ID   UB2L3_PONAB             Reviewed;         154 AA.
AC   Q5R5I4;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 L3;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme L3;
DE   AltName: Full=Ubiquitin carrier protein L3;
DE   AltName: Full=Ubiquitin-protein ligase L3;
GN   Name=UBE2L3;
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=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Ubiquitin-conjugating enzyme E2 that specifically acts with
CC       HECT-type and RBR family E3 ubiquitin-protein ligases. Does not
CC       function with most RING-containing E3 ubiquitin-protein ligases because
CC       it lacks intrinsic E3-independent reactivity with lysine: in contrast,
CC       it has activity with the RBR family E3 enzymes, such as PRKN, RNF31 and
CC       ARIH1, that function like RING-HECT hybrids. Accepts ubiquitin from the
CC       E1 complex and catalyzes its covalent attachment to other proteins. In
CC       vitro catalyzes 'Lys-11'-linked polyubiquitination. Involved in the
CC       selective degradation of short-lived and abnormal proteins. Down-
CC       regulated during the S-phase it is involved in progression through the
CC       cell cycle. Regulates nuclear hormone receptors transcriptional
CC       activity. May play a role in myelopoiesis.
CC       {ECO:0000250|UniProtKB:P68036}.
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   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SUBUNIT: Interacts with PRKN; involved in ubiquitination and
CC       degradation of misfolded proteins. Interacts with UBE3A. Interacts with
CC       CCNB1IP1, CBL, ZAP70, RNF19A, RNF19B and RNF144B. Interacts with ARIH1.
CC       Interacts with ARIH2 (via RING-type 1). Interacts with NCOA1; they
CC       functionally interact to regulate progesterone receptor transcriptional
CC       activity. Interacts with NDFIP1 (via N-terminus); the interaction
CC       mediates recruitment of UBE2L3 to ITCH and causes MAP3K7
CC       ubiquitination. {ECO:0000250|UniProtKB:P68036}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P68036}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P68036}.
CC   -!- DOMAIN: In contrast to other ubiquitin-conjugating enzymes E2, residues
CC       essential for lysine reactivity are absent: Pro and a His residues are
CC       present instead of an Asp and an Asp residues in positions 88 and 119,
CC       respectively. {ECO:0000250|UniProtKB:P68036}.
CC   -!- PTM: Ubiquitinated. The alteration of UBE2L3 protein levels during the
CC       S-phase of the cell cycle is due to ubiquitin-dependent proteasomal
CC       degradation. Autoubiquitinated in vitro.
CC       {ECO:0000250|UniProtKB:P68036}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; CR860875; CAH92982.1; -; mRNA.
DR   RefSeq; NP_001127614.1; NM_001134142.1.
DR   AlphaFoldDB; Q5R5I4; -.
DR   BMRB; Q5R5I4; -.
DR   SMR; Q5R5I4; -.
DR   STRING; 9601.ENSPPYP00000012943; -.
DR   GeneID; 100174693; -.
DR   KEGG; pon:100174693; -.
DR   CTD; 7332; -.
DR   eggNOG; KOG0422; Eukaryota.
DR   InParanoid; Q5R5I4; -.
DR   OrthoDB; 5486024at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
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:0044770; P:cell cycle phase transition; ISS:UniProtKB.
DR   GO; GO:0008283; P:cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0071385; P:cellular response to glucocorticoid stimulus; ISS:UniProtKB.
DR   GO; GO:0071383; P:cellular response to steroid hormone stimulus; ISS:UniProtKB.
DR   GO; GO:0070979; P:protein K11-linked ubiquitination; ISS:UniProtKB.
DR   GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; ISS:UniProtKB.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR24067:SF370; UBIQUITIN-CONJUGATING ENZYME; 1.
DR   PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS00183; UBC_1; 1.
DR   PROSITE; PS50127; UBC_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation; Transferase;
KW   Ubl conjugation; Ubl conjugation pathway.
FT   CHAIN           1..154
FT                   /note="Ubiquitin-conjugating enzyme E2 L3"
FT                   /id="PRO_0000281856"
FT   DOMAIN          2..149
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   ACT_SITE        86
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
FT   MOD_RES         131
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P68036"
SQ   SEQUENCE   154 AA;  17890 MW;  F4BC0093BE3C9B55 CRC64;
     MAASRRLMKE LEEIRKCGMK NFRNIRVDEA NLLTWQGLIV PDNPPYDKGA FRIEINFPAE
     YPFKPPKITF KTKIYHPNID EKGQVCLPVI SAENWKPATK TDQVIQSLIA LVNDPQPEHP
     LRADLAEEYS KDRKKFCKNA EEFTKKYGEK RPVD
//