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Protein

Ubiquitin-activating enzyme E1 1

Gene

UBA1

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

Catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation through the ubiquitin-proteasome system. Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP.3 Publications

Catalytic activityi

ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine.2 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.2 Publications
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei444 – 4441ATP; via amide nitrogen1 Publication
Binding sitei470 – 4701ATP1 Publication
Binding sitei481 – 4811ATP1 Publication
Binding sitei494 – 4941ATP1 Publication
Active sitei600 – 6001Glycyl thioester intermediatePROSITE-ProRule annotation1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi544 – 5452ATP1 Publication

GO - Molecular functioni

GO - Biological processi

  • modification-dependent protein catabolic process Source: GO_Central
  • protein ubiquitination Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31969-MONOMER.
ReactomeiR-SCE-1169408. ISG15 antiviral mechanism.
R-SCE-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-activating enzyme E1 1 (EC:6.2.1.452 Publications)
Gene namesi
Name:UBA1
Ordered Locus Names:YKL210W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XI

Organism-specific databases

EuPathDBiFungiDB:YKL210W.
SGDiS000001693. UBA1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • cytosol Source: GO_Central
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi912 – 9121I → P: Strongly reduces formation of the thioester intermediate with ubiquitin; when associated with P-914. 1 Publication
Mutagenesisi914 – 9141S → P: Strongly reduces formation of the thioester intermediate with ubiquitin; when associated with P-912. 1 Publication
Mutagenesisi1004 – 10041E → K: Strongly reduces formation of the thioester intermediate with ubiquitin. 1 Publication
Mutagenesisi1014 – 10141D → K: Strongly reduces formation of the thioester intermediate with ubiquitin; when associated with K-1016. 1 Publication
Mutagenesisi1016 – 10161E → K: Strongly reduces formation of the thioester intermediate with ubiquitin; when associated with K-1014. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 10241023Ubiquitin-activating enzyme E1 1PRO_0000194977Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei265 – 2651PhosphoserineCombined sources
Cross-linki595 – 595Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki608 – 608Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei914 – 9141PhosphoserineCombined sources

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP22515.
PRIDEiP22515.

PTM databases

iPTMnetiP22515.

Interactioni

Subunit structurei

Monomer. Binds simultaneously two ubiquitin chains.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
UBI4P618642EBI-19703,EBI-19797From a different organism.

Protein-protein interaction databases

BioGridi33955. 61 interactions.
DIPiDIP-4853N.
IntActiP22515. 16 interactions.
MINTiMINT-489454.

Structurei

Secondary structure

1
1024
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi16 – 2611Combined sources
Helixi28 – 347Combined sources
Beta strandi38 – 425Combined sources
Helixi46 – 5813Combined sources
Beta strandi61 – 666Combined sources
Helixi73 – 775Combined sources
Helixi84 – 863Combined sources
Helixi91 – 10010Combined sources
Beta strandi108 – 1103Combined sources
Helixi117 – 1226Combined sources
Beta strandi124 – 1285Combined sources
Helixi134 – 14714Combined sources
Beta strandi150 – 1578Combined sources
Beta strandi160 – 1667Combined sources
Beta strandi171 – 1777Combined sources
Beta strandi183 – 1897Combined sources
Beta strandi194 – 1985Combined sources
Beta strandi210 – 2156Combined sources
Helixi220 – 2234Combined sources
Beta strandi231 – 2344Combined sources
Beta strandi237 – 2393Combined sources
Helixi244 – 2463Combined sources
Beta strandi254 – 2585Combined sources
Beta strandi262 – 2643Combined sources
Helixi269 – 2746Combined sources
Helixi283 – 2875Combined sources
Helixi288 – 30518Combined sources
Turni306 – 3083Combined sources
Helixi316 – 33217Combined sources
Turni334 – 3374Combined sources
Helixi345 – 3539Combined sources
Turni354 – 3563Combined sources
Helixi360 – 37920Combined sources
Beta strandi387 – 3926Combined sources
Helixi394 – 3963Combined sources
Turni400 – 4023Combined sources
Turni407 – 4104Combined sources
Helixi418 – 4247Combined sources
Helixi426 – 4338Combined sources
Beta strandi436 – 4405Combined sources
Helixi444 – 45613Combined sources
Turni457 – 4593Combined sources
Beta strandi465 – 4695Combined sources
Helixi476 – 4805Combined sources
Helixi487 – 4893Combined sources
Helixi494 – 50512Combined sources
Helixi507 – 5093Combined sources
Turni510 – 5123Combined sources
Beta strandi513 – 5164Combined sources
Helixi522 – 5243Combined sources
Turni525 – 5273Combined sources
Helixi530 – 5345Combined sources
Beta strandi537 – 5415Combined sources
Helixi546 – 55914Combined sources
Beta strandi563 – 5697Combined sources
Beta strandi572 – 5787Combined sources
Turni580 – 5823Combined sources
Helixi586 – 5883Combined sources
Helixi599 – 6035Combined sources
Helixi609 – 62416Combined sources
Helixi626 – 63611Combined sources
Helixi640 – 6478Combined sources
Helixi651 – 66313Combined sources
Helixi669 – 68416Combined sources
Helixi686 – 6949Combined sources
Beta strandi704 – 7085Combined sources
Helixi725 – 74218Combined sources
Helixi755 – 7639Combined sources
Helixi797 – 8026Combined sources
Helixi808 – 8114Combined sources
Helixi830 – 84415Combined sources
Helixi852 – 8598Combined sources
Helixi867 – 88519Combined sources
Helixi891 – 8933Combined sources
Beta strandi896 – 9005Combined sources
Turni901 – 9044Combined sources
Beta strandi905 – 9095Combined sources
Beta strandi916 – 9194Combined sources
Beta strandi922 – 9254Combined sources
Turni926 – 9283Combined sources
Beta strandi930 – 9367Combined sources
Helixi939 – 95012Combined sources
Beta strandi953 – 9597Combined sources
Beta strandi962 – 9665Combined sources
Helixi971 – 9777Combined sources
Helixi982 – 9909Combined sources
Beta strandi1000 – 10089Combined sources
Beta strandi1019 – 10235Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CMMX-ray2.70A/C10-1024[»]
4NNJX-ray2.40A/C9-1024[»]
ProteinModelPortaliP22515.
SMRiP22515. Positions 11-1024.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22515.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati27 – 1641381-1Add
BLAST
Repeati425 – 5791551-2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni27 – 5795532 approximate repeatsAdd
BLAST

Sequence similaritiesi

Belongs to the ubiquitin-activating E1 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00390000016689.
HOGENOMiHOG000167329.
InParanoidiP22515.
KOiK03178.
OMAiQNGVHFI.
OrthoDBiEOG092C3FGE.

Family and domain databases

Gene3Di1.10.3240.10. 2 hits.
3.40.50.720. 4 hits.
InterProiIPR032420. E1_4HB.
IPR032418. E1_FCCH.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR018965. Ub-activating_enz_E1_C.
IPR019572. UBA_E1_Cys.
IPR018075. UBQ-activ_enz_E1.
IPR018074. UBQ-activ_enz_E1_CS.
IPR033127. UBQ-activ_enz_E1_Cys_AS.
IPR000011. UBQ/SUMO-activ_enz_E1-like.
[Graphical view]
PfamiPF16191. E1_4HB. 1 hit.
PF16190. E1_FCCH. 1 hit.
PF09358. E1_UFD. 1 hit.
PF00899. ThiF. 2 hits.
PF10585. UBA_e1_thiolCys. 1 hit.
[Graphical view]
PRINTSiPR01849. UBIQUITINACT.
SMARTiSM00985. UBA_e1_C. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 2 hits.
TIGRFAMsiTIGR01408. Ube1. 1 hit.
PROSITEiPS00536. UBIQUITIN_ACTIVAT_1. 1 hit.
PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P22515-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSNNSGLSA AGEIDESLYS RQLYVLGKEA MLKMQTSNVL ILGLKGLGVE
60 70 80 90 100
IAKNVVLAGV KSMTVFDPEP VQLADLSTQF FLTEKDIGQK RGDVTRAKLA
110 120 130 140 150
ELNAYVPVNV LDSLDDVTQL SQFQVVVATD TVSLEDKVKI NEFCHSSGIR
160 170 180 190 200
FISSETRGLF GNTFVDLGDE FTVLDPTGEE PRTGMVSDIE PDGTVTMLDD
210 220 230 240 250
NRHGLEDGNF VRFSEVEGLD KLNDGTLFKV EVLGPFAFRI GSVKEYGEYK
260 270 280 290 300
KGGIFTEVKV PRKISFKSLK QQLSNPEFVF SDFAKFDRAA QLHLGFQALH
310 320 330 340 350
QFAVRHNGEL PRTMNDEDAN ELIKLVTDLS VQQPEVLGEG VDVNEDLIKE
360 370 380 390 400
LSYQARGDIP GVVAFFGGLV AQEVLKACSG KFTPLKQFMY FDSLESLPDP
410 420 430 440 450
KNFPRNEKTT QPVNSRYDNQ IAVFGLDFQK KIANSKVFLV GSGAIGCEML
460 470 480 490 500
KNWALLGLGS GSDGYIVVTD NDSIEKSNLN RQFLFRPKDV GKNKSEVAAE
510 520 530 540 550
AVCAMNPDLK GKINAKIDKV GPETEEIFND SFWESLDFVT NALDNVDART
560 570 580 590 600
YVDRRCVFYR KPLLESGTLG TKGNTQVIIP RLTESYSSSR DPPEKSIPLC
610 620 630 640 650
TLRSFPNKID HTIAWAKSLF QGYFTDSAEN VNMYLTQPNF VEQTLKQSGD
660 670 680 690 700
VKGVLESISD SLSSKPHNFE DCIKWARLEF EKKFNHDIKQ LLFNFPKDAK
710 720 730 740 750
TSNGEPFWSG AKRAPTPLEF DIYNNDHFHF VVAGASLRAY NYGIKSDDSN
760 770 780 790 800
SKPNVDEYKS VIDHMIIPEF TPNANLKIQV NDDDPDPNAN AANGSDEIDQ
810 820 830 840 850
LVSSLPDPST LAGFKLEPVD FEKDDDTNHH IEFITACSNC RAQNYFIETA
860 870 880 890 900
DRQKTKFIAG RIIPAIATTT SLVTGLVNLE LYKLIDNKTD IEQYKNGFVN
910 920 930 940 950
LALPFFGFSE PIASPKGEYN NKKYDKIWDR FDIKGDIKLS DLIEHFEKDE
960 970 980 990 1000
GLEITMLSYG VSLLYASFFP PKKLKERLNL PITQLVKLVT KKDIPAHVST
1010 1020
MILEICADDK EGEDVEVPFI TIHL
Length:1,024
Mass (Da):114,266
Last modified:June 1, 1994 - v2
Checksum:i8910804DF9156661
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti526 – 5261E → K in CAA39056 (PubMed:1989885).Curated
Sequence conflicti736 – 7361S → N in CAA39056 (PubMed:1989885).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55386 Genomic DNA. Translation: CAA39056.1.
Z28210 Genomic DNA. Translation: CAA82055.1.
X15428 Genomic DNA. Translation: CAA33468.1.
BK006944 Genomic DNA. Translation: DAA08959.1.
PIRiS38048.
RefSeqiNP_012712.1. NM_001179775.1.

Genome annotation databases

EnsemblFungiiYKL210W; YKL210W; YKL210W.
GeneIDi853670.
KEGGisce:YKL210W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55386 Genomic DNA. Translation: CAA39056.1.
Z28210 Genomic DNA. Translation: CAA82055.1.
X15428 Genomic DNA. Translation: CAA33468.1.
BK006944 Genomic DNA. Translation: DAA08959.1.
PIRiS38048.
RefSeqiNP_012712.1. NM_001179775.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CMMX-ray2.70A/C10-1024[»]
4NNJX-ray2.40A/C9-1024[»]
ProteinModelPortaliP22515.
SMRiP22515. Positions 11-1024.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33955. 61 interactions.
DIPiDIP-4853N.
IntActiP22515. 16 interactions.
MINTiMINT-489454.

PTM databases

iPTMnetiP22515.

Proteomic databases

MaxQBiP22515.
PRIDEiP22515.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKL210W; YKL210W; YKL210W.
GeneIDi853670.
KEGGisce:YKL210W.

Organism-specific databases

EuPathDBiFungiDB:YKL210W.
SGDiS000001693. UBA1.

Phylogenomic databases

GeneTreeiENSGT00390000016689.
HOGENOMiHOG000167329.
InParanoidiP22515.
KOiK03178.
OMAiQNGVHFI.
OrthoDBiEOG092C3FGE.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciYEAST:G3O-31969-MONOMER.
ReactomeiR-SCE-1169408. ISG15 antiviral mechanism.
R-SCE-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

EvolutionaryTraceiP22515.
PROiP22515.

Family and domain databases

Gene3Di1.10.3240.10. 2 hits.
3.40.50.720. 4 hits.
InterProiIPR032420. E1_4HB.
IPR032418. E1_FCCH.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR018965. Ub-activating_enz_E1_C.
IPR019572. UBA_E1_Cys.
IPR018075. UBQ-activ_enz_E1.
IPR018074. UBQ-activ_enz_E1_CS.
IPR033127. UBQ-activ_enz_E1_Cys_AS.
IPR000011. UBQ/SUMO-activ_enz_E1-like.
[Graphical view]
PfamiPF16191. E1_4HB. 1 hit.
PF16190. E1_FCCH. 1 hit.
PF09358. E1_UFD. 1 hit.
PF00899. ThiF. 2 hits.
PF10585. UBA_e1_thiolCys. 1 hit.
[Graphical view]
PRINTSiPR01849. UBIQUITINACT.
SMARTiSM00985. UBA_e1_C. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 2 hits.
TIGRFAMsiTIGR01408. Ube1. 1 hit.
PROSITEiPS00536. UBIQUITIN_ACTIVAT_1. 1 hit.
PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiUBA1_YEAST
AccessioniPrimary (citable) accession number: P22515
Secondary accession number(s): D6VWZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: June 1, 1994
Last modified: September 7, 2016
This is version 173 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

There are two active sites within the E1 molecule, allowing it to accommodate two ubiquitin moieties at a time, with a new ubiquitin forming an adenylate intermediate as the previous one is transferred to the thiol site.1 Publication
Present with 17700 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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 XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: 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.