ID RT107_YEAST Reviewed; 1070 AA. AC P38850; D3DLA3; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 27-MAR-2024, entry version 181. DE RecName: Full=Regulator of Ty1 transposition protein 107; DE AltName: Full=Establishes silent chromatin protein 4; GN Name=RTT107; Synonyms=ESC4; OrderedLocusNames=YHR154W; 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 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 [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 FUNCTION, AND PHOSPHORYLATION BY MEC1. RX PubMed=14988729; DOI=10.1038/sj.emboj.7600129; RA Rouse J.; RT "Esc4p, a new target of Mec1p (ATR), promotes resumption of DNA synthesis RT after DNA damage."; RL EMBO J. 23:1188-1197(2004). RN [6] RP INTERACTION WITH RAD55 AND MMS22, AND SUBCELLULAR LOCATION. RX PubMed=16569515; DOI=10.1016/j.dnarep.2006.02.005; RA Chin J.K., Bashkirov V.I., Heyer W.-D., Romesberg F.E.; RT "Esc4/Rtt107 and the control of recombination during replication."; RL DNA Repair 5:618-628(2006). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-532, 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 [8] RP FUNCTION, AND INTERACTION WITH RTT101. RX PubMed=17978089; DOI=10.1091/mbc.e07-09-0961; RA Roberts T.M., Zaidi I.W., Vaisica J.A., Peter M., Brown G.W.; RT "Regulation of rtt107 recruitment to stalled DNA replication forks by the RT cullin rtt101 and the rtt109 acetyltransferase."; RL Mol. Biol. Cell 19:171-180(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304; THR-532; SER-591; RP SER-593; SER-800 AND SER-806, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-532; SER-720 AND SER-806, 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). RN [11] RP INTERACTION WITH MMS22, AND IDENTIFICATION IN A COMPLEX WITH RTT101 AND RP MMS1. RX PubMed=20139071; DOI=10.1074/jbc.m109.082107; RA Mimura S., Yamaguchi T., Ishii S., Noro E., Katsura T., Obuse C., RA Kamura T.; RT "Cul8/Rtt101 forms a variety of protein complexes that regulate DNA damage RT response and transcriptional silencing."; RL J. Biol. Chem. 285:9858-9867(2010). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 820-1070 IN COMPLEX WITH HTA1. RX PubMed=22262834; DOI=10.1074/jbc.m111.311860; RA Li X., Liu K., Li F., Wang J., Huang H., Wu J., Shi Y.; RT "Structure of C-terminal tandem BRCT repeats of Rtt107 protein reveals RT critical role in interaction with phosphorylated histone H2A during DNA RT damage repair."; RL J. Biol. Chem. 287:9137-9146(2012). CC -!- FUNCTION: Required for resumption of chromosome replication after DNA CC damage, specifically in S phase. Is recruited to chromatin in the CC presence of RTT109 and RTT101 in response to stalled replication forks CC and acts as a scaffold during DNA repair. {ECO:0000269|PubMed:14988729, CC ECO:0000269|PubMed:17978089}. CC -!- SUBUNIT: Forms a complex with the cullin-RING ligase (CRL) RTT101(MMS1- CC MMS22). Interacts with MMS22 and RTT101. Interacts with histone H2A; CC requires H2A to be phosphorylated (gamma-H2A). Interacts with RAD55. CC {ECO:0000269|PubMed:16569515, ECO:0000269|PubMed:17978089, CC ECO:0000269|PubMed:20139071, ECO:0000269|PubMed:22262834}. CC -!- INTERACTION: CC P38850; Q06164: MMS22; NbExp=9; IntAct=EBI-24788, EBI-31156; CC P38850; P47050: RTT101; NbExp=5; IntAct=EBI-24788, EBI-25861; CC P38850; Q12098: SLX4; NbExp=6; IntAct=EBI-24788, EBI-37788; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095, CC ECO:0000269|PubMed:16569515}. Note=Recruited to chromatin in response CC to replication fork stalling. CC -!- PTM: Phosphorylated by MEC1. {ECO:0000269|PubMed:14988729}. CC -!- MISCELLANEOUS: Present with 1380 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. 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; U10397; AAB68978.1; -; Genomic_DNA. DR EMBL; BK006934; DAA06847.1; -; Genomic_DNA. DR PIR; S46755; S46755. DR RefSeq; NP_012024.1; NM_001179285.1. DR PDB; 3T7I; X-ray; 2.30 A; A/B=820-1070. DR PDB; 3T7J; X-ray; 2.04 A; A/B=820-1070. DR PDB; 3T7K; X-ray; 2.03 A; A/B=820-1070. DR PDB; 6J0V; X-ray; 2.31 A; A/B=1-513. DR PDB; 6J0W; X-ray; 2.40 A; A/B=1-513. DR PDB; 6J0X; X-ray; 2.31 A; A/B/C/D=1-513. DR PDB; 6J0Y; X-ray; 1.80 A; A/B=2-513. DR PDBsum; 3T7I; -. DR PDBsum; 3T7J; -. DR PDBsum; 3T7K; -. DR PDBsum; 6J0V; -. DR PDBsum; 6J0W; -. DR PDBsum; 6J0X; -. DR PDBsum; 6J0Y; -. DR AlphaFoldDB; P38850; -. DR SMR; P38850; -. DR BioGRID; 36588; 440. DR ComplexPortal; CPX-1157; CUL8-MMS1-MMS22-ESC4 E3 ubiquitin ligase complex. DR ComplexPortal; CPX-1355; RTT107-SLX4-SLX1 complex. DR DIP; DIP-6297N; -. DR IntAct; P38850; 28. DR MINT; P38850; -. DR STRING; 4932.YHR154W; -. DR GlyGen; P38850; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; P38850; -. DR MaxQB; P38850; -. DR PaxDb; 4932-YHR154W; -. DR PeptideAtlas; P38850; -. DR EnsemblFungi; YHR154W_mRNA; YHR154W; YHR154W. DR GeneID; 856559; -. DR KEGG; sce:YHR154W; -. DR AGR; SGD:S000001197; -. DR SGD; S000001197; RTT107. DR VEuPathDB; FungiDB:YHR154W; -. DR eggNOG; KOG2043; Eukaryota. DR HOGENOM; CLU_002149_0_0_1; -. DR InParanoid; P38850; -. DR OMA; QRFYIQR; -. DR OrthoDB; 19990at2759; -. DR BioCyc; YEAST:G3O-31189-MONOMER; -. DR PRO; PR:P38850; -. DR Proteomes; UP000002311; Chromosome VIII. DR RNAct; P38850; Protein. DR GO; GO:0071944; C:cell periphery; HDA:SGD. DR GO; GO:0035361; C:Cul8-RING ubiquitin ligase complex; IDA:SGD. DR GO; GO:0005634; C:nucleus; HDA:SGD. DR GO; GO:1990683; P:DNA double-strand break attachment to nuclear envelope; IMP:SGD. DR GO; GO:0006302; P:double-strand break repair; IMP:SGD. DR GO; GO:0006334; P:nucleosome assembly; NAS:ComplexPortal. DR GO; GO:2000001; P:regulation of DNA damage checkpoint; IMP:SGD. DR GO; GO:1903775; P:regulation of DNA double-strand break processing; IMP:SGD. DR GO; GO:0010526; P:retrotransposon silencing; IMP:SGD. DR Gene3D; 3.40.50.10190; BRCT domain; 4. DR IDEAL; IID50173; -. DR InterPro; IPR001357; BRCT_dom. DR InterPro; IPR036420; BRCT_dom_sf. DR InterPro; IPR031906; RTT107_BRCT_6. DR PANTHER; PTHR47667; REGULATOR OF TY1 TRANSPOSITION PROTEIN 107; 1. DR PANTHER; PTHR47667:SF1; REGULATOR OF TY1 TRANSPOSITION PROTEIN 107; 1. DR Pfam; PF00533; BRCT; 1. DR Pfam; PF12738; PTCB-BRCT; 1. DR Pfam; PF16770; RTT107_BRCT_5; 1. DR Pfam; PF16771; RTT107_BRCT_6; 1. DR SMART; SM00292; BRCT; 4. DR SUPFAM; SSF52113; BRCT domain; 2. DR PROSITE; PS50172; BRCT; 2. PE 1: Evidence at protein level; KW 3D-structure; DNA damage; DNA repair; Nucleus; Phosphoprotein; KW Reference proteome; Repeat. FT CHAIN 1..1070 FT /note="Regulator of Ty1 transposition protein 107" FT /id="PRO_0000097502" FT DOMAIN 2..103 FT /note="BRCT 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033" FT DOMAIN 117..213 FT /note="BRCT 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033" FT DOMAIN 260..352 FT /note="BRCT 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033" FT DOMAIN 369..453 FT /note="BRCT 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033" FT DOMAIN 829..910 FT /note="BRCT 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033" FT DOMAIN 934..1049 FT /note="BRCT 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033" FT REGION 572..659 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 722..753 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 583..659 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 732..753 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 304 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 532 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198" FT MOD_RES 591 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 593 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 720 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 800 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 806 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956, FT ECO:0007744|PubMed:19779198" FT TURN 6..9 FT /evidence="ECO:0007829|PDB:6J0X" FT STRAND 11..16 FT /evidence="ECO:0007829|PDB:6J0Y" FT HELIX 19..21 FT /evidence="ECO:0007829|PDB:6J0Y" FT HELIX 22..34 FT /evidence="ECO:0007829|PDB:6J0Y" FT STRAND 37..44 FT /evidence="ECO:0007829|PDB:6J0Y" FT HELIX 45..47 FT /evidence="ECO:0007829|PDB:6J0Y" FT HELIX 50..52 FT /evidence="ECO:0007829|PDB:6J0Y" FT HELIX 57..64 FT /evidence="ECO:0007829|PDB:6J0Y" FT STRAND 71..73 FT /evidence="ECO:0007829|PDB:6J0Y" FT HELIX 82..86 FT /evidence="ECO:0007829|PDB:6J0Y" FT HELIX 96..105 FT /evidence="ECO:0007829|PDB:6J0Y" FT HELIX 112..114 FT /evidence="ECO:0007829|PDB:6J0Y" FT TURN 121..124 FT /evidence="ECO:0007829|PDB:6J0Y" FT STRAND 126..129 FT /evidence="ECO:0007829|PDB:6J0Y" FT TURN 131..133 FT /evidence="ECO:0007829|PDB:6J0Y" FT HELIX 136..148 FT /evidence="ECO:0007829|PDB:6J0Y" FT STRAND 152..157 FT /evidence="ECO:0007829|PDB:6J0Y" FT STRAND 163..165 FT /evidence="ECO:0007829|PDB:6J0Y" FT HELIX 173..178 FT /evidence="ECO:0007829|PDB:6J0Y" FT STRAND 196..199 FT /evidence="ECO:0007829|PDB:6J0Y" FT STRAND 202..204 FT /evidence="ECO:0007829|PDB:6J0X" FT HELIX 207..215 FT /evidence="ECO:0007829|PDB:6J0Y" FT HELIX 221..226 FT /evidence="ECO:0007829|PDB:6J0Y" FT HELIX 236..247 FT /evidence="ECO:0007829|PDB:6J0Y" FT HELIX 256..259 FT /evidence="ECO:0007829|PDB:6J0Y" FT TURN 263..268 FT /evidence="ECO:0007829|PDB:6J0Y" FT STRAND 270..273 FT /evidence="ECO:0007829|PDB:6J0Y" FT HELIX 281..293 FT /evidence="ECO:0007829|PDB:6J0Y" FT STRAND 297..300 FT /evidence="ECO:0007829|PDB:6J0Y" FT HELIX 307..313 FT /evidence="ECO:0007829|PDB:6J0Y" FT STRAND 319..321 FT /evidence="ECO:0007829|PDB:6J0Y" FT HELIX 328..336 FT /evidence="ECO:0007829|PDB:6J0Y" FT STRAND 341..343 FT /evidence="ECO:0007829|PDB:6J0Y" FT HELIX 345..354 FT /evidence="ECO:0007829|PDB:6J0Y" FT HELIX 360..362 FT /evidence="ECO:0007829|PDB:6J0Y" FT HELIX 365..367 FT /evidence="ECO:0007829|PDB:6J0Y" FT TURN 377..379 FT /evidence="ECO:0007829|PDB:6J0Y" FT STRAND 381..386 FT /evidence="ECO:0007829|PDB:6J0Y" FT HELIX 390..402 FT /evidence="ECO:0007829|PDB:6J0Y" FT STRAND 405..410 FT /evidence="ECO:0007829|PDB:6J0Y" FT STRAND 415..422 FT /evidence="ECO:0007829|PDB:6J0Y" FT HELIX 425..434 FT /evidence="ECO:0007829|PDB:6J0Y" FT TURN 437..439 FT /evidence="ECO:0007829|PDB:6J0Y" FT STRAND 442..444 FT /evidence="ECO:0007829|PDB:6J0Y" FT HELIX 446..455 FT /evidence="ECO:0007829|PDB:6J0Y" FT HELIX 464..466 FT /evidence="ECO:0007829|PDB:6J0Y" FT HELIX 471..473 FT /evidence="ECO:0007829|PDB:6J0Y" FT HELIX 475..477 FT /evidence="ECO:0007829|PDB:6J0Y" FT HELIX 822..827 FT /evidence="ECO:0007829|PDB:3T7K" FT STRAND 837..844 FT /evidence="ECO:0007829|PDB:3T7K" FT HELIX 851..859 FT /evidence="ECO:0007829|PDB:3T7K" FT STRAND 862..864 FT /evidence="ECO:0007829|PDB:3T7K" FT HELIX 870..872 FT /evidence="ECO:0007829|PDB:3T7K" FT STRAND 876..878 FT /evidence="ECO:0007829|PDB:3T7K" FT HELIX 886..891 FT /evidence="ECO:0007829|PDB:3T7K" FT STRAND 899..901 FT /evidence="ECO:0007829|PDB:3T7K" FT HELIX 904..913 FT /evidence="ECO:0007829|PDB:3T7K" FT HELIX 927..930 FT /evidence="ECO:0007829|PDB:3T7I" FT HELIX 937..942 FT /evidence="ECO:0007829|PDB:3T7K" FT STRAND 945..947 FT /evidence="ECO:0007829|PDB:3T7K" FT HELIX 949..952 FT /evidence="ECO:0007829|PDB:3T7K" FT STRAND 957..961 FT /evidence="ECO:0007829|PDB:3T7K" FT HELIX 968..977 FT /evidence="ECO:0007829|PDB:3T7K" FT STRAND 982..986 FT /evidence="ECO:0007829|PDB:3T7K" FT TURN 988..990 FT /evidence="ECO:0007829|PDB:3T7K" FT HELIX 993..995 FT /evidence="ECO:0007829|PDB:3T7K" FT STRAND 1011..1015 FT /evidence="ECO:0007829|PDB:3T7K" FT HELIX 1019..1032 FT /evidence="ECO:0007829|PDB:3T7K" FT STRAND 1038..1041 FT /evidence="ECO:0007829|PDB:3T7K" FT HELIX 1043..1051 FT /evidence="ECO:0007829|PDB:3T7K" FT STRAND 1063..1067 FT /evidence="ECO:0007829|PDB:3T7K" SQ SEQUENCE 1070 AA; 123017 MW; 767931285BB52580 CRC64; MSTSLLFEQL NFLILVAAEA ELPIAHSTRK LLMDNSCNNC QIYELYNENL KDVKTDKDWF MNKFGPQTVH FVISNTINFP FYKIVYFDLL IPVVSHTWVQ DSVKTKRHLR TNMYSPNPFH LLRDCQVYIS KSSFNKCEYI LYSDLLHLLG GTLVNYISNR TTHVIVQSPQ DPIIATVSKL TFGSFSSSST NKHTEKPLRE WKFVYPIWIL YHFKMAKPLK GELATLCELD MQDTSEEQLF AKWEEVIGDK QTSSSQLTLH PNKTLFKNHH FAISPDLNFF TPLYWFLKGF IEDLDGKVTP LSFSDDLKSV YQAFPDIDCY IGHSANSPIL EKTKSIKPEI HVGNVSWLFY MFALQKFTPV SQCKLIHQPF HAKLFTSKEL TVAYTNYFGS QRFYIQRLVE ILGGLSTPEL TRKNTHLITK STIGKKFKVA KKWSLDPQNA IIVTNHMWLE QCYMNNSKLN PKDSRFQNFK LDDNMGWNIG QIGMDHSSLP TPKNLSMVTY DTQSISEKPP PTNDQMDQIN DNTNVLSKKD GTPISSFENS IDEKIDKLQK ISGEVAVTHS GDLERSFVSR PSRASFPVVD SKKSNLQKKD SNSDISMETE VFCEGHEKRE EKEFTKPITE YDAPKKQEIR EQSRKKNDID YKKEEEETEL QVQLGQRTKR EIKTSKKNEK EKETNECHIE VDQMTNEKQG EESTGKLIST EDVTSKKDTD KFSHLFEGLS DNDDHINDEK PAVNSKYTTP KTSQNITSGV DTPTTAQTQV FMPSSGNSRL AKTQAAKRLH TDIESLNEFQ KNFKRKRIDS EEISLSQDVE RSNNNKELAT KAEKILARFN ELPNYDLKAV CTGCFHDGFN EVDIEILNQL GIKIFDNIKE TDKLNCIFAP KILRTEKFLK SLSFEPLKFA LKPEFIIDLL KQIHSKKDKL SQININLFDY EINGINESII SKTKLPTKVF ERANIRCINL VNDIPGGVDT IGSVLKAHGI EKINVLRSKK CTFEDIIPND VSKQENGGIF KYVLIVTKAS QVKKFTKLIN DRDKNETILI VEWNWCVESI FHLNVDFTSK KNVLYQKKNN //