SGT1_YEAST
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 03-AUG-2022, entry version 180.
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}.
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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; 676.
DR DIP; DIP-1628N; -.
DR IntAct; Q08446; 10.
DR MINT; Q08446; -.
DR STRING; 4932.YOR057W; -.
DR iPTMnet; Q08446; -.
DR MaxQB; Q08446; -.
DR PaxDb; Q08446; -.
DR PRIDE; Q08446; -.
DR EnsemblFungi; YOR057W_mRNA; YOR057W; YOR057W.
DR GeneID; 854222; -.
DR KEGG; sce:YOR057W; -.
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; WYQSHDS; -.
DR BioCyc; YEAST:G3O-33597-MON; -.
DR Reactome; R-SCE-844456; The NLRP3 inflammasome.
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: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:0050821; P:protein stabilization; IBA:GO_Central.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:SGD.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 2.60.40.790; -; 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; PTHR45862; 1.
DR Pfam; PF04969; CS; 1.
DR Pfam; PF05002; SGS; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF49764; SSF49764; 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
