UBA1_RAT
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 03-AUG-2022, entry version 140.
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 -!- 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 STRING; 10116.ENSRNOP00000033950; -.
DR iPTMnet; Q5U300; -.
DR PhosphoSitePlus; Q5U300; -.
DR jPOST; Q5U300; -.
DR PaxDb; Q5U300; -.
DR PRIDE; Q5U300; -.
DR GeneID; 314432; -.
DR KEGG; rno:314432; -.
DR UCSC; RGD:1359327; rat.
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 OMA; GANLHAF; -.
DR OrthoDB; 91748at2759; -.
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 tissues.
DR Genevisible; Q5U300; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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; IEA:Ensembl.
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; ISO:RGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:RGD.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 1.10.10.2660; -; 1.
DR Gene3D; 2.40.30.180; -; 1.
DR Gene3D; 3.10.290.60; -; 1.
DR Gene3D; 3.50.50.80; -; 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 PANTHER; PTHR10953; PTHR10953; 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_thiolCys; 1.
DR PRINTS; PR01849; UBIQUITINACT.
DR SMART; SM00985; UBA_e1_C; 1.
DR SUPFAM; SSF69572; SSF69572; 2.
DR TIGRFAMs; TIGR01408; Ube1; 1.
DR PROSITE; PS00536; UBIQUITIN_ACTIVAT_1; 1.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
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
