RBA50_YEAST
ID RBA50_YEAST Reviewed; 439 AA.
AC Q04418; D6VTE8;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=RNA polymerase II-associated protein RBA50;
DE AltName: Full=RNA polymerase II-associated protein of 50 kDa;
GN Name=RBA50; OrderedLocusNames=YDR527W;
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=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 [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 192-194.
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 INDUCTION.
RX PubMed=12161108; DOI=10.1016/s0143-4160(02)00110-0;
RA Lombardia L.J., Becerra M., Rodriguez-Belmonte E., Hauser N.C.,
RA Cerdan M.E.;
RT "Genome-wide analysis of yeast transcription upon calcium shortage.";
RL Cell Calcium 32:83-91(2002).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
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 FUNCTION.
RX PubMed=15282305; DOI=10.1128/mcb.24.16.7043-7058.2004;
RA Jeronimo C., Langelier M.-F., Zeghouf M., Cojocaru M., Bergeron D.,
RA Baali D., Forget D., Mnaimneh S., Davierwala A.P., Pootoolal J., Chandy M.,
RA Canadien V., Beattie B.K., Richards D.P., Workman J.L., Hughes T.R.,
RA Greenblatt J., Coulombe B.;
RT "RPAP1, a novel human RNA polymerase II-associated protein affinity
RT purified with recombinant wild-type and mutated polymerase subunits.";
RL Mol. Cell. Biol. 24:7043-7058(2004).
RN [8]
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: Forms an interface between the RNA polymerase II enzyme and
CC chaperone/scaffolding proteins, suggesting that it is required to
CC connect RNA polymerase II to regulators of protein complex formation.
CC {ECO:0000250, ECO:0000269|PubMed:15282305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14690591}.
CC -!- INDUCTION: Down-regulated at low calcium levels.
CC {ECO:0000269|PubMed:12161108}.
CC -!- MISCELLANEOUS: Present with 688 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RPAP1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U33057; AAB64966.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12358.2; -; Genomic_DNA.
DR PIR; S69582; S69582.
DR RefSeq; NP_010816.4; NM_001180835.4.
DR AlphaFoldDB; Q04418; -.
DR BioGRID; 32576; 196.
DR DIP; DIP-4127N; -.
DR IntAct; Q04418; 8.
DR STRING; 4932.YDR527W; -.
DR MaxQB; Q04418; -.
DR PaxDb; Q04418; -.
DR PRIDE; Q04418; -.
DR EnsemblFungi; YDR527W_mRNA; YDR527W; YDR527W.
DR GeneID; 852139; -.
DR KEGG; sce:YDR527W; -.
DR SGD; S000002935; RBA50.
DR VEuPathDB; FungiDB:YDR527W; -.
DR eggNOG; KOG1894; Eukaryota.
DR GeneTree; ENSGT00390000007594; -.
DR HOGENOM; CLU_031074_0_0_1; -.
DR InParanoid; Q04418; -.
DR OMA; IHFPRPP; -.
DR BioCyc; YEAST:G3O-30041-MON; -.
DR PRO; PR:Q04418; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04418; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:SGD.
DR InterPro; IPR013929; RNA_pol_II_AP1_C.
DR InterPro; IPR013930; RNA_pol_II_AP1_N.
DR InterPro; IPR039913; RPAP1/Rba50.
DR PANTHER; PTHR21483; PTHR21483; 1.
DR Pfam; PF08620; RPAP1_C; 1.
DR Pfam; PF08621; RPAP1_N; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..439
FT /note="RNA polymerase II-associated protein RBA50"
FT /id="PRO_0000255972"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 192..194
FT /note="EEA -> GEG (in Ref. 1; AAB64966)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 439 AA; 50192 MW; 1880B5F6CE81BEC1 CRC64;
MDLLGDIVEK DTSDSVESND NGTLSTNNCG TGFPELYKPK KISSWKERLR EKRAQKKKTS
GKDAEKQQTS TDAPLSEAKS IHNENIKVLQ GMSDEQIVQE REDLYNSLDP KLIAKLLKNI
NKRAKDENNT PLFAEIEGAS GTWVGGNKQG IYDLPPLDDE DVDVALEIRP MLGKDAKHVQ
FEEAGKEKDV EEEAKTNDDV DDIAPLDFQM AQCIDHMKNE ELFKDVHFIK EESQNEINLE
KLDINDPNFN DKLHEKYFPD LPKEVDKLKW MQPVQQKTDK NYIIEDVSEC RFDFNGDLVP
PTRQIDSTIH SGLHHHSDSP ELAGYTIVEL EHLARSTFPS QRCIAIQTLG RILYKLGQKS
YYQLVPEIDA DTYKEDGSIS NVMDKIYSMF WDLIKDGKVI ESLEISSDEK FTRNLSVRNY
AIDALWLWKQ GGGDFRTKK
