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P22515 (UBA1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-activating enzyme E1 1
Gene names
Name:UBA1
Ordered Locus Names:YKL210W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length1024 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 an ubiquitin-E1 thioester and free AMP.

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Monomer.

Subcellular location

Cytoplasm. Nucleus.

Post-translational modification

The N-terminus is blocked.

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. Ref.5

Sequence similarities

Belongs to the ubiquitin-activating E1 family.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   DomainRepeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processprotein ubiquitination

Inferred from direct assay Ref.1. Source: SGD

   Cellular componentcytoplasm

Inferred from direct assay. Source: SGD

nucleus

Inferred from direct assay. Source: SGD

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ligase activity

Inferred from electronic annotation. Source: UniProtKB-KW

ubiquitin activating enzyme activity

Inferred from direct assay Ref.1. Source: SGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

UBI1P618642EBI-19703,EBI-19797From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10241024Ubiquitin-activating enzyme E1 1
PRO_0000194977

Regions

Repeat27 – 1641381-1
Repeat425 – 5791551-2
Nucleotide binding444 – 47330ATP By similarity
Region27 – 5795532 approximate repeats

Sites

Active site6001Glycyl thioester intermediate By similarity

Amino acid modifications

Modified residue1871Phosphoserine Ref.7
Modified residue2651Phosphoserine Ref.6
Modified residue9141Phosphoserine Ref.7

Experimental info

Sequence conflict5261E → K in CAA39056. Ref.1
Sequence conflict7361S → N in CAA39056. Ref.1

Secondary structure

1 ................................................................................................................................................................. 1024
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P22515 [UniParc].

Last modified June 1, 1994. Version 2.
Checksum: 8910804DF9156661

FASTA1,024114,266
        10         20         30         40         50         60 
MSSNNSGLSA AGEIDESLYS RQLYVLGKEA MLKMQTSNVL ILGLKGLGVE IAKNVVLAGV 

        70         80         90        100        110        120 
KSMTVFDPEP VQLADLSTQF FLTEKDIGQK RGDVTRAKLA ELNAYVPVNV LDSLDDVTQL 

       130        140        150        160        170        180 
SQFQVVVATD TVSLEDKVKI NEFCHSSGIR FISSETRGLF GNTFVDLGDE FTVLDPTGEE 

       190        200        210        220        230        240 
PRTGMVSDIE PDGTVTMLDD NRHGLEDGNF VRFSEVEGLD KLNDGTLFKV EVLGPFAFRI 

       250        260        270        280        290        300 
GSVKEYGEYK KGGIFTEVKV PRKISFKSLK QQLSNPEFVF SDFAKFDRAA QLHLGFQALH 

       310        320        330        340        350        360 
QFAVRHNGEL PRTMNDEDAN ELIKLVTDLS VQQPEVLGEG VDVNEDLIKE LSYQARGDIP 

       370        380        390        400        410        420 
GVVAFFGGLV AQEVLKACSG KFTPLKQFMY FDSLESLPDP KNFPRNEKTT QPVNSRYDNQ 

       430        440        450        460        470        480 
IAVFGLDFQK KIANSKVFLV GSGAIGCEML KNWALLGLGS GSDGYIVVTD NDSIEKSNLN 

       490        500        510        520        530        540 
RQFLFRPKDV GKNKSEVAAE AVCAMNPDLK GKINAKIDKV GPETEEIFND SFWESLDFVT 

       550        560        570        580        590        600 
NALDNVDART YVDRRCVFYR KPLLESGTLG TKGNTQVIIP RLTESYSSSR DPPEKSIPLC 

       610        620        630        640        650        660 
TLRSFPNKID HTIAWAKSLF QGYFTDSAEN VNMYLTQPNF VEQTLKQSGD VKGVLESISD 

       670        680        690        700        710        720 
SLSSKPHNFE DCIKWARLEF EKKFNHDIKQ LLFNFPKDAK TSNGEPFWSG AKRAPTPLEF 

       730        740        750        760        770        780 
DIYNNDHFHF VVAGASLRAY NYGIKSDDSN SKPNVDEYKS VIDHMIIPEF TPNANLKIQV 

       790        800        810        820        830        840 
NDDDPDPNAN AANGSDEIDQ LVSSLPDPST LAGFKLEPVD FEKDDDTNHH IEFITACSNC 

       850        860        870        880        890        900 
RAQNYFIETA DRQKTKFIAG RIIPAIATTT SLVTGLVNLE LYKLIDNKTD IEQYKNGFVN 

       910        920        930        940        950        960 
LALPFFGFSE PIASPKGEYN NKKYDKIWDR FDIKGDIKLS DLIEHFEKDE GLEITMLSYG 

       970        980        990       1000       1010       1020 
VSLLYASFFP PKKLKERLNL PITQLVKLVT KKDIPAHVST MILEICADDK EGEDVEVPFI 


TIHL

« Hide

References

« Hide 'large scale' references
[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: 1989885] [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. expand/collapse author list , 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: 8196765] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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: 2569166] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 940-1024.
Strain: ATCC 204508 / S288c.
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
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: 17287358] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265, MASS SPECTROMETRY.
[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: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187 AND SER-914, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X55386 Genomic DNA. Translation: CAA39056.1.
Z28210 Genomic DNA. Translation: CAA82055.1.
X15428 Genomic DNA. Translation: CAA33468.1.
BK006944 Genomic DNA. Translation: DAA08959.1.
PIRS38048.
RefSeqNP_012712.1. NM_001179775.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3CMMX-ray2.70A/C10-1024[»]
ProteinModelPortalP22515.
SMRP22515. Positions 11-1024.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-4853N.
IntActP22515. 45 interactions.
MINTMINT-489454.
STRINGP22515.

Proteomic databases

PeptideAtlasP22515.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYKL210W; YKL210W; YKL210W.
GeneID853670.
KEGGsce:YKL210W.
NMPDRfig|4932.3.peg.3690.

Organism-specific databases

CYGDYKL210w.
SGDS000001693. UBA1.

Phylogenomic databases

eggNOGfuNOG04951.
GeneTreeEFGT00050000001311.
HOGENOMHBG356508.
OMAGMEGLNG.
OrthoDBEOG4NKG3P.

Gene expression databases

ArrayExpressP22515.
GenevestigatorP22515.
GermOnlineYKL210W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR009036. 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]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 4 hits.
G3DSA:1.10.3240.10. Ub-like_act_enz_cat_cys_dom. 1 hit.
KOK03178.
PfamPF00899. ThiF. 2 hits.
PF09358. UBA_e1_C. 1 hit.
PF10585. UBA_e1_thiolCys. 1 hit.
PF02134. UBACT. 2 hits.
[Graphical view]
PRINTSPR01849. UBIQUITINACT.
SMARTSM00985. UBA_e1_C. 1 hit.
[Graphical view]
SUPFAMSSF69572. MoeB. 2 hits.
TIGRFAMsTIGR01408. Ube1. 1 hit.
PROSITEPS00536. UBIQUITIN_ACTIVAT_1. 1 hit.
PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio974614.

Entry information

Entry nameUBA1_YEAST
AccessionPrimary (citable) accession number: P22515
Secondary accession number(s): D6VWZ3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: June 1, 1994
Last modified: January 25, 2012
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

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

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents