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DHX32_MOUSE
ID   DHX32_MOUSE             Reviewed;         744 AA.
AC   Q8BZS9; Q3TFU4; Q8VH39; Q922N6;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Putative pre-mRNA-splicing factor ATP-dependent RNA helicase DHX32;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAH box protein 32;
DE   AltName: Full=MuDDX32;
GN   Name=Dhx32; Synonyms=Ddx32;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   PubMed=12163057; DOI=10.1016/s0145-2126(02)00040-1;
RA   Abdelhaleem M.;
RT   "The novel helicase homologue DDX32 is down-regulated in acute
RT   lymphoblastic leukemia.";
RL   Leuk. Res. 26:945-954(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Amnion, Cecum, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-744 (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Mitochondrion
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BZS9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BZS9-2; Sequence=VSP_026428;
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AY065980; AAL47579.1; -; mRNA.
DR   EMBL; AK033624; BAC28397.1; -; mRNA.
DR   EMBL; AK169005; BAE40804.1; -; mRNA.
DR   EMBL; AK172504; BAE43038.1; -; mRNA.
DR   EMBL; BC006911; AAH06911.1; -; mRNA.
DR   EMBL; BC022920; AAH22920.1; -; mRNA.
DR   CCDS; CCDS21936.1; -. [Q8BZS9-1]
DR   RefSeq; NP_001272959.1; NM_001286030.1. [Q8BZS9-2]
DR   RefSeq; NP_001272960.1; NM_001286031.1. [Q8BZS9-2]
DR   RefSeq; NP_001272961.1; NM_001286032.1.
DR   RefSeq; NP_598702.1; NM_133941.2. [Q8BZS9-2]
DR   RefSeq; XP_006507200.1; XM_006507137.1. [Q8BZS9-2]
DR   RefSeq; XP_006507201.1; XM_006507138.1. [Q8BZS9-2]
DR   AlphaFoldDB; Q8BZS9; -.
DR   SMR; Q8BZS9; -.
DR   BioGRID; 221655; 2.
DR   STRING; 10090.ENSMUSP00000033290; -.
DR   iPTMnet; Q8BZS9; -.
DR   PhosphoSitePlus; Q8BZS9; -.
DR   EPD; Q8BZS9; -.
DR   MaxQB; Q8BZS9; -.
DR   PaxDb; Q8BZS9; -.
DR   PRIDE; Q8BZS9; -.
DR   ProteomicsDB; 279653; -. [Q8BZS9-1]
DR   ProteomicsDB; 279654; -. [Q8BZS9-2]
DR   Antibodypedia; 32435; 164 antibodies from 23 providers.
DR   DNASU; 101437; -.
DR   Ensembl; ENSMUST00000033290; ENSMUSP00000033290; ENSMUSG00000030986. [Q8BZS9-2]
DR   Ensembl; ENSMUST00000063669; ENSMUSP00000066067; ENSMUSG00000030986. [Q8BZS9-2]
DR   GeneID; 101437; -.
DR   KEGG; mmu:101437; -.
DR   UCSC; uc009kdj.1; mouse. [Q8BZS9-2]
DR   UCSC; uc012fvg.1; mouse. [Q8BZS9-1]
DR   CTD; 55760; -.
DR   MGI; MGI:2141813; Dhx32.
DR   VEuPathDB; HostDB:ENSMUSG00000030986; -.
DR   eggNOG; KOG0925; Eukaryota.
DR   GeneTree; ENSGT00940000157227; -.
DR   HOGENOM; CLU_001832_5_11_1; -.
DR   InParanoid; Q8BZS9; -.
DR   OMA; NKEQKMC; -.
DR   OrthoDB; 354219at2759; -.
DR   PhylomeDB; Q8BZS9; -.
DR   TreeFam; TF105735; -.
DR   BioGRID-ORCS; 101437; 0 hits in 73 CRISPR screens.
DR   ChiTaRS; Dhx32; mouse.
DR   PRO; PR:Q8BZS9; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q8BZS9; protein.
DR   Bgee; ENSMUSG00000030986; Expressed in epithelium of lens and 235 other tissues.
DR   ExpressionAtlas; Q8BZS9; baseline and differential.
DR   Genevisible; Q8BZS9; MM.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF04408; HA2; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   SMART; SM00847; HA2; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Helicase; Hydrolase;
KW   Mitochondrion; Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN           1..744
FT                   /note="Putative pre-mRNA-splicing factor ATP-dependent RNA
FT                   helicase DHX32"
FT                   /id="PRO_0000292664"
FT   DOMAIN          72..270
FT                   /note="Helicase ATP-binding"
FT   DOMAIN          258..438
FT                   /note="Helicase C-terminal"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           185..188
FT                   /note="DEAH box"
FT   COMPBIAS        8..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         85..92
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7L7V1"
FT   VAR_SEQ         1
FT                   /note="M -> MSSLREEM (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12163057,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_026428"
FT   CONFLICT        462
FT                   /note="D -> N (in Ref. 2; BAC28397)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        479
FT                   /note="G -> E (in Ref. 3; BAE40804)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   744 AA;  83941 MW;  8B287F5726EFB569 CRC64;
     MDEEELDHPN ASPEKRYFPE SLDSSDGDEE GVLACEDLEL NPFDGLPYSS RYYKLLKERE
     ELPIWKEKYS FMESLLQNQV VVVSGDSKCG KSSQVPQWCA EYCLSIHYQH GGVICTQAHK
     QTAVQLALRV ADEMDVNIGH EVGYVIPFEN CCTTETILRY CTDDMLQREM MSNPFLGSYG
     VIILDDVHER SLATDVLLGL LKDVLLARPE LKLIVNCSPL LTSKLSSYYG DVPVIEVRNK
     HPVEVVYLSG AQKDSFESVI RLIFEIHRSG EKGDVVVFLA CEQDIEKTYE LVCQEGSNLN
     PDVGDLVVIP LYPKEKCSLF RPVDETEKRC QVYQRRVVLT TSCGESLIWS HTVKFVIDVG
     LERRQVYNPR IRANSLVLQP ISQSQAEIRK QLLGSSPSGK LFCLYTEEFA SKDMRPLKPA
     EMQEANLTSM VLFMKRVDIA GLGRCDFMNR PAPESLMQAL EDLDYLAALD NDGNLSEFGI
     IMSEFPLDPQ LSKSILASCE FDCVDEMLTI AAMVTAPSCF LHVPHGAEEA AVTCWKTFLH
     PEGDHFTLIN VYNAYQDTVL NSANEHCVEM WCHDCFLSCS ALRMADVIRA ELLEIIKRIE
     LPYAEPAFGS KENGLNIKKA LLSGYFMQIA RDVDGSGNYL MLTHKQVAQL HPLSSYSITK
     KMPEWVLFHQ FSISENNYIR VASAVSPELF MQLVPQYYFS NLPPSESKDI LQQAAGHLPT
     ETVNKDQDVC DKCPDATEQR CTIQ
 
 
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