CBF3B_YEAST
ID CBF3B_YEAST Reviewed; 608 AA.
AC P40969; D6VZZ0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Centromere DNA-binding protein complex CBF3 subunit B;
DE Short=Centromere protein 3;
GN Name=CEP3; Synonyms=CBF3, CBF3B, CSL1; OrderedLocusNames=YMR168C;
GN ORFNames=YM8520.17C;
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=AC 502;
RX PubMed=7957085; DOI=10.1002/j.1460-2075.1994.tb06851.x;
RA Lechner J.;
RT "A zinc finger protein, essential for chromosome segregation, constitutes a
RT putative DNA binding subunit of the Saccharomyces cerevisiae kinetochore
RT complex, Cbf3.";
RL EMBO J. 13:5203-5211(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7876302; DOI=10.1083/jcb.128.5.749;
RA Strunnikov A.V., Kingsbury J., Koshland D.;
RT "CEP3 encodes a centromere protein of Saccharomyces cerevisiae.";
RL J. Cell Biol. 128:749-760(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [4]
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 [5]
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 [6]
RP ASSEMBLY OF THE CBF3 COMPLEX.
RX PubMed=15090617; DOI=10.1091/mbc.e03-12-0887;
RA Rodrigo-Brenni M.C., Thomas S., Bouck D.C., Kaplan K.B.;
RT "Sgt1p and Skp1p modulate the assembly and turnover of CBF3 complexes
RT required for proper kinetochore function.";
RL Mol. Biol. Cell 15:3366-3378(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, 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).
CC -!- FUNCTION: Acts as a component of the centromere DNA-binding protein
CC complex CBF3, which is essential for chromosome segregation and
CC movement of centromeres along microtubules. CBF3 is required for the
CC recruitment of other kinetochore complexes to CEN DNA. It plays a role
CC in the attachment of chromosomes to the spindle and binds selectively
CC to a highly conserved DNA sequence called CDEIII, found in centromers
CC and in several promoters.
CC -!- SUBUNIT: Component of the CBF3 copmplex, which is formed of CBF3A/CBF2,
CC CBF3B/CEP3, CBF3C/CTF13 and CBF3D.
CC -!- INTERACTION:
CC P40969; P40969: CEP3; NbExp=2; IntAct=EBI-4077, EBI-4077;
CC P40969; P35203: CTF13; NbExp=2; IntAct=EBI-4077, EBI-4085;
CC P40969; P22216: RAD53; NbExp=2; IntAct=EBI-4077, EBI-17843;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome, centromere.
CC -!- MISCELLANEOUS: Present with 1900 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X81396; CAA57159.1; -; Genomic_DNA.
DR EMBL; U12339; AAA57074.1; -; Genomic_DNA.
DR EMBL; Z49705; CAA89804.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10064.1; -; Genomic_DNA.
DR PIR; S51790; S51790.
DR RefSeq; NP_013891.1; NM_001182672.1.
DR PDB; 2QUQ; X-ray; 2.80 A; A=47-608.
DR PDB; 2VEQ; X-ray; 2.49 A; A=48-608.
DR PDB; 6F07; EM; 3.60 A; A/B=1-608.
DR PDB; 6FE8; EM; 3.70 A; A/B=47-608.
DR PDB; 6GSA; EM; 4.20 A; A/B=47-608.
DR PDB; 6GYS; EM; 4.40 A; B/C/I/J=1-608.
DR PDB; 7K79; EM; 4.00 A; L/O=1-608.
DR PDB; 7K7G; EM; 4.20 A; M=1-48.
DR PDBsum; 2QUQ; -.
DR PDBsum; 2VEQ; -.
DR PDBsum; 6F07; -.
DR PDBsum; 6FE8; -.
DR PDBsum; 6GSA; -.
DR PDBsum; 6GYS; -.
DR PDBsum; 7K79; -.
DR PDBsum; 7K7G; -.
DR AlphaFoldDB; P40969; -.
DR SMR; P40969; -.
DR BioGRID; 35346; 603.
DR ComplexPortal; CPX-1898; CBF3 complex.
DR DIP; DIP-5956N; -.
DR IntAct; P40969; 11.
DR MINT; P40969; -.
DR STRING; 4932.YMR168C; -.
DR iPTMnet; P40969; -.
DR MaxQB; P40969; -.
DR PaxDb; P40969; -.
DR PRIDE; P40969; -.
DR EnsemblFungi; YMR168C_mRNA; YMR168C; YMR168C.
DR GeneID; 855204; -.
DR KEGG; sce:YMR168C; -.
DR SGD; S000004778; CEP3.
DR VEuPathDB; FungiDB:YMR168C; -.
DR eggNOG; ENOG502QVHC; Eukaryota.
DR HOGENOM; CLU_457054_0_0_1; -.
DR InParanoid; P40969; -.
DR OMA; WQSYEYW; -.
DR BioCyc; YEAST:G3O-32858-MON; -.
DR EvolutionaryTrace; P40969; -.
DR PRO; PR:P40969; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P40969; protein.
DR GO; GO:0031518; C:CBF3 complex; IDA:SGD.
DR GO; GO:0000776; C:kinetochore; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0019237; F:centromeric DNA binding; IDA:SGD.
DR GO; GO:0008301; F:DNA binding, bending; IDA:SGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051382; P:kinetochore assembly; IDA:ComplexPortal.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP:SGD.
DR GO; GO:0000921; P:septin ring assembly; IMP:SGD.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR031760; Cep3_C.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR Pfam; PF16846; Cep3; 1.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF57701; SSF57701; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Centromere; Chromosome; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..608
FT /note="Centromere DNA-binding protein complex CBF3 subunit
FT B"
FT /id="PRO_0000114941"
FT DNA_BIND 14..42
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT HELIX 58..71
FT /evidence="ECO:0007829|PDB:2VEQ"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:2VEQ"
FT HELIX 75..79
FT /evidence="ECO:0007829|PDB:2VEQ"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:2VEQ"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:2VEQ"
FT HELIX 96..105
FT /evidence="ECO:0007829|PDB:2VEQ"
FT HELIX 108..121
FT /evidence="ECO:0007829|PDB:2VEQ"
FT HELIX 123..130
FT /evidence="ECO:0007829|PDB:2VEQ"
FT HELIX 134..146
FT /evidence="ECO:0007829|PDB:2VEQ"
FT HELIX 154..173
FT /evidence="ECO:0007829|PDB:2VEQ"
FT HELIX 176..182
FT /evidence="ECO:0007829|PDB:2VEQ"
FT HELIX 186..192
FT /evidence="ECO:0007829|PDB:2VEQ"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:2VEQ"
FT HELIX 204..222
FT /evidence="ECO:0007829|PDB:2VEQ"
FT TURN 223..227
FT /evidence="ECO:0007829|PDB:2VEQ"
FT HELIX 231..240
FT /evidence="ECO:0007829|PDB:2VEQ"
FT TURN 241..244
FT /evidence="ECO:0007829|PDB:2VEQ"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:2VEQ"
FT HELIX 250..265
FT /evidence="ECO:0007829|PDB:2VEQ"
FT HELIX 280..302
FT /evidence="ECO:0007829|PDB:2VEQ"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:2QUQ"
FT HELIX 338..356
FT /evidence="ECO:0007829|PDB:2VEQ"
FT TURN 357..360
FT /evidence="ECO:0007829|PDB:2VEQ"
FT HELIX 367..385
FT /evidence="ECO:0007829|PDB:2VEQ"
FT HELIX 394..422
FT /evidence="ECO:0007829|PDB:2VEQ"
FT HELIX 427..443
FT /evidence="ECO:0007829|PDB:2VEQ"
FT HELIX 444..446
FT /evidence="ECO:0007829|PDB:2VEQ"
FT TURN 447..449
FT /evidence="ECO:0007829|PDB:2VEQ"
FT HELIX 451..455
FT /evidence="ECO:0007829|PDB:2VEQ"
FT HELIX 457..476
FT /evidence="ECO:0007829|PDB:2VEQ"
FT HELIX 480..495
FT /evidence="ECO:0007829|PDB:2VEQ"
FT HELIX 498..500
FT /evidence="ECO:0007829|PDB:2VEQ"
FT HELIX 501..522
FT /evidence="ECO:0007829|PDB:2VEQ"
FT STRAND 530..534
FT /evidence="ECO:0007829|PDB:2VEQ"
FT HELIX 536..550
FT /evidence="ECO:0007829|PDB:2VEQ"
FT HELIX 555..562
FT /evidence="ECO:0007829|PDB:2VEQ"
FT HELIX 589..600
FT /evidence="ECO:0007829|PDB:2VEQ"
FT HELIX 603..606
FT /evidence="ECO:0007829|PDB:2VEQ"
SQ SEQUENCE 608 AA; 71358 MW; 2E24A0508080A09B CRC64;
MFNRTTQLKS KHPCSVCTRR KVKCDRMIPC GNCRKRGQDS ECMKSTKLIT ASSSKEYLPD
LLLFWQNYEY WITNIGLYKT KQRDLTRTPA NLDTDTEECM FWMNYLQKDQ SFQLMNFAME
NLGALYFGSI GDISELYLRV EQYWDRRADK NHSVDGKYWD ALIWSVFTMC IYYMPVEKLA
EIFSVYPLHE YLGSNKRLNW EDGMQLVMCQ NFARCSLFQL KQCDFMAHPD IRLVQAYLIL
ATTTFPYDEP LLANSLLTQC IHTFKNFHVD DFRPLLNDDP VESIAKVTLG RIFYRLCGCD
YLQSGPRKPI ALHTEVSSLL QHAAYLQDLP NVDVYREENS TEVLYWKIIS LDRDLDQYLN
KSSKPPLKTL DAIRRELDIF QYKVDSLEED FRSNNSRFQK FIALFQISTV SWKLFKMYLI
YYDTADSLLK VIHYSKVIIS LIVNNFHAKS EFFNRHPMVM QTITRVVSFI SFYQIFVESA
AVKQLLVDLT ELTANLPTIF GSKLDKLVYL TERLSKLKLL WDKVQLLDSG DSFYHPVFKI
LQNDIKIIEL KNDEMFSLIK GLGSLVPLNK LRQESLLEEE DENNTEPSDF RTIVEEFQSE
YNISDILS
