LDB19_YEAST
ID LDB19_YEAST Reviewed; 818 AA.
AC Q12502; D6W320;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Protein LDB19;
DE AltName: Full=Low dye-binding protein 19;
GN Name=LDB19; OrderedLocusNames=YOR322C; ORFNames=O6152;
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 96604 / S288c / FY1679;
RX PubMed=8896266;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1021::aid-yea981>3.0.co;2-7;
RA Pearson B.M., Hernando Y., Payne J., Wolf S.S., Kalogeropoulos A.,
RA Schweizer M.;
RT "Sequencing of a 35.71 kb DNA segment on the right arm of yeast chromosome
RT XV reveals regions of similarity to chromosomes I and XIII.";
RL Yeast 12:1021-1031(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 DRUG RESISTANCE.
RX PubMed=10407277;
RX DOI=10.1002/(sici)1097-0061(199907)15:10b<973::aid-yea402>3.0.co;2-l;
RA Rieger K.-J., El-Alama M., Stein G., Bradshaw C., Slonimski P.P.,
RA Maundrell K.;
RT "Chemotyping of yeast mutants using robotics.";
RL Yeast 15:973-986(1999).
RN [5]
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 [6]
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 [7]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-486, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=14557538; DOI=10.1073/pnas.2135500100;
RA Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
RT "A subset of membrane-associated proteins is ubiquitinated in response to
RT mutations in the endoplasmic reticulum degradation machinery.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
RN [8]
RP FUNCTION.
RX PubMed=15993632; DOI=10.1016/j.fgb.2005.05.002;
RA Corbacho I., Olivero I., Hernandez L.M.;
RT "A genome-wide screen for Saccharomyces cerevisiae nonessential genes
RT involved in mannosyl phosphate transfer to mannoprotein-linked
RT oligosaccharides.";
RL Fungal Genet. Biol. 42:773-790(2005).
RN [9]
RP PERIODIC EXPRESSION DURING CELL CYCLE.
RX PubMed=16278933; DOI=10.1002/yea.1302;
RA de Lichtenberg U., Wernersson R., Jensen T.S., Nielsen H.B., Fausboell A.,
RA Schmidt P., Hansen F.B., Knudsen S., Brunak S.;
RT "New weakly expressed cell cycle-regulated genes in yeast.";
RL Yeast 22:1191-1201(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-93, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384 AND THR-619, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-808, 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 -!- FUNCTION: May be involved in protein-linked oligosaccharide
CC phosphorylation since the deletion reduces the negative charge of the
CC cell surface. Involved in the resistance to EDTA, cadmium chloride,
CC cycloheximide, 6-dimethylaminopurine, methyl caffeate, beta-chloro-L-
CC alanine, caffeine and cerulenin. {ECO:0000269|PubMed:15993632}.
CC -!- INTERACTION:
CC Q12502; P39940: RSP5; NbExp=3; IntAct=EBI-2113927, EBI-16219;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Golgi
CC apparatus {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Expressed periodically during cell division with a peak
CC during M phase.
CC -!- MISCELLANEOUS: Present with 295 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the LDB19 family. {ECO:0000305}.
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DR EMBL; X90565; CAA62178.1; -; Genomic_DNA.
DR EMBL; Z75230; CAA99642.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11086.1; -; Genomic_DNA.
DR PIR; S58333; S58333.
DR RefSeq; NP_014967.3; NM_001183742.3.
DR AlphaFoldDB; Q12502; -.
DR BioGRID; 34708; 189.
DR IntAct; Q12502; 4.
DR MINT; Q12502; -.
DR STRING; 4932.YOR322C; -.
DR iPTMnet; Q12502; -.
DR MaxQB; Q12502; -.
DR PaxDb; Q12502; -.
DR PRIDE; Q12502; -.
DR EnsemblFungi; YOR322C_mRNA; YOR322C; YOR322C.
DR GeneID; 854500; -.
DR KEGG; sce:YOR322C; -.
DR SGD; S000005849; LDB19.
DR VEuPathDB; FungiDB:YOR322C; -.
DR eggNOG; ENOG502QS9U; Eukaryota.
DR HOGENOM; CLU_012509_0_0_1; -.
DR InParanoid; Q12502; -.
DR OMA; LRMQFKL; -.
DR BioCyc; YEAST:G3O-33801-MON; -.
DR ChiTaRS; LDB19; yeast.
DR PRO; PR:Q12502; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12502; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0000138; C:Golgi trans cisterna; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:SGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0002092; P:positive regulation of receptor internalization; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR GO; GO:0070086; P:ubiquitin-dependent endocytosis; IMP:SGD.
DR Gene3D; 2.60.40.640; -; 1.
DR InterPro; IPR014752; Arrestin-like_C.
DR InterPro; IPR024391; LDB19_N.
DR Pfam; PF13002; LDB19; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cytoplasm; Golgi apparatus; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..818
FT /note="Protein LDB19"
FT /id="PRO_0000240388"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..644
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 93
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 619
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 808
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CROSSLNK 486
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:14557538"
SQ SEQUENCE 818 AA; 89826 MW; 3F3C10ABE1E44F99 CRC64;
MAFSRLTSTH QSNHNGYSNS NKKGQSLPLT LSIDVESPPC VLYGSAMESS GAVLSGLFTV
TVVDPYSSAE DKSLKNTESN VSTTSKSLKR KSTFGSALSS RLSSLSASTS NISPSTSSTS
ISHSPTPANL RIMAGYTKIT ITSVTLSLVQ KIHFHKPFVP NISSMQTCMN CKTKITNMKS
WEIQSNTQDL SVGSHSYPFS YLIPGSVPCS SSLGATAETQ VKYELIAVVT YIDPHRNSFS
SGHSTPRKEG SSSKKRLLQL AMPIAVTRSI PRGPDKNSLR VFPPTELTAA AVLPNVVYPK
STFPLEMKLD GVSSGDRRWR MRKLSWRIEE TTRVKAHACP VHKHELRQLE EQVKIKESEK
SKKPRSHIKR YGELGPQIRV AVNSLENMPS QRLPGEPGRE QAPNSSGPAS TGNVGLDDEN
PVNEDEEDQP GSEFIHPSDD ALRQELLMQQ QRARQQQLQQ ELKNNSSLFT EEVRIISKGE
MKSGWKTDFD NNGKIELVTE IDCMGLNSGV SNPVMHASTL QTPSTGNKKP SINVACDIQD
PNLGLYVSHI LAVEIVVAEE TLQYANGQPI RKPNSKNKKE TNNNTMNVHN PDQRLAELSP
IFANRNTPKV RRMGPEDITP VNSNKSNHST NKEKASNGAS NSNIVSVPTG AARVLRMQFR
LTVTERSGLG ISWDEEVPPI YQDVELLSPP CYELSINNGI KNKLYSTMST PVRSEDDFVG
GSDEDIGNYE SQGLEPGPNV QEVTITQNKL TIPPTAHHYQ PASSSQRSLT TVQSPPLESV
VSVQGSVPFR GHVLTPHSTR DIRIQNFSDF LDSNRITQ
