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UniProtKB/Swiss-Prot entry P52286


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SKP1_YEAST
Primary accession number P52286
Secondary accession number Q07186
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 86)
Name and origin of the protein
Protein name Suppressor of kinetochore protein 1
Synonyms Centromere DNA-binding protein complex CBF3 subunit D
E3 ubiquitin ligase complex SCF subunit SKP1
Gene name
Name: SKP1
Synonyms: CBF3D
OrderedLocusNames: YDR328C
ORFNames: D9798.14
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
STRAIN=ATCC 204508 / S288c;
DOI=10.1016/S0092-8674(00)80099-9; PubMed=8706132 [NCBI, ExPASy, EBI, Israel, Japan]
Connelly C., Hieter P.;
"Budding yeast SKP1 encodes an evolutionarily conserved kinetochore protein required for cell cycle progression.";
Cell 86:275-285(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH CDC4.
STRAIN=ATCC 204508 / S288c;
DOI=10.1016/S0092-8674(00)80098-7; PubMed=8706131 [NCBI, ExPASy, EBI, Israel, Japan]
Bai C., Sen P., Hofmann K., Ma L., Goebl M., Harper J.W., Elledge S.J.;
"SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box.";
Cell 86:263-274(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan]
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., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
PROTEIN SEQUENCE OF 2-24, AND CHARACTERIZATION.
PubMed=8670864 [NCBI, ExPASy, EBI, Israel, Japan]
Stemmann O., Lechner J.;
"The Saccharomyces cerevisiae kinetochore contains a cyclin-CDK complexing homologue, as identified by in vitro reconstitution.";
EMBO J. 15:3611-3620(1996).
[6]
FUNCTION, AND SUBUNIT.
DOI=10.1016/S0092-8674(00)80403-1; PubMed=9346238 [NCBI, ExPASy, EBI, Israel, Japan]
Skowyra D., Craig K.L., Tyers M., Elledge S.J., Harper J.W.;
"F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex.";
Cell 91:209-219(1997).
[7]
FUNCTION, AND SUBUNIT.
DOI=10.1016/S0092-8674(00)80404-3; PubMed=9346239 [NCBI, ExPASy, EBI, Israel, Japan]
Feldman R.M., Correll C.C., Kaplan K.B., Deshaies R.J.;
"A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p.";
Cell 91:221-230(1997).
[8]
FUNCTION, AND INTERACTION WITH MET30 AND CDC53.
PubMed=9499404 [NCBI, ExPASy, EBI, Israel, Japan]
Patton E.E., Willems A.R., Sa D., Kuras L., Thomas D., Craig K.L., Tyers M.;
"Cdc53 is a scaffold protein for multiple Cdc34/Skp1/F-box protein complexes that regulate cell division and methionine biosynthesis in yeast.";
Genes Dev. 12:692-705(1998).
[9]
SUBUNIT.
DOI=10.1093/emboj/19.2.282; PubMed=10637232 [NCBI, ExPASy, EBI, Israel, Japan]
Rouillon A., Barbey R., Patton E.E., Tyers M., Thomas D.;
"Feedback-regulated degradation of the transcriptional activator Met4 is triggered by the SCF(Met30) complex.";
EMBO J. 19:282-294(2000).
[10]
INTERACTION WITH RCY1.
DOI=10.1128/MCB.21.9.3105-3117.2001; PubMed=11287615 [NCBI, ExPASy, EBI, Israel, Japan]
Galan J.M., Wiederkehr A., Seol J.H., Haguenauer-Tsapis R., Deshaies R.J., Riezman H., Peter M.;
"Skp1p and the F-box protein Rcy1p form a non-SCF complex involved in recycling of the SNARE Snc1p in yeast.";
Mol. Cell. Biol. 21:3105-3117(2001).
[11]
IDENTIFICATION IN THE RAVE COMPLEX WITH RAV1 AND RAV2.
DOI=10.1038/35070067; PubMed=11283612 [NCBI, ExPASy, EBI, Israel, Japan]
Seol J.H., Shevchenko A., Shevchenko A., Deshaies R.J.;
"Skp1 forms multiple protein complexes, including RAVE, a regulator of V-ATPase assembly.";
Nat. Cell Biol. 3:384-391(2001).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 AND THR-177, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[13]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 7-166.
DOI=10.1016/S0092-8674(03)00034-5; PubMed=12553912 [NCBI, ExPASy, EBI, Israel, Japan]
Orlicky S., Tang X., Willems A., Tyers M., Sicheri F.;
"Structural basis for phosphodependent substrate selection and orientation by the SCFCdc4 ubiquitin ligase.";
Cell 112:243-256(2003).
[14]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan]
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[15]
INTERACTION WITH MET30.
DOI=10.1074/jbc.M308875200; PubMed=14660673 [NCBI, ExPASy, EBI, Israel, Japan]
Brunson L.E., Dixon C., Kozubowski L., Mathias N.;
"The amino-terminal portion of the F-box protein Met30p mediates its nuclear import and assimilation into an SCF complex.";
J. Biol. Chem. 279:6674-6682(2004).
[16]
ASSEMBLY OF THE CBF3 COMPLEX, AND INTERACTION WITH CBF3C AND SGT1.
DOI=10.1091/mbc.E03-12-0887; PubMed=15090617 [NCBI, ExPASy, EBI, Israel, Japan]
Rodrigo-Brenni M.C., Thomas S., Bouck D.C., Kaplan K.B.;
"Sgt1p and Skp1p modulate the assembly and turnover of CBF3 complexes required for proper kinetochore function.";
Mol. Biol. Cell 15:3366-3378(2004).
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 centromers 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.
  • PATHWAY: Protein modification; protein ubiquitination.
  • SUBUNIT: Component of the E3 ubiquitin ligase complexes SCF with HRT1, some cullins like CDC53, and some F-box proteins like MET30 and CDC4. 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, CBF3D and SGT1.
  • INTERACTION:
    P38352:-; NbExp=1; IntAct=EBI-4090, EBI-21172;
    Q03899:-; NbExp=1; IntAct=EBI-4090, EBI-36201;
    Q06479:-; NbExp=1; IntAct=EBI-4090, EBI-35627;
    P41002:CCNF (xeno); NbExp=1; IntAct=EBI-4090, EBI-1207574;
    P07834:CDC4; NbExp=3; IntAct=EBI-4090, EBI-4434;
    Q12018:CDC53; NbExp=4; IntAct=EBI-4090, EBI-4321;
    P38308:COS111; NbExp=1; IntAct=EBI-4090, EBI-20947;
    P35203:CTF13; NbExp=1; IntAct=EBI-4090, EBI-4085;
    P32324:EFT1; NbExp=1; IntAct=EBI-4090, EBI-6333;
    P24814:GRR1; NbExp=2; IntAct=EBI-4090, EBI-7898;
    P39014:MET30; NbExp=5; IntAct=EBI-4090, EBI-11507;
    O74991:pof3 (xeno); NbExp=1; IntAct=EBI-4090, EBI-1153554;
    P47104:RAV1; NbExp=1; IntAct=EBI-4090, EBI-25471;
  • SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Kinetochore.
  • SIMILARITY: Belongs to the SKP1 family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U43179; AAB17500.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U61764; AAC49492.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U32517; AAB64763.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY557730; AAS56056.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S59793; S59793.
RefSeq NP_010615.1; -.
3D structure databases
PDB
1NEX; X-ray; 2.70 A; A/C=1-194.[ExPASy / RCSB / EBI]
PDBsum 1NEX; -.
ModBase P52286.
Protein-protein interaction databases
DIP DIP:1236N; -.
IntAct P52286; 56.
Organism-specific databases
CYGD YDR328c; -.
SGD S000002736; SKP1.
Yeast-GFP YDR328C.
Gene expression databases
GermOnline YDR328C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0031518; Cellular component: CBF3 complex (inferred from direct assay from SGD).
GO:0000777; Cellular component: condensed chromosome kinetochore (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0043291; Cellular component: RAVE complex (inferred from physical interaction from SGD).
GO:0019005; Cellular component: SCF ubiquitin ligase complex (inferred from direct assay from SGD).
GO:0003688; Molecular function: DNA replication origin binding (inferred from physical interaction from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0000910; Biological process: cytokinesis (inferred from mutant phenotype from SGD).
GO:0000082; Biological process: G1/S transition of mitotic cell cycle (inferred from mutant phenotype from SGD).
GO:0000086; Biological process: G2/M transition of mitotic cell cycle (inferred from mutant phenotype from SGD).
GO:0051382; Biological process: kinetochore assembly (inferred from direct assay from SGD).
GO:0045116; Biological process: protein neddylation (inferred from genetic interaction from SGD).
GO:0042787; Biological process: protein ubiquitination during ubiquitin-dependent protein catabolic process (inferred from direct assay from SGD).
GO:0007096; Biological process: regulation of exit from mitosis (inferred from mutant phenotype from SGD).
GO:0043254; Biological process: regulation of protein complex assembly (inferred from physical interaction from SGD).
GO:0031146; Biological process: SCF-dependent proteasomal ubiquitin-dependent protein catabolic process (inferred from direct assay from SGD).
GO:0000921; Biological process: septin ring assembly (inferred from mutant phenotype from SGD).
GO:0007035; Biological process: vacuolar acidification (inferred from genetic interaction from SGD).
QuickGo view.
Family and domain databases
InterPro IPR011333; BTB/POZ_fold.
IPR016897; E3_ubiquit_lig_SCF_Skp.
IPR001232; Skp1_comp.
IPR016072; Skp1_comp_dimer.
IPR016073; Skp1_comp_POZ.
Graphical view of domain structure.
Gene3D G3DSA:3.30.710.10; BTB/POZ_fold; 1.
PANTHER PTHR11165; Skp1; 1.
Pfam PF01466; Skp1; 1.
PF03931; Skp1_POZ; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF028729; E3_ubiquit_lig_SCF_Skp; 1.
SMART SM00512; Skp1; 1.
SMART graphical view of domain structure.
Proteomic databases
PeptideAtlas P52286; -.
Proteomics databases
PRIDE P52286; -.
Genome annotation databases
Ensembl YDR328C; Saccharomyces cerevisiae. [Contig view]
GeneID 851928; -.
GenomeReviews Z71256_GR; YDR328C.
KEGG sce:YDR328C; -.
NMPDR fig|4932.3.peg.1381; -.
Phylogenomic databases
HOGENOM P52286; -.
Other
LinkHub P52286; -.
NextBio 969983; -.
ProtoNet P52286.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Chromosomal protein; Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding; Kinetochore; Nucleus; Phosphoprotein; Ubl conjugation pathway.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   194  193     Suppressor of kinetochore protein 1. PRO_0000187257
COMPBIAS   66    74  9     Asp/Glu-rich (highly acidic). 
MOD_RES   4     4        Phosphoserine. 
MOD_RES   177   177        Phosphothreonine. 
CONFLICT   48    48        E -> D (in Ref. 2; AAC49492). 
STRAND   5     9  5      
STRAND   15    19  5      
HELIX   20    23  4      
HELIX   27    31  5      
STRAND   76    78  3      
HELIX   84    96  13      
TURN   97    99  3      
HELIX   118   123  6      
HELIX   128   141  14      
HELIX   144   158  15      
HELIX   163   170  8      
HELIX   178   182  5      
Sequence information
Length: 194 AA [This is the length of the unprocessed precursor] Molecular weight: 22330 Da [This is the MW of the unprocessed precursor] CRC64: 746DDE6470A69432 [This is a checksum on the sequence]
        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 

P52286 in FASTA format

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