UB2E1_HUMAN
ID UB2E1_HUMAN Reviewed; 193 AA.
AC P51965; B2RBX4; C9J8K2; K4DI90;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 E1;
DE EC=2.3.2.23 {ECO:0000269|PubMed:20061386};
DE AltName: Full=(E3-independent) E2 ubiquitin-conjugating enzyme E1;
DE EC=2.3.2.24 {ECO:0000269|PubMed:17588522};
DE AltName: Full=E2 ubiquitin-conjugating enzyme E1;
DE AltName: Full=UbcH6;
DE AltName: Full=Ubiquitin carrier protein E1;
DE AltName: Full=Ubiquitin-protein ligase E1;
GN Name=UBE2E1; Synonyms=UBCH6;
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] (ISOFORM 1).
RX PubMed=8576257; DOI=10.1074/jbc.271.5.2795;
RA Nuber U., Schwarz S., Kaiser P., Schneider R., Scheffner M.;
RT "Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7 (E2-F1) and
RT characterization of their interaction with E6-AP and RSP5.";
RL J. Biol. Chem. 271:2795-2800(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Amygdala;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Cervix carcinoma, Colon, and Hypothalamus;
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 FUNCTION, AND ISGYLATION AT LYS-136.
RX PubMed=16428300; DOI=10.1093/jb/mvi172;
RA Takeuchi T., Iwahara S., Saeki Y., Sasajima H., Yokosawa H.;
RT "Link between the ubiquitin conjugation system and the ISG15 conjugation
RT system: ISG15 conjugation to the UbcH6 ubiquitin E2 enzyme.";
RL J. Biochem. 138:711-719(2005).
RN [7]
RP CATALYTIC ACTIVITY AS E3-INDEPENDENT E2 UBIQUITIN-CONJUGATING ENZYME.
RX PubMed=17588522; DOI=10.1016/j.molcel.2007.05.014;
RA Hoeller D., Hecker C.M., Wagner S., Rogov V., Doetsch V., Dikic I.;
RT "E3-independent monoubiquitination of ubiquitin-binding proteins.";
RL Mol. Cell 26:891-898(2007).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=18845142; DOI=10.1016/j.yexcr.2008.09.011;
RA Espinosa A., Oke V., Elfving A., Nyberg F., Covacu R., Wahren-Herlenius M.;
RT "The autoantigen Ro52 is an E3 ligase resident in the cytoplasm but enters
RT the nucleus upon cellular exposure to nitric oxide.";
RL Exp. Cell Res. 314:3605-3613(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
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 [11]
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13] {ECO:0007744|PDB:3BZH}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS), 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. Catalyzes the covalent
CC attachment of ISG15 to other proteins. Mediates the selective
CC degradation of short-lived and abnormal proteins. In vitro also
CC catalyzes 'Lys-48'-linked polyubiquitination.
CC {ECO:0000269|PubMed:16428300, 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 -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-
CC cysteine + N(6)-monoubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.24; Evidence={ECO:0000269|PubMed:17588522};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SUBUNIT: Interacts with RNF14.
CC -!- INTERACTION:
CC P51965; Q96FW1: OTUB1; NbExp=3; IntAct=EBI-348546, EBI-1058491;
CC P51965; Q8N7H5: PAF1; NbExp=2; IntAct=EBI-348546, EBI-2607770;
CC P51965; Q9Y3C5: RNF11; NbExp=2; IntAct=EBI-348546, EBI-396669;
CC P51965; Q5VTR2: RNF20; NbExp=2; IntAct=EBI-348546, EBI-2372238;
CC P51965; Q96BH1: RNF25; NbExp=3; IntAct=EBI-348546, EBI-2129220;
CC P51965; Q8ND25: ZNRF1; NbExp=3; IntAct=EBI-348546, EBI-2129250;
CC P51965; Q99PZ6: ospG; Xeno; NbExp=3; IntAct=EBI-348546, EBI-9316527;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18845142}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P51965-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P51965-2; Sequence=VSP_045884;
CC Name=3;
CC IsoId=P51965-3; Sequence=VSP_047200;
CC -!- PTM: ISGylation suppresses ubiquitin E2 enzyme activity.
CC {ECO:0000269|PubMed:16428300}.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X92963; CAA63539.1; -; mRNA.
DR EMBL; AK314854; BAG37371.1; -; mRNA.
DR EMBL; AC020626; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC124914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW64329.1; -; Genomic_DNA.
DR EMBL; CH471055; EAW64331.1; -; Genomic_DNA.
DR EMBL; CH471055; EAW64332.1; -; Genomic_DNA.
DR EMBL; BC009139; AAH09139.1; -; mRNA.
DR EMBL; BI223271; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BI666638; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS2638.1; -. [P51965-1]
DR CCDS; CCDS2639.1; -. [P51965-3]
DR CCDS; CCDS56244.1; -. [P51965-2]
DR RefSeq; NP_001189405.1; NM_001202476.1. [P51965-2]
DR RefSeq; NP_003332.1; NM_003341.4. [P51965-1]
DR RefSeq; NP_872607.1; NM_182666.2. [P51965-3]
DR PDB; 1XR9; X-ray; 1.79 A; C=83-91.
DR PDB; 3BZH; X-ray; 1.60 A; A=1-193.
DR PDB; 4JJQ; X-ray; 1.95 A; B=5-14.
DR PDB; 5LBN; X-ray; 1.42 A; A=37-193.
DR PDB; 6FGA; X-ray; 2.82 A; I/J/K/L/M/N/O=37-193.
DR PDBsum; 1XR9; -.
DR PDBsum; 3BZH; -.
DR PDBsum; 4JJQ; -.
DR PDBsum; 5LBN; -.
DR PDBsum; 6FGA; -.
DR AlphaFoldDB; P51965; -.
DR SMR; P51965; -.
DR BioGRID; 113172; 160.
DR CORUM; P51965; -.
DR IntAct; P51965; 77.
DR MINT; P51965; -.
DR STRING; 9606.ENSP00000303709; -.
DR BindingDB; P51965; -.
DR ChEMBL; CHEMBL4105876; -.
DR MoonDB; P51965; Predicted.
DR iPTMnet; P51965; -.
DR PhosphoSitePlus; P51965; -.
DR SwissPalm; P51965; -.
DR BioMuta; UBE2E1; -.
DR DMDM; 1717857; -.
DR EPD; P51965; -.
DR jPOST; P51965; -.
DR MassIVE; P51965; -.
DR MaxQB; P51965; -.
DR PaxDb; P51965; -.
DR PeptideAtlas; P51965; -.
DR PRIDE; P51965; -.
DR ProteomicsDB; 56463; -. [P51965-1]
DR ProteomicsDB; 9057; -.
DR Antibodypedia; 45210; 119 antibodies from 22 providers.
DR CPTC; P51965; 3 antibodies.
DR DNASU; 7324; -.
DR Ensembl; ENST00000306627.8; ENSP00000303709.3; ENSG00000170142.12. [P51965-1]
DR Ensembl; ENST00000346855.7; ENSP00000329113.4; ENSG00000170142.12. [P51965-3]
DR Ensembl; ENST00000424381.5; ENSP00000411351.1; ENSG00000170142.12. [P51965-2]
DR GeneID; 7324; -.
DR KEGG; hsa:7324; -.
DR MANE-Select; ENST00000306627.8; ENSP00000303709.3; NM_003341.5; NP_003332.1.
DR UCSC; uc003cch.4; human. [P51965-1]
DR CTD; 7324; -.
DR DisGeNET; 7324; -.
DR GeneCards; UBE2E1; -.
DR HGNC; HGNC:12477; UBE2E1.
DR HPA; ENSG00000170142; Low tissue specificity.
DR MIM; 602916; gene.
DR neXtProt; NX_P51965; -.
DR OpenTargets; ENSG00000170142; -.
DR PharmGKB; PA37127; -.
DR VEuPathDB; HostDB:ENSG00000170142; -.
DR eggNOG; KOG0417; Eukaryota.
DR GeneTree; ENSGT00940000156415; -.
DR HOGENOM; CLU_030988_14_4_1; -.
DR InParanoid; P51965; -.
DR OMA; MYSSINT; -.
DR PhylomeDB; P51965; -.
DR TreeFam; TF101117; -.
DR BRENDA; 2.3.2.23; 2681.
DR BRENDA; 2.3.2.24; 2681.
DR BRENDA; 2.3.2.25; 2681.
DR PathwayCommons; P51965; -.
DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
DR Reactome; R-HSA-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR Reactome; R-HSA-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-HSA-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR Reactome; R-HSA-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-HSA-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
DR Reactome; R-HSA-176412; Phosphorylation of the APC/C.
DR Reactome; R-HSA-179409; APC-Cdc20 mediated degradation of Nek2A.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-HSA-68867; Assembly of the pre-replicative complex.
DR Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-HSA-8853884; Transcriptional Regulation by VENTX.
DR Reactome; R-HSA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-HSA-9687136; Aberrant regulation of mitotic exit in cancer due to RB1 defects.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; P51965; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 7324; 16 hits in 1089 CRISPR screens.
DR ChiTaRS; UBE2E1; human.
DR EvolutionaryTrace; P51965; -.
DR GeneWiki; UBE2E1; -.
DR GenomeRNAi; 7324; -.
DR Pharos; P51965; Tbio.
DR PRO; PR:P51965; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P51965; protein.
DR Bgee; ENSG00000170142; Expressed in cartilage tissue and 214 other tissues.
DR ExpressionAtlas; P51965; baseline and differential.
DR Genevisible; P51965; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042296; F:ISG15 transferase activity; IDA:HGNC-UCL.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:BHF-UCL.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0033523; P:histone H2B ubiquitination; IDA:UniProtKB.
DR GO; GO:0010390; P:histone monoubiquitination; IDA:UniProtKB.
DR GO; GO:0032020; P:ISG15-protein conjugation; IDA:HGNC-UCL.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:BHF-UCL.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:ProtInc.
DR CDD; cd00195; UBCc; 1.
DR DisProt; DP02191; -.
DR Gene3D; 3.10.110.10; -; 1.
DR IDEAL; IID00633; -.
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; Alternative splicing; ATP-binding;
KW Isopeptide bond; Nucleotide-binding; Nucleus; Reference proteome;
KW Transferase; Ubl conjugation; Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:21406692"
FT CHAIN 2..193
FT /note="Ubiquitin-conjugating enzyme E2 E1"
FT /id="PRO_0000082470"
FT DOMAIN 47..193
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 131
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:21406692"
FT CROSSLNK 136
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ISG15)"
FT VAR_SEQ 1..50
FT /note="MSDDDSRASTSSSSSSSSNQQTEKETNTPKKKESKVSMSKNSKLLSTSAK
FT -> MKEVGRPREVRGRPGKS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045884"
FT VAR_SEQ 51..67
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_047200"
FT VARIANT 25
FT /note="E -> D (in dbSNP:rs36060625)"
FT /id="VAR_061868"
FT CONFLICT 131
FT /note="C -> R (in Ref. 5; BI223271)"
FT /evidence="ECO:0000305"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:3BZH"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:5LBN"
FT HELIX 47..61
FT /evidence="ECO:0007829|PDB:5LBN"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:5LBN"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:5LBN"
FT TURN 90..93
FT /evidence="ECO:0007829|PDB:5LBN"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:5LBN"
FT TURN 104..107
FT /evidence="ECO:0007829|PDB:5LBN"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:5LBN"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:5LBN"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:3BZH"
FT HELIX 145..157
FT /evidence="ECO:0007829|PDB:5LBN"
FT HELIX 167..175
FT /evidence="ECO:0007829|PDB:5LBN"
FT HELIX 177..191
FT /evidence="ECO:0007829|PDB:5LBN"
SQ SEQUENCE 193 AA; 21404 MW; 2FBC50BE2A6A0008 CRC64;
MSDDDSRAST SSSSSSSSNQ QTEKETNTPK KKESKVSMSK NSKLLSTSAK RIQKELADIT
LDPPPNCSAG PKGDNIYEWR STILGPPGSV YEGGVFFLDI TFTPEYPFKP PKVTFRTRIY
HCNINSQGVI CLDILKDNWS PALTISKVLL SICSLLTDCN PADPLVGSIA TQYMTNRAEH
DRMARQWTKR YAT
