SMY2_YEAST
ID SMY2_YEAST Reviewed; 740 AA.
AC P32909; D6VQG8;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Protein SMY2;
DE AltName: Full=Suppressor of MYO2-66 protein;
GN Name=SMY2; OrderedLocusNames=YBR172C; ORFNames=YBR1233;
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].
RA Lillie S.H., Brown S.S.;
RT "Characterization of a suppressor of the MYO2 gene in yeast.";
RL Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
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] OF 273-740.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8212898; DOI=10.1002/yea.320090811;
RA Schaaff-Gerstenschlaeger I., Bauer A., Boles E., Zimmermann F.K.;
RT "Sequence and function analysis of a 4.3 kb fragment of Saccharomyces
RT cerevisiae chromosome II including three open reading frames.";
RL Yeast 9:915-921(1993).
RN [5]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
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 EAP1 AND MSL5.
RX PubMed=16120600; DOI=10.1074/mcp.m500129-mcp200;
RA Kofler M., Motzny K., Freund C.;
RT "GYF domain proteomics reveals interaction sites in known and novel target
RT proteins.";
RL Mol. Cell. Proteomics 4:1797-1811(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129 AND SER-602, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND SER-602, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; THR-311; SER-545 AND
RP SER-602, AND 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: Suppressor of the MYO2 gene.
CC -!- SUBUNIT: Interacts with EAP1 and MSL5 (via the GYP domain).
CC {ECO:0000269|PubMed:16120600}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 486 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SMY2/mpd2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35057.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA85133.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M90654; AAA35057.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z36041; CAA85133.1; ALT_INIT; Genomic_DNA.
DR EMBL; X74437; CAA52452.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07288.1; -; Genomic_DNA.
DR PIR; S27458; S27458.
DR RefSeq; NP_009731.4; NM_001178520.3.
DR PDB; 3FMA; X-ray; 2.50 A; A/B/C/D/E=193-290.
DR PDB; 3K3V; X-ray; 1.80 A; A=193-290.
DR PDBsum; 3FMA; -.
DR PDBsum; 3K3V; -.
DR AlphaFoldDB; P32909; -.
DR SMR; P32909; -.
DR BioGRID; 32872; 92.
DR DIP; DIP-705N; -.
DR IntAct; P32909; 19.
DR MINT; P32909; -.
DR STRING; 4932.YBR172C; -.
DR iPTMnet; P32909; -.
DR MaxQB; P32909; -.
DR PaxDb; P32909; -.
DR PRIDE; P32909; -.
DR EnsemblFungi; YBR172C_mRNA; YBR172C; YBR172C.
DR GeneID; 852470; -.
DR KEGG; sce:YBR172C; -.
DR SGD; S000000376; SMY2.
DR VEuPathDB; FungiDB:YBR172C; -.
DR eggNOG; KOG1862; Eukaryota.
DR GeneTree; ENSGT00940000176785; -.
DR HOGENOM; CLU_019270_0_0_1; -.
DR InParanoid; P32909; -.
DR OMA; TENNNTH; -.
DR BioCyc; YEAST:G3O-29120-MON; -.
DR EvolutionaryTrace; P32909; -.
DR PRO; PR:P32909; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P32909; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:SGD.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IGI:SGD.
DR CDD; cd00072; GYF; 1.
DR Gene3D; 3.30.1490.40; -; 1.
DR InterPro; IPR003169; GYF.
DR InterPro; IPR035445; GYF-like_dom_sf.
DR Pfam; PF02213; GYF; 1.
DR SMART; SM00444; GYF; 1.
DR SUPFAM; SSF55277; SSF55277; 1.
DR PROSITE; PS50829; GYF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..740
FT /note="Protein SMY2"
FT /id="PRO_0000071996"
FT DOMAIN 205..261
FT /note="GYF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00101"
FT REGION 346..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 369..440
FT /evidence="ECO:0000255"
FT COMPBIAS 351..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 129
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 311
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 602
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:3K3V"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:3K3V"
FT HELIX 223..231
FT /evidence="ECO:0007829|PDB:3K3V"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:3K3V"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:3K3V"
FT HELIX 260..268
FT /evidence="ECO:0007829|PDB:3K3V"
FT HELIX 274..282
FT /evidence="ECO:0007829|PDB:3K3V"
SQ SEQUENCE 740 AA; 81397 MW; FAF5B6FA7F374060 CRC64;
MIAPDSQRLF GSFDEQFKDL KLDSVDTENN NTHGVSTILD SSPASVNNNT NGAVAASVNT
VPGSTFRSNT PLLGGRHPLS RTSSLIDSIG IQRAASPFSS MKEPFIPQSS GVMSSSFWHG
DHPESRVSTP VQQHPLLQRN ESSSSFSYAA NLGVNLSTHS LAVDITPLST PTAAQSHVNL
FPSSDIPPNM SMNGMSQLPA PVSVESSWRY IDTQGQIHGP FTTQMMSQWY IGGYFASTLQ
ISRLGSTPET LGINDIFITL GELMTKLEKY DTDPFTTFDK LHVQTTSSDS INLNLAPYAS
GVAATGTIKA TENDIFKPLT HDNIWDMDGG TTSKGVDIKL ASATTISQTD ESHKQEYKST
TMLEKGKKEK SESVAKALLD EQEKRNRELK RKEEARLSKK QKQKEDDLLK KQKEQKEQKE
KEALEAEKQK KSEKTKKDTQ TQTEGFKTSK DLPSLNSSSA NPAPWASKVK VNNAIETSIK
NGVSSTGKKK GEPLGLQQRN SKEEKQKEEL KSVLNWANKS SLPSNQTIDI KSQFQKSPKG
MKESSPLKEL EDPNFIEEQK KLWEKVQSSS KQVKSTSSAS TTTSSWTTVT SKGKAPIGTV
VSPYSKTNTS LNSSLTAKTS TTSTTTTFAS MNNVSPRQEF IKWCKSQMKL NSGITNNNVL
ELLLSLPTGP ESKELIQETI YANSDVMDGR RFATEFIKRR VACEKQGDDP LSWNEALALS
GNDDDGWEFQ VVSKKKGRKH
