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P14164

- ABF1_YEAST

UniProt

P14164 - ABF1_YEAST

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Protein

ARS-binding factor 1

Gene

ABF1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.12 Publications

GO - Molecular functioni

  1. DNA replication origin binding Source: SGD
  2. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: SGD
  3. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: SGD
  4. sequence-specific DNA binding Source: SGD
  5. sequence-specific DNA binding, bending Source: SGD

GO - Biological processi

  1. chromatin remodeling Source: SGD
  2. chromatin silencing at silent mating-type cassette Source: SGD
  3. DNA-dependent DNA replication Source: SGD
  4. global genome nucleotide-excision repair Source: SGD
  5. negative regulation of transcription from RNA polymerase II promoter Source: SGD
  6. positive regulation of transcription from RNA polymerase II promoter Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

DNA damage, DNA repair, DNA replication, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31897-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
ARS-binding factor 1
Alternative name(s):
Bidirectionally acting factor 1
DNA replication enhancer-binding protein OBF1
SFB-B
Gene namesi
Name:ABF1
Synonyms:BAF1, OBF1, REB2, SBF1
Ordered Locus Names:YKL112W
ORF Names:YKL505
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XI

Organism-specific databases

SGDiS000001595. ABF1.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. nucleotide-excision repair factor 4 complex Source: SGD
  2. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi57 – 571H → Q: Loss of DNA binding. 1 Publication
Mutagenesisi71 – 711C → S: Loss of DNA binding. 1 Publication
Mutagenesisi625 – 6251K → I: Leads to mislocalization into the cytoplasm. 1 Publication
Mutagenesisi720 – 7201S → A: Strongly reduces phosphorylation by CK2. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 731731ARS-binding factor 1PRO_0000064807Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei189 – 1891Phosphothreonine1 Publication
Modified residuei193 – 1931Phosphoserine1 Publication
Modified residuei467 – 4671Phosphoserine1 Publication
Modified residuei554 – 5541Phosphoserine1 Publication
Modified residuei618 – 6181Phosphoserine1 Publication
Modified residuei624 – 6241Phosphoserine; by PKCSequence Analysis
Modified residuei720 – 7201Phosphoserine; by CK24 Publications

Post-translational modificationi

Extensively phosphorylated on Ser and Thr residues.5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP14164.
PaxDbiP14164.
PeptideAtlasiP14164.

Expressioni

Gene expression databases

GenevestigatoriP14164.

Interactioni

Subunit structurei

Component of the global genome repair (GGR) complex composed of at least ABF1, RAD7 and RAD16. Interacts with PSE1.2 Publications

Protein-protein interaction databases

BioGridi34022. 37 interactions.
DIPiDIP-2199N.
IntActiP14164. 26 interactions.
MINTiMINT-2783533.
STRINGi4932.YKL112W.

Structurei

3D structure databases

ProteinModelPortaliP14164.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni624 – 6285C-terminal sequence 1
Regioni639 – 66224C-terminal sequence 2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi94 – 294201Asn-richAdd
BLAST
Compositional biasi449 – 51062Asn-richAdd
BLAST

Domaini

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 ABF1.1 Publication

Sequence similaritiesi

Belongs to the BAF1 family.Curated

Phylogenomic databases

eggNOGiNOG43177.
InParanoidiP14164.
KOiK09249.
OMAiACHLKNC.
OrthoDBiEOG7KSXM9.

Family and domain databases

InterProiIPR006774. BAF1_ABF1.
[Graphical view]
PfamiPF04684. BAF1_ABF1. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P14164 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDKLVVNYYE YKHPIINKDL AIGAHGGKKF PTLGAWYDVI NEYEFQTRCP
60 70 80 90 100
IILKNSHRNK HFTFACHLKN CPFKVLLSYA GNAASSETSS PSANNNTNPP
110 120 130 140 150
GTPDHIHHHS NNMNNEDNDN NNGSNNKVSN DSKLDFVTDD LEYHLANTHP
160 170 180 190 200
DDTNDKVESR SNEVNGNNDD DADANNIFKQ QGVTIKNDTE DDSINKASID
210 220 230 240 250
RGLDDESGPT HGNDSGNHRH NEEDDVHTQM TKNYSDVVND EDINVAIANA
260 270 280 290 300
VANVDSQSNN KHDGKDDDAT NNNDGQDNNT NNDHNNNSNI NNNNVGSHGI
310 320 330 340 350
SSHSPSSIRD TSMNLDVFNS ATDDIPGPFV VTKIEPYHSH PLEDNLSLGK
360 370 380 390 400
FILTKIPKIL QNDLKFDQIL ESSYNNSNHT VSKFKVSHYV EESGLLDILM
410 420 430 440 450
QRYGLTAEDF EKRLLSQIAR RITTYKARFV LKKKKMGEYN DLQPSSSSNN
460 470 480 490 500
NNNNDGELSG TNLRSNSIDY AKHQEISSAG TSSNTTKNVN NNKNDSNDDN
510 520 530 540 550
NGNNNNDASN LMESVLDKTS SHRYQPKKMP SVNKWSKPDQ ITHSDVSMVG
560 570 580 590 600
LDESNDGGNE NVHPTLAEVD AQEARETAQL AIDKINSYKR SIDDKNGDGH
610 620 630 640 650
NNSSRNVVDE NLINDMDSED AHKSKRQHLS DITLEERNED DKLPHEVAEQ
660 670 680 690 700
LRLLSSHLKE VENLHQNNDD DVDDVMVDVD VESQYNKNTT HHNNHHSQPH
710 720 730
HDEEDVAGLI GKADDEEDLS DENIQPELRG Q
Length:731
Mass (Da):81,753
Last modified:October 5, 2010 - v4
Checksum:iBE338DA7C9514DC3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti125 – 1251N → K in CAA34421. (PubMed:2686983)Curated
Sequence conflicti128 – 1281V → A in CAA35966. (PubMed:2620828)Curated
Sequence conflicti128 – 1281V → A in AAA66311. (PubMed:2511628)Curated
Sequence conflicti128 – 1281V → A in AAA34823. (PubMed:2034654)Curated
Sequence conflicti148 – 1481T → I in CAA35966. (PubMed:2620828)Curated
Sequence conflicti148 – 1481T → I in AAA66311. (PubMed:2511628)Curated
Sequence conflicti148 – 1481T → I in AAA34823. (PubMed:2034654)Curated
Sequence conflicti279 – 2802NT → TN in CAA35966. (PubMed:2620828)Curated
Sequence conflicti279 – 2802NT → TN in AAA66311. (PubMed:2511628)Curated
Sequence conflicti279 – 2802NT → TN in AAA34823. (PubMed:2034654)Curated
Sequence conflicti690 – 6901T → N in CAA35966. (PubMed:2620828)Curated
Sequence conflicti690 – 6901T → N in AAA66311. (PubMed:2511628)Curated
Sequence conflicti690 – 6901T → N in AAA34823. (PubMed:2034654)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiS29870.
RefSeqiNP_012810.1. NM_001179678.1.

Genome annotation databases

EnsemblFungiiYKL112W; YKL112W; YKL112W.
GeneIDi853748.
KEGGisce:YKL112W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi S29870.
RefSeqi NP_012810.1. NM_001179678.1.

3D structure databases

ProteinModelPortali P14164.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 34022. 37 interactions.
DIPi DIP-2199N.
IntActi P14164. 26 interactions.
MINTi MINT-2783533.
STRINGi 4932.YKL112W.

Proteomic databases

MaxQBi P14164.
PaxDbi P14164.
PeptideAtlasi P14164.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YKL112W ; YKL112W ; YKL112W .
GeneIDi 853748.
KEGGi sce:YKL112W.

Organism-specific databases

SGDi S000001595. ABF1.

Phylogenomic databases

eggNOGi NOG43177.
InParanoidi P14164.
KOi K09249.
OMAi ACHLKNC.
OrthoDBi EOG7KSXM9.

Enzyme and pathway databases

BioCyci YEAST:G3O-31897-MONOMER.

Miscellaneous databases

NextBioi 974810.

Gene expression databases

Genevestigatori P14164.

Family and domain databases

InterProi IPR006774. BAF1_ABF1.
[Graphical view ]
Pfami PF04684. BAF1_ABF1. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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].

Entry informationi

Entry nameiABF1_YEAST
AccessioniPrimary (citable) accession number: P14164
Secondary accession number(s): D6VXH6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: October 5, 2010
Last modified: October 29, 2014
This is version 131 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 4820 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

External Data

Dasty 3