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Protein

Bud site selection protein 14

Gene

BUD14

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

Important for bud site selection. Seems to be a regulatory subunit of the BUD14-GLC7 type-I phosphatase complex. The BUD14-GLC7 complex is necessary to regulate microtubule dynamics at the cortex and may function as a specific activator of the dynein complex.2 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein phosphatase type 1 regulator activity Source: SGD

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • cytoskeleton organization Source: SGD
  • negative regulation of actin filament polymerization Source: SGD
  • regulation of cell shape during vegetative growth phase Source: SGD
  • regulation of cytokinesis Source: SGD
  • regulation of formin-nucleated actin cable assembly Source: SGD
  • regulation of protein localization Source: SGD
  • regulation of transcription, DNA-templated Source: SGD
  • regulation of vesicle-mediated transport Source: SGD
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division

Enzyme and pathway databases

BioCyciYEAST:G3O-28873-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Bud site selection protein 14
Gene namesi
Name:BUD14
Ordered Locus Names:YAR014C
ORF Names:FUN2
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:YAR014C.
SGDiS000000069. BUD14.

Subcellular locationi

GO - Cellular componenti

  • cellular bud neck Source: SGD
  • cellular bud tip Source: SGD
  • incipient cellular bud site Source: SGD
  • Kelch-containing formin regulatory complex Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 707706Bud site selection protein 14PRO_0000065012Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei159 – 1591PhosphotyrosineCombined sources
Modified residuei160 – 1601PhosphoserineCombined sources
Modified residuei162 – 1621PhosphoserineCombined sources
Modified residuei177 – 1771PhosphothreonineCombined sources
Modified residuei212 – 2121PhosphoserineCombined sources
Modified residuei222 – 2221PhosphoserineCombined sources
Modified residuei376 – 3761PhosphoserineCombined sources
Modified residuei378 – 3781PhosphoserineCombined sources
Modified residuei401 – 4011PhosphoserineCombined sources
Modified residuei507 – 5071PhosphoserineCombined sources
Modified residuei655 – 6551PhosphoserineCombined sources
Modified residuei658 – 6581PhosphoserineCombined sources
Modified residuei670 – 6701PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP27637.

PTM databases

iPTMnetiP27637.

Interactioni

Subunit structurei

Interacts with GLC7.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-20747,EBI-20747
BEM2P399603EBI-20747,EBI-3517
GLC7P325987EBI-20747,EBI-13715
KIN2P131863EBI-20747,EBI-9723

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi31798. 169 interactions.
DIPiDIP-1756N.
IntActiP27637. 98 interactions.
MINTiMINT-403701.

Structurei

3D structure databases

ProteinModelPortaliP27637.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini259 – 32062SH3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3 domain

Phylogenomic databases

HOGENOMiHOG000095277.
InParanoidiP27637.
OMAiNCWKNEN.
OrthoDBiEOG7MSMZD.

Family and domain databases

InterProiIPR001452. SH3_domain.
[Graphical view]
PfamiPF00018. SH3_1. 1 hit.
[Graphical view]
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P27637-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNKEEHVDE TSASGVKEVS SIAARHDNGY APSLITSTSG MDSFQSHALL
60 70 80 90 100
NDPTLIEDYS DIINNRPTSG SKLTLGNEDS ESMGGSVVVT PTSNKSSPFN
110 120 130 140 150
SKLNILSNAA EKGHDVLRNR DDDKELEEEN VEKHMHSNSK RDQRHYKENS
160 170 180 190 200
SELPDSYDYS DSEFEDNLER RLQEIETDSV DSADKDEVHF SVNNTMNPDV
210 220 230 240 250
DDFSDGLKYA ISEDEDEEEN YSDDDDFDRK FQDSGFQGEK DDLEEENDDY
260 270 280 290 300
QPLSPPRELD PDKLYALYAF NGHDSSHCQL GQDEPCILLN DQDAYWWLVK
310 320 330 340 350
RITDGKIGFA PAEILETFPE RLARLNCWKN ENMSSQSVAS SDSKDDSISS
360 370 380 390 400
GNKNQSDAES IIPTPALNGY GKGNKSVSFN DVVGYADRFI DDAIEDTSLD
410 420 430 440 450
SNDDGGEGNG QSYDDDVDND KETKVTHRDE YTEAKLNFGK FQDDDTSDVV
460 470 480 490 500
SDVSFSTSLN TPLNVKKVRR QDNKNESEPK TSSSKDREDD YNANRYVGQE
510 520 530 540 550
KSEPVDSDYD TDLKKVFEAP RMPFANGMAK SDSQNSLSTI GEFSPSSSEW
560 570 580 590 600
TNESPSTPIV EESSSIPSSR AIKDISQYIH AKSKIEETTN VENTEGQIQA
610 620 630 640 650
SLGSSGGMAN QTDAEQPKEE LEKHHSTPEE EKQSTLSLHS SSEEDFYMDE
660 670 680 690 700
QRAVSSASIN SSLSGSRALS NTNMSDPASK PNSLVQHLYA PVFDRMDVLM

KQLDEIIRK
Length:709
Mass (Da):78,981
Last modified:July 27, 2011 - v4
Checksum:iF123511A4C592EB4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti439 – 4391G → A no nucleotide entry (PubMed:7941740).Curated
Sequence conflicti439 – 4391G → A in AAC04962 (PubMed:7731988).Curated
Sequence conflicti573 – 59523KDISQ…VENTE → RTFTYIMQNRKLRDNKRGKH R no nucleotide entry (PubMed:7941740).CuratedAdd
BLAST
Sequence conflicti573 – 59523KDISQ…VENTE → RTFTYIMQNRKLRDNKRGKH R in AAC04962 (PubMed:7731988).CuratedAdd
BLAST
Sequence conflicti609 – 6091A → P no nucleotide entry (PubMed:7941740).Curated
Sequence conflicti609 – 6091A → P in AAC04962 (PubMed:7731988).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L22015 Genomic DNA. Translation: AAC04962.2.
M67445 Genomic DNA. Translation: AAA34397.1.
BK006935 Genomic DNA. Translation: DAA06993.2.
PIRiS40904.
RefSeqiNP_009408.3. NM_001178215.2.

Genome annotation databases

EnsemblFungiiYAR014C; YAR014C; YAR014C.
GeneIDi851271.
KEGGisce:YAR014C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L22015 Genomic DNA. Translation: AAC04962.2.
M67445 Genomic DNA. Translation: AAA34397.1.
BK006935 Genomic DNA. Translation: DAA06993.2.
PIRiS40904.
RefSeqiNP_009408.3. NM_001178215.2.

3D structure databases

ProteinModelPortaliP27637.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31798. 169 interactions.
DIPiDIP-1756N.
IntActiP27637. 98 interactions.
MINTiMINT-403701.

PTM databases

iPTMnetiP27637.

Proteomic databases

MaxQBiP27637.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYAR014C; YAR014C; YAR014C.
GeneIDi851271.
KEGGisce:YAR014C.

Organism-specific databases

EuPathDBiFungiDB:YAR014C.
SGDiS000000069. BUD14.

Phylogenomic databases

HOGENOMiHOG000095277.
InParanoidiP27637.
OMAiNCWKNEN.
OrthoDBiEOG7MSMZD.

Enzyme and pathway databases

BioCyciYEAST:G3O-28873-MONOMER.

Miscellaneous databases

PROiP27637.

Family and domain databases

InterProiIPR001452. SH3_domain.
[Graphical view]
PfamiPF00018. SH3_1. 1 hit.
[Graphical view]
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 42 kbp SPO7-CENI-CDC15 region."
    Clark M.W., Keng T., Storms R.K., Zhong W.-W., Fortin N., Zeng B., Delaney S., Ouellette B.F.F., Barton A.B., Kaback D.B., Bussey H.
    Yeast 10:535-541(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204511 / S288c / AB972.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Fisk D., Cherry J.M.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO C-TERMINUS.
  4. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 439; 573-595 AND 609.
    Strain: ATCC 204508 / S288c.
  5. "A directed DNA sequencing strategy based upon Tn3 transposon mutagenesis: application to the ADE1 locus on Saccharomyces cerevisiae chromosome I."
    Davies C.J., Hutchison C.A. III
    Nucleic Acids Res. 19:5731-5738(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-142.
  6. "A genomic study of the bipolar bud site selection pattern in Saccharomyces cerevisiae."
    Ni L., Snyder M.
    Mol. Biol. Cell 12:2147-2170(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "The Glc7p-interacting protein Bud14p attenuates polarized growth, pheromone response, and filamentous growth in Saccharomyces cerevisiae."
    Cullen P.J., Sprague G.F. Jr.
    Eukaryot. Cell 1:884-894(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GLC7.
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "The Bud14p-Glc7p complex functions as a cortical regulator of dynein in budding yeast."
    Knaus M., Cameroni E., Pedruzzi I., Tatchell K., De Virgilio C., Peter M.
    EMBO J. 24:3000-3011(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GLC7, FUNCTION OF THE BUD14-GLC7 COMPLEX.
  10. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212; SER-222 AND SER-658, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  11. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; SER-376 AND SER-378, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-159; SER-160; SER-162; THR-177; SER-212; SER-222; SER-376; SER-378; SER-401; SER-507; SER-655; SER-658 AND SER-670, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiBUD14_YEAST
AccessioniPrimary (citable) accession number: P27637
Secondary accession number(s): D6VPM3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 147 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 538 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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