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BBP1_YEAST
ID   BBP1_YEAST              Reviewed;         385 AA.
AC   Q12365; D6W3B6;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=Spindle pole component BBP1;
DE   AltName: Full=BFR1-binding protein 1;
GN   Name=BBP1; OrderedLocusNames=YPL255W; ORFNames=P0745;
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=ATCC 204508 / S288c;
RA   Xue Z., Shan X., Melese T.;
RL   Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [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, SUBCELLULAR LOCATION, AND INTERACTION WITH KAR1; MPS2 AND SPC29.
RX   PubMed=10654940; DOI=10.1093/emboj/19.3.421;
RA   Schramm C., Elliott S., Shevchenko A., Schiebel E.;
RT   "The Bbp1p-Mps2p complex connects the SPB to the nuclear envelope and is
RT   essential for SPB duplication.";
RL   EMBO J. 19:421-433(2000).
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   DOMAIN, SUBCELLULAR LOCATION, SUBUNIT, FUNCTION, AND INTERACTION WITH CDC5.
RX   PubMed=14767068; DOI=10.1091/mbc.e03-07-0461;
RA   Park C.J., Song S., Giddings T.H. Jr., Ro H.S., Sakchaisri K., Park J.E.,
RA   Seong Y.S., Winey M., Lee K.S.;
RT   "Requirement for Bbp1p in the proper mitotic functions of Cdc5p in
RT   Saccharomyces cerevisiae.";
RL   Mol. Biol. Cell 15:1711-1723(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, 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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, 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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-73, 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: Component of the spindle pole body (SPB) required for
CC       insertion of the nascent SPB into the nuclear envelope and for the
CC       proper execution of spindle pole body (SPB) duplication. Connects the
CC       central plaque of the SPB with the half-bridge. Required for proper
CC       localization of CDC5 at the SPB and for proper M-phase progression.
CC       {ECO:0000269|PubMed:10654940, ECO:0000269|PubMed:14767068}.
CC   -!- SUBUNIT: Homodimer. Interacts with KAR1, MPS2 and SPC29.
CC       {ECO:0000269|PubMed:10654940, ECO:0000269|PubMed:14767068}.
CC   -!- INTERACTION:
CC       Q12365; P53159: MPS2; NbExp=6; IntAct=EBI-3448, EBI-23834;
CC       Q12365; P33419: SPC29; NbExp=3; IntAct=EBI-3448, EBI-12041;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, spindle pole body {ECO:0000269|PubMed:10654940,
CC       ECO:0000269|PubMed:14767068}. Note=Associates with the periphary of the
CC       central plaque.
CC   -!- DOMAIN: The C-ter coiled-coil domain is sufficient for localization and
CC       homodimerization. {ECO:0000269|PubMed:14767068}.
CC   -!- MISCELLANEOUS: Present with 922 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the BBP1 family. {ECO:0000305}.
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DR   EMBL; X92658; CAA63347.1; -; Genomic_DNA.
DR   EMBL; Z73610; CAA97980.1; -; Genomic_DNA.
DR   EMBL; Z73611; CAA97981.1; -; Genomic_DNA.
DR   EMBL; AY693019; AAT93038.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11182.1; -; Genomic_DNA.
DR   PIR; S61566; S61566.
DR   RefSeq; NP_015068.1; NM_001184069.1.
DR   AlphaFoldDB; Q12365; -.
DR   BioGRID; 35908; 53.
DR   ComplexPortal; CPX-1287; MPS2-BBP1 spindle pole body anchor complex.
DR   DIP; DIP-4418N; -.
DR   IntAct; Q12365; 16.
DR   MINT; Q12365; -.
DR   STRING; 4932.YPL255W; -.
DR   iPTMnet; Q12365; -.
DR   MaxQB; Q12365; -.
DR   PaxDb; Q12365; -.
DR   PRIDE; Q12365; -.
DR   EnsemblFungi; YPL255W_mRNA; YPL255W; YPL255W.
DR   GeneID; 855820; -.
DR   KEGG; sce:YPL255W; -.
DR   SGD; S000006176; BBP1.
DR   VEuPathDB; FungiDB:YPL255W; -.
DR   eggNOG; ENOG502RYZ2; Eukaryota.
DR   HOGENOM; CLU_711875_0_0_1; -.
DR   InParanoid; Q12365; -.
DR   OMA; AQDDTNY; -.
DR   BioCyc; YEAST:G3O-34140-MON; -.
DR   PRO; PR:Q12365; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; Q12365; protein.
DR   GO; GO:0005823; C:central plaque of spindle pole body; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR   GO; GO:0106084; C:mitotic nuclear membrane microtubule tethering complex; IPI:ComplexPortal.
DR   GO; GO:0005635; C:nuclear envelope; IDA:ComplexPortal.
DR   GO; GO:0005816; C:spindle pole body; IC:ComplexPortal.
DR   GO; GO:0005198; F:structural molecule activity; IDA:SGD.
DR   GO; GO:1990608; P:mitotic spindle pole body localization; IDA:ComplexPortal.
DR   GO; GO:0071988; P:protein localization to spindle pole body; IMP:SGD.
DR   GO; GO:0030474; P:spindle pole body duplication; IMP:SGD.
DR   InterPro; IPR029330; Bbp1_C.
DR   InterPro; IPR029328; Bbp1_N.
DR   Pfam; PF15272; BBP1_C; 1.
DR   Pfam; PF15271; BBP1_N; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome.
FT   CHAIN           1..385
FT                   /note="Spindle pole component BBP1"
FT                   /id="PRO_0000064840"
FT   REGION          34..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          229..355
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        34..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..76
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         29
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         73
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         115
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
SQ   SEQUENCE   385 AA;  45384 MW;  3A1A827E7664E4E0 CRC64;
     MNQEDNTGGG GIFGLFKWTK DALFGTDISP SMKYKDQEER RDRSRYAQDD TNFSMKFGND
     SNRRSTNLSR SNSWSGLDST LHRKYELLPE YNENGFNSIV NGDHHSKERI RSLRSPAPIV
     PREPLRNEPT DTFGHRLHTK RRTINELSNS QIPFIPPQED DPLLSKLFNK DGVNEVRRSP
     YKLSVKDIPG KFPSPLTKRD EIDNYYVRDE DACHKNREYK KAYFDLFAQM DLNSRDLEDL
     CEDVREQREQ FHRNEQTYKQ AYEEMRAELV NELKKSKTLF ENYYSLGQKY KSLKKVLDQT
     ISHEAELATS RERLYQEEDL KNFEIQTLKQ RLSDLELKYT NLQIEKDMQR DNYESEIHDL
     LLQLSLRNNE RKDTSAGSNI FSTGQ
 
 
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