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P22515

- UBA1_YEAST

UniProt

P22515 - UBA1_YEAST

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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: 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 intermediatePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi444 – 47330ATPBy similarityAdd
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.
ReactomeiREACT_270320. ISG15 antiviral mechanism.
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 1PRO_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

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

eggNOGiCOG0476.
GeneTreeiENSGT00390000016689.
HOGENOMiHOG000167329.
InParanoidiP22515.
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

        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 .
PIRi S38048.
RefSeqi NP_012712.1. NM_001179775.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P22515.
KOi K03178.
OMAi KFHPVKQ.
OrthoDBi EOG7FZ07P.

Enzyme and pathway databases

UniPathwayi UPA00143 .
BioCyci YEAST:G3O-31969-MONOMER.
Reactomei REACT_270320. ISG15 antiviral mechanism.

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: November 26, 2014
This is version 153 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.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

External Data

Dasty 3