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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

Pathwayi: 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)DescriptionActionsGraphical viewLength
Binding sitei52ATPBy similarity1
Binding sitei76ATPBy similarity1
Metal bindingi162ZincBy similarity1
Metal bindingi165ZincBy similarity1
Active sitei177Glycyl thioester intermediatePROSITE-ProRule annotation1
Metal bindingi435ZincBy similarity1
Metal bindingi438ZincBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi28 – 33ATPBy similarity6
Nucleotide bindingi60 – 63ATPBy similarity4
Nucleotide bindingi121 – 126ATPBy similarity6

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.
ReactomeiR-SCE-3065676. SUMO is conjugated to E1 (UBA2:SAE1).
R-SCE-3065678. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
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
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR390C.
SGDiS000002798. UBA2.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi177C → A or S: Loss of function. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001949791 – 636Ubiquitin-activating enzyme E1-likeAdd BLAST636

Post-translational modificationi

Multiubiquitinated in vivo.

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiP52488.
PRIDEiP52488.
TopDownProteomicsiP52488.

PTM databases

iPTMnetiP52488.

Interactioni

Subunit structurei

Heterodimer of UBA2 and AOS1. The complex binds SMT3.

Protein-protein interaction databases

BioGridi32451. 27 interactors.
DIPiDIP-2296N.
IntActiP52488. 9 interactors.
MINTiMINT-657883.

Structurei

Secondary structure

1636
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi442 – 448Combined sources7
Helixi450 – 455Combined sources6
Helixi458 – 469Combined sources12
Beta strandi473 – 479Combined sources7
Turni480 – 483Combined sources4
Beta strandi484 – 488Combined sources5
Turni493 – 496Combined sources4
Turni499 – 503Combined sources5
Beta strandi509 – 515Combined sources7
Beta strandi518 – 522Combined sources5
Beta strandi525 – 531Combined sources7
Beta strandi535 – 538Combined sources4
Beta strandi549 – 551Combined sources3

3D structure databases

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

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi619 – 622Nuclear localization signalSequence analysis4

Sequence similaritiesi

Belongs to the ubiquitin-activating E1 family.Curated

Phylogenomic databases

GeneTreeiENSGT00550000074924.
HOGENOMiHOG000216514.
InParanoidiP52488.
KOiK10685.
OMAiHHGNIMD.
OrthoDBiEOG092C3FGE.

Family and domain databases

Gene3Di1.10.3240.10. 1 hit.
3.40.50.720. 2 hits.
InterProiIPR016040. NAD(P)-bd_dom.
IPR030661. SAE2/Uba2.
IPR000594. ThiF_NAD_FAD-bd.
IPR019572. UBA_E1_Cys.
IPR033127. UBQ-activ_enz_E1_Cys_AS.
[Graphical view]
PfamiPF00899. ThiF. 1 hit.
PF10585. UBA_e1_thiolCys. 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 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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ONGX-ray2.30A/C439-563[»]
3ONHX-ray1.60A439-563[»]
ProteinModelPortaliP52488.
SMRiP52488.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32451. 27 interactors.
DIPiDIP-2296N.
IntActiP52488. 9 interactors.
MINTiMINT-657883.

PTM databases

iPTMnetiP52488.

Proteomic databases

MaxQBiP52488.
PRIDEiP52488.
TopDownProteomicsiP52488.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YDR390C.
SGDiS000002798. UBA2.

Phylogenomic databases

GeneTreeiENSGT00550000074924.
HOGENOMiHOG000216514.
InParanoidiP52488.
KOiK10685.
OMAiHHGNIMD.
OrthoDBiEOG092C3FGE.

Enzyme and pathway databases

UniPathwayiUPA00886.
BioCyciYEAST:G3O-29938-MONOMER.
BRENDAi6.2.1.B9. 984.
ReactomeiR-SCE-3065676. SUMO is conjugated to E1 (UBA2:SAE1).
R-SCE-3065678. SUMO is transferred from E1 to E2 (UBE2I, UBC9).

Miscellaneous databases

PROiP52488.

Family and domain databases

Gene3Di1.10.3240.10. 1 hit.
3.40.50.720. 2 hits.
InterProiIPR016040. NAD(P)-bd_dom.
IPR030661. SAE2/Uba2.
IPR000594. ThiF_NAD_FAD-bd.
IPR019572. UBA_E1_Cys.
IPR033127. UBQ-activ_enz_E1_Cys_AS.
[Graphical view]
PfamiPF00899. ThiF. 1 hit.
PF10585. UBA_e1_thiolCys. 1 hit.
[Graphical view]
PIRSFiPIRSF039133. SUMO_E1B. 1 hit.
SUPFAMiSSF69572. SSF69572. 2 hits.
PROSITEiPS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 162 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

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 one 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.