P33338 · SLA2_YEAST
- ProteinProtein SLA2
- GeneSLA2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids968 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Required for cellular morphogenesis and polarization of the cortical cytoskeleton. It might act in concert with proteins such as CDC42 and CDC43 to limit the region of cortical patch formation to the cortex of the bud. Required for the accumulation and/or maintenance of plasma membrane H+-ATPase on the cell surface.
Miscellaneous
Present with 40600 molecules/cell in log phase SD medium.
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 | actin cortical patch | |
Cellular Component | cellular bud neck | |
Cellular Component | cellular bud tip | |
Cellular Component | clathrin-coated vesicle | |
Cellular Component | cortical actin cytoskeleton | |
Cellular Component | incipient cellular bud site | |
Cellular Component | mating projection tip | |
Cellular Component | plasma membrane | |
Molecular Function | actin filament binding | |
Molecular Function | clathrin adaptor activity | |
Molecular Function | clathrin light chain binding | |
Molecular Function | phosphatidylinositol-3,4-bisphosphate binding | |
Molecular Function | phosphatidylinositol-3,5-bisphosphate binding | |
Biological Process | actin cortical patch assembly | |
Biological Process | actin filament organization | |
Biological Process | clathrin coat assembly | |
Biological Process | endocytosis | |
Biological Process | negative regulation of Arp2/3 complex-mediated actin nucleation |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein SLA2
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP33338
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 772-791 | Helical | ||||
Sequence: LLSLALMIIDAVVALVKAAI |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000071945 | 1-968 | Protein SLA2 | |||
Sequence: MSRIDSDLQKALKKACSVEETAPKRKHVRACIVYTWDHQSSKAVFTTLKTLPLANDEVQLFKMLIVLHKIIQEGHPSALAEAIRDRDWIRSLGRVHSGGSSYSKLIREYVRYLVLKLDFHAHHRGFNNGTFEYEEYVSLVSVSDPDEGYETILDLMSLQDSLDEFSQIIFASIQSERRNTECKISALIPLIAESYGIYKFITSMLRAMHRQLNDAEGDAALQPLKERYELQHARLFEFYADCSSVKYLTTLVTIPKLPVDAPDVFLINDVDESKEIKFKKREPSVTPARTPARTPTPTPPVVAEPAISPRPVSQRTTSTPTGYLQTMPTGATTGMMIPTATGAANAIFPQATAQMQPDFWANQQAQFANEQNRLEQERVQQLQQQQAQQELFQQQLQKAQQDMMNMQLQQQNQHQNDLIALTNQYEKDQALLQQYDQRVQQLESEITTMDSTASKQLANKDEQLTALQDQLDVWERKYESLAKLYSQLRQEHLNLLPRFKKLQLKVNSAQESIQKKEQLEHKLKQKDLQMAELVKDRDRARLELERSINNAEADSAAATAAAETMTQDKMNPILDAILESGINTIQESVYNLDSPLSWSGPLTPPTFLLSLLESTSENATEFATSFNNLIVDGLAHGDQTEVIHCVSDFSTSMATLVTNSKAYAVTTLPQEQSDQILTLVKRCAREAQYFFEDLMSENLNQVGDEEKTDIVINANVDMQEKLQELSLAIEPLLNIQSVKSNKETNPHSELVATADKIVKSSEHLRVDVPKPLLSLALMIIDAVVALVKAAIQCQNEIATTTSIPLNQFYLKNSRWTEGLISAAKAVAGATNVLITTASKLITSEDNENTSPEQFIVASKEVAASTIQLVAASRVKTSIHSKAQDKLEHCSKDVTDACRSLGNHVMGMIEDDHSTSQQQQPLDFTSEHTLKTAEMEQQVEILKLEQSLSNARKRLGEIRRHAYYNQDDD | ||||||
Modified residue | 294 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 298 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 308 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 555 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P33338 | ENT1 Q12518 | 3 | EBI-17323, EBI-31494 | |
BINARY | P33338 | LAS17 Q12446 | 3 | EBI-17323, EBI-10022 | |
BINARY | P33338 | SLA1 P32790 | 3 | EBI-17323, EBI-17313 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-127 | ENTH | ||||
Sequence: MSRIDSDLQKALKKACSVEETAPKRKHVRACIVYTWDHQSSKAVFTTLKTLPLANDEVQLFKMLIVLHKIIQEGHPSALAEAIRDRDWIRSLGRVHSGGSSYSKLIREYVRYLVLKLDFHAHHRGFN | ||||||
Region | 280-324 | Disordered | ||||
Sequence: KREPSVTPARTPARTPTPTPPVVAEPAISPRPVSQRTTSTPTGYL | ||||||
Compositional bias | 290-306 | Pro residues | ||||
Sequence: TPARTPTPTPPVVAEPA | ||||||
Compositional bias | 310-324 | Polar residues | ||||
Sequence: RPVSQRTTSTPTGYL | ||||||
Domain | 717-965 | I/LWEQ | ||||
Sequence: DMQEKLQELSLAIEPLLNIQSVKSNKETNPHSELVATADKIVKSSEHLRVDVPKPLLSLALMIIDAVVALVKAAIQCQNEIATTTSIPLNQFYLKNSRWTEGLISAAKAVAGATNVLITTASKLITSEDNENTSPEQFIVASKEVAASTIQLVAASRVKTSIHSKAQDKLEHCSKDVTDACRSLGNHVMGMIEDDHSTSQQQQPLDFTSEHTLKTAEMEQQVEILKLEQSLSNARKRLGEIRRHAYYNQ |
Sequence similarities
Belongs to the SLA2 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length968
- Mass (Da)108,911
- Last updated2011-09-21 v5
- ChecksumE592E09D8040C0E9
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 52 | in Ref. 2; AAA74726 | ||||
Sequence: P → A | ||||||
Compositional bias | 290-306 | Pro residues | ||||
Sequence: TPARTPTPTPPVVAEPA | ||||||
Compositional bias | 310-324 | Polar residues | ||||
Sequence: RPVSQRTTSTPTGYL | ||||||
Sequence conflict | 344 | in Ref. 3; CAA96148/CAA96149 | ||||
Sequence: A → R | ||||||
Sequence conflict | 560 | in Ref. 5; AAA19161 | ||||
Sequence: A → R | ||||||
Sequence conflict | 915 | in Ref. 5; AAA19161 | ||||
Sequence: S → C |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z22811 EMBL· GenBank· DDBJ | CAA80464.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L12352 EMBL· GenBank· DDBJ | AAA74726.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z71519 EMBL· GenBank· DDBJ | CAA96149.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z71518 EMBL· GenBank· DDBJ | CAA96148.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U07938 EMBL· GenBank· DDBJ | AAA19161.1 EMBL· GenBank· DDBJ | Unassigned DNA | Frameshift | |
Z69381 EMBL· GenBank· DDBJ | CAA93355.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006947 EMBL· GenBank· DDBJ | DAA10316.2 EMBL· GenBank· DDBJ | Genomic DNA |