ID SGT1_YEAST Reviewed; 395 AA. AC Q08446; D6W2C0; E9P8U7; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 186. DE RecName: Full=Protein SGT1 {ECO:0000303|PubMed:10445024, ECO:0000303|PubMed:12456005}; DE AltName: Full=Suppressor of G2 allele of SKP1 {ECO:0000303|PubMed:10445024}; GN Name=SGT1 {ECO:0000312|SGD:S000005583}; OrderedLocusNames=YOR057W; GN ORFNames=YOR29-08; 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]. RX PubMed=9133743; RX DOI=10.1002/(sici)1097-0061(19970330)13:4<379::aid-yea85>3.0.co;2-g; RA Valens M., Bohn C., Daignan-Fornier B., Dang V.-D., Bolotin-Fukuhara M.; RT "The sequence of a 54.7 kb fragment of yeast chromosome XV reveals the RT presence of two tRNAs and 24 new open reading frames."; RL Yeast 13:379-390(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169874; RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."; RL Nature 387:98-102(1997). RN [3] 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 [4] 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 [5] RP FUNCTION, INTERACTION WITH SKP1, INTERACTION WITH THE SCF COMPLEX, AND RP MUTANTS SGT1-3 AND SGT1-5. RX PubMed=10445024; DOI=10.1016/s1097-2765(00)80184-7; RA Kitagawa K., Skowyra D., Elledge S.J., Harper J.W., Hieter P.; RT "SGT1 encodes an essential component of the yeast kinetochore assembly RT pathway and a novel subunit of the SCF ubiquitin ligase complex."; RL Mol. Cell 4:21-33(1999). RN [6] RP FUNCTION, INTERACTION WITH CIR1, AND MUTANT A364A. RX PubMed=12456005; DOI=10.1128/ec.1.4.568-582.2002; RA Dubacq C., Guerois R., Courbeyrette R., Kitagawa K., Mann C.; RT "Sgt1p contributes to cyclic AMP pathway activity and physically interacts RT with the adenylyl cyclase Cyr1p/Cdc35p in budding yeast."; RL Eukaryot. Cell 1:568-582(2002). RN [7] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168 AND SER-171, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ADR376; RX PubMed=17330950; DOI=10.1021/pr060559j; RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., RA Elias J.E., Gygi S.P.; RT "Large-scale phosphorylation analysis of alpha-factor-arrested RT Saccharomyces cerevisiae."; RL J. Proteome Res. 6:1190-1197(2007). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168 AND SER-171, AND RP IDENTIFICATION BY 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 SER-168 AND SER-171, AND RP IDENTIFICATION BY 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 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-32, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22106047; DOI=10.1002/pmic.201100166; RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.; RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae."; RL Proteomics 12:236-240(2012). CC -!- FUNCTION: Involved in ubiquitination and subsequent proteasomal CC degradation of target proteins. Required for both entry into S phase CC and kinetochore function. Also involved in cyclic AMP (cAMP) pathway, CC possibly by participating in the assembly or the conformational CC activation of specific multiprotein complexes. CC {ECO:0000269|PubMed:10445024, ECO:0000269|PubMed:12456005}. CC -!- SUBUNIT: Interacts with SKP1/CBF3D. Part of SCF E3 ubiquitin ligase CC complexes containing SKP1, CDC53, HRT1 and some F-box proteins. CC Interacts with CIR1/CDC35. {ECO:0000269|PubMed:10445024, CC ECO:0000269|PubMed:12456005}. CC -!- INTERACTION: CC Q08446; P35203: CTF13; NbExp=3; IntAct=EBI-17070, EBI-4085; CC Q08446; P02829: HSP82; NbExp=2; IntAct=EBI-17070, EBI-8659; CC Q08446; P52286: SKP1; NbExp=8; IntAct=EBI-17070, EBI-4090; CC -!- MISCELLANEOUS: Present with 1340 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the SGT1 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U88830; AAB48841.1; -; Genomic_DNA. DR EMBL; Z70678; CAA94542.1; -; Genomic_DNA. DR EMBL; Z74965; CAA99250.1; -; Genomic_DNA. DR EMBL; AY558043; AAS56369.1; -; Genomic_DNA. DR EMBL; BK006948; DAA10836.1; -; Genomic_DNA. DR PIR; S66940; S66940. DR RefSeq; NP_014700.1; NM_001183476.1. DR PDB; 5AN3; X-ray; 2.82 A; A/B/C=1-150. DR PDBsum; 5AN3; -. DR AlphaFoldDB; Q08446; -. DR SMR; Q08446; -. DR BioGRID; 34455; 679. DR DIP; DIP-1628N; -. DR IntAct; Q08446; 10. DR MINT; Q08446; -. DR STRING; 4932.YOR057W; -. DR GlyGen; Q08446; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; Q08446; -. DR MaxQB; Q08446; -. DR PaxDb; 4932-YOR057W; -. DR PeptideAtlas; Q08446; -. DR EnsemblFungi; YOR057W_mRNA; YOR057W; YOR057W. DR GeneID; 854222; -. DR KEGG; sce:YOR057W; -. DR AGR; SGD:S000005583; -. DR SGD; S000005583; SGT1. DR VEuPathDB; FungiDB:YOR057W; -. DR eggNOG; KOG1309; Eukaryota. DR GeneTree; ENSGT00940000173366; -. DR HOGENOM; CLU_039532_3_0_1; -. DR InParanoid; Q08446; -. DR OMA; KIREDWY; -. DR OrthoDB; 5479399at2759; -. DR BioCyc; YEAST:G3O-33597-MONOMER; -. DR Reactome; R-SCE-844456; The NLRP3 inflammasome. DR BioGRID-ORCS; 854222; 4 hits in 10 CRISPR screens. DR PRO; PR:Q08446; -. DR Proteomes; UP000002311; Chromosome XV. DR RNAct; Q08446; Protein. DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:SGD. DR GO; GO:0051087; F:protein-folding chaperone binding; IDA:SGD. DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:SGD. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051382; P:kinetochore assembly; IDA:SGD. DR GO; GO:0065003; P:protein-containing complex assembly; IDA:SGD. DR CDD; cd06466; p23_CS_SGT1_like; 1. DR Gene3D; 2.60.40.790; -; 1. DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1. DR InterPro; IPR007052; CS_dom. DR InterPro; IPR008978; HSP20-like_chaperone. DR InterPro; IPR007699; SGS_dom. DR InterPro; IPR044563; Sgt1-like. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR PANTHER; PTHR45862; PROTEIN SGT1 HOMOLOG; 1. DR PANTHER; PTHR45862:SF1; PROTEIN SGT1 HOMOLOG; 1. DR Pfam; PF04969; CS; 1. DR Pfam; PF05002; SGS; 1. DR SUPFAM; SSF49764; HSP20-like chaperones; 1. DR SUPFAM; SSF48452; TPR-like; 1. DR PROSITE; PS51203; CS; 1. DR PROSITE; PS51048; SGS; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell cycle; Isopeptide bond; Phosphoprotein; KW Reference proteome; Ubl conjugation; Ubl conjugation pathway. FT CHAIN 1..395 FT /note="Protein SGT1" FT /id="PRO_0000185393" FT DOMAIN 182..277 FT /note="CS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547" FT DOMAIN 312..395 FT /note="SGS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00386" FT REGION 137..175 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 373..395 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 137..156 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 157..175 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 168 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198" FT MOD_RES 171 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198" FT CROSSLNK 32 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0007744|PubMed:22106047" FT MUTAGEN 31 FT /note="L->P: In sgt1-3; induces arrest of cell division in FT G2/M; when associated with L-99 and I-213." FT MUTAGEN 99 FT /note="F->L: In sgt1-3; induces arrest of cell division in FT G2/M; when associated with P-31 I-213." FT MUTAGEN 213 FT /note="N->I: In sgt1-3; induces arrest of cell division in FT G2/M; when associated with P-31 and L-99." FT MUTAGEN 220 FT /note="D->V: In sgt1-5; induces arrest of cell division in FT G2/M; when associated with K-364." FT MUTAGEN 364 FT /note="E->K: In sgt1-5; induces arrest of cell division in FT G2/M; when associated with V-220." FT MUTAGEN 371 FT /note="S->N: In A364a; suppressor of the cdc35-1 allele." FT CONFLICT 13 FT /note="A -> T (in Ref. 4; AAS56369)" FT /evidence="ECO:0000305" FT HELIX 4..15 FT /evidence="ECO:0007829|PDB:5AN3" FT HELIX 20..33 FT /evidence="ECO:0007829|PDB:5AN3" FT HELIX 38..52 FT /evidence="ECO:0007829|PDB:5AN3" FT HELIX 56..58 FT /evidence="ECO:0007829|PDB:5AN3" FT HELIX 61..79 FT /evidence="ECO:0007829|PDB:5AN3" FT HELIX 84..100 FT /evidence="ECO:0007829|PDB:5AN3" FT HELIX 104..116 FT /evidence="ECO:0007829|PDB:5AN3" FT HELIX 124..133 FT /evidence="ECO:0007829|PDB:5AN3" SQ SEQUENCE 395 AA; 44860 MW; 5DE65874BE155552 CRC64; MPVEKDLKTA YKALYDEKEP LKALHLYDEI LKGSPTNLTA LIFKAACLEK LYFGFSDWHS DATMENAKEL LDKALMTAEG RGDRSKIGLV NFRYFVHFFN IKDYELAQSY FKKAKNLGYV DDTLPLWEDR LETKLNKKNK KQKDSTNKHT IKPVESIENR GDNNSSHSPI SPLKIETAPQ ESPKFKIDWY QSSTSVTISL FTVNLPESKE QVNIYISPND RRTLSISYQV PKSGSEFQYN AKLSHEVDPK AVSLKIFPKK LEITLSKIDS TQWKKLEEDI LTESSRLSDE GKNSDSATRL LSAETASKER LSYPSSSKKK IDWSKLDIDE EADEEAGSAD SFFQKLYAGA DPDTKRAMMK SFIESNGTAL STDWEDVSKG TVKTSPPEGM EPKHW //