SGT2_YEAST
ID SGT2_YEAST Reviewed; 346 AA.
AC Q12118; D6W273;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Small glutamine-rich tetratricopeptide repeat-containing protein 2;
DE AltName: Full=SGT/UBP;
DE AltName: Full=Viral protein U-binding protein;
GN Name=SGT2; OrderedLocusNames=YOR007C; ORFNames=UNF346;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=8896276;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1091::aid-yea22>3.0.co;2-i;
RA Sterky F., Holmberg A., Pettersson B., Uhlen M.;
RT "The sequence of a 30 kb fragment on the left arm of chromosome XV from
RT Saccharomyces cerevisiae reveals 15 open reading frames, five of which
RT correspond to previously identified genes.";
RL Yeast 12:1091-1095(1996).
RN [2]
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 [3]
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 [4]
RP PROTEIN SEQUENCE OF 131-142 AND 158-171, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (JUN-2005) to UniProtKB.
RN [5]
RP FUNCTION.
RX PubMed=12482202; DOI=10.1379/1466-1268(2002)007<0258:sgrpvp>2.0.co;2;
RA Angeletti P.C., Walker D., Panganiban A.T.;
RT "Small glutamine-rich protein/viral protein U-binding protein is a novel
RT cochaperone that affects heat shock protein 70 activity.";
RL Cell Stress Chaperones 7:258-268(2002).
RN [6]
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 [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 INTERACTION WITH HSC82; HSP104; MDY2; SSA1 AND SSA2.
RX PubMed=17441508; DOI=10.1379/csc-220r.1;
RA Liou S.-T., Cheng M.-Y., Wang C.;
RT "SGT2 and MDY2 interact with molecular chaperone YDJ1 in Saccharomyces
RT cerevisiae.";
RL Cell Stress Chaperones 12:59-70(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-308, 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 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).
CC -!- FUNCTION: Co-chaperone that binds to the molecular chaperone Hsp70
CC (SSA1 and SSA2). Regulates Hsp70 ATPase activity (By similarity).
CC Required for recovery from heat shock. {ECO:0000250,
CC ECO:0000269|PubMed:12482202}.
CC -!- SUBUNIT: Interacts with HSC82, HSP104, MDY2, SSA1 AND SSA2.
CC {ECO:0000269|PubMed:17441508}.
CC -!- INTERACTION:
CC Q12118; P40515: FIS1; NbExp=3; IntAct=EBI-31784, EBI-25059;
CC Q12118; Q12125: GET4; NbExp=5; IntAct=EBI-31784, EBI-36940;
CC Q12118; Q12285: MDY2; NbExp=15; IntAct=EBI-31784, EBI-34904;
CC Q12118; P22214: SEC22; NbExp=4; IntAct=EBI-31784, EBI-16577;
CC Q12118; Q12118: SGT2; NbExp=4; IntAct=EBI-31784, EBI-31784;
CC Q12118; P25491: YDJ1; NbExp=2; IntAct=EBI-31784, EBI-10420;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 9424 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SGT family. {ECO:0000305}.
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DR EMBL; U43491; AAC49487.1; -; Genomic_DNA.
DR EMBL; Z74915; CAA99195.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10789.1; -; Genomic_DNA.
DR PIR; S61991; S61991.
DR RefSeq; NP_014649.1; NM_001183426.1.
DR PDB; 2LXB; NMR; -; A/B=2-72.
DR PDB; 2LXC; NMR; -; B/C=2-72.
DR PDB; 3ZDM; X-ray; 1.80 A; A/B/D/E=1-72.
DR PDB; 4ASV; NMR; -; A/B=1-78.
DR PDB; 4ASW; NMR; -; A/B=1-78.
DR PDB; 5LYN; X-ray; 2.00 A; A/B=96-225.
DR PDB; 5LYP; X-ray; 1.55 A; A=93-229.
DR PDBsum; 2LXB; -.
DR PDBsum; 2LXC; -.
DR PDBsum; 3ZDM; -.
DR PDBsum; 4ASV; -.
DR PDBsum; 4ASW; -.
DR PDBsum; 5LYN; -.
DR PDBsum; 5LYP; -.
DR AlphaFoldDB; Q12118; -.
DR BMRB; Q12118; -.
DR SMR; Q12118; -.
DR BioGRID; 34410; 267.
DR ComplexPortal; CPX-1861; GET4-GET5 transmembrane domain recognition complex.
DR DIP; DIP-1983N; -.
DR IntAct; Q12118; 19.
DR MINT; Q12118; -.
DR STRING; 4932.YOR007C; -.
DR TCDB; 3.A.21.1.1; the c-terminal tail-anchored membrane protein biogenesis/ insertion complex (tamp-b) family.
DR iPTMnet; Q12118; -.
DR MaxQB; Q12118; -.
DR PaxDb; Q12118; -.
DR PRIDE; Q12118; -.
DR EnsemblFungi; YOR007C_mRNA; YOR007C; YOR007C.
DR GeneID; 854168; -.
DR KEGG; sce:YOR007C; -.
DR SGD; S000005533; SGT2.
DR VEuPathDB; FungiDB:YOR007C; -.
DR eggNOG; KOG0553; Eukaryota.
DR HOGENOM; CLU_044224_1_0_1; -.
DR InParanoid; Q12118; -.
DR OMA; ASGQHEK; -.
DR BioCyc; YEAST:G3O-33557-MON; -.
DR Reactome; R-SCE-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR PRO; PR:Q12118; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12118; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0072380; C:TRC complex; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0060090; F:molecular adaptor activity; IMP:SGD.
DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0009408; P:response to heat; IMP:SGD.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR032374; SGTA_dimer.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF16546; SGTA_dimer; 1.
DR Pfam; PF00515; TPR_1; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Direct protein sequencing;
KW Phosphoprotein; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..346
FT /note="Small glutamine-rich tetratricopeptide repeat-
FT containing protein 2"
FT /id="PRO_0000106370"
FT REPEAT 102..135
FT /note="TPR 1"
FT REPEAT 136..169
FT /note="TPR 2"
FT REPEAT 170..203
FT /note="TPR 3"
FT REPEAT 205..229
FT /note="TPR 4"
FT REGION 219..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 308
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT HELIX 5..21
FT /evidence="ECO:0007829|PDB:3ZDM"
FT HELIX 27..44
FT /evidence="ECO:0007829|PDB:3ZDM"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:3ZDM"
FT HELIX 51..56
FT /evidence="ECO:0007829|PDB:3ZDM"
FT HELIX 58..68
FT /evidence="ECO:0007829|PDB:3ZDM"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:2LXB"
FT HELIX 96..114
FT /evidence="ECO:0007829|PDB:5LYP"
FT HELIX 118..131
FT /evidence="ECO:0007829|PDB:5LYP"
FT HELIX 136..148
FT /evidence="ECO:0007829|PDB:5LYP"
FT HELIX 152..165
FT /evidence="ECO:0007829|PDB:5LYP"
FT HELIX 170..182
FT /evidence="ECO:0007829|PDB:5LYP"
FT HELIX 186..200
FT /evidence="ECO:0007829|PDB:5LYP"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:5LYP"
FT HELIX 206..224
FT /evidence="ECO:0007829|PDB:5LYP"
SQ SEQUENCE 346 AA; 37218 MW; 33539B74F742BD3C CRC64;
MSASKEEIAA LIVNYFSSIV EKKEISEDGA DSLNVAMDCI SEAFGFEREA VSGILGKSEF
KGQHLADILN SASRVPESNK KDDAENVEIN IPEDDAETKA KAEDLKMQGN KAMANKDYEL
AINKYTEAIK VLPTNAIYYA NRAAAHSSLK EYDQAVKDAE SAISIDPSYF RGYSRLGFAK
YAQGKPEEAL EAYKKVLDIE GDNATEAMKR DYESAKKKVE QSLNLEKTVP EQSRDADVDA
SQGASAGGLP DLGSLLGGGL GGLMNNPQLM QAAQKMMSNP GAMQNIQKMM QDPSIRQMAE
GFASGGGTPN LSDLMNNPAL RNMAGNLFGG AGAQSTDETP DNENKQ
