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UniProtKB - P22515 (UBA1_YEAST)
Protein
Ubiquitin-activating enzyme E1 1
Gene
UBA1
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
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 PublicationsMiscellaneous
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
Catalytic activityi
- ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine.2 Publications EC:6.2.1.45
: protein ubiquitination Pathwayi
This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.2 PublicationsView all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 444 | ATP; via amide nitrogen1 Publication | 1 | |
Binding sitei | 470 | ATP1 Publication | 1 | |
Binding sitei | 481 | ATP1 Publication | 1 | |
Binding sitei | 494 | ATP1 Publication | 1 | |
Active sitei | 600 | Glycyl thioester intermediatePROSITE-ProRule annotation1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 544 – 545 | ATP1 Publication | 2 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- ubiquitin activating enzyme activity Source: SGD
GO - Biological processi
- cellular response to DNA damage stimulus Source: GO_Central
- protein modification by small protein conjugation Source: GO_Central
- protein ubiquitination Source: SGD
- ubiquitin-dependent protein catabolic process Source: GO_Central
Keywordsi
Molecular function | Ligase |
Biological process | Ubl conjugation pathway |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
Reactomei | R-SCE-8866652, Synthesis of active ubiquitin: roles of E1 and E2 enzymes R-SCE-983168, Antigen processing: Ubiquitination & Proteasome degradation |
UniPathwayi | UPA00143 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:UBA1 Ordered Locus Names:YKL210W |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
SGDi | S000001693, UBA1 |
VEuPathDBi | FungiDB:YKL210W |
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 912 | I → P: Strongly reduces formation of the thioester intermediate with ubiquitin; when associated with P-914. 1 Publication | 1 | |
Mutagenesisi | 914 | S → P: Strongly reduces formation of the thioester intermediate with ubiquitin; when associated with P-912. 1 Publication | 1 | |
Mutagenesisi | 1004 | E → K: Strongly reduces formation of the thioester intermediate with ubiquitin. 1 Publication | 1 | |
Mutagenesisi | 1014 | D → K: Strongly reduces formation of the thioester intermediate with ubiquitin; when associated with K-1016. 1 Publication | 1 | |
Mutagenesisi | 1016 | E → K: Strongly reduces formation of the thioester intermediate with ubiquitin; when associated with K-1014. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedCombined sources | |||
ChainiPRO_0000194977 | 2 – 1024 | Ubiquitin-activating enzyme E1 1Add BLAST | 1023 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylserineCombined sources | 1 | |
Modified residuei | 265 | PhosphoserineCombined sources | 1 | |
Cross-linki | 595 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources | ||
Cross-linki | 608 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources | ||
Modified residuei | 914 | PhosphoserineCombined sources | 1 |
Post-translational modificationi
The N-terminus is blocked.
Keywords - PTMi
Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
MaxQBi | P22515 |
PaxDbi | P22515 |
PRIDEi | P22515 |
PTM databases
iPTMneti | P22515 |
Interactioni
Subunit structurei
Monomer. Binds simultaneously two ubiquitin chains.
1 PublicationProtein-protein interaction databases
BioGRIDi | 33955, 154 interactors |
DIPi | DIP-4853N |
IntActi | P22515, 29 interactors |
MINTi | P22515 |
STRINGi | 4932.YKL210W |
Miscellaneous databases
RNActi | P22515, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P22515 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P22515 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Repeati | 27 – 164 | 1-1Add BLAST | 138 | |
Repeati | 425 – 579 | 1-2Add BLAST | 155 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 27 – 579 | 2 approximate repeatsAdd BLAST | 553 |
Sequence similaritiesi
Belongs to the ubiquitin-activating E1 family.Curated
Keywords - Domaini
RepeatPhylogenomic databases
eggNOGi | KOG2012, Eukaryota |
GeneTreei | ENSGT00940000166138 |
HOGENOMi | CLU_002556_0_0_1 |
InParanoidi | P22515 |
OMAi | GANLHAF |
Family and domain databases
Gene3Di | 1.10.10.2660, 1 hit 2.40.30.180, 1 hit 3.10.290.60, 1 hit 3.50.50.80, 1 hit |
InterProi | View protein in InterPro IPR032420, E1_4HB IPR032418, E1_FCCH IPR042302, E1_FCCH_sf IPR045886, ThiF/MoeB/HesA IPR000594, ThiF_NAD_FAD-bd IPR018965, Ub-activating_enz_E1_C IPR042449, Ub-E1_IAD_1 IPR038252, UBA_E1_C_sf IPR019572, UBA_E1_SCCH IPR042063, Ubi_acti_E1_SCCH IPR035985, Ubiquitin-activating_enz 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 |
PANTHERi | PTHR10953, PTHR10953, 1 hit |
Pfami | View protein in Pfam PF16191, E1_4HB, 1 hit PF16190, E1_FCCH, 1 hit PF09358, E1_UFD, 1 hit PF00899, ThiF, 2 hits PF10585, UBA_e1_thiolCys, 1 hit |
PRINTSi | PR01849, UBIQUITINACT |
SMARTi | View protein in SMART SM00985, UBA_e1_C, 1 hit |
SUPFAMi | SSF69572, SSF69572, 2 hits |
TIGRFAMsi | TIGR01408, Ube1, 1 hit |
PROSITEi | View protein in PROSITE PS00536, UBIQUITIN_ACTIVAT_1, 1 hit PS00865, UBIQUITIN_ACTIVAT_2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P22515-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 526 | E → K in CAA39056 (PubMed:1989885).Curated | 1 | |
Sequence conflicti | 736 | S → N in CAA39056 (PubMed:1989885).Curated | 1 |
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 |
PIRi | S38048 |
RefSeqi | NP_012712.1, NM_001179775.1 |
Genome annotation databases
EnsemblFungii | YKL210W_mRNA; YKL210W; YKL210W |
GeneIDi | 853670 |
KEGGi | sce:YKL210W |
Similar proteinsi
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 |
PIRi | S38048 |
RefSeqi | NP_012712.1, NM_001179775.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3CMM | X-ray | 2.70 | A/C | 10-1024 | [»] | |
4NNJ | X-ray | 2.40 | A/C | 9-1024 | [»] | |
5L6H | X-ray | 2.30 | A/C | 1-1024 | [»] | |
5L6I | X-ray | 2.76 | A/C | 1-1024 | [»] | |
5L6J | X-ray | 2.68 | A/C | 1-1024 | [»] | |
5TR4 | X-ray | 2.20 | A/C | 9-1024 | [»] | |
6NYA | X-ray | 2.06 | A/D | 11-1024 | [»] | |
6ZQH | X-ray | 2.03 | A/C | 1-1024 | [»] | |
7K5J | X-ray | 3.42 | A/C/D/G/I/K/S/U | 11-1024 | [»] | |
SMRi | P22515 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 33955, 154 interactors |
DIPi | DIP-4853N |
IntActi | P22515, 29 interactors |
MINTi | P22515 |
STRINGi | 4932.YKL210W |
PTM databases
iPTMneti | P22515 |
Proteomic databases
MaxQBi | P22515 |
PaxDbi | P22515 |
PRIDEi | P22515 |
Genome annotation databases
EnsemblFungii | YKL210W_mRNA; YKL210W; YKL210W |
GeneIDi | 853670 |
KEGGi | sce:YKL210W |
Organism-specific databases
SGDi | S000001693, UBA1 |
VEuPathDBi | FungiDB:YKL210W |
Phylogenomic databases
eggNOGi | KOG2012, Eukaryota |
GeneTreei | ENSGT00940000166138 |
HOGENOMi | CLU_002556_0_0_1 |
InParanoidi | P22515 |
OMAi | GANLHAF |
Enzyme and pathway databases
UniPathwayi | UPA00143 |
Reactomei | R-SCE-8866652, Synthesis of active ubiquitin: roles of E1 and E2 enzymes R-SCE-983168, Antigen processing: Ubiquitination & Proteasome degradation |
Miscellaneous databases
EvolutionaryTracei | P22515 |
PROi | PR:P22515 |
RNActi | P22515, protein |
Family and domain databases
Gene3Di | 1.10.10.2660, 1 hit 2.40.30.180, 1 hit 3.10.290.60, 1 hit 3.50.50.80, 1 hit |
InterProi | View protein in InterPro IPR032420, E1_4HB IPR032418, E1_FCCH IPR042302, E1_FCCH_sf IPR045886, ThiF/MoeB/HesA IPR000594, ThiF_NAD_FAD-bd IPR018965, Ub-activating_enz_E1_C IPR042449, Ub-E1_IAD_1 IPR038252, UBA_E1_C_sf IPR019572, UBA_E1_SCCH IPR042063, Ubi_acti_E1_SCCH IPR035985, Ubiquitin-activating_enz 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 |
PANTHERi | PTHR10953, PTHR10953, 1 hit |
Pfami | View protein in Pfam PF16191, E1_4HB, 1 hit PF16190, E1_FCCH, 1 hit PF09358, E1_UFD, 1 hit PF00899, ThiF, 2 hits PF10585, UBA_e1_thiolCys, 1 hit |
PRINTSi | PR01849, UBIQUITINACT |
SMARTi | View protein in SMART SM00985, UBA_e1_C, 1 hit |
SUPFAMi | SSF69572, SSF69572, 2 hits |
TIGRFAMsi | TIGR01408, Ube1, 1 hit |
PROSITEi | View protein in PROSITE PS00536, UBIQUITIN_ACTIVAT_1, 1 hit PS00865, UBIQUITIN_ACTIVAT_2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | UBA1_YEAST | |
Accessioni | P22515Primary (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: | February 23, 2022 | |
This is version 215 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD - Yeast chromosome XI
Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families