SYH1_YEAST
ID SYH1_YEAST Reviewed; 849 AA.
AC Q02875; D6W3R2;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=SMY2 homolog 2;
GN Name=SYH1; OrderedLocusNames=YPL105C;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
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 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 [4]
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 [5]
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 [6]
RP COPURIFICATION WITH RIBOSOMAL COMPLEXES, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16702403; DOI=10.1101/gad.1422006;
RA Fleischer T.C., Weaver C.M., McAfee K.J., Jennings J.L., Link A.J.;
RT "Systematic identification and functional screens of uncharacterized
RT proteins associated with eukaryotic ribosomal complexes.";
RL Genes Dev. 20:1294-1307(2006).
RN [7]
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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-350, 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).
CC -!- SUBUNIT: Interacts with ribosomes. Interacts with EAP1 and MSL5 (via
CC the GYP domain). {ECO:0000269|PubMed:16120600}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 830 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SMY2/mpd2 family. {ECO:0000305}.
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DR EMBL; U43281; AAB68195.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11328.1; -; Genomic_DNA.
DR PIR; S61962; S61962.
DR RefSeq; NP_015220.1; NM_001183919.1.
DR AlphaFoldDB; Q02875; -.
DR SMR; Q02875; -.
DR BioGRID; 36076; 151.
DR DIP; DIP-961N; -.
DR IntAct; Q02875; 4.
DR MINT; Q02875; -.
DR STRING; 4932.YPL105C; -.
DR iPTMnet; Q02875; -.
DR MaxQB; Q02875; -.
DR PaxDb; Q02875; -.
DR PRIDE; Q02875; -.
DR EnsemblFungi; YPL105C_mRNA; YPL105C; YPL105C.
DR GeneID; 855999; -.
DR KEGG; sce:YPL105C; -.
DR SGD; S000006026; SYH1.
DR VEuPathDB; FungiDB:YPL105C; -.
DR eggNOG; KOG1862; Eukaryota.
DR GeneTree; ENSGT00940000176785; -.
DR HOGENOM; CLU_019270_0_0_1; -.
DR InParanoid; Q02875; -.
DR OMA; RQEFLRW; -.
DR BioCyc; YEAST:G3O-34007-MON; -.
DR PRO; PR:Q02875; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q02875; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0051664; P:nuclear pore localization; 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 Coiled coil; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..849
FT /note="SMY2 homolog 2"
FT /id="PRO_0000238645"
FT DOMAIN 149..205
FT /note="GYF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00101"
FT REGION 305..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 410..484
FT /evidence="ECO:0000255"
FT COMPBIAS 317..341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 350
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 849 AA; 94357 MW; 4DEDBB3300C53AE5 CRC64;
MNPINSLAFD LHSVKLADAN SDTAALSNSN TPTMNNAALL QRPSSIMDSI GVQRVPSPFV
PGSNAISGAS TVPFNAYDAE ITGSPLQISA NQENNSAFSA ASSNLHMNAS SPSVLNKPSS
TFPNVAPYLY NATGPAPNVG NQPPPPGIES QWKYIDSNGN IQGPFGTNNM SQWYQGGYFT
PTLQICRLAT SPEPFGVNDR FIRLGELTTL VNNYQDPFVA FDFIVIRALN AVPLVAPTSS
EKQKVESRDL IPVADVHSDD FTYEEILGLK FEDGSYYHET QVWVPVDGRH ITKVDRIPKI
SAYTAPLSTT SSRSNKTTSS HEEKVPSHEE ASPEEQEVFS EEGRTVSNIT NEEESIVKNP
TKQEEESRGS EKEQNILDQV QPEIEEVDRK DVISTADEPK SKDTPQMTSE EQKRFAKAEL
MAQKLLEEQQ RQEEEKKRRE EQRKLKKEKK LKQKQKKEEE KLKKKKKEEG KLEKEKQKEL
LNNILTGDTE TPSSENTATS ITTNLAPWAN KKPEGAVYNQ ISSALEDLKK ENSSKKEKKP
NRTQLDREQA LKLQKEILSS AQIPKTQTGS AWGIKPQQPI KVDIKGELMK DSTKINSQSK
INKANNGDIK PDSTFIEEQK KLWEQVQKKT KKFNRASSLD DFISRTPSPS SSALNSSNTS
NAWTTVSSKS TTHIASTMPV AGNQSKSYIS LDTLRSSGGL STATKTKMSD KSKQIGSSTS
IPTLKARQVK PSRIPAYPGN ASVSKRQEFL RWCRSQLKLN TGVQPDNVLE MLLSLPPGSE
SKEIIADTIY SYSSTMDGRR FATDFIKKRL ECEEEINDPL SWSEVLAMPE GSSEDWEFQV
VGKKKGKRF
