UBA1_BOVIN
ID UBA1_BOVIN Reviewed; 1058 AA.
AC A3KMV5;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 106.
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;
GN Name=UBA1; Synonyms=UBE1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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:0000305}.
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DR EMBL; BC133293; AAI33294.1; -; mRNA.
DR RefSeq; NP_001095947.1; NM_001102477.1.
DR RefSeq; XP_005228124.1; XM_005228067.3.
DR RefSeq; XP_005228125.1; XM_005228068.2.
DR RefSeq; XP_005228126.1; XM_005228069.2.
DR AlphaFoldDB; A3KMV5; -.
DR SMR; A3KMV5; -.
DR BioGRID; 159880; 1.
DR STRING; 9913.ENSBTAP00000022299; -.
DR PaxDb; A3KMV5; -.
DR PeptideAtlas; A3KMV5; -.
DR PRIDE; A3KMV5; -.
DR Ensembl; ENSBTAT00000022299; ENSBTAP00000022299; ENSBTAG00000016764.
DR GeneID; 282869; -.
DR KEGG; bta:282869; -.
DR CTD; 7317; -.
DR VEuPathDB; HostDB:ENSBTAG00000016764; -.
DR VGNC; VGNC:36561; UBA1.
DR eggNOG; KOG2012; Eukaryota.
DR GeneTree; ENSGT00940000158975; -.
DR HOGENOM; CLU_002556_0_0_1; -.
DR InParanoid; A3KMV5; -.
DR OrthoDB; 91748at2759; -.
DR TreeFam; TF300586; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000016764; Expressed in adenohypophysis and 105 other tissues.
DR ExpressionAtlas; A3KMV5; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
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 2: Evidence at transcript 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_0000328362"
FT REPEAT 63..199
FT /note="1-1"
FT REPEAT 459..611
FT /note="1-2"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..611
FT /note="2 approximate repeats"
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: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:0000250|UniProtKB:P22314"
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:0000250|UniProtKB:P22314"
FT MOD_RES 980
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P22314"
SQ SEQUENCE 1058 AA; 117830 MW; D723D3903025D982 CRC64;
MSSSPLSKKR RVSGPDPKPG SNCSPAHSVL SEVPSVPANG MAKNVSDADI DEGLYSRQLY
VLGHEAMKRL QTSSVLVSGL RGLGVEIAKN IILGGVKAVT LHDQGTAQWA DLSSQFYLRE
EDIGKNRAEV SQPRLAELNS YVPVSAYTGP LVEDFLSDFQ VVVLTNSPLE DQLRVGEFCH
SHGIKLVVAD TRGLFGQLFC DFGEEMILTD SNGEQPLSAM VSMVTKDNPG VVTCLDEARH
GFESGDFVSF SEVQGMIELN GSQPMEIKVL GPYTFSICDT SNFSDYIRGG IVSQVKVPKK
ISFKSLPASL AEPDFVMTDF AKYSRPAQLH IGFQALHHFC AQHGRSPRPH NEEDAAELVT
IAQAVNARSL PAVQQGSLDE DLIRKLAYVA AGDLAPINAF IGGLAAQEVM KACSGKFMPI
MQWLYFDALE CLPEDKEALT EDKCLPRQNR YDGQVAVFGS DLQERLGKQK YFLVGAGAIG
CELLKNFAMI GLGCAEDGEI VVTDMDTIEK SNLNRQFLFR PWDVTKLKSD TAAAAVRQMN
PHIRVTSHQN RVGPDTERIY DDDFFQNLDG VTNALDNVDA RMYMDRRCVY YRKPLLESGT
LGTKGNVQVV IPFLTESYSS SQDPPEKSIP ICTLKNFPNA IEHTLQWARD EFEGLFKQPA
ENVNQYLTDP KFVERTLRLA GTQPLEVLEA VQRSLVLQRP QTWADCVTWA CHHWHTQYSN
NIRQLLHNFP PDQLTSSGAP FWSGPKRCPH PLTFDVSNPL HLDYVIAAAN LFAQTYGLTG
SQDRAAVATL LQSVQVPEFT PKSGVKIHVS DQELQSANAS VDDSRLEELK ATLPSPEKLP
GFKMYPIDFE KDDDTNFHMD FIVAASNLRA ENYDIPPADR HKSKLIAGKI IPAIATTTAA
VVGLVCLELY KVVQGHRQLN SYKNGFLNLA LPFFGFSEPL AAPRHQYYNQ EWTLWDRFEV
QGLQPNGEEM TLKQFLDYFK TEHKLEITML SQGVSMLYSF FMPAAKLKER LDQPMTEIVS
RVSKRKLGRH VRALVLELCC NDESGEDVEV PYVRYTIR
