位置:首页 > 蛋白库 > DBP5_YEAST
DBP5_YEAST
ID   DBP5_YEAST              Reviewed;         482 AA.
AC   P20449; D6W2B2;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 211.
DE   RecName: Full=ATP-dependent RNA helicase DBP5;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 5;
DE   AltName: Full=Helicase CA5/6;
DE   AltName: Full=Ribonucleic acid-trafficking protein 8;
GN   Name=DBP5; Synonyms=RAT8; OrderedLocusNames=YOR046C;
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].
RA   Chang T.-H.;
RL   Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 237-425.
RX   PubMed=2406722; DOI=10.1073/pnas.87.4.1571;
RA   Chang T.-H., Arenas J., Abelson J.;
RT   "Identification of five putative yeast RNA helicase genes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:1571-1575(1990).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-171; LEU-220;
RP   PHE-236; VAL-345 AND THR-466.
RX   PubMed=9564047; DOI=10.1093/emboj/17.9.2651;
RA   Tseng S.S.-I., Weaver P.L., Liu Y., Hitomi M., Tartakoff A.M., Chang T.-H.;
RT   "Dbp5p, a cytosolic RNA helicase, is required for poly(A)+ RNA export.";
RL   EMBO J. 17:2651-2662(1998).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PRO-170; LEU-267 AND
RP   ILE-385.
RX   PubMed=9564048; DOI=10.1093/emboj/17.9.2663;
RA   Snay-Hodge C.A., Colot H.V., Goldstein A.L., Cole C.N.;
RT   "Dbp5p/Rat8p is a yeast nuclear pore-associated DEAD-box protein essential
RT   for RNA export.";
RL   EMBO J. 17:2663-2676(1998).
RN   [7]
RP   FUNCTION, INTERACTION WITH NUP159, ASSOCIATION WITH THE NUCLEAR PORE
RP   COMPLEX, AND SUBCELLULAR LOCATION.
RX   PubMed=10428971; DOI=10.1093/emboj/18.15.4332;
RA   Schmitt C., von Kobbe C., Bachi A., Pante N., Rodrigues J.P., Boscheron C.,
RA   Rigaut G., Wilm M., Seraphin B., Carmo-Fonseca M., Izaurralde E.;
RT   "Dbp5, a DEAD-box protein required for mRNA export, is recruited to the
RT   cytoplasmic fibrils of nuclear pore complex via a conserved interaction
RT   with CAN/Nup159p.";
RL   EMBO J. 18:4332-4347(1999).
RN   [8]
RP   FUNCTION, INTERACTION WITH GLE1, SUBCELLULAR LOCATION, AND ASSOCIATION WITH
RP   THE NUCLEAR PORE COMPLEX.
RX   PubMed=10610322; DOI=10.1093/emboj/18.20.5761;
RA   Strahm Y., Fahrenkrog B., Zenklusen D., Rychner E., Kantor J., Rosbach M.,
RA   Stutz F.;
RT   "The RNA export factor Gle1p is located on the cytoplasmic fibrils of the
RT   NPC and physically interacts with the FG-nucleoporin Rip1p, the DEAD-box
RT   protein Rat8p/Dbp5p and a new protein Ymr255p.";
RL   EMBO J. 18:5761-5777(1999).
RN   [9]
RP   FUNCTION, INTERACTION WITH NUP159 AND GLE1, ASSOCIATION WITH THE NUCLEAR
RP   PORE COMPLEX, AND SUBCELLULAR LOCATION.
RX   PubMed=10523319; DOI=10.1093/emboj/18.20.5778;
RA   Hodge C.A., Colot H.V., Stafford P., Cole C.N.;
RT   "Rat8p/Dbp5p is a shuttling transport factor that interacts with
RT   Rat7p/Nup159p and Gle1p and suppresses the mRNA export defect of xpo1-1
RT   cells.";
RL   EMBO J. 18:5778-5788(1999).
RN   [10]
RP   FUNCTION.
RX   PubMed=11350039; DOI=10.1017/s1355838201010147;
RA   Hilleren P., Parker R.;
RT   "Defects in the mRNA export factors Rat7p, Gle1p, Mex67p, and Rat8p cause
RT   hyperadenylation during 3'-end formation of nascent transcripts.";
RL   RNA 7:753-764(2001).
RN   [11]
RP   FUNCTION.
RX   PubMed=12192043; DOI=10.1128/mcb.22.18.6441-6457.2002;
RA   Hammell C.M., Gross S., Zenklusen D., Heath C.V., Stutz F., Moore C.,
RA   Cole C.N.;
RT   "Coupling of termination, 3' processing, and mRNA export.";
RL   Mol. Cell. Biol. 22:6441-6457(2002).
RN   [12]
RP   FUNCTION, AND INTERACTION WITH TFB1; TFB2 AND RAD3.
RX   PubMed=12686617; DOI=10.1091/mbc.e02-09-0602;
RA   Estruch F., Cole C.N.;
RT   "An early function during transcription for the yeast mRNA export factor
RT   Dbp5p/Rat8p suggested by its genetic and physical interactions with
RT   transcription factor IIH components.";
RL   Mol. Biol. Cell 14:1664-1676(2003).
RN   [13]
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   [14]
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   [15]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15280434; DOI=10.1242/jcs.01296;
RA   Takemura R., Inoue Y., Izawa S.;
RT   "Stress response in yeast mRNA export factor: reversible changes in Rat8p
RT   localization are caused by ethanol stress but not heat shock.";
RL   J. Cell Sci. 117:4189-4197(2004).
RN   [16]
RP   FUNCTION, INTERACTION WITH NUP159, AND SUBCELLULAR LOCATION.
RX   PubMed=15574330; DOI=10.1016/j.molcel.2004.10.032;
RA   Weirich C.S., Erzberger J.P., Berger J.M., Weis K.;
RT   "The N-terminal domain of Nup159 forms a beta-propeller that functions in
RT   mRNA export by tethering the helicase Dbp5 to the nuclear pore.";
RL   Mol. Cell 16:749-760(2004).
RN   [17]
RP   FUNCTION, AND INTERACTION WITH GFD1 AND ZDS1.
RX   PubMed=15619606; DOI=10.1074/jbc.m413025200;
RA   Estruch F., Hodge C.A., Rodriguez-Navarro S., Cole C.N.;
RT   "Physical and genetic interactions link the yeast protein Zds1p with mRNA
RT   nuclear export.";
RL   J. Biol. Chem. 280:9691-9697(2005).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, 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   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-162, 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   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93, 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: ATP-dependent RNA helicase associated with the nuclear pore
CC       complex and essential for mRNA export from the nucleus. May participate
CC       in a terminal step of mRNA export through the removal of proteins that
CC       accompany mRNA through the nucleopore complex. Contributes to the
CC       blocking of bulk poly(A)+ mRNA export in ethanol-stressed cells. May
CC       also be involved in early transcription. {ECO:0000269|PubMed:10428971,
CC       ECO:0000269|PubMed:10523319, ECO:0000269|PubMed:10610322,
CC       ECO:0000269|PubMed:11350039, ECO:0000269|PubMed:12192043,
CC       ECO:0000269|PubMed:12686617, ECO:0000269|PubMed:15280434,
CC       ECO:0000269|PubMed:15574330, ECO:0000269|PubMed:15619606,
CC       ECO:0000269|PubMed:9564047, ECO:0000269|PubMed:9564048}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- SUBUNIT: Associates with the nuclear pore complex. Interacts with
CC       NUP159, GLE1, GFD1 and ZDS1. The interaction with NUP159 is necessary
CC       for the association to the nuclear pore complex. Interacts also with
CC       the TFIIH complex subunits TFB1, TFB2 and RAD3.
CC       {ECO:0000269|PubMed:10428971, ECO:0000269|PubMed:10523319,
CC       ECO:0000269|PubMed:10610322, ECO:0000269|PubMed:12686617,
CC       ECO:0000269|PubMed:15574330, ECO:0000269|PubMed:15619606}.
CC   -!- INTERACTION:
CC       P20449; Q04839: GFD1; NbExp=2; IntAct=EBI-5617, EBI-27549;
CC       P20449; Q12315: GLE1; NbExp=8; IntAct=EBI-5617, EBI-7635;
CC       P20449; P50111: ZDS1; NbExp=3; IntAct=EBI-5617, EBI-29626;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nuclear pore complex. Nucleus
CC       membrane; Peripheral membrane protein; Cytoplasmic side. Note=Nuclear
CC       pore complex cytoplasmic fibrils. Accumulates in the nucleus rapidly
CC       and reversibly in response to ethanol stress.
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC       family of RNA helicases and controls ATP binding and hydrolysis.
CC   -!- MISCELLANEOUS: Present with 14900 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX19/DBP5
CC       subfamily. {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; U28135; AAB01679.1; -; Genomic_DNA.
DR   EMBL; Z74954; CAA99237.1; -; Genomic_DNA.
DR   EMBL; Z74955; CAA99239.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10828.1; -; Genomic_DNA.
DR   PIR; S66920; S66920.
DR   RefSeq; NP_014689.1; NM_001183465.1.
DR   PDB; 2KBE; NMR; -; A=71-296.
DR   PDB; 2KBF; NMR; -; A=296-482.
DR   PDB; 3GFP; X-ray; 1.80 A; A=296-482.
DR   PDB; 3PEU; X-ray; 2.60 A; A=297-482.
DR   PDB; 3PEV; X-ray; 2.50 A; A=297-482.
DR   PDB; 3PEW; X-ray; 1.50 A; A=91-482.
DR   PDB; 3PEY; X-ray; 1.40 A; A=91-482.
DR   PDB; 3RRM; X-ray; 2.88 A; A=91-482.
DR   PDB; 3RRN; X-ray; 4.00 A; A=91-482.
DR   PDB; 5ELX; X-ray; 1.81 A; A=91-481.
DR   PDBsum; 2KBE; -.
DR   PDBsum; 2KBF; -.
DR   PDBsum; 3GFP; -.
DR   PDBsum; 3PEU; -.
DR   PDBsum; 3PEV; -.
DR   PDBsum; 3PEW; -.
DR   PDBsum; 3PEY; -.
DR   PDBsum; 3RRM; -.
DR   PDBsum; 3RRN; -.
DR   PDBsum; 5ELX; -.
DR   AlphaFoldDB; P20449; -.
DR   SMR; P20449; -.
DR   BioGRID; 34447; 490.
DR   DIP; DIP-2352N; -.
DR   IntAct; P20449; 9.
DR   MINT; P20449; -.
DR   STRING; 4932.YOR046C; -.
DR   iPTMnet; P20449; -.
DR   MaxQB; P20449; -.
DR   PaxDb; P20449; -.
DR   PRIDE; P20449; -.
DR   EnsemblFungi; YOR046C_mRNA; YOR046C; YOR046C.
DR   GeneID; 854211; -.
DR   KEGG; sce:YOR046C; -.
DR   SGD; S000005572; DBP5.
DR   VEuPathDB; FungiDB:YOR046C; -.
DR   eggNOG; KOG0332; Eukaryota.
DR   GeneTree; ENSGT00940000173368; -.
DR   HOGENOM; CLU_003041_1_0_1; -.
DR   InParanoid; P20449; -.
DR   OMA; EYCTPIQ; -.
DR   BioCyc; YEAST:G3O-33590-MON; -.
DR   EvolutionaryTrace; P20449; -.
DR   PRO; PR:P20449; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; P20449; protein.
DR   GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044614; C:nuclear pore cytoplasmic filaments; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0005844; C:polysome; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0008186; F:ATP-dependent activity, acting on RNA; IDA:SGD.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IDA:SGD.
DR   GO; GO:0006406; P:mRNA export from nucleus; IMP:SGD.
DR   GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:SGD.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006415; P:translational termination; IGI:SGD.
DR   GO; GO:0006409; P:tRNA export from nucleus; IDA:SGD.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cytoplasm; Helicase; Hydrolase; Membrane;
KW   mRNA transport; Nuclear pore complex; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Protein transport; Reference proteome; RNA-binding;
KW   Translocation; Transport.
FT   CHAIN           1..482
FT                   /note="ATP-dependent RNA helicase DBP5"
FT                   /id="PRO_0000055019"
FT   DOMAIN          125..292
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          303..480
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           92..120
FT                   /note="Q motif"
FT   MOTIF           239..242
FT                   /note="DEAD box"
FT   BINDING         138..145
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         86
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956"
FT   MOD_RES         93
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         162
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MUTAGEN         170
FT                   /note="P->H: In RAT8-7; accumulates poly(A)+ RNA in the
FT                   nucleus at 16 degrees Celsius."
FT                   /evidence="ECO:0000269|PubMed:9564048"
FT   MUTAGEN         171
FT                   /note="S->P: In DBP5-2; accumulates poly(A)+ RNA in the
FT                   nucleus at 37 degrees Celsius; when associated with L-236
FT                   and F-245."
FT                   /evidence="ECO:0000269|PubMed:9564047"
FT   MUTAGEN         220
FT                   /note="L->P: In DBP5-1; accumulates poly(A)+ RNA in the
FT                   nucleus at 37 degrees Celsius; when associated with S-466."
FT                   /evidence="ECO:0000269|PubMed:9564047"
FT   MUTAGEN         236
FT                   /note="F->L: In DBP5-2; accumulates poly(A)+ RNA in the
FT                   nucleus at 37 degrees Celsius; when associated with P-171
FT                   and F-245."
FT                   /evidence="ECO:0000269|PubMed:9564047"
FT   MUTAGEN         267
FT                   /note="L->P: In RAT8-2; accumulates poly(A)+ RNA in the
FT                   nucleus at 16 and 37 degrees Celsius."
FT                   /evidence="ECO:0000269|PubMed:9564048"
FT   MUTAGEN         345
FT                   /note="V->F: In DBP5-2; accumulates poly(A)+ RNA in the
FT                   nucleus at 37 degrees Celsius; when associated with P-171
FT                   and L-236."
FT                   /evidence="ECO:0000269|PubMed:9564047"
FT   MUTAGEN         385
FT                   /note="I->D: In RAT8-3; accumulates poly(A)+ RNA in the
FT                   nucleus at 16 and 37 degrees Celsius."
FT                   /evidence="ECO:0000269|PubMed:9564048"
FT   MUTAGEN         466
FT                   /note="T->S: In DBP5-1; accumulates poly(A)+ RNA in the
FT                   nucleus at 37 degrees Celsius; when associated with P-220."
FT                   /evidence="ECO:0000269|PubMed:9564047"
FT   STRAND          78..80
FT                   /evidence="ECO:0007829|PDB:2KBE"
FT   HELIX           83..85
FT                   /evidence="ECO:0007829|PDB:2KBE"
FT   HELIX           87..90
FT                   /evidence="ECO:0007829|PDB:2KBE"
FT   HELIX           94..97
FT                   /evidence="ECO:0007829|PDB:2KBE"
FT   HELIX           101..109
FT                   /evidence="ECO:0007829|PDB:3PEY"
FT   STRAND          110..113
FT                   /evidence="ECO:0007829|PDB:2KBE"
FT   HELIX           117..127
FT                   /evidence="ECO:0007829|PDB:3PEY"
FT   STRAND          128..130
FT                   /evidence="ECO:0007829|PDB:3RRM"
FT   STRAND          134..137
FT                   /evidence="ECO:0007829|PDB:3PEY"
FT   HELIX           144..155
FT                   /evidence="ECO:0007829|PDB:3PEY"
FT   STRAND          165..168
FT                   /evidence="ECO:0007829|PDB:3PEY"
FT   HELIX           172..185
FT                   /evidence="ECO:0007829|PDB:3PEY"
FT   TURN            186..188
FT                   /evidence="ECO:0007829|PDB:3PEY"
FT   STRAND          193..197
FT                   /evidence="ECO:0007829|PDB:3PEY"
FT   STRAND          203..205
FT                   /evidence="ECO:0007829|PDB:5ELX"
FT   STRAND          210..214
FT                   /evidence="ECO:0007829|PDB:3PEY"
FT   HELIX           216..224
FT                   /evidence="ECO:0007829|PDB:3PEY"
FT   STRAND          235..239
FT                   /evidence="ECO:0007829|PDB:3PEY"
FT   HELIX           241..246
FT                   /evidence="ECO:0007829|PDB:3PEY"
FT   HELIX           250..259
FT                   /evidence="ECO:0007829|PDB:3PEY"
FT   TURN            261..264
FT                   /evidence="ECO:0007829|PDB:2KBE"
FT   STRAND          266..272
FT                   /evidence="ECO:0007829|PDB:3PEY"
FT   HELIX           276..285
FT                   /evidence="ECO:0007829|PDB:3PEY"
FT   STRAND          290..292
FT                   /evidence="ECO:0007829|PDB:3PEY"
FT   HELIX           296..298
FT                   /evidence="ECO:0007829|PDB:3PEY"
FT   TURN            301..303
FT                   /evidence="ECO:0007829|PDB:3GFP"
FT   STRAND          304..310
FT                   /evidence="ECO:0007829|PDB:3PEY"
FT   HELIX           314..325
FT                   /evidence="ECO:0007829|PDB:3PEY"
FT   TURN            326..329
FT                   /evidence="ECO:0007829|PDB:3PEY"
FT   STRAND          330..336
FT                   /evidence="ECO:0007829|PDB:3PEY"
FT   HELIX           340..352
FT                   /evidence="ECO:0007829|PDB:3PEY"
FT   STRAND          358..360
FT                   /evidence="ECO:0007829|PDB:3PEY"
FT   STRAND          362..364
FT                   /evidence="ECO:0007829|PDB:3RRM"
FT   HELIX           366..377
FT                   /evidence="ECO:0007829|PDB:3PEY"
FT   TURN            378..380
FT                   /evidence="ECO:0007829|PDB:2KBF"
FT   STRAND          383..386
FT                   /evidence="ECO:0007829|PDB:3PEY"
FT   HELIX           388..390
FT                   /evidence="ECO:0007829|PDB:3PEY"
FT   STRAND          391..393
FT                   /evidence="ECO:0007829|PDB:3PEY"
FT   STRAND          399..406
FT                   /evidence="ECO:0007829|PDB:3PEY"
FT   STRAND          413..415
FT                   /evidence="ECO:0007829|PDB:3PEY"
FT   HELIX           417..424
FT                   /evidence="ECO:0007829|PDB:3PEY"
FT   HELIX           425..427
FT                   /evidence="ECO:0007829|PDB:3PEV"
FT   STRAND          434..440
FT                   /evidence="ECO:0007829|PDB:3PEY"
FT   HELIX           443..455
FT                   /evidence="ECO:0007829|PDB:3PEY"
FT   TURN            456..458
FT                   /evidence="ECO:0007829|PDB:3PEU"
FT   STRAND          462..465
FT                   /evidence="ECO:0007829|PDB:3GFP"
FT   HELIX           469..480
FT                   /evidence="ECO:0007829|PDB:3PEY"
SQ   SEQUENCE   482 AA;  53874 MW;  C50CAFE8C060D46B CRC64;
     MSDTKRDPAD LLASLKIDNE KEDTSEVSTK ETVKSQPEKT ADSIKPAEKL VPKVEEKKTK
     QEDSNLISSE YEVKVKLADI QADPNSPLYS AKSFDELGLA PELLKGIYAM KFQKPSKIQE
     RALPLLLHNP PRNMIAQSQS GTGKTAAFSL TMLTRVNPED ASPQAICLAP SRELARQTLE
     VVQEMGKFTK ITSQLIVPDS FEKNKQINAQ VIVGTPGTVL DLMRRKLMQL QKIKIFVLDE
     ADNMLDQQGL GDQCIRVKRF LPKDTQLVLF SATFADAVRQ YAKKIVPNAN TLELQTNEVN
     VDAIKQLYMD CKNEADKFDV LTELYGLMTI GSSIIFVATK KTANVLYGKL KSEGHEVSIL
     HGDLQTQERD RLIDDFREGR SKVLITTNVL ARGIDIPTVS MVVNYDLPTL ANGQADPATY
     IHRIGRTGRF GRKGVAISFV HDKNSFNILS AIQKYFGDIE MTRVPTDDWD EVEKIVKKVL
     KD
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024