ULA1_YEAST
ID ULA1_YEAST Reviewed; 462 AA.
AC Q12059; D6W409;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=NEDD8-activating enzyme E1 regulatory subunit;
DE AltName: Full=E1 N-terminus-related protein 2;
DE AltName: Full=Ubiquitin-activating enzyme E1-like 1;
DE AltName: Full=Ubiquitin-like activation protein 1;
GN Name=ULA1; Synonyms=ENR2; OrderedLocusNames=YPL003W; ORFNames=LPA14W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 200912 / DF5;
RX PubMed=9545234; DOI=10.1093/emboj/17.8.2208;
RA Liakopoulos D., Doenges G., Matuschewski K., Jentsch S.;
RT "A novel protein modification pathway related to the ubiquitin system.";
RL EMBO J. 17:2208-2214(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION.
RX PubMed=9531531; DOI=10.1101/gad.12.7.914;
RA Lammer D., Mathias N., Laplaza J.M., Jiang W., Liu Y., Callis J., Goebl M.,
RA Estelle M.;
RT "Modification of yeast Cdc53p by the ubiquitin-related protein Rub1p
RT affects function of the SCFCdc4 complex.";
RL Genes Dev. 12:914-926(1998).
CC -!- FUNCTION: Regulatory subunit of the dimeric UBA3-ULA1 E1 enzyme. E1
CC activates NEDD8/RUB1 by first adenylating its C-terminal glycine
CC residue with ATP, thereafter linking this residue to the side chain of
CC the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP.
CC E1 finally transfers NEDD8 to the catalytic cysteine of UBC12.
CC {ECO:0000269|PubMed:9531531, ECO:0000269|PubMed:9545234}.
CC -!- PATHWAY: Protein modification; protein neddylation.
CC -!- SUBUNIT: Heterodimer of UBA3 and ULA1. The complex binds NEDD8 and
CC UBC12 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q12059; Q99344: UBA3; NbExp=4; IntAct=EBI-32882, EBI-37997;
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. ULA1
CC subfamily. {ECO:0000305}.
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DR EMBL; Y16889; CAA76515.1; -; Genomic_DNA.
DR EMBL; Z71255; CAA95038.1; -; Genomic_DNA.
DR EMBL; Z48483; CAA88383.1; -; Genomic_DNA.
DR EMBL; U33335; AAB68102.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11425.1; -; Genomic_DNA.
DR PIR; S52528; S52528.
DR RefSeq; NP_015322.1; NM_001183817.1.
DR AlphaFoldDB; Q12059; -.
DR SMR; Q12059; -.
DR BioGRID; 36174; 117.
DR ComplexPortal; CPX-1414; UBA3-ULA1 E1 enzyme.
DR DIP; DIP-1718N; -.
DR IntAct; Q12059; 5.
DR MINT; Q12059; -.
DR STRING; 4932.YPL003W; -.
DR MaxQB; Q12059; -.
DR PaxDb; Q12059; -.
DR PRIDE; Q12059; -.
DR TopDownProteomics; Q12059; -.
DR EnsemblFungi; YPL003W_mRNA; YPL003W; YPL003W.
DR GeneID; 856104; -.
DR KEGG; sce:YPL003W; -.
DR SGD; S000005924; ULA1.
DR VEuPathDB; FungiDB:YPL003W; -.
DR eggNOG; KOG2016; Eukaryota.
DR HOGENOM; CLU_019618_2_0_1; -.
DR InParanoid; Q12059; -.
DR OMA; NENGMPE; -.
DR BioCyc; YEAST:G3O-33922-MON; -.
DR Reactome; R-SCE-8951664; Neddylation.
DR UniPathway; UPA00885; -.
DR PRO; PR:Q12059; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12059; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0120123; C:ubiquitin activating enzyme complex; IPI:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019781; F:NEDD8 activating enzyme activity; IDA:SGD.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR GO; GO:0045116; P:protein neddylation; IDA:SGD.
DR InterPro; IPR030667; APP-BP1.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953; PTHR10953; 1.
DR PIRSF; PIRSF039099; APP-BP1; 1.
DR SUPFAM; SSF69572; SSF69572; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Nucleotide-binding; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..462
FT /note="NEDD8-activating enzyme E1 regulatory subunit"
FT /id="PRO_0000194962"
SQ SEQUENCE 462 AA; 52853 MW; BCAB8F0962245001 CRC64;
MERYDRQLRL WGALGQDSLN RSRVCVVGPA TPLLQEVFKN LVLAGISSLT WLKVECAVQS
GSLFLAELKK DLEPLASKQL EYEENDLRKT LQQPQYDWTR FSVVILTCIG EQTAMLDLNE
IRRQRGTKFP PVLNTFVSGF YGYIYLVLSE THFVLQAHPD SKKYDLRLQN PWPELINYVD
TFDLSKMDTA TFSGIPYTVL LMKCIAKLER DGNNGRITID QMKKVLDQIC LPLGNDVIYE
PNYVEAKRYA YLACSQNDCC KELEDLLRNL EISDYGNDWH DTYNYEILTL LLTLKNIAKE
NGELSFQPLT GTLPDMESTT ENYIRLKKLY EVKAKLDKSR VEESLARSKK IVSQDVLETF
CSHYGEVRKI LPPKSDLLGI FSTSNALLDA LVMVQFWEQP AVTAEDKDEF IGLRVDDNYS
VMAFFGGAVV QEAIKLITHH YVPIDNLFLY NGINNSSATY KI
