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Database: UniProt
Entry: Q5R7J6
LinkDB: Q5R7J6
Original site: Q5R7J6 
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   03-SEP-2014, entry version 75.
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   ProteinModelPortal; Q5R7J6; -.
DR   SMR; Q5R7J6; 3-152.
DR   BindingDB; 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; DVAKHYK; -.
DR   OrthoDB; EOG7XWPQB; -.
DR   TreeFam; TF101126; -.
DR   UniPathway; UPA00143; -.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0031372; C:UBC13-MMS2 complex; IEA:Ensembl.
DR   GO; GO:0035370; C:UBC13-UEV1A complex; ISS:UniProtKB.
DR   GO; GO:0000151; C:ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR   GO; GO:0000729; P:DNA double-strand break processing; IEA:Ensembl.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:Ensembl.
DR   GO; GO:0016574; P:histone ubiquitination; IEA:Ensembl.
DR   GO; GO:0045739; P:positive regulation of DNA repair; IEA:Ensembl.
DR   GO; GO:0031058; P:positive regulation of histone modification; IEA:Ensembl.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
DR   GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; IEA:Ensembl.
DR   GO; GO:0006301; P:postreplication repair; IEA:Ensembl.
DR   GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR   GO; GO:0033182; P:regulation of histone ubiquitination; IEA:Ensembl.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:Ensembl.
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; 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
//
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