UBA1_RABIT
ID UBA1_RABIT Reviewed; 1058 AA.
AC Q29504;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme 1;
DE EC=6.2.1.45 {ECO:0000305|PubMed:9322736};
DE AltName: Full=Ubiquitin-activating enzyme E1;
GN Name=UBA1; Synonyms=UBE1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=9322736; DOI=10.1016/s0378-1119(97)00154-6;
RA Sun B., Jeyaseelan K., Chung M.C.M., Teo T.S.;
RT "Rabbit ubiquitin-activating enzyme E1: cDNA cloning, sequence and
RT expression.";
RL Gene 196:19-23(1997).
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 (PubMed:9322736). Essential for the formation of radiation-induced
CC foci, timely DNA repair and for response to replication stress.
CC Promotes the recruitment of TP53BP1 and BRCA1 at DNA damage sites (By
CC similarity). {ECO:0000250|UniProtKB:P22314,
CC ECO:0000305|PubMed:9322736}.
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:0000305|PubMed:9322736};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:9322736}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P22314}.
CC Mitochondrion {ECO:0000250|UniProtKB:P22314}. Nucleus
CC {ECO:0000250|UniProtKB:P22314}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9322736}.
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; U58653; AAC48768.1; -; mRNA.
DR RefSeq; NP_001075840.1; NM_001082371.2.
DR AlphaFoldDB; Q29504; -.
DR SMR; Q29504; -.
DR BioGRID; 1172246; 5.
DR IntAct; Q29504; 8.
DR STRING; 9986.ENSOCUP00000007237; -.
DR GeneID; 100009225; -.
DR KEGG; ocu:100009225; -.
DR CTD; 7317; -.
DR eggNOG; KOG2012; Eukaryota.
DR InParanoid; Q29504; -.
DR OrthoDB; 91748at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001811; Unplaced.
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; IEA:UniProtKB-EC.
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 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_0000194936"
FT REPEAT 63..199
FT /note="1-1"
FT REPEAT 459..611
FT /note="1-2"
FT REGION 1..47
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: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; 117688 MW; 1196EAC5EEEC06A5 CRC64;
MSSSPLSKKR RVSGPDPKPG SNCSPAQSVL PQVPSAPTNG MAKNGSEADI DEGLYSRQLY
VLGHEAMKRL QTSSVLVSGL RGLGVEIAKN IILGGVKAVT LHDQGTAQWA DLSSQFYLRE
EDIGKNRAEV SQPRLAELNS YVPVTAYTGP LVEDFLSGFQ VVVLTNSPLE DQLRVGEFCH
SRGIKLVVAD TRGLFGQLFC DFGEEMILTD SNGEQPLSTM VSMVTKDNPG VVTCLDEARH
GFESGDFVSF SEVQGMTELN GNQPIEIKVL GPYTFSICDT SNFSDYIRGG IVSQVKVPKK
ISFKSLSASL AEPDFVMTDF AKFSRPAQLH IGFQALHKFC AQHSRPPRPR NEEDAAELVT
LARAVNSKAS SAVQQDSLDE DLIRNLAFVA AGDLAPINAF IGGLAAQEVM KACSGKFMPI
MQWLYFDALE CLPEDKESLT EDKCLPRQNR YDGQVAVFGS DLQEKLGRQK YFLVGAGAIG
CELLKNFAMI GLGCGENGEI IVTDMDTIEK SNLNRQFLFR PWDVTKLKSD TAAAAVHQMN
PHIRVTSHQN RVGPDTERIY DDDFFQTLDG VANALDNVDA RMYMDRRCVY YRKPLLESGT
LGTKGNVQVV IPFLTESYSS SQDPPEKSIP ICTLKNFPNA IEHTLQWARD EFEGLFKQPA
ENVNQYLTDP KFVERTLRLA GTQPLEVLEA VQRSLVLQLP QSWADCVTWA CHHWHTQYSN
NIRQLLHNFP PDQLTSSGAP FWSGPKRCPH PLTFDVSNPL HLDYVMAAAN LFAQTYGLAG
SQDRAAVATL LQSVQVPEFT PKSGVKIHVS DQELQSANAS VDDSRLEELK ATLPSPDKLP
GFKMYPIDFE KDDDSNFHMD FIVAASNLRA ENYDIPPADR HKSKLIAGKI IPAIATTTAA
VVGLVCLELY KVVQGHRHLD SYKNGFLNLA LPFFGFSEPL AAPRHQYYNQ EWTLWDRFEV
QGLQPNGEEM TLKQFLDYFK TEHKLEITML SQGVSMLYSF FMPAAKLKER LDQPMTEIVS
RVSKRKLGRH VRALVLELCC NDESGEDVEV PYVRYTIR
