ID   UB2V1_PONAB             Reviewed;         147 AA.
AC   Q5R4Z6;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 variant 1;
DE            Short=UEV-1;
GN   Name=UBE2V1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Has no ubiquitin ligase activity on its own. The UBE2V1-UBE2N
CC       heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin
CC       chains that are linked through 'Lys-63'. This type of poly-
CC       ubiquitination activates IKK and does not seem to involve protein
CC       degradation by the proteasome. Plays a role in the activation of NF-
CC       kappa-B mediated by IL1B, TNF, TRAF6 and TRAF2. Mediates
CC       transcriptional activation of target genes. Plays a role in the control
CC       of progress through the cell cycle and differentiation. Plays a role in
CC       the error-free DNA repair pathway and contributes to the survival of
CC       cells after DNA damage (By similarity). Promotes TRIM5 capsid-specific
CC       restriction activity and the UBE2V1-UBE2N heterodimer acts in concert
CC       with TRIM5 to generate 'Lys-63'-linked polyubiquitin chains which
CC       activate the MAP3K7/TAK1 complex which in turn results in the induction
CC       and expression of NF-kappa-B and MAPK-responsive inflammatory genes (By
CC       similarity). Together with RNF135 and UBE2N, catalyzes the viral RNA-
CC       dependent 'Lys-63'-linked polyubiquitination of RIG-I/DDX58 to activate
CC       the downstream signaling pathway that leads to interferon beta
CC       production (By similarity). UBE2V1-UBE2N together with TRAF3IP2 E3
CC       ubiquitin ligase mediate 'Lys-63'-linked polyubiquitination of TRAF6, a
CC       component of IL17A-mediated signaling pathway. {ECO:0000250,
CC       ECO:0000250|UniProtKB:Q13404}.
CC   -!- SUBUNIT: Heterodimer with UBE2N. 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       TRAF6 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Excluded from the
CC       nucleolus. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; CR861091; CAH93170.1; -; mRNA.
DR   AlphaFoldDB; Q5R4Z6; -.
DR   BMRB; Q5R4Z6; -.
DR   SMR; Q5R4Z6; -.
DR   STRING; 9601.ENSPPYP00000012429; -.
DR   eggNOG; KOG0896; Eukaryota.
DR   eggNOG; KOG3011; Eukaryota.
DR   InParanoid; Q5R4Z6; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0035370; C:UBC13-UEV1A complex; ISS:UniProtKB.
DR   GO; GO:0000151; C:ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR   Gene3D; 3.10.110.10; -; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   Pfam; PF00179; UQ_con; 1.
DR   SUPFAM; SSF54495; SSF54495; 1.
DR   PROSITE; PS50127; UBC_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Nucleus; Reference proteome; Ubl conjugation pathway.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q13404"
FT   CHAIN           2..147
FT                   /note="Ubiquitin-conjugating enzyme E2 variant 1"
FT                   /id="PRO_0000292583"
FT   DOMAIN          12..147
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13404"
SQ   SEQUENCE   147 AA;  16465 MW;  2D0A8163DDD286B5 CRC64;
     MAATMGSGVK VPRNFRLLEE LEEGQKGVGD GTVSWGLEDD EDMTLTRWTG MIIGPPRTIY
     ENRIYSLKIE CGPKCPEAPP FVRFVTKINM NGVNSSNGVV DPRAISVLAK WQNSYSIKVV
     LQELRRLMMS KENMKLPQPP EGQCYSN