ID   UBA1_RAT                Reviewed;        1058 AA.
AC   Q5U300;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   27-MAR-2024, entry version 148.
DE   RecName: Full=Ubiquitin-like modifier-activating enzyme 1 {ECO:0000250|UniProtKB:Q02053};
DE            EC=6.2.1.45 {ECO:0000250|UniProtKB:P22314};
DE   AltName: Full=Ubiquitin-activating enzyme E1 {ECO:0000250|UniProtKB:Q02053};
GN   Name=Uba1 {ECO:0000312|EMBL:AAH85791.1, ECO:0000312|RGD:1359327};
GN   Synonyms=Ube1 {ECO:0000250|UniProtKB:Q02053};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:EDL97701.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000312|EMBL:AAH85791.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Brown Norway {ECO:0000269|PubMed:15489334};
RC   TISSUE=Kidney {ECO:0000312|EMBL:AAH85791.1};
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   [3] {ECO:0000305, ECO:0000312|EMBL:EDL97701.1}
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RA   Maurya D.K., Bhargava P.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-835, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Catalyzes the first step in ubiquitin conjugation to mark
CC       cellular proteins for degradation through the ubiquitin-proteasome
CC       system. Activates ubiquitin by first adenylating its C-terminal glycine
CC       residue with ATP, and thereafter linking this residue to the side chain
CC       of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free
CC       AMP. Essential for the formation of radiation-induced foci, timely DNA
CC       repair and for response to replication stress. Promotes the recruitment
CC       of TP53BP1 and BRCA1 at DNA damage sites.
CC       {ECO:0000250|UniProtKB:P22314}.
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:0000250|UniProtKB:P22314}.
CC   -!- SUBUNIT: Monomer. Interacts with GAN (via BTB domain) (By similarity).
CC       {ECO:0000250|UniProtKB:Q02053}.
CC   -!- INTERACTION:
CC       Q5U300; Q9H2C0: GAN; Xeno; NbExp=2; IntAct=EBI-40204881, EBI-764342;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P22314}.
CC       Mitochondrion {ECO:0000250|UniProtKB:P22314}. Nucleus
CC       {ECO:0000250|UniProtKB:P22314}.
CC   -!- PTM: ISGylated. {ECO:0000250|UniProtKB:P22314}.
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:0000255}.
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DR   EMBL; CH474009; EDL97701.1; -; Genomic_DNA.
DR   EMBL; CH474009; EDL97702.1; -; Genomic_DNA.
DR   EMBL; BC085791; AAH85791.1; -; mRNA.
DR   RefSeq; NP_001014102.1; NM_001014080.1.
DR   RefSeq; XP_006256674.1; XM_006256612.3.
DR   RefSeq; XP_006256675.2; XM_006256613.3.
DR   AlphaFoldDB; Q5U300; -.
DR   BMRB; Q5U300; -.
DR   SMR; Q5U300; -.
DR   BioGRID; 260716; 4.
DR   IntAct; Q5U300; 1.
DR   STRING; 10116.ENSRNOP00000033950; -.
DR   GlyGen; Q5U300; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q5U300; -.
DR   PhosphoSitePlus; Q5U300; -.
DR   SwissPalm; Q5U300; -.
DR   jPOST; Q5U300; -.
DR   PaxDb; 10116-ENSRNOP00000033950; -.
DR   Ensembl; ENSRNOT00055028048; ENSRNOP00055022563; ENSRNOG00055016495.
DR   Ensembl; ENSRNOT00060037267; ENSRNOP00060030747; ENSRNOG00060021167.
DR   Ensembl; ENSRNOT00065034509; ENSRNOP00065027656; ENSRNOG00065020374.
DR   GeneID; 314432; -.
DR   KEGG; rno:314432; -.
DR   UCSC; RGD:1359327; rat.
DR   AGR; RGD:1359327; -.
DR   CTD; 7317; -.
DR   RGD; 1359327; Uba1.
DR   VEuPathDB; HostDB:ENSRNOG00000019164; -.
DR   eggNOG; KOG2012; Eukaryota.
DR   HOGENOM; CLU_002556_0_0_1; -.
DR   InParanoid; Q5U300; -.
DR   OrthoDB; 20494at2759; -.
DR   PhylomeDB; Q5U300; -.
DR   TreeFam; TF300586; -.
DR   Reactome; R-RNO-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR   Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q5U300; -.
DR   Proteomes; UP000002494; Chromosome X.
DR   Proteomes; UP000234681; Chromosome x.
DR   Bgee; ENSRNOG00000019164; Expressed in spleen and 19 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0000792; C:heterochromatin; ISO:RGD.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004839; F:ubiquitin activating enzyme activity; ISO:RGD.
DR   GO; GO:0006974; P:DNA damage response; ISO:RGD.
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; Q5U300; RN.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cytoplasm; Ligase; Mitochondrion;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Ubl conjugation; 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_0000365096"
FT   REPEAT          63..199
FT                   /note="1-1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          459..611
FT                   /note="1-2"
FT                   /evidence="ECO:0000255"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          63..611
FT                   /note="2 approximate repeats"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        18..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        632
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q02053,
FT                   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:0000250|UniProtKB:P22314"
FT   MOD_RES         21
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q02053"
FT   MOD_RES         24
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q02053"
FT   MOD_RES         46
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         55
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q02053"
FT   MOD_RES         528
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q02053"
FT   MOD_RES         671
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P22314"
FT   MOD_RES         800
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P22314"
FT   MOD_RES         810
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P22314"
FT   MOD_RES         816
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q02053"
FT   MOD_RES         820
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P22314"
FT   MOD_RES         835
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         980
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P22314"
SQ   SEQUENCE   1058 AA;  117788 MW;  FAC21190A3014F79 CRC64;
     MSSSPLSKKR RVSGPDPKPG SNCSSAQSVL SEVSSVPTNG MAKNGSEADI DESLYSRQLY
     VLGHEAMKML QTSSVLVSGL RGLGVEIAKN IILGGVKAVT LHDQGTTQWA DLSSQFYLRE
     EDIGKNRAEV SQPRLAELNS YVPVTAYTGP LVEDFLSGFQ VVVLTNSPLE EQLRVGEFCH
     SRGIKLVVAD TRGLFGQLFC DFGEEMVLTD SNGEQPLSAM VSMVTKDNPG VVTCLDEARH
     GFETGDFVSF SEVQGMVQLN GCQPIEIKVL GPYTFSICDT SNFSDYIRGG IVSQVKVPKK
     ISFKSLPASL AEPDFVMTDF AKYSRPAQLH IGFQALHQFC AQHNRPPRPR NEEDATELVT
     LAQAVNARSP PAVQQDNVDE DLIRKLAYVA AGDLAPINAF IGGLAAQEVM KACSGKFMPI
     MQWLYFDALE CLPEDKEALT EDKCLPRQNR YDGQVAVFGS DLQEKLGKQK YFLVGAGAIG
     CELLKNFAMI GLGCGEGGEV VVTDMDTIEK SNLNRQFLFR PWDVTKLKSD TAAAAVRQMN
     PYIQVTSHQN RVGPDTERIY DDDFFQNLDG VANALDNVDA 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
//