GenomeNet

Database: UniProt
Entry: DHX35_HUMAN
LinkDB: DHX35_HUMAN
Original site: DHX35_HUMAN 
ID   DHX35_HUMAN             Reviewed;         703 AA.
AC   Q9H5Z1; A2RTX3; B4E0J0; F5GXM6; Q5THR0; Q9H4H7; Q9H6T6;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   24-JAN-2024, entry version 187.
DE   RecName: Full=Probable ATP-dependent RNA helicase DHX35;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAH box protein 35;
GN   Name=DHX35; Synonyms=C20orf15, DDX35;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Ileal mucosa, and Thymus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPLICEOSOMAL
RP   C COMPLEX.
RX   PubMed=11991638; DOI=10.1017/s1355838202021088;
RA   Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT   "Purification and characterization of native spliceosomes suitable for
RT   three-dimensional structural analysis.";
RL   RNA 8:426-439(2002).
CC   -!- FUNCTION: May be involved in pre-mRNA splicing.
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.
CC       {ECO:0000269|PubMed:11991638}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9H5Z1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9H5Z1-2; Sequence=VSP_047178;
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB15166.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; AK026412; BAB15476.1; -; mRNA.
DR   EMBL; AK025541; BAB15166.1; ALT_INIT; mRNA.
DR   EMBL; AK303396; BAG64452.1; -; mRNA.
DR   EMBL; AL023803; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471077; EAW76006.1; -; Genomic_DNA.
DR   EMBL; BC132669; AAI32670.1; -; mRNA.
DR   CCDS; CCDS13310.1; -. [Q9H5Z1-1]
DR   CCDS; CCDS54463.1; -. [Q9H5Z1-2]
DR   RefSeq; NP_001177738.1; NM_001190809.1. [Q9H5Z1-2]
DR   RefSeq; NP_068750.2; NM_021931.3. [Q9H5Z1-1]
DR   AlphaFoldDB; Q9H5Z1; -.
DR   SMR; Q9H5Z1; -.
DR   BioGRID; 121945; 67.
DR   CORUM; Q9H5Z1; -.
DR   IntAct; Q9H5Z1; 32.
DR   MINT; Q9H5Z1; -.
DR   STRING; 9606.ENSP00000252011; -.
DR   iPTMnet; Q9H5Z1; -.
DR   MetOSite; Q9H5Z1; -.
DR   PhosphoSitePlus; Q9H5Z1; -.
DR   SwissPalm; Q9H5Z1; -.
DR   BioMuta; DHX35; -.
DR   EPD; Q9H5Z1; -.
DR   jPOST; Q9H5Z1; -.
DR   MassIVE; Q9H5Z1; -.
DR   MaxQB; Q9H5Z1; -.
DR   PaxDb; 9606-ENSP00000252011; -.
DR   PeptideAtlas; Q9H5Z1; -.
DR   ProteomicsDB; 24470; -.
DR   ProteomicsDB; 80942; -. [Q9H5Z1-1]
DR   Pumba; Q9H5Z1; -.
DR   Antibodypedia; 26936; 86 antibodies from 20 providers.
DR   DNASU; 60625; -.
DR   Ensembl; ENST00000252011.8; ENSP00000252011.3; ENSG00000101452.15. [Q9H5Z1-1]
DR   Ensembl; ENST00000373323.8; ENSP00000362420.3; ENSG00000101452.15. [Q9H5Z1-2]
DR   GeneID; 60625; -.
DR   KEGG; hsa:60625; -.
DR   MANE-Select; ENST00000252011.8; ENSP00000252011.3; NM_021931.4; NP_068750.2.
DR   UCSC; uc002xjh.4; human. [Q9H5Z1-1]
DR   AGR; HGNC:15861; -.
DR   CTD; 60625; -.
DR   GeneCards; DHX35; -.
DR   HGNC; HGNC:15861; DHX35.
DR   HPA; ENSG00000101452; Low tissue specificity.
DR   neXtProt; NX_Q9H5Z1; -.
DR   OpenTargets; ENSG00000101452; -.
DR   PharmGKB; PA27222; -.
DR   VEuPathDB; HostDB:ENSG00000101452; -.
DR   eggNOG; KOG0922; Eukaryota.
DR   GeneTree; ENSGT00940000156142; -.
DR   InParanoid; Q9H5Z1; -.
DR   OMA; FHEVMET; -.
DR   OrthoDB; 5488182at2759; -.
DR   PhylomeDB; Q9H5Z1; -.
DR   TreeFam; TF105843; -.
DR   PathwayCommons; Q9H5Z1; -.
DR   Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR   SignaLink; Q9H5Z1; -.
DR   BioGRID-ORCS; 60625; 204 hits in 1171 CRISPR screens.
DR   ChiTaRS; DHX35; human.
DR   GenomeRNAi; 60625; -.
DR   Pharos; Q9H5Z1; Tbio.
DR   PRO; PR:Q9H5Z1; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; Q9H5Z1; Protein.
DR   Bgee; ENSG00000101452; Expressed in lower esophagus muscularis layer and 132 other cell types or tissues.
DR   ExpressionAtlas; Q9H5Z1; baseline and differential.
DR   Genevisible; Q9H5Z1; HS.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0004386; F:helicase activity; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR   CDD; cd17980; DEXHc_DHX35; 1.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR048333; HA2_WH.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF136; ATP-DEPENDENT RNA HELICASE DHX35-RELATED; 1.
DR   Pfam; PF21010; HA2_C; 1.
DR   Pfam; PF04408; HA2_N; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Helicase; Hydrolase; mRNA processing;
KW   mRNA splicing; Nucleotide-binding; Reference proteome; Spliceosome.
FT   CHAIN           1..703
FT                   /note="Probable ATP-dependent RNA helicase DHX35"
FT                   /id="PRO_0000055168"
FT   DOMAIN          64..229
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          261..438
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           176..179
FT                   /note="DEAH box"
FT   BINDING         77..84
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   VAR_SEQ         59..89
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_047178"
FT   VARIANT         189
FT                   /note="I -> T (in dbSNP:rs36053162)"
FT                   /id="VAR_052184"
FT   VARIANT         703
FT                   /note="P -> L (in dbSNP:rs3752302)"
FT                   /id="VAR_020211"
FT   CONFLICT        35
FT                   /note="T -> I (in Ref. 1; BAG64452)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        582
FT                   /note="R -> G (in Ref. 1; BAB15476)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   703 AA;  78910 MW;  CFC03B2A90CE5819 CRC64;
     MAAPVGPVKF WRPGTEGPGV SISEERQSLA ENSGTTVVYN PYAALSIEQQ RQKLPVFKLR
     NHILYLIENY QTVVIVGETG CGKSTQIPQY LAEAGWTAEG RVVGVTQPRR VAAVTVAGRV
     AEERGAVLGH EVGYCIRFDD CTDQLATRIK FLTDGMLVRE MMVDPLLTKY SVIMLDEAHE
     RTLYTDIAIG LLKKIQKKRG DLRLIVASAT LDADKFRDFF NQNETSDPAR DTCVILTVEG
     RTFPVDIFYL QSPVPDYIKS TVETVVKIHQ TEGDGDVLAF LTGQEEVETV VSMLIEQARA
     LARTGMKRHL RVLPMYAGLP SFEQMKVFER VSRSVRKVIV ATNVAETSIT ISGIVYVIDC
     GFVKLRAYNP RTAIECLVVV PVSQASANQR AGRGGRSRSG KCYRLYTEEA FDKLPQSTVP
     EMQRSNLAPV ILQLKALGID NVLRFHFMSP PPAQSMVQAL ELLYALGGLD KDCRLTEPLG
     MRIAEFPLNP MFAKMLLESG NFGCSQEILS IAAMMQIQNI FVVPPNQKSH AIRVHRKFAV
     EEGDHLTMLN IYEAFIKHNK DSKWCQEHFL NYKGLVRAAT VREQLKKLLV KFQVPRKSSE
     GDPDLVLRCI VSGFFANAAR FHSTGAYRTI RDDHELHIHP ASVLYAEKPP RWVIYNEVIQ
     TSKYYMRDVT AIESAWLLEL APHFYQQGTH LSLKAKRAKV QDP
//
DBGET integrated database retrieval system