UB2G1_HUMAN
ID UB2G1_HUMAN Reviewed; 170 AA.
AC P62253; B2R7P2; D3DTK0; Q99462;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 G1;
DE EC=2.3.2.23 {ECO:0000269|PubMed:20061386};
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 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 [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=8893823; DOI=10.1159/000134403;
RA Watanabe T.K., Kawai A., Fujiwara T., Maekawa H., Hirai Y., Nakamura Y.,
RA Takahashi E.;
RT "Molecular cloning of UBE2G, encoding a human skeletal muscle-specific
RT ubiquitin-conjugating enzyme homologous to UBC7 of C. elegans.";
RL Cytogenet. Cell Genet. 74:146-148(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Caudate nucleus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph, and Prostate;
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 [6]
RP PROTEIN SEQUENCE OF 2-11, AND ACETYLATION AT THR-2.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [7]
RP FUNCTION.
RX PubMed=19103148; DOI=10.1016/j.abb.2008.12.001;
RA Pabarcus M.K., Hoe N., Sadeghi S., Patterson C., Wiertz E., Correia M.A.;
RT "CYP3A4 ubiquitination by gp78 (the tumor autocrine motility factor
RT receptor, AMFR) and CHIP E3 ligases.";
RL Arch. Biochem. Biophys. 483:66-74(2009).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20061386; DOI=10.1074/jbc.m109.089003;
RA David Y., Ziv T., Admon A., Navon A.;
RT "The E2 ubiquitin-conjugating enzymes direct polyubiquitination to
RT preferred lysines.";
RL J. Biol. Chem. 285:8595-8604(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12] {ECO:0007744|PDB:2AWF}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 8-160, AND AUTOUBIQUITINATION.
RX PubMed=22496338; DOI=10.1074/mcp.o111.013706;
RA Sheng Y., Hong J.H., Doherty R., Srikumar T., Shloush J., Avvakumov G.V.,
RA Walker J.R., Xue S., Neculai D., Wan J.W., Kim S.K., Arrowsmith C.H.,
RA Raught B., Dhe-Paganon S.;
RT "A human ubiquitin conjugating enzyme (E2)-HECT E3 ligase structure-
RT function screen.";
RL Mol. Cell. Proteomics 11:329-341(2012).
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:0000269|PubMed:19103148, ECO:0000269|PubMed:20061386}.
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, ECO:0000269|PubMed:20061386};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- INTERACTION:
CC P62253; P06307: CCK; NbExp=3; IntAct=EBI-2340619, EBI-6624398;
CC P62253; P62879: GNB2; NbExp=3; IntAct=EBI-2340619, EBI-356942;
CC P62253; P13473-2: LAMP2; NbExp=3; IntAct=EBI-2340619, EBI-21591415;
CC P62253; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-2340619, EBI-5280197;
CC P62253; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-2340619, EBI-2623095;
CC -!- TISSUE SPECIFICITY: Widely expressed, mainly in skeletal muscle.
CC {ECO:0000269|PubMed:8893823}.
CC -!- PTM: Autoubiquitinated in vitro. {ECO:0000269|PubMed:22496338}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH26288.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D78514; BAA11410.1; -; mRNA.
DR EMBL; BT007416; AAP36084.1; -; mRNA.
DR EMBL; AK313059; BAG35889.1; -; mRNA.
DR EMBL; CH471108; EAW90445.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90446.1; -; Genomic_DNA.
DR EMBL; BC002775; AAH02775.1; -; mRNA.
DR EMBL; BC026288; AAH26288.2; ALT_INIT; mRNA.
DR CCDS; CCDS32532.1; -.
DR RefSeq; NP_003333.1; NM_003342.4.
DR PDB; 2AWF; X-ray; 2.10 A; A=8-160.
DR PDB; 6D68; X-ray; 2.36 A; A/B=1-170.
DR PDBsum; 2AWF; -.
DR PDBsum; 6D68; -.
DR AlphaFoldDB; P62253; -.
DR SMR; P62253; -.
DR BioGRID; 113174; 35.
DR IntAct; P62253; 8.
DR STRING; 9606.ENSP00000380178; -.
DR iPTMnet; P62253; -.
DR PhosphoSitePlus; P62253; -.
DR SwissPalm; P62253; -.
DR BioMuta; UBE2G1; -.
DR DMDM; 51338681; -.
DR EPD; P62253; -.
DR jPOST; P62253; -.
DR MassIVE; P62253; -.
DR MaxQB; P62253; -.
DR PaxDb; P62253; -.
DR PeptideAtlas; P62253; -.
DR PRIDE; P62253; -.
DR ProteomicsDB; 57375; -.
DR Antibodypedia; 1153; 238 antibodies from 31 providers.
DR DNASU; 7326; -.
DR Ensembl; ENST00000396981.7; ENSP00000380178.2; ENSG00000132388.13.
DR GeneID; 7326; -.
DR KEGG; hsa:7326; -.
DR MANE-Select; ENST00000396981.7; ENSP00000380178.2; NM_003342.5; NP_003333.1.
DR UCSC; uc002fxs.4; human.
DR CTD; 7326; -.
DR DisGeNET; 7326; -.
DR GeneCards; UBE2G1; -.
DR HGNC; HGNC:12482; UBE2G1.
DR HPA; ENSG00000132388; Tissue enhanced (skeletal).
DR MIM; 601569; gene.
DR neXtProt; NX_P62253; -.
DR OpenTargets; ENSG00000132388; -.
DR PharmGKB; PA37131; -.
DR VEuPathDB; HostDB:ENSG00000132388; -.
DR eggNOG; KOG0425; Eukaryota.
DR GeneTree; ENSGT00940000155228; -.
DR HOGENOM; CLU_030988_10_1_1; -.
DR InParanoid; P62253; -.
DR OMA; GFFKCHL; -.
DR OrthoDB; 1317014at2759; -.
DR PhylomeDB; P62253; -.
DR TreeFam; TF101118; -.
DR BRENDA; 2.3.2.23; 2681.
DR BRENDA; 2.3.2.24; 2681.
DR PathwayCommons; P62253; -.
DR Reactome; R-HSA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; P62253; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 7326; 33 hits in 1083 CRISPR screens.
DR ChiTaRS; UBE2G1; human.
DR EvolutionaryTrace; P62253; -.
DR GeneWiki; UBE2G1; -.
DR GenomeRNAi; 7326; -.
DR Pharos; P62253; Tbio.
DR PRO; PR:P62253; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P62253; protein.
DR Bgee; ENSG00000132388; Expressed in sperm and 208 other tissues.
DR ExpressionAtlas; P62253; baseline and differential.
DR Genevisible; P62253; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IDA: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 IDEAL; IID00634; -.
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 3D-structure; Acetylation; ATP-binding; Direct protein sequencing;
KW Nucleotide-binding; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..170
FT /note="Ubiquitin-conjugating enzyme E2 G1"
FT /id="PRO_0000424514"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..170
FT /note="Ubiquitin-conjugating enzyme E2 G1, N-terminally
FT processed"
FT /id="PRO_0000082480"
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:0007744|PubMed:22814378"
FT MOD_RES 2
FT /note="N-acetylthreonine; in Ubiquitin-conjugating enzyme
FT E2 G1, N-terminally processed"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT HELIX 8..19
FT /evidence="ECO:0007829|PDB:2AWF"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:2AWF"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:2AWF"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:2AWF"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:2AWF"
FT TURN 63..66
FT /evidence="ECO:0007829|PDB:2AWF"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:2AWF"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:6D68"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:2AWF"
FT HELIX 117..128
FT /evidence="ECO:0007829|PDB:2AWF"
FT HELIX 139..147
FT /evidence="ECO:0007829|PDB:6D68"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:6D68"
FT HELIX 152..168
FT /evidence="ECO:0007829|PDB:6D68"
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
