ABF1_YEAST
ID ABF1_YEAST Reviewed; 731 AA.
AC P14164; D6VXH6;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 4.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=ARS-binding factor 1;
DE AltName: Full=Bidirectionally acting factor 1;
DE AltName: Full=DNA replication enhancer-binding protein OBF1;
DE AltName: Full=SFB-B;
GN Name=ABF1; Synonyms=BAF1, OBF1, REB2, SBF1; OrderedLocusNames=YKL112W;
GN ORFNames=YKL505;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 128-154 AND 535-555,
RP AND MUTAGENESIS OF HIS-57 AND CYS-71.
RX PubMed=2686983; DOI=10.1002/j.1460-2075.1989.tb08612.x;
RA Halfter H., Kavety B., Vandekerckhove J., Kiefer F., Gallwitz D.;
RT "Sequence, expression and mutational analysis of BAF1, a transcriptional
RT activator and ARS1-binding protein of the yeast Saccharomyces cerevisiae.";
RL EMBO J. 8:4265-4272(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2620828; DOI=10.1101/gad.3.12a.1926;
RA Rhode P.R., Sweder K.S., Oegema K.F., Campbell J.L.;
RT "The gene encoding ARS-binding factor I is essential for the viability of
RT yeast.";
RL Genes Dev. 3:1926-1939(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2511628; DOI=10.1126/science.2511628;
RA Diffley J.F.X., Stillman B.;
RT "Similarity between the transcriptional silencer binding proteins ABF1 and
RT RAP1.";
RL Science 246:1034-1038(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PHOSPHORYLATION.
RX PubMed=2034654; DOI=10.1073/pnas.88.10.4089;
RA Francesconi S.C., Eisenberg S.;
RT "The multifunctional protein OBF1 is phosphorylated at serine and threonine
RT residues in Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:4089-4093(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1561835; DOI=10.1002/yea.320080207;
RA Jacquier A., Legrain P., Dujon B.;
RT "Sequence of a 10.7 kb segment of yeast chromosome XI identifies the APN1
RT and the BAF1 loci and reveals one tRNA gene and several new open reading
RT frames including homologs to RAD2 and kinases.";
RL Yeast 8:121-132(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [7]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 585-731.
RX PubMed=8065362; DOI=10.1128/mcb.14.9.6306-6316.1994;
RA Butler A.R., White J.H., Folawiyo Y., Edlin A., Gardiner D., Stark M.J.R.;
RT "Two Saccharomyces cerevisiae genes which control sensitivity to G1 arrest
RT induced by Kluyveromyces lactis toxin.";
RL Mol. Cell. Biol. 14:6306-6316(1994).
RN [9]
RP PHOSPHORYLATION AT SER-720, AND MUTAGENESIS OF SER-720.
RX PubMed=7608180; DOI=10.1074/jbc.270.27.16153;
RA Upton T., Wiltshire S., Francesconi S., Eisenberg S.;
RT "ABF1 Ser-720 is a predominant phosphorylation site for casein kinase II of
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 270:16153-16159(1995).
RN [10]
RP DNA-BINDING.
RX PubMed=9430660; DOI=10.1074/jbc.273.3.1298;
RA Feng L., Wang B., Jong A.;
RT "Saccharomyces cerevisiae Cdc6 stimulates Abf1 DNA binding activity.";
RL J. Biol. Chem. 273:1298-1302(1998).
RN [11]
RP IDENTIFICATION IN THE GGR COMPLEX, AND FUNCTION.
RX PubMed=10601031; DOI=10.1101/gad.13.23.3052;
RA Reed S.H., Akiyama M., Stillman B., Friedberg E.C.;
RT "Yeast autonomously replicating sequence binding factor is involved in
RT nucleotide excision repair.";
RL Genes Dev. 13:3052-3058(1999).
RN [12]
RP FUNCTION.
RX PubMed=10684934; DOI=10.1093/nar/28.6.1390;
RA Lascaris R.F., Groot E., Hoen P.B., Mager W.H., Planta R.J.;
RT "Different roles for abf1p and a T-rich promoter element in nucleosome
RT organization of the yeast RPS28A gene.";
RL Nucleic Acids Res. 28:1390-1396(2000).
RN [13]
RP FUNCTION.
RX PubMed=11713306; DOI=10.1093/nar/29.22.4570;
RA Bodmer-Glavas M., Edler K., Barberis A.;
RT "RNA polymerase II and III transcription factors can stimulate DNA
RT replication by modifying origin chromatin structures.";
RL Nucleic Acids Res. 29:4570-4580(2001).
RN [14]
RP FUNCTION.
RX PubMed=12200417; DOI=10.1074/jbc.m202578200;
RA Fourel G., Miyake T., Defossez P.-A., Li R., Gilson E.;
RT "General regulatory factors (GRFs) as genome partitioners.";
RL J. Biol. Chem. 277:41736-41743(2002).
RN [15]
RP FUNCTION, AND DOMAIN.
RX PubMed=11756546; DOI=10.1128/mcb.22.2.505-516.2002;
RA Miyake T., Loch C.M., Li R.;
RT "Identification of a multifunctional domain in autonomously replicating
RT sequence-binding factor 1 required for transcriptional activation, DNA
RT replication, and gene silencing.";
RL Mol. Cell. Biol. 22:505-516(2002).
RN [16]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [17]
RP FUNCTION OF THE GGR COMPLEX.
RX PubMed=15177043; DOI=10.1016/j.dnarep.2003.11.004;
RA Yu S., Owen-Hughes T., Friedberg E.C., Waters R., Reed S.H.;
RT "The yeast Rad7/Rad16/Abf1 complex generates superhelical torsion in DNA
RT that is required for nucleotide excision repair.";
RL DNA Repair 3:277-287(2004).
RN [18]
RP FUNCTION.
RX PubMed=15456886; DOI=10.1128/mcb.24.20.9152-9164.2004;
RA Yarragudi A., Miyake T., Li R., Morse R.H.;
RT "Comparison of ABF1 and RAP1 in chromatin opening and transactivator
RT potentiation in the budding yeast Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 24:9152-9164(2004).
RN [19]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-625, AND INTERACTION WITH PSE1.
RX PubMed=15522095; DOI=10.1111/j.1600-0854.2004.00233.x;
RA Loch C.M., Mosammaparast N., Miyake T., Pemberton L.F., Li R.;
RT "Functional and physical interactions between autonomously replicating
RT sequence-binding factor 1 and the nuclear transport machinery.";
RL Traffic 5:925-935(2004).
RN [20]
RP DNA-BINDING.
RX PubMed=16083878; DOI=10.1016/j.febslet.2005.07.009;
RA Beinoraviciute-Kellner R., Lipps G., Krauss G.;
RT "In vitro selection of DNA binding sites for ABF1 protein from
RT Saccharomyces cerevisiae.";
RL FEBS Lett. 579:4535-4540(2005).
RN [21]
RP DNA-BINDING, AND FUNCTION.
RX PubMed=16908533; DOI=10.1128/mcb.01197-06;
RA Zou Y., Yu Q., Bi X.;
RT "Asymmetric positioning of nucleosomes and directional establishment of
RT transcriptionally silent chromatin by Saccharomyces cerevisiae silencers.";
RL Mol. Cell. Biol. 26:7806-7819(2006).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467 AND SER-720, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [23]
RP DNA-BINDING, AND FUNCTION.
RX PubMed=17158163; DOI=10.1093/nar/gkl1059;
RA Yarragudi A., Parfrey L.W., Morse R.H.;
RT "Genome-wide analysis of transcriptional dependence and probable target
RT sites for Abf1 and Rap1 in Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 35:193-202(2007).
RN [24]
RP DNA-BINDING.
RX PubMed=19130580; DOI=10.1002/elps.200800218;
RA Yang Q., Zhao Y.C., Xiong Q., Cheng J.;
RT "Rapid chip-based capillary electrophoretic mobility shift assay with
RT negative pressure injection for the binding study of transcription factor
RT Abf1 in Saccharomyces cerevisiae.";
RL Electrophoresis 29:5003-5009(2008).
RN [25]
RP DNA-BINDING, AND FUNCTION.
RX PubMed=18305101; DOI=10.1091/mbc.e07-12-1242;
RA Schlecht U., Erb I., Demougin P., Robine N., Borde V., van Nimwegen E.,
RA Nicolas A., Primig M.;
RT "Genome-wide expression profiling, in vivo DNA binding analysis, and
RT probabilistic motif prediction reveal novel Abf1 target genes during
RT fermentation, respiration, and sporulation in yeast.";
RL Mol. Biol. Cell 19:2193-2207(2008).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-189; SER-193; SER-554;
RP SER-618 AND SER-720, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [27]
RP FUNCTION.
RX PubMed=18996839; DOI=10.1074/jbc.m806830200;
RA Yu S., Smirnova J.B., Friedberg E.C., Stillman B., Akiyama M.,
RA Owen-Hughes T., Waters R., Reed S.H.;
RT "ABF1-binding sites promote efficient global genome nucleotide excision
RT repair.";
RL J. Biol. Chem. 284:966-973(2009).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-720, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [29]
RP DNA-BINDING.
RX PubMed=20098497; DOI=10.1371/journal.pcbi.1000649;
RA Goh W.S., Orlov Y., Li J., Clarke N.D.;
RT "Blurring of high-resolution data shows that the effect of intrinsic
RT nucleosome occupancy on transcription factor binding is mostly regional,
RT not local.";
RL PLoS Comput. Biol. 6:E1000649-E1000649(2010).
RN [30]
RP FUNCTION.
RX PubMed=21081559; DOI=10.1093/nar/gkq1161;
RA Ganapathi M., Palumbo M.J., Ansari S.A., He Q., Tsui K., Nislow C.,
RA Morse R.H.;
RT "Extensive role of the general regulatory factors, Abf1 and Rap1, in
RT determining genome-wide chromatin structure in budding yeast.";
RL Nucleic Acids Res. 39:2032-2044(2011).
RN [31]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-18, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: General regulatory factor (GRF) that contributes to
CC transcriptional activation of a large number of genes, as well as to
CC DNA replication, silencing and telomere structure. Involved in the
CC transcription activation of a subset of ribosomal protein genes. Binds
CC the ARS-elements found in many promoters. Binds to the sequence 5'-
CC TCN(7)ACG-3'. Influences on genome-wide nucleosome occupancy and
CC affects chromatin structure, and probably dynamics. As a component of
CC the global genome repair (GGR) complex, promotes global genome
CC nucleotide excision repair (GG-NER) which removes DNA damage from
CC nontranscribing DNA. Component of the regulatory network controlling
CC mitotic and meiotic cell cycle progression.
CC {ECO:0000269|PubMed:10601031, ECO:0000269|PubMed:10684934,
CC ECO:0000269|PubMed:11713306, ECO:0000269|PubMed:11756546,
CC ECO:0000269|PubMed:12200417, ECO:0000269|PubMed:15177043,
CC ECO:0000269|PubMed:15456886, ECO:0000269|PubMed:16908533,
CC ECO:0000269|PubMed:17158163, ECO:0000269|PubMed:18305101,
CC ECO:0000269|PubMed:18996839, ECO:0000269|PubMed:21081559}.
CC -!- SUBUNIT: Component of the global genome repair (GGR) complex composed
CC of at least ABF1, RAD7 and RAD16. Interacts with PSE1.
CC {ECO:0000269|PubMed:10601031, ECO:0000269|PubMed:15522095}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15522095}.
CC -!- DOMAIN: Contains 2 important clusters of amino acid residues in the C
CC terminus (C-terminal sequence 1 or CS1, residues 624 to 628; and CS2,
CC residues 639 to 662). CS1 specifically participates in transcriptional
CC silencing and/or repression in a context-dependent manner, whereas CS2
CC is universally required for all functions of ABF1.
CC {ECO:0000269|PubMed:11756546}.
CC -!- PTM: Extensively phosphorylated on Ser and Thr residues.
CC {ECO:0000269|PubMed:2034654, ECO:0000269|PubMed:7608180}.
CC -!- MISCELLANEOUS: Present with 4820 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the BAF1 family. {ECO:0000305}.
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DR EMBL; X16385; CAA34421.1; -; Genomic_DNA.
DR EMBL; X51654; CAA35966.1; -; Genomic_DNA.
DR EMBL; M29067; AAA66311.1; -; Genomic_DNA.
DR EMBL; M63578; AAA34823.1; -; Genomic_DNA.
DR EMBL; S93804; AAB22002.1; -; Genomic_DNA.
DR EMBL; Z28111; CAA81951.1; -; Genomic_DNA.
DR EMBL; X77511; CAA54647.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09046.1; -; Genomic_DNA.
DR PIR; S29870; S29870.
DR RefSeq; NP_012810.1; NM_001179678.1.
DR AlphaFoldDB; P14164; -.
DR BioGRID; 34022; 403.
DR ComplexPortal; CPX-1709; Nucleotide excision repair factor 4 complex.
DR DIP; DIP-2199N; -.
DR IntAct; P14164; 26.
DR MINT; P14164; -.
DR STRING; 4932.YKL112W; -.
DR iPTMnet; P14164; -.
DR MaxQB; P14164; -.
DR PaxDb; P14164; -.
DR PRIDE; P14164; -.
DR EnsemblFungi; YKL112W_mRNA; YKL112W; YKL112W.
DR GeneID; 853748; -.
DR KEGG; sce:YKL112W; -.
DR SGD; S000001595; ABF1.
DR VEuPathDB; FungiDB:YKL112W; -.
DR eggNOG; ENOG502QSTW; Eukaryota.
DR HOGENOM; CLU_031229_0_0_1; -.
DR InParanoid; P14164; -.
DR OMA; HRNKHFT; -.
DR BioCyc; YEAST:G3O-31897-MON; -.
DR PRO; PR:P14164; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P14164; protein.
DR GO; GO:0000113; C:nucleotide-excision repair factor 4 complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003688; F:DNA replication origin binding; IDA:SGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:SGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0044374; F:sequence-specific DNA binding, bending; IDA:SGD.
DR GO; GO:0006338; P:chromatin remodeling; IDA:SGD.
DR GO; GO:0006261; P:DNA-templated DNA replication; IDA:SGD.
DR GO; GO:0070911; P:global genome nucleotide-excision repair; IDA:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IMP:SGD.
DR InterPro; IPR006774; BAF1_ABF1.
DR Pfam; PF04684; BAF1_ABF1; 1.
PE 1: Evidence at protein level;
KW Activator; Direct protein sequencing; DNA damage; DNA repair;
KW DNA replication; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..731
FT /note="ARS-binding factor 1"
FT /id="PRO_0000064807"
FT REGION 84..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..628
FT /note="C-terminal sequence 1"
FT REGION 639..662
FT /note="C-terminal sequence 2"
FT REGION 687..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..643
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..714
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 189
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 624
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000255"
FT MOD_RES 720
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:7608180,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CROSSLNK 18
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 57
FT /note="H->Q: Loss of DNA binding."
FT /evidence="ECO:0000269|PubMed:2686983"
FT MUTAGEN 71
FT /note="C->S: Loss of DNA binding."
FT /evidence="ECO:0000269|PubMed:2686983"
FT MUTAGEN 625
FT /note="K->I: Leads to mislocalization into the cytoplasm."
FT /evidence="ECO:0000269|PubMed:15522095"
FT MUTAGEN 720
FT /note="S->A: Strongly reduces phosphorylation by CK2."
FT /evidence="ECO:0000269|PubMed:7608180"
FT CONFLICT 125
FT /note="N -> K (in Ref. 1; CAA34421)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="V -> A (in Ref. 2; CAA35966, 3; AAA66311 and 4;
FT AAA34823)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="T -> I (in Ref. 2; CAA35966, 3; AAA66311 and 4;
FT AAA34823)"
FT /evidence="ECO:0000305"
FT CONFLICT 279..280
FT /note="NT -> TN (in Ref. 2; CAA35966, 3; AAA66311 and 4;
FT AAA34823)"
FT /evidence="ECO:0000305"
FT CONFLICT 690
FT /note="T -> N (in Ref. 2; CAA35966, 3; AAA66311 and 4;
FT AAA34823)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 731 AA; 81753 MW; BE338DA7C9514DC3 CRC64;
MDKLVVNYYE YKHPIINKDL AIGAHGGKKF PTLGAWYDVI NEYEFQTRCP IILKNSHRNK
HFTFACHLKN CPFKVLLSYA GNAASSETSS PSANNNTNPP GTPDHIHHHS NNMNNEDNDN
NNGSNNKVSN DSKLDFVTDD LEYHLANTHP DDTNDKVESR SNEVNGNNDD DADANNIFKQ
QGVTIKNDTE DDSINKASID RGLDDESGPT HGNDSGNHRH NEEDDVHTQM TKNYSDVVND
EDINVAIANA VANVDSQSNN KHDGKDDDAT NNNDGQDNNT NNDHNNNSNI NNNNVGSHGI
SSHSPSSIRD TSMNLDVFNS ATDDIPGPFV VTKIEPYHSH PLEDNLSLGK FILTKIPKIL
QNDLKFDQIL ESSYNNSNHT VSKFKVSHYV EESGLLDILM QRYGLTAEDF EKRLLSQIAR
RITTYKARFV LKKKKMGEYN DLQPSSSSNN NNNNDGELSG TNLRSNSIDY AKHQEISSAG
TSSNTTKNVN NNKNDSNDDN NGNNNNDASN LMESVLDKTS SHRYQPKKMP SVNKWSKPDQ
ITHSDVSMVG LDESNDGGNE NVHPTLAEVD AQEARETAQL AIDKINSYKR SIDDKNGDGH
NNSSRNVVDE NLINDMDSED AHKSKRQHLS DITLEERNED DKLPHEVAEQ LRLLSSHLKE
VENLHQNNDD DVDDVMVDVD VESQYNKNTT HHNNHHSQPH HDEEDVAGLI GKADDEEDLS
DENIQPELRG Q
