ID   U2QL1_HUMAN             Reviewed;         161 AA.
AC   A1L167;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   27-MAR-2024, entry version 120.
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   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, CHROMOSOMAL TRANSLOCATION, INTERACTION WITH
RP   FBXW7, INVOLVEMENT IN RCC, MUTAGENESIS OF CYS-88, AND ACTIVE SITE.
RX   PubMed=24000165; DOI=10.1002/humu.22433;
RA   Wake N.C., Ricketts C.J., Morris M.R., Prigmore E., Gribble S.M.,
RA   Skytte A.B., Brown M., Clarke N., Banks R.E., Hodgson S., Turnell A.S.,
RA   Maher E.R., Woodward E.R.;
RT   "UBE2QL1 is disrupted by a constitutional translocation associated with
RT   renal tumor predisposition and is a novel candidate renal tumor suppressor
RT   gene.";
RL   Hum. Mutat. 34:1650-1661(2013).
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:0000269|PubMed:24000165}.
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:0000269|PubMed:24000165}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24000165}.
CC   -!- DISEASE: Note=A chromosomal aberration involving UBE2QL1 has been found
CC       in a sporadic case of renal cell carcinoma (RCC). Translocation
CC       t(5;19)(p15.3;q12). No gene is disrupted by the chromosome 19
CC       breakpoint. {ECO:0000269|PubMed:24000165}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI27724.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAI50555.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BC127723; AAI27724.1; ALT_INIT; mRNA.
DR   EMBL; BC150554; AAI50555.1; ALT_INIT; mRNA.
DR   CCDS; CCDS47189.1; -.
DR   RefSeq; NP_001138633.1; NM_001145161.2.
DR   AlphaFoldDB; A1L167; -.
DR   SMR; A1L167; -.
DR   BioGRID; 126384; 1.
DR   STRING; 9606.ENSP00000382713; -.
DR   iPTMnet; A1L167; -.
DR   PhosphoSitePlus; A1L167; -.
DR   BioMuta; UBE2QL1; -.
DR   PaxDb; 9606-ENSP00000382713; -.
DR   PeptideAtlas; A1L167; -.
DR   ProteomicsDB; 132; -.
DR   DNASU; 134111; -.
DR   Ensembl; ENST00000399816.4; ENSP00000382713.3; ENSG00000215218.4.
DR   Ensembl; ENST00000708565.1; ENSP00000517282.1; ENSG00000291747.1.
DR   GeneID; 134111; -.
DR   KEGG; hsa:134111; -.
DR   MANE-Select; ENST00000399816.4; ENSP00000382713.3; NM_001145161.3; NP_001138633.1.
DR   UCSC; uc003jdp.5; human.
DR   AGR; HGNC:37269; -.
DR   CTD; 134111; -.
DR   DisGeNET; 134111; -.
DR   GeneCards; UBE2QL1; -.
DR   HGNC; HGNC:37269; UBE2QL1.
DR   HPA; ENSG00000215218; Group enriched (brain, heart muscle, retina, skeletal muscle, tongue).
DR   MIM; 615832; gene.
DR   neXtProt; NX_A1L167; -.
DR   OpenTargets; ENSG00000215218; -.
DR   PharmGKB; PA165660602; -.
DR   VEuPathDB; HostDB:ENSG00000215218; -.
DR   eggNOG; KOG0897; Eukaryota.
DR   GeneTree; ENSGT00940000161612; -.
DR   HOGENOM; CLU_089409_1_0_1; -.
DR   InParanoid; A1L167; -.
DR   OMA; WHVRLHQ; -.
DR   OrthoDB; 37924at2759; -.
DR   PhylomeDB; A1L167; -.
DR   TreeFam; TF313338; -.
DR   BRENDA; 2.3.2.23; 2681.
DR   PathwayCommons; A1L167; -.
DR   SignaLink; A1L167; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 134111; 11 hits in 1148 CRISPR screens.
DR   ChiTaRS; UBE2QL1; human.
DR   GenomeRNAi; 134111; -.
DR   Pharos; A1L167; Tbio.
DR   PRO; PR:A1L167; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; A1L167; Protein.
DR   Bgee; ENSG00000215218; Expressed in endothelial cell and 165 other cell types or tissues.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:MGI.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS50127; UBC_2; 1.
DR   Genevisible; A1L167; HS.
PE   1: Evidence at protein level;
KW   ATP-binding; Chromosomal rearrangement; Nucleotide-binding; Nucleus;
KW   Reference proteome; Transferase; Ubl conjugation pathway.
FT   CHAIN           1..161
FT                   /note="Ubiquitin-conjugating enzyme E2Q-like protein 1"
FT                   /id="PRO_0000335811"
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                   ECO:0000269|PubMed:24000165"
FT   MUTAGEN         88
FT                   /note="C->A: Unable to bind ubiquitin."
FT                   /evidence="ECO:0000269|PubMed:24000165"
FT   MUTAGEN         88
FT                   /note="C->S: Enhanced ubiquitin binding."
FT                   /evidence="ECO:0000269|PubMed:24000165"
SQ   SEQUENCE   161 AA;  18338 MW;  B2062702B5EFB2A2 CRC64;
     MKELQDIARL SDRFISVELV DESLFDWNVK LHQVDKDSVL WQDMKETNTE FILLNLTFPD
     NFPFSPPFMR VLSPRLENGY VLDGGAICME LLTPRGWSSA YTVEAVMRQF AASLVKGQGR
     ICRKAGKSKK SFSRKEAEAT FKSLVKTHEK YGWVTPPVSD G
//