NBA1_YEAST
ID NBA1_YEAST Reviewed; 501 AA.
AC Q08229; D6W1Z7;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Protein NBA1;
DE AltName: Full=NAP1 and bud neck-associated protein 1;
GN Name=NBA1; OrderedLocusNames=YOL070C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [2]
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 [3]
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 [4]
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 [5]
RP PHOSPHORYLATION BY CDC28.
RX PubMed=14574415; DOI=10.1038/nature02062;
RA Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D., Shah K.,
RA Shokat K.M., Morgan D.O.;
RT "Targets of the cyclin-dependent kinase Cdk1.";
RL Nature 425:859-864(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND COPURIFICATION WITH RIBOSOMES.
RX PubMed=16702403; DOI=10.1101/gad.1422006;
RA Fleischer T.C., Weaver C.M., McAfee K.J., Jennings J.L., Link A.J.;
RT "Systematic identification and functional screens of uncharacterized
RT proteins associated with eukaryotic ribosomal complexes.";
RL Genes Dev. 20:1294-1307(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH NAP1, SUBCELLULAR
RP LOCATION, AND REGION.
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138; SER-208 AND THR-403, AND
RP IDENTIFICATION BY 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).
CC -!- SUBUNIT: Interacts with NAP1 (via the central domain consisting of
CC amino acids 143 to 362). Copurifies with ribosomes.
CC {ECO:0000269|PubMed:18086883}.
CC -!- INTERACTION:
CC Q08229; Q99299: AIM44; NbExp=5; IntAct=EBI-36841, EBI-29423;
CC Q08229; P29366: BEM1; NbExp=6; IntAct=EBI-36841, EBI-3508;
CC Q08229; P38041: BOI1; NbExp=3; IntAct=EBI-36841, EBI-3719;
CC Q08229; P11433: CDC24; NbExp=6; IntAct=EBI-36841, EBI-4220;
CC Q08229; P53939: NIS1; NbExp=3; IntAct=EBI-36841, EBI-28760;
CC Q08229; P32793: YSC84; NbExp=2; IntAct=EBI-36841, EBI-24460;
CC -!- SUBCELLULAR LOCATION: Bud neck {ECO:0000269|PubMed:18086883}. Cytoplasm
CC {ECO:0000269|PubMed:14562095}. Note=Assembles at the inner surface of
CC the cell membrane. Localizes to the septin cortex prior to bud
CC emergence and to actin cap in unbudded cells.
CC {ECO:0000269|PubMed:18086883}.
CC -!- PTM: Phosphorylated by CDC28. {ECO:0000269|PubMed:14574415}.
CC -!- MISCELLANEOUS: Present with 6490 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z74812; CAA99080.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10713.1; -; Genomic_DNA.
DR PIR; S66763; S66763.
DR RefSeq; NP_014571.1; NM_001183325.1.
DR AlphaFoldDB; Q08229; -.
DR BioGRID; 34331; 132.
DR DIP; DIP-1680N; -.
DR IntAct; Q08229; 16.
DR MINT; Q08229; -.
DR STRING; 4932.YOL070C; -.
DR iPTMnet; Q08229; -.
DR MaxQB; Q08229; -.
DR PaxDb; Q08229; -.
DR PRIDE; Q08229; -.
DR TopDownProteomics; Q08229; -.
DR EnsemblFungi; YOL070C_mRNA; YOL070C; YOL070C.
DR GeneID; 854084; -.
DR KEGG; sce:YOL070C; -.
DR SGD; S000005431; NBA1.
DR VEuPathDB; FungiDB:YOL070C; -.
DR eggNOG; ENOG502R6DJ; Eukaryota.
DR HOGENOM; CLU_544174_0_0_1; -.
DR InParanoid; Q08229; -.
DR OMA; TTRTMIT; -.
DR BioCyc; YEAST:G3O-33475-MON; -.
DR PRO; PR:Q08229; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08229; protein.
DR GO; GO:0032153; C:cell division site; IDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0032174; C:cellular bud neck septin collar; IDA:SGD.
DR GO; GO:0032177; C:cellular bud neck split septin rings; IDA:SGD.
DR GO; GO:0005621; C:cellular bud scar; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0007120; P:axial cellular bud site selection; IMP:SGD.
DR GO; GO:0045184; P:establishment of protein localization; IMP:SGD.
DR GO; GO:2001107; P:negative regulation of Rho guanyl-nucleotide exchange factor activity; IGI:SGD.
DR GO; GO:1901900; P:regulation of protein localization to cell division site; IMP:SGD.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..501
FT /note="Protein NBA1"
FT /id="PRO_0000235925"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..501
FT /note="Necessary for the normal cellular distribution and
FT bud neck targeting"
FT REGION 338..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 403
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 501 AA; 55923 MW; 8128246D00B9C03D CRC64;
MSEEREENGI SRATLNTQRL SAMIDSLNNE KDDRLFPSPT TTRTMITEEK ADQSDVFKPP
SRLLRSPAGD VSLPPGDNRS SMISNYSGII QEGVEVSYVV KNRQQTQERR TSKDSNSLYS
LKEPVSKNEL PSLPMLPSEA TLTKHLSDNQ STKSNTNADE IVIKPVTNAK PVGRFNSNTS
KKVEGRGSLK LLSSPLRQEK VMRSSIGSGN LASESGSSTY NTKFHQSIQE QLEEEEEGNV
SDKLSIVSSV IPELYTTTNE APKAINPIRS ETNDYNPTIP PRSKDRPRSR LFIEEGDGEG
DLLTEEILPT PVQPGGHYKN SSQISTVSEQ KSESYYSAAT SMPPEEETYL TRPLPSTPNE
DSRVTSNLKR DDTLKAIHDR ANHTSTSTNK QDDDMYEDII EETPKKTKLK KDTKKKLNKK
KSVKELRSFD IDTLNQLLSV TKGTLIGSEF AQLGMKIEEK RALERLVDSL SRLTADMVLD
PDRYEEGLKR LDKATKALEG F
