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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) (Ubiquitin carrier protein N) (Ubiquitin-protein ligase N)

 UBE2N_MOUSE             Reviewed;         152 AA.
P61089; Q16781; Q3TSL6; Q6ZWZ0; Q9DAJ6;
26-APR-2004, integrated into UniProtKB/Swiss-Prot.
26-APR-2004, sequence version 1.
23-MAY-2018, entry version 158.
RecName: Full=Ubiquitin-conjugating enzyme E2 N;
EC=2.3.2.23 {ECO:0000269|PubMed:22424771, ECO:0000269|PubMed:28039360};
AltName: Full=Bendless-like ubiquitin-conjugating enzyme;
AltName: Full=E2 ubiquitin-conjugating enzyme N;
AltName: Full=Ubc13;
AltName: Full=Ubiquitin carrier protein N;
AltName: Full=Ubiquitin-protein ligase N;
Name=Ube2n; Synonyms=Blu;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=ICR X Swiss Webster;
Rugarli E.I., Valsecchi V., Ballabio A.;
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=B-cell;
PubMed=12039045; DOI=10.1016/S0378-1119(02)00409-2;
Ashley C., Pastushok L., McKenna S., Ellison M.J., Xiao W.;
"Roles of mouse UBC13 in DNA postreplication repair and Lys63-linked
ubiquitination.";
Gene 285:183-191(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Cerebellum, Olfactory bulb, and Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Eye, and Mammary gland;
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).
[5]
PROTEIN SEQUENCE OF 15-24; 34-68; 95-102 AND 131-141, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
Lubec G., Klug S., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[6]
INTERACTION 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).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
FUNCTION, CATALYTIC ACTIVITY, AND ENZYME REGULATION.
PubMed=22424771; DOI=10.1016/j.molcel.2012.01.025;
Cardamone M.D., Krones A., Tanasa B., Taylor H., Ricci L., Ohgi K.A.,
Glass C.K., Rosenfeld M.G., Perissi V.;
"A protective strategy against hyperinflammatory responses requiring
the nontranscriptional actions of GPS2.";
Mol. Cell 46:91-104(2012).
[9]
FUNCTION, CATALYTIC ACTIVITY, AND ENZYME REGULATION.
PubMed=28039360; DOI=10.1074/jbc.M116.755132;
Lentucci C., Belkina A.C., Cederquist C.T., Chan M., Johnson H.E.,
Prasad S., Lopacinski A., Nikolajczyk B.S., Monti S.,
Snyder-Cappione J., Tanasa B., Cardamone M.D., Perissi V.;
"Inhibition of Ubc13-mediated ubiquitination by GPS2 regulates
multiple stages of B Cell development.";
J. Biol. Chem. 292:2754-2772(2017).
[10]
ENZYME REGULATION.
PubMed=28123943; DOI=10.1016/j.molmet.2016.10.007;
Cederquist C.T., Lentucci C., Martinez-Calejman C., Hayashi V.,
Orofino J., Guertin D., Fried S.K., Lee M.J., Cardamone M.D.,
Perissi V.;
"Systemic insulin sensitivity is regulated by GPS2 inhibition of AKT
ubiquitination and activation in adipose tissue.";
Mol. Metab. 6:125-137(2017).
[11]
ENZYME REGULATION.
PubMed=29499132; DOI=10.1016/j.molcel.2018.01.037;
Cardamone M.D., Tanasa B., Cederquist C.T., Huang J., Mahdaviani K.,
Li W., Rosenfeld M.G., Liesa M., Perissi V.;
"Mitochondrial retrograde signaling in mammals is mediated by the
transcriptional cofactor GPS2 via direct mitochondria-to-nucleus
translocation.";
Mol. Cell 69:757-772(2018).
-!- FUNCTION: The UBE2V1-UBE2N and UBE2V2-UBE2N heterodimers catalyze
the synthesis of non-canonical 'Lys-63'-linked polyubiquitin
chains (PubMed:22424771, PubMed:28039360). 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:0000250|UniProtKB:P61088,
ECO:0000269|PubMed:22424771, ECO:0000269|PubMed:28039360}.
-!- 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:22424771, ECO:0000269|PubMed:28039360}.
-!- ENZYME REGULATION: Activity is inhibited by binding to OTUB1,
which prevents 'Lys-63'-linked polyubiquitination (By similarity).
Activity is inhibited by GPS2, leading to prevent 'Lys-63'-linked
polyubiquitination (PubMed:22424771, PubMed:28039360,
PubMed:28123943, PubMed:29499132). {ECO:0000250|UniProtKB:P61088,
ECO:0000269|PubMed:22424771, ECO:0000269|PubMed:28039360,
ECO:0000269|PubMed:28123943, ECO:0000269|PubMed:29499132}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-!- SUBUNIT: Heterodimer with UBE2V2 (By similarity). Interacts
(UBE2V2-UBE2N heterodimer) with the E3 ligase STUB1 (via the U-box
domain); the complex has a specific 'Lys-63'-linked
polyubiquitination activity (By similarity). Interacts with RNF8
and RNF168 (By similarity). Interacts with RNF11 (By similarity).
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 (By similarity). Interacts
with ARIH2 (via RING-type 2) (By similarity). Interacts with
OTUB1; leading to inhibit E2-conjugating activity (By similarity).
Interacts with GPS2; leading to inhibit E2-conjugating activity
(PubMed:22424771). {ECO:0000250|UniProtKB:P61088,
ECO:0000269|PubMed:22424771}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P61088}.
Cytoplasm {ECO:0000250|UniProtKB:P61088}.
-!- PTM: Conjugation to ISG15 impairs formation of the thioester bond
with ubiquitin but not interaction with UBE2V2.
{ECO:0000250|UniProtKB:P61088}.
-!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-!- SEQUENCE CAUTION:
Sequence=BAE36659.1; Type=Frameshift; Positions=105; Evidence={ECO:0000305};
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EMBL; Y09873; CAA71001.1; -; mRNA.
EMBL; AY039837; AAK74128.1; -; mRNA.
EMBL; AK005302; BAB23941.1; -; mRNA.
EMBL; AK005788; BAB24239.1; -; mRNA.
EMBL; AK161968; BAE36659.1; ALT_FRAME; mRNA.
EMBL; BC034898; AAH34898.3; -; mRNA.
EMBL; BC067069; AAH67069.1; -; mRNA.
CCDS; CCDS48677.1; -.
RefSeq; NP_542127.1; NM_080560.3.
UniGene; Mm.371667; -.
UniGene; Mm.440187; -.
UniGene; Mm.486592; -.
ProteinModelPortal; P61089; -.
SMR; P61089; -.
BioGrid; 220301; 21.
CORUM; P61089; -.
IntAct; P61089; 8.
MINT; P61089; -.
STRING; 10090.ENSMUSP00000096932; -.
iPTMnet; P61089; -.
PhosphoSitePlus; P61089; -.
SwissPalm; P61089; -.
REPRODUCTION-2DPAGE; IPI00165854; -.
REPRODUCTION-2DPAGE; P61089; -.
EPD; P61089; -.
MaxQB; P61089; -.
PaxDb; P61089; -.
PRIDE; P61089; -.
TopDownProteomics; P61089; -.
Ensembl; ENSMUST00000099329; ENSMUSP00000096932; ENSMUSG00000074781.
GeneID; 93765; -.
KEGG; mmu:93765; -.
UCSC; uc007gwm.1; mouse.
CTD; 7334; -.
MGI; MGI:1934835; Ube2n.
eggNOG; KOG0417; Eukaryota.
eggNOG; COG5078; LUCA.
GeneTree; ENSGT00540000070023; -.
HOGENOM; HOG000233455; -.
HOVERGEN; HBG063308; -.
InParanoid; P61089; -.
KO; K10580; -.
OMA; IDKWSPA; -.
OrthoDB; EOG091G0VPD; -.
PhylomeDB; P61089; -.
TreeFam; TF101126; -.
UniPathway; UPA00143; -.
PRO; PR:P61089; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000074781; -.
CleanEx; MM_UBE2N; -.
ExpressionAtlas; P61089; baseline and differential.
Genevisible; P61089; MM.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0001650; C:fibrillar center; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0031372; C:UBC13-MMS2 complex; ISS:HGNC.
GO; GO:0035370; C:UBC13-UEV1A complex; ISS:UniProtKB.
GO; GO:0000151; C:ubiquitin ligase complex; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0043130; F:ubiquitin binding; ISS:HGNC.
GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:UniProtKB.
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; ISS:UniProtKB.
GO; GO:0000729; P:DNA double-strand break processing; ISS:HGNC.
GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:HGNC.
GO; GO:0016574; P:histone ubiquitination; ISS:HGNC.
GO; GO:0045739; P:positive regulation of DNA repair; ISS:HGNC.
GO; GO:0031058; P:positive regulation of histone modification; ISS:HGNC.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:HGNC.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:HGNC.
GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; ISS:HGNC.
GO; GO:0006301; P:postreplication repair; ISS:HGNC.
GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; ISS:HGNC.
GO; GO:0033182; P:regulation of histone ubiquitination; ISS:HGNC.
GO; GO:0050852; P:T cell receptor signaling pathway; ISS:HGNC.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:MGI.
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;
Acetylation; ATP-binding; Complete proteome; Cytoplasm;
Direct protein sequencing; 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_0000082504.
ACT_SITE 87 87 Glycyl thioester intermediate.
MOD_RES 82 82 N6-acetyllysine.
{ECO:0000250|UniProtKB:P61088}.
CROSSLNK 92 92 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ISG15).
{ECO:0000250|UniProtKB:P61088}.
CONFLICT 114 114 A -> D (in Ref. 3; BAB24239).
{ECO:0000305}.
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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U1063r CLIA HR6B,RAD6 homolog B,Rad6b,Rat,Rattus norvegicus,Ube2b,Ubiquitin carrier protein B,Ubiquitin-conjugating enzyme E2 B,Ubiquitin-conjugating enzyme E2(14k),Ubiquitin-protein ligase B 96T


 

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