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P14164 (ABF1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ARS-binding factor 1
Alternative name(s):
Bidirectionally acting factor 1
DNA replication enhancer-binding protein OBF1
SFB-B
Gene names
Name:ABF1
Synonyms:BAF1, OBF1, REB2, SBF1
Ordered Locus Names:YKL112W
ORF Names:YKL505
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length731 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

General regulatory factor (GRF) that contributes to transcriptional activation of a large number of genes, as well as to DNA replication, silencing and telomere structure. Involved in the transcription activation of a subset of ribosomal protein genes. Binds the ARS-elements found in many promoters. Binds to the sequence 5'-TCN7ACG-3'. Influences on genome-wide nucleosome occupancy and affects chromatin structure, and probably dynamics. As a component of the global genome repair (GGR) complex, promotes global genome nucleotide excision repair (GG-NER) which removes DNA damage from nontranscribing DNA. Component of the regulatory network controlling mitotic and meiotic cell cycle progression. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.21 Ref.23 Ref.25 Ref.27 Ref.30

Subunit structure

Component of the global genome repair (GGR) complex composed of at least ABF1, RAD7 and RAD16. Interacts with PSE1. Ref.11 Ref.19

Subcellular location

Nucleus Ref.19.

Domain

Contains 2 important clusters of amino acid residues in the C terminus (C-terminal sequence 1 or CS1, residues 624 to 628; and CS2, residues 639 to 662). CS1 specifically participates in transcriptional silencing and/or repression in a context-dependent manner, whereas CS2 is universally required for all functions of ABF1. Ref.15

Post-translational modification

Extensively phosphorylated on Ser and Thr residues. Ref.4 Ref.9

Miscellaneous

Present with 4820 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the BAF1 family.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
DNA replication
Transcription
Transcription regulation
   Cellular componentNucleus
   LigandDNA-binding
   Molecular functionActivator
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA-dependent DNA replication

Inferred from direct assay Ref.15. Source: SGD

chromatin remodeling

Inferred from direct assay Ref.12Ref.13. Source: SGD

chromatin silencing at silent mating-type cassette

Inferred from mutant phenotype Ref.21PubMed 8582634. Source: SGD

global genome nucleotide-excision repair

Inferred from direct assay Ref.17. Source: SGD

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 15192094. Source: SGD

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 15192094. Source: SGD

   Cellular_componentnucleotide-excision repair factor 4 complex

Inferred from direct assay Ref.11. Source: SGD

nucleus

Inferred from direct assay Ref.19. Source: SGD

   Molecular_functionDNA replication origin binding

Inferred from direct assay PubMed 16824194PubMed 3281162. Source: SGD

RNA polymerase II core promoter proximal region sequence-specific DNA binding

Inferred from direct assay PubMed 7663308. Source: SGD

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from direct assay PubMed 7663308. Source: SGD

sequence-specific DNA binding

Inferred from direct assay PubMed 3275867PubMed 7663308. Source: SGD

sequence-specific DNA binding, bending

Inferred from direct assay PubMed 8206955. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 731731ARS-binding factor 1
PRO_0000064807

Regions

Region624 – 6285C-terminal sequence 1
Region639 – 66224C-terminal sequence 2
Compositional bias94 – 294201Asn-rich
Compositional bias449 – 51062Asn-rich

Amino acid modifications

Modified residue1891Phosphothreonine Ref.26
Modified residue1931Phosphoserine Ref.26
Modified residue4671Phosphoserine Ref.22
Modified residue5541Phosphoserine Ref.26
Modified residue6181Phosphoserine Ref.26
Modified residue6241Phosphoserine; by PKC Potential
Modified residue7201Phosphoserine; by CK2 Ref.9 Ref.22 Ref.26 Ref.28

Experimental info

Mutagenesis571H → Q: Loss of DNA binding. Ref.1
Mutagenesis711C → S: Loss of DNA binding. Ref.1
Mutagenesis6251K → I: Leads to mislocalization into the cytoplasm. Ref.19
Mutagenesis7201S → A: Strongly reduces phosphorylation by CK2. Ref.9
Sequence conflict1251N → K in CAA34421. Ref.1
Sequence conflict1281V → A in CAA35966. Ref.2
Sequence conflict1281V → A in AAA66311. Ref.3
Sequence conflict1281V → A in AAA34823. Ref.4
Sequence conflict1481T → I in CAA35966. Ref.2
Sequence conflict1481T → I in AAA66311. Ref.3
Sequence conflict1481T → I in AAA34823. Ref.4
Sequence conflict279 – 2802NT → TN in CAA35966. Ref.2
Sequence conflict279 – 2802NT → TN in AAA66311. Ref.3
Sequence conflict279 – 2802NT → TN in AAA34823. Ref.4
Sequence conflict6901T → N in CAA35966. Ref.2
Sequence conflict6901T → N in AAA66311. Ref.3
Sequence conflict6901T → N in AAA34823. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P14164 [UniParc].

Last modified October 5, 2010. Version 4.
Checksum: BE338DA7C9514DC3

FASTA73181,753
        10         20         30         40         50         60 
MDKLVVNYYE YKHPIINKDL AIGAHGGKKF PTLGAWYDVI NEYEFQTRCP IILKNSHRNK 

        70         80         90        100        110        120 
HFTFACHLKN CPFKVLLSYA GNAASSETSS PSANNNTNPP GTPDHIHHHS NNMNNEDNDN 

       130        140        150        160        170        180 
NNGSNNKVSN DSKLDFVTDD LEYHLANTHP DDTNDKVESR SNEVNGNNDD DADANNIFKQ 

       190        200        210        220        230        240 
QGVTIKNDTE DDSINKASID RGLDDESGPT HGNDSGNHRH NEEDDVHTQM TKNYSDVVND 

       250        260        270        280        290        300 
EDINVAIANA VANVDSQSNN KHDGKDDDAT NNNDGQDNNT NNDHNNNSNI NNNNVGSHGI 

       310        320        330        340        350        360 
SSHSPSSIRD TSMNLDVFNS ATDDIPGPFV VTKIEPYHSH PLEDNLSLGK FILTKIPKIL 

       370        380        390        400        410        420 
QNDLKFDQIL ESSYNNSNHT VSKFKVSHYV EESGLLDILM QRYGLTAEDF EKRLLSQIAR 

       430        440        450        460        470        480 
RITTYKARFV LKKKKMGEYN DLQPSSSSNN NNNNDGELSG TNLRSNSIDY AKHQEISSAG 

       490        500        510        520        530        540 
TSSNTTKNVN NNKNDSNDDN NGNNNNDASN LMESVLDKTS SHRYQPKKMP SVNKWSKPDQ 

       550        560        570        580        590        600 
ITHSDVSMVG LDESNDGGNE NVHPTLAEVD AQEARETAQL AIDKINSYKR SIDDKNGDGH 

       610        620        630        640        650        660 
NNSSRNVVDE NLINDMDSED AHKSKRQHLS DITLEERNED DKLPHEVAEQ LRLLSSHLKE 

       670        680        690        700        710        720 
VENLHQNNDD DVDDVMVDVD VESQYNKNTT HHNNHHSQPH HDEEDVAGLI GKADDEEDLS 

       730 
DENIQPELRG Q 

« Hide

References

« Hide 'large scale' references
[1]"Sequence, expression and mutational analysis of BAF1, a transcriptional activator and ARS1-binding protein of the yeast Saccharomyces cerevisiae."
Halfter H., Kavety B., Vandekerckhove J., Kiefer F., Gallwitz D.
EMBO J. 8:4265-4272(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 128-154 AND 535-555, MUTAGENESIS OF HIS-57 AND CYS-71.
[2]"The gene encoding ARS-binding factor I is essential for the viability of yeast."
Rhode P.R., Sweder K.S., Oegema K.F., Campbell J.L.
Genes Dev. 3:1926-1939(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Similarity between the transcriptional silencer binding proteins ABF1 and RAP1."
Diffley J.F.X., Stillman B.
Science 246:1034-1038(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"The multifunctional protein OBF1 is phosphorylated at serine and threonine residues in Saccharomyces cerevisiae."
Francesconi S.C., Eisenberg S.
Proc. Natl. Acad. Sci. U.S.A. 88:4089-4093(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PHOSPHORYLATION.
[5]"Sequence of a 10.7 kb segment of yeast chromosome XI identifies the APN1 and the BAF1 loci and reveals one tRNA gene and several new open reading frames including homologs to RAD2 and kinases."
Jacquier A., Legrain P., Dujon B.
Yeast 8:121-132(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[7]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[8]"Two Saccharomyces cerevisiae genes which control sensitivity to G1 arrest induced by Kluyveromyces lactis toxin."
Butler A.R., White J.H., Folawiyo Y., Edlin A., Gardiner D., Stark M.J.R.
Mol. Cell. Biol. 14:6306-6316(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 585-731.
[9]"ABF1 Ser-720 is a predominant phosphorylation site for casein kinase II of Saccharomyces cerevisiae."
Upton T., Wiltshire S., Francesconi S., Eisenberg S.
J. Biol. Chem. 270:16153-16159(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-720, MUTAGENESIS OF SER-720.
[10]"Saccharomyces cerevisiae Cdc6 stimulates Abf1 DNA binding activity."
Feng L., Wang B., Jong A.
J. Biol. Chem. 273:1298-1302(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING.
[11]"Yeast autonomously replicating sequence binding factor is involved in nucleotide excision repair."
Reed S.H., Akiyama M., Stillman B., Friedberg E.C.
Genes Dev. 13:3052-3058(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE GGR COMPLEX, FUNCTION.
[12]"Different roles for abf1p and a T-rich promoter element in nucleosome organization of the yeast RPS28A gene."
Lascaris R.F., Groot E., Hoen P.B., Mager W.H., Planta R.J.
Nucleic Acids Res. 28:1390-1396(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"RNA polymerase II and III transcription factors can stimulate DNA replication by modifying origin chromatin structures."
Bodmer-Glavas M., Edler K., Barberis A.
Nucleic Acids Res. 29:4570-4580(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"General regulatory factors (GRFs) as genome partitioners."
Fourel G., Miyake T., Defossez P.-A., Li R., Gilson E.
J. Biol. Chem. 277:41736-41743(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"Identification of a multifunctional domain in autonomously replicating sequence-binding factor 1 required for transcriptional activation, DNA replication, and gene silencing."
Miyake T., Loch C.M., Li R.
Mol. Cell. Biol. 22:505-516(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DOMAIN.
[16]"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] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[17]"The yeast Rad7/Rad16/Abf1 complex generates superhelical torsion in DNA that is required for nucleotide excision repair."
Yu S., Owen-Hughes T., Friedberg E.C., Waters R., Reed S.H.
DNA Repair 3:277-287(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE GGR COMPLEX.
[18]"Comparison of ABF1 and RAP1 in chromatin opening and transactivator potentiation in the budding yeast Saccharomyces cerevisiae."
Yarragudi A., Miyake T., Li R., Morse R.H.
Mol. Cell. Biol. 24:9152-9164(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[19]"Functional and physical interactions between autonomously replicating sequence-binding factor 1 and the nuclear transport machinery."
Loch C.M., Mosammaparast N., Miyake T., Pemberton L.F., Li R.
Traffic 5:925-935(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-625, INTERACTION WITH PSE1.
[20]"In vitro selection of DNA binding sites for ABF1 protein from Saccharomyces cerevisiae."
Beinoraviciute-Kellner R., Lipps G., Krauss G.
FEBS Lett. 579:4535-4540(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING.
[21]"Asymmetric positioning of nucleosomes and directional establishment of transcriptionally silent chromatin by Saccharomyces cerevisiae silencers."
Zou Y., Yu Q., Bi X.
Mol. Cell. Biol. 26:7806-7819(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING, FUNCTION.
[22]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467 AND SER-720, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[23]"Genome-wide analysis of transcriptional dependence and probable target sites for Abf1 and Rap1 in Saccharomyces cerevisiae."
Yarragudi A., Parfrey L.W., Morse R.H.
Nucleic Acids Res. 35:193-202(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING, FUNCTION.
[24]"Rapid chip-based capillary electrophoretic mobility shift assay with negative pressure injection for the binding study of transcription factor Abf1 in Saccharomyces cerevisiae."
Yang Q., Zhao Y.C., Xiong Q., Cheng J.
Electrophoresis 29:5003-5009(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING.
[25]"Genome-wide expression profiling, in vivo DNA binding analysis, and probabilistic motif prediction reveal novel Abf1 target genes during fermentation, respiration, and sporulation in yeast."
Schlecht U., Erb I., Demougin P., Robine N., Borde V., van Nimwegen E., Nicolas A., Primig M.
Mol. Biol. Cell 19:2193-2207(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING, FUNCTION.
[26]"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 THR-189; SER-193; SER-554; SER-618 AND SER-720, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"ABF1-binding sites promote efficient global genome nucleotide excision repair."
Yu S., Smirnova J.B., Friedberg E.C., Stillman B., Akiyama M., Owen-Hughes T., Waters R., Reed S.H.
J. Biol. Chem. 284:966-973(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[28]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-720, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"Blurring of high-resolution data shows that the effect of intrinsic nucleosome occupancy on transcription factor binding is mostly regional, not local."
Goh W.S., Orlov Y., Li J., Clarke N.D.
PLoS Comput. Biol. 6:E1000649-E1000649(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING.
[30]"Extensive role of the general regulatory factors, Abf1 and Rap1, in determining genome-wide chromatin structure in budding yeast."
Ganapathi M., Palumbo M.J., Ansari S.A., He Q., Tsui K., Nislow C., Morse R.H.
Nucleic Acids Res. 39:2032-2044(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[31]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X16385 Genomic DNA. Translation: CAA34421.1.
X51654 Genomic DNA. Translation: CAA35966.1.
M29067 Genomic DNA. Translation: AAA66311.1.
M63578 Genomic DNA. Translation: AAA34823.1.
S93804 Genomic DNA. Translation: AAB22002.1.
Z28111 Genomic DNA. Translation: CAA81951.1.
X77511 Genomic DNA. Translation: CAA54647.1.
BK006944 Genomic DNA. Translation: DAA09046.1.
PIRS29870.
RefSeqNP_012810.1. NM_001179678.1.

3D structure databases

ProteinModelPortalP14164.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34022. 37 interactions.
DIPDIP-2199N.
IntActP14164. 26 interactions.
MINTMINT-2783533.
STRING4932.YKL112W.

Proteomic databases

MaxQBP14164.
PaxDbP14164.
PeptideAtlasP14164.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYKL112W; YKL112W; YKL112W.
GeneID853748.
KEGGsce:YKL112W.

Organism-specific databases

SGDS000001595. ABF1.

Phylogenomic databases

eggNOGNOG43177.
KOK09249.
OMAACHLKNC.
OrthoDBEOG7KSXM9.

Enzyme and pathway databases

BioCycYEAST:G3O-31897-MONOMER.

Gene expression databases

GenevestigatorP14164.

Family and domain databases

InterProIPR006774. BAF1_ABF1.
[Graphical view]
PfamPF04684. BAF1_ABF1. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio974810.

Entry information

Entry nameABF1_YEAST
AccessionPrimary (citable) accession number: P14164
Secondary accession number(s): D6VXH6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: October 5, 2010
Last modified: July 9, 2014
This is version 129 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XI

Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families