P52286 (SKP1_YEAST) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 128.
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: Suppressor of kinetochore protein 1 Alternative name(s): Centromere DNA-binding protein complex CBF3 subunit D E3 ubiquitin ligase complex SCF subunit SKP1 | ||||||||
| 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 | 194 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Essential component of the E3 ubiquitin ligase complex SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins like phosphorylated SIC1. Participates in the attachment of chromosomes to the spindle. Acts as a regulatory component of the centromere DNA-binding protein complex CBF3, which is essential for chromosome segregation and movement of centromeres along microtubules. CBF3 is required for the recruitment of other kinetochore complexes to CEN DNA. It plays a role in the attachment of chromosomes to the spindle and binds selectively to a highly conserved DNA sequence called CDEIII, found in centromeres and in several promoters. The association of CBF3C with CBF3D and SGT1 is required for CBF3C activation and CBF3 assembly. SKP1/CBF3D could retrieve cyclins or cyclin-CDK-like proteins into the kinetochore thus providing cell cycle-regulated kinetochore activity. Involved in the regulation of methionine biosynthesis genes. Facilitates association of CDC53 with CDC4 and of ROY1 with YPT52. Ref.1 Ref.2 Ref.7 Ref.8 Ref.9 Ref.10 Ref.19 |
| Pathway | |
| Subunit structure | Component of the E3 ubiquitin ligase complexes SCF with HRT1, some cullins like CDC53, and some F-box proteins like MET30 CDC4 and SAF1. Interacts with CDC53 and MET30 to form the E3 ubiquitin ligase complex SCF(Met30) which also contains MET4. Forms complex SCF(Cdc4) together with CDC4 and CDC53. Component of the CBF3 complex, which is formed of CBF3A/CBF2, CBF3B/CEP3, CBF3C/CTF13 and CBF3D. Component of the RAVE complex composed of RAV1, RAV2 and SKP1/CBF3D. Interacts with RCY1, ROY1, CBF3D and SGT1. Ref.2 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.17 Ref.18 Ref.19 |
| Subcellular location | Cytoplasm. Nucleus. Chromosome › centromere › kinetochore Ref.16. |
| Sequence similarities | Belongs to the SKP1 family. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| BOP2 | Q06150 | 3 | EBI-4090,EBI-34293 | |
| CDC4 | P07834 | 12 | EBI-4090,EBI-4434 | |
| CDC53 | Q12018 | 15 | EBI-4090,EBI-4321 | |
| COS111 | P38308 | 2 | EBI-4090,EBI-20947 | |
| CTF13 | P35203 | 7 | EBI-4090,EBI-4085 | |
| EFT2 | P32324 | 2 | EBI-4090,EBI-6333 | |
| GRR1 | P24814 | 9 | EBI-4090,EBI-7898 | |
| MDM30 | Q05930 | 3 | EBI-4090,EBI-31799 | |
| MET30 | P39014 | 14 | EBI-4090,EBI-11507 | |
| RAV1 | P47104 | 5 | EBI-4090,EBI-25471 | |
| ROY1 | Q04847 | 4 | EBI-4090,EBI-27556 | |
| SAF1 | P38352 | 4 | EBI-4090,EBI-21172 | |
| SGT1 | Q08446 | 7 | EBI-4090,EBI-17070 | |
| UFO1 | Q04511 | 4 | EBI-4090,EBI-20020 | |
| YDR131C | Q03899 | 3 | EBI-4090,EBI-36201 | |
| YLR352W | Q06479 | 4 | EBI-4090,EBI-35627 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.6 | ||||||||||||||||||||||||||||
| Chain | 2 – 194 | 193 | Suppressor of kinetochore protein 1 | PRO_0000187257 | |||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||
| Region | 135 – 194 | 60 | Interaction with the F-box domain of F-box proteins By similarity | ||||||||||||||||||||||||||||
| Compositional bias | 66 – 74 | 9 | Asp/Glu-rich (highly acidic) | ||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||
| Modified residue | 4 | 1 | Phosphoserine Ref.14 | ||||||||||||||||||||||||||||
| Modified residue | 177 | 1 | Phosphothreonine Ref.14 | ||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||
| Sequence conflict | 48 | 1 | E → D in AAC49492. Ref.2 | ||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||
| Beta strand | 5 – 9 | 5 | |||||||||||||||||||||||||||||
| Beta strand | 15 – 19 | 5 | |||||||||||||||||||||||||||||
| Helix | 20 – 23 | 4 | |||||||||||||||||||||||||||||
| Helix | 27 – 34 | 8 | |||||||||||||||||||||||||||||
| Beta strand | 76 – 78 | 3 | |||||||||||||||||||||||||||||
| Helix | 84 – 96 | 13 | |||||||||||||||||||||||||||||
| Turn | 97 – 99 | 3 | |||||||||||||||||||||||||||||
| Helix | 118 – 123 | 6 | |||||||||||||||||||||||||||||
| Helix | 128 – 140 | 13 | |||||||||||||||||||||||||||||
| Helix | 144 – 158 | 15 | |||||||||||||||||||||||||||||
| Helix | 163 – 170 | 8 | |||||||||||||||||||||||||||||
| Helix | 178 – 185 | 8 | |||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Budding yeast SKP1 encodes an evolutionarily conserved kinetochore protein required for cell cycle progression." Connelly C., Hieter P. Cell 86:275-285(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. Strain: ATCC 204508 / S288c. |
| [2] | "SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box." Bai C., Sen P., Hofmann K., Ma L., Goebl M., Harper J.W., Elledge S.J. Cell 86:263-274(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH CDC4. Strain: ATCC 204508 / S288c. |
| [3] | "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. Zaccaria P.Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c. |
| [4] | Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c. |
| [5] | "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J.Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c. |
| [6] | "The Saccharomyces cerevisiae kinetochore contains a cyclin-CDK complexing homologue, as identified by in vitro reconstitution." Stemmann O., Lechner J. EMBO J. 15:3611-3620(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-24, CHARACTERIZATION. |
| [7] | "F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex." Skowyra D., Craig K.L., Tyers M., Elledge S.J., Harper J.W. Cell 91:209-219(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT. |
| [8] | "A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p." Feldman R.M., Correll C.C., Kaplan K.B., Deshaies R.J. Cell 91:221-230(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT. |
| [9] | "Non-SCF-type F-box protein Roy1/Ymr258c interacts with a Rab5-like GTPase Ypt52 and inhibits Ypt52 function." Liu Y., Nakatsukasa K., Kotera M., Kanada A., Nishimura T., Kishi T., Mimura S., Kamura T. Mol. Biol. Cell 22:1575-1584(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ROY1. |
| [10] | "Cdc53 is a scaffold protein for multiple Cdc34/Skp1/F-box protein complexes that regulate cell division and methionine biosynthesis in yeast." Patton E.E., Willems A.R., Sa D., Kuras L., Thomas D., Craig K.L., Tyers M. Genes Dev. 12:692-705(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH MET30 AND CDC53. |
| [11] | "Feedback-regulated degradation of the transcriptional activator Met4 is triggered by the SCF(Met30) complex." Rouillon A., Barbey R., Patton E.E., Tyers M., Thomas D. EMBO J. 19:282-294(2000) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT. |
| [12] | "Skp1p and the F-box protein Rcy1p form a non-SCF complex involved in recycling of the SNARE Snc1p in yeast." Galan J.M., Wiederkehr A., Seol J.H., Haguenauer-Tsapis R., Deshaies R.J., Riezman H., Peter M. Mol. Cell. Biol. 21:3105-3117(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RCY1. |
| [13] | "Skp1 forms multiple protein complexes, including RAVE, a regulator of V-ATPase assembly." Seol J.H., Shevchenko A., Shevchenko A., Deshaies R.J. Nat. Cell Biol. 3:384-391(2001) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE RAVE COMPLEX WITH RAV1 AND RAV2. |
| [14] | "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-4 AND THR-177, MASS SPECTROMETRY. |
| [15] | "Structural basis for phosphodependent substrate selection and orientation by the SCFCdc4 ubiquitin ligase." Orlicky S., Tang X., Willems A., Tyers M., Sicheri F. Cell 112:243-256(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 7-166. |
| [16] | "Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. |
| [17] | "The amino-terminal portion of the F-box protein Met30p mediates its nuclear import and assimilation into an SCF complex." Brunson L.E., Dixon C., Kozubowski L., Mathias N. J. Biol. Chem. 279:6674-6682(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MET30. |
| [18] | "Sgt1p and Skp1p modulate the assembly and turnover of CBF3 complexes required for proper kinetochore function." Rodrigo-Brenni M.C., Thomas S., Bouck D.C., Kaplan K.B. Mol. Biol. Cell 15:3366-3378(2004) [PubMed] [Europe PMC] [Abstract] Cited for: ASSEMBLY OF THE CBF3 COMPLEX, INTERACTION WITH CBF3C AND SGT1. |
| [19] | "Skp1-Cullin-F-box-dependent degradation of Aah1p requires its interaction with the F-box protein Saf1p." Escusa S., Laporte D., Massoni A., Boucherie H., Dautant A., Daignan-Fornier B. J. Biol. Chem. 282:20097-20103(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE SCF(SAF1) COMPLEX. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | U43179 Genomic DNA. Translation: AAB17500.1. U61764 mRNA. Translation: AAC49492.1. U32517 Genomic DNA. Translation: AAB64763.1. AY557730 Genomic DNA. Translation: AAS56056.1. BK006938 Genomic DNA. Translation: DAA12170.1. | ||||||||||||||||||||||||
| PIR | S59793. | ||||||||||||||||||||||||
| RefSeq | NP_010615.3. NM_001180636.3. | ||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P52286. | ||||||||||||||||||||||||
| SMR | P52286. Positions 4-188. | ||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||
| DIP | DIP-1236N. | ||||||||||||||||||||||||
| IntAct | P52286. 75 interactions. | ||||||||||||||||||||||||
| MINT | MINT-384072. | ||||||||||||||||||||||||
| STRING | 4932.YDR328C. | ||||||||||||||||||||||||
Proteomic databases | |||||||||||||||||||||||||
| PaxDb | P52286. | ||||||||||||||||||||||||
| PeptideAtlas | P52286. | ||||||||||||||||||||||||
| PRIDE | P52286. | ||||||||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||
| EnsemblFungi | YDR328C; YDR328C; YDR328C. | ||||||||||||||||||||||||
| GeneID | 851928. | ||||||||||||||||||||||||
| KEGG | sce:YDR328C. sce:YDR332W. | ||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||
| SGD | S000002736. SKP1. | ||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||
| eggNOG | COG5201. | ||||||||||||||||||||||||
| GeneTree | ENSGT00390000012652. | ||||||||||||||||||||||||
| HOGENOM | HOG000172184. | ||||||||||||||||||||||||
| KO | K03094. | ||||||||||||||||||||||||
| OMA | PVEIANG. | ||||||||||||||||||||||||
| OrthoDB | EOG4T1MX2. | ||||||||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||||||||
| UniPathway | UPA00143. | ||||||||||||||||||||||||
Gene expression databases | |||||||||||||||||||||||||
| Genevestigator | P52286. | ||||||||||||||||||||||||
| GermOnline | YDR328C. Saccharomyces cerevisiae. | ||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||
| Gene3D | 3.30.710.10. 1 hit. | ||||||||||||||||||||||||
| InterPro | IPR011333. BTB/POZ_fold. IPR016897. E3_ubiquit_lig_SCF_Skp. IPR001232. Skp1_comp. IPR016072. Skp1_comp_dimer. IPR016073. Skp1_comp_POZ. [Graphical view] | ||||||||||||||||||||||||
| PANTHER | PTHR11165. PTHR11165. 1 hit. | ||||||||||||||||||||||||
| Pfam | PF01466. Skp1. 1 hit. PF03931. Skp1_POZ. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| PIRSF | PIRSF028729. E3_ubiquit_lig_SCF_Skp. 1 hit. | ||||||||||||||||||||||||
| SMART | SM00512. Skp1. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| SUPFAM | SSF54695. BTB/POZ_fold. 1 hit. SSF81382. Skp1_comp_dimer. 1 hit. | ||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||
Other | |||||||||||||||||||||||||
| EvolutionaryTrace | P52286. | ||||||||||||||||||||||||
| NextBio | 969983. | ||||||||||||||||||||||||
Entry information
| Entry name | SKP1_YEAST | ||||||||
| Accession | Primary (citable) accession number: P52286 Secondary accession number(s): D6VSW0, Q07186 | ||||||||
| 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 IV Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
