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Protein

Centromere DNA-binding protein complex CBF3 subunit B

Gene

CEP3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a component of the centromere DNA-binding protein complex CBF3, which is essential for chromosome segregation and movement of centromeres along microtubules. CBF3 is required for the recruitment of other kinetochore complexes to CEN DNA. It plays a role in the attachment of chromosomes to the spindle and binds selectively to a highly conserved DNA sequence called CDEIII, found in centromers and in several promoters.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi14 – 42Zn(2)-C6 fungal-typePROSITE-ProRule annotationAdd BLAST29

GO - Molecular functioni

GO - Biological processi

  • mitotic spindle assembly checkpoint Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter by a nonfermentable carbon source Source: GO_Central
  • septin ring assembly Source: SGD
Complete GO annotation...

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-32858-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Centromere DNA-binding protein complex CBF3 subunit B
Short name:
Centromere protein 3
Gene namesi
Name:CEP3
Synonyms:CBF3, CBF3B, CSL1
Ordered Locus Names:YMR168C
ORF Names:YM8520.17C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YMR168C.
SGDiS000004778. CEP3.

Subcellular locationi

GO - Cellular componenti

  • CBF3 complex Source: SGD
  • condensed nuclear chromosome kinetochore Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001149411 – 608Centromere DNA-binding protein complex CBF3 subunit BAdd BLAST608

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei575PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP40969.
PRIDEiP40969.

PTM databases

iPTMnetiP40969.

Interactioni

Subunit structurei

Component of the CBF3 copmplex, which is formed of CBF3A/CBF2, CBF3B/CEP3, CBF3C/CTF13 and CBF3D.

Binary interactionsi

WithEntry#Exp.IntActNotes
CTF13P352032EBI-4077,EBI-4085

Protein-protein interaction databases

BioGridi35346. 78 interactors.
DIPiDIP-5956N.
IntActiP40969. 10 interactors.
MINTiMINT-416717.

Structurei

Secondary structure

1608
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi58 – 71Combined sources14
Turni72 – 74Combined sources3
Helixi75 – 79Combined sources5
Helixi85 – 87Combined sources3
Turni92 – 95Combined sources4
Helixi96 – 105Combined sources10
Helixi108 – 121Combined sources14
Helixi123 – 130Combined sources8
Helixi134 – 146Combined sources13
Helixi154 – 173Combined sources20
Helixi176 – 182Combined sources7
Helixi186 – 192Combined sources7
Helixi200 – 202Combined sources3
Helixi204 – 222Combined sources19
Turni223 – 227Combined sources5
Helixi231 – 240Combined sources10
Turni241 – 244Combined sources4
Helixi245 – 248Combined sources4
Helixi250 – 265Combined sources16
Helixi280 – 302Combined sources23
Helixi313 – 315Combined sources3
Helixi338 – 356Combined sources19
Turni357 – 360Combined sources4
Helixi367 – 385Combined sources19
Helixi394 – 422Combined sources29
Helixi427 – 443Combined sources17
Helixi444 – 446Combined sources3
Turni447 – 449Combined sources3
Helixi451 – 455Combined sources5
Helixi457 – 476Combined sources20
Helixi480 – 495Combined sources16
Helixi498 – 500Combined sources3
Helixi501 – 522Combined sources22
Beta strandi530 – 534Combined sources5
Helixi536 – 550Combined sources15
Helixi555 – 562Combined sources8
Helixi589 – 600Combined sources12
Helixi603 – 606Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QUQX-ray2.80A47-608[»]
2VEQX-ray2.49A48-608[»]
ProteinModelPortaliP40969.
SMRiP40969.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40969.

Family & Domainsi

Sequence similaritiesi

Contains 1 Zn(2)-C6 fungal-type DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000111345.
InParanoidiP40969.
KOiK11575.
OMAiHAAYLED.
OrthoDBiEOG092C1C0B.

Family and domain databases

Gene3Di4.10.240.10. 1 hit.
InterProiIPR031760. Cep3_C.
IPR001138. Zn2-C6_fun-type_DNA-bd.
[Graphical view]
PfamiPF16846. Cep3. 1 hit.
PF00172. Zn_clus. 1 hit.
[Graphical view]
SMARTiSM00066. GAL4. 1 hit.
[Graphical view]
SUPFAMiSSF57701. SSF57701. 1 hit.
PROSITEiPS00463. ZN2_CY6_FUNGAL_1. 1 hit.
PS50048. ZN2_CY6_FUNGAL_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40969-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFNRTTQLKS KHPCSVCTRR KVKCDRMIPC GNCRKRGQDS ECMKSTKLIT
60 70 80 90 100
ASSSKEYLPD LLLFWQNYEY WITNIGLYKT KQRDLTRTPA NLDTDTEECM
110 120 130 140 150
FWMNYLQKDQ SFQLMNFAME NLGALYFGSI GDISELYLRV EQYWDRRADK
160 170 180 190 200
NHSVDGKYWD ALIWSVFTMC IYYMPVEKLA EIFSVYPLHE YLGSNKRLNW
210 220 230 240 250
EDGMQLVMCQ NFARCSLFQL KQCDFMAHPD IRLVQAYLIL ATTTFPYDEP
260 270 280 290 300
LLANSLLTQC IHTFKNFHVD DFRPLLNDDP VESIAKVTLG RIFYRLCGCD
310 320 330 340 350
YLQSGPRKPI ALHTEVSSLL QHAAYLQDLP NVDVYREENS TEVLYWKIIS
360 370 380 390 400
LDRDLDQYLN KSSKPPLKTL DAIRRELDIF QYKVDSLEED FRSNNSRFQK
410 420 430 440 450
FIALFQISTV SWKLFKMYLI YYDTADSLLK VIHYSKVIIS LIVNNFHAKS
460 470 480 490 500
EFFNRHPMVM QTITRVVSFI SFYQIFVESA AVKQLLVDLT ELTANLPTIF
510 520 530 540 550
GSKLDKLVYL TERLSKLKLL WDKVQLLDSG DSFYHPVFKI LQNDIKIIEL
560 570 580 590 600
KNDEMFSLIK GLGSLVPLNK LRQESLLEEE DENNTEPSDF RTIVEEFQSE

YNISDILS
Length:608
Mass (Da):71,358
Last modified:February 1, 1995 - v1
Checksum:i2E24A0508080A09B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81396 Genomic DNA. Translation: CAA57159.1.
U12339 Genomic DNA. Translation: AAA57074.1.
Z49705 Genomic DNA. Translation: CAA89804.1.
BK006946 Genomic DNA. Translation: DAA10064.1.
PIRiS51790.
RefSeqiNP_013891.1. NM_001182672.1.

Genome annotation databases

EnsemblFungiiYMR168C; YMR168C; YMR168C.
GeneIDi855204.
KEGGisce:YMR168C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81396 Genomic DNA. Translation: CAA57159.1.
U12339 Genomic DNA. Translation: AAA57074.1.
Z49705 Genomic DNA. Translation: CAA89804.1.
BK006946 Genomic DNA. Translation: DAA10064.1.
PIRiS51790.
RefSeqiNP_013891.1. NM_001182672.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QUQX-ray2.80A47-608[»]
2VEQX-ray2.49A48-608[»]
ProteinModelPortaliP40969.
SMRiP40969.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35346. 78 interactors.
DIPiDIP-5956N.
IntActiP40969. 10 interactors.
MINTiMINT-416717.

PTM databases

iPTMnetiP40969.

Proteomic databases

MaxQBiP40969.
PRIDEiP40969.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR168C; YMR168C; YMR168C.
GeneIDi855204.
KEGGisce:YMR168C.

Organism-specific databases

EuPathDBiFungiDB:YMR168C.
SGDiS000004778. CEP3.

Phylogenomic databases

HOGENOMiHOG000111345.
InParanoidiP40969.
KOiK11575.
OMAiHAAYLED.
OrthoDBiEOG092C1C0B.

Enzyme and pathway databases

BioCyciYEAST:G3O-32858-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP40969.
PROiP40969.

Family and domain databases

Gene3Di4.10.240.10. 1 hit.
InterProiIPR031760. Cep3_C.
IPR001138. Zn2-C6_fun-type_DNA-bd.
[Graphical view]
PfamiPF16846. Cep3. 1 hit.
PF00172. Zn_clus. 1 hit.
[Graphical view]
SMARTiSM00066. GAL4. 1 hit.
[Graphical view]
SUPFAMiSSF57701. SSF57701. 1 hit.
PROSITEiPS00463. ZN2_CY6_FUNGAL_1. 1 hit.
PS50048. ZN2_CY6_FUNGAL_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCBF3B_YEAST
AccessioniPrimary (citable) accession number: P40969
Secondary accession number(s): D6VZZ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 2, 2016
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1900 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.