NBP1_YEAST
ID NBP1_YEAST Reviewed; 319 AA.
AC P52919; D6VZ91;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=NAP1-binding protein;
GN Name=NBP1; OrderedLocusNames=YLR457C; ORFNames=L9122.6;
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].
RC STRAIN=SFY526;
RA Okuda A., Fujii-Nakata T., Kikuchi A.;
RL Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
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 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 INTERACTION WITH NDC1 AND MPS2.
RX PubMed=16436507; DOI=10.1091/mbc.e05-07-0668;
RA Araki Y., Lau C.K., Maekawa H., Jaspersen S.L., Giddings T.H. Jr.,
RA Schiebel E., Winey M.;
RT "The Saccharomyces cerevisiae spindle pole body (SPB) component Nbp1p is
RT required for SPB membrane insertion and interacts with the integral
RT membrane proteins Ndc1p and Mps2p.";
RL Mol. Biol. Cell 17:1959-1970(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260, 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).
CC -!- SUBUNIT: Interacts with NDC1 and MPS2. {ECO:0000269|PubMed:16436507}.
CC -!- INTERACTION:
CC P52919; P40069: KAP123; NbExp=6; IntAct=EBI-11886, EBI-9166;
CC P52919; P53159: MPS2; NbExp=2; IntAct=EBI-11886, EBI-23834;
CC -!- MISCELLANEOUS: Present with 339 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D43632; BAA07740.1; -; Genomic_DNA.
DR EMBL; U22383; AAB64721.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09757.1; -; Genomic_DNA.
DR PIR; S59416; S59416.
DR RefSeq; NP_013562.3; NM_001182345.3.
DR AlphaFoldDB; P52919; -.
DR SMR; P52919; -.
DR BioGRID; 31716; 94.
DR DIP; DIP-3852N; -.
DR IntAct; P52919; 15.
DR MINT; P52919; -.
DR STRING; 4932.YLR457C; -.
DR iPTMnet; P52919; -.
DR MaxQB; P52919; -.
DR PaxDb; P52919; -.
DR PRIDE; P52919; -.
DR EnsemblFungi; YLR457C_mRNA; YLR457C; YLR457C.
DR GeneID; 851180; -.
DR KEGG; sce:YLR457C; -.
DR SGD; S000004449; NBP1.
DR VEuPathDB; FungiDB:YLR457C; -.
DR eggNOG; ENOG502RYR8; Eukaryota.
DR GeneTree; ENSGT00940000176561; -.
DR HOGENOM; CLU_071874_1_0_1; -.
DR InParanoid; P52919; -.
DR OMA; ENISPAC; -.
DR BioCyc; YEAST:G3O-32510-MON; -.
DR PRO; PR:P52919; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P52919; protein.
DR GO; GO:0005823; C:central plaque of spindle pole body; IDA:SGD.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; IDA:SGD.
DR GO; GO:0005816; C:spindle pole body; IDA:SGD.
DR GO; GO:0008289; F:lipid binding; IDA:SGD.
DR GO; GO:0030474; P:spindle pole body duplication; IMP:SGD.
DR GO; GO:0070631; P:spindle pole body localization; IMP:SGD.
DR InterPro; IPR013743; NBP1_fun.
DR Pfam; PF08537; NBP1; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..319
FT /note="NAP1-binding protein"
FT /id="PRO_0000096745"
FT REGION 34..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..51
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 319 AA; 37354 MW; CFC1BE0F7295A495 CRC64;
MLKSVQGLWK DFFGIRDDGR KREYGSLDEV RKRSALRSRR KQMRPTGKSV LKRPRKVTDR
KTEEKIRTNR RKTPKRRLTK IFQTIRDVFS NDNENMSKMQ NVCGDMTRIL KKRSQGRPSY
MDTDTAKSRI LRSDAFKRKI SELKYNKQRI SELRSGSSDG SSGKDRNQSL YLDREILLQR
QIKKRDEKIK ALESKLQSLQ EALNYSNEKY RILEDLLDSS NIHPSYTKSR RTMSNLAREN
DEIKPLKIDL SPSPIRRTNS LFTSSPMKTY NRDGNIPEMQ PLQENISPAC PTPPYRSRET
EKEDETLSPI SVDFSSYLS
