ID H7BXY3_HUMAN Unreviewed; 1166 AA.
AC H7BXY3;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=ATP-dependent RNA helicase DHX30 {ECO:0000256|ARBA:ARBA00039388};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
DE AltName: Full=DEAH box protein 30 {ECO:0000256|ARBA:ARBA00042917};
GN Name=DHX30 {ECO:0000313|Ensembl:ENSP00000343442.4};
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 {ECO:0000313|Ensembl:ENSP00000343442.4, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000343442.4, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [2] {ECO:0007829|PubMed:18669648}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [3] {ECO:0007829|PubMed:19413330}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [4] {ECO:0007829|PubMed:19690332}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [5] {ECO:0007829|PubMed:21269460}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6] {ECO:0007829|PubMed:23186163}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=23186163;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [7] {ECO:0007829|PubMed:24275569}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8] {ECO:0007829|PubMed:25944712}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [9] {ECO:0000313|Ensembl:ENSP00000343442.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001556};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix, mitochondrion nucleoid
CC {ECO:0000256|ARBA:ARBA00004436}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000256|ARBA:ARBA00008792}.
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DR EMBL; AC026318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC139667; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001317919.1; NM_001330990.1.
DR RefSeq; XP_011531798.1; XM_011533496.1.
DR RefSeq; XP_011531799.1; XM_011533497.2.
DR RefSeq; XP_011531800.1; XM_011533498.1.
DR AlphaFoldDB; H7BXY3; -.
DR SMR; H7BXY3; -.
DR IntAct; H7BXY3; 1.
DR MINT; H7BXY3; -.
DR MetOSite; H7BXY3; -.
DR EPD; H7BXY3; -.
DR MassIVE; H7BXY3; -.
DR MaxQB; H7BXY3; -.
DR PeptideAtlas; H7BXY3; -.
DR ProteomicsDB; 43438; -.
DR Antibodypedia; 13009; 186 antibodies from 23 providers.
DR DNASU; 22907; -.
DR Ensembl; ENST00000348968.8; ENSP00000343442.4; ENSG00000132153.15.
DR GeneID; 22907; -.
DR UCSC; uc062jex.1; human.
DR CTD; 22907; -.
DR HGNC; HGNC:16716; DHX30.
DR VEuPathDB; HostDB:ENSG00000132153; -.
DR GeneTree; ENSGT00940000158279; -.
DR OrthoDB; 1095660at2759; -.
DR BioGRID-ORCS; 22907; 155 hits in 1168 CRISPR screens.
DR ChiTaRS; DHX30; human.
DR GenomeRNAi; 22907; -.
DR Proteomes; UP000005640; Chromosome 3.
DR Bgee; ENSG00000132153; Expressed in left testis and 175 other cell types or tissues.
DR ExpressionAtlas; H7BXY3; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR CDD; cd17976; DEXHc_DHX30; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 3.30.160.20; -; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
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:SF229; ATP-DEPENDENT RNA HELICASE DHX30; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion nucleoid {ECO:0000256|ARBA:ARBA00023271};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Proteomics identification {ECO:0007829|EPD:H7BXY3,
KW ECO:0007829|MaxQB:H7BXY3};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640}.
FT DOMAIN 416..584
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 626..799
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 122..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1166 AA; 130550 MW; 9440308B2EECBF0B CRC64;
MCVNPTPGGT ISRASRDLLK EFPQPKNLLN SVIGRALGIS HAKDKLVYVH TNGPKKKKVT
LHIKWPKSVE VEGYGSKKID AERQAAAAAC QLFKGWGLLG PRNELFDAAK YRVLADRFGS
PADSWWRPEP TMPPTSWRQL NPESIRPGGP GGLSRSLGRE EEEDEEEELE EGTIDVTDFL
SMTQQDSHAP LRDSRGSSFE MTDDDSAIRA LTQFPLPKNL LAKVIQIATS SSTAKNLMQF
HTVGTKTKLS TLTLLWPCPM TFVAKGRRKA EAENKAAALA CKKLKSLGLV DRNNEPLTHA
MYNLASLREL GETQRRPCTI QVPEPILRKI ETFLNHYPVE SSWIAPELRL QSDDILPLGK
DSGPLSDPIT GKPYVPLLEA EEVRLSQSLL ELWRRRGPVW QEAPQLPVDP HRDTILNAIE
QHPVVVISGD TGCGKTTRIP QLLLERYVTE GRGARCNVII TQPRRISAVS VAQRVSHELG
PSLRRNVGFQ VRLESKPPSR GGALLFCTVG ILLRKLQSNP SLEGVSHVIV DEVHERDVNT
DFLLILLKGL QRLNPALRLV LMSATGDNER FSRYFGGCPV IKVPGFMYPV KEHYLEDILA
KLGKHQYLHR HRHHESEDEC ALDLDLVTDL VLHIDARGEP GGILCFLPGW QEIKGVQQRL
QEALGMHESK YLILPVHSNI PMMDQKAIFQ QPPVGVRKIV LATNIAETSI TINDIVHVVD
SGLHKEERYD LKTKVSCLET VWVSRANVIQ RRGRAGRCQS GFAYHLFPRS RLEKMVPFQV
PEILRTPLEN LVLQAKIHMP EKTAVEFLSK AVDSPNIKAV DEAVILLQEI GVLDQREYLT
TLGQRLAHIS TDPRLAKAIV LAAIFRCLHP LLVVVSCLTR DPFSSSLQNR AEVDKVKALL
SHDSGSDHLA FVRAVAGWEE VLRWQDRSSR ENYLEENLLY APSLRFIHGL IKQFSENIYE
AFLVGKPSDC TLASAQCNEY SEEEELVKGV LMAGLYPNLI QVRQGKVTRQ GKFKPNSVTY
RTKSGNILLH KSTINREATR LRSRWLTYFM AVKSNGSVFV RDSSQVHPLA VLLLTDGDVH
IRDDGRRATI SLSDSDLLRL EGDSRTVRLL KELRRALGRM VERSLRSELA ALPPSVQEEH
GQLLALLAEL LRGPCGSFDV RKTADD
//
