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P52286 (SKP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Name:SKP1
Synonyms:CBF3D
Ordered Locus Names:YDR328C
ORF Names:D9798.14
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length194 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Protein modification; protein ubiquitination.

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. Chromosomecentromerekinetochore Ref.16.

Sequence similarities

Belongs to the SKP1 family.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCentromere
Chromosome
Cytoplasm
Kinetochore
Nucleus
   LigandDNA-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG1/S transition of mitotic cell cycle

Inferred from mutant phenotype Ref.2Ref.1. Source: SGD

G2/M transition of mitotic cell cycle

Inferred from mutant phenotype Ref.2Ref.1. Source: SGD

SCF-dependent proteasomal ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.7Ref.8. Source: SGD

cytokinesis

Inferred from mutant phenotype PubMed 17205042. Source: SGD

kinetochore assembly

Inferred from direct assay PubMed 12084919. Source: SGD

protein neddylation

Inferred from mutant phenotype PubMed 9531531. Source: SGD

protein ubiquitination involved in ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.7Ref.8. Source: SGD

regulation of exit from mitosis

Inferred from mutant phenotype PubMed 17205042. Source: SGD

regulation of protein complex assembly

Inferred from physical interaction Ref.13. Source: SGD

septin ring assembly

Inferred from mutant phenotype PubMed 16330709. Source: SGD

vacuolar acidification

Inferred from mutant phenotype Ref.13. Source: SGD

   Cellular_componentCBF3 complex

Inferred from direct assay Ref.6Ref.1. Source: SGD

RAVE complex

Inferred from physical interaction Ref.13PubMed 11844802. Source: SGD

SCF ubiquitin ligase complex

Inferred from direct assay Ref.7Ref.8. Source: SGD

condensed chromosome kinetochore

Inferred from electronic annotation. Source: UniProtKB-SubCell

kinetochore

Traceable author statement PubMed 12769845. Source: SGD

nucleus

Inferred from direct assay PubMed 11080155. Source: SGD

   Molecular_functionDNA replication origin binding

Inferred from physical interaction PubMed 16421250. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 194193Suppressor of kinetochore protein 1
PRO_0000187257

Regions

Region135 – 19460Interaction with the F-box domain of F-box proteins By similarity
Compositional bias66 – 749Asp/Glu-rich (highly acidic)

Amino acid modifications

Modified residue41Phosphoserine Ref.14
Modified residue1771Phosphothreonine Ref.14

Experimental info

Sequence conflict481E → D in AAC49492. Ref.2

Secondary structure

....................... 194
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P52286 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 746DDE6470A69432

FASTA19422,330
        10         20         30         40         50         60 
MVTSNVVLVS GEGERFTVDK KIAERSLLLK NYLNDMHDSN LQNNSDSESD SDSETNHKSK 

        70         80         90        100        110        120 
DNNNGDDDDE DDDEIVMPVP NVRSSVLQKV IEWAEHHRDS NFPDEDDDDS RKSAPVDSWD 

       130        140        150        160        170        180 
REFLKVDQEM LYEIILAANY LNIKPLLDAG CKVVAEMIRG RSPEEIRRTF NIVNDFTPEE 

       190 
EAAIRRENEW AEDR 

« Hide

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. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., 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. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., 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.
PIRS59793.
RefSeqNP_010615.3. NM_001180636.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NEXX-ray2.70A/C1-194[»]
3MKSX-ray2.60A/C2-194[»]
3V7DX-ray2.31A/C1-194[»]
ProteinModelPortalP52286.
SMRP52286. Positions 4-188.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-1236N.
IntActP52286. 75 interactions.
MINTMINT-384072.
STRING4932.YDR328C.

Proteomic databases

PaxDbP52286.
PeptideAtlasP52286.
PRIDEP52286.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR328C; YDR328C; YDR328C.
GeneID851928.
KEGGsce:YDR328C.
sce:YDR332W.

Organism-specific databases

SGDS000002736. SKP1.

Phylogenomic databases

eggNOGCOG5201.
GeneTreeENSGT00390000012652.
HOGENOMHOG000172184.
KOK03094.
OMAPVEIANG.
OrthoDBEOG4T1MX2.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

GenevestigatorP52286.
GermOnlineYDR328C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D3.30.710.10. 1 hit.
InterProIPR011333. BTB/POZ_fold.
IPR016897. E3_ubiquit_lig_SCF_Skp.
IPR001232. Skp1_comp.
IPR016072. Skp1_comp_dimer.
IPR016073. Skp1_comp_POZ.
[Graphical view]
PANTHERPTHR11165. PTHR11165. 1 hit.
PfamPF01466. Skp1. 1 hit.
PF03931. Skp1_POZ. 1 hit.
[Graphical view]
PIRSFPIRSF028729. E3_ubiquit_lig_SCF_Skp. 1 hit.
SMARTSM00512. Skp1. 1 hit.
[Graphical view]
SUPFAMSSF54695. BTB/POZ_fold. 1 hit.
SSF81382. Skp1_comp_dimer. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP52286.
NextBio969983.

Entry information

Entry nameSKP1_YEAST
AccessionPrimary (citable) accession number: P52286
Secondary accession number(s): D6VSW0, Q07186
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal 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