PAM1_YEAST
ID PAM1_YEAST Reviewed; 830 AA.
AC P37304; D6VSN1; Q03789;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Protein PAM1;
GN Name=PAM1; OrderedLocusNames=YDR251W; ORFNames=YD8419.18, YD9320A.01;
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].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=8106383; DOI=10.1016/s0021-9258(17)41880-1;
RA Hu G.-Z., Ronne H.;
RT "Overexpression of yeast PAM1 gene permits survival without protein
RT phosphatase 2A and induces a filamentous phenotype.";
RL J. Biol. Chem. 269:3429-3435(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
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 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-659, 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-659 AND SER-767, 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-659 AND SER-732, 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 -!- FUNCTION: Not known. It is a suppressor of protein phosphatase 2A
CC depletion.
CC -!- INTERACTION:
CC P37304; Q03306: PKH3; NbExp=3; IntAct=EBI-12870, EBI-37683;
CC -!- MISCELLANEOUS: Present with 300 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PAM1/SVL3 family. {ECO:0000305}.
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DR EMBL; X73454; CAA51833.1; -; Genomic_DNA.
DR EMBL; Z49701; CAA89737.1; -; Genomic_DNA.
DR EMBL; Z70202; CAA94090.1; -; Genomic_DNA.
DR EMBL; Z68329; CAA92708.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12091.1; -; Genomic_DNA.
DR PIR; S54547; S54547.
DR RefSeq; NP_010537.3; NM_001180559.3.
DR AlphaFoldDB; P37304; -.
DR SMR; P37304; -.
DR BioGRID; 32301; 100.
DR DIP; DIP-5213N; -.
DR IntAct; P37304; 12.
DR MINT; P37304; -.
DR STRING; 4932.YDR251W; -.
DR iPTMnet; P37304; -.
DR MaxQB; P37304; -.
DR PaxDb; P37304; -.
DR PRIDE; P37304; -.
DR EnsemblFungi; YDR251W_mRNA; YDR251W; YDR251W.
DR GeneID; 851838; -.
DR KEGG; sce:YDR251W; -.
DR SGD; S000002659; PAM1.
DR VEuPathDB; FungiDB:YDR251W; -.
DR eggNOG; ENOG502QT3Z; Eukaryota.
DR GeneTree; ENSGT00940000176320; -.
DR HOGENOM; CLU_010717_0_0_1; -.
DR InParanoid; P37304; -.
DR OMA; CHLNTIN; -.
DR BioCyc; YEAST:G3O-29823-MON; -.
DR PRO; PR:P37304; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P37304; protein.
DR GO; GO:0005933; C:cellular bud; HDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR013328; 6PGD_dom2.
PE 1: Evidence at protein level;
KW Coiled coil; Phosphoprotein; Reference proteome.
FT CHAIN 1..830
FT /note="Protein PAM1"
FT /id="PRO_0000058220"
FT REGION 426..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 796..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 379..400
FT COILED 481..514
FT COMPBIAS 428..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..820
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 659
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 732
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 767
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 256
FT /note="S -> T (in Ref. 1; CAA51833)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 830 AA; 92872 MW; 23DC105C4AB45FB9 CRC64;
MTSALRVLVC GDHPNLILYT SRFQHAKNIE FYLVNNSKNA NYEVSSLFYG TERFQIQNHF
QSLLDLVDLN NENGGLVFDL IIMSASSLQE IPQVLRDIKP MMNKTTKILF ESSGFIYLEP
FIKASVDLSL SNIFSIFTDY DIRRLDNGSY KQFTTANAKS FSVSIGQTTS VHENSYSSDI
IPILNTFQKL FQKLFPRDVV TLYDHSPSAF LAKEWELALP QICFDPLLII LEEKNPSTLD
DHVLAKPLIS GLLGESLLII KKMGIAMNNP NFQNEQTILK HWKNKCEDLP DGPALLYNFI
HKASSLNIDL LLLQPILLAD DFGVKTPYLE CLFTMMTQYQ LLNKGDSEWF IRKDENTALT
RVDDLQNSIA LKDGKIMQLQ NSESTLKNEI KELQSQVLSL KQEVSSSKAN NGQELEILKK
KVQMGDNSLF DRPNSNTNGI SPSDNIVDVD LNYERSDQGN NSSGNDSRRQ SFFNSTSDTT
LSRDETSLKE RELEVRMKEL ELQERELELQ RKALQQQQQY QQRPPKQVYS GPSGTPTSGN
NNNKSYNPNR KSSYSQPQHV AMMTSRGLHG PSAASSSPVI SANNFVDPVS SGTPYSSNSS
RFSQQIPSQQ YMHTVKPTSR KNRSSVMPNI GYVPGLTNNE YGRKFNGNGM NGTQSRLNSL
SNQSTFRSQQ GPPITQQKSF QNNGGSMRTN RIPSANYNIS NQQSGFVNSI SSPNLSNLEN
RNTVQNSRNA DSAPCVNQLN SDSPPQLQSL SQNGTSKVPQ INITQPSPIQ TNFATSDNPA
AVIKLGTPSE DTVSAAATAN NISTMGDESR KEDVKEKKKK KFSFFGKRKK
