P17555 (CAP_YEAST) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 124.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Adenylyl cyclase-associated protein Short name=CAP | ||||||||
| Gene names |
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| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome] | ||||||||
| Taxonomic identifier | 559292 [NCBI] | ||||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › ![]() |
Protein attributes
| Sequence length | 526 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | The N-terminal domain binds to adenylyl cyclase, thereby enabling adenylyl cyclase to be activated by upstream regulatory signals, such as Ras. The C-terminal domain is required for normal cellular morphology and growth control. |
| Subunit structure | Homodimer. |
| Subcellular location | Cytoplasm › cytoskeleton › actin patch. Note: Cortical actin patches. Ref.6 |
| Miscellaneous | Present with 8760 molecules/cell in log phase SD medium. |
| Sequence similarities | Belongs to the CAP family. Contains 1 C-CAP/cofactor C-like domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm Cytoskeleton |
| Ligand | Actin-binding |
| PTM | Phosphoprotein |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | Ras protein signal transduction Inferred from mutant phenotype PubMed 9774417. Source: SGD cell morphogenesisInferred from electronic annotation. Source: InterPro cytoskeleton organizationTraceable author statement Ref.6. Source: SGD |
| Cellular_component | actin cortical patch Inferred from direct assay Ref.6. Source: SGD mating projection tipInferred from direct assay PubMed 19053807. Source: SGD |
| Molecular_function | adenylate cyclase binding Traceable author statement Ref.6. Source: SGD cytoskeletal protein bindingTraceable author statement Ref.6. Source: SGD |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| itself | 3 | EBI-4024,EBI-4024 | ||
| ABP1 | P15891 | 5 | EBI-4024,EBI-2036 | |
| ACT1 | P60010 | 5 | EBI-4024,EBI-2169 | |
| RPL3 | P14126 | 3 | EBI-4024,EBI-15364 | |
| TEF2 | P02994 | 3 | EBI-4024,EBI-6314 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 526 | 526 | Adenylyl cyclase-associated protein | PRO_0000205706 | |||||||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||||||
| Domain | 369 – 504 | 136 | C-CAP/cofactor C-like | ||||||||||||||||||||||||||||||||||||||
| Region | 1 – 168 | 168 | Adenyl cyclase-binding | ||||||||||||||||||||||||||||||||||||||
| Region | 354 – 361 | 8 | Interaction with SH3 domain of ABP1 | ||||||||||||||||||||||||||||||||||||||
| Region | 370 – 526 | 157 | Dimerization and actin-binding | ||||||||||||||||||||||||||||||||||||||
| Motif | 169 – 369 | 201 | SH3-binding | ||||||||||||||||||||||||||||||||||||||
| Compositional bias | 262 – 300 | 39 | Ala/Pro/Ser-rich | ||||||||||||||||||||||||||||||||||||||
| Compositional bias | 277 – 282 | 6 | Poly-Pro | ||||||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||||||
| Modified residue | 454 | 1 | Phosphoserine Ref.8 | ||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 371 – 375 | 5 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 378 – 382 | 5 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 391 – 394 | 4 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 400 – 415 | 16 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 417 – 433 | 17 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 435 – 437 | 3 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 439 – 453 | 15 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 456 – 462 | 7 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 464 – 469 | 6 | |||||||||||||||||||||||||||||||||||||||
| Turn | 473 – 476 | 4 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 478 – 483 | 6 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 485 – 492 | 8 | |||||||||||||||||||||||||||||||||||||||
| Helix | 495 – 497 | 3 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 500 – 503 | 4 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 508 – 513 | 6 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 516 – 521 | 6 | |||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning and characterization of CAP, the S. cerevisiae gene encoding the 70 kd adenylyl cyclase-associated protein." Field J., Vojtek A., Ballester R., Bolger G., Colicelli J., Ferguson K., Gerst J., Kataoka T., Michaeli T., Powers S., Riggs M., Rodgers L., Wieland I., Wheland B., Wigler M. Cell 61:319-327(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "SRV2, a gene required for RAS activation of adenylate cyclase in yeast." Fedor-Chaiken M., Deschenes R.J., Broach J.R. Cell 61:329-340(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c. |
| [3] | "A 43.5 kb segment of yeast chromosome XIV, which contains MFA2, MEP2, CAP/SRV2, NAM9, FKB1/FPR1/RBP1, MOM22 and CPT1, predicts an adenosine deaminase gene and 14 new open reading frames." Mallet L., Bussereau F., Jacquet M. Yeast 11:1195-1209(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c. |
| [4] | "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. Hani J.Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c. |
| [5] | Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c. |
| [6] | "A conserved proline-rich region of the Saccharomyces cerevisiae cyclase-associated protein binds SH3 domains and modulates cytoskeletal localization." Freeman N.L., Lila T., Mintzer K.A., Chen Z., Pahk A.J., Ren R., Drubin D.G., Field J. Mol. Cell. Biol. 16:548-556(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ABP1, SUBCELLULAR LOCATION. |
| [7] | "Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. |
| [8] | "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-454, MASS SPECTROMETRY. |
| [9] | "Crystal structure of the actin binding domain of the cyclase-associated protein." Dodatko T., Fedorov A.A., Grynberg M., Patskovsky Y., Rozwarski D.A., Jaroszewski L., Aronoff-Spencer E., Kondraskina E., Irving T., Godzik A., Almo S.C. Biochemistry 43:10628-10641(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 368-526. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | M58284 mRNA. Translation: AAA63569.1. M32663 Genomic DNA. Translation: AAA35094.1. Z46843 Genomic DNA. Translation: CAA86887.1. Z71414 Genomic DNA. Translation: CAA96020.1. BK006947 Genomic DNA. Translation: DAA10410.1. | ||||||||||||||||||
| PIR | A34896. | ||||||||||||||||||
| RefSeq | NP_014261.1. NM_001182976.1. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P17555. | ||||||||||||||||||
| SMR | P17555. Positions 78-252, 369-524. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| DIP | DIP-77N. | ||||||||||||||||||
| IntAct | P17555. 40 interactions. | ||||||||||||||||||
| MINT | MINT-582270. | ||||||||||||||||||
| STRING | 4932.YNL138W. | ||||||||||||||||||
Proteomic databases | |||||||||||||||||||
| PaxDb | P17555. | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| EnsemblFungi | YNL138W; YNL138W; YNL138W. | ||||||||||||||||||
| GeneID | 855584. | ||||||||||||||||||
| KEGG | sce:YNL138W. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| CYGD | YNL138w. | ||||||||||||||||||
| SGD | S000005082. SRV2. | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| eggNOG | NOG254262. | ||||||||||||||||||
| GeneTree | ENSGT00390000017955. | ||||||||||||||||||
| HOGENOM | HOG000206192. | ||||||||||||||||||
| OMA | LFENEGR. | ||||||||||||||||||
| OrthoDB | EOG4K9FND. | ||||||||||||||||||
Gene expression databases | |||||||||||||||||||
| Genevestigator | P17555. | ||||||||||||||||||
| GermOnline | YNL138W. Saccharomyces cerevisiae. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| Gene3D | 2.160.20.70. 1 hit. | ||||||||||||||||||
| InterPro | IPR001837. Adenylate_cyclase-assoc_CAP. IPR013912. Adenylate_cyclase-assoc_CAP_C. IPR013992. Adenylate_cyclase-assoc_CAP_N. IPR017901. C-CAP_CF_C-like. IPR016098. CAP/MinC_C. IPR018106. CAP_CS. IPR006599. CARP_motif. [Graphical view] | ||||||||||||||||||
| PANTHER | PTHR10652. PTHR10652. 1 hit. | ||||||||||||||||||
| Pfam | PF08603. CAP_C. 1 hit. PF01213. CAP_N. 1 hit. [Graphical view] | ||||||||||||||||||
| SMART | SM00673. CARP. 2 hits. [Graphical view] | ||||||||||||||||||
| SUPFAM | SSF101278. Adenylate_cyclase-assoc_CAP_N. 1 hit. SSF69340. CARP. 1 hit. | ||||||||||||||||||
| PROSITE | PS51329. C_CAP_COFACTOR_C. 1 hit. PS01088. CAP_1. 1 hit. PS01089. CAP_2. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other | |||||||||||||||||||
| EvolutionaryTrace | P17555. | ||||||||||||||||||
| NextBio | 979715. | ||||||||||||||||||
Entry information
| Entry name | CAP_YEAST | ||||||||
| Accession | Primary (citable) accession number: P17555 Secondary accession number(s): D6W144 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |
| Yeast chromosome XIV Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
