YEF3_YEAST
ID YEF3_YEAST Reviewed; 956 AA.
AC P32618; D3DLK6; Q66RC2;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Uncharacterized protein YEL043W;
GN OrderedLocusNames=YEL043W; ORFNames=SYGP-ORF14;
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=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 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 [4]
RP DOMAIN FIBRONECTIN TYPE-III.
RX PubMed=8994808; DOI=10.1016/s0960-9822(02)70765-3;
RA Bateman A., Chothia C.;
RT "Fibronectin type III domains in yeast detected by a hidden Markov model.";
RL Curr. Biol. 6:1544-1546(1996).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-154, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-154, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501; SER-520 AND SER-802, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-154; SER-520; SER-802;
RP SER-842 AND SER-895, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 -!- INTERACTION:
CC P32618; P53253: NNF2; NbExp=3; IntAct=EBI-22354, EBI-23229;
CC -!- MISCELLANEOUS: Present with 149 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U18779; AAB64999.1; -; Genomic_DNA.
DR EMBL; AY723799; AAU09716.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07610.1; -; Genomic_DNA.
DR PIR; S30834; S30834.
DR RefSeq; NP_010871.3; NM_001178858.3.
DR AlphaFoldDB; P32618; -.
DR SMR; P32618; -.
DR BioGRID; 36686; 226.
DR DIP; DIP-2682N; -.
DR IntAct; P32618; 8.
DR MINT; P32618; -.
DR STRING; 4932.YEL043W; -.
DR iPTMnet; P32618; -.
DR MaxQB; P32618; -.
DR PaxDb; P32618; -.
DR PRIDE; P32618; -.
DR EnsemblFungi; YEL043W_mRNA; YEL043W; YEL043W.
DR GeneID; 856668; -.
DR KEGG; sce:YEL043W; -.
DR SGD; S000000769; YEL043W.
DR VEuPathDB; FungiDB:YEL043W; -.
DR eggNOG; ENOG502R2RI; Eukaryota.
DR HOGENOM; CLU_012632_0_0_1; -.
DR InParanoid; P32618; -.
DR OMA; NYSKGFT; -.
DR BioCyc; YEAST:G3O-30163-MON; -.
DR PRO; PR:P32618; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P32618; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IBA:GO_Central.
DR GO; GO:0005795; C:Golgi stack; IBA:GO_Central.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0048211; P:Golgi vesicle docking; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0061025; P:membrane fusion; IBA:GO_Central.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..956
FT /note="Uncharacterized protein YEL043W"
FT /id="PRO_0000202607"
FT DOMAIN 40..141
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 152..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..956
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 154
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 802
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 842
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 895
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 467
FT /note="F -> S (in Ref. 3; AAU09716)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 956 AA; 106133 MW; 3F78B09A0FCA03AF CRC64;
MPVSVITTVL ACLWLSYRLY KFLTIPVSSI VSTLKIKTPP ATKVSIDKIA TDSVTIHWEN
EPVKAEDNGS ADRNFISHYL LYLNNTQLAI FPNNPNSLYT CCSITGLEAE TQYQLDFITI
NNKGFINKLP SIYCMTKARE ANEALKTRKW RRNTITSSTA MQPRNSKSEP APLPSHYSSV
SLSTFSSNIT NSATSNNGSN LPAYTSLTTL KDLDSFSIDD LKKILICAQE DLHDVLSQQT
SLLQDFQESK LELELELDNL KTHWSHEIDL RKSLKSNIKS LENSKLLTDL KIEKLNKKID
KSKEKISKMR NDMQKWSQED TELLSKDTIK EKYFKLLNES NASVANINKE IESLQNEISK
MEESNKRLNA SKKSLITSIV VNANVENDKP IASGELSAVL KKLNDFTLEK NGFLSNAGEE
FLSKLNADSS LIKMIKQELS IDQELEANWK LQRSNLLKKI SALENQFNEM SLNNRNLKTK
LMVQPYKNNG DSLAATNSNN SAEKNRSSGS IQLPLSNNMS RTGSIDLISN NNKSINNSNA
DSAPPLRLHN PVSYSPSNEP IQPSSSLLSQ LTQDTDNRSM LSNHISSNNE NKQQPSSYSH
ALPTTATANA TATATATNGH SRSNLWTTAQ FAQPSHQQVS TELDQAFEYD NANHLISGLQ
NMIYDETDYP DNISNYSKGF TTDELDNYWT KQQPQVRSTN ESLFSTTGTP MSSYKANPVI
SPYSSSHLRQ TSNATNTNPM HPQSLLAATL NDPSLQSFVR SGSFYSAPQP ANSLQNNING
NETENISPRI SSDFNLLVPN LSPRLSNDVP IVPGNNTTLT PSHSNILTMN HQPTADNITR
RSFHASSPPF NSIWNSNTNQ LSPPLEEQYH LDVPVGPKVP AKEPSPKPSH KRNQSNSSIS
SAWSKFKHKS ASSPANADTD IQDSSTPSTS PSGRRMSKLL SKSGMNNLFN PHSHDS
