SKP1_YEAST
ID SKP1_YEAST Reviewed; 194 AA.
AC P52286; D6VSW0; Q07186;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Suppressor of kinetochore protein 1;
DE AltName: Full=Centromere DNA-binding protein complex CBF3 subunit D;
DE AltName: Full=E3 ubiquitin ligase complex SCF subunit SKP1;
GN Name=SKP1; Synonyms=CBF3D; OrderedLocusNames=YDR328C; ORFNames=D9798.14;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8706132; DOI=10.1016/s0092-8674(00)80099-9;
RA Connelly C., Hieter P.;
RT "Budding yeast SKP1 encodes an evolutionarily conserved kinetochore protein
RT required for cell cycle progression.";
RL Cell 86:275-285(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH CDC4.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8706131; DOI=10.1016/s0092-8674(00)80098-7;
RA Bai C., Sen P., Hofmann K., Ma L., Goebl M., Harper J.W., Elledge S.J.;
RT "SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery
RT through a novel motif, the F-box.";
RL Cell 86:263-274(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP PROTEIN SEQUENCE OF 2-24, AND CHARACTERIZATION.
RX PubMed=8670864; DOI=10.1002/j.1460-2075.1996.tb00730.x;
RA Stemmann O., Lechner J.;
RT "The Saccharomyces cerevisiae kinetochore contains a cyclin-CDK complexing
RT homologue, as identified by in vitro reconstitution.";
RL EMBO J. 15:3611-3620(1996).
RN [7]
RP FUNCTION, AND SUBUNIT.
RX PubMed=9346238; DOI=10.1016/s0092-8674(00)80403-1;
RA Skowyra D., Craig K.L., Tyers M., Elledge S.J., Harper J.W.;
RT "F-box proteins are receptors that recruit phosphorylated substrates to the
RT SCF ubiquitin-ligase complex.";
RL Cell 91:209-219(1997).
RN [8]
RP FUNCTION, AND SUBUNIT.
RX PubMed=9346239; DOI=10.1016/s0092-8674(00)80404-3;
RA Feldman R.M., Correll C.C., Kaplan K.B., Deshaies R.J.;
RT "A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of
RT the phosphorylated CDK inhibitor Sic1p.";
RL Cell 91:221-230(1997).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-177, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-177, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [11]
RP FUNCTION, AND INTERACTION WITH ROY1.
RX PubMed=21389113; DOI=10.1091/mbc.e10-08-0716;
RA Liu Y., Nakatsukasa K., Kotera M., Kanada A., Nishimura T., Kishi T.,
RA Mimura S., Kamura T.;
RT "Non-SCF-type F-box protein Roy1/Ymr258c interacts with a Rab5-like GTPase
RT Ypt52 and inhibits Ypt52 function.";
RL Mol. Biol. Cell 22:1575-1584(2011).
RN [12]
RP FUNCTION, AND INTERACTION WITH MET30 AND CDC53.
RX PubMed=9499404; DOI=10.1101/gad.12.5.692;
RA Patton E.E., Willems A.R., Sa D., Kuras L., Thomas D., Craig K.L.,
RA Tyers M.;
RT "Cdc53 is a scaffold protein for multiple Cdc34/Skp1/F-box protein
RT complexes that regulate cell division and methionine biosynthesis in
RT yeast.";
RL Genes Dev. 12:692-705(1998).
RN [13]
RP SUBUNIT.
RX PubMed=10637232; DOI=10.1093/emboj/19.2.282;
RA Rouillon A., Barbey R., Patton E.E., Tyers M., Thomas D.;
RT "Feedback-regulated degradation of the transcriptional activator Met4 is
RT triggered by the SCF(Met30) complex.";
RL EMBO J. 19:282-294(2000).
RN [14]
RP INTERACTION WITH RCY1.
RX PubMed=11287615; DOI=10.1128/mcb.21.9.3105-3117.2001;
RA Galan J.M., Wiederkehr A., Seol J.H., Haguenauer-Tsapis R., Deshaies R.J.,
RA Riezman H., Peter M.;
RT "Skp1p and the F-box protein Rcy1p form a non-SCF complex involved in
RT recycling of the SNARE Snc1p in yeast.";
RL Mol. Cell. Biol. 21:3105-3117(2001).
RN [15]
RP IDENTIFICATION IN THE RAVE COMPLEX WITH RAV1 AND RAV2.
RX PubMed=11283612; DOI=10.1038/35070067;
RA Seol J.H., Shevchenko A., Shevchenko A., Deshaies R.J.;
RT "Skp1 forms multiple protein complexes, including RAVE, a regulator of V-
RT ATPase assembly.";
RL Nat. Cell Biol. 3:384-391(2001).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 7-166.
RX PubMed=12553912; DOI=10.1016/s0092-8674(03)00034-5;
RA Orlicky S., Tang X., Willems A., Tyers M., Sicheri F.;
RT "Structural basis for phosphodependent substrate selection and orientation
RT by the SCFCdc4 ubiquitin ligase.";
RL Cell 112:243-256(2003).
RN [18]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [19]
RP INTERACTION WITH MET30.
RX PubMed=14660673; DOI=10.1074/jbc.m308875200;
RA Brunson L.E., Dixon C., Kozubowski L., Mathias N.;
RT "The amino-terminal portion of the F-box protein Met30p mediates its
RT nuclear import and assimilation into an SCF complex.";
RL J. Biol. Chem. 279:6674-6682(2004).
RN [20]
RP ASSEMBLY OF THE CBF3 COMPLEX, AND INTERACTION WITH CBF3C AND SGT1.
RX PubMed=15090617; DOI=10.1091/mbc.e03-12-0887;
RA Rodrigo-Brenni M.C., Thomas S., Bouck D.C., Kaplan K.B.;
RT "Sgt1p and Skp1p modulate the assembly and turnover of CBF3 complexes
RT required for proper kinetochore function.";
RL Mol. Biol. Cell 15:3366-3378(2004).
RN [21]
RP FUNCTION, AND IDENTIFICATION IN THE SCF(SAF1) COMPLEX.
RX PubMed=17517885; DOI=10.1074/jbc.m702425200;
RA Escusa S., Laporte D., Massoni A., Boucherie H., Dautant A.,
RA Daignan-Fornier B.;
RT "Skp1-Cullin-F-box-dependent degradation of Aah1p requires its interaction
RT with the F-box protein Saf1p.";
RL J. Biol. Chem. 282:20097-20103(2007).
CC -!- FUNCTION: Essential component of the E3 ubiquitin ligase complex SCF
CC (SKP1-CUL1-F-box protein) ubiquitin ligase complex, which mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins like phosphorylated SIC1. Participates in the attachment of
CC chromosomes to the spindle. Acts as a regulatory component of the
CC centromere DNA-binding protein complex CBF3, which is essential for
CC chromosome segregation and movement of centromeres along microtubules.
CC CBF3 is required for the recruitment of other kinetochore complexes to
CC CEN DNA. It plays a role in the attachment of chromosomes to the
CC spindle and binds selectively to a highly conserved DNA sequence called
CC CDEIII, found in centromeres and in several promoters. The association
CC of CBF3C with CBF3D and SGT1 is required for CBF3C activation and CBF3
CC assembly. SKP1/CBF3D could retrieve cyclins or cyclin-CDK-like proteins
CC into the kinetochore thus providing cell cycle-regulated kinetochore
CC activity. Involved in the regulation of methionine biosynthesis genes.
CC Facilitates association of CDC53 with CDC4 and of ROY1 with YPT52.
CC {ECO:0000269|PubMed:17517885, ECO:0000269|PubMed:21389113,
CC ECO:0000269|PubMed:8706131, ECO:0000269|PubMed:8706132,
CC ECO:0000269|PubMed:9346238, ECO:0000269|PubMed:9346239,
CC ECO:0000269|PubMed:9499404}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the E3 ubiquitin ligase complexes SCF with HRT1,
CC some cullins like CDC53, and some F-box proteins like MET30 CDC4 and
CC SAF1. Interacts with CDC53 and MET30 to form the E3 ubiquitin ligase
CC complex SCF(Met30) which also contains MET4. Forms complex SCF(Cdc4)
CC together with CDC4 and CDC53. Component of the CBF3 complex, which is
CC formed of CBF3A/CBF2, CBF3B/CEP3, CBF3C/CTF13 and CBF3D. Component of
CC the RAVE complex composed of RAV1, RAV2 and SKP1/CBF3D. Interacts with
CC RCY1, ROY1, CBF3D and SGT1. {ECO:0000269|PubMed:10637232,
CC ECO:0000269|PubMed:11283612, ECO:0000269|PubMed:11287615,
CC ECO:0000269|PubMed:14660673, ECO:0000269|PubMed:15090617,
CC ECO:0000269|PubMed:17517885, ECO:0000269|PubMed:21389113,
CC ECO:0000269|PubMed:8706131, ECO:0000269|PubMed:9346238,
CC ECO:0000269|PubMed:9346239, ECO:0000269|PubMed:9499404}.
CC -!- INTERACTION:
CC P52286; Q06150: BOP2; NbExp=3; IntAct=EBI-4090, EBI-34293;
CC P52286; P07834: CDC4; NbExp=14; IntAct=EBI-4090, EBI-4434;
CC P52286; Q12018: CDC53; NbExp=29; IntAct=EBI-4090, EBI-4321;
CC P52286; P35203: CTF13; NbExp=8; IntAct=EBI-4090, EBI-4085;
CC P52286; P47005: DAS1; NbExp=4; IntAct=EBI-4090, EBI-26114;
CC P52286; Q08496: DIA2; NbExp=4; IntAct=EBI-4090, EBI-31943;
CC P52286; P32324: EFT2; NbExp=2; IntAct=EBI-4090, EBI-6333;
CC P52286; P24814: GRR1; NbExp=9; IntAct=EBI-4090, EBI-7898;
CC P52286; Q12347: HRT3; NbExp=5; IntAct=EBI-4090, EBI-30029;
CC P52286; Q05930: MDM30; NbExp=5; IntAct=EBI-4090, EBI-31799;
CC P52286; P39014: MET30; NbExp=14; IntAct=EBI-4090, EBI-11507;
CC P52286; P47104: RAV1; NbExp=5; IntAct=EBI-4090, EBI-25471;
CC P52286; P39531: RCY1; NbExp=4; IntAct=EBI-4090, EBI-26224;
CC P52286; Q04847: ROY1; NbExp=4; IntAct=EBI-4090, EBI-27556;
CC P52286; P38352: SAF1; NbExp=4; IntAct=EBI-4090, EBI-21172;
CC P52286; Q08446: SGT1; NbExp=8; IntAct=EBI-4090, EBI-17070;
CC P52286; P42843: SKP2; NbExp=5; IntAct=EBI-4090, EBI-28370;
CC P52286; P47822: SRB7; NbExp=2; IntAct=EBI-4090, EBI-18046;
CC P52286; Q05947: UCC1; NbExp=4; IntAct=EBI-4090, EBI-33647;
CC P52286; Q04511: UFO1; NbExp=6; IntAct=EBI-4090, EBI-20020;
CC P52286; Q03899: YDR131C; NbExp=4; IntAct=EBI-4090, EBI-36201;
CC P52286; Q06640: YDR306C; NbExp=3; IntAct=EBI-4090, EBI-34097;
CC P52286; Q06479: YLR352W; NbExp=3; IntAct=EBI-4090, EBI-35627;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}. Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:14562095}.
CC -!- SIMILARITY: Belongs to the SKP1 family. {ECO:0000305}.
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DR EMBL; U43179; AAB17500.1; -; Genomic_DNA.
DR EMBL; U61764; AAC49492.1; -; mRNA.
DR EMBL; U32517; AAB64763.1; -; Genomic_DNA.
DR EMBL; AY557730; AAS56056.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12170.1; -; Genomic_DNA.
DR PIR; S59793; S59793.
DR RefSeq; NP_010615.3; NM_001180636.3.
DR PDB; 1NEX; X-ray; 2.70 A; A/C=1-194.
DR PDB; 3MKS; X-ray; 2.60 A; A/C=2-194.
DR PDB; 3V7D; X-ray; 2.31 A; A/C=1-194.
DR PDB; 5AN3; X-ray; 2.82 A; D=1-35, D=65-158.
DR PDB; 6F07; EM; 3.60 A; D=1-194.
DR PDB; 6FE8; EM; 3.70 A; C=2-194.
DR PDB; 6GSA; EM; 4.20 A; C=2-194.
DR PDB; 6GYP; EM; 3.60 A; D=1-194.
DR PDB; 6GYS; EM; 4.40 A; D/K=1-194.
DR PDB; 6GYU; EM; 3.00 A; D=1-194.
DR PDB; 7K79; EM; 4.00 A; N=1-194.
DR PDB; 7PMN; EM; 3.20 A; K=1-194.
DR PDBsum; 1NEX; -.
DR PDBsum; 3MKS; -.
DR PDBsum; 3V7D; -.
DR PDBsum; 5AN3; -.
DR PDBsum; 6F07; -.
DR PDBsum; 6FE8; -.
DR PDBsum; 6GSA; -.
DR PDBsum; 6GYP; -.
DR PDBsum; 6GYS; -.
DR PDBsum; 6GYU; -.
DR PDBsum; 7K79; -.
DR PDBsum; 7PMN; -.
DR AlphaFoldDB; P52286; -.
DR SMR; P52286; -.
DR BioGRID; 32385; 153.
DR ComplexPortal; CPX-1627; RAVE complex.
DR ComplexPortal; CPX-1898; CBF3 complex.
DR ComplexPortal; CPX-3234; SCF-Cdc4 ubiquitin ligase complex.
DR ComplexPortal; CPX-3241; SCF-Grr1 ubiquitin ligase complex.
DR ComplexPortal; CPX-3242; SCF-Mdm30 ubiquitin ligase complex.
DR ComplexPortal; CPX-3243; SCF-Ufo1 ubiquitin ligase complex.
DR ComplexPortal; CPX-3244; SCF-Das1 ubiquitin ligase complex.
DR ComplexPortal; CPX-3249; SCF-Met30 ubiquitin ligase complex.
DR ComplexPortal; CPX-3250; SCF-Dia2 ubiquitin ligase complex.
DR ComplexPortal; CPX-3253; SCF-Ylr352w ubiquitin ligase complex.
DR ComplexPortal; CPX-3254; SCF-Saf1 ubiquitin ligase complex.
DR ComplexPortal; CPX-3255; SCF-Hrt3 ubiquitin ligase complex.
DR ComplexPortal; CPX-3681; SCF-Ydr131c ubiquitin ligase complex.
DR DIP; DIP-1236N; -.
DR IntAct; P52286; 81.
DR MINT; P52286; -.
DR STRING; 4932.YDR328C; -.
DR MoonDB; P52286; Predicted.
DR iPTMnet; P52286; -.
DR MaxQB; P52286; -.
DR PaxDb; P52286; -.
DR PRIDE; P52286; -.
DR EnsemblFungi; YDR328C_mRNA; YDR328C; YDR328C.
DR GeneID; 851928; -.
DR KEGG; sce:YDR328C; -.
DR SGD; S000002736; SKP1.
DR VEuPathDB; FungiDB:YDR328C; -.
DR eggNOG; KOG1724; Eukaryota.
DR GeneTree; ENSGT00390000012652; -.
DR HOGENOM; CLU_059252_4_0_1; -.
DR InParanoid; P52286; -.
DR OMA; PLKSADM; -.
DR BioCyc; YEAST:G3O-29884-MON; -.
DR Reactome; R-SCE-68949; Orc1 removal from chromatin.
DR Reactome; R-SCE-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR ChiTaRS; SKP1; yeast.
DR EvolutionaryTrace; P52286; -.
DR PRO; PR:P52286; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P52286; protein.
DR GO; GO:0031518; C:CBF3 complex; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0012505; C:endomembrane system; IC:ComplexPortal.
DR GO; GO:0000776; C:kinetochore; IDA:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0043291; C:RAVE complex; IPI:SGD.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:SGD.
DR GO; GO:0097602; F:cullin family protein binding; IBA:GO_Central.
DR GO; GO:0003688; F:DNA replication origin binding; IDA:SGD.
DR GO; GO:0071406; P:cellular response to methylmercury; IC:ComplexPortal.
DR GO; GO:0010458; P:exit from mitosis; IMP:SGD.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IDA:ComplexPortal.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:SGD.
DR GO; GO:0051382; P:kinetochore assembly; IDA:SGD.
DR GO; GO:0008053; P:mitochondrial fusion; IC:ComplexPortal.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IC:ComplexPortal.
DR GO; GO:2000766; P:negative regulation of cytoplasmic translation; IMP:SGD.
DR GO; GO:0010828; P:positive regulation of glucose transmembrane transport; IDA:ComplexPortal.
DR GO; GO:0045116; P:protein neddylation; IMP:SGD.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:SGD.
DR GO; GO:0007096; P:regulation of exit from mitosis; IMP:SGD.
DR GO; GO:0019222; P:regulation of metabolic process; IC:ComplexPortal.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0043254; P:regulation of protein-containing complex assembly; IPI:SGD.
DR GO; GO:0031335; P:regulation of sulfur amino acid metabolic process; IC:ComplexPortal.
DR GO; GO:0000409; P:regulation of transcription by galactose; IC:ComplexPortal.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:SGD.
DR GO; GO:0000921; P:septin ring assembly; IMP:SGD.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IDA:ComplexPortal.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:SGD.
DR GO; GO:0007035; P:vacuolar acidification; IMP:SGD.
DR GO; GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; IDA:ComplexPortal.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR016897; SKP1.
DR InterPro; IPR001232; SKP1-like.
DR InterPro; IPR036296; SKP1-like_dim_sf.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR016072; Skp1_comp_dimer.
DR InterPro; IPR016073; Skp1_comp_POZ.
DR PANTHER; PTHR11165; PTHR11165; 1.
DR Pfam; PF01466; Skp1; 1.
DR Pfam; PF03931; Skp1_POZ; 2.
DR PIRSF; PIRSF028729; E3_ubiquit_lig_SCF_Skp; 1.
DR SMART; SM00512; Skp1; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF81382; SSF81382; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Centromere; Chromosome; Cytoplasm; Direct protein sequencing;
KW DNA-binding; Kinetochore; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8670864"
FT CHAIN 2..194
FT /note="Suppressor of kinetochore protein 1"
FT /id="PRO_0000187257"
FT REGION 38..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..194
FT /note="Interaction with the F-box domain of F-box proteins"
FT /evidence="ECO:0000250"
FT COMPBIAS 50..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 177
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CONFLICT 48
FT /note="E -> D (in Ref. 2; AAC49492)"
FT /evidence="ECO:0000305"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:6GYU"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:3V7D"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:3V7D"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:3V7D"
FT HELIX 84..96
FT /evidence="ECO:0007829|PDB:3V7D"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:3V7D"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:6GYU"
FT HELIX 118..123
FT /evidence="ECO:0007829|PDB:3V7D"
FT HELIX 128..140
FT /evidence="ECO:0007829|PDB:3V7D"
FT HELIX 144..158
FT /evidence="ECO:0007829|PDB:3V7D"
FT HELIX 163..170
FT /evidence="ECO:0007829|PDB:3V7D"
FT HELIX 178..185
FT /evidence="ECO:0007829|PDB:3V7D"
FT TURN 188..191
FT /evidence="ECO:0007829|PDB:6GYU"
SQ SEQUENCE 194 AA; 22330 MW; 746DDE6470A69432 CRC64;
MVTSNVVLVS GEGERFTVDK KIAERSLLLK NYLNDMHDSN LQNNSDSESD SDSETNHKSK
DNNNGDDDDE DDDEIVMPVP NVRSSVLQKV IEWAEHHRDS NFPDEDDDDS RKSAPVDSWD
REFLKVDQEM LYEIILAANY LNIKPLLDAG CKVVAEMIRG RSPEEIRRTF NIVNDFTPEE
EAAIRRENEW AEDR
