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DDX23_PONAB
ID   DDX23_PONAB             Reviewed;         820 AA.
AC   Q5RC67;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Probable ATP-dependent RNA helicase DDX23 {ECO:0000250|UniProtKB:Q9BUQ8};
DE            EC=3.6.4.13 {ECO:0000305};
DE   AltName: Full=DEAD box protein 23;
GN   Name=DDX23 {ECO:0000250|UniProtKB:Q9BUQ8};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in pre-mRNA splicing and its phosphorylated form (by
CC       SRPK2) is required for spliceosomal B complex formation. Independently
CC       of its spliceosome formation function, required for the suppression of
CC       incorrect R-loops formed during transcription; R-loops are composed of
CC       a DNA:RNA hybrid and the associated non-template single-stranded DNA.
CC       {ECO:0000250|UniProtKB:Q9BUQ8}.
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         Evidence={ECO:0000250|UniProtKB:Q9BUQ8};
CC   -!- SUBUNIT: The phosphorylated form (by SRPK2) is a component of the
CC       U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at
CC       least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, WDR57,
CC       SNRNP40, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39.
CC       Identified in the spliceosome C complex. Interacts with ERBB4.
CC       Interacts with ERCC6. {ECO:0000250|UniProtKB:Q9BUQ8}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BUQ8}.
CC       Chromosome {ECO:0000250|UniProtKB:Q9BUQ8}. Note=During transcription,
CC       accumulates at chromatin loci where unscheduled R-loops form and
CC       colocalizes with paused 'Ser-5'-phosphorlyated POLR2A/RNA polymerase II
CC       and kinase SRPK2. {ECO:0000250|UniProtKB:Q9BUQ8}.
CC   -!- PTM: In vitro phosphorylated by CLK1 and U1 snRNP-associated protein
CC       kinase. Phosphorylated by SRPK2 and this phosphorylation is required
CC       for its association with the tri-snRNP (U4/U6-U5 tri-small nuclear
CC       ribonucleoproteins) and subsequent spliceosomal B complex formation.
CC       May be phosphorylated by SRPK2 on Ser residues in the SR domain; the
CC       phosphorylation is required for the removal of inappropriate R-loops
CC       during transcription. {ECO:0000250|UniProtKB:Q9BUQ8}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX23/PRP28
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CR858413; CAH90640.1; -; mRNA.
DR   RefSeq; NP_001125347.1; NM_001131875.1.
DR   AlphaFoldDB; Q5RC67; -.
DR   SMR; Q5RC67; -.
DR   STRING; 9601.ENSPPYP00000005101; -.
DR   GeneID; 100172249; -.
DR   KEGG; pon:100172249; -.
DR   CTD; 9416; -.
DR   eggNOG; KOG0333; Eukaryota.
DR   InParanoid; Q5RC67; -.
DR   OrthoDB; 820037at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0000785; C:chromatin; 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:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0062176; P:R-loop disassembly; ISS:UniProtKB.
DR   GO; GO:0008380; P:RNA splicing; 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; 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   2: Evidence at transcript level;
KW   ATP-binding; Chromosome; Helicase; Hydrolase; Isopeptide bond;
KW   mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Spliceosome; Ubl conjugation.
FT   CHAIN           1..820
FT                   /note="Probable ATP-dependent RNA helicase DDX23"
FT                   /id="PRO_0000055129"
FT   DOMAIN          422..627
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          651..799
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           391..419
FT                   /note="Q motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00552"
FT   MOTIF           549..552
FT                   /note="DEAD box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   COMPBIAS        1..40
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..61
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..244
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         435..442
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         14
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUQ8"
FT   MOD_RES         16
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUQ8"
FT   MOD_RES         107
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUQ8"
FT   MOD_RES         109
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUQ8"
FT   CROSSLNK        686
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUQ8"
FT   CROSSLNK        811
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUQ8"
SQ   SEQUENCE   820 AA;  95600 MW;  CBB9738A19E68305 CRC64;
     MAGELADKKD RDASPSKEER KRSRTPDRER DRDRDRKSSP SKDRKRHRSR DRRRGGSRSR
     SRSRSKSAER ERRHKERERD KERDRNKKDR DRDKDGHRRD KDRKRSSLSP GRGKDFKSRK
     DRDSKKDEED EHGDKKPKAQ PLSLEELLAK KKAEEEAEAK PKFLSKAERE AEALKRRQQE
     VEERQRMLEE ERKKRKQFQD LGRKMLEDPQ ERERRERRER MERETNGNED EEGRQKIREE
     KDKSKELHAI KERYLGGIKK RRRTRHLNDR KFVFEWDASE DTSIDYNPLY KERHQVQLLG
     RGFIAGIDLK QQKREQSRFY GDLMEKRRTL EEKEQEEARF RKLRKKEAKQ RWDDRHWSQK
     KLDEMTDRDW RIFREDYSIT TKGGKIPNPI RSWKDSSLPP HILEVIDKCG YKEPTPIQRQ
     AIPIGLQNRD IIGVAETGSG KTAAFLIPLL VWITTLPKID RIEESDQGPY AIILAPTREL
     AQQIEEETIK FGKPLGIRTV AVIGGISRED QGFRLRMGCE IVIATPGRLI DVLENRYLVP
     SRCTYVVLDE ADRMIDMGFE PDVQKILEHM PVSNQKPDTD EAEDPEKMLA NFESGKHKYR
     QTVMFTATMP PAVERLARSY LRRPAVVYIG SAGKPHERVE QKVFLMSESE KRKKLLAILE
     QGFDPPIIIF VNQKKGCDVL AKSLEKMGYN ACTLHGGKGQ EQREFALSNL KAGAKDILVA
     TDVAGRGIDI QDVSMVVNYD MAKNIEDYIH RIGRTGRAGK SGVAITFLTK EDSAVFYELK
     QAILESPVSS CPPELANHPD AQHKPGTILT KKRREETIFA
 
 
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