ID   UBA1_MOUSE              Reviewed;        1058 AA.
AC   Q02053; A6H6S6; P31253; Q542H8;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   27-MAR-2024, entry version 222.
DE   RecName: Full=Ubiquitin-like modifier-activating enzyme 1;
DE            EC=6.2.1.45 {ECO:0000250|UniProtKB:P22314};
DE   AltName: Full=Ubiquitin-activating enzyme E1;
DE   AltName: Full=Ubiquitin-activating enzyme E1 X;
DE   AltName: Full=Ubiquitin-like modifier-activating enzyme 1 X;
GN   Name=Uba1; Synonyms=Sbx, Ube1, Ube1ax, Ube1x;
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], FUNCTION, AND PATHWAY.
RX   PubMed=1511901; DOI=10.1016/0378-1119(92)90200-9;
RA   Imai N., Kaneda S., Nagai Y., Seno T., Ayusawa D., Hanaoka F., Yamao F.;
RT   "Cloning and sequence of a functionally active cDNA encoding the mouse
RT   ubiquitin-activating enzyme E1.";
RL   Gene 118:279-282(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Ovary, and Thymus;
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].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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 69-81; 90-97; 175-182; 227-239; 351-368; 375-384;
RP   386-411; 451-465; 471-485; 538-551; 559-581; 593-604; 636-671; 679-693;
RP   785-802; 844-851; 870-880; 890-923; 945-980 AND 1011-1021, AND
RP   IDENTIFICATION BY 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   NUCLEOTIDE SEQUENCE [MRNA] OF 615-1058.
RC   STRAIN=129/Sv;
RX   PubMed=1684224; DOI=10.1038/354483a0;
RA   Mitchell M.J., Woods D.R., Tucker P.K., Opp J.S., Bishop C.E.;
RT   "Homology of a candidate spermatogenic gene from the mouse Y chromosome to
RT   the ubiquitin-activating enzyme E1.";
RL   Nature 354:483-487(1991).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 655-763.
RC   STRAIN=BALB/c AnCr; TISSUE=Liver;
RX   PubMed=7714913; DOI=10.1007/bf00166597;
RA   Chang B.H.-J., Li W.H.;
RT   "Estimating the intensity of male-driven evolution in rodents by using X-
RT   linked and Y-linked Ube 1 genes and pseudogenes.";
RL   J. Mol. Evol. 40:70-77(1995).
RN   [8]
RP   REGULATION OF EXPRESSION BY THE THYROID HORMONE RECEPTOR.
RX   PubMed=7937138; DOI=10.1093/nar/22.20.4132;
RA   Caubin J., Iglesias T., Bernal J., Munoz A., Marquez G., Barbero J.L.,
RA   Zaballos A.;
RT   "Isolation of genomic DNA fragments corresponding to genes modulated in
RT   vivo by a transcription factor.";
RL   Nucleic Acids Res. 22:4132-4138(1994).
RN   [9]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=8948595; DOI=10.1006/dbio.1996.0305;
RA   Odorisio T., Mahadevaiah S.K., McCarrey J.R., Burgoyne P.S.;
RT   "Transcriptional analysis of the candidate spermatogenesis gene Ube1y and
RT   of the closely related Ube1x shows that they are coexpressed in
RT   spermatogonia and spermatids but are repressed in pachytene
RT   spermatocytes.";
RL   Dev. Biol. 180:336-343(1996).
RN   [10]
RP   ISGYLATION.
RX   PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
RA   Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
RA   Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
RT   "Proteomic identification of proteins conjugated to ISG15 in mouse and
RT   human cells.";
RL   Biochem. Biophys. Res. Commun. 336:496-506(2005).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-55, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Mast cell;
RX   PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-816 AND SER-820, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-21; SER-24; SER-46;
RP   SER-810; SER-816; SER-820 AND SER-835, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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   [14]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-671, SUCCINYLATION [LARGE SCALE
RP   ANALYSIS] AT LYS-528, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 626-891.
RX   PubMed=15774460; DOI=10.1074/jbc.m502583200;
RA   Szczepanowski R.H., Filipek R., Bochtler M.;
RT   "Crystal structure of a fragment of mouse ubiquitin-activating enzyme.";
RL   J. Biol. Chem. 280:22006-22011(2005).
CC   -!- FUNCTION: Catalyzes the first step in ubiquitin conjugation to mark
CC       cellular proteins for degradation through the ubiquitin-proteasome
CC       system (PubMed:1511901). Activates ubiquitin by first adenylating its
CC       C-terminal glycine residue with ATP, and thereafter linking this
CC       residue to the side chain of a cysteine residue in E1, yielding a
CC       ubiquitin-E1 thioester and free AMP. Essential for the formation of
CC       radiation-induced foci, timely DNA repair and for response to
CC       replication stress. Promotes the recruitment of TP53BP1 and BRCA1 at
CC       DNA damage sites. {ECO:0000250|UniProtKB:P22314,
CC       ECO:0000305|PubMed:1511901}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
CC         = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-
CC         L-cysteine.; EC=6.2.1.45; Evidence={ECO:0000250|UniProtKB:P22314};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000305|PubMed:1511901}.
CC   -!- SUBUNIT: Monomer. Interacts with GAN (via BTB domain).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P22314}.
CC       Mitochondrion {ECO:0000250|UniProtKB:P22314}. Nucleus
CC       {ECO:0000250|UniProtKB:P22314}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed. In testis, expressed in A
CC       spermatogonia and spermatids but at very low levels in pachytene
CC       spermatocytes. {ECO:0000269|PubMed:8948595}.
CC   -!- DEVELOPMENTAL STAGE: In testis, highly expressed from 14.5 days post
CC       coitum (dpc) until the day of birth, with levels falling after 10 days
CC       post partum (dpp) but peaking again at 28 dpp.
CC       {ECO:0000269|PubMed:8948595}.
CC   -!- INDUCTION: May be modulated by the thyroid hormone receptor.
CC   -!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
CC   -!- MISCELLANEOUS: There are two active sites within the E1 molecule,
CC       allowing it to accommodate two ubiquitin moieties at a time, with a new
CC       ubiquitin forming an adenylate intermediate as the previous one is
CC       transferred to the thiol site. {ECO:0000250|UniProtKB:P22515}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA44465.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; D10576; BAA01433.1; -; mRNA.
DR   EMBL; AK088057; BAC40121.1; -; mRNA.
DR   EMBL; AK088528; BAC40405.1; -; mRNA.
DR   EMBL; AK143416; BAE25369.1; -; mRNA.
DR   EMBL; AK171667; BAE42599.1; -; mRNA.
DR   EMBL; AL807240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC058630; AAH58630.1; -; mRNA.
DR   EMBL; BC145984; AAI45985.1; -; mRNA.
DR   EMBL; X62580; CAA44465.1; ALT_FRAME; mRNA.
DR   EMBL; U09051; AAC52169.1; -; Genomic_DNA.
DR   EMBL; U09055; AAC52171.1; -; Genomic_DNA.
DR   CCDS; CCDS30044.1; -.
DR   PIR; I48756; I48756.
DR   PIR; I63168; I63168.
DR   PIR; JC1254; JC1254.
DR   RefSeq; NP_001129557.1; NM_001136085.2.
DR   RefSeq; NP_001263245.1; NM_001276316.1.
DR   RefSeq; NP_001263246.1; NM_001276317.1.
DR   RefSeq; NP_033483.2; NM_009457.4.
DR   PDB; 1Z7L; X-ray; 2.80 A; A/B/C=626-891.
DR   PDB; 2LZJ; NMR; -; A=202-312.
DR   PDB; 2V31; NMR; -; A=202-312.
DR   PDBsum; 1Z7L; -.
DR   PDBsum; 2LZJ; -.
DR   PDBsum; 2V31; -.
DR   AlphaFoldDB; Q02053; -.
DR   BMRB; Q02053; -.
DR   SMR; Q02053; -.
DR   BioGRID; 204410; 63.
DR   ELM; Q02053; -.
DR   IntAct; Q02053; 9.
DR   MINT; Q02053; -.
DR   STRING; 10090.ENSMUSP00000001989; -.
DR   ChEMBL; CHEMBL5169143; -.
DR   GlyGen; Q02053; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q02053; -.
DR   MetOSite; Q02053; -.
DR   PhosphoSitePlus; Q02053; -.
DR   SwissPalm; Q02053; -.
DR   EPD; Q02053; -.
DR   jPOST; Q02053; -.
DR   MaxQB; Q02053; -.
DR   PaxDb; 10090-ENSMUSP00000001989; -.
DR   ProteomicsDB; 298351; -.
DR   Pumba; Q02053; -.
DR   Antibodypedia; 345; 466 antibodies from 40 providers.
DR   DNASU; 22201; -.
DR   Ensembl; ENSMUST00000001989.9; ENSMUSP00000001989.9; ENSMUSG00000001924.16.
DR   Ensembl; ENSMUST00000089217.11; ENSMUSP00000086626.5; ENSMUSG00000001924.16.
DR   GeneID; 22201; -.
DR   KEGG; mmu:22201; -.
DR   UCSC; uc009stl.2; mouse.
DR   AGR; MGI:98890; -.
DR   CTD; 7317; -.
DR   MGI; MGI:98890; Uba1.
DR   VEuPathDB; HostDB:ENSMUSG00000001924; -.
DR   eggNOG; KOG2012; Eukaryota.
DR   GeneTree; ENSGT00940000158975; -.
DR   HOGENOM; CLU_002556_0_0_1; -.
DR   InParanoid; Q02053; -.
DR   OMA; GANLHAF; -.
DR   OrthoDB; 20494at2759; -.
DR   PhylomeDB; Q02053; -.
DR   TreeFam; TF300586; -.
DR   BRENDA; 6.2.1.45; 3474.
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; 22201; 31 hits in 77 CRISPR screens.
DR   ChiTaRS; Uba1; mouse.
DR   EvolutionaryTrace; Q02053; -.
DR   PRO; PR:Q02053; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q02053; Protein.
DR   Bgee; ENSMUSG00000001924; Expressed in cortical plate and 271 other cell types or tissues.
DR   ExpressionAtlas; Q02053; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0030057; C:desmosome; IEA:Ensembl.
DR   GO; GO:0010008; C:endosome membrane; IEA:Ensembl.
DR   GO; GO:0000792; C:heterochromatin; IEA:Ensembl.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004839; F:ubiquitin activating enzyme activity; IDA:MGI.
DR   GO; GO:0006974; P:DNA damage response; ISO:MGI.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   CDD; cd01491; Ube1_repeat1; 1.
DR   CDD; cd01490; Ube1_repeat2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 2.40.30.180; Ubiquitin-activating enzyme E1, FCCH domain; 1.
DR   Gene3D; 3.50.50.80; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 1; 1.
DR   Gene3D; 3.40.50.12550; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 2; 1.
DR   Gene3D; 1.10.10.2660; Ubiquitin-activating enzyme E1, SCCH domain; 1.
DR   Gene3D; 3.10.290.60; Ubiquitin-activating enzyme E1, UFD domain; 1.
DR   InterPro; IPR032420; E1_4HB.
DR   InterPro; IPR032418; E1_FCCH.
DR   InterPro; IPR042302; E1_FCCH_sf.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR018965; Ub-activating_enz_E1_C.
DR   InterPro; IPR042449; Ub-E1_IAD_1.
DR   InterPro; IPR038252; UBA_E1_C_sf.
DR   InterPro; IPR019572; UBA_E1_SCCH.
DR   InterPro; IPR042063; Ubi_acti_E1_SCCH.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   InterPro; IPR018075; UBQ-activ_enz_E1.
DR   InterPro; IPR018074; UBQ-activ_enz_E1_CS.
DR   InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR   InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR   NCBIfam; TIGR01408; Ube1; 1.
DR   PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR   PANTHER; PTHR10953:SF155; UBIQUITIN-LIKE MODIFIER-ACTIVATING ENZYME 1; 1.
DR   Pfam; PF16191; E1_4HB; 1.
DR   Pfam; PF16190; E1_FCCH; 1.
DR   Pfam; PF09358; E1_UFD; 1.
DR   Pfam; PF00899; ThiF; 2.
DR   Pfam; PF10585; UBA_E1_SCCH; 1.
DR   PRINTS; PR01849; UBIQUITINACT.
DR   SMART; SM00985; UBA_e1_C; 1.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 2.
DR   PROSITE; PS00536; UBIQUITIN_ACTIVAT_1; 1.
DR   PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
DR   Genevisible; Q02053; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; ATP-binding; Cytoplasm;
KW   Direct protein sequencing; Ligase; Mitochondrion; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation;
KW   Ubl conjugation pathway.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P22314"
FT   CHAIN           2..1058
FT                   /note="Ubiquitin-like modifier-activating enzyme 1"
FT                   /id="PRO_0000194935"
FT   REPEAT          63..199
FT                   /note="1-1"
FT   REPEAT          459..611
FT                   /note="1-2"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          63..611
FT                   /note="2 approximate repeats"
FT   COMPBIAS        20..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        632
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10132"
FT   BINDING         478
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P22515"
FT   BINDING         504
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P22515"
FT   BINDING         515
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P22515"
FT   BINDING         528
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P22515"
FT   BINDING         576..577
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P22515"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P22314"
FT   MOD_RES         4
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P22314"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         21
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         24
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         46
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         55
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:17947660"
FT   MOD_RES         528
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         671
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         800
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P22314"
FT   MOD_RES         810
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         816
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         820
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         835
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         980
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P22314"
FT   CONFLICT        963
FT                   /note="L -> V (in Ref. 6; CAA44465)"
FT                   /evidence="ECO:0000305"
FT   TURN            203..205
FT                   /evidence="ECO:0007829|PDB:2LZJ"
FT   STRAND          218..225
FT                   /evidence="ECO:0007829|PDB:2LZJ"
FT   STRAND          227..234
FT                   /evidence="ECO:0007829|PDB:2LZJ"
FT   STRAND          246..255
FT                   /evidence="ECO:0007829|PDB:2LZJ"
FT   HELIX           257..260
FT                   /evidence="ECO:0007829|PDB:2LZJ"
FT   STRAND          265..278
FT                   /evidence="ECO:0007829|PDB:2LZJ"
FT   HELIX           280..282
FT                   /evidence="ECO:0007829|PDB:2LZJ"
FT   STRAND          288..294
FT                   /evidence="ECO:0007829|PDB:2LZJ"
FT   HELIX           631..635
FT                   /evidence="ECO:0007829|PDB:1Z7L"
FT   HELIX           641..656
FT                   /evidence="ECO:0007829|PDB:1Z7L"
FT   HELIX           658..666
FT                   /evidence="ECO:0007829|PDB:1Z7L"
FT   HELIX           671..677
FT                   /evidence="ECO:0007829|PDB:1Z7L"
FT   HELIX           683..695
FT                   /evidence="ECO:0007829|PDB:1Z7L"
FT   TURN            696..698
FT                   /evidence="ECO:0007829|PDB:1Z7L"
FT   HELIX           703..718
FT                   /evidence="ECO:0007829|PDB:1Z7L"
FT   HELIX           720..728
FT                   /evidence="ECO:0007829|PDB:1Z7L"
FT   STRAND          740..742
FT                   /evidence="ECO:0007829|PDB:1Z7L"
FT   HELIX           759..775
FT                   /evidence="ECO:0007829|PDB:1Z7L"
FT   HELIX           784..792
FT                   /evidence="ECO:0007829|PDB:1Z7L"
FT   STRAND          809..811
FT                   /evidence="ECO:0007829|PDB:1Z7L"
FT   HELIX           824..832
FT                   /evidence="ECO:0007829|PDB:1Z7L"
FT   HELIX           836..838
FT                   /evidence="ECO:0007829|PDB:1Z7L"
FT   HELIX           858..872
FT                   /evidence="ECO:0007829|PDB:1Z7L"
FT   HELIX           880..886
FT                   /evidence="ECO:0007829|PDB:1Z7L"
SQ   SEQUENCE   1058 AA;  117809 MW;  95D8152ED5C8E037 CRC64;
     MSSSPLSKKR RVSGPDPKPG SNCSPAQSAL SEVSSVPTNG MAKNGSEADI DESLYSRQLY
     VLGHEAMKML QTSSVLVSGL RGLGVEIAKN IILGGVKAVT LHDQGTTQWA DLSSQFYLRE
     EDIGKNRAEV SQPRLAELNS YVPVTAYTGP LVEDFLSSFQ VVVLTNSPLE AQLRVGEFCH
     SRGIKLVVAD TRGLFGQLFC DFGEEMVLTD SNGEQPLSAM VSMVTKDNPG VVTCLDEARH
     GFETGDFVSF SEVQGMIQLN GCQPMEIKVL GPYTFSICDT SNFSDYIRGG IVSQVKVPKK
     ISFKSLPASL VEPDFVMTDF AKYSRPAQLH IGFQALHQFC ALHNQPPRPR NEEDATELVG
     LAQAVNARSP PSVKQNSLDE DLIRKLAYVA AGDLAPINAF IGGLAAQEVM KACSGKFMPI
     MQWLYFDALE CLPEDKEALT EEKCLPRQNR YDGQVAVFGS DFQEKLSKQK YFLVGAGAIG
     CELLKNFAMI GLGCGEGGEV VVTDMDTIEK SNLNRQFLFR PWDVTKLKSD TAAAAVRQMN
     PYIQVTSHQN RVGPDTERIY DDDFFQNLDG VANALDNIDA RMYMDRRCVY YRKPLLESGT
     LGTKGNVQVV IPFLTESYSS SQDPPEKSIP ICTLKNFPNA IEHTLQWARD EFEGLFKQPA
     ENVNQYLTDS KFVERTLRLA GTQPLEVLEA VQRSLVLQRP QTWGDCVTWA CHHWHTQYCN
     NIRQLLHNFP PDQLTSSGAP FWSGPKRCPH PLTFDVNNTL HLDYVMAAAN LFAQTYGLTG
     SQDRAAVASL LQSVQVPEFT PKSGVKIHVS DQELQSANAS VDDSRLEELK ATLPSPDKLP
     GFKMYPIDFE KDDDSNFHMD FIVAASNLRA ENYDISPADR HKSKLIAGKI IPAIATTTAA
     VVGLVCLELY KVVQGHQQLD SYKNGFLNLA LPFFGFSEPL AAPRHQYYNQ EWTLWDRFEV
     QGLQPNGEEM TLKQFLDYFK TEHKLEITML SQGVSMLYSF FMPAAKLKER LDQPMTEIVS
     RVSKRKLGRH VRALVLELCC NDESGEDVEV PYVRYTIR
//