ID   YHP7_YEAST              Reviewed;         366 AA.
AC   P38809; D3DL47;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   02-SEP-2026, entry version 148.
DE   RecName: Full=Uncharacterized protein YHR097C;
GN   OrderedLocusNames=YHR097C;
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=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA   Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA   Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA   Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA   St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA   Waterston R., Wilson R., Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
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   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-78; LYS-187 AND LYS-242, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=SUB592;
RX   PubMed=12872131; DOI=10.1038/nbt849;
RA   Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA   Roelofs J., Finley D., Gygi S.P.;
RT   "A proteomics approach to understanding protein ubiquitination.";
RL   Nat. Biotechnol. 21:921-926(2003).
RN   [4]
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-189, 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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288; SER-294 AND SER-359, AND
RP   IDENTIFICATION BY 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   [7]
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69 AND THR-76, AND
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- SIMILARITY: Belongs to the pal1 family. {ECO:0000305}.
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DR   EMBL; U00060; AAB68935.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06791.1; -; Genomic_DNA.
DR   PIR; S46727; S46727.
DR   AlphaFoldDB; P38809; -.
DR   BioGRID; 36530; 77.
DR   FunCoup; P38809; 146.
DR   IntAct; P38809; 14.
DR   MINT; P38809; -.
DR   STRING; 4932.YHR097C; -.
DR   GlyGen; P38809; 5 sites, 1 O-linked glycan (5 sites).
DR   iPTMnet; P38809; -.
DR   PaxDb; 4932-YHR097C; -.
DR   PeptideAtlas; P38809; -.
DR   EnsemblFungi; YHR097C_mRNA; YHR097C; YHR097C.
DR   KEGG; sce:YHR097C; -.
DR   AGR; SGD:S000001139; -.
DR   SGD; S000001139; YHR097C.
DR   VEuPathDB; FungiDB:YHR097C; -.
DR   eggNOG; ENOG502QPHY; Eukaryota.
DR   HOGENOM; CLU_041195_1_0_1; -.
DR   InParanoid; P38809; -.
DR   OMA; INHAQES; -.
DR   OrthoDB; 5352132at2759; -.
DR   BioCyc; YEAST:G3O-31142-MONOMER; -.
DR   BioGRID-ORCS; 856497; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P38809; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P38809; protein.
DR   GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0034399; C:nuclear periphery; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   InterPro; IPR013226; Pal1.
DR   PANTHER; PTHR28307; PROTEIN PAL1; 1.
DR   PANTHER; PTHR28307:SF2; PROTEIN PAL1; 1.
DR   Pfam; PF08316; Pal1; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN           1..366
FT                   /note="Uncharacterized protein YHR097C"
FT                   /id="PRO_0000202907"
FT   REGION          1..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          313..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..108
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        316..327
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..338
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..349
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..366
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         69
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         76
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         189
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MOD_RES         288
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MOD_RES         294
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MOD_RES         359
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   CROSSLNK        78
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:12872131"
FT   CROSSLNK        187
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:12872131"
FT   CROSSLNK        242
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:12872131"
SQ   SEQUENCE   366 AA;  40663 MW;  AD04D034CBD6764D CRC64;
     MNQTGRTIGG PQNGVNTVIN PFRVSPSEDR VSSRDETPRN YNNPFLNEDD TRRAHNSSVS
     NSRQERLPSY EEAAGTPKQQ APYPKEKKRS SGSNSHQHNH HHHRRTSHGH RDKDKQKSKS
     RTKVKPPKNV DTIDKMDVTG LFGGSFHHDG PFDACTPQRN KNNKVAPVLA FPADGPNNTV
     GGRTSKKSTL DEVFGRETVD DDSETLNQLQ DRAYLFNKAN SSTTTLDAIK PNSKNITQFD
     SKMKTELVHG PITMGLGSTT FLDGAPASSA AIEQDVINHA QESRRKNSIA RKKSLPSRRH
     LQVNNNNLKL VKTHSGHLEQ KDVDDNRTSV PVTATQGSGH EDVVKKENTG NKLLRRVKSL
     KTSKKH
//