UBE2N_MOUSE
ID UBE2N_MOUSE Reviewed; 152 AA.
AC P61089; Q16781; Q3TSL6; Q6ZWZ0; Q9DAJ6;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 N;
DE EC=2.3.2.23 {ECO:0000269|PubMed:22424771, ECO:0000269|PubMed:28039360};
DE AltName: Full=Bendless-like ubiquitin-conjugating enzyme;
DE AltName: Full=E2 ubiquitin-conjugating enzyme N;
DE AltName: Full=Ubc13;
DE AltName: Full=Ubiquitin carrier protein N;
DE AltName: Full=Ubiquitin-protein ligase N;
GN Name=Ube2n; Synonyms=Blu;
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=ICR X Swiss Webster;
RA Rugarli E.I., Valsecchi V., Ballabio A.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=B-cell;
RX PubMed=12039045; DOI=10.1016/s0378-1119(02)00409-2;
RA Ashley C., Pastushok L., McKenna S., Ellison M.J., Xiao W.;
RT "Roles of mouse UBC13 in DNA postreplication repair and Lys63-linked
RT ubiquitination.";
RL Gene 285:183-191(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Olfactory bulb, and 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye, and Mammary gland;
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 PROTEIN SEQUENCE OF 15-24; 34-68; 95-102 AND 131-141, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP INTERACTION WITH STUB1 AND UBE2V1.
RX PubMed=16307917; DOI=10.1016/j.molcel.2005.09.023;
RA Zhang M., Windheim M., Roe S.M., Peggie M., Cohen P., Prodromou C.,
RA Pearl L.H.;
RT "Chaperoned ubiquitylation -- crystal structures of the CHIP U box E3
RT ubiquitin ligase and a CHIP-Ubc13-Uev1a complex.";
RL Mol. Cell 20:525-538(2005).
RN [7]
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).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=22424771; DOI=10.1016/j.molcel.2012.01.025;
RA Cardamone M.D., Krones A., Tanasa B., Taylor H., Ricci L., Ohgi K.A.,
RA Glass C.K., Rosenfeld M.G., Perissi V.;
RT "A protective strategy against hyperinflammatory responses requiring the
RT nontranscriptional actions of GPS2.";
RL Mol. Cell 46:91-104(2012).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=28039360; DOI=10.1074/jbc.m116.755132;
RA Lentucci C., Belkina A.C., Cederquist C.T., Chan M., Johnson H.E.,
RA Prasad S., Lopacinski A., Nikolajczyk B.S., Monti S., Snyder-Cappione J.,
RA Tanasa B., Cardamone M.D., Perissi V.;
RT "Inhibition of Ubc13-mediated ubiquitination by GPS2 regulates multiple
RT stages of B Cell development.";
RL J. Biol. Chem. 292:2754-2772(2017).
RN [10]
RP ACTIVITY REGULATION.
RX PubMed=28123943; DOI=10.1016/j.molmet.2016.10.007;
RA Cederquist C.T., Lentucci C., Martinez-Calejman C., Hayashi V., Orofino J.,
RA Guertin D., Fried S.K., Lee M.J., Cardamone M.D., Perissi V.;
RT "Systemic insulin sensitivity is regulated by GPS2 inhibition of AKT
RT ubiquitination and activation in adipose tissue.";
RL Mol. Metab. 6:125-137(2017).
RN [11]
RP FUNCTION.
RX PubMed=28469175; DOI=10.1038/ncomms15138;
RA Shi Y., Yuan B., Zhu W., Zhang R., Li L., Hao X., Chen S., Hou F.;
RT "Ube2D3 and Ube2N are essential for RIG-I-mediated MAVS aggregation in
RT antiviral innate immunity.";
RL Nat. Commun. 8:15138-15138(2017).
RN [12]
RP ACTIVITY REGULATION.
RX PubMed=29499132; DOI=10.1016/j.molcel.2018.01.037;
RA Cardamone M.D., Tanasa B., Cederquist C.T., Huang J., Mahdaviani K., Li W.,
RA Rosenfeld M.G., Liesa M., Perissi V.;
RT "Mitochondrial retrograde signaling in mammals is mediated by the
RT transcriptional cofactor GPS2 via direct mitochondria-to-nucleus
RT translocation.";
RL Mol. Cell 69:757-772(2018).
CC -!- FUNCTION: The UBE2V1-UBE2N and UBE2V2-UBE2N heterodimers catalyze the
CC synthesis of non-canonical 'Lys-63'-linked polyubiquitin chains
CC (PubMed:22424771, PubMed:28039360). This type of polyubiquitination
CC does not lead to protein degradation by the proteasome. Mediates
CC transcriptional activation of target genes. Plays a role in the control
CC of progress through the cell cycle and differentiation. Plays a role in
CC the error-free DNA repair pathway and contributes to the survival of
CC cells after DNA damage. Acts together with the E3 ligases, HLTF and
CC SHPRH, in the 'Lys-63'-linked poly-ubiquitination of PCNA upon
CC genotoxic stress, which is required for DNA repair. Appears to act
CC together with E3 ligase RNF5 in the 'Lys-63'-linked polyubiquitination
CC of JKAMP thereby regulating JKAMP function by decreasing its
CC association with components of the proteasome and ERAD. Promotes TRIM5
CC capsid-specific restriction activity and the UBE2V1-UBE2N heterodimer
CC acts in concert with TRIM5 to generate 'Lys-63'-linked polyubiquitin
CC chains which activate the MAP3K7/TAK1 complex which in turn results in
CC the induction and expression of NF-kappa-B and MAPK-responsive
CC inflammatory genes. Together with RNF135 and UB2V1, catalyzes the RNA-
CC dependent 'Lys-63'-linked polyubiquitination of RIG-I/DDX58 to activate
CC the downstream signaling pathway that leads to interferon beta
CC production (PubMed:22424771). UBE2V1-UBE2N together with TRAF3IP2 E3
CC ubiquitin ligase mediate 'Lys-63'-linked polyubiquitination of TRAF6, a
CC component of IL17A-mediated signaling pathway.
CC {ECO:0000250|UniProtKB:P61088, ECO:0000269|PubMed:22424771,
CC ECO:0000269|PubMed:28039360}.
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:22424771,
CC ECO:0000269|PubMed:28039360};
CC -!- ACTIVITY REGULATION: Activity is inhibited by binding to OTUB1, which
CC prevents 'Lys-63'-linked polyubiquitination (By similarity). Activity
CC is inhibited by GPS2, leading to prevent 'Lys-63'-linked
CC polyubiquitination (PubMed:22424771, PubMed:28039360, PubMed:28123943,
CC PubMed:29499132). {ECO:0000250|UniProtKB:P61088,
CC ECO:0000269|PubMed:22424771, ECO:0000269|PubMed:28039360,
CC ECO:0000269|PubMed:28123943, ECO:0000269|PubMed:29499132}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SUBUNIT: Heterodimer with UBE2V2 (By similarity). Interacts (UBE2V2-
CC UBE2N heterodimer) with the E3 ligase STUB1 (via the U-box domain); the
CC complex has a specific 'Lys-63'-linked polyubiquitination activity (By
CC similarity). Interacts with RNF8 and RNF168 (By similarity). Interacts
CC with RNF11 (By similarity). Interacts with the E3 ligases, HLTF and
CC SHPRH; the interactions promote the 'Lys-63'-linked polyubiquitination
CC of PCNA upon genotoxic stress and lead to DNA repair (By similarity).
CC Interacts with ARIH2 (via RING-type 2) (By similarity). Interacts with
CC OTUB1; leading to inhibit E2-conjugating activity (By similarity).
CC Interacts with GPS2; leading to inhibit E2-conjugating activity
CC (PubMed:22424771). Interacts with DDX58 and RNF135; involved in DDX58
CC ubiquitination and activation (By similarity).
CC {ECO:0000250|UniProtKB:P61088, ECO:0000269|PubMed:22424771}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P61088}. Cytoplasm
CC {ECO:0000250|UniProtKB:P61088}.
CC -!- PTM: Conjugation to ISG15 impairs formation of the thioester bond with
CC ubiquitin but not interaction with UBE2V2.
CC {ECO:0000250|UniProtKB:P61088}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE36659.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Y09873; CAA71001.1; -; mRNA.
DR EMBL; AY039837; AAK74128.1; -; mRNA.
DR EMBL; AK005302; BAB23941.1; -; mRNA.
DR EMBL; AK005788; BAB24239.1; -; mRNA.
DR EMBL; AK161968; BAE36659.1; ALT_FRAME; mRNA.
DR EMBL; BC034898; AAH34898.3; -; mRNA.
DR EMBL; BC067069; AAH67069.1; -; mRNA.
DR CCDS; CCDS48677.1; -.
DR RefSeq; NP_542127.1; NM_080560.3.
DR AlphaFoldDB; P61089; -.
DR BMRB; P61089; -.
DR SMR; P61089; -.
DR BioGRID; 220301; 39.
DR ComplexPortal; CPX-604; UBC13-MMS2 ubiquitin-conjugating enzyme E2 complex.
DR ComplexPortal; CPX-616; UBC13-UEV1A ubiquitin-conjugating enzyme E2 complex.
DR CORUM; P61089; -.
DR IntAct; P61089; 6.
DR STRING; 10090.ENSMUSP00000096932; -.
DR iPTMnet; P61089; -.
DR PhosphoSitePlus; P61089; -.
DR SwissPalm; P61089; -.
DR REPRODUCTION-2DPAGE; IPI00165854; -.
DR REPRODUCTION-2DPAGE; P61089; -.
DR CPTAC; non-CPTAC-3678; -.
DR CPTAC; non-CPTAC-3887; -.
DR EPD; P61089; -.
DR jPOST; P61089; -.
DR MaxQB; P61089; -.
DR PaxDb; P61089; -.
DR PRIDE; P61089; -.
DR ProteomicsDB; 297695; -.
DR TopDownProteomics; P61089; -.
DR Antibodypedia; 1151; 379 antibodies from 39 providers.
DR DNASU; 93765; -.
DR Ensembl; ENSMUST00000099329; ENSMUSP00000096932; ENSMUSG00000074781.
DR GeneID; 93765; -.
DR KEGG; mmu:93765; -.
DR UCSC; uc007gwm.1; mouse.
DR CTD; 7334; -.
DR MGI; MGI:1934835; Ube2n.
DR VEuPathDB; HostDB:ENSMUSG00000074781; -.
DR eggNOG; KOG0417; Eukaryota.
DR GeneTree; ENSGT00540000070023; -.
DR HOGENOM; CLU_030988_13_2_1; -.
DR InParanoid; P61089; -.
DR OMA; QWKVNES; -.
DR OrthoDB; 1345547at2759; -.
DR PhylomeDB; P61089; -.
DR TreeFam; TF101126; -.
DR Reactome; R-MMU-1169408; ISG15 antiviral mechanism.
DR Reactome; R-MMU-168638; NOD1/2 Signaling Pathway.
DR Reactome; R-MMU-202424; Downstream TCR signaling.
DR Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-MMU-450302; activated TAK1 mediates p38 MAPK activation.
DR Reactome; R-MMU-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-MMU-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-MMU-5693571; Nonhomologous End-Joining (NHEJ).
DR Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-MMU-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-MMU-69473; G2/M DNA damage checkpoint.
DR Reactome; R-MMU-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-MMU-9020702; Interleukin-1 signaling.
DR Reactome; R-MMU-937039; IRAK1 recruits IKK complex.
DR Reactome; R-MMU-937041; IKK complex recruitment mediated by RIP1.
DR Reactome; R-MMU-9646399; Aggrephagy.
DR Reactome; R-MMU-975144; IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 93765; 36 hits in 111 CRISPR screens.
DR ChiTaRS; Ube2n; mouse.
DR PRO; PR:P61089; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P61089; protein.
DR Bgee; ENSMUSG00000074781; Expressed in spermatid and 227 other tissues.
DR ExpressionAtlas; P61089; baseline and differential.
DR Genevisible; P61089; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0031372; C:UBC13-MMS2 complex; ISS:HGNC-UCL.
DR GO; GO:0035370; C:UBC13-UEV1A complex; ISS:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043130; F:ubiquitin binding; ISS:HGNC-UCL.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:UniProtKB.
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:0000729; P:DNA double-strand break processing; ISS:HGNC-UCL.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:HGNC-UCL.
DR GO; GO:0016574; P:histone ubiquitination; ISS:HGNC-UCL.
DR GO; GO:0045739; P:positive regulation of DNA repair; ISS:HGNC-UCL.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; ISO:MGI.
DR GO; GO:0031058; P:positive regulation of histone modification; ISS:HGNC-UCL.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:HGNC-UCL.
DR GO; GO:1902533; P:positive regulation of intracellular signal transduction; ISO:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:HGNC-UCL.
DR GO; GO:1902523; P:positive regulation of protein K63-linked ubiquitination; ISO:MGI.
DR GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; ISS:HGNC-UCL.
DR GO; GO:0006301; P:postreplication repair; ISS:HGNC-UCL.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; ISS:HGNC-UCL.
DR GO; GO:0033182; P:regulation of histone ubiquitination; ISS:HGNC-UCL.
DR GO; GO:0050852; P:T cell receptor signaling pathway; ISS:HGNC-UCL.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:MGI.
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; Cytoplasm; Direct protein sequencing; DNA damage;
KW DNA repair; Isopeptide bond; Nucleotide-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..152
FT /note="Ubiquitin-conjugating enzyme E2 N"
FT /id="PRO_0000082504"
FT DOMAIN 3..149
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 87
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT MOD_RES 82
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P61088"
FT CROSSLNK 92
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ISG15)"
FT /evidence="ECO:0000250|UniProtKB:P61088"
FT CONFLICT 114
FT /note="A -> D (in Ref. 3; BAB24239)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 152 AA; 17138 MW; FACD84D883D77407 CRC64;
MAGLPRRIIK ETQRLLAEPV PGIKAEPDES NARYFHVVIA GPQDSPFEGG TFKLELFLPE
EYPMAAPKVR FMTKIYHPNV DKLGRICLDI LKDKWSPALQ IRTVLLSIQA LLSAPNPDDP
LANDVAEQWK TNEAQAIETA RAWTRLYAMN NI
