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Protein

Bud site selection protein 4

Gene

BUD4

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

Required for establishment of the axial budding pattern in haploid cells. Cooperates with other bud site selection proteins to recognize a spatial landmark during mitosis and they subsequently become a landmark for downstream polarity establishment factors that coordinate axial budding and cytokinesis. Involved in the septin organization at the bud neck.2 Publications

GO - Molecular functioni

  • GTP binding Source: SGD

GO - Biological processi

  • axial cellular bud site selection Source: SGD
  • protein localization to bud neck Source: SGD
  • septin ring organization Source: SGD
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division

Enzyme and pathway databases

BioCyciYEAST:G3O-31719-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Bud site selection protein 4
Gene namesi
Name:BUD4
Ordered Locus Names:YJR092W
ORF Names:J1905
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJR092W.
SGDiS000003852. BUD4.

Subcellular locationi

GO - Cellular componenti

  • cellular bud neck contractile ring Source: SGD
  • cellular bud scar Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14471447Bud site selection protein 4PRO_0000065017Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei10 – 101PhosphoserineCombined sources
Modified residuei78 – 781PhosphoserineCombined sources
Modified residuei81 – 811PhosphoserineCombined sources
Modified residuei91 – 911PhosphoserineCombined sources
Modified residuei96 – 961PhosphoserineCombined sources
Modified residuei167 – 1671PhosphoserineCombined sources
Modified residuei365 – 3651PhosphothreonineCombined sources
Modified residuei367 – 3671PhosphoserineCombined sources
Modified residuei511 – 5111PhosphoserineCombined sources
Modified residuei616 – 6161PhosphoserineCombined sources
Modified residuei805 – 8051PhosphoserineCombined sources
Modified residuei811 – 8111PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated by CDC28.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP47136.
PeptideAtlasiP47136.

PTM databases

iPTMnetiP47136.

Expressioni

Inductioni

Cell cycle-dependent with low levels at START and a peak in mitosis (at protein level).1 Publication

Interactioni

Subunit structurei

Interacts with AXL1, AXL2, IQG1 and SEC3.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AXL2P389282EBI-3848,EBI-3397
CDC10P253422EBI-3848,EBI-4174
IQG1Q122804EBI-3848,EBI-35351

Protein-protein interaction databases

BioGridi33846. 52 interactions.
DIPiDIP-4971N.
IntActiP47136. 13 interactions.
MINTiMINT-522781.

Structurei

3D structure databases

ProteinModelPortaliP47136.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1302 – 1413112PHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni768 – 879112Interaction with IQG1Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi181 – 1899Asp/Glu-rich (acidic)

Sequence similaritiesi

Contains 1 PH domain.PROSITE-ProRule annotation

Phylogenomic databases

InParanoidiP47136.
OMAiEWDYLFA.
OrthoDBiEOG7N63VZ.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PfamiPF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P47136-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHDAESTVDS LLKEIDNEME QTKSNITQNG SEDTPHNWKL PLQEIGDDTM
60 70 80 90 100
EMLVKHNTRS NATENSRGRS PSKMSTISNE SLNLGLLRVN SELEESPAAV
110 120 130 140 150
HQERIKNSVA NGALGHANSP KVLNNLKNMA QDIDKLARDE EKPVKLSSSP
160 170 180 190 200
LKFTLKSTQP LLSYPESPIH RSSIEIETNY DDEDEEEEDA YTCLTQSPQI
210 220 230 240 250
LHSPSRIPIT NAVSINKLNL DFTLNPNESD KSLVSDTSVD STGRELDTKT
260 270 280 290 300
IPELPFCMSS TPEMTPVDEK CNLPSKLLNT SNNSHSDSRS PTASVEDLNI
310 320 330 340 350
STNLPGADSS QNNPVTTDAD ALIENDVVRD LQQNMEHIDD AFDEKKVLDE
360 370 380 390 400
GCSNEPVTFL GENDTRSIVY SNKGTNANVQ EFSQEDSLAH SEPKFKDLNA
410 420 430 440 450
TSDDVWNEDK ETDANISTST KSEESYIADY KVTRQEDWDT KKLHQESEHA
460 470 480 490 500
NEQPAIIPQK DSSEETFTEL NNESEFQRNF KDGEEYRIVQ HEESLYGQRT
510 520 530 540 550
KSPEENIING SEIGVDHGEA AEVNEPLAKT SAEEHDLSSS CEDQSVSEAR
560 570 580 590 600
NKDRIEEKEV ETKDENIETE KDESEYHKVE ENEEPEHVPL LPPLPRWEEI
610 620 630 640 650
QFNEPFIDEN DTSNDSIDLT RSMKPSDYIS IWHIQEEEIK SNSPESIANS
660 670 680 690 700
QFSQQSSITT ASTVDSKKDN GSTSFKFKPR IVSRSRIYNP KSRVSSLNYY
710 720 730 740 750
DNEDYILSNS EWNALDPMRR NTLISKRIQD NIRTQKGHAP LIRPSIMKLN
760 770 780 790 800
GEDSGFQNHF LEVEQPQEHE NIPLSTHLSE QDITTNVGLD EQKLPTNTQD
810 820 830 840 850
EAEISIREIE SAGDITFNRG DLLSLSFDEE LGQDFANFLD ALDHDSTSFN
860 870 880 890 900
HGPDDSSSFQ RDSSKKSFNS LWESSYELKP PPSIRKQPIA PDVLQKLLES
910 920 930 940 950
DTKDDADLEK IREERITEPR TGLGIGMLKT PVKDVSIALA ASIKGYEASF
960 970 980 990 1000
SDTDSRPEGM NNSDAITLNM FDDFEEDKMT PSTPVRSISP IKRHVSSPFK
1010 1020 1030 1040 1050
VVKAGNKQEN NEINIKAEEE IEPMTQQETD GLKQDIPPLL AQTKDNVEAK
1060 1070 1080 1090 1100
EETITQLEEP QDVEQEFPDM GTLYLSIKAI STLALYGTKS HRATYAIVFD
1110 1120 1130 1140 1150
NGENVVQTPW ESLPYDGNIR INKEFELPID FKGKAETSSA SSERDSYKKC
1160 1170 1180 1190 1200
VITLKCKYEK PRHELVEIVD KVPVGKSFFG KTKYKFEKKY VQKKPKQDEW
1210 1220 1230 1240 1250
DYLFAQDGSF ARCEIEINEE FLKNVAFNTS HMHYNMINKW SRIADKIHGS
1260 1270 1280 1290 1300
KRLYELPRKA PHKVASLDVE ACFLERTSAF EQFPKQFSLV NKIVSKYKLQ
1310 1320 1330 1340 1350
QNIYKEGYLL QDGGDLKGKI ENRFFKLHGS QLSGYHEISR KAKIDINLLK
1360 1370 1380 1390 1400
VTKVLRNEDI QADNGGQRNF TDWVLFNECF QLVFDDGERI TFNAECSNEE
1410 1420 1430 1440
KSDWYNKLQE VVELNVFHQP WVKKYCEKLA EEEKTRTTGH NLKQDFN
Length:1,447
Mass (Da):164,486
Last modified:October 1, 1996 - v2
Checksum:i1D056B9FF1B7067B
GO

Sequence cautioni

The sequence CAA89620.1 differs from that shown. Reason: Frameshift at positions 290, 304 and 328. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti340 – 3401D → E in CAA89620 (PubMed:8641269).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41641 Genomic DNA. Translation: AAB17116.1.
Z49592 Genomic DNA. Translation: CAA89620.1. Frameshift.
Z49591 Genomic DNA. Translation: CAA89619.1.
BK006943 Genomic DNA. Translation: DAA08876.1.
PIRiS57113.
RefSeqiNP_012625.5. NM_001181749.3.

Genome annotation databases

EnsemblFungiiYJR092W; YJR092W; YJR092W.
GeneIDi853554.
KEGGisce:YJR092W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41641 Genomic DNA. Translation: AAB17116.1.
Z49592 Genomic DNA. Translation: CAA89620.1. Frameshift.
Z49591 Genomic DNA. Translation: CAA89619.1.
BK006943 Genomic DNA. Translation: DAA08876.1.
PIRiS57113.
RefSeqiNP_012625.5. NM_001181749.3.

3D structure databases

ProteinModelPortaliP47136.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33846. 52 interactions.
DIPiDIP-4971N.
IntActiP47136. 13 interactions.
MINTiMINT-522781.

PTM databases

iPTMnetiP47136.

Proteomic databases

MaxQBiP47136.
PeptideAtlasiP47136.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJR092W; YJR092W; YJR092W.
GeneIDi853554.
KEGGisce:YJR092W.

Organism-specific databases

EuPathDBiFungiDB:YJR092W.
SGDiS000003852. BUD4.

Phylogenomic databases

InParanoidiP47136.
OMAiEWDYLFA.
OrthoDBiEOG7N63VZ.

Enzyme and pathway databases

BioCyciYEAST:G3O-31719-MONOMER.

Miscellaneous databases

PROiP47136.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PfamiPF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The BUD4 protein of yeast, required for axial budding, is localized to the mother/BUD neck in a cell cycle-dependent manner."
    Sanders S.L., Herskowitz I.
    J. Cell Biol. 134:413-427(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
  2. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
    Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
    , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
    EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Subcellular localization of Axl1, the cell type-specific regulator of polarity."
    Lord M., Inose F., Hiroko T., Hata T., Fujita A., Chant J.
    Curr. Biol. 12:1347-1352(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AXL1.
  5. "Iqg1p links spatial and secretion landmarks to polarity and cytokinesis."
    Osman M.A., Konopka J.B., Cerione R.A.
    J. Cell Biol. 159:601-611(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IQG1 AND SEC3.
  6. "The roles of bud-site-selection proteins during haploid invasive growth in yeast."
    Cullen P.J., Sprague G.F. Jr.
    Mol. Biol. Cell 13:2990-3004(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. Cited for: PHOSPHORYLATION BY CDC28.
  10. "Interplay between septin organization, cell cycle and cell shape in yeast."
    Gladfelter A.S., Kozubowski L., Zyla T.R., Lew D.J.
    J. Cell Sci. 118:1617-1628(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Sequential and distinct roles of the cadherin domain-containing protein Axl2p in cell polarization in yeast cell cycle."
    Gao X.D., Sperber L.M., Kane S.A., Tong Z., Tong A.H., Boone C., Bi E.
    Mol. Biol. Cell 18:2542-2560(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AXL2.
  12. "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-10; SER-78; SER-81; SER-91 AND SER-96, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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 SER-167; THR-365; SER-367; SER-511; SER-616; SER-805 AND SER-811, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiBUD4_YEAST
AccessioniPrimary (citable) accession number: P47136
Secondary accession number(s): D6VWR0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1600 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 X
    Yeast (Saccharomyces cerevisiae) chromosome X: 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.