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P25558

- BUD3_YEAST

UniProt

P25558 - BUD3_YEAST

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Protein
Bud site selection protein 3
Gene
BUD3, YCL014W, YCL012W, YCL013W, YCL12W, YCL13W, YCL14W
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Co-assembles with BUD4 at bud sites. BUD4 and BUD3 may cooperate to recognize a spatial landmark (the neck filaments) during mitosis and they subsequently become a landmark for establishing the axial budding pattern in G1.

GO - Molecular functioni

  1. Rho guanyl-nucleotide exchange factor activity Source: InterPro
  2. protein binding Source: IntAct

GO - Biological processi

  1. axial cellular bud site selection Source: SGD
Complete GO annotation...

Keywords - Biological processi

Cell cycle

Enzyme and pathway databases

BioCyciYEAST:G3O-29281-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Bud site selection protein 3
Gene namesi
Name:BUD3
Ordered Locus Names:YCL014W
ORF Names:YCL012W, YCL013W, YCL12W, YCL13W, YCL14W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome III

Organism-specific databases

CYGDiYCL014w.
SGDiS000000520. BUD3.

Subcellular locationi

GO - Cellular componenti

  1. cellular bud neck Source: SGD
  2. cellular bud neck contractile ring Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16361636Bud site selection protein 3
PRO_0000065016Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei766 – 7661Phosphoserine1 Publication
Modified residuei1045 – 10451Phosphothreonine1 Publication
Modified residuei1063 – 10631Phosphoserine2 Publications
Modified residuei1075 – 10751Phosphoserine3 Publications
Modified residuei1134 – 11341Phosphoserine2 Publications
Modified residuei1149 – 11491Phosphoserine1 Publication
Modified residuei1157 – 11571Phosphothreonine2 Publications
Modified residuei1160 – 11601Phosphoserine2 Publications
Modified residuei1228 – 12281Phosphoserine1 Publication
Modified residuei1254 – 12541Phosphoserine2 Publications
Modified residuei1257 – 12571Phosphoserine2 Publications
Modified residuei1390 – 13901Phosphoserine1 Publication
Modified residuei1412 – 14121Phosphoserine2 Publications
Modified residuei1429 – 14291Phosphothreonine1 Publication
Modified residuei1440 – 14401Phosphothreonine2 Publications
Modified residuei1443 – 14431Phosphoserine2 Publications
Modified residuei1501 – 15011Phosphoserine1 Publication
Modified residuei1549 – 15491Phosphoserine1 Publication
Modified residuei1589 – 15891Phosphoserine1 Publication
Modified residuei1614 – 16141Phosphoserine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP25558.
PaxDbiP25558.
PeptideAtlasiP25558.

Expressioni

Gene expression databases

GenevestigatoriP25558.

Interactioni

Subunit structurei

Interacts with AXL2.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
AXL2P389282EBI-3840,EBI-3397

Protein-protein interaction databases

BioGridi30969. 64 interactions.
DIPiDIP-4969N.
IntActiP25558. 7 interactions.
MINTiMINT-522762.

Structurei

3D structure databases

ProteinModelPortaliP25558.

Family & Domainsi

Sequence similaritiesi

Belongs to the BUD3 family.

Phylogenomic databases

eggNOGiNOG40287.
HOGENOMiHOG000000894.
OrthoDBiEOG72G1H3.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
InterProiIPR000219. DH-domain.
IPR021895. DUF3507.
[Graphical view]
PfamiPF12015. DUF3507. 1 hit.
[Graphical view]
SMARTiSM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.

Sequencei

Sequence statusi: Complete.

P25558-1 [UniParc]FASTAAdd to Basket

« Hide

MEKDLSSLYS EKKDKENDET LFNIKLSKSV VETTPLNGHS LFDDDKSLSD     50
WTDNVFTQSV FYHGSDDLIW GKFFVCVYKS PNSNKLNAII FDKLGTSCFE 100
SVDISSNSQY YPAIENLSPS DQESNVKKCI AVILLQRYPL LSPSDLSQIL 150
SNKSENCDYD PPYAGDLASS CQLITAVPPE DLGKRFFTSG LLQNRFVSST 200
LLDVIYENNE STIELNNRLV FHLGEQLEQL FNPVTEYSPE QTEYGYKAPE 250
DELPTESDDD LVKAICNELL QLQTNFTFNL VEFLQKFLIA LRVRVLNEEI 300
NGLSTTKLNR LFPPTIDEVT RINCIFLDSL KTAIPYGSLE VLKACSITIP 350
YFYKAYTRHE AATKNFSKDI KLFIRHFSNV IPEREVYTEM KIESIIKGPQ 400
EKLLKLKLII ERLWKSKKWR PKNQEMAKKC YNNIIDVIDS FGKLDSPLHS 450
YSTRVFTPSG KILTELAKCW PVELQYKWLK RRVVGVYDVV DLNDENKRNL 500
LVIFSDYVVF INILEAESYY TSDGSNRPLI SDILMNSLIN EVPLPSKIPK 550
LKVERHCYID EVLVSILDKS TLRFDRLKGK DSFSMVCKLS SAFISSSSVA 600
DLITKARILE KDTAFHLFKA SRSHFTLYST AHELCAYDSE KIKSKFALFL 650
NIPPSKEILE VNNLHLAFFA RFCSNDGRDN IVILDVLTKH DDKHIEVTSD 700
NIVFTIINQL AIEIPICFSS LNSSMAKDLL CVNENLIKNL EHQLEEVKHP 750
STDEHRAVNS KLSGASDFDA THEKKRSYGT ITTFRSYTSD LKDSPSGDNS 800
NVTKETKEIL PVKPTKKSSK KPREIQKKTK TNASKAEHIE KKKPNKGKGF 850
FGVLKNVFGS KSKSKPSPVQ RVPKKISQRH PKSPVKKPMT SEKKSSPKRA 900
VVSSPKIKKK STSFSTKESQ TAKSSLRAVE FKSDDLIGKP PDVGNGAHPQ 950
ENTRISSVVR DTKYVSYNPS QPVTENTSNE KNVEPKADQS TKQDNISNFA 1000
DVEVSASSYP EKLDAETDDQ IIGKATNSSS VHGNKELPDL AEVTTANRVS 1050
TTSAGDQRID TQSEFLRAAD VENLSDDDEH RQNESRVFND DLFGDFIPKH 1100
YRNKQENINS SSNLFPEGKV PQEKGVSNEN TNISLKTNED ASTLTQKLSP 1150
QASKVLTENS NELKDTNNEG KDAKDIKLGD DYSDKETAKE ITKPKNFVEG 1200
ITERKEIFPT IPRLAPPASK INFQRSPSYI ELFQGMRVVL DKHDAHYNWK 1250
RLASQVSLSE GLKVNTEEDA AIINKSQDDA KAERMTQISE VIEYEMQQPI 1300
PTYLPKAHLD DSGIEKSDDK FFEIEEELKE ELKGSKTGNE DVGNNNPSNS 1350
IPKIEKPPAF KVIRTSPVRI IGRTFEDTRK YENGSPSDIS FTYDTHNNDE 1400
PDKRLMELKF PSQDEIPDDR FYTPAEEPTA EFPVEELPNT PRSINVTTSN 1450
NKSTDDKLSS GNIDQKPTEL LDDLEFSSFN IAFGNTSMST DNMKISSDLS 1500
SNKTVLGNAQ KVQESPSGPL IYVLPQSSTK HEKEGFLRKK QKDEPIWVSP 1550
SKIDFADLSR RTKALTPERN TVPLKNNDSR KYKYTGEGSI GNMTNMLLTK 1600
DASYAYLKDF VALSDDEDED GKQNCAVGGP EKLKFY 1636
Length:1,636
Mass (Da):184,719
Last modified:November 1, 1995 - v2
Checksum:i9E4E46BA5C3A3F69
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U17580 Genomic DNA. Translation: AAA86315.1.
X59720 Genomic DNA. Translation: CAA42346.2.
BK006937 Genomic DNA. Translation: DAA07468.1.
PIRiS74285.
S74286.
RefSeqiNP_009914.2. NM_001178662.1.

Genome annotation databases

EnsemblFungiiYCL014W; YCL014W; YCL014W.
GeneIDi850345.
KEGGisce:YCL014W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U17580 Genomic DNA. Translation: AAA86315.1 .
X59720 Genomic DNA. Translation: CAA42346.2 .
BK006937 Genomic DNA. Translation: DAA07468.1 .
PIRi S74285.
S74286.
RefSeqi NP_009914.2. NM_001178662.1.

3D structure databases

ProteinModelPortali P25558.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 30969. 64 interactions.
DIPi DIP-4969N.
IntActi P25558. 7 interactions.
MINTi MINT-522762.

Proteomic databases

MaxQBi P25558.
PaxDbi P25558.
PeptideAtlasi P25558.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YCL014W ; YCL014W ; YCL014W .
GeneIDi 850345.
KEGGi sce:YCL014W.

Organism-specific databases

CYGDi YCL014w.
SGDi S000000520. BUD3.

Phylogenomic databases

eggNOGi NOG40287.
HOGENOMi HOG000000894.
OrthoDBi EOG72G1H3.

Enzyme and pathway databases

BioCyci YEAST:G3O-29281-MONOMER.

Miscellaneous databases

NextBioi 965797.

Gene expression databases

Genevestigatori P25558.

Family and domain databases

Gene3Di 1.20.900.10. 1 hit.
InterProi IPR000219. DH-domain.
IPR021895. DUF3507.
[Graphical view ]
Pfami PF12015. DUF3507. 1 hit.
[Graphical view ]
SMARTi SM00325. RhoGEF. 1 hit.
[Graphical view ]
SUPFAMi SSF48065. SSF48065. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Role of Bud3p in producing the axial budding pattern of yeast."
    Chant J., Mischke M., Mitchell E., Herskowitz I., Pringle J.R.
    J. Cell Biol. 129:767-778(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The complete DNA sequence of yeast chromosome III."
    Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M.
    , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
    Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Gromadka R.
    Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  4. Valles G., Volckaerts G.
    Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. "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-1075 AND SER-1614, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  7. "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.
  8. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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-1063; SER-1075; SER-1134; SER-1149; THR-1157; SER-1160; SER-1254; SER-1257; SER-1412; THR-1440; SER-1443 AND SER-1614, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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-766; THR-1045; SER-1063; SER-1075; SER-1134; THR-1157; SER-1160; SER-1228; SER-1254; SER-1257; SER-1390; SER-1412; THR-1429; THR-1440; SER-1443; SER-1501; SER-1549; SER-1589 AND SER-1614, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiBUD3_YEAST
AccessioniPrimary (citable) accession number: P25558
Secondary accession number(s): D6VQZ9
, P25556, P25557, P87007
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: November 1, 1995
Last modified: June 11, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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 III
    Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

External Data

Dasty 3

Similar proteinsi