UBE2N_MACFA
ID UBE2N_MACFA Reviewed; 152 AA.
AC Q4R4I1;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 N;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme N;
DE AltName: Full=Ubiquitin carrier protein N;
DE AltName: Full=Ubiquitin-protein ligase N;
GN Name=UBE2N; ORFNames=QtrA-13863;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Temporal cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The UBE2V1-UBE2N and UBE2V2-UBE2N heterodimers catalyze the
CC synthesis of non-canonical 'Lys-63'-linked polyubiquitin chains. This
CC type of polyubiquitination does not lead to protein degradation by the
CC proteasome. Mediates transcriptional activation of target genes. Plays
CC a role in the control of progress through the cell cycle and
CC differentiation. Plays a role in the error-free DNA repair pathway and
CC contributes to the survival of cells after DNA damage. Acts together
CC with the E3 ligases, HLTF and SHPRH, in the 'Lys-63'-linked poly-
CC ubiquitination of PCNA upon genotoxic stress, which is required for DNA
CC repair. Appears to act together with E3 ligase RNF5 in the 'Lys-63'-
CC linked polyubiquitination of JKAMP thereby regulating JKAMP function by
CC decreasing its association with components of the proteasome and ERAD.
CC Promotes TRIM5 capsid-specific restriction activity and the UBE2V1-
CC UBE2N heterodimer acts in concert with TRIM5 to generate 'Lys-63'-
CC linked polyubiquitin chains which activate the MAP3K7/TAK1 complex
CC which in turn results in the induction and expression of NF-kappa-B and
CC MAPK-responsive inflammatory genes. Together with RNF135 and UB2V1,
CC catalyzes the viral RNA-dependent 'Lys-63'-linked polyubiquitination of
CC RIG-I/DDX58 to activate the downstream signaling pathway that leads to
CC interferon beta production (By similarity). UBE2V1-UBE2N together with
CC TRAF3IP2 E3 ubiquitin ligase mediate 'Lys-63'-linked polyubiquitination
CC of TRAF6, a component of IL17A-mediated signaling pathway.
CC {ECO:0000250|UniProtKB:P61088}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-
CC ProRule:PRU10133};
CC -!- ACTIVITY REGULATION: Activity is inhibited by binding to OTUB1, which
CC prevents 'Lys-63'-linked polyubiquitination.
CC {ECO:0000250|UniProtKB:P61088}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SUBUNIT: Heterodimer with UBE2V2. Interacts (UBE2V2-UBE2N heterodimer)
CC with the E3 ligase STUB1 (via the U-box domain); the complex has a
CC specific 'Lys-63'-linked polyubiquitination activity. Interacts with
CC RNF8 and RNF168. Interacts with RNF11. Interacts with the E3 ligases,
CC HLTF and SHPRH; the interactions promote the 'Lys-63'-linked
CC polyubiquitination of PCNA upon genotoxic stress and lead to DNA
CC repair. Interacts with ARIH2 (via RING-type 2). Interacts with OTUB1;
CC leading to inhibit E2-conjugating activity. Interacts with DDX58 and
CC RNF135; involved in DDX58 ubiquitination and activation (By
CC similarity). {ECO:0000250|UniProtKB:P61088}.
CC -!- PTM: Conjugation to ISG15 impairs formation of the thioester bond with
CC ubiquitin but not interaction with UBE2V2.
CC {ECO:0000250|UniProtKB:P61088}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; AB169913; BAE01994.1; -; mRNA.
DR RefSeq; NP_001271807.1; NM_001284878.1.
DR AlphaFoldDB; Q4R4I1; -.
DR BMRB; Q4R4I1; -.
DR SMR; Q4R4I1; -.
DR STRING; 9541.XP_005571918.1; -.
DR GeneID; 101866684; -.
DR CTD; 7334; -.
DR eggNOG; KOG0417; Eukaryota.
DR OrthoDB; 1345547at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0035370; C:UBC13-UEV1A complex; ISS:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:UniProtKB-EC.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; DNA damage; DNA repair; Isopeptide bond;
KW Nucleotide-binding; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..152
FT /note="Ubiquitin-conjugating enzyme E2 N"
FT /id="PRO_0000082503"
FT DOMAIN 3..149
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 87
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT MOD_RES 82
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P61088"
FT CROSSLNK 92
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ISG15)"
FT /evidence="ECO:0000250|UniProtKB:P61088"
SQ SEQUENCE 152 AA; 17112 MW; E27627D883C5F697 CRC64;
MAGLPRRIIK ETQRLLAEPV PGIKAEPDES NARYFHVVIA GPQDSPFEGG TFKLELFLPE
EYPMAAPKVR FMTKIYHPNV DKSGRICLDI LKDKWSPALQ IRTVLLSIQA LLSAPNPDDP
LANDVAEQWK TNEAQAIETA RAWTRLYAMN NI
