ID   UB2L3_MOUSE             Reviewed;         154 AA.
AC   P68037; P51966; P70653; Q9HAV1;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 163.
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=UbcM4;
DE   AltName: Full=Ubiquitin carrier protein L3;
DE   AltName: Full=Ubiquitin-protein ligase L3;
GN   Name=Ube2l3; Synonyms=Ubce7;
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 [MRNA].
RC   STRAIN=BALB/cJ; TISSUE=Brain;
RX   PubMed=8901595; DOI=10.1073/pnas.93.22.12412;
RA   Harbers K., Mueller U., Grams A., Li E., Jaenisch R., Franz T.;
RT   "Provirus integration into a gene encoding a ubiquitin-conjugating enzyme
RT   results in a placental defect and embryonic lethality.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:12412-12417(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8563171; DOI=10.1007/bf00354295;
RA   Robinson P.A., Leek J.P., Thompson J., Carr I.M., Bailey A., Moynihan T.P.,
RA   Coletta P.L., Lench N.J., Markham A.F.;
RT   "A human ubiquitin conjugating enzyme, L-UBC, maps in the Alzheimer's
RT   disease locus on chromosome 14q24.3.";
RL   Mamm. Genome 6:725-731(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   INTERACTION WITH NDFIP1.
RX   PubMed=25632008; DOI=10.4049/jimmunol.1402742;
RA   Kathania M., Zeng M., Yadav V.N., Moghaddam S.J., Yang B., Venuprasad K.;
RT   "Ndfip1 regulates itch ligase activity and airway inflammation via UbcH7.";
RL   J. Immunol. 194:2160-2167(2015).
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 ubiquitination
CC       (PubMed:25632008). {ECO:0000250|UniProtKB:P68036,
CC       ECO:0000269|PubMed:25632008}.
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; S81004; AAB36018.1; -; Genomic_DNA.
DR   EMBL; X97042; CAA65755.1; -; mRNA.
DR   EMBL; AJ130961; CAA10265.1; -; mRNA.
DR   EMBL; AK007265; BAB24925.1; -; mRNA.
DR   CCDS; CCDS27997.1; -.
DR   PIR; JC6163; JC6163.
DR   RefSeq; NP_033482.1; NM_009456.2.
DR   AlphaFoldDB; P68037; -.
DR   BMRB; P68037; -.
DR   SMR; P68037; -.
DR   BioGRID; 204407; 22.
DR   IntAct; P68037; 1.
DR   MINT; P68037; -.
DR   STRING; 10090.ENSMUSP00000156121; -.
DR   GlyGen; P68037; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P68037; -.
DR   PhosphoSitePlus; P68037; -.
DR   SwissPalm; P68037; -.
DR   CPTAC; non-CPTAC-3679; -.
DR   EPD; P68037; -.
DR   jPOST; P68037; -.
DR   PaxDb; 10090-ENSMUSP00000111363; -.
DR   PeptideAtlas; P68037; -.
DR   ProteomicsDB; 298349; -.
DR   Pumba; P68037; -.
DR   Antibodypedia; 82546; 1 antibodies from 1 providers.
DR   DNASU; 22195; -.
DR   Ensembl; ENSMUST00000090192.12; ENSMUSP00000087658.6; ENSMUSG00000038965.18.
DR   Ensembl; ENSMUST00000232139.2; ENSMUSP00000156121.2; ENSMUSG00000038965.18.
DR   GeneID; 22195; -.
DR   KEGG; mmu:22195; -.
DR   UCSC; uc007ykl.1; mouse.
DR   AGR; MGI:109240; -.
DR   CTD; 7332; -.
DR   MGI; MGI:109240; Ube2l3.
DR   VEuPathDB; HostDB:ENSMUSG00000038965; -.
DR   eggNOG; KOG0422; Eukaryota.
DR   GeneTree; ENSGT00940000153654; -.
DR   HOGENOM; CLU_030988_13_3_1; -.
DR   InParanoid; P68037; -.
DR   OMA; ADLHTWH; -.
DR   OrthoDB; 5486024at2759; -.
DR   PhylomeDB; P68037; -.
DR   TreeFam; TF313043; -.
DR   Reactome; R-MMU-5357905; Regulation of TNFR1 signaling.
DR   Reactome; R-MMU-5675482; Regulation of necroptotic cell death.
DR   Reactome; R-MMU-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR   Reactome; R-MMU-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR   Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 22195; 15 hits in 42 CRISPR screens.
DR   ChiTaRS; Ube2l3; mouse.
DR   PRO; PR:P68037; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; P68037; Protein.
DR   Bgee; ENSMUSG00000038965; Expressed in spermatid and 267 other cell types or tissues.
DR   ExpressionAtlas; P68037; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0098793; C:presynapse; IEA:Ensembl.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
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; IDA:MGI.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR   GO; GO:0097027; F:ubiquitin-protein transferase activator activity; ISO:MGI.
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:0031398; P:positive regulation of protein ubiquitination; ISO:MGI.
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   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:MGI.
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.
DR   Genevisible; P68037; MM.
PE   1: Evidence at protein 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_0000082477"
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"
FT   CONFLICT        102
FT                   /note="D -> V (in Ref. 1; AAB36018)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   154 AA;  17862 MW;  F5A30243BE3C9985 CRC64;
     MAASRRLMKE LEEIRKCGMK NFRNIQVDEA NLLTWQGLIV PDNPPYDKGA FRIEINFPAE
     YPFKPPKITF KTKIYHPNID EKGQVCLPVI SAENWKPATK TDQVIQSLIA LVNDPQPEHP
     LRADLAEEYS KDRKKFCKNA EEFTKKYGEK RPVD
//