NAP1_YEAST
ID NAP1_YEAST Reviewed; 417 AA.
AC P25293; D6VXA9; P87196;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Nucleosome assembly protein {ECO:0000303|PubMed:2016313};
GN Name=NAP1 {ECO:0000303|PubMed:2016313};
GN OrderedLocusNames=YKR048C {ECO:0000312|SGD:S000001756};
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], AND FUNCTION.
RX PubMed=2016313; DOI=10.1016/s0021-9258(20)89604-5;
RA Ishimi Y., Kikuchi A.;
RT "Identification and molecular cloning of yeast homolog of nucleosome
RT assembly protein I which facilitates nucleosome assembly in vitro.";
RL J. Biol. Chem. 266:7025-7029(1991).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP PROTEIN SEQUENCE OF 251-256, FUNCTION, INTERACTION WITH CLB2, AND
RP SUBCELLULAR LOCATION.
RX PubMed=7622566; DOI=10.1083/jcb.130.3.661;
RA Kellogg D.R., Kikuchi A., Fujii-Nakata T., Turck C.W., Murray A.W.;
RT "Members of the NAP/SET family of proteins interact specifically with B-
RT type cyclins.";
RL J. Cell Biol. 130:661-673(1995).
RN [6]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP GIN4 COMPLEX.
RX PubMed=12058072; DOI=10.1091/mbc.01-10-0500;
RA Mortensen E.M., McDonald H., Yates J. III, Kellogg D.R.;
RT "Cell cycle-dependent assembly of a Gin4-septin complex.";
RL Mol. Biol. Cell 13:2091-2105(2002).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; THR-24; SER-27; SER-76
RP AND SER-177, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [11]
RP FUNCTION, INTERACTION WITH RPL18A OR RPL18B; CKA2; CKI1; TEF1 OR TEF2;
RP FOL1; HSC82; HTA2; HTB2; HTZ1; KAP114; KCC4; NIS1; SSA1; SSA2; SSB1; SSC1;
RP SHM1; SIP5; TCO89 AND NBA1, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
RP PHOSPHORYLATION AT SER-82; SER-98; SER-104 AND SER-140, PHOSPHORYLATION AT
RP SER-159; SER-177 AND SER-397 BY CK2, MUTAGENESIS OF LEU-99; SER-159;
RP SER-177 AND SER-397, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18086883; DOI=10.1128/mcb.01035-07;
RA Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F.,
RA Pemberton L.F.;
RT "Phosphorylation by casein kinase 2 regulates Nap1 localization and
RT function.";
RL Mol. Cell. Biol. 28:1313-1325(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; THR-24; SER-27; SER-76;
RP SER-140 AND SER-177, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; THR-24; SER-27; THR-53;
RP SER-69; SER-76; SER-82 AND SER-177, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [14]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-50, 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).
RN [15]
RP INTERACTION WITH HISTONE H3/H4 HETERODIMERS.
RX PubMed=27036862; DOI=10.1093/nar/gkw209;
RA Hammond C.M., Sundaramoorthy R., Larance M., Lamond A., Stevens M.A.,
RA El-Mkami H., Norman D.G., Owen-Hughes T.;
RT "The histone chaperone Vps75 forms multiple oligomeric assemblies capable
RT of mediating exchange between histone H3-H4 tetramers and Asf1-H3-H4
RT complexes.";
RL Nucleic Acids Res. 44:6157-6172(2016).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), AND SUBUNIT.
RX PubMed=16432217; DOI=10.1073/pnas.0508002103;
RA Park Y.-J., Luger K.;
RT "The structure of nucleosome assembly protein 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:1248-1253(2006).
CC -!- FUNCTION: Acidic protein, which assembles histones into an octamer (in
CC vitro). Involved in the regulation of the localization and the function
CC of the septins during mitosis. Involved in the function of B-type
CC cyclins. {ECO:0000269|PubMed:12058072, ECO:0000269|PubMed:18086883,
CC ECO:0000269|PubMed:2016313, ECO:0000269|PubMed:7622566}.
CC -!- SUBUNIT: Component of the GIN4 complex composed of at least BNI5, CDC3,
CC CDC10, CDC11, CDC12, GIN4, NAP1 and SHS1 which forms a ring at the bud
CC neck (PubMed:12058072). Homodimer (in-vitro) (PubMed:16432217).
CC Interacts with the B-type cyclin CLB2 (PubMed:7622566). Interacts with
CC 60S ribosomal protein L18 (RPL18A or RPL18B), CKA2, CKI1, eukaryotic
CC elongation factor 1 complex eEF1A (TEF1 or TEF2), FOL1, HSC82, HTA2,
CC HTB2, HTZ1, KAP114, KCC4, NIS1, SSA1, SSA2, SSB1, SSC1, SHM1, SIP5 and
CC TCO89 (PubMed:18086883). Interacts with NBA1 (PubMed:18086883).
CC Interacts with histone H3/H4 heterodimers (PubMed:27036862).
CC {ECO:0000269|PubMed:12058072, ECO:0000269|PubMed:16432217,
CC ECO:0000269|PubMed:18086883, ECO:0000269|PubMed:27036862,
CC ECO:0000269|PubMed:7622566}.
CC -!- INTERACTION:
CC P25293; Q99299: AIM44; NbExp=5; IntAct=EBI-11850, EBI-29423;
CC P25293; P20485: CKI1; NbExp=5; IntAct=EBI-11850, EBI-9699;
CC P25293; Q12263: GIN4; NbExp=11; IntAct=EBI-11850, EBI-7595;
CC P25293; P04911: HTA1; NbExp=3; IntAct=EBI-11850, EBI-8072;
CC P25293; P25389: KCC4; NbExp=5; IntAct=EBI-11850, EBI-9607;
CC P25293; P25293: NAP1; NbExp=4; IntAct=EBI-11850, EBI-11850;
CC P25293; P53939: NIS1; NbExp=5; IntAct=EBI-11850, EBI-28760;
CC P25293; P38615: RIM11; NbExp=8; IntAct=EBI-11850, EBI-10642;
CC P25293; Q07794: RTT109; NbExp=2; IntAct=EBI-11850, EBI-2887026;
CC P25293; Q08921: TCO89; NbExp=2; IntAct=EBI-11850, EBI-37395;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Bud neck.
CC Note=Phosphorylation by CK2 promotes the import into the nucleus.
CC -!- DOMAIN: The acidic domains are probably involved in the interaction
CC with histones. {ECO:0000269|PubMed:16432217}.
CC -!- PTM: Phosphorylation by CK2 is required for normal progression through
CC S phase. CK2 phosphorylation is not required for correct bud formation
CC nor histone binding. {ECO:0000269|PubMed:18086883}.
CC -!- DISRUPTION PHENOTYPE: Exhibits a large proportion of multinucleate
CC cells. Elongated buds. The percentage of elongated buds is
CC significantly increased when GIN4 or CKI1 is also deleted. Small
CC decrease in the percentage of cells with elongated buds is observed in
CC NAP1 and CKA2 double mutant. NAP1 and CKI1 double mutant exhibits
CC increased sensitivity to benomyl. Increased resistance to benomyl in
CC NAP1 and CKA2 double mutant. {ECO:0000269|PubMed:18086883}.
CC -!- MISCELLANEOUS: Present with 8070 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the nucleosome assembly protein (NAP) family.
CC {ECO:0000305}.
CC -!- CAUTION: NAP-I was previously referred to as AP-I. {ECO:0000305}.
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DR EMBL; M63555; AAA34811.1; -; Genomic_DNA.
DR EMBL; AY692777; AAT92796.1; -; Genomic_DNA.
DR EMBL; Z28272; CAA82124.2; -; Genomic_DNA.
DR EMBL; Z28273; CAA82125.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09199.1; -; Genomic_DNA.
DR PIR; S38122; S38122.
DR RefSeq; NP_012974.1; NM_001179838.1.
DR PDB; 2AYU; X-ray; 3.00 A; A=1-417.
DR PDB; 2Z2R; X-ray; 3.20 A; A/B=74-365.
DR PDB; 5G2E; X-ray; 6.70 A; A/B/E/F/I/J/M/N/Q/R/U/V=74-372.
DR PDBsum; 2AYU; -.
DR PDBsum; 2Z2R; -.
DR PDBsum; 5G2E; -.
DR AlphaFoldDB; P25293; -.
DR SMR; P25293; -.
DR BioGRID; 34179; 477.
DR ComplexPortal; CPX-1712; Gin4 serine/threonine kinase complex.
DR DIP; DIP-1380N; -.
DR IntAct; P25293; 91.
DR MINT; P25293; -.
DR STRING; 4932.YKR048C; -.
DR iPTMnet; P25293; -.
DR MaxQB; P25293; -.
DR PaxDb; P25293; -.
DR PRIDE; P25293; -.
DR EnsemblFungi; YKR048C_mRNA; YKR048C; YKR048C.
DR GeneID; 853922; -.
DR KEGG; sce:YKR048C; -.
DR SGD; S000001756; NAP1.
DR VEuPathDB; FungiDB:YKR048C; -.
DR eggNOG; KOG1507; Eukaryota.
DR GeneTree; ENSGT00940000167738; -.
DR HOGENOM; CLU_038841_1_0_1; -.
DR InParanoid; P25293; -.
DR OMA; NSAYNDE; -.
DR BioCyc; YEAST:G3O-32018-MON; -.
DR EvolutionaryTrace; P25293; -.
DR PRO; PR:P25293; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P25293; protein.
DR GO; GO:0032153; C:cell division site; IDA:SGD.
DR GO; GO:0032174; C:cellular bud neck septin collar; IDA:SGD.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:1990317; C:Gin4 complex; IPI:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0030332; F:cyclin binding; IPI:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008047; F:enzyme activator activity; IDA:SGD.
DR GO; GO:0042393; F:histone binding; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0051082; F:unfolded protein binding; IDA:SGD.
DR GO; GO:0007117; P:budding cell bud growth; IMP:SGD.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; IMP:SGD.
DR GO; GO:0006334; P:nucleosome assembly; IDA:SGD.
DR GO; GO:0006337; P:nucleosome disassembly; IDA:SGD.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IDA:SGD.
DR GO; GO:2000617; P:positive regulation of histone H3-K9 acetylation; IMP:CACAO.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IMP:SGD.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IDA:ComplexPortal.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IDA:SGD.
DR GO; GO:0098841; P:protein localization to cell division site after cytokinesis; IMP:SGD.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IGI:SGD.
DR GO; GO:0000921; P:septin ring assembly; IC:ComplexPortal.
DR GO; GO:0000920; P:septum digestion after cytokinesis; IC:ComplexPortal.
DR InterPro; IPR037231; NAP-like_sf.
DR InterPro; IPR002164; NAP_family.
DR PANTHER; PTHR11875; PTHR11875; 1.
DR Pfam; PF00956; NAP; 1.
DR SUPFAM; SSF143113; SSF143113; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..417
FT /note="Nucleosome assembly protein"
FT /id="PRO_0000185659"
FT DNA_BIND 330..356
FT /note="H-T-H motif"
FT /evidence="ECO:0000255"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..362
FT /note="Interaction with NBA1"
FT /evidence="ECO:0000269|PubMed:18086883"
FT REGION 364..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..400
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 20
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 24
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 53
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18086883,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18086883"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18086883"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18086883,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 159
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:18086883"
FT MOD_RES 177
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:18086883,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 397
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:18086883"
FT CROSSLNK 50
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 99
FT /note="L->S: Predominantly cytoplasmic; when associated
FT with A-159, A-177 and S-397."
FT /evidence="ECO:0000269|PubMed:18086883"
FT MUTAGEN 159
FT /note="S->A: Significant reduction in phosphorylation; when
FT associated with A-397. Complete inhibition of
FT phosphorylation; when associated with A-177 and A-397.
FT Leads to a prolonged S phase and a shortened passage
FT through G1; when associated with A-177 and A-397.
FT Predominantly cytoplasmic; when associated with S-99, A-177
FT and A-397."
FT /evidence="ECO:0000269|PubMed:18086883"
FT MUTAGEN 159
FT /note="S->D: Leads to a prolonged S phase and a shortened
FT passage through G1; when associated with A-177 and A-397."
FT /evidence="ECO:0000269|PubMed:18086883"
FT MUTAGEN 177
FT /note="S->A: Significant reduction in phosphorylation; when
FT associated with A-397. Complete inhibition of
FT phosphorylation; when associated with A-159 and A-397.
FT Leads to a prolonged S phase and a shortened passage
FT through G1; when associated with A-159 and A-397.
FT Predominantly cytoplasmic; when associated with S-99, A-159
FT and A-397."
FT /evidence="ECO:0000269|PubMed:18086883"
FT MUTAGEN 177
FT /note="S->D: Leads to a prolonged S phase and a shortened
FT passage through G1; when associated with A-159 and A-397."
FT /evidence="ECO:0000269|PubMed:18086883"
FT MUTAGEN 397
FT /note="S->A: Significant reduction in phosphorylation; when
FT associated with either A-159 or A-177. Complete inhibition
FT of phosphorylation; when associated with A-159 and A-177.
FT Leads to a prolonged S phase and a shortened passage
FT through G1; when associated with A-159 and A-177.
FT Predominantly cytoplasmic; when associated with S-99; A-159
FT and A-177."
FT /evidence="ECO:0000269|PubMed:18086883"
FT MUTAGEN 397
FT /note="S->D: Leads to a prolonged S phase and a shortened
FT passage through G1; when associated with A-159 and A-177."
FT /evidence="ECO:0000269|PubMed:18086883"
FT CONFLICT 2
FT /note="S -> T (in Ref. 1; AAA34811)"
FT /evidence="ECO:0000305"
FT CONFLICT 103..104
FT /note="QS -> LC (in Ref. 1; AAA34811)"
FT /evidence="ECO:0000305"
FT CONFLICT 137..138
FT /note="RI -> TM (in Ref. 1; AAA34811)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="E -> D (in Ref. 1; AAA34811)"
FT /evidence="ECO:0000305"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:2AYU"
FT HELIX 77..87
FT /evidence="ECO:0007829|PDB:2AYU"
FT HELIX 90..140
FT /evidence="ECO:0007829|PDB:2AYU"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:2AYU"
FT HELIX 147..159
FT /evidence="ECO:0007829|PDB:2AYU"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:2AYU"
FT HELIX 188..194
FT /evidence="ECO:0007829|PDB:2AYU"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:2AYU"
FT HELIX 205..208
FT /evidence="ECO:0007829|PDB:2AYU"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:2AYU"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:2AYU"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:2AYU"
FT STRAND 228..235
FT /evidence="ECO:0007829|PDB:2AYU"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:2AYU"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:2AYU"
FT STRAND 246..257
FT /evidence="ECO:0007829|PDB:2AYU"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:2AYU"
FT STRAND 265..271
FT /evidence="ECO:0007829|PDB:2AYU"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:2AYU"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:2AYU"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:2Z2R"
FT STRAND 304..308
FT /evidence="ECO:0007829|PDB:2AYU"
FT HELIX 312..316
FT /evidence="ECO:0007829|PDB:2AYU"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:2AYU"
FT HELIX 332..350
FT /evidence="ECO:0007829|PDB:2AYU"
FT TURN 351..355
FT /evidence="ECO:0007829|PDB:2AYU"
FT HELIX 356..361
FT /evidence="ECO:0007829|PDB:2AYU"
FT HELIX 363..369
FT /evidence="ECO:0007829|PDB:2AYU"
SQ SEQUENCE 417 AA; 47885 MW; C0F97FBA1B9EEA83 CRC64;
MSDPIRTKPK SSMQIDNAPT PHNTPASVLN PSYLKNGNPV RAQAQEQDDK IGTINEEDIL
ANQPLLLQSI QDRLGSLVGQ DSGYVGGLPK NVKEKLLSLK TLQSELFEVE KEFQVEMFEL
ENKFLQKYKP IWEQRSRIIS GQEQPKPEQI AKGQEIVESL NETELLVDEE EKAQNDSEEE
QVKGIPSFWL TALENLPIVC DTITDRDAEV LEYLQDIGLE YLTDGRPGFK LLFRFDSSAN
PFFTNDILCK TYFYQKELGY SGDFIYDHAE GCEISWKDNA HNVTVDLEMR KQRNKTTKQV
RTIEKITPIE SFFNFFDPPK IQNEDQDEEL EEDLEERLAL DYSIGEQLKD KLIPRAVDWF
TGAALEFEFE EDEEEADEDE DEEEDDDHGL EDDDGESAEE QDDFAGRPEQ APECKQS
