YM11_YEAST
ID YM11_YEAST Reviewed; 943 AA.
AC P39523; D6VZU7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Uncharacterized protein YMR124W;
GN OrderedLocusNames=YMR124W; ORFNames=YM8564.06;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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] OF 770-943.
RA Pandit S., Sternglanz R.;
RL Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553 AND SER-766, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-586; SER-619; SER-681;
RP SER-766 AND SER-771, 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).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- INTERACTION:
CC P39523; P40091: PEA2; NbExp=6; IntAct=EBI-27256, EBI-13106;
CC P39523; P40075: SCS2; NbExp=4; IntAct=EBI-27256, EBI-16735;
CC P39523; Q07657: SHS1; NbExp=5; IntAct=EBI-27256, EBI-22083;
CC -!- MISCELLANEOUS: Present with 166 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z49273; CAA89273.1; -; Genomic_DNA.
DR EMBL; L07650; AAA35122.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10021.1; -; Genomic_DNA.
DR PIR; S54493; S54493.
DR RefSeq; NP_013843.1; NM_001182625.1.
DR PDB; 6LP3; X-ray; 3.55 A; A/B/D/E=746-943.
DR PDBsum; 6LP3; -.
DR AlphaFoldDB; P39523; -.
DR SMR; P39523; -.
DR BioGRID; 35301; 138.
DR DIP; DIP-2977N; -.
DR IntAct; P39523; 115.
DR MINT; P39523; -.
DR STRING; 4932.YMR124W; -.
DR iPTMnet; P39523; -.
DR MaxQB; P39523; -.
DR PaxDb; P39523; -.
DR PRIDE; P39523; -.
DR EnsemblFungi; YMR124W_mRNA; YMR124W; YMR124W.
DR GeneID; 855154; -.
DR KEGG; sce:YMR124W; -.
DR SGD; S000004731; YMR124W.
DR VEuPathDB; FungiDB:YMR124W; -.
DR eggNOG; ENOG502S6M4; Eukaryota.
DR HOGENOM; CLU_312205_0_0_1; -.
DR InParanoid; P39523; -.
DR OMA; KTELYKQ; -.
DR BioCyc; YEAST:G3O-32817-MON; -.
DR PRO; PR:P39523; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P39523; protein.
DR GO; GO:0005935; C:cellular bud neck; IPI:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0061163; P:endoplasmic reticulum polarization; IDA:SGD.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Phosphoprotein; Reference proteome.
FT CHAIN 1..943
FT /note="Uncharacterized protein YMR124W"
FT /id="PRO_0000203298"
FT REGION 37..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 553
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 586
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 681
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 766
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 771
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 943 AA; 105914 MW; 6631BEFBCD62E601 CRC64;
MDAGLSTMAT RNGQSSARVK LRNNLLNNDI GNIDIRDETP ISRNGNDSNI NIQPSSVPQQ
QQQQQQYYRN GMNEAPIQAP LQQRQIPMQN YSQQQRQQQQ YNFEYSNPHM NEIPLMQHNF
TKPSLSNNRD NVNGKKASSF TQSSFSNFFK HKHQFGKSKK NTKGTGGGGD GDDDDEVILD
DSANSDLTFN DIQTFGHKGG DKYGYGGDST PIIPTLVTKD RGNMSNTEYR KYITNQRKTA
MNAMAKQTKN GTLASLPPRA MSLQSFPNGN PLMQAPTPHP RFQPNKMVSA NYSRSNSLMS
GPPGQFRQPQ QQRMLPMNNY NNHPGQFQNT PPVMPSGQQP PQQPRTLSLT NGPRYSPQNP
RPFAGHQQIS QRQQQQQQQL QLHPMSEGYR TMSLQSQNVP QGFNPWSPND NDRKAVSMKQ
PISQSSISSK NNSAYSIPNV QNNSLTTFSP SSPTDATAMP NSTKQGSSPL KKQVNIDQPI
ENKGKLNVLQ LSTPQQNELK EKERKLAEME KSLREREALV EEKEKERAEK NTEANEEEEI
SHESDDLNLR PASALETGLK DLKLESESAV ANRASLSTFS STFSDSPSKQ RIINTRTGMY
KLENSTDINE YVTAQEFPSP GKYNSNSDNG EMNTTNEVDF DFNTSKRASL LQSIPERDPK
RNVSDATIKR RESDGNGRRL SNVNISMNQE NINNDTFLYK KNNRDGHLSA VSHMSSSSRR
SFISNTLPLN IDSASESDNF VPHMDGSPSK TKSAPVSYDK DGMNASEEDF SFDNTLAKPY
EPLYARRGDI TSAGSTSGED SSQPKMITIS GEQLNLITEN KELMNELTLV STELAESIKR
ETELEERIRL YETNNSAPSF DDSSSVSFSD FEKELRKKSS KIVQLIQQLN DERLKRFIAE
EQLLLQENGT KPSSMELVGR IENLNKLIDE RDSEIEMLKG RLQ