CBF3A_YEAST
ID CBF3A_YEAST Reviewed; 956 AA.
AC P32504; D6VUS0; E9P954;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Centromere DNA-binding protein complex CBF3 subunit A;
DE AltName: Full=Centromere-binding factor 2;
DE AltName: Full=Chromosome transmission fidelity protein 14;
DE AltName: Full=Kinetochore protein CTF14;
GN Name=CBF2; Synonyms=CBF3A, CEP2, CTF14, NDC10; OrderedLocusNames=YGR140W;
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], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8486733; DOI=10.1083/jcb.121.3.513;
RA Jiang W., Lechner J., Carbon J.;
RT "Isolation and characterization of a gene (CBF2) specifying a protein
RT component of the budding yeast kinetochore.";
RL J. Cell Biol. 121:513-519(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8486732; DOI=10.1083/jcb.121.3.503;
RA Goh P.-Y., Kilmartin J.V.;
RT "NDC10: a gene involved in chromosome segregation in Saccharomyces
RT cerevisiae.";
RL J. Cell Biol. 121:503-512(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 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 [6]
RP INTERACTION WITH CTF19.
RX PubMed=10323865; DOI=10.1101/gad.13.9.1140;
RA Ortiz J., Stemmann O., Rank S., Lechner J.;
RT "A putative protein complex consisting of Ctf19, Mcm21, and Okp1 represents
RT a missing link in the budding yeast kinetochore.";
RL Genes Dev. 13:1140-1155(1999).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=10427094; DOI=10.1083/jcb.146.2.415;
RA Zeng X., Kahana J.A., Silver P.A., Morphew M.K., McIntosh J.R., Fitch I.T.,
RA Carbon J., Saunders W.S.;
RT "Slk19p is a centromere protein that functions to stabilize mitotic
RT spindles.";
RL J. Cell Biol. 146:415-425(1999).
RN [8]
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 [9]
RP ASSEMBLY OF THE CBF3 COMPLEX, AND INTERACTION WITH CBF3D AND SGT1.
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-566, 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 TYR-706, 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 -!- 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. CBF2 strongly interacts with BIR1.
CC Interacts with the central kinetochore protein CTF19.
CC {ECO:0000269|PubMed:10323865, ECO:0000269|PubMed:15090617}.
CC -!- INTERACTION:
CC P32504; P35203: CTF13; NbExp=5; IntAct=EBI-4069, EBI-4085;
CC P32504; P53267: DAM1; NbExp=2; IntAct=EBI-4069, EBI-23268;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10427094}.
CC Chromosome, centromere {ECO:0000269|PubMed:10427094}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, spindle pole body
CC {ECO:0000269|PubMed:10427094}. Note=Spindle midzone during anaphase B.
CC -!- MISCELLANEOUS: Present with 1350 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z21627; CAA79753.1; -; Genomic_DNA.
DR EMBL; X69300; CAA49158.1; -; Genomic_DNA.
DR EMBL; Z72925; CAA97153.1; -; Genomic_DNA.
DR EMBL; AY723816; AAU09733.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08231.1; -; Genomic_DNA.
DR PIR; S64449; S64449.
DR RefSeq; NP_011656.3; NM_001181269.3.
DR PDB; 4ACO; X-ray; 1.89 A; A=1-956.
DR PDB; 6GSA; EM; 4.20 A; E=2-553.
DR PDB; 6GYP; EM; 3.60 A; E=1-956.
DR PDB; 6GYS; EM; 4.40 A; E/L=1-956.
DR PDB; 6GYU; EM; 3.00 A; E=1-956.
DR PDBsum; 4ACO; -.
DR PDBsum; 6GSA; -.
DR PDBsum; 6GYP; -.
DR PDBsum; 6GYS; -.
DR PDBsum; 6GYU; -.
DR AlphaFoldDB; P32504; -.
DR SMR; P32504; -.
DR BioGRID; 33386; 349.
DR ComplexPortal; CPX-1898; CBF3 complex.
DR DIP; DIP-5955N; -.
DR IntAct; P32504; 39.
DR MINT; P32504; -.
DR STRING; 4932.YGR140W; -.
DR CarbonylDB; P32504; -.
DR iPTMnet; P32504; -.
DR MaxQB; P32504; -.
DR PaxDb; P32504; -.
DR PRIDE; P32504; -.
DR EnsemblFungi; YGR140W_mRNA; YGR140W; YGR140W.
DR GeneID; 853041; -.
DR KEGG; sce:YGR140W; -.
DR SGD; S000003372; CBF2.
DR VEuPathDB; FungiDB:YGR140W; -.
DR eggNOG; ENOG502QVZD; Eukaryota.
DR HOGENOM; CLU_320281_0_0_1; -.
DR InParanoid; P32504; -.
DR OMA; LEWFTPN; -.
DR BioCyc; YEAST:G3O-30844-MON; -.
DR PRO; PR:P32504; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P32504; protein.
DR GO; GO:0031518; C:CBF3 complex; IDA:SGD.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000776; C:kinetochore; IDA:ComplexPortal.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005819; C:spindle; IDA:SGD.
DR GO; GO:0051233; C:spindle midzone; IDA:SGD.
DR GO; GO:0005816; C:spindle pole body; IEA:UniProtKB-SubCell.
DR GO; GO:0019237; F:centromeric DNA binding; IDA:SGD.
DR GO; GO:0008301; F:DNA binding, bending; IDA:SGD.
DR GO; GO:0007059; P:chromosome segregation; IMP:SGD.
DR GO; GO:0051382; P:kinetochore assembly; IDA:ComplexPortal.
DR GO; GO:0000022; P:mitotic spindle elongation; IMP:SGD.
DR GO; GO:0000921; P:septin ring assembly; IMP:SGD.
DR DisProt; DP02033; -.
DR Gene3D; 1.10.150.130; -; 1.
DR Gene3D; 1.10.443.20; -; 1.
DR InterPro; IPR010998; Integrase_recombinase_N.
DR InterPro; IPR038279; Ndc10_dom2_sf.
DR InterPro; IPR031872; NDC10_II.
DR InterPro; IPR022210; TF_GCR1-like.
DR Pfam; PF12550; GCR1_C; 1.
DR Pfam; PF16787; NDC10_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Centromere; Chromosome; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..956
FT /note="Centromere DNA-binding protein complex CBF3 subunit
FT A"
FT /id="PRO_0000089369"
FT REGION 544..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..667
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..703
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 706
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 418
FT /note="T -> A (in Ref. 5; AAU09733)"
FT /evidence="ECO:0000305"
FT CONFLICT 774
FT /note="K -> Q (in Ref. 1; CAA79753)"
FT /evidence="ECO:0000305"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:6GYU"
FT HELIX 45..58
FT /evidence="ECO:0007829|PDB:4ACO"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:6GYU"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:6GYU"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:4ACO"
FT HELIX 82..91
FT /evidence="ECO:0007829|PDB:4ACO"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:4ACO"
FT HELIX 108..138
FT /evidence="ECO:0007829|PDB:4ACO"
FT HELIX 148..167
FT /evidence="ECO:0007829|PDB:4ACO"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:6GYU"
FT HELIX 177..181
FT /evidence="ECO:0007829|PDB:6GYU"
FT HELIX 184..193
FT /evidence="ECO:0007829|PDB:4ACO"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:4ACO"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:4ACO"
FT HELIX 208..224
FT /evidence="ECO:0007829|PDB:4ACO"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:4ACO"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:4ACO"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:4ACO"
FT STRAND 249..255
FT /evidence="ECO:0007829|PDB:4ACO"
FT STRAND 266..272
FT /evidence="ECO:0007829|PDB:4ACO"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:4ACO"
FT HELIX 282..295
FT /evidence="ECO:0007829|PDB:4ACO"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:4ACO"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:4ACO"
FT TURN 314..317
FT /evidence="ECO:0007829|PDB:4ACO"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:4ACO"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:4ACO"
FT HELIX 335..348
FT /evidence="ECO:0007829|PDB:4ACO"
FT HELIX 356..359
FT /evidence="ECO:0007829|PDB:4ACO"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:4ACO"
FT HELIX 371..377
FT /evidence="ECO:0007829|PDB:4ACO"
FT HELIX 380..383
FT /evidence="ECO:0007829|PDB:4ACO"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:4ACO"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:4ACO"
FT HELIX 401..407
FT /evidence="ECO:0007829|PDB:4ACO"
FT TURN 412..414
FT /evidence="ECO:0007829|PDB:6GYU"
FT HELIX 429..432
FT /evidence="ECO:0007829|PDB:4ACO"
FT HELIX 438..444
FT /evidence="ECO:0007829|PDB:4ACO"
FT HELIX 447..449
FT /evidence="ECO:0007829|PDB:4ACO"
FT HELIX 452..478
FT /evidence="ECO:0007829|PDB:4ACO"
FT HELIX 483..486
FT /evidence="ECO:0007829|PDB:4ACO"
FT HELIX 488..491
FT /evidence="ECO:0007829|PDB:4ACO"
FT HELIX 493..503
FT /evidence="ECO:0007829|PDB:4ACO"
FT HELIX 504..506
FT /evidence="ECO:0007829|PDB:4ACO"
FT TURN 518..520
FT /evidence="ECO:0007829|PDB:4ACO"
FT HELIX 521..524
FT /evidence="ECO:0007829|PDB:4ACO"
FT HELIX 527..531
FT /evidence="ECO:0007829|PDB:4ACO"
SQ SEQUENCE 956 AA; 111917 MW; C93FB7E033931E3D CRC64;
MRSSILFLLK LMKIMDVQQQ QEAMSSEDRF QELVDSLKPR TAHQYKTYYT KYIQWCQLNQ
IIPTPEDNSV NSVPYKDLPI SAELIHWFLL DTLITDDKPG EKREETEDLD EEEENSFKIA
TLKKIIGSLN FLSKLCKVHE NPNANIDTKY LESVTKLHTH WIDSQKAITT NETNNTNTQV
LCPPLLKVSL NLWNPETNHL SEKFFKTCSE KLRFLVDFQL RSYLNLSFEE RSKIRFGSLK
LGKRDRDAII YHKVTHSAEK KDTPGHHQLL ALLPQDCPFI CPQTTLAAYL YLRFYGIPSV
SKGDGFPNLN ADENGSLLQD IPILRGKSLT TYPREETFSN YYTTVFRYCH LPYKRREYFN
KCNLVYPTWD EDTFRTFFNE ENHGNWLEQP EAFAFPDKIP FDFKKIMNFK SPYTSYSTNA
KKDPFPPPKD LLVQIFPEID EYKRHDYEGL SQNSRDFLDL MEVLRERFLS NLPWIYKFFP
NHDIFQDPIF GNSDFQSYFN DKTIHSKGSP ILSFDILPGF NKIYKNKTNF YSLLIERPSQ
LTFASSHNPD THPTQKQESE GPLQMSQLDT TQLNELLKQQ SFEYVQFQTL SNFQILLSVF
NKIFEKLEMK KSSRGYILHQ LNLFKITLDE RIKKSKIDDA DKFIRDNQPI KKEENIVNED
GPNTSRRTKR PKQIRLLSIA DSSDESSTED SNVFKKDGES IEDGAYGENE DENDSEMQEQ
LKSMINELIN SKISTFLRDQ MDQFELKINA LLDKILEEKV TRIIEQKLGS HTGKFSTLKR
PQLYMTEEHN VGFDMEVPKK LRTSGKYAET VKDNDDHQAM STTASPSPEQ DQEAKSYTDE
QEFMLDKSID SIEGIILEWF TPNAKYANQC VHSMNKSGNK SWRANCEALY KERKSIVEFY
IYLVNHESLD RYKAVDICEK LRDQNEGSFS RLAKFLRKWR HDHQNSFDGL LVYLSN
