ID   UBE12_ARATH             Reviewed;        1077 AA.
AC   P92974;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   02-SEP-2026, entry version 181.
DE   RecName: Full=Ubiquitin-activating enzyme E1 2;
DE            Short=AtUBA2 {ECO:0000303|PubMed:9076989};
DE            EC=6.2.1.45 {ECO:0000269|PubMed:9076989};
GN   Name=UBA2; OrderedLocusNames=At5g06460; ORFNames=MHF15.2;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. Columbia;
RX   PubMed=9076989; DOI=10.1046/j.1365-313x.1997.11020213.x;
RA   Hatfield P.M., Gosink M.M., Carpenter T.B., Vierstra R.D.;
RT   "The ubiquitin-activating enzyme (E1) gene family in Arabidopsis
RT   thaliana.";
RL   Plant J. 11:213-226(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA   Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT   features of the regions of 1,044,062 bp covered by thirteen physically
RT   assigned P1 clones.";
RL   DNA Res. 4:291-300(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=17217463; DOI=10.1111/j.1365-313x.2006.02978.x;
RA   Goritschnig S., Zhang Y., Li X.;
RT   "The ubiquitin pathway is required for innate immunity in Arabidopsis.";
RL   Plant J. 49:540-551(2007).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Columbia;
RX   PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA   Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA   Rathjen J.P., Peck S.C.;
RT   "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT   thaliana.";
RL   J. Proteomics 72:439-451(2009).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
CC   -!- FUNCTION: Activates ubiquitin by first adenylating its C-terminal
CC       glycine residue with ATP, and thereafter linking this residue to the
CC       side chain of a cysteine residue in E1, yielding a ubiquitin-E1
CC       thioester and free AMP. {ECO:0000269|PubMed:9076989}.
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:0000269|PubMed:9076989};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000269|PubMed:9076989}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves, flowers, roots and stems.
CC       Detected in germinating seeds, cotyledons, hypocotyls, vascular
CC       tissues, anthers, filaments, pollen, style, stigma, sepals, petals,
CC       ovary, developing ovules, funiculi and silique walls.
CC       {ECO:0000269|PubMed:9076989}.
CC   -!- DEVELOPMENTAL STAGE: Expressed over the entire range of development.
CC       {ECO:0000269|PubMed:9076989}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype and no changes in disease
CC       susceptibility. {ECO:0000269|PubMed:17217463}.
CC   -!- MISCELLANEOUS: Both UBA1 and UBA2 are able to activate ubiquitin and
CC       transfer it to the E2s with equal efficiency.
CC       {ECO:0000269|PubMed:9076989}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC       {ECO:0000305}.
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DR   EMBL; U40566; AAB37569.1; -; Genomic_DNA.
DR   EMBL; AB006700; BAB08968.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91020.1; -; Genomic_DNA.
DR   EMBL; OZ408687; CAO7051282.1; -; Genomic_DNA.
DR   AlphaFoldDB; P92974; -.
DR   SMR; P92974; -.
DR   BioGRID; 15813; 31.
DR   FunCoup; P92974; 4401.
DR   IntAct; P92974; 1.
DR   STRING; 3702.P92974; -.
DR   iPTMnet; P92974; -.
DR   PaxDb; 3702-P92974; -.
DR   ProteomicsDB; 228718; -.
DR   GeneID; 830534; -.
DR   KEGG; ath:AT5G06460; -.
DR   Araport; AT5G06460; -.
DR   TAIR; AT5G06460; UBA 2.
DR   eggNOG; KOG2012; Eukaryota.
DR   HOGENOM; CLU_002556_0_0_1; -.
DR   InParanoid; P92974; -.
DR   OMA; WVKSPSK; -.
DR   OrthoDB; 10252231at2759; -.
DR   PhylomeDB; P92974; -.
DR   BRENDA; 2.3.2.23; 399.
DR   BRENDA; 6.2.1.45; 399.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:P92974; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; P92974; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0004839; F:ubiquitin activating enzyme activity; IMP:TIGR.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR   GO; GO:0006974; P:DNA damage response; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:TAIR.
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   FunFam; 3.40.50.12550:FF:000001; Ubiquitin-activating enzyme E1 1; 1.
DR   FunFam; 3.40.50.720:FF:000015; Ubiquitin-activating enzyme E1 1; 1.
DR   FunFam; 1.10.10.2660:FF:000002; Ubiquitin-activating enzyme E1 2; 1.
DR   FunFam; 3.10.290.60:FF:000001; Ubiquitin-activating enzyme E1 2; 1.
DR   FunFam; 3.50.50.80:FF:000003; Ubiquitin-activating enzyme E1 2; 1.
DR   FunFam; 2.40.30.180:FF:000001; ubiquitin-like modifier-activating enzyme 1; 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:SF235; UBIQUITIN-ACTIVATING ENZYME E1 2; 1.
DR   Pfam; PF16191; E1_4HB; 1.
DR   Pfam; PF16190; E1_FCCH; 1.
DR   Pfam; PF09358; E1_UFD; 1.
DR   Pfam; PF00899; ThiF; 1.
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.
PE   1: Evidence at protein level;
KW   ATP-binding; Ligase; Nucleotide-binding; Reference proteome;
KW   Ubl conjugation pathway.
FT   CHAIN           1..1077
FT                   /note="Ubiquitin-activating enzyme E1 2"
FT                   /id="PRO_0000399396"
FT   REGION          16..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        653
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10132"
FT   BINDING         499
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P22515"
FT   BINDING         525
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P22515"
FT   BINDING         536
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P22515"
FT   BINDING         549
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P22515"
FT   BINDING         597..598
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P22515"
SQ   SEQUENCE   1077 AA;  119624 MW;  CE39A36AAA99A218 CRC64;
     MEPFVVKENI IASASSPMKK RRIDHTESAD GSAINASNSS SIGLNNSIGG NDTVMSMAEF
     GNDNSNNQEI DEDLHSRQLA VYGRETMRKL FASNVLISGM QGLGVEIAKN IILAGVKSVT
     LHDENVVELW DLSSNFVFTE EDIGKNRALA SVHKLQELNN AVAVSTLTGK LTKEQLSDFQ
     VVVFVDISFE KATEIDDYCH SHQPPIAFIK ADVRGLFGSL FCDFGPHFTV LDVDGEEPHS
     GIIASVSNEN PGFVSCVDDE RLEFEDGNLV VFSEVEGMTE LNDGKPRKIK NVKPFSFTLE
     EDTSSYGQYM KGGIVTQVKQ PKVLNFKPLR EALKDPGDFL LSDFSKFDRP PLLHLAFQAL
     DRFSSQAGRF PFAGSEEDAQ KLVEIAVDIN EGLGDARLED VNSKLLRHLA FGSRAVLNPM
     AAMFGGIVGQ EVVKACSGKF HPIFQFFYFD SVESLPKEPL DASEFRPQNS RYDAQISVFG
     STLQKKLEDA RVFVVGAGAL GCEFLKNLAL MGVSCGTQGK LTVTDDDVIE KSNLSRQFLF
     RDWNIGQAKS TVAATAAAGI NSRLNIDALQ NRVGPETENV FDDSFWENLT VVVNALDNVT
     ARLYVDSRCV YFQKPLLESG TLGAKCNTQM VIPHLTENYG ASRDPPEKQA PMCTVHSFPH
     NIDHCLTWAR SEFEGLLEKT PAEVNAYLSD PVEYMKAMRT AGDAQARDTL GRVVECLEKE
     KCNSFQDCIT WARLRFEDYF ANRVKQLCYT FPEDAATSTG APFWSAPKRF PRPLQFSSTD
     LSHINFVMAA SILRAETFGI PTPEWAKTRA GLAEAVERVI VPDFEPKKDA TIVTDEKATT
     LSTASVDDAA VIDELNAKLV RCRMSLQPEF RMKAIQFEKD DDTNYHMDMI AGLANMRARN
     YSVPEVDKLK AKFIAGRIIP AIATSTAMAT GFVCLEMYKV LDGSHKVEDY RNTFANLALP
     LFSMAEPVPP KVVKHQDQSW TVWDRWVMRG NPTLRELLDW LKEKGLNAYS ISCGSSLLYN
     SMFSRHKERM NRRVVDLARD VAGVELPAYR RHVDVVVACE DDNDADVDIP LVSVYFA
//