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Protein

ATP-dependent RNA helicase DHX29

Gene

DHX29

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

ATP-binding RNA helicase involved in translation initiation. Part of the 43S preinitiation complex that is required for efficient initiation on mammalian mRNAs with structured 5'-UTRs by promoting efficient NTPase-dependent 48S complex formation. Specifically binds to the 40S ribosome near the mRNA entrance. Does not possess a processive helicase activity.2 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi595 – 6028ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent RNA helicase activity Source: GO_Central
  • poly(A) RNA binding Source: UniProtKB
  • ribosomal small subunit binding Source: UniProtKB
  • translation initiation factor activity Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Initiation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent RNA helicase DHX29 (EC:3.6.4.13)
Alternative name(s):
DEAH box protein 29
Nucleic acid helicase DDXx
Gene namesi
Name:DHX29
Synonyms:DDX29
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:15815. DHX29.

Subcellular locationi

GO - Cellular componenti

  • eukaryotic 43S preinitiation complex Source: UniProtKB
  • mitochondrion Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27215.

Polymorphism and mutation databases

BioMutaiDHX29.
DMDMi110278938.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13691369ATP-dependent RNA helicase DHX29PRO_0000245535Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei71 – 711PhosphoserineCombined sources
Modified residuei192 – 1921PhosphoserineCombined sources
Modified residuei200 – 2001PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ7Z478.
MaxQBiQ7Z478.
PaxDbiQ7Z478.
PeptideAtlasiQ7Z478.
PRIDEiQ7Z478.

PTM databases

iPTMnetiQ7Z478.
PhosphoSiteiQ7Z478.

Expressioni

Gene expression databases

BgeeiQ7Z478.
CleanExiHS_DHX29.
ExpressionAtlasiQ7Z478. baseline and differential.
GenevisibleiQ7Z478. HS.

Organism-specific databases

HPAiHPA038317.
HPA038318.

Interactioni

Subunit structurei

Part of the 43S preinitiation complex that contains at least Met-tRNA, EIF1, EIF1A (EIF1AX or EIF1AY), EIF2S1, EIF2S2, EIF2S3, EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L, EIF3M, DHX29 and the 40S ribosomal subunit.1 Publication

Protein-protein interaction databases

BioGridi120001. 26 interactions.
IntActiQ7Z478. 12 interactions.
MINTiMINT-1376685.
STRINGi9606.ENSP00000251636.

Structurei

3D structure databases

ProteinModelPortaliQ7Z478.
SMRiQ7Z478. Positions 520-754, 868-1292.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini582 – 755174Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini849 – 1026178Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili221 – 31191Sequence analysisAdd
BLAST
Coiled coili492 – 51928Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi702 – 7054DEAH box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi10 – 5344Ala-richAdd
BLAST
Compositional biasi789 – 7935Poly-Glu

Sequence similaritiesi

Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0920. Eukaryota.
COG1643. LUCA.
GeneTreeiENSGT00760000119189.
HOGENOMiHOG000247063.
HOVERGENiHBG081436.
InParanoidiQ7Z478.
KOiK18995.
OrthoDBiEOG7SV0TS.
PhylomeDBiQ7Z478.
TreeFamiTF324744.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR011709. DUF1605.
IPR007502. Helicase-assoc_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF04408. HA2. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07717. OB_NTP_bind. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00847. HA2. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS00690. DEAH_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7Z478-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGGKNKKHKA PAAAVVRAAV SASRAKSAEA GIAGEAQSKK PVSRPATAAA
60 70 80 90 100
AAAGSREPRV KQGPKIYSFN STNDSSGPAN LDKSILKVVI NNKLEQRIIG
110 120 130 140 150
VINEHKKQNN DKGMISGRLT AKKLQDLYMA LQAFSFKTKD IEDAMTNTLL
160 170 180 190 200
YGGDLHSALD WLCLNLSDDA LPEGFSQEFE EQQPKSRPKF QSPQIQATIS
210 220 230 240 250
PPLQPKTKTY EEDPKSKPKK EEKNMEVNMK EWILRYAEQQ NEEEKNENSK
260 270 280 290 300
SLEEEEKFDP NERYLHLAAK LLDAKEQAAT FKLEKNKQGQ KEAQEKIRKF
310 320 330 340 350
QREMETLEDH PVFNPAMKIS HQQNERKKPP VATEGESALN FNLFEKSAAA
360 370 380 390 400
TEEEKDKKKE PHDVRNFDYT ARSWTGKSPK QFLIDWVRKN LPKSPNPSFE
410 420 430 440 450
KVPVGRYWKC RVRVIKSEDD VLVVCPTILT EDGMQAQHLG ATLALYRLVK
460 470 480 490 500
GQSVHQLLPP TYRDVWLEWS DAEKKREELN KMETNKPRDL FIAKLLNKLK
510 520 530 540 550
QQQQQQQQHS ENKRENSEDP EESWENLVSD EDFSALSLES ANVEDLEPVR
560 570 580 590 600
NLFRKLQSTP KYQKLLKERQ QLPVFKHRDS IVETLKRHRV VVVAGETGSG
610 620 630 640 650
KSTQVPHFLL EDLLLNEWEA SKCNIVCTQP RRISAVSLAN RVCDELGCEN
660 670 680 690 700
GPGGRNSLCG YQIRMESRAC ESTRLLYCTT GVLLRKLQED GLLSNVSHVI
710 720 730 740 750
VDEVHERSVQ SDFLLIILKE ILQKRSDLHL ILMSATVDSE KFSTYFTHCP
760 770 780 790 800
ILRISGRSYP VEVFHLEDII EETGFVLEKD SEYCQKFLEE EEEVTINVTS
810 820 830 840 850
KAGGIKKYQE YIPVQTGAHA DLNPFYQKYS SRTQHAILYM NPHKINLDLI
860 870 880 890 900
LELLAYLDKS PQFRNIEGAV LIFLPGLAHI QQLYDLLSND RRFYSERYKV
910 920 930 940 950
IALHSILSTQ DQAAAFTLPP PGVRKIVLAT NIAETGITIP DVVFVIDTGR
960 970 980 990 1000
TKENKYHESS QMSSLVETFV SKASALQRQG RAGRVRDGFC FRMYTRERFE
1010 1020 1030 1040 1050
GFMDYSVPEI LRVPLEELCL HIMKCNLGSP EDFLSKALDP PQLQVISNAM
1060 1070 1080 1090 1100
NLLRKIGACE LNEPKLTPLG QHLAALPVNV KIGKMLIFGA IFGCLDPVAT
1110 1120 1130 1140 1150
LAAVMTEKSP FTTPIGRKDE ADLAKSALAM ADSDHLTIYN AYLGWKKARQ
1160 1170 1180 1190 1200
EGGYRSEITY CRRNFLNRTS LLTLEDVKQE LIKLVKAAGF SSSTTSTSWE
1210 1220 1230 1240 1250
GNRASQTLSF QEIALLKAVL VAGLYDNVGK IIYTKSVDVT EKLACIVETA
1260 1270 1280 1290 1300
QGKAQVHPSS VNRDLQTHGW LLYQEKIRYA RVYLRETTLI TPFPVLLFGG
1310 1320 1330 1340 1350
DIEVQHRERL LSIDGWIYFQ APVKIAVIFK QLRVLIDSVL RKKLENPKMS
1360
LENDKILQII TELIKTENN
Length:1,369
Mass (Da):155,236
Last modified:July 11, 2006 - v2
Checksum:iF720A77D224C7F59
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti121 – 1211A → D in CAH56172 (PubMed:17974005).Curated
Sequence conflicti185 – 1851K → E in CAH56153 (PubMed:17974005).Curated
Sequence conflicti356 – 3561D → G in AAK64516 (Ref. 1) Curated
Sequence conflicti885 – 8851D → G in CAH56172 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti309 – 3091D → A.
Corresponds to variant rs35874395 [ dbSNP | Ensembl ].
VAR_052180
Natural varianti630 – 6301P → H.1 Publication
Corresponds to variant rs17854904 [ dbSNP | Ensembl ].
VAR_026985

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY036974 mRNA. Translation: AAK64516.1.
BC056219 mRNA. Translation: AAH56219.1.
AL834496 mRNA. Translation: CAD39154.1.
BX648101 mRNA. Translation: CAH56172.1.
BX648269 mRNA. Translation: CAH56153.1.
AL079292 mRNA. Translation: CAB45191.1.
AF070639 mRNA. Translation: AAC25394.1.
CCDSiCCDS34158.1.
RefSeqiNP_061903.2. NM_019030.2.
UniGeneiHs.593268.

Genome annotation databases

EnsembliENST00000251636; ENSP00000251636; ENSG00000067248.
GeneIDi54505.
KEGGihsa:54505.
UCSCiuc003jpx.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY036974 mRNA. Translation: AAK64516.1.
BC056219 mRNA. Translation: AAH56219.1.
AL834496 mRNA. Translation: CAD39154.1.
BX648101 mRNA. Translation: CAH56172.1.
BX648269 mRNA. Translation: CAH56153.1.
AL079292 mRNA. Translation: CAB45191.1.
AF070639 mRNA. Translation: AAC25394.1.
CCDSiCCDS34158.1.
RefSeqiNP_061903.2. NM_019030.2.
UniGeneiHs.593268.

3D structure databases

ProteinModelPortaliQ7Z478.
SMRiQ7Z478. Positions 520-754, 868-1292.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120001. 26 interactions.
IntActiQ7Z478. 12 interactions.
MINTiMINT-1376685.
STRINGi9606.ENSP00000251636.

PTM databases

iPTMnetiQ7Z478.
PhosphoSiteiQ7Z478.

Polymorphism and mutation databases

BioMutaiDHX29.
DMDMi110278938.

Proteomic databases

EPDiQ7Z478.
MaxQBiQ7Z478.
PaxDbiQ7Z478.
PeptideAtlasiQ7Z478.
PRIDEiQ7Z478.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000251636; ENSP00000251636; ENSG00000067248.
GeneIDi54505.
KEGGihsa:54505.
UCSCiuc003jpx.4. human.

Organism-specific databases

CTDi54505.
GeneCardsiDHX29.
H-InvDBHIX0004866.
HGNCiHGNC:15815. DHX29.
HPAiHPA038317.
HPA038318.
MIMi612720. gene.
neXtProtiNX_Q7Z478.
PharmGKBiPA27215.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0920. Eukaryota.
COG1643. LUCA.
GeneTreeiENSGT00760000119189.
HOGENOMiHOG000247063.
HOVERGENiHBG081436.
InParanoidiQ7Z478.
KOiK18995.
OrthoDBiEOG7SV0TS.
PhylomeDBiQ7Z478.
TreeFamiTF324744.

Miscellaneous databases

ChiTaRSiDHX29. human.
GenomeRNAii54505.
NextBioi56869.
PROiQ7Z478.
SOURCEiSearch...

Gene expression databases

BgeeiQ7Z478.
CleanExiHS_DHX29.
ExpressionAtlasiQ7Z478. baseline and differential.
GenevisibleiQ7Z478. HS.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR011709. DUF1605.
IPR007502. Helicase-assoc_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF04408. HA2. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07717. OB_NTP_bind. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00847. HA2. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS00690. DEAH_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a new member of the DDx subfamily of helicases."
    Abdelhaleem M.M.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-630.
    Tissue: Brain.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 57-1369.
    Tissue: Amygdala, Fetal kidney and Testis.
  4. Bassi M.T., Banfi S., Riboni M., Ballabio A., Borsani G.
    Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 561-1369.
  5. Yu W., Gibbs R.A.
    Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1119-1369.
    Tissue: Brain.
  6. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192 AND SER-200, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Translation initiation on mammalian mRNAs with structured 5'UTRs requires DExH-box protein DHX29."
    Pisareva V.P., Pisarev A.V., Komar A.A., Hellen C.U.T., Pestova T.V.
    Cell 135:1237-1250(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RIBOSOME-BINDING, IDENTIFICATION BY MASS SPECTROMETRY.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192 AND SER-200, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71 AND SER-200, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. "Structure of the mammalian ribosomal 43S preinitiation complex bound to the scanning factor DHX29."
    Hashem Y., des Georges A., Dhote V., Langlois R., Liao H.Y., Grassucci R.A., Hellen C.U., Pestova T.V., Frank J.
    Cell 153:1108-1119(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.6 ANGSTROMS) IN COMPLEX WITH THE 43S PRE-INITIATION COMPLEX, FUNCTION, SUBUNIT.

Entry informationi

Entry nameiDHX29_HUMAN
AccessioniPrimary (citable) accession number: Q7Z478
Secondary accession number(s): O75549
, Q63HN0, Q63HN3, Q8IWW2, Q8N3A1, Q9UMH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: July 11, 2006
Last modified: April 13, 2016
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.