UB2G1_MOUSE
ID UB2G1_MOUSE Reviewed; 170 AA.
AC P62254; Q4VAA6; Q99462;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 G1;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme G1;
DE AltName: Full=E217K;
DE AltName: Full=UBC7;
DE AltName: Full=Ubiquitin carrier protein G1;
DE AltName: Full=Ubiquitin-protein ligase G1;
DE Contains:
DE RecName: Full=Ubiquitin-conjugating enzyme E2 G1, N-terminally processed;
GN Name=Ube2g1; Synonyms=Ube2g;
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=Head;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
CC -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-, as
CC well as 'Lys-63'-linked polyubiquitination. May be involved in
CC degradation of muscle-specific proteins. Mediates polyubiquitination of
CC CYP3A4. {ECO:0000250|UniProtKB:P62253}.
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:0000250|UniProtKB:P62253, ECO:0000255|PROSITE-
CC ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:P62253}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; AK013902; BAB29048.1; -; mRNA.
DR EMBL; BC096474; AAH96474.1; -; mRNA.
DR CCDS; CCDS36217.1; -.
DR RefSeq; NP_080261.2; NM_025985.4.
DR AlphaFoldDB; P62254; -.
DR SMR; P62254; -.
DR BioGRID; 211962; 5.
DR IntAct; P62254; 1.
DR MINT; P62254; -.
DR STRING; 10090.ENSMUSP00000021148; -.
DR iPTMnet; P62254; -.
DR PhosphoSitePlus; P62254; -.
DR SwissPalm; P62254; -.
DR REPRODUCTION-2DPAGE; IPI00310850; -.
DR REPRODUCTION-2DPAGE; P62254; -.
DR EPD; P62254; -.
DR PaxDb; P62254; -.
DR PeptideAtlas; P62254; -.
DR PRIDE; P62254; -.
DR ProteomicsDB; 297774; -.
DR Antibodypedia; 1153; 238 antibodies from 31 providers.
DR DNASU; 67128; -.
DR Ensembl; ENSMUST00000021148; ENSMUSP00000021148; ENSMUSG00000020794.
DR GeneID; 67128; -.
DR KEGG; mmu:67128; -.
DR UCSC; uc007jzc.1; mouse.
DR CTD; 7326; -.
DR MGI; MGI:1914378; Ube2g1.
DR VEuPathDB; HostDB:ENSMUSG00000020794; -.
DR eggNOG; KOG0425; Eukaryota.
DR GeneTree; ENSGT00940000155228; -.
DR HOGENOM; CLU_030988_10_1_1; -.
DR InParanoid; P62254; -.
DR OMA; GFFKCHL; -.
DR OrthoDB; 1317014at2759; -.
DR PhylomeDB; P62254; -.
DR TreeFam; TF101118; -.
DR Reactome; R-MMU-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 67128; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Ube2g1; mouse.
DR PRO; PR:P62254; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P62254; protein.
DR Bgee; ENSMUSG00000020794; Expressed in primary oocyte and 269 other tissues.
DR ExpressionAtlas; P62254; baseline and differential.
DR Genevisible; P62254; MM.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0030163; P:protein catabolic process; ISO:MGI.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:ParkinsonsUK-UCL.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
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 Acetylation; ATP-binding; Nucleotide-binding; Reference proteome;
KW Transferase; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..170
FT /note="Ubiquitin-conjugating enzyme E2 G1"
FT /id="PRO_0000424516"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62253"
FT CHAIN 2..170
FT /note="Ubiquitin-conjugating enzyme E2 G1, N-terminally
FT processed"
FT /id="PRO_0000082481"
FT DOMAIN 5..166
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 90
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P62253"
FT MOD_RES 2
FT /note="N-acetylthreonine; in Ubiquitin-conjugating enzyme
FT E2 G1, N-terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P62253"
SQ SEQUENCE 170 AA; 19509 MW; 36B61766D995B332 CRC64;
MTELQSALLL RRQLAELNKN PVEGFSAGLI DDNDLYRWEV LIIGPPDTLY EGGVFKAHLT
FPKDYPLRPP KMKFITEIWH PNVDKNGDVC ISILHEPGED KYGYEKPEER WLPIHTVETI
MISVISMLAD PNGDSPANVD AAKEWREDRN GEFKRKVARC VRKSQETAFE
