UB2L6_MOUSE
ID UB2L6_MOUSE Reviewed; 153 AA.
AC Q9QZU9; Q3U8R0; Q922F1; Q9CQN0;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Ubiquitin/ISG15-conjugating enzyme E2 L6;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme L6;
DE AltName: Full=UbcM8;
DE AltName: Full=Ubiquitin carrier protein L6;
DE AltName: Full=Ubiquitin-protein ligase L6;
GN Name=Ube2l6; Synonyms=Ubce8;
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].
RA Cook G., Lawshe A., MacArthur C.A.;
RT "Progression from mammary hyperplasia to adenocarcinoma in MMTV-FGF8b
RT transgenic mice is associated with altered expression of CD63,
RT IGFBP7/mac25, alpha-synuclein, and UbcM8.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Embryo, and Embryonic liver;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, and Spleen;
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).
CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin or ISG15 to
CC other proteins. Functions in the E6/E6-AP-induced ubiquitination of
CC p53/TP53. Promotes ubiquitination and subsequent proteasomal
CC degradation of FLT3. {ECO:0000250|UniProtKB:O14933}.
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 RNF19A, RNF19B and RNF144B. Interacts with FLT3
CC (tyrosine phosphorylated). {ECO:0000250|UniProtKB:O14933}.
CC -!- PTM: ISGylated. {ECO:0000250|UniProtKB:O14933}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD55978.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF159230; AAD55978.1; ALT_INIT; mRNA.
DR EMBL; AK010942; BAB27282.1; -; mRNA.
DR EMBL; AK013452; BAB28861.1; -; mRNA.
DR EMBL; AK152010; BAE30873.1; -; mRNA.
DR EMBL; AK152113; BAE30957.1; -; mRNA.
DR EMBL; AK168695; BAE40539.1; -; mRNA.
DR EMBL; AK171629; BAE42574.1; -; mRNA.
DR EMBL; CH466519; EDL27303.1; -; Genomic_DNA.
DR EMBL; BC008238; AAH08238.1; -; mRNA.
DR CCDS; CCDS16194.2; -.
DR RefSeq; NP_064333.2; NM_019949.2.
DR AlphaFoldDB; Q9QZU9; -.
DR SMR; Q9QZU9; -.
DR STRING; 10090.ENSMUSP00000099702; -.
DR iPTMnet; Q9QZU9; -.
DR PhosphoSitePlus; Q9QZU9; -.
DR MaxQB; Q9QZU9; -.
DR PaxDb; Q9QZU9; -.
DR PRIDE; Q9QZU9; -.
DR ProteomicsDB; 298173; -.
DR Antibodypedia; 1142; 361 antibodies from 34 providers.
DR DNASU; 56791; -.
DR Ensembl; ENSMUST00000102642; ENSMUSP00000099702; ENSMUSG00000027078.
DR GeneID; 56791; -.
DR KEGG; mmu:56791; -.
DR UCSC; uc012byn.1; mouse.
DR CTD; 9246; -.
DR MGI; MGI:1914500; Ube2l6.
DR VEuPathDB; HostDB:ENSMUSG00000027078; -.
DR eggNOG; KOG0422; Eukaryota.
DR GeneTree; ENSGT00940000161981; -.
DR HOGENOM; CLU_030988_13_3_1; -.
DR InParanoid; Q9QZU9; -.
DR OMA; RPNLEEP; -.
DR OrthoDB; 1420213at2759; -.
DR PhylomeDB; Q9QZU9; -.
DR TreeFam; TF313043; -.
DR Reactome; R-MMU-1169408; ISG15 antiviral mechanism.
DR Reactome; R-MMU-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 56791; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Ube2l6; mouse.
DR PRO; PR:Q9QZU9; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9QZU9; protein.
DR Bgee; ENSMUSG00000027078; Expressed in blood and 92 other tissues.
DR ExpressionAtlas; Q9QZU9; baseline and differential.
DR Genevisible; Q9QZU9; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042296; F:ISG15 transferase activity; IDA:MGI.
DR GO; GO:0043130; F:ubiquitin binding; ISO:MGI.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0019787; F:ubiquitin-like protein transferase activity; IDA:MGI.
DR GO; GO:0032020; P:ISG15-protein conjugation; IDA:MGI.
DR GO; GO:0019941; P:modification-dependent protein catabolic process; IDA:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Nucleotide-binding; Reference proteome; Transferase;
KW Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..153
FT /note="Ubiquitin/ISG15-conjugating enzyme E2 L6"
FT /id="PRO_0000082479"
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 CONFLICT 29
FT /note="D -> Y (in Ref. 1; AAD55978)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="F -> L (in Ref. 4; AAH08238)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 153 AA; 17841 MW; 71EEFF050CDE57F1 CRC64;
MMASKRVAKE LESLSKELPP YLRQLSSDDA NVLVWHMLLL PDQLPYGLKA FQVRIDFPRE
YPFKPPTLRF TTKIYHPNVR EDGLVCLPLI SNENWKPYTK PYQVLEALNV LVSKPNLEEP
VRLELADLLT QNPEMFRKKA EEFTLKFGVD RPS
