P25558 · BUD3_YEAST
- ProteinBud site selection protein 3
- GeneBUD3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1636 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
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.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cellular bud neck | |
Cellular Component | cellular bud neck contractile ring | |
Molecular Function | guanyl-nucleotide exchange factor activity | |
Biological Process | axial cellular bud site selection | |
Biological Process | cytogamy |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBud site selection protein 3
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP25558
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000065016 | 1-1636 | Bud site selection protein 3 | |||
Sequence: MEKDLSSLYSEKKDKENDETLFNIKLSKSVVETTPLNGHSLFDDDKSLSDWTDNVFTQSVFYHGSDDLIWGKFFVCVYKSPNSNKLNAIIFDKLGTSCFESVDISSNSQYYPAIENLSPSDQESNVKKCIAVILLQRYPLLSPSDLSQILSNKSENCDYDPPYAGDLASSCQLITAVPPEDLGKRFFTSGLLQNRFVSSTLLDVIYENNESTIELNNRLVFHLGEQLEQLFNPVTEYSPEQTEYGYKAPEDELPTESDDDLVKAICNELLQLQTNFTFNLVEFLQKFLIALRVRVLNEEINGLSTTKLNRLFPPTIDEVTRINCIFLDSLKTAIPYGSLEVLKACSITIPYFYKAYTRHEAATKNFSKDIKLFIRHFSNVIPEREVYTEMKIESIIKGPQEKLLKLKLIIERLWKSKKWRPKNQEMAKKCYNNIIDVIDSFGKLDSPLHSYSTRVFTPSGKILTELAKCWPVELQYKWLKRRVVGVYDVVDLNDENKRNLLVIFSDYVVFINILEAESYYTSDGSNRPLISDILMNSLINEVPLPSKIPKLKVERHCYIDEVLVSILDKSTLRFDRLKGKDSFSMVCKLSSAFISSSSVADLITKARILEKDTAFHLFKASRSHFTLYSTAHELCAYDSEKIKSKFALFLNIPPSKEILEVNNLHLAFFARFCSNDGRDNIVILDVLTKHDDKHIEVTSDNIVFTIINQLAIEIPICFSSLNSSMAKDLLCVNENLIKNLEHQLEEVKHPSTDEHRAVNSKLSGASDFDATHEKKRSYGTITTFRSYTSDLKDSPSGDNSNVTKETKEILPVKPTKKSSKKPREIQKKTKTNASKAEHIEKKKPNKGKGFFGVLKNVFGSKSKSKPSPVQRVPKKISQRHPKSPVKKPMTSEKKSSPKRAVVSSPKIKKKSTSFSTKESQTAKSSLRAVEFKSDDLIGKPPDVGNGAHPQENTRISSVVRDTKYVSYNPSQPVTENTSNEKNVEPKADQSTKQDNISNFADVEVSASSYPEKLDAETDDQIIGKATNSSSVHGNKELPDLAEVTTANRVSTTSAGDQRIDTQSEFLRAADVENLSDDDEHRQNESRVFNDDLFGDFIPKHYRNKQENINSSSNLFPEGKVPQEKGVSNENTNISLKTNEDASTLTQKLSPQASKVLTENSNELKDTNNEGKDAKDIKLGDDYSDKETAKEITKPKNFVEGITERKEIFPTIPRLAPPASKINFQRSPSYIELFQGMRVVLDKHDAHYNWKRLASQVSLSEGLKVNTEEDAAIINKSQDDAKAERMTQISEVIEYEMQQPIPTYLPKAHLDDSGIEKSDDKFFEIEEELKEELKGSKTGNEDVGNNNPSNSIPKIEKPPAFKVIRTSPVRIIGRTFEDTRKYENGSPSDISFTYDTHNNDEPDKRLMELKFPSQDEIPDDRFYTPAEEPTAEFPVEELPNTPRSINVTTSNNKSTDDKLSSGNIDQKPTELLDDLEFSSFNIAFGNTSMSTDNMKISSDLSSNKTVLGNAQKVQESPSGPLIYVLPQSSTKHEKEGFLRKKQKDEPIWVSPSKIDFADLSRRTKALTPERNTVPLKNNDSRKYKYTGEGSIGNMTNMLLTKDASYAYLKDFVALSDDEDEDGKQNCAVGGPEKLKFY | ||||||
Modified residue | 766 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 792 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 963 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Modified residue | 1045 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1063 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1075 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1134 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1149 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1157 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1160 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1228 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1254 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1257 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1390 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1412 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1429 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1440 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1443 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1501 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1549 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1589 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1614 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with AXL2.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P25558 | AXL2 P38928 | 2 | EBI-3840, EBI-3397 | |
BINARY | P25558 | BUD4 P47136 | 2 | EBI-3840, EBI-3848 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 789-806 | Polar residues | ||||
Sequence: SDLKDSPSGDNSNVTKET | ||||||
Region | 789-998 | Disordered | ||||
Sequence: SDLKDSPSGDNSNVTKETKEILPVKPTKKSSKKPREIQKKTKTNASKAEHIEKKKPNKGKGFFGVLKNVFGSKSKSKPSPVQRVPKKISQRHPKSPVKKPMTSEKKSSPKRAVVSSPKIKKKSTSFSTKESQTAKSSLRAVEFKSDDLIGKPPDVGNGAHPQENTRISSVVRDTKYVSYNPSQPVTENTSNEKNVEPKADQSTKQDNISN | ||||||
Compositional bias | 809-847 | Basic and acidic residues | ||||
Sequence: ILPVKPTKKSSKKPREIQKKTKTNASKAEHIEKKKPNKG | ||||||
Compositional bias | 906-927 | Polar residues | ||||
Sequence: KIKKKSTSFSTKESQTAKSSLR | ||||||
Compositional bias | 949-980 | Polar residues | ||||
Sequence: PQENTRISSVVRDTKYVSYNPSQPVTENTSNE | ||||||
Region | 1025-1063 | Disordered | ||||
Sequence: ATNSSSVHGNKELPDLAEVTTANRVSTTSAGDQRIDTQS | ||||||
Compositional bias | 1044-1060 | Polar residues | ||||
Sequence: TTANRVSTTSAGDQRID | ||||||
Region | 1107-1130 | Disordered | ||||
Sequence: NINSSSNLFPEGKVPQEKGVSNEN | ||||||
Region | 1152-1179 | Disordered | ||||
Sequence: ASKVLTENSNELKDTNNEGKDAKDIKLG | ||||||
Compositional bias | 1164-1179 | Basic and acidic residues | ||||
Sequence: KDTNNEGKDAKDIKLG | ||||||
Region | 1331-1354 | Disordered | ||||
Sequence: ELKGSKTGNEDVGNNNPSNSIPKI | ||||||
Compositional bias | 1338-1352 | Polar residues | ||||
Sequence: GNEDVGNNNPSNSIP | ||||||
Region | 1435-1465 | Disordered | ||||
Sequence: EELPNTPRSINVTTSNNKSTDDKLSSGNIDQ | ||||||
Compositional bias | 1440-1465 | Polar residues | ||||
Sequence: TPRSINVTTSNNKSTDDKLSSGNIDQ |
Sequence similarities
Belongs to the BUD3 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,636
- Mass (Da)184,719
- Last updated1995-11-01 v2
- Checksum9E4E46BA5C3A3F69
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 789-806 | Polar residues | ||||
Sequence: SDLKDSPSGDNSNVTKET | ||||||
Compositional bias | 809-847 | Basic and acidic residues | ||||
Sequence: ILPVKPTKKSSKKPREIQKKTKTNASKAEHIEKKKPNKG | ||||||
Compositional bias | 906-927 | Polar residues | ||||
Sequence: KIKKKSTSFSTKESQTAKSSLR | ||||||
Compositional bias | 949-980 | Polar residues | ||||
Sequence: PQENTRISSVVRDTKYVSYNPSQPVTENTSNE | ||||||
Compositional bias | 1044-1060 | Polar residues | ||||
Sequence: TTANRVSTTSAGDQRID | ||||||
Compositional bias | 1164-1179 | Basic and acidic residues | ||||
Sequence: KDTNNEGKDAKDIKLG | ||||||
Compositional bias | 1338-1352 | Polar residues | ||||
Sequence: GNEDVGNNNPSNSIP | ||||||
Compositional bias | 1440-1465 | Polar residues | ||||
Sequence: TPRSINVTTSNNKSTDDKLSSGNIDQ |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U17580 EMBL· GenBank· DDBJ | AAA86315.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X59720 EMBL· GenBank· DDBJ | CAA42346.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006937 EMBL· GenBank· DDBJ | DAA07468.1 EMBL· GenBank· DDBJ | Genomic DNA |