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DDX5_PANTR
ID   DDX5_PANTR              Reviewed;         614 AA.
AC   A5A6J2;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Probable ATP-dependent RNA helicase DDX5;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 5;
GN   Name=DDX5;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=17574350; DOI=10.1016/j.gene.2007.04.013;
RA   Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I.,
RA   Kusuda J., Gojobori T., Hashimoto K., Hirai M.;
RT   "Mapping of chimpanzee full-length cDNAs onto the human genome unveils
RT   large potential divergence of the transcriptome.";
RL   Gene 399:1-10(2007).
CC   -!- FUNCTION: Involved in the alternative regulation of pre-mRNA splicing;
CC       its RNA helicase activity is necessary for increasing tau exon 10
CC       inclusion and occurs in a RBM4-dependent manner. Binds to the tau pre-
CC       mRNA in the stem-loop region downstream of exon 10. The rate of ATP
CC       hydrolysis is highly stimulated by single-stranded RNA. Involved in
CC       transcriptional regulation; the function is independent of the RNA
CC       helicase activity. Transcriptional coactivator for androgen receptor AR
CC       but probably not ESR1. Synergizes with DDX17 and SRA1 RNA to activate
CC       MYOD1 transcriptional activity and involved in skeletal muscle
CC       differentiation. Transcriptional coactivator for p53/TP53 and involved
CC       in p53/TP53 transcriptional response to DNA damage and p53/TP53-
CC       dependent apoptosis. Transcriptional coactivator for RUNX2 and involved
CC       in regulation of osteoblast differentiation. Acts as transcriptional
CC       repressor in a promoter-specific manner; the function probably involves
CC       association with histone deacetylases, such as HDAC1. As component of a
CC       large PER complex is involved in the inhibition of 3' transcriptional
CC       termination of circadian target genes such as PER1 and NR1D1 and the
CC       control of the circadian rhythms (By similarity). {ECO:0000250}.
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: Identified in the spliceosome C complex. Component of a
CC       ribonucleoprotein complex containing mRNAs and RNA-binding proteins
CC       including DDX5, HNRNPH2 and SRSF1 as well as splicing regulator ARVCF.
CC       Interacts with RBM4; the interaction occurs in an RNA-independent
CC       manner. Interacts with AGO1 and AGO2. Interacts with ESR1, AR, EP300,
CC       CREBBP, POLR2A, TP53, RUNX2 and HDAC1. Self-associates. Interacts with
CC       DDX17. Interacts with BRDT. The large PER complex involved in the
CC       repression of transcriptional termination is composed of at least PER2,
CC       CDK9, DDX5, DHX9, NCBP1 and POLR2A (active) (By similarity). Interacts
CC       with DHX36; this interaction occurs in a RNA-dependent manner (By
CC       similarity). Interacts with NUPR1 (By similarity). Interacts with ERCC6
CC       (By similarity). Interacts with DDX3X in the cytoplasm; this
CC       interaction may be more efficient when both proteins are
CC       unphosphorylated (By similarity). {ECO:0000250|UniProtKB:P17844,
CC       ECO:0000250|UniProtKB:Q61656}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P17844}. Nucleus,
CC       nucleolus {ECO:0000250|UniProtKB:P17844}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P17844}. Note=During the G0 phase, predominantly
CC       located in the nucleus. Cytoplasmic levels increase during the G1/S
CC       phase. During the M phase, located at the vicinity of the condensed
CC       chromosomes. At G1, localizes in the cytoplasm.
CC       {ECO:0000250|UniProtKB:P17844}.
CC   -!- PTM: Sumoylated; sumoylation, promoted by PIAS1, promotes interaction
CC       with HDAC1 and transcriptional repression activity. Sumoylation also
CC       significantly increases stability, and reduces polyubiquitination (By
CC       similarity). {ECO:0000250|UniProtKB:P17844}.
CC   -!- PTM: Polyubiquitinated, leading to proteasomal degradation.
CC       {ECO:0000250|UniProtKB:P17844}.
CC   -!- PTM: Weakly phosphorylated in the G1/S phase of the cell cycle and much
CC       more at G2/M, especially at Thr and Tyr residues.
CC       {ECO:0000250|UniProtKB:P17844}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX5/DBP2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AB222120; BAF62365.1; -; mRNA.
DR   RefSeq; NP_001138306.1; NM_001144834.1.
DR   AlphaFoldDB; A5A6J2; -.
DR   SMR; A5A6J2; -.
DR   STRING; 9598.ENSPTRP00000016210; -.
DR   PaxDb; A5A6J2; -.
DR   GeneID; 455267; -.
DR   KEGG; ptr:455267; -.
DR   CTD; 1655; -.
DR   eggNOG; KOG0331; Eukaryota.
DR   InParanoid; A5A6J2; -.
DR   OrthoDB; 638613at2759; -.
DR   Proteomes; UP000002277; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR   GO; GO:0050681; F:nuclear androgen receptor binding; ISS:UniProtKB.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR   GO; GO:0043021; F:ribonucleoprotein complex binding; ISS:UniProtKB.
DR   GO; GO:0003724; F:RNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0030521; P:androgen receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:UniProtKB.
DR   GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; ISS:UniProtKB.
DR   GO; GO:0061614; P:miRNA transcription; ISS:UniProtKB.
DR   GO; GO:0045445; P:myoblast differentiation; ISS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; ISS:UniProtKB.
DR   GO; GO:0043517; P:positive regulation of DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
DR   GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0060765; P:regulation of androgen receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0045667; P:regulation of osteoblast differentiation; ISS:UniProtKB.
DR   GO; GO:2001014; P:regulation of skeletal muscle cell differentiation; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
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; IPR012587; P68_rpt.
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   Pfam; PF08061; P68HR; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM01414; P68HR; 2.
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   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Biological rhythms; Cytoplasm; Helicase;
KW   Hydrolase; Isopeptide bond; Methylation; mRNA processing; mRNA splicing;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   RNA-binding; Spliceosome; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..614
FT                   /note="Probable ATP-dependent RNA helicase DDX5"
FT                   /id="PRO_0000295282"
FT   DOMAIN          125..300
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          328..475
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          477..614
FT                   /note="Transactivation domain"
FT                   /evidence="ECO:0000250"
FT   REGION          477..504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           94..122
FT                   /note="Q motif"
FT   MOTIF           248..251
FT                   /note="DEAD box"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         114..116
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   BINDING         121
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         138..145
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         24
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P17844"
FT   MOD_RES         32
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P17844"
FT   MOD_RES         33
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P17844"
FT   MOD_RES         40
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P17844"
FT   MOD_RES         236
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61656"
FT   MOD_RES         297
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P17844"
FT   MOD_RES         480
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P17844"
FT   MOD_RES         520
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P17844"
FT   CROSSLNK        32
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P17844"
FT   CROSSLNK        45
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P17844"
FT   CROSSLNK        53
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO); alternate"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        53
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P17844"
FT   CROSSLNK        53
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P17844"
FT   CROSSLNK        340
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P17844"
FT   CROSSLNK        343
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P17844"
FT   CROSSLNK        388
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P17844"
FT   CROSSLNK        391
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P17844"
FT   CROSSLNK        411
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P17844"
FT   CROSSLNK        437
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P17844"
FT   CROSSLNK        451
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P17844"
FT   CROSSLNK        470
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P17844"
FT   CROSSLNK        523
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P17844"
SQ   SEQUENCE   614 AA;  69119 MW;  C2EE4FB0B759513F CRC64;
     MSGYSSDRDR GRDRGFGAPR FGGSRAGPLS GKKFGNPGEK LVKKKWNLDE LPKFEKNFYQ
     EHPDLARRTA QEVETYRRSK EITVRGHNCP KPVLNFYEAN FPANVMDVIA RQNFTEPTAI
     QAQGWPVALS GLDMVGVAQT GSGKTLSYLL PAIVHINHQP FLERGDGPIC LVLAPTRELA
     QQVQQVAAEY CRACRLKSTC IYGGAPKGPQ IRDLERGVEN CIATPGRLID FLECGKTNLR
     RTTYLVLDEA DRMLDMGFEP QIRKIVDQIR PDRQTLMWSA TWPKEVRQLA EDFLKDYIHI
     NIGALELSAN HNILQIVDVC HDVEKDEKLI RLMEEIMSEK ENKTIVFVET KRRCDELTRK
     MRRDGWPAMG IHGDKSQQER DWVLNEFKHG KAPILIATDV ASRGLDVEDV KFVINYDYPN
     SSEDYIHRIG RTARSTKTGT AYTFFTPNNI KQVSDLISVL REANQAINPK LLQLVEDRGS
     GRSRGRGGMK DDRRDRYSAG KRGGFNTFRD RENYDRGYSS LLKRDFGAKT QNGVYSAANY
     TNGSFGSNFV SAGIQASFRT GNPTGTYQNG YDSTQQYGSN VPNMHNGMNQ QAYAYPATAA
     APMIGYPMPT GYSQ
 
 
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