ID   U2QL1_MOUSE             Reviewed;         161 AA.
AC   A0PJN4; Q6PDR7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2Q-like protein 1;
DE            EC=2.3.2.23;
DE   AltName: Full=E2Q-like ubiquitin-conjugating enzyme 1;
GN   Name=Ube2ql1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Probable E2 ubiquitin-protein ligase that catalyzes the
CC       covalent attachment of ubiquitin to target proteins. May facilitate the
CC       monoubiquitination and degradation of MTOR and CCNE1 through
CC       interaction with FBXW7. {ECO:0000250|UniProtKB:A1L167}.
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};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SUBUNIT: Interacts with FBXW7. {ECO:0000250|UniProtKB:A1L167}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:A1L167}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI16980.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAI16982.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BC058543; AAH58543.1; -; mRNA.
DR   EMBL; BC116979; AAI16980.1; ALT_INIT; mRNA.
DR   EMBL; BC116981; AAI16982.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001138634.1; NM_001145162.1.
DR   AlphaFoldDB; A0PJN4; -.
DR   SMR; A0PJN4; -.
DR   STRING; 10090.ENSMUSP00000070906; -.
DR   iPTMnet; A0PJN4; -.
DR   PhosphoSitePlus; A0PJN4; -.
DR   PaxDb; A0PJN4; -.
DR   PRIDE; A0PJN4; -.
DR   ProteomicsDB; 298084; -.
DR   DNASU; 76980; -.
DR   GeneID; 76980; -.
DR   KEGG; mmu:76980; -.
DR   CTD; 134111; -.
DR   MGI; MGI:1924230; Ube2ql1.
DR   eggNOG; KOG0897; Eukaryota.
DR   InParanoid; A0PJN4; -.
DR   OrthoDB; 1214134at2759; -.
DR   PhylomeDB; A0PJN4; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 76980; 1 hit in 74 CRISPR screens.
DR   PRO; PR:A0PJN4; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; A0PJN4; protein.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; ISO:MGI.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   CDD; cd00195; UBCc; 1.
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   ATP-binding; Nucleotide-binding; Nucleus; Reference proteome; Transferase;
KW   Ubl conjugation pathway.
FT   CHAIN           1..161
FT                   /note="Ubiquitin-conjugating enzyme E2Q-like protein 1"
FT                   /id="PRO_0000335812"
FT   DOMAIN          1..154
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   ACT_SITE        88
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   CONFLICT        33
FT                   /note="Q -> P (in Ref. 1; AAH58543)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   161 AA;  18364 MW;  A7DC159CFA09DA00 CRC64;
     MKELQDIARL SDRFISVELV NENLFDWNVK LHQVDKDSVL WQDMKETNTE FILLNLTFPD
     NFPFSPPFMR VLSPRLENGY VLDGGAICME LLTPRGWSSA YTVEAVMRQF AASLVKGQGR
     ICRKAGKSKK SFSRKEAEAT FKSLVKTHEK YGWVTPPVSD G