ID UBE2N_PONAB Reviewed; 152 AA.
AC Q5R7J6;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 01-MAY-2013, entry version 66.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 N;
DE EC=6.3.2.19;
DE AltName: Full=Ubiquitin carrier protein N;
DE AltName: Full=Ubiquitin-protein ligase N;
GN Name=UBE2N;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The UBE2V1-UBE2N and UBE2V2-UBE2N heterodimers catalyze
CC the synthesis of non-canonical 'Lys-63'-linked polyubiquitin
CC chains. This type of polyubiquitination does not lead to protein
CC degradation by the proteasome. Mediates transcriptional activation
CC of target genes. Plays a role in the control of progress through
CC the cell cycle and differentiation. Plays a role in the error-free
CC DNA repair pathway and contributes to the survival of cells after
CC DNA damage. Acts together with the E3 ligases, HLTF and SHPRH, in
CC the 'Lys-63'-linked poly-ubiquitination of PCNA upon genotoxic
CC stress, which is required for DNA repair. Appears to act together
CC with E3 ligase RNF5 in the 'Lys-63'-linked polyubiquitination of
CC JKAMP thereby regulating JKAMP function by decreasing its
CC association with components of the proteasome and ERAD (By
CC similarity). Promotes TRIM5 capsid-specific restriction activity
CC and the UBE2V1-UBE2N heterodimer acts in concert with TRIM5 to
CC generate 'Lys-63'-linked polyubiquitin chains which activate the
CC MAP3K7/TAK1 complex which in turn results in the induction and
CC expression of NF-kappa-B and MAPK-responsive inflammatory genes
CC (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP +
CC diphosphate + protein N-ubiquityllysine.
CC -!- ENZYME REGULATION: Activity is inhibited by binding to OTUB1,
CC which prevents 'Lys-63'-linked polyubiquitination (By similarity).
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Heterodimer with UBE2V2. Interacts (UBE2V2-UBE2N
CC heterodimer) with the E3 ligase STUB1 (via the U-box domain); the
CC complex has a specific 'Lys-63'-linked polyubiquitination
CC activity. Interacts with RNF8 and RNF168. Interacts with RNF11.
CC Interacts with the E3 ligases, HLTF and SHPRH; the interactions
CC promote the 'Lys-63'-linked polyubiquitination of PCNA upon
CC genotoxic stress and lead to DNA repair. Interacts with ARIH2 (via
CC RING-type 2). Interacts with OTUB1; leading to inhibit E2-
CC conjugating activity (By similarity).
CC -!- PTM: Conjugation to ISG15 impairs formation of the thioester bond
CC with ubiquitin but not interaction with UBE2V2 (By similarity).
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
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DR EMBL; CR860119; CAH92264.1; -; mRNA.
DR RefSeq; NP_001127530.1; NM_001134058.1.
DR UniGene; Pab.18824; -.
DR ProteinModelPortal; Q5R7J6; -.
DR PRIDE; Q5R7J6; -.
DR Ensembl; ENSPPYT00000005723; ENSPPYP00000005510; ENSPPYG00000004832.
DR GeneID; 100174607; -.
DR KEGG; pon:100174607; -.
DR CTD; 7334; -.
DR GeneTree; ENSGT00540000070023; -.
DR HOVERGEN; HBG063308; -.
DR InParanoid; Q5R7J6; -.
DR KO; K10580; -.
DR OMA; DDNLRYF; -.
DR UniPathway; UPA00143; -.
DR BindingDB; Q5R7J6; -.
DR GO; GO:0005634; C:nucleus; IEA:Compara.
DR GO; GO:0031372; C:UBC13-MMS2 complex; IEA:Compara.
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:0004842; F:ubiquitin-protein ligase activity; ISS:UniProtKB.
DR GO; GO:0000729; P:DNA double-strand break processing; IEA:Compara.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:Compara.
DR GO; GO:0016574; P:histone ubiquitination; IEA:Compara.
DR GO; GO:0045739; P:positive regulation of DNA repair; IEA:Compara.
DR GO; GO:0031058; P:positive regulation of histone modification; IEA:Compara.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IEA:Compara.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Compara.
DR GO; GO:0051443; P:positive regulation of ubiquitin-protein ligase activity; IEA:Compara.
DR GO; GO:0006301; P:postreplication repair; IEA:Compara.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0033182; P:regulation of histone ubiquitination; IEA:Compara.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IEA:Compara.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:Compara.
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; UBQ-conjugat/RWD-like; 1.
DR PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1.
DR PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Complete proteome; DNA damage; DNA repair;
KW Isopeptide bond; Ligase; Nucleotide-binding; Reference proteome;
KW Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1 152 Ubiquitin-conjugating enzyme E2 N.
FT /FTId=PRO_0000082505.
FT ACT_SITE 87 87 Glycyl thioester intermediate.
FT MOD_RES 82 82 N6-acetyllysine (By similarity).
FT CROSSLNK 92 92 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ISG15) (By
FT similarity).
SQ SEQUENCE 152 AA; 17138 MW; FACD84D883D77407 CRC64;
MAGLPRRIIK ETQRLLAEPV PGIKAEPDES NARYFHVVIA GPQDSPFEGG TFKLELFLPE
EYPMAAPKVR FMTKIYHPNV DKLGRICLDI LKDKWSPALQ IRTVLLSIQA LLSAPNPDDP
LANDVAEQWK TNEAQAIETA RAWTRLYAMN NI
//
