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Putative pre-mRNA-splicing factor ATP-dependent RNA helicase DHX32 (EC 3.6.4.13) (DEAD/H box 32) (DEAD/H helicase-like protein 1) (DHLP1) (DEAH box protein 32) (HuDDX32)

 DHX32_HUMAN             Reviewed;         743 AA.
Q7L7V1; A8MSV2; D3DRF9; Q49AG5; Q5T3L0; Q5T3L5; Q96NY1; Q9BUN0;
Q9H769; Q9NSL5; Q9NV74; Q9NVJ7;
26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
10-OCT-2018, entry version 131.
RecName: Full=Putative pre-mRNA-splicing factor ATP-dependent RNA helicase DHX32;
EC=3.6.4.13;
AltName: Full=DEAD/H box 32;
AltName: Full=DEAD/H helicase-like protein 1;
Short=DHLP1;
AltName: Full=DEAH box protein 32;
AltName: Full=HuDDX32;
Name=DHX32; Synonyms=DDX32;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF
230-414 (ISOFORM 2), INDUCTION, AND TISSUE SPECIFICITY.
TISSUE=Myeloid leukemia cell;
PubMed=12163057; DOI=10.1016/S0145-2126(02)00040-1;
Abdelhaleem M.;
"The novel helicase homologue DDX32 is down-regulated in acute
lymphoblastic leukemia.";
Leuk. Res. 26:945-954(2002).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=12527204; DOI=10.1016/S0378-1119(02)01098-3;
Meng X., Liu J., Shen Z.;
"Genomic structure of the human BCCIP gene and its expression in
cancer.";
Gene 302:139-146(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon, and Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, Kidney, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 238-743 (ISOFORM 1).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[8]
INDUCTION.
PubMed=16414036; DOI=10.1016/j.cellimm.2005.12.003;
Alli Z., Nam E.H., Beimnet K., Abdelhaleem M.;
"The activation-induced expression of DHX32 in Jurkat T cells is
specific and involves calcium and nuclear factor of activated T
cells.";
Cell. Immunol. 237:141-146(2005).
[9]
TISSUE SPECIFICITY.
PubMed=16181624; DOI=10.1016/j.yexmp.2005.07.002;
Alli Z., Ho M., Abdelhaleem M.;
"Expression of DHX32 in lymphoid tissues.";
Exp. Mol. Pathol. 79:219-223(2005).
[10]
SUBCELLULAR LOCATION.
PubMed=16959245; DOI=10.1016/j.yexmp.2006.07.005;
Alli Z., Ackerley C., Chen Y., Al-Saud B., Abdelhaleem M.;
"Nuclear and mitochondrial localization of the putative RNA helicase
DHX32.";
Exp. Mol. Pathol. 81:245-248(2006).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[12]
VARIANT [LARGE SCALE ANALYSIS] ARG-209.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- INTERACTION:
Q3B820:FAM161A; NbExp=7; IntAct=EBI-2807297, EBI-719941;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16959245}.
Mitochondrion {ECO:0000269|PubMed:16959245}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q7L7V1-1; Sequence=Displayed;
Name=2;
IsoId=Q7L7V1-2; Sequence=VSP_026427;
-!- TISSUE SPECIFICITY: Expressed in lymphoid tissues (at protein
level). Expressed in brain, heart, skeletal muscle, colon, thymus,
spleen, kidney, liver, small intestine, placenta, lung, lymphoid
tissues and blood leukocytes. {ECO:0000269|PubMed:12163057,
ECO:0000269|PubMed:16181624}.
-!- INDUCTION: Up-regulated by ionomycin in T-lymphocytes. Down-
regulated in acute lymphoblastic leukemia.
{ECO:0000269|PubMed:12163057, ECO:0000269|PubMed:16414036}.
-!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH37925.1; Type=Frameshift; Positions=439; Evidence={ECO:0000305};
Sequence=BAB15029.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF427340; AAL26550.1; -; mRNA.
EMBL; AF427341; AAL26551.1; -; mRNA.
EMBL; AY064247; AAL55437.1; -; Genomic_DNA.
EMBL; AY064250; AAL55441.1; -; mRNA.
EMBL; AK001556; BAA91754.1; -; mRNA.
EMBL; AK001751; BAA91882.1; -; mRNA.
EMBL; AK024869; BAB15029.1; ALT_INIT; mRNA.
EMBL; AL360176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471066; EAW49216.1; -; Genomic_DNA.
EMBL; CH471066; EAW49217.1; -; Genomic_DNA.
EMBL; BC002473; AAH02473.3; -; mRNA.
EMBL; BC037925; AAH37925.1; ALT_FRAME; mRNA.
EMBL; BC068471; AAH68471.1; -; mRNA.
EMBL; AL162051; CAB82394.1; -; mRNA.
CCDS; CCDS7652.1; -. [Q7L7V1-1]
PIR; T47184; T47184.
RefSeq; NP_060650.2; NM_018180.2. [Q7L7V1-1]
RefSeq; XP_016871893.1; XM_017016404.1.
RefSeq; XP_016871894.1; XM_017016405.1.
UniGene; Hs.370292; -.
ProteinModelPortal; Q7L7V1; -.
SMR; Q7L7V1; -.
BioGrid; 120878; 9.
IntAct; Q7L7V1; 2.
STRING; 9606.ENSP00000284690; -.
iPTMnet; Q7L7V1; -.
PhosphoSitePlus; Q7L7V1; -.
BioMuta; DHX32; -.
DMDM; 74759011; -.
EPD; Q7L7V1; -.
MaxQB; Q7L7V1; -.
PaxDb; Q7L7V1; -.
PeptideAtlas; Q7L7V1; -.
PRIDE; Q7L7V1; -.
ProteomicsDB; 68827; -.
ProteomicsDB; 68828; -. [Q7L7V1-2]
DNASU; 55760; -.
Ensembl; ENST00000284690; ENSP00000284690; ENSG00000089876. [Q7L7V1-1]
GeneID; 55760; -.
KEGG; hsa:55760; -.
UCSC; uc001ljf.1; human. [Q7L7V1-1]
CTD; 55760; -.
DisGeNET; 55760; -.
EuPathDB; HostDB:ENSG00000089876.11; -.
GeneCards; DHX32; -.
HGNC; HGNC:16717; DHX32.
HPA; HPA048872; -.
MIM; 607960; gene.
neXtProt; NX_Q7L7V1; -.
OpenTargets; ENSG00000089876; -.
PharmGKB; PA27219; -.
eggNOG; KOG0925; Eukaryota.
eggNOG; COG1643; LUCA.
GeneTree; ENSGT00900000140964; -.
HOVERGEN; HBG039428; -.
InParanoid; Q7L7V1; -.
KO; K18994; -.
OMA; YSSRYYK; -.
OrthoDB; EOG091G025L; -.
PhylomeDB; Q7L7V1; -.
TreeFam; TF105735; -.
ChiTaRS; DHX32; human.
GeneWiki; DHX32; -.
GenomeRNAi; 55760; -.
PRO; PR:Q7L7V1; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000089876; Expressed in 229 organ(s), highest expression level in epithelium of bronchus.
ExpressionAtlas; Q7L7V1; baseline and differential.
Genevisible; Q7L7V1; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004004; F:ATP-dependent RNA helicase activity; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; IBA:GO_Central.
GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
InterPro; IPR011709; DUF1605.
InterPro; IPR007502; Helicase-assoc_dom.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF04408; HA2; 1.
Pfam; PF07717; OB_NTP_bind; 1.
SMART; SM00847; HA2; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; ATP-binding; Complete proteome;
Helicase; Hydrolase; Mitochondrion; Nucleotide-binding; Nucleus;
Polymorphism; Reference proteome.
CHAIN 1 743 Putative pre-mRNA-splicing factor ATP-
dependent RNA helicase DHX32.
/FTId=PRO_0000292663.
DOMAIN 72 238 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
NP_BIND 85 92 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
MOTIF 185 188 DEAH box.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
VAR_SEQ 284 364 Missing (in isoform 2).
{ECO:0000303|PubMed:12163057}.
/FTId=VSP_026427.
VARIANT 209 209 P -> R (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035843.
VARIANT 271 271 E -> D (in dbSNP:rs11244674).
/FTId=VAR_052181.
VARIANT 301 301 D -> A (in dbSNP:rs35772239).
/FTId=VAR_052182.
VARIANT 430 430 V -> L (in dbSNP:rs17153669).
/FTId=VAR_052183.
CONFLICT 26 26 D -> G (in Ref. 3; BAA91754).
{ECO:0000305}.
CONFLICT 123 123 V -> M (in Ref. 3; BAA91882).
{ECO:0000305}.
CONFLICT 171 171 M -> V (in Ref. 3; BAA91754).
{ECO:0000305}.
CONFLICT 231 231 N -> F (in Ref. 1; AAL26551).
{ECO:0000305}.
CONFLICT 459 459 L -> S (in Ref. 3; BAA91882).
{ECO:0000305}.
CONFLICT 496 496 A -> G (in Ref. 3; BAA91882).
{ECO:0000305}.
CONFLICT 499 499 E -> G (in Ref. 6; AAH37925).
{ECO:0000305}.
CONFLICT 567 567 V -> A (in Ref. 3; BAB15029).
{ECO:0000305}.
CONFLICT 590 590 E -> G (in Ref. 6; AAH37925).
{ECO:0000305}.
CONFLICT 686 686 P -> L (in Ref. 3; BAA91882).
{ECO:0000305}.
SEQUENCE 743 AA; 84419 MW; D6D5C570561C468A CRC64;
MEEEGLECPN SSSEKRYFPE SLDSSDGDEE EVLACEDLEL NPFDGLPYSS RYYKLLKERE
DLPIWKEKYS FMENLLQNQI VIVSGDAKCG KSAQVPQWCA EYCLSIHYQH GGVICTQVHK
QTVVQLALRV ADEMDVNIGH EVGYVIPFEN CCTNETILRY CTDDMLQREM MSNPFLGSYG
VIILDDIHER SIATDVLLGL LKDVLLARPE LKLIINSSPH LISKLNSYYG NVPVIEVKNK
HPVEVVYLSE AQKDSFESIL RLIFEIHHSG EKGDIVVFLA CEQDIEKVCE TVYQGSNLNP
DLGELVVVPL YPKEKCSLFK PLDETEKRCQ VYQRRVVLTT SSGEFLIWSN SVRFVIDVGV
ERRKVYNPRI RANSLVMQPI SQSQAEIRKQ ILGSSSSGKF FCLYTEEFAS KDMTPLKPAE
MQEANLTSMV LFMKRIDIAG LGHCDFMNRP APESLMQALE DLDYLAALDN DGNLSEFGII
MSEFPLDPQL SKSILASCEF DCVDEVLTIA AMVTAPNCFS HVPHGAEEAA LTCWKTFLHP
EGDHFTLISI YKAYQDTTLN SSSEYCVEKW CRDYFLNCSA LRMADVIRAE LLEIIKRIEL
PYAEPAFGSK ENTLNIKKAL LSGYFMQIAR DVDGSGNYLM LTHKQVAQLH PLSGYSITKK
MPEWVLFHKF SISENNYIRI TSEISPELFM QLVPQYYFSN LPPSESKDIL QQVVDHLSPV
STMNKEQQMC ETCPETEQRC TLQ


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EIAAB10782 ATP-dependent RNA helicase DDX3X,DBX,DDX3,DDX3X,DEAD box protein 3, X-chromosomal,DEAD box, X isoform,Helicase-like protein 2,HLP2,Homo sapiens,Human
EIAAB10697 ATP-dependent RNA helicase DDX19B,DBP5,DDX19,DDX19B,DEAD box protein 19B,DEAD box RNA helicase DEAD5,Homo sapiens,Human,TDBP


 

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