RT102_YEAST
ID RT102_YEAST Reviewed; 157 AA.
AC P53330; D6VV52;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Regulator of Ty1 transposition protein 102;
GN Name=RTT102; OrderedLocusNames=YGR275W; ORFNames=G9378;
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 204508 / S288c;
RX PubMed=9133740;
RX DOI=10.1002/(sici)1097-0061(19970330)13:4<365::aid-yea78>3.0.co;2-f;
RA Ruzzi M., Marconi A., Saliola M., Fabiani L., Montebove F., Frontali L.;
RT "The sequence of a 8 kb segment on the right arm of yeast chromosome VII
RT identifies four new open reading frames and the genes for yTAFII145.";
RL Yeast 13:365-368(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP IDENTIFICATION.
RX PubMed=11779788; DOI=10.1093/genetics/159.4.1449;
RA Scholes D.T., Banerjee M., Bowen B., Curcio M.J.;
RT "Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have
RT conserved roles in genome maintenance.";
RL Genetics 159:1449-1465(2001).
RN [6]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [7]
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 [8]
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 [9]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12775844; DOI=10.1126/science.1084337;
RA Cliften P.F., Sudarsanam P., Desikan A., Fulton L., Fulton B., Majors J.,
RA Waterston R., Cohen B.A., Johnston M.;
RT "Finding functional features in Saccharomyces genomes by phylogenetic
RT footprinting.";
RL Science 301:71-76(2003).
RN [10]
RP INTERACTION WITH STH1 AND SWI3, AND IDENTIFICATION IN THE SWI/SNF COMPLEX.
RX PubMed=15506919; DOI=10.1042/bst0320899;
RA Lee K.K., Prochasson P., Florens L., Swanson S.K., Washburn M.P.,
RA Workman J.L.;
RT "Proteomic analysis of chromatin-modifying complexes in Saccharomyces
RT cerevisiae identifies novel subunits.";
RL Biochem. Soc. Trans. 32:899-903(2004).
RN [11]
RP IDENTIFICATION IN THE RSC COMPLEX.
RX PubMed=14759368; DOI=10.1016/s1097-2765(04)00003-6;
RA Krogan N.J., Peng W.-T., Cagney G., Robinson M.D., Haw R., Zhong G.,
RA Guo X., Zhang X., Canadien V., Richards D.P., Beattie B.K., Lalev A.,
RA Zhang W., Davierwala A.P., Mnaimneh S., Starostine A., Tikuisis A.P.,
RA Grigull J., Datta N., Bray J.E., Hughes T.R., Emili A., Greenblatt J.F.;
RT "High-definition macromolecular composition of yeast RNA-processing
RT complexes.";
RL Mol. Cell 13:225-239(2004).
RN [12]
RP IDENTIFICATION IN THE RSC COMPLEX.
RX PubMed=14729968; DOI=10.1128/mcb.24.3.1232-1244.2003;
RA Baetz K.K., Krogan N.J., Emili A., Greenblatt J., Hieter P.;
RT "The ctf13-30/CTF13 genomic haploinsufficiency modifier screen identifies
RT the yeast chromatin remodeling complex RSC, which is required for the
RT establishment of sister chromatid cohesion.";
RL Mol. Cell. Biol. 24:1232-1244(2004).
RN [13]
RP IDENTIFICATION IN THE SWI/SNF COMPLEX.
RX PubMed=14660704; DOI=10.1074/mcp.m300099-mcp200;
RA Graumann J., Dunipace L.A., Seol J.H., McDonald W.H., Yates J.R. III,
RA Wold B.J., Deshaies R.J.;
RT "Applicability of tandem affinity purification MudPIT to pathway proteomics
RT in yeast.";
RL Mol. Cell. Proteomics 3:226-237(2004).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77 AND SER-122, 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: Probable component of the chromatin structure-remodeling
CC complex (RSC) which is involved in transcription regulation and
CC nucleosome positioning. RSC is responsible for the transfer of a
CC histone octamer from a nucleosome core particle to naked DNA. The
CC reaction requires ATP and involves an activated RSC-nucleosome
CC intermediate. Remodeling reaction also involves DNA translocation, DNA
CC twist and conformational change. As a reconfigurer of centromeric and
CC flanking nucleosomes, RSC complex is required both for proper
CC kinetochore function in chromosome segregation and, via a PKC1-
CC dependent signaling pathway, for organization of the cellular
CC cytoskeleton. Probable component of the SWI/SNF complex, an ATP-
CC dependent chromatin-remodeling complex, is required for the positive
CC and negative regulation of gene expression of a large number of genes.
CC It changes chromatin structure by altering DNA-histone contacts within
CC a nucleosome, leading eventually to a change in nucleosome position,
CC thus facilitating or repressing binding of gene-specific transcription
CC factors.
CC -!- SUBUNIT: Interacts with STH1 and SWI3. Component of the two forms of
CC the RSC complex composed of at least either RSC1 or RSC2, and ARP7,
CC ARP9, LDB7, NPL6, RSC3, RSC30, RSC4, RSC58, RSC6, RSC8, RSC9, SFH1,
CC STH1, HTL1 and probably RTT102. The complexes interact with histone and
CC histone variant components of centromeric chromatin. Probable
CC additional component of the SWI/SNF global transcription activator
CC complex. The 1.14 MDa SWI/SNF complex is composed of 11 different
CC subunits: one copy each of SWI1, SNF2/SWI2, SNF5, SNF12/SWP73,
CC ARP7/SWP61, ARP9/SWP59; two copies each of SWI3, SNF6, SNF11, SWP82;
CC and three copies of TAF14/SWP29. {ECO:0000269|PubMed:14660704,
CC ECO:0000269|PubMed:14729968, ECO:0000269|PubMed:14759368,
CC ECO:0000269|PubMed:15506919}.
CC -!- INTERACTION:
CC P53330; P32597: STH1; NbExp=5; IntAct=EBI-23637, EBI-18410;
CC P53330; P32591: SWI3; NbExp=2; IntAct=EBI-23637, EBI-18622;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1550 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS56708.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA58897.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA97305.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X84098; CAA58897.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z73060; CAA97305.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY558382; AAS56708.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006941; DAA08363.1; -; Genomic_DNA.
DR PIR; S64608; S64608.
DR RefSeq; NP_011791.4; NM_001181404.3.
DR PDB; 4I6M; X-ray; 2.80 A; D=1-157.
DR PDB; 5TGC; X-ray; 3.25 A; C/F=1-157.
DR PDB; 6KW3; EM; 7.13 A; h=1-157.
DR PDB; 6KW4; EM; 7.55 A; h=1-157.
DR PDB; 6KW5; EM; 10.13 A; h=1-157.
DR PDB; 6TDA; EM; 15.00 A; V=1-157.
DR PDB; 6UXW; EM; 8.96 A; Z=1-157.
DR PDB; 6V92; EM; 20.00 A; P=1-157.
DR PDB; 6VZ4; EM; 3.90 A; N=1-157.
DR PDB; 6VZG; EM; 4.20 A; N=1-157.
DR PDB; 7C4J; EM; 2.89 A; J=1-157.
DR PDB; 7EGP; EM; 6.90 A; L=1-157.
DR PDBsum; 4I6M; -.
DR PDBsum; 5TGC; -.
DR PDBsum; 6KW3; -.
DR PDBsum; 6KW4; -.
DR PDBsum; 6KW5; -.
DR PDBsum; 6TDA; -.
DR PDBsum; 6UXW; -.
DR PDBsum; 6V92; -.
DR PDBsum; 6VZ4; -.
DR PDBsum; 6VZG; -.
DR PDBsum; 7C4J; -.
DR PDBsum; 7EGP; -.
DR AlphaFoldDB; P53330; -.
DR SMR; P53330; -.
DR BioGRID; 33525; 139.
DR ComplexPortal; CPX-1150; SWI/SNF chromatin remodelling complex.
DR ComplexPortal; CPX-1888; RSC chromatin remodelling complex, variant RSC2.
DR ComplexPortal; CPX-1889; RSC chromatin remodelling complex, variant RSC1.
DR DIP; DIP-3864N; -.
DR IntAct; P53330; 55.
DR MINT; P53330; -.
DR STRING; 4932.YGR275W; -.
DR iPTMnet; P53330; -.
DR MaxQB; P53330; -.
DR PaxDb; P53330; -.
DR PRIDE; P53330; -.
DR EnsemblFungi; YGR275W_mRNA; YGR275W; YGR275W.
DR GeneID; 853192; -.
DR KEGG; sce:YGR275W; -.
DR SGD; S000003507; RTT102.
DR VEuPathDB; FungiDB:YGR275W; -.
DR eggNOG; ENOG502SEGN; Eukaryota.
DR HOGENOM; CLU_118233_0_0_1; -.
DR InParanoid; P53330; -.
DR OMA; KESWRYD; -.
DR BioCyc; YEAST:G3O-30940-MON; -.
DR PRO; PR:P53330; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53330; protein.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0016586; C:RSC-type complex; IDA:SGD.
DR GO; GO:0016514; C:SWI/SNF complex; IDA:SGD.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0007059; P:chromosome segregation; IMP:SGD.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IC:ComplexPortal.
DR GO; GO:0006337; P:nucleosome disassembly; IDA:SGD.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:SGD.
DR DisProt; DP01392; -.
DR InterPro; IPR018304; Rtt102.
DR Pfam; PF09510; Rtt102p; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..157
FT /note="Regulator of Ty1 transposition protein 102"
FT /id="PRO_0000097501"
FT REGION 95..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:4I6M"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:4I6M"
SQ SEQUENCE 157 AA; 17795 MW; D71CA1234D0D0176 CRC64;
MDPQTLITKA NKVSYYGNPT SKESWRYDWY QPSKVSSNVQ QPQQQLGDME NNLEKYPFRY
KTWLRNQEDE KNLQRESCED ILDLKEFDRR ILKKSLMTSH TKGDTSKATG APSANQGDEA
LSVDDIRGAV GNSEAIPGLS AGVNNDNTKE SKDVKMN
