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P22515

- UBA1_YEAST

UniProt

P22515 - UBA1_YEAST

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Protein
Ubiquitin-activating enzyme E1 1
Gene
UBA1, YKL210W
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei600 – 6001Glycyl thioester intermediate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi444 – 47330ATP By similarity
Add
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ubiquitin activating enzyme activity Source: SGD

GO - Biological processi

  1. 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.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-activating enzyme E1 1
Gene namesi
Name:UBA1
Ordered Locus Names:YKL210W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XI

Organism-specific databases

CYGDiYKL210w.
SGDiS000001693. UBA1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 10241023Ubiquitin-activating enzyme E1 1
PRO_0000194977Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei265 – 2651Phosphoserine1 Publication
Modified residuei914 – 9141Phosphoserine1 Publication

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP22515.
PaxDbiP22515.
PeptideAtlasiP22515.
PRIDEiP22515.

Expressioni

Gene expression databases

GenevestigatoriP22515.

Interactioni

Subunit structurei

Monomer.

Binary interactionsi

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

Protein-protein interaction databases

BioGridi33955. 58 interactions.
DIPiDIP-4853N.
IntActiP22515. 16 interactions.
MINTiMINT-489454.
STRINGi4932.YKL210W.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP22515.

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0476.
GeneTreeiENSGT00390000016689.
HOGENOMiHOG000167329.
KOiK03178.
OMAiKFHPVKQ.
OrthoDBiEOG7FZ07P.

Family and domain databases

Gene3Di1.10.3240.10. 2 hits.
3.40.50.720. 4 hits.
InterProiIPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR018965. Ub-activating_enz_e1_C.
IPR023280. Ub-like_act_enz_cat_cys_dom.
IPR000127. UBact_repeat.
IPR019572. Ubiquitin-activating_enzyme.
IPR018075. UBQ-activ_enz_E1.
IPR018074. UBQ-activ_enz_E1_AS.
IPR000011. UBQ/SUMO-activ_enz_E1-like.
[Graphical view]
PfamiPF00899. ThiF. 2 hits.
PF09358. UBA_e1_C. 1 hit.
PF10585. UBA_e1_thiolCys. 1 hit.
PF02134. UBACT. 2 hits.
[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

MSSNNSGLSA AGEIDESLYS RQLYVLGKEA MLKMQTSNVL ILGLKGLGVE     50
IAKNVVLAGV KSMTVFDPEP VQLADLSTQF FLTEKDIGQK RGDVTRAKLA 100
ELNAYVPVNV LDSLDDVTQL SQFQVVVATD TVSLEDKVKI NEFCHSSGIR 150
FISSETRGLF GNTFVDLGDE FTVLDPTGEE PRTGMVSDIE PDGTVTMLDD 200
NRHGLEDGNF VRFSEVEGLD KLNDGTLFKV EVLGPFAFRI GSVKEYGEYK 250
KGGIFTEVKV PRKISFKSLK QQLSNPEFVF SDFAKFDRAA QLHLGFQALH 300
QFAVRHNGEL PRTMNDEDAN ELIKLVTDLS VQQPEVLGEG VDVNEDLIKE 350
LSYQARGDIP GVVAFFGGLV AQEVLKACSG KFTPLKQFMY FDSLESLPDP 400
KNFPRNEKTT QPVNSRYDNQ IAVFGLDFQK KIANSKVFLV GSGAIGCEML 450
KNWALLGLGS GSDGYIVVTD NDSIEKSNLN RQFLFRPKDV GKNKSEVAAE 500
AVCAMNPDLK GKINAKIDKV GPETEEIFND SFWESLDFVT NALDNVDART 550
YVDRRCVFYR KPLLESGTLG TKGNTQVIIP RLTESYSSSR DPPEKSIPLC 600
TLRSFPNKID HTIAWAKSLF QGYFTDSAEN VNMYLTQPNF VEQTLKQSGD 650
VKGVLESISD SLSSKPHNFE DCIKWARLEF EKKFNHDIKQ LLFNFPKDAK 700
TSNGEPFWSG AKRAPTPLEF DIYNNDHFHF VVAGASLRAY NYGIKSDDSN 750
SKPNVDEYKS VIDHMIIPEF TPNANLKIQV NDDDPDPNAN AANGSDEIDQ 800
LVSSLPDPST LAGFKLEPVD FEKDDDTNHH IEFITACSNC RAQNYFIETA 850
DRQKTKFIAG RIIPAIATTT SLVTGLVNLE LYKLIDNKTD IEQYKNGFVN 900
LALPFFGFSE PIASPKGEYN NKKYDKIWDR FDIKGDIKLS DLIEHFEKDE 950
GLEITMLSYG VSLLYASFFP PKKLKERLNL PITQLVKLVT KKDIPAHVST 1000
MILEICADDK EGEDVEVPFI TIHL 1024
Length:1,024
Mass (Da):114,266
Last modified:June 1, 1994 - v2
Checksum:i8910804DF9156661
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti526 – 5261E → K in CAA39056. 1 Publication
Sequence conflicti736 – 7361S → N in CAA39056. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P22515.
SMRi P22515. Positions 11-1024.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33955. 58 interactions.
DIPi DIP-4853N.
IntActi P22515. 16 interactions.
MINTi MINT-489454.
STRINGi 4932.YKL210W.

Proteomic databases

MaxQBi P22515.
PaxDbi P22515.
PeptideAtlasi P22515.
PRIDEi P22515.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YKL210W ; YKL210W ; YKL210W .
GeneIDi 853670.
KEGGi sce:YKL210W.

Organism-specific databases

CYGDi YKL210w.
SGDi S000001693. UBA1.

Phylogenomic databases

eggNOGi COG0476.
GeneTreei ENSGT00390000016689.
HOGENOMi HOG000167329.
KOi K03178.
OMAi KFHPVKQ.
OrthoDBi EOG7FZ07P.

Enzyme and pathway databases

UniPathwayi UPA00143 .
BioCyci YEAST:G3O-31969-MONOMER.

Miscellaneous databases

EvolutionaryTracei P22515.
NextBioi 974614.
PROi P22515.

Gene expression databases

Genevestigatori P22515.

Family and domain databases

Gene3Di 1.10.3240.10. 2 hits.
3.40.50.720. 4 hits.
InterProi IPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR018965. Ub-activating_enz_e1_C.
IPR023280. Ub-like_act_enz_cat_cys_dom.
IPR000127. UBact_repeat.
IPR019572. Ubiquitin-activating_enzyme.
IPR018075. UBQ-activ_enz_E1.
IPR018074. UBQ-activ_enz_E1_AS.
IPR000011. UBQ/SUMO-activ_enz_E1-like.
[Graphical view ]
Pfami PF00899. ThiF. 2 hits.
PF09358. UBA_e1_C. 1 hit.
PF10585. UBA_e1_thiolCys. 1 hit.
PF02134. UBACT. 2 hits.
[Graphical view ]
PRINTSi PR01849. UBIQUITINACT.
SMARTi SM00985. UBA_e1_C. 1 hit.
[Graphical view ]
SUPFAMi SSF69572. SSF69572. 2 hits.
TIGRFAMsi TIGR01408. Ube1. 1 hit.
PROSITEi PS00536. UBIQUITIN_ACTIVAT_1. 1 hit.
PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "UBA 1: an essential yeast gene encoding ubiquitin-activating enzyme."
    McGrath J.P., Jentsch S., Varshavsky A.
    EMBO J. 10:227-236(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: ATCC 204508 / S288c.
  2. "Complete DNA sequence of yeast chromosome XI."
    Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
    , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
    Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "The yeast STE6 gene encodes a homologue of the mammalian multidrug resistance P-glycoprotein."
    McGrath J.P., Varshavsky A.
    Nature 340:400-404(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 940-1024.
    Strain: ATCC 204508 / S288c.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-914, IDENTIFICATION BY MASS SPECTROMETRY [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].
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  10. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

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 3, 2014
This is version 150 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.
Present with 17700 molecules/cell in log phase SD medium.

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

External Data

Dasty 3

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