natl. Acad. Sci. U.S.A. 105:3768-3773(2008).
[14]
INTERACTION WITH HLTF.
PubMed=18719106; DOI=10.1073/pnas.0805685105;
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.;
"Polyubiquitination of proliferating cell nuclear antigen by HLTF and
SHPRH prevents genomic instability from stalled replication forks.";
Proc. Natl. Acad. Sci. U.S.A. 105:12411-12416(2008).
[15]
INTERACTION WITH RNF168.
PubMed=19203578; DOI=10.1016/j.cell.2008.12.042;
Stewart G.S., Panier S., Townsend K., Al-Hakim A.K., Kolas N.K.,
Miller E.S., Nakada S., Ylanko J., Olivarius S., Mendez M.,
Oldreive C., Wildenhain J., Tagliaferro A., Pelletier L.,
Taubenheim N., Durandy A., Byrd P.J., Stankovic T., Taylor A.M.R.,
Durocher D.;
"The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling
cascade at sites of DNA damage.";
Cell 136:420-434(2009).
[16]
FUNCTION IN UBIQUITINATION OF JKAMP.
PubMed=19269966; DOI=10.1074/jbc.M808222200;
Tcherpakov M., Delaunay A., Toth J., Kadoya T., Petroski M.D.,
Ronai Z.A.;
"Regulation of endoplasmic reticulum-associated degradation by RNF5-
dependent ubiquitination of JNK-associated membrane protein (JAMP).";
J. Biol. Chem. 284:12099-12109(2009).
[17]
INTERACTION WITH ARIH2, AND SUBCELLULAR LOCATION.
PubMed=19340006; DOI=10.1038/leu.2009.57;
Marteijn J.A., van der Meer L.T., Smit J.J., Noordermeer S.M.,
Wissink W., Jansen P., Swarts H.G., Hibbert R.G., de Witte T.,
Sixma T.K., Jansen J.H., van der Reijden B.A.;
"The ubiquitin ligase Triad1 inhibits myelopoiesis through UbcH7 and
Ubc13 interacting domains.";
Leukemia 23:1480-1489(2009).
[18]
INTERACTION WITH RNF11.
PubMed=18615712; DOI=10.1002/prot.22120;
Scheper J., Oliva B., Villa-Freixa J., Thomson T.M.;
"Analysis of electrostatic contributions to the selectivity of
interactions between RING-finger domains and ubiquitin-conjugating
enzymes.";
Proteins 74:92-103(2009).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-82, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[20]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=20061386; DOI=10.1074/jbc.M109.089003;
David Y., Ziv T., Admon A., Navon A.;
"The E2 ubiquitin-conjugating enzymes direct polyubiquitination to
preferred lysines.";
J. Biol. Chem. 285:8595-8604(2010).
[21]
ENZYME REGULATION, AND INTERACTION WITH OTUB1.
PubMed=20725033; DOI=10.1038/nature09297;
Nakada S., Tai I., Panier S., Al-Hakim A., Iemura S., Juang Y.C.,
O'Donnell L., Kumakubo A., Munro M., Sicheri F., Gingras A.C.,
Natsume T., Suda T., Durocher D.;
"Non-canonical inhibition of DNA damage-dependent ubiquitination by
OTUB1.";
Nature 466:941-946(2010).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[23]
FUNCTION.
PubMed=21512573; DOI=10.1038/nature09976;
Pertel T., Hausmann S., Morger D., Zueger S., Guerra J., Lascano J.,
Reinhard C., Santoni F.A., Uchil P.D., Chatel L., Bisiaux A.,
Albert M.L., Strambio-De-Castillia C., Mothes W., Pizzato M.,
Gruetter M.G., Luban J.;
"TRIM5 is an innate immune sensor for the retrovirus capsid lattice.";
Nature 472:361-365(2011).
[24]
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=21659603; DOI=10.1126/science.1203430;
Cotta-Ramusino C., McDonald E.R. III, Hurov K., Sowa M.E.,
Harper J.W., Elledge S.J.;
"A DNA damage response screen identifies RHINO, a 9-1-1 and TopBP1
interacting protein required for ATR signaling.";
Science 332:1313-1317(2011).
[25]
ISGYLATION, AND DISULFIDE BOND.
PubMed=22693631; DOI=10.1371/journal.pone.0038294;
Bade V.N., Nickels J., Keusekotten K., Praefcke G.J.;
"Covalent protein modification with ISG15 via a conserved cysteine in
the hinge region.";
PLoS ONE 7:E38294-E38294(2012).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[27]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH UBE2V2.
PubMed=11473255; DOI=10.1038/90373;
Moraes T.F., Edwards R.A., McKenna S., Pastushok L., Xiao W.,
Glover J.N.M., Ellison M.J.;
"Crystal structure of the human ubiquitin conjugating enzyme complex,
hMms2-hUbc13.";
Nat. Struct. Biol. 8:669-673(2001).
[28]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 2-152 IN COMPLEX WITH STUB1
AND UBE2V1.
PubMed=16307917; DOI=10.1016/j.molcel.2005.09.023;
Zhang M., Windheim M., Roe S.M., Peggie M., Cohen P., Prodromou C.,
Pearl L.H.;
"Chaperoned ubiquitylation -- crystal structures of the CHIP U box E3
ubiquitin ligase and a CHIP-Ubc13-Uev1a complex.";
Mol. Cell 20:525-538(2005).
[29]
X-RAY CRYSTALLOGRAPHY (4.8 ANGSTROMS) OF 1-150 IN COMPLEX WITH RNF8
AND UBE2V2.
PubMed=22589545; DOI=10.1074/jbc.M112.359653;
Campbell S.J., Edwards R.A., Leung C.C., Neculai D., Hodge C.D.,
Dhe-Paganon S., Glover J.N.;
"Molecular insights into the function of RING Finger (RNF)-containing
proteins hRNF8 and hRNF168 in Ubc13/Mms2-dependent ubiquitylation.";
J. Biol. Chem. 287:23900-23910(2012).
[30]
X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 25-271 IN COMPLEX WITH UBE2V2
AND OTUB1, ENZYME REGULATION, AND INTERACTION WITH OTUB1.
PubMed=22325355; DOI=10.1016/j.molcel.2012.01.011;
Juang Y.C., Landry M.C., Sanches M., Vittal V., Leung C.C.,
Ceccarelli D.F., Mateo A.R., Pruneda J.N., Mao D.Y., Szilard R.K.,
Orlicky S., Munro M., Brzovic P.S., Klevit R.E., Sicheri F.,
Durocher D.;
"OTUB1 co-opts Lys48-linked ubiquitin recognition to suppress E2
enzyme function.";
Mol. Cell 45:384-397(2012).
[31]
X-RAY CRYSTALLOGRAPHY (3.11 ANGSTROMS) IN COMPLEX WITH OUTB1 AND
UBIQUITIN, ENZYME REGULATION, AND INTERACTION WITH OTUB1.
PubMed=22367539; DOI=10.1038/nature10911;
Wiener R., Zhang X., Wang T., Wolberger C.;
"The mechanism of OTUB1-mediated inhibition of ubiquitination.";
Nature 483:618-622(2012).
-!- 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. 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. {ECO:0000269|PubMed:10089880,
ECO:0000269|PubMed:14562038, ECO:0000269|PubMed:19269966,
ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:21512573}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E1 ubiquitin-activating
enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
= [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2
ubiquitin-conjugating enzyme]-L-cysteine. {ECO:0000255|PROSITE-
ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133,
ECO:0000269|PubMed:20061386}.
-!- ENZYME REGULATION: Activity is inhibited by binding to OTUB1,
which prevents 'Lys-63'-linked polyubiquitination.
{ECO:0000269|PubMed:20725033, ECO:0000269|PubMed:22325355,
ECO:0000269|PubMed:22367539}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-!- SUBUNIT: 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. {ECO:0000269|PubMed:10089880,
ECO:0000269|PubMed:11473255, ECO:0000269|PubMed:14562038,
ECO:0000269|PubMed:16215985, ECO:0000269|PubMed:16307917,
ECO:0000269|PubMed:17108083, ECO:0000269|PubMed:17130289,
ECO:0000269|PubMed:18316726, ECO:0000269|PubMed:18615712,
ECO:0000269|PubMed:18719106, ECO:0000269|PubMed:19203578,
ECO:0000269|PubMed:19340006, ECO:0000269|PubMed:20725033,
ECO:0000269|PubMed:22325355, ECO:0000269|PubMed:22367539,
ECO:0000269|PubMed:22589545}.
-!- INTERACTION:
Q13489:BIRC3; NbExp=2; IntAct=EBI-1052908, EBI-517709;
Q14527:HLTF; NbExp=4; IntAct=EBI-1052908, EBI-1045161;
Q6UWE0:LRSAM1; NbExp=3; IntAct=EBI-1052908, EBI-720984;
Q62925:Map3k1 (xeno); NbExp=45; IntAct=EBI-1052908, EBI-636664;
Q8VSD5:ORF169b (xeno); NbExp=2; IntAct=EBI-1052908, EBI-15974371;
Q9XVR6:otub-1 (xeno); NbExp=2; IntAct=EBI-1052908, EBI-316044;
Q96FW1-1:OTUB1; NbExp=5; IntAct=EBI-1052908, EBI-15972141;
Q9BYM8:RBCK1; NbExp=2; IntAct=EBI-1052908, EBI-2340624;
Q6PCD5:RFWD3; NbExp=2; IntAct=EBI-1052908, EBI-2129159;
Q9Y3C5:RNF11; NbExp=4; IntAct=EBI-1052908, EBI-396669;
O43567:RNF13; NbExp=2; IntAct=EBI-1052908, EBI-2129183;
Q8IYW5:RNF168; NbExp=2; IntAct=EBI-1052908, EBI-914207;
Q8N6D2:RNF182; NbExp=2; IntAct=EBI-1052908, EBI-2130099;
Q149N8-1:SHPRH; NbExp=2; IntAct=EBI-1052908, EBI-15612386;
Q9UNE7:STUB1; NbExp=5; IntAct=EBI-1052908, EBI-357085;
Q9WUD1:Stub1 (xeno); NbExp=2; IntAct=EBI-1052908, EBI-773027;
Q9Y4K3:TRAF6; NbExp=8; IntAct=EBI-1052908, EBI-359276;
Q13049:TRIM32; NbExp=3; IntAct=EBI-1052908, EBI-742790;
Q13404:UBE2V1; NbExp=18; IntAct=EBI-1052908, EBI-1050671;
Q13404-2:UBE2V1; NbExp=2; IntAct=EBI-1052908, EBI-15972179;
Q15819:UBE2V2; NbExp=4; IntAct=EBI-1052908, EBI-714329;
P98170:XIAP; NbExp=2; IntAct=EBI-1052908, EBI-517127;
Q8ND25:ZNRF1; NbExp=4; IntAct=EBI-1052908, EBI-2129250;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19340006}.
Cytoplasm {ECO:0000269|PubMed:19340006}.
-!- PTM: Conjugation to ISG15 impairs formation of the thioester bond
with ubiquitin but not interaction with UBE2V2.
{ECO:0000269|PubMed:16112642}.
-!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
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EMBL; D83004; BAA11675.1; -; mRNA.
EMBL; BT006873; AAP35519.1; -; mRNA.
EMBL; BC000396; AAH00396.1; -; mRNA.
EMBL; BC003365; AAH03365.1; -; mRNA.
EMBL; BC108704; AAI08705.1; -; mRNA.
CCDS; CCDS31875.1; -.
PIR; JC4894; JC4894.
RefSeq; NP_003339.1; NM_003348.3.
UniGene; Hs.524630; -.
PDB; 1J7D; X-ray; 1.85 A; B=1-152.
PDB; 2C2V; X-ray; 2.90 A; B/E/H/K=2-152.
PDB; 3HCT; X-ray; 2.10 A; B=1-152.
PDB; 3HCU; X-ray; 2.60 A; B/D=1-152.
PDB; 3VON; X-ray; 3.15 A; C/E/G/J/L/N/Q/S/U/X/Z/b/e/g/i/l/n/p=3-150.
PDB; 3W31; X-ray; 2.96 A; B=1-152.
PDB; 4DHI; X-ray; 1.80 A; D=1-152.
PDB; 4DHJ; X-ray; 2.35 A; C/G/K/N=1-152.
PDB; 4DHZ; X-ray; 3.11 A; F=1-152.
PDB; 4IP3; X-ray; 2.30 A; B=1-152.
PDB; 4NR3; X-ray; 1.80 A; B=2-150.
PDB; 4NRG; X-ray; 1.95 A; B=1-152.
PDB; 4NRI; X-ray; 2.30 A; B=3-150.
PDB; 4ONL; X-ray; 1.35 A; B=1-152.
PDB; 4ONM; X-ray; 1.35 A; B=1-152.
PDB; 4ONN; X-ray; 1.50 A; B=1-152.
PDB; 4ORH; X-ray; 4.80 A; B/F/J=1-152.
PDB; 4TKP; X-ray; 2.08 A; A=2-152.
PDB; 4WHV; X-ray; 8.30 A; B/E/H/K=1-152.
PDB; 5AIT; X-ray; 3.40 A; B/E=1-152.
PDB; 5AIU; X-ray; 2.21 A; B/E=1-152.
PDB; 5EYA; X-ray; 2.40 A; A/B=1-152.
PDBsum; 1J7D; -.
PDBsum; 2C2V; -.
PDBsum; 3HCT; -.
PDBsum; 3HCU; -.
PDBsum; 3VON; -.
PDBsum; 3W31; -.
PDBsum; 4DHI; -.
PDBsum; 4DHJ; -.
PDBsum; 4DHZ; -.
PDBsum; 4IP3; -.
PDBsum; 4NR3; -.
PDBsum; 4NRG; -.
PDBsum; 4NRI; -.
PDBsum; 4ONL; -.
PDBsum; 4ONM; -.
PDBsum; 4ONN; -.
PDBsum; 4ORH; -.
PDBsum; 4TKP; -.
PDBsum; 4WHV; -.
PDBsum; 5AIT; -.
PDBsum; 5AIU; -.
PDBsum; 5EYA; -.
ProteinModelPortal; P61088; -.
SMR; P61088; -.
BioGrid; 113182; 210.
CORUM; P61088; -.
DIP; DIP-29829N; -.
IntAct; P61088; 138.
MINT; MINT-5001139; -.
STRING; 9606.ENSP00000316176; -.
BindingDB; P61088; -.
ChEMBL; CHEMBL6089; -.
iPTMnet; P61088; -.
PhosphoSitePlus; P61088; -.
SwissPalm; P61088; -.
BioMuta; UBE2N; -.
DMDM; 46577660; -.
OGP; Q16781; -.
REPRODUCTION-2DPAGE; IPI00003949; -.
EPD; P61088; -.
PaxDb; P61088; -.
PeptideAtlas; P61088; -.
PRIDE; P61088; -.
TopDownProteomics; P61088; -.
DNASU; 7334; -.
Ensembl; ENST00000318066; ENSP00000316176; ENSG00000177889.
GeneID; 7334; -.
KEGG; hsa:7334; -.
CTD; 7334; -.
DisGeNET; 7334; -.
EuPathDB; HostDB:ENSG00000177889.9; -.
GeneCards; UBE2N; -.
HGNC; HGNC:12492; UBE2N.
HPA; HPA044976; -.
MIM; 603679; gene.
neXtProt; NX_P61088; -.
OpenTargets; ENSG00000177889; -.
PharmGKB; PA37141; -.
eggNOG; KOG0417; Eukaryota.
eggNOG; COG5078; LUCA.
GeneTree; ENSGT00540000070023; -.
HOGENOM; HOG000233455; -.
HOVERGEN; HBG063308; -.
InParanoid; P61088; -.
KO; K10580; -.
OMA; IDKWSPA; -.
PhylomeDB; P61088; -.
TreeFam; TF101126; -.
BRENDA; 2.3.2.B6; 2681.
Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
Reactome; R-HSA-168927; TICAM1, RIP1-mediated IKK complex recruitment.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-HSA-446652; Interleukin-1 family signaling.
Reactome; R-HSA-450302; activated TAK1 mediates p38 MAPK activation.
Reactome; R-HSA-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER.
Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
Reactome; R-HSA-937039; IRAK1 recruits IKK complex.
Reactome; R-HSA-937041; IKK complex recruitment mediated by RIP1.
Reactome; R-HSA-975110; TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
Reactome; R-HSA-975144; IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SignaLink; P61088; -.
SIGNOR; P61088; -.
UniPathway; UPA00143; -.
ChiTaRS; UBE2N; human.
EvolutionaryTrace; P61088; -.
GeneWiki; UBE2N; -.
GenomeRNAi; 7334; -.
PRO; PR:P61088; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000177889; -.
CleanEx; HS_UBE2N; -.
ExpressionAtlas; P61088; baseline and differential.
Genevisible; P61088; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0001650; C:fibrillar center; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:MGI.
GO; GO:0031372; C:UBC13-MMS2 complex; IDA:HGNC.
GO; GO:0035370; C:UBC13-UEV1A complex; IDA:UniProtKB.
GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0043130; F:ubiquitin binding; IDA:HGNC.
GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:Ensembl.
GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0000187; P:activation of MAPK activity; TAS:Reactome.
GO; GO:0006464; P:cellular protein modification process; TAS:ProtInc.
GO; GO:0000729; P:DNA double-strand break processing; IMP:HGNC.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:HGNC.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; TAS:Reactome.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0070911; P:global genome nucleotide-excision repair; TAS:Reactome.
GO; GO:0016574; P:histone ubiquitination; IMP:HGNC.
GO; GO:0007254; P:JNK cascade; TAS:Reactome.
GO; GO:0070423; P:nucleotide-binding oligomerization domain containing signaling pathway; TAS:Reactome.
GO; GO:0045739; P:positive regulation of DNA repair; IMP:HGNC.
GO; GO:0031058; P:positive regulation of histone modification; IMP:HGNC.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:HGNC.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; IMP:HGNC.
GO; GO:0006301; P:postreplication repair; IMP:HGNC.
GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IMP:HGNC.
GO; GO:0006508; P:proteolysis; TAS:ProtInc.
GO; GO:0006282; P:regulation of DNA repair; TAS:ProtInc.
GO; GO:0033182; P:regulation of histone ubiquitination; IMP:HGNC.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; IMP:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:Ensembl.
CDD; cd00195; UBCc; 1.
Gene3D; 3.10.110.10; -; 1.
InterPro; IPR000608; UBQ-conjugat_E2.
InterPro; IPR023313; UBQ-conjugating_AS.
InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
Pfam; PF00179; UQ_con; 1.
SUPFAM; SSF54495; SSF54495; 1.
PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1.
PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Complete proteome; Cytoplasm;
Direct protein sequencing; Disulfide bond; DNA damage; DNA repair;
Isopeptide bond; Nucleotide-binding; Nucleus; Reference proteome;
Transferase; Ubl conjugation; Ubl conjugation pathway.
CHAIN 1 152 Ubiquitin-conjugating enzyme E2 N.
/FTId=PRO_0000082502.
ACT_SITE 87 87 Glycyl thioester intermediate.
MOD_RES 82 82 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
DISULFID 87 87 Interchain (with C-78 in ISG15).
{ECO:0000269|PubMed:22693631}.
CROSSLNK 92 92 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ISG15).
{ECO:0000269|PubMed:16112642,
ECO:0000269|PubMed:16122702}.
MUTAGEN 87 87 C->A: Loss of polyubiquitination of PCNA.
Impairs interaction with SHPRH.
{ECO:0000269|PubMed:17130289,
ECO:0000269|PubMed:17135271}.
MUTAGEN 92 92 K->R: No ISGylation.
{ECO:0000269|PubMed:16112642,
ECO:0000269|PubMed:16122702}.
MUTAGEN 94 94 K->R: No effect on ISGylation.
{ECO:0000269|PubMed:16112642}.
HELIX 6 17 {ECO:0000244|PDB:4ONL}.
STRAND 23 27 {ECO:0000244|PDB:4ONL}.
STRAND 34 40 {ECO:0000244|PDB:4ONL}.
TURN 46 49 {ECO:0000244|PDB:4ONL}.
STRAND 51 57 {ECO:0000244|PDB:4ONL}.
TURN 60 64 {ECO:0000244|PDB:4ONL}.
STRAND 68 71 {ECO:0000244|PDB:4ONL}.
STRAND 78 80 {ECO:0000244|PDB:5AIT}.
HELIX 89 91 {ECO:0000244|PDB:4ONL}.
TURN 92 94 {ECO:0000244|PDB:4ONM}.
HELIX 101 113 {ECO:0000244|PDB:4ONL}.
STRAND 121 123 {ECO:0000244|PDB:4ONL}.
HELIX 124 131 {ECO:0000244|PDB:4ONL}.
HELIX 133 147 {ECO:0000244|PDB:4ONL}.
STRAND 148 150 {ECO:0000244|PDB:4DHI}.
SEQUENCE 152 AA; 17138 MW; FACD84D883D77407 CRC64;
MAGLPRRIIK ETQRLLAEPV PGIKAEPDES NARYFHVVIA GPQDSPFEGG TFKLELFLPE
EYPMAAPKVR FMTKIYHPNV DKLGRICLDI LKDKWSPALQ IRTVLLSIQA LLSAPNPDDP
LANDVAEQWK TNEAQAIETA RAWTRLYAMN NI


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