UBA2_YEAST
ID UBA2_YEAST Reviewed; 636 AA.
AC P52488; D6VT24;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Ubiquitin-activating enzyme E1-like;
DE AltName: Full=Polymerase-interacting protein 2;
DE AltName: Full=SMT3-activating enzyme subunit 2;
GN Name=UBA2; Synonyms=PIP2, UAL1; OrderedLocusNames=YDR390C;
GN ORFNames=D9509.10;
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].
RX PubMed=7629121; DOI=10.1074/jbc.270.30.18099;
RA Dohmen R.J., Stappen R., McGrath J.P., Forrova H., Kolarov J., Goffeau A.,
RA Varshavsky A.;
RT "An essential yeast gene encoding a homolog of ubiquitin-activating
RT enzyme.";
RL J. Biol. Chem. 270:18099-18109(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kolarov J.;
RL Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 200060 / W303;
RA del Olmo M., Gross S., Moore C.L.;
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [5]
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 [6]
RP FUNCTION.
RX PubMed=9312010; DOI=10.1093/emboj/16.18.5509;
RA Johnson E.S., Schwienhorst I., Dohmen R.J., Blobel G.;
RT "The ubiquitin-like protein Smt3p is activated for conjugation to other
RT proteins by an Aos1p/Uba2p heterodimer.";
RL EMBO J. 16:5509-5519(1997).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: The dimeric enzyme acts as a SMT3 E1 ligase. It mediates ATP-
CC dependent activation of SMT3 and formation of a thioester with a
CC conserved cysteine residue on AOS1. {ECO:0000269|PubMed:9312010}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Heterodimer of UBA2 and AOS1. The complex binds SMT3.
CC -!- INTERACTION:
CC P52488; Q06624: AOS1; NbExp=3; IntAct=EBI-19710, EBI-15107;
CC P52488; Q12306: SMT3; NbExp=2; IntAct=EBI-19710, EBI-17490;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Multiubiquitinated in vivo.
CC -!- MISCELLANEOUS: Present with 18800 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA82980.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z48725; CAA88617.1; -; Genomic_DNA.
DR EMBL; Z30326; CAA82980.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U17263; AAB46626.1; -; Genomic_DNA.
DR EMBL; U32274; AAB64832.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12234.1; -; Genomic_DNA.
DR PIR; A57178; A57178.
DR RefSeq; NP_010678.3; NM_001180698.3.
DR PDB; 3ONG; X-ray; 2.30 A; A/C=439-563.
DR PDB; 3ONH; X-ray; 1.60 A; A=439-563.
DR PDBsum; 3ONG; -.
DR PDBsum; 3ONH; -.
DR AlphaFoldDB; P52488; -.
DR SMR; P52488; -.
DR BioGRID; 32451; 33.
DR ComplexPortal; CPX-3238; SUMO activating enzyme complex.
DR DIP; DIP-2296N; -.
DR IntAct; P52488; 10.
DR MINT; P52488; -.
DR STRING; 4932.YDR390C; -.
DR iPTMnet; P52488; -.
DR MaxQB; P52488; -.
DR PaxDb; P52488; -.
DR PRIDE; P52488; -.
DR TopDownProteomics; P52488; -.
DR EnsemblFungi; YDR390C_mRNA; YDR390C; YDR390C.
DR GeneID; 851998; -.
DR KEGG; sce:YDR390C; -.
DR SGD; S000002798; UBA2.
DR VEuPathDB; FungiDB:YDR390C; -.
DR eggNOG; KOG2013; Eukaryota.
DR GeneTree; ENSGT00550000074924; -.
DR HOGENOM; CLU_013325_7_3_1; -.
DR InParanoid; P52488; -.
DR OMA; PGKTECF; -.
DR BioCyc; YEAST:G3O-29938-MON; -.
DR BRENDA; 6.2.1.45; 984.
DR Reactome; R-SCE-3065676; SUMO is conjugated to E1 (UBA2:SAE1).
DR Reactome; R-SCE-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
DR UniPathway; UPA00886; -.
DR PRO; PR:P52488; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P52488; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0031510; C:SUMO activating enzyme complex; IPI:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019948; F:SUMO activating enzyme activity; IEA:InterPro.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR GO; GO:0016925; P:protein sumoylation; IDA:SGD.
DR Gene3D; 1.10.10.520; -; 1.
DR Gene3D; 3.50.50.80; -; 1.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR042449; Ub-E1_IAD_1.
DR InterPro; IPR023318; Ub_act_enz_dom_a_sf.
DR InterPro; IPR030661; Uba2.
DR InterPro; IPR019572; UBA_E1_SCCH.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR PANTHER; PTHR10953; PTHR10953; 1.
DR PANTHER; PTHR10953:SF5; PTHR10953:SF5; 1.
DR Pfam; PF00899; ThiF; 1.
DR Pfam; PF10585; UBA_e1_thiolCys; 1.
DR PIRSF; PIRSF039133; SUMO_E1B; 1.
DR SUPFAM; SSF69572; SSF69572; 1.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Metal-binding; Nucleotide-binding;
KW Nucleus; Reference proteome; Ubl conjugation; Ubl conjugation pathway;
KW Zinc.
FT CHAIN 1..636
FT /note="Ubiquitin-activating enzyme E1-like"
FT /id="PRO_0000194979"
FT REGION 581..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 619..622
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 602..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 177
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10132"
FT BINDING 28..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 60..63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 121..126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 435
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 438
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MUTAGEN 177
FT /note="C->A,S: Loss of function."
FT STRAND 442..448
FT /evidence="ECO:0007829|PDB:3ONH"
FT HELIX 450..455
FT /evidence="ECO:0007829|PDB:3ONH"
FT HELIX 458..469
FT /evidence="ECO:0007829|PDB:3ONH"
FT STRAND 473..479
FT /evidence="ECO:0007829|PDB:3ONH"
FT TURN 480..483
FT /evidence="ECO:0007829|PDB:3ONH"
FT STRAND 484..488
FT /evidence="ECO:0007829|PDB:3ONH"
FT TURN 493..496
FT /evidence="ECO:0007829|PDB:3ONH"
FT TURN 499..503
FT /evidence="ECO:0007829|PDB:3ONH"
FT STRAND 509..515
FT /evidence="ECO:0007829|PDB:3ONH"
FT STRAND 518..522
FT /evidence="ECO:0007829|PDB:3ONH"
FT STRAND 525..531
FT /evidence="ECO:0007829|PDB:3ONH"
FT STRAND 535..538
FT /evidence="ECO:0007829|PDB:3ONG"
FT STRAND 549..551
FT /evidence="ECO:0007829|PDB:3ONH"
SQ SEQUENCE 636 AA; 71259 MW; DBF800E1458B3B10 CRC64;
MPRETSLVTI IGEDSYKKLR SSRCLLVGAG GIGSELLKDI ILMEFGEIHI VDLDTIDLSN
LNRQFLFRQK DIKQPKSTTA VKAVQHFNNS KLVPYQGNVM DISTFPLHWF EQFDIIFNAL
DNLAARRYVN KISQFLSLPL IESGTAGFDG YMQPIIPGKT ECFECTKKET PKTFPVCTIR
STPSQPIHCI VWAKNFLFNQ LFASETSGNE DDNNQDWGTD DAEEIKRIKQ ETNELYELQK
IIISRDASRI PEILNKLFIQ DINKLLAIEN LWKTRTKPVP LSDSQINTPT KTAQSASNSV
GTIQEQISNF INITQKLMDR YPKEQNHIEF DKDDADTLEF VATAANIRSH IFNIPMKSVF
DIKQIAGNII PAIATTNAIV AGASSLISLR VLNLLKYAPT TKYTDLNMAF TAKASNLSQN
RYLSNPKLAP PNKNCPVCSK VCRGVIKLSS DCLNKMKLSD FVVLIREKYS YPQDISLLDA
SNQRLLFDYD FEDLNDRTLS EINLGNGSII LFSDEEGDTM IRKAIELFLD VDDELPCNTC
SLPDVEVPLI KANNSPSKNE EEEKNEKGAD VVATTNSHGK DGIVILDDDE GEITIDAEPI
NGSKKRPVDT EISEAPSNKR TKLVNEPTNS DIVELD
