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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)DescriptionActionsGraphical viewLength
Binding sitei444ATP; via amide nitrogen1 Publication1
Binding sitei470ATP1 Publication1
Binding sitei481ATP1 Publication1
Binding sitei494ATP1 Publication1
Active sitei600Glycyl thioester intermediatePROSITE-ProRule annotation1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi544 – 545ATP1 Publication2

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-8866652. Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
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)DescriptionActionsGraphical viewLength
Mutagenesisi912I → P: Strongly reduces formation of the thioester intermediate with ubiquitin; when associated with P-914. 1 Publication1
Mutagenesisi914S → P: Strongly reduces formation of the thioester intermediate with ubiquitin; when associated with P-912. 1 Publication1
Mutagenesisi1004E → K: Strongly reduces formation of the thioester intermediate with ubiquitin. 1 Publication1
Mutagenesisi1014D → K: Strongly reduces formation of the thioester intermediate with ubiquitin; when associated with K-1016. 1 Publication1
Mutagenesisi1016E → K: Strongly reduces formation of the thioester intermediate with ubiquitin; when associated with K-1014. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001949772 – 1024Ubiquitin-activating enzyme E1 1Add BLAST1023

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei265PhosphoserineCombined sources1
Cross-linki595Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki608Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei914PhosphoserineCombined sources1

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 interactors.
DIPiDIP-4853N.
IntActiP22515. 16 interactors.
MINTiMINT-489454.

Structurei

Secondary structure

11024
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi16 – 26Combined sources11
Helixi28 – 34Combined sources7
Beta strandi38 – 42Combined sources5
Helixi46 – 58Combined sources13
Beta strandi61 – 66Combined sources6
Helixi73 – 77Combined sources5
Helixi84 – 86Combined sources3
Helixi91 – 100Combined sources10
Beta strandi108 – 110Combined sources3
Helixi117 – 122Combined sources6
Beta strandi124 – 128Combined sources5
Helixi134 – 147Combined sources14
Beta strandi150 – 157Combined sources8
Beta strandi160 – 166Combined sources7
Beta strandi171 – 177Combined sources7
Beta strandi183 – 189Combined sources7
Beta strandi194 – 198Combined sources5
Beta strandi210 – 215Combined sources6
Helixi220 – 223Combined sources4
Beta strandi231 – 234Combined sources4
Beta strandi237 – 239Combined sources3
Helixi244 – 246Combined sources3
Beta strandi254 – 258Combined sources5
Beta strandi262 – 264Combined sources3
Helixi269 – 274Combined sources6
Helixi283 – 287Combined sources5
Helixi288 – 305Combined sources18
Turni306 – 308Combined sources3
Helixi316 – 332Combined sources17
Turni334 – 337Combined sources4
Helixi345 – 353Combined sources9
Turni354 – 356Combined sources3
Helixi360 – 379Combined sources20
Beta strandi387 – 392Combined sources6
Helixi394 – 396Combined sources3
Turni400 – 402Combined sources3
Turni407 – 410Combined sources4
Helixi418 – 424Combined sources7
Helixi426 – 433Combined sources8
Beta strandi436 – 440Combined sources5
Helixi444 – 456Combined sources13
Turni457 – 459Combined sources3
Beta strandi465 – 469Combined sources5
Helixi476 – 480Combined sources5
Helixi487 – 489Combined sources3
Helixi494 – 505Combined sources12
Helixi507 – 509Combined sources3
Turni510 – 512Combined sources3
Beta strandi513 – 516Combined sources4
Helixi522 – 524Combined sources3
Turni525 – 527Combined sources3
Helixi530 – 534Combined sources5
Beta strandi537 – 541Combined sources5
Helixi546 – 559Combined sources14
Beta strandi563 – 569Combined sources7
Beta strandi572 – 578Combined sources7
Turni580 – 582Combined sources3
Helixi586 – 588Combined sources3
Helixi599 – 603Combined sources5
Helixi609 – 624Combined sources16
Helixi626 – 636Combined sources11
Helixi640 – 647Combined sources8
Helixi651 – 663Combined sources13
Helixi669 – 684Combined sources16
Helixi686 – 694Combined sources9
Beta strandi704 – 708Combined sources5
Helixi725 – 742Combined sources18
Helixi755 – 763Combined sources9
Helixi797 – 802Combined sources6
Helixi808 – 811Combined sources4
Helixi830 – 844Combined sources15
Helixi852 – 859Combined sources8
Helixi867 – 885Combined sources19
Helixi891 – 893Combined sources3
Beta strandi896 – 900Combined sources5
Turni901 – 904Combined sources4
Beta strandi905 – 909Combined sources5
Beta strandi916 – 919Combined sources4
Beta strandi922 – 925Combined sources4
Turni926 – 928Combined sources3
Beta strandi930 – 936Combined sources7
Helixi939 – 950Combined sources12
Beta strandi953 – 959Combined sources7
Beta strandi962 – 966Combined sources5
Helixi971 – 977Combined sources7
Helixi982 – 990Combined sources9
Beta strandi1000 – 1008Combined sources9
Beta strandi1019 – 1023Combined sources5

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP22515.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati27 – 1641-1Add BLAST138
Repeati425 – 5791-2Add BLAST155

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni27 – 5792 approximate repeatsAdd BLAST553

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)DescriptionActionsGraphical viewLength
Sequence conflicti526E → K in CAA39056 (PubMed:1989885).Curated1
Sequence conflicti736S → N in CAA39056 (PubMed:1989885).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3CMMX-ray2.70A/C10-1024[»]
4NNJX-ray2.40A/C9-1024[»]
ProteinModelPortaliP22515.
SMRiP22515.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33955. 61 interactors.
DIPiDIP-4853N.
IntActiP22515. 16 interactors.
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-8866652. Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
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: November 30, 2016
This is version 176 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.