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P25558 (BUD3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bud site selection protein 3
Gene names
Name:BUD3
Ordered Locus Names:YCL014W
ORF Names:YCL012W, YCL013W, YCL12W, YCL13W, YCL14W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length1636 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Interacts with AXL2. Ref.8

Sequence similarities

Belongs to the BUD3 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

AXL2P389282EBI-3840,EBI-3397

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 16361636Bud site selection protein 3
PRO_0000065016

Amino acid modifications

Modified residue71Phosphoserine Ref.10 Ref.11
Modified residue101Phosphoserine Ref.11
Modified residue4461Phosphoserine Ref.11
Modified residue7771Phosphoserine Ref.11
Modified residue7941Phosphoserine Ref.10
Modified residue9131Phosphoserine Ref.11
Modified residue10631Phosphoserine Ref.11
Modified residue10751Phosphoserine Ref.7 Ref.10 Ref.11
Modified residue11101Phosphoserine Ref.10
Modified residue11111Phosphoserine Ref.10
Modified residue11341Phosphoserine Ref.11
Modified residue11491Phosphoserine Ref.11
Modified residue11531Phosphoserine Ref.11
Modified residue11571Phosphothreonine Ref.10 Ref.11
Modified residue11601Phosphoserine Ref.10 Ref.11
Modified residue11831Phosphoserine Ref.6 Ref.10 Ref.11
Modified residue12291Phosphotyrosine Ref.11
Modified residue12541Phosphoserine Ref.11
Modified residue12571Phosphoserine Ref.11
Modified residue13661Phosphoserine Ref.9
Modified residue14121Phosphoserine Ref.10 Ref.11
Modified residue14401Phosphothreonine Ref.11
Modified residue14431Phosphoserine Ref.11
Modified residue15001Phosphoserine Ref.11
Modified residue15011Phosphoserine Ref.11
Modified residue15151Phosphoserine Ref.11
Modified residue15661Phosphothreonine Ref.10
Modified residue16031Phosphoserine Ref.11
Modified residue16141Phosphoserine Ref.7 Ref.10 Ref.11

Sequences

Sequence LengthMass (Da)Tools
P25558 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: 9E4E46BA5C3A3F69

FASTA1,636184,719
        10         20         30         40         50         60 
MEKDLSSLYS EKKDKENDET LFNIKLSKSV VETTPLNGHS LFDDDKSLSD WTDNVFTQSV 

        70         80         90        100        110        120 
FYHGSDDLIW GKFFVCVYKS PNSNKLNAII FDKLGTSCFE SVDISSNSQY YPAIENLSPS 

       130        140        150        160        170        180 
DQESNVKKCI AVILLQRYPL LSPSDLSQIL SNKSENCDYD PPYAGDLASS CQLITAVPPE 

       190        200        210        220        230        240 
DLGKRFFTSG LLQNRFVSST LLDVIYENNE STIELNNRLV FHLGEQLEQL FNPVTEYSPE 

       250        260        270        280        290        300 
QTEYGYKAPE DELPTESDDD LVKAICNELL QLQTNFTFNL VEFLQKFLIA LRVRVLNEEI 

       310        320        330        340        350        360 
NGLSTTKLNR LFPPTIDEVT RINCIFLDSL KTAIPYGSLE VLKACSITIP YFYKAYTRHE 

       370        380        390        400        410        420 
AATKNFSKDI KLFIRHFSNV IPEREVYTEM KIESIIKGPQ EKLLKLKLII ERLWKSKKWR 

       430        440        450        460        470        480 
PKNQEMAKKC YNNIIDVIDS FGKLDSPLHS YSTRVFTPSG KILTELAKCW PVELQYKWLK 

       490        500        510        520        530        540 
RRVVGVYDVV DLNDENKRNL LVIFSDYVVF INILEAESYY TSDGSNRPLI SDILMNSLIN 

       550        560        570        580        590        600 
EVPLPSKIPK LKVERHCYID EVLVSILDKS TLRFDRLKGK DSFSMVCKLS SAFISSSSVA 

       610        620        630        640        650        660 
DLITKARILE KDTAFHLFKA SRSHFTLYST AHELCAYDSE KIKSKFALFL NIPPSKEILE 

       670        680        690        700        710        720 
VNNLHLAFFA RFCSNDGRDN IVILDVLTKH DDKHIEVTSD NIVFTIINQL AIEIPICFSS 

       730        740        750        760        770        780 
LNSSMAKDLL CVNENLIKNL EHQLEEVKHP STDEHRAVNS KLSGASDFDA THEKKRSYGT 

       790        800        810        820        830        840 
ITTFRSYTSD LKDSPSGDNS NVTKETKEIL PVKPTKKSSK KPREIQKKTK TNASKAEHIE 

       850        860        870        880        890        900 
KKKPNKGKGF FGVLKNVFGS KSKSKPSPVQ RVPKKISQRH PKSPVKKPMT SEKKSSPKRA 

       910        920        930        940        950        960 
VVSSPKIKKK STSFSTKESQ TAKSSLRAVE FKSDDLIGKP PDVGNGAHPQ ENTRISSVVR 

       970        980        990       1000       1010       1020 
DTKYVSYNPS QPVTENTSNE KNVEPKADQS TKQDNISNFA DVEVSASSYP EKLDAETDDQ 

      1030       1040       1050       1060       1070       1080 
IIGKATNSSS VHGNKELPDL AEVTTANRVS TTSAGDQRID TQSEFLRAAD VENLSDDDEH 

      1090       1100       1110       1120       1130       1140 
RQNESRVFND DLFGDFIPKH YRNKQENINS SSNLFPEGKV PQEKGVSNEN TNISLKTNED 

      1150       1160       1170       1180       1190       1200 
ASTLTQKLSP QASKVLTENS NELKDTNNEG KDAKDIKLGD DYSDKETAKE ITKPKNFVEG 

      1210       1220       1230       1240       1250       1260 
ITERKEIFPT IPRLAPPASK INFQRSPSYI ELFQGMRVVL DKHDAHYNWK RLASQVSLSE 

      1270       1280       1290       1300       1310       1320 
GLKVNTEEDA AIINKSQDDA KAERMTQISE VIEYEMQQPI PTYLPKAHLD DSGIEKSDDK 

      1330       1340       1350       1360       1370       1380 
FFEIEEELKE ELKGSKTGNE DVGNNNPSNS IPKIEKPPAF KVIRTSPVRI IGRTFEDTRK 

      1390       1400       1410       1420       1430       1440 
YENGSPSDIS FTYDTHNNDE PDKRLMELKF PSQDEIPDDR FYTPAEEPTA EFPVEELPNT 

      1450       1460       1470       1480       1490       1500 
PRSINVTTSN NKSTDDKLSS GNIDQKPTEL LDDLEFSSFN IAFGNTSMST DNMKISSDLS 

      1510       1520       1530       1540       1550       1560 
SNKTVLGNAQ KVQESPSGPL IYVLPQSSTK HEKEGFLRKK QKDEPIWVSP SKIDFADLSR 

      1570       1580       1590       1600       1610       1620 
RTKALTPERN TVPLKNNDSR KYKYTGEGSI GNMTNMLLTK DASYAYLKDF VALSDDEDED 

      1630 
GKQNCAVGGP EKLKFY

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1183, MASS SPECTROMETRY.
Strain: YAL6B.
[7]"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, MASS SPECTROMETRY.
Strain: ADR376.
[8]"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.
[9]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1366, MASS SPECTROMETRY.
[10]"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-794; SER-1075; SER-1110; SER-1111; THR-1157; SER-1160; SER-1183; SER-1412; THR-1566 AND SER-1614, MASS SPECTROMETRY.
[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-7; SER-10; SER-446; SER-777; SER-913; SER-1063; SER-1075; SER-1134; SER-1149; SER-1153; THR-1157; SER-1160; SER-1183; TYR-1229; SER-1254; SER-1257; SER-1412; THR-1440; SER-1443; SER-1500; SER-1501; SER-1515; SER-1603 AND SER-1614, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U17580 Genomic DNA. Translation: AAA86315.1.
X59720 Genomic DNA. Translation: CAA42346.2.
BK006937 Genomic DNA. Translation: DAA07468.1.
PIRS74285.
S74286.
RefSeqNP_009914.2. NM_001178662.1.

3D structure databases

ProteinModelPortalP25558.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-4969N.
IntActP25558. 9 interactions.
MINTMINT-522762.

Proteomic databases

PaxDbP25558.
PeptideAtlasP25558.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYCL014W; YCL014W; YCL014W.
GeneID850345.
KEGGsce:YCL014W.

Organism-specific databases

CYGDYCL014w.
SGDS000000520. BUD3.

Phylogenomic databases

eggNOGNOG40287.
HOGENOMHOG000000894.
OrthoDBEOG4D82F0.

Gene expression databases

GenevestigatorP25558.
GermOnlineYCL014W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D1.20.900.10. 1 hit.
InterProIPR000219. DH-domain.
IPR021895. DUF3507.
[Graphical view]
PfamPF12015. DUF3507. 1 hit.
[Graphical view]
SMARTSM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMSSF48065. DH-domain. 1 hit.
ProtoNetSearch...

Other

NextBio965797.

Entry information

Entry nameBUD3_YEAST
AccessionPrimary (citable) accession number: P25558
Secondary accession number(s): D6VQZ9 expand/collapse secondary AC list , P25556, P25557, P87007
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: November 1, 1995
Last modified: April 3, 2013
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome III

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents