位置:首页 > 蛋白库 > RFX1_YEAST
RFX1_YEAST
ID   RFX1_YEAST              Reviewed;         811 AA.
AC   P48743; D6VYI0;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=RFX-like DNA-binding protein RFX1;
GN   Name=RFX1; Synonyms=CRT1; OrderedLocusNames=YLR176C; ORFNames=L9470.18;
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=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
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   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   [4]
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, 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   -!- INTERACTION:
CC       P48743; P14922: CYC8; NbExp=2; IntAct=EBI-15036, EBI-18215;
CC       P48743; P16649: TUP1; NbExp=2; IntAct=EBI-15036, EBI-19654;
CC   -!- MISCELLANEOUS: Present with 377 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the RFX family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00858}.
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; U17246; AAB67470.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09496.1; -; Genomic_DNA.
DR   PIR; S51421; S51421.
DR   RefSeq; NP_013277.1; NM_001182063.1.
DR   AlphaFoldDB; P48743; -.
DR   SMR; P48743; -.
DR   BioGRID; 31447; 176.
DR   DIP; DIP-6790N; -.
DR   IntAct; P48743; 18.
DR   MINT; P48743; -.
DR   STRING; 4932.YLR176C; -.
DR   iPTMnet; P48743; -.
DR   MaxQB; P48743; -.
DR   PaxDb; P48743; -.
DR   PRIDE; P48743; -.
DR   EnsemblFungi; YLR176C_mRNA; YLR176C; YLR176C.
DR   GeneID; 850873; -.
DR   KEGG; sce:YLR176C; -.
DR   SGD; S000004166; RFX1.
DR   VEuPathDB; FungiDB:YLR176C; -.
DR   eggNOG; KOG3712; Eukaryota.
DR   GeneTree; ENSGT01050000244970; -.
DR   HOGENOM; CLU_011526_2_0_1; -.
DR   InParanoid; P48743; -.
DR   OMA; AQYASSC; -.
DR   BioCyc; YEAST:G3O-32301-MON; -.
DR   PRO; PR:P48743; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; P48743; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR   GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:SGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR003150; DNA-bd_RFX.
DR   InterPro; IPR039779; RFX-like.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR12619; PTHR12619; 1.
DR   Pfam; PF02257; RFX_DNA_binding; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS51526; RFX_DBD; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Phosphoprotein; Reference proteome.
FT   CHAIN           1..811
FT                   /note="RFX-like DNA-binding protein RFX1"
FT                   /id="PRO_0000215295"
FT   DNA_BIND        285..360
FT                   /note="RFX-type winged-helix"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00858"
FT   REGION          48..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          111..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          181..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          377..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..85
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..209
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        400..432
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         173
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   811 AA;  90584 MW;  116A88B7DDE4FBF0 CRC64;
     MVIFKERKPT ENLFTRKIPA KYFIFSPSFL SVHYFEFYLP MSGDNNIEPT SRGSNDNSNG
     PSNGSSVNSN RYSLNAPKYS SQPPPASHTY LPPMSVNIPP IASKSSSIYS LLHQSSPRPE
     TPNPILPPLI GSGPGSHKPS PTPTQPPAQP ATQRQPATYS VYPASISLNR SNSSAYPLSF
     KSEETLNNNP PTAAKRTNTF PSIPSSTKKQ KTSQEKRISS ISRRNTQEII AKQIAENNKS
     KTIEEYAQIV KHAEIKVLSM DSQNTSKAAL QLAEQNRERE RQVFALLWLM KNCKSQHDSY
     VPRGKIFAQY ASSCSQNNLK PLSQASLGKL IRTVFPDLTT RRLGMRGQSK YHYCGLKLTV
     NESGSVSLNN NNASLSLVHN NDPISPLSSP SPSSPSPQVP NVSSPFSLNR KSLSRTGSPV
     KQSSNDNPNE PELESQHPNE TEANKLDSLP PAANNPTGTL SSDELTFTHD LIEKVFNCND
     KLSDNYNTQI LSNTEHPLLT SYKLDFPKIP AGVLPTDTDS DVISSLESLY HIHCNSVYEC
     IKFLKSDNIS NALFFSNSNS ISPTMFNLFI SEPLIDWVTK CDLITYTGLI KFFSQFIIHS
     NEISDSIIQK LESMIKLLPE QINKAVLELP KALVQRKLSI INNFTKLVKK LIKLLKFILN
     FLKSFPIFKS GMNNDWKNIV NLDDILEMMI NEDDTNSETN TIMQHLQGFC QVFVTKFLNS
     SMSVSNDPSV SIECKSLNEM IKDFCSFISL QSKFSCLKLI DCSTRFRNAI IGDISLKSNE
     NLLSWLFLNN VMGQLLNYCF EVMKFVNGLK V
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024