P43612 · SA155_YEAST
- ProteinSIT4-associating protein SAP155
- GeneSAP155
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1002 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Positive regulator of protein phosphatase SIT4. Involved in directing expression of TOR-repressed genes and in dephosphorylation of NPR1 in response to nutrient starvation. Negatively modulates K+ efflux of the cell by the Na+-K+/H+ antiporter NHA1.
Miscellaneous
Present with 5960 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 | cytosol | |
Cellular Component | nucleus | |
Cellular Component | protein serine/threonine phosphatase complex | |
Cellular Component | U2-type spliceosomal complex | |
Molecular Function | protein phosphatase binding | |
Molecular Function | protein phosphatase regulator activity | |
Biological Process | G1/S transition of mitotic cell cycle | |
Biological Process | negative regulation of potassium ion export across plasma membrane |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSIT4-associating protein SAP155
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP43612
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000097561 | 1-1002 | SIT4-associating protein SAP155 | |||
Sequence: MSFWPFGQNLNHSNINKILDEYFHVLHELERINPSVGKAIPAIFNNVQERGTSDSLDSIPEEYSHGDEVKTARGDQKSRFEKDDQQERYEKEEEERSMNSSESSTTSFSSGSTSKTDLDEEDISNATAPMMVTTKNLDNSFIERMLVETELLNELSRQNKTLLDFICFGFFFDKKTNKKVNNMEYLVDQLMECISKIKTATTVDLNNLIDYQEQQQLDDSSQEDVYVESDTEQEEEKEDDNNSNNKKRRKRGSSSFGNDDINNNDDDDDANEDDESAYLTKATIISEIFSLDIWLISESLVKNQSYLNKIWSIINQPNFNSENSPLVPIFLKINQNLLLTRQDQYLNFIRTERSFVDDMLKHVDISLLMDFFLKIISTDKIESPTGIIELVYDQNLISKCLSFLNNKESPADIQACVGDFLKALIAISANAPLDDISIGPNSLTRQLASPESIAKLVDIMINQRGAALNTTVSIVIELIRKNNSDYDQVNLLTTTIKTHPPSNRDPIYLGYLLRKFSNHLSDFFQIILDIENDANIPLHENQLHEKFKPLGFERFKVVELIAELLHCSNMGLMNSKRAERIARRRDKVRSQLSHHLQDALNDLSIEEKEQLKTKHSPTRDTDHDLKNNNGKIDNDNNDNDDESDYGDEIDESFEIPYINMKQNIKLRTDPTVGDLFKIKLYDTRIVSKIMELFLTHPWNNFWHNVIFDIIQQIFNGRMDFSYNSFLVLSLFNLKSSYQFMTDIVISDEKGTDVSRFSPVIRDPNFDFKITTDFILRGYQDSYKFYELRKMNLGYMGHIVLIAEEVVKFSKLYKVELISPDIQVILQTEEWQYYSEEVLNETRMMYSKILGGGSYIDDGNGNIIPQLPDNTTVLTPNGDASNNNEILDSDTGSSNGTSGGGQLINVESLEEQLSLSTESDLHNKLREMLINRAQEDVDNKNTENGVFILGPPEDKNSNSNINNTNHNSNNSNNNDNNDNNDNDNDNTRNYNEDADNDNDYDHE | ||||||
Modified residue | 58 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 255 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 613 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 618 | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Hyperphosphorylated in the absence of SIT4.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Associates with the SIT4 protein phosphatase catalytic subunit in a cell-cycle-dependent manner.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P43612 | SIT4 P20604 | 10 | EBI-16370, EBI-13707 | |
BINARY | P43612 | TIP41 Q12199 | 3 | EBI-16370, EBI-38123 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 51-131 | Disordered | ||||
Sequence: GTSDSLDSIPEEYSHGDEVKTARGDQKSRFEKDDQQERYEKEEEERSMNSSESSTTSFSSGSTSKTDLDEEDISNATAPMM | ||||||
Compositional bias | 60-99 | Basic and acidic residues | ||||
Sequence: PEEYSHGDEVKTARGDQKSRFEKDDQQERYEKEEEERSMN | ||||||
Compositional bias | 100-114 | Polar residues | ||||
Sequence: SSESSTTSFSSGSTS | ||||||
Region | 214-273 | Disordered | ||||
Sequence: QQQLDDSSQEDVYVESDTEQEEEKEDDNNSNNKKRRKRGSSSFGNDDINNNDDDDDANED | ||||||
Compositional bias | 223-238 | Acidic residues | ||||
Sequence: EDVYVESDTEQEEEKE | ||||||
Compositional bias | 239-255 | Basic and acidic residues | ||||
Sequence: DDNNSNNKKRRKRGSSS | ||||||
Compositional bias | 609-636 | Basic and acidic residues | ||||
Sequence: EQLKTKHSPTRDTDHDLKNNNGKIDNDN | ||||||
Region | 609-645 | Disordered | ||||
Sequence: EQLKTKHSPTRDTDHDLKNNNGKIDNDNNDNDDESDY | ||||||
Region | 868-901 | Disordered | ||||
Sequence: DNTTVLTPNGDASNNNEILDSDTGSSNGTSGGGQ | ||||||
Region | 940-1002 | Disordered | ||||
Sequence: NTENGVFILGPPEDKNSNSNINNTNHNSNNSNNNDNNDNNDNDNDNTRNYNEDADNDNDYDHE | ||||||
Compositional bias | 952-979 | Polar residues | ||||
Sequence: EDKNSNSNINNTNHNSNNSNNNDNNDNN | ||||||
Compositional bias | 980-1002 | Basic and acidic residues | ||||
Sequence: DNDNDNTRNYNEDADNDNDYDHE |
Sequence similarities
Belongs to the SAPS family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,002
- Mass (Da)115,002
- Last updated2011-09-21 v4
- Checksum50CDC17130333022
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 60-99 | Basic and acidic residues | ||||
Sequence: PEEYSHGDEVKTARGDQKSRFEKDDQQERYEKEEEERSMN | ||||||
Compositional bias | 100-114 | Polar residues | ||||
Sequence: SSESSTTSFSSGSTS | ||||||
Compositional bias | 223-238 | Acidic residues | ||||
Sequence: EDVYVESDTEQEEEKE | ||||||
Compositional bias | 239-255 | Basic and acidic residues | ||||
Sequence: DDNNSNNKKRRKRGSSS | ||||||
Compositional bias | 609-636 | Basic and acidic residues | ||||
Sequence: EQLKTKHSPTRDTDHDLKNNNGKIDNDN | ||||||
Sequence conflict | 663 | in Ref. 3 and 4; BAA09279 | ||||
Sequence: N → T | ||||||
Sequence conflict | 668 | in Ref. 2; CAC42243 | ||||
Sequence: T → G | ||||||
Sequence conflict | 674-690 | in Ref. 1; AA sequence | ||||
Sequence: DLFKIKLYDTRIVSKIM → TYSKSNYMIRDCFQNN | ||||||
Sequence conflict | 815-824 | in Ref. 1; AAC49303 | ||||
Sequence: ELISPDIQVI → DYISRYSSN | ||||||
Compositional bias | 952-979 | Polar residues | ||||
Sequence: EDKNSNSNINNTNHNSNNSNNNDNNDNN | ||||||
Compositional bias | 980-1002 | Basic and acidic residues | ||||
Sequence: DNDNDNTRNYNEDADNDNDYDHE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U50560 EMBL· GenBank· DDBJ | AAC49303.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ318331 EMBL· GenBank· DDBJ | CAC42243.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
D50617 EMBL· GenBank· DDBJ | BAA09279.1 EMBL· GenBank· DDBJ | Genomic DNA | Frameshift | |
BK006940 EMBL· GenBank· DDBJ | DAA12483.2 EMBL· GenBank· DDBJ | Genomic DNA |