NBP2_YEAST
ID NBP2_YEAST Reviewed; 236 AA.
AC Q12163; D6VSE2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=NAP1-binding protein 2;
GN Name=NBP2; OrderedLocusNames=YDR162C;
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 (DEC-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14573466; DOI=10.1093/genetics/165.2.517;
RA Ohkuni K., Okuda A., Kikuchi A.;
RT "Yeast Nap1-binding protein Nbp2p is required for mitotic growth at high
RT temperatures and for cell wall integrity.";
RL Genetics 165:517-529(2003).
RN [6]
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 [7]
RP FUNCTION, AND INTERACTION WITH PTC1 AND PBS2.
RX PubMed=14685261; DOI=10.1038/sj.emboj.7600036;
RA Mapes J., Ota I.M.;
RT "Nbp2 targets the Ptc1-type 2C Ser/Thr phosphatase to the HOG MAPK
RT pathway.";
RL EMBO J. 23:302-311(2004).
RN [8]
RP FUNCTION.
RX PubMed=16977319; DOI=10.1038/sj.emboj.7601319;
RA Du Y., Walker L., Novick P., Ferro-Novick S.;
RT "Ptc1p regulates cortical ER inheritance via Slt2p.";
RL EMBO J. 25:4413-4422(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196, AND IDENTIFICATION BY
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102; SER-196 AND SER-235, AND
RP IDENTIFICATION BY 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-196, 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 -!- FUNCTION: Negatively regulates the high-osmolarity glycerol (HOG)
CC pathway through its negative regulation of the HOG1 kinase activity.
CC Mediates the binding between the PTC1 phosphatase and the PBS2 MAP/ERK
CC kinase (MEK). With PTC1, regulates endoplasmic reticulum inheritance
CC through the cell wall integrity (CWI) MAPK pathway by modulating the
CC MAPK, SLT2. {ECO:0000269|PubMed:14573466, ECO:0000269|PubMed:14685261,
CC ECO:0000269|PubMed:16977319}.
CC -!- SUBUNIT: Interacts with PBS2 and PTC1. {ECO:0000269|PubMed:14685261}.
CC -!- INTERACTION:
CC Q12163; P40563: AIM21; NbExp=4; IntAct=EBI-34713, EBI-25376;
CC Q12163; P48562: CLA4; NbExp=3; IntAct=EBI-34713, EBI-4750;
CC Q12163; P08018: PBS2; NbExp=3; IntAct=EBI-34713, EBI-12972;
CC Q12163; P35182: PTC1; NbExp=4; IntAct=EBI-34713, EBI-12784;
CC Q12163; Q03497: STE20; NbExp=6; IntAct=EBI-34713, EBI-18285;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14573466}.
CC -!- MISCELLANEOUS: Present with 521 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; D43693; BAA07790.1; -; Genomic_DNA.
DR EMBL; Z50046; CAA90382.1; -; Genomic_DNA.
DR EMBL; AY557678; AAS56004.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12002.1; -; Genomic_DNA.
DR PIR; S57986; S57986.
DR RefSeq; NP_010446.3; NM_001180469.3.
DR PDB; 1YN8; X-ray; 1.70 A; A/B/C/D/E/F=113-170.
DR PDB; 2LCS; NMR; -; A=110-172.
DR PDBsum; 1YN8; -.
DR PDBsum; 2LCS; -.
DR AlphaFoldDB; Q12163; -.
DR BMRB; Q12163; -.
DR SMR; Q12163; -.
DR BioGRID; 32213; 709.
DR DIP; DIP-1538N; -.
DR IntAct; Q12163; 12.
DR MINT; Q12163; -.
DR STRING; 4932.YDR162C; -.
DR iPTMnet; Q12163; -.
DR MaxQB; Q12163; -.
DR PaxDb; Q12163; -.
DR PRIDE; Q12163; -.
DR EnsemblFungi; YDR162C_mRNA; YDR162C; YDR162C.
DR GeneID; 851740; -.
DR KEGG; sce:YDR162C; -.
DR SGD; S000002569; NBP2.
DR VEuPathDB; FungiDB:YDR162C; -.
DR eggNOG; ENOG502RZ32; Eukaryota.
DR HOGENOM; CLU_069841_1_0_1; -.
DR InParanoid; Q12163; -.
DR OMA; PFYLTHM; -.
DR BioCyc; YEAST:G3O-29752-MON; -.
DR EvolutionaryTrace; Q12163; -.
DR PRO; PR:Q12163; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12163; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IMP:SGD.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IMP:SGD.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..236
FT /note="NAP1-binding protein 2"
FT /id="PRO_0000257822"
FT DOMAIN 110..171
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:1YN8"
FT STRAND 136..144
FT /evidence="ECO:0007829|PDB:1YN8"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:1YN8"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:1YN8"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:1YN8"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:1YN8"
SQ SEQUENCE 236 AA; 26571 MW; A7458854D5000EA6 CRC64;
MATMETTTQK DTNILKSGLK KTIGVLNEAV LQNGREVEAV QAGNSDTMED TETTTIGYIS
IKDYAYADSN PLHYGYFDGD NEEDEMVSDS SNGEDTYNKR QSITLPDDYI VNQRAVALYD
FEPENDNELR LAEGDIVFIS YKHGQGWLVA ENESGSKTGL VPEEFVSYIQ PEDGENEVEN
KARPFYLTHL ITQSVSPKNN IDNTNEDEYD DNDEWEDIDD VAEVEADMKT KLDISD
