Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ubiquitin-activating enzyme E1-like

Gene

UBA2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The dimeric enzyme acts as a SMT3 E1 ligase. It mediates ATP-dependent activation of SMT3 and formation of a thioester with a conserved cysteine residue on AOS1.1 Publication

Pathway: protein sumoylation

This protein is involved in the pathway protein sumoylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein sumoylation and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei52 – 521ATPBy similarity
Binding sitei76 – 761ATPBy similarity
Metal bindingi162 – 1621ZincBy similarity
Metal bindingi165 – 1651ZincBy similarity
Active sitei177 – 1771Glycyl thioester intermediatePROSITE-ProRule annotation
Metal bindingi435 – 4351ZincBy similarity
Metal bindingi438 – 4381ZincBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi28 – 336ATPBy similarity
Nucleotide bindingi60 – 634ATPBy similarity
Nucleotide bindingi121 – 1266ATPBy similarity

GO - Molecular functioni

GO - Biological processi

  • protein sumoylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-29938-MONOMER.
BRENDAi6.2.1.B9. 984.
ReactomeiREACT_326849. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
REACT_338960. SUMO is conjugated to E1 (UBA2:SAE1).
UniPathwayiUPA00886.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-activating enzyme E1-like
Alternative name(s):
Polymerase-interacting protein 2
SMT3-activating enzyme subunit 2
Gene namesi
Name:UBA2
Synonyms:PIP2, UAL1
Ordered Locus Names:YDR390C
ORF Names:D9509.10
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome IV

Organism-specific databases

CYGDiYDR390c.
EuPathDBiFungiDB:YDR390C.
SGDiS000002798. UBA2.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: SGD
  • SUMO activating enzyme complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi177 – 1771C → A or S: Loss of function.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 636636Ubiquitin-activating enzyme E1-likePRO_0000194979Add
BLAST

Post-translational modificationi

Multiubiquitinated in vivo.

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiP52488.
PaxDbiP52488.
PeptideAtlasiP52488.

Interactioni

Subunit structurei

Heterodimer of UBA2 and AOS1. The complex binds SMT3.

Protein-protein interaction databases

BioGridi32451. 27 interactions.
DIPiDIP-2296N.
IntActiP52488. 9 interactions.
MINTiMINT-657883.
STRINGi4932.YDR390C.

Structurei

Secondary structure

1
636
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi442 – 4487Combined sources
Helixi450 – 4556Combined sources
Helixi458 – 46912Combined sources
Beta strandi473 – 4797Combined sources
Turni480 – 4834Combined sources
Beta strandi484 – 4885Combined sources
Turni493 – 4964Combined sources
Turni499 – 5035Combined sources
Beta strandi509 – 5157Combined sources
Beta strandi518 – 5225Combined sources
Beta strandi525 – 5317Combined sources
Beta strandi535 – 5384Combined sources
Beta strandi549 – 5513Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ONGX-ray2.30A/C439-563[»]
3ONHX-ray1.60A439-563[»]
ProteinModelPortaliP52488.
SMRiP52488. Positions 19-552.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi619 – 6224Nuclear localization signalSequence Analysis

Sequence similaritiesi

Belongs to the ubiquitin-activating E1 family.Curated

Phylogenomic databases

eggNOGiCOG0476.
GeneTreeiENSGT00550000074924.
HOGENOMiHOG000216514.
InParanoidiP52488.
KOiK10685.
OMAiRRYVNKM.
OrthoDBiEOG7FZ07P.

Family and domain databases

Gene3Di1.10.3240.10. 1 hit.
3.40.50.720. 2 hits.
InterProiIPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR030661. SAE2/Uba2.
IPR000594. ThiF_NAD_FAD-bd.
IPR023280. Ub-like_act_enz_cat_cys_dom.
IPR000127. UBact_repeat.
IPR019572. Ubiquitin-activating_enzyme.
IPR018074. UBQ-activ_enz_E1_AS.
[Graphical view]
PfamiPF00899. ThiF. 1 hit.
PF10585. UBA_e1_thiolCys. 1 hit.
PF02134. UBACT. 1 hit.
[Graphical view]
PIRSFiPIRSF039133. SUMO_E1B. 1 hit.
SUPFAMiSSF69572. SSF69572. 2 hits.
PROSITEiPS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P52488-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRETSLVTI IGEDSYKKLR SSRCLLVGAG GIGSELLKDI ILMEFGEIHI
60 70 80 90 100
VDLDTIDLSN LNRQFLFRQK DIKQPKSTTA VKAVQHFNNS KLVPYQGNVM
110 120 130 140 150
DISTFPLHWF EQFDIIFNAL DNLAARRYVN KISQFLSLPL IESGTAGFDG
160 170 180 190 200
YMQPIIPGKT ECFECTKKET PKTFPVCTIR STPSQPIHCI VWAKNFLFNQ
210 220 230 240 250
LFASETSGNE DDNNQDWGTD DAEEIKRIKQ ETNELYELQK IIISRDASRI
260 270 280 290 300
PEILNKLFIQ DINKLLAIEN LWKTRTKPVP LSDSQINTPT KTAQSASNSV
310 320 330 340 350
GTIQEQISNF INITQKLMDR YPKEQNHIEF DKDDADTLEF VATAANIRSH
360 370 380 390 400
IFNIPMKSVF DIKQIAGNII PAIATTNAIV AGASSLISLR VLNLLKYAPT
410 420 430 440 450
TKYTDLNMAF TAKASNLSQN RYLSNPKLAP PNKNCPVCSK VCRGVIKLSS
460 470 480 490 500
DCLNKMKLSD FVVLIREKYS YPQDISLLDA SNQRLLFDYD FEDLNDRTLS
510 520 530 540 550
EINLGNGSII LFSDEEGDTM IRKAIELFLD VDDELPCNTC SLPDVEVPLI
560 570 580 590 600
KANNSPSKNE EEEKNEKGAD VVATTNSHGK DGIVILDDDE GEITIDAEPI
610 620 630
NGSKKRPVDT EISEAPSNKR TKLVNEPTNS DIVELD
Length:636
Mass (Da):71,259
Last modified:October 1, 1996 - v1
Checksum:iDBF800E1458B3B10
GO

Sequence cautioni

The sequence CAA82980.1 differs from that shown. Reason: Frameshift at positions 180 and 268. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48725 Genomic DNA. Translation: CAA88617.1.
Z30326 Genomic DNA. Translation: CAA82980.1. Frameshift.
U17263 Genomic DNA. Translation: AAB46626.1.
U32274 Genomic DNA. Translation: AAB64832.1.
BK006938 Genomic DNA. Translation: DAA12234.1.
PIRiA57178.
RefSeqiNP_010678.3. NM_001180698.3.

Genome annotation databases

EnsemblFungiiYDR390C; YDR390C; YDR390C.
GeneIDi851998.
KEGGisce:YDR390C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48725 Genomic DNA. Translation: CAA88617.1.
Z30326 Genomic DNA. Translation: CAA82980.1. Frameshift.
U17263 Genomic DNA. Translation: AAB46626.1.
U32274 Genomic DNA. Translation: AAB64832.1.
BK006938 Genomic DNA. Translation: DAA12234.1.
PIRiA57178.
RefSeqiNP_010678.3. NM_001180698.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ONGX-ray2.30A/C439-563[»]
3ONHX-ray1.60A439-563[»]
ProteinModelPortaliP52488.
SMRiP52488. Positions 19-552.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32451. 27 interactions.
DIPiDIP-2296N.
IntActiP52488. 9 interactions.
MINTiMINT-657883.
STRINGi4932.YDR390C.

Proteomic databases

MaxQBiP52488.
PaxDbiP52488.
PeptideAtlasiP52488.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR390C; YDR390C; YDR390C.
GeneIDi851998.
KEGGisce:YDR390C.

Organism-specific databases

CYGDiYDR390c.
EuPathDBiFungiDB:YDR390C.
SGDiS000002798. UBA2.

Phylogenomic databases

eggNOGiCOG0476.
GeneTreeiENSGT00550000074924.
HOGENOMiHOG000216514.
InParanoidiP52488.
KOiK10685.
OMAiRRYVNKM.
OrthoDBiEOG7FZ07P.

Enzyme and pathway databases

UniPathwayiUPA00886.
BioCyciYEAST:G3O-29938-MONOMER.
BRENDAi6.2.1.B9. 984.
ReactomeiREACT_326849. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
REACT_338960. SUMO is conjugated to E1 (UBA2:SAE1).

Miscellaneous databases

NextBioi970178.
PROiP52488.

Family and domain databases

Gene3Di1.10.3240.10. 1 hit.
3.40.50.720. 2 hits.
InterProiIPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR030661. SAE2/Uba2.
IPR000594. ThiF_NAD_FAD-bd.
IPR023280. Ub-like_act_enz_cat_cys_dom.
IPR000127. UBact_repeat.
IPR019572. Ubiquitin-activating_enzyme.
IPR018074. UBQ-activ_enz_E1_AS.
[Graphical view]
PfamiPF00899. ThiF. 1 hit.
PF10585. UBA_e1_thiolCys. 1 hit.
PF02134. UBACT. 1 hit.
[Graphical view]
PIRSFiPIRSF039133. SUMO_E1B. 1 hit.
SUPFAMiSSF69572. SSF69572. 2 hits.
PROSITEiPS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "An essential yeast gene encoding a homolog of ubiquitin-activating enzyme."
    Dohmen R.J., Stappen R., McGrath J.P., Forrova H., Kolarov J., Goffeau A., Varshavsky A.
    J. Biol. Chem. 270:18099-18109(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Kolarov J.
    Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. del Olmo M., Gross S., Moore C.L.
    Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 200060 / W303.
  4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. "The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer."
    Johnson E.S., Schwienhorst I., Dohmen R.J., Blobel G.
    EMBO J. 16:5509-5519(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiUBA2_YEAST
AccessioniPrimary (citable) accession number: P52488
Secondary accession number(s): D6VT24
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 24, 2015
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 18800 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.