BSP1_YEAST
ID BSP1_YEAST Reviewed; 576 AA.
AC Q06604; D6W4H2;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Protein BSP1;
DE AltName: Full=Binding of synaptojanin polyphosphoinositide phosphatase domain protein 1;
GN Name=BSP1; OrderedLocusNames=YPR171W;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 INTERACTION WITH CAP1; RVS167 AND SLA1, AND SUBCELLULAR LOCATION.
RX PubMed=11489916; DOI=10.1083/jcb.200104057;
RA Drees B.L., Sundin B.A., Brazeau E., Caviston J.P., Chen G.-C., Guo W.,
RA Kozminski K.G., Lau M.W., Moskow J.J., Tong A., Schenkman L.R.,
RA McKenzie A. III, Brennwald P.J., Longtine M., Bi E., Chan C., Novick P.,
RA Boone C., Pringle J.R., Davis T.N., Fields S., Drubin D.G.;
RT "A protein interaction map for cell polarity development.";
RL J. Cell Biol. 154:549-571(2001).
RN [4]
RP FUNCTION, INTERACTION WITH INP52 AND INP53, AND SUBCELLULAR LOCATION.
RX PubMed=12606027; DOI=10.1016/s0014-5793(03)00067-x;
RA Wicky S., Frischmuth S., Singer-Krueger B.;
RT "Bsp1p/Ypr171p is an adapter that directly links some synaptojanin family
RT members to the cortical actin cytoskeleton in yeast.";
RL FEBS Lett. 537:35-41(2003).
RN [5]
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 [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 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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-309 AND SER-320, AND
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-88 AND SER-185, 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: Cortical patch protein involved in endocytosis. May serve as
CC an adapter to link INP52 and INP53 to the cortical actin cytoskeleton.
CC {ECO:0000269|PubMed:12606027}.
CC -!- SUBUNIT: Interacts with CAP1, RVS167, SLA1, INP52 and INP53. The INP52
CC and INP53 C-terminal Sac1 domains are required for the binding with
CC BSP1. {ECO:0000269|PubMed:11489916, ECO:0000269|PubMed:12606027}.
CC -!- INTERACTION:
CC Q06604; P15891: ABP1; NbExp=2; IntAct=EBI-37047, EBI-2036;
CC Q06604; P50942: INP52; NbExp=4; IntAct=EBI-37047, EBI-28834;
CC Q06604; P43603: LSB3; NbExp=7; IntAct=EBI-37047, EBI-22980;
CC Q06604; P39743: RVS167; NbExp=5; IntAct=EBI-37047, EBI-14500;
CC Q06604; P0CF34: SDC25; NbExp=2; IntAct=EBI-37047, EBI-6315249;
CC Q06604; P32790: SLA1; NbExp=5; IntAct=EBI-37047, EBI-17313;
CC Q06604; P32793: YSC84; NbExp=6; IntAct=EBI-37047, EBI-24460;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC Cytoplasm, cytoskeleton, actin patch. Note=Peripheral membrane protein
CC in a PtdIns(4)P and PtdIns(4,5)P2 manner.
CC -!- PTM: Phosphorylated by CDC28. {ECO:0000269|PubMed:14574415}.
CC -!- MISCELLANEOUS: Present with 704 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U25842; AAB68105.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11588.1; -; Genomic_DNA.
DR PIR; S59829; S59829.
DR RefSeq; NP_015497.1; NM_001184268.1.
DR AlphaFoldDB; Q06604; -.
DR BioGRID; 36344; 119.
DR DIP; DIP-2756N; -.
DR IntAct; Q06604; 22.
DR MINT; Q06604; -.
DR STRING; 4932.YPR171W; -.
DR iPTMnet; Q06604; -.
DR MaxQB; Q06604; -.
DR PaxDb; Q06604; -.
DR PRIDE; Q06604; -.
DR EnsemblFungi; YPR171W_mRNA; YPR171W; YPR171W.
DR GeneID; 856301; -.
DR KEGG; sce:YPR171W; -.
DR SGD; S000006375; BSP1.
DR VEuPathDB; FungiDB:YPR171W; -.
DR eggNOG; ENOG502S4ZF; Eukaryota.
DR HOGENOM; CLU_518734_0_0_1; -.
DR InParanoid; Q06604; -.
DR OMA; HIDYLDS; -.
DR BioCyc; YEAST:G3O-34298-MON; -.
DR PRO; PR:Q06604; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q06604; protein.
DR GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0016020; C:membrane; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:SGD.
DR GO; GO:0051666; P:actin cortical patch localization; IMP:SGD.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Cytoskeleton; Endocytosis; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..576
FT /note="Protein BSP1"
FT /id="PRO_0000228137"
FT REGION 24..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..560
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..576
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
SQ SEQUENCE 576 AA; 64666 MW; 7A33A775FCA1F3CD CRC64;
MTKYERDPEL VNFLSKVEDL NSKRYSNIPS SKPAGEALSP VRSHNSGEYR RADMMTGKNV
EGCDNLAYRS AYNYEMTFSP KKTHYSLSEL NLERITPRPD LEGSASQKEK KFLISEEDYL
LLQKLKASQT YNDSNADKNL PSFEKGPRMP SRGRPRPREK EIITIQYDFE LPGRADIPSS
SSSSSPPPLP TRRDHIKITD GNEEKPLLPT RPNKAEVTES PSSRSIKPDA VVPERVKPAP
PVSRSTKPAS FLSSLEDNKL TKAKSYNSEM ETPKTTVKSS HIDYLDSIQL KPTTLSPTMK
NKPKPTPPSP PAKRIPRSES FIKSMLNSNL TTTSKPSLPE KPQKLRNANL AAHKTKPSIP
PKKVELNIVL PELRPVETSP TKQNFENSID LPKLRSSNRN IKKEEEDSIP EAIKGIQNLK
KTKQQKPAIP QKKSFLTNNS KNTTLKNGDD INKLNDEIEA LSLRNNLKKR PPTAPQRKIS
LPEALRKVEL MKKSKTEPVL ESSNELSINA KLDAIIASRN LRASNTLPEL SGVNTNIATS
DKYTTSRDET VKETKPLVHP NKNRTRGPRR KLPTRV
