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Q9GZR7 (DDX24_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP-dependent RNA helicase DDX24

EC=3.6.4.13
Alternative name(s):
DEAD box protein 24
Gene names
Name:DDX24
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length859 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

ATP-dependent RNA helicase Potential.

Catalytic activity

ATP + H2O = ADP + phosphate.

Tissue specificity

Ubiquitous. Most abundant in heart and brain, but with lowest levels in thymus and small intestine.

Sequence similarities

Belongs to the DEAD box helicase family. DDX24/MAK5 subfamily.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Ontologies

Keywords
   Coding sequence diversityPolymorphism
   LigandATP-binding
Nucleotide-binding
RNA-binding
   Molecular functionHelicase
Hydrolase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Non-traceable author statement Ref.1. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

nucleolus

Inferred from direct assay. Source: LIFEdb

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent RNA helicase activity

Non-traceable author statement. Source: UniProtKB

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 859859ATP-dependent RNA helicase DDX24
PRO_0000055029

Regions

Domain224 – 528305Helicase ATP-binding
Domain578 – 723146Helicase C-terminal
Nucleotide binding237 – 2448ATP By similarity
Motif192 – 22029Q motif
Motif471 – 4744DEAD box
Compositional bias83 – 897Poly-Glu
Compositional bias153 – 1619Poly-Lys
Compositional bias835 – 84511Poly-Lys

Amino acid modifications

Modified residue171N6-acetyllysine Ref.10
Modified residue711N6-acetyllysine Ref.10
Modified residue821Phosphoserine Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.13
Modified residue941Phosphoserine Ref.7 Ref.9
Modified residue2871Phosphoserine Ref.7 Ref.9
Modified residue2951Phosphoserine Ref.7 Ref.9
Modified residue3021Phosphothreonine Ref.7

Natural variations

Natural variant3161E → K.
Corresponds to variant rs35413935 [ dbSNP | Ensembl ].
VAR_052162

Sequences

Sequence LengthMass (Da)Tools
Q9GZR7 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: B01B1170B2CFA0F7

FASTA85996,332
        10         20         30         40         50         60 
MKLKDTKSRP KQSSCGKFQT KGIKVVGKWK EVKIDPNMFA DGQMDDLVCF EELTDYQLVS 

        70         80         90        100        110        120 
PAKNPSSLFS KEAPKRKAQA VSEEEEEEEG KSSSPKKKIK LKKSKNVATE GTSTQKEFEV 

       130        140        150        160        170        180 
KDPELEAQGD DMVCDDPEAG EMTSENLVQT APKKKKNKGK KGLEPSQSTA AKVPKKAKTW 

       190        200        210        220        230        240 
IPEVHDQKAD VSAWKDLFVP RPVLRALSFL GFSAPTPIQA LTLAPAIRDK LDILGAAETG 

       250        260        270        280        290        300 
SGKTLAFAIP MIHAVLQWQK RNAAPPPSNT EAPPGETRTE AGAETRSPGK AEAESDALPD 

       310        320        330        340        350        360 
DTVIESEALP SDIAAEARAK TGGTVSDQAL LFGDDDAGEG PSSLIREKPV PKQNENEEEN 

       370        380        390        400        410        420 
LDKEQTGNLK QELDDKSATC KAYPKRPLLG LVLTPTRELA VQVKQHIDAV ARFTGIKTAI 

       430        440        450        460        470        480 
LVGGMSTQKQ QRMLNRRPEI VVATPGRLWE LIKEKHYHLR NLRQLRCLVV DEADRMVEKG 

       490        500        510        520        530        540 
HFAELSQLLE MLNDSQYNPK RQTLVFSATL TLVHQAPARI LHKKHTKKMD KTAKLDLLMQ 

       550        560        570        580        590        600 
KIGMRGKPKV IDLTRNEATV ETLTETKIHC ETDEKDFYLY YFLMQYPGRS LVFANSISCI 

       610        620        630        640        650        660 
KRLSGLLKVL DIMPLTLHAC MHQKQRLRNL EQFARLEDCV LLATDVAARG LDIPKVQHVI 

       670        680        690        700        710        720 
HYQVPRTSEI YVHRSGRTAR ATNEGLSLML IGPEDVINFK KIYKTLKKDE DIPLFPVQTK 

       730        740        750        760        770        780 
YMDVVKERIR LARQIEKSEY RNFQACLHNS WIEQAAAALE IELEEDMYKG GKADQQEERR 

       790        800        810        820        830        840 
RQKQMKVLKK ELRHLLSQPL FTESQKTKYP TQSGKPPLLV SAPSKSESAL SCLSKQKKKK 

       850 
TKKPKEPQPE QPQPSTSAN 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of human DDX24 and mouse Ddx24, two novel putative DEAD-box proteins, and mapping DDX24 to human chromosome 14q32."
Zhao Y., Yu L., Fu Q., Chen W., Jiang J., Gao J., Zhao S.
Genomics 67:351-355(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Colon.
[4]"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].
Tissue: Uterus.
[5]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[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-82, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-94; SER-287; SER-295 AND THR-302, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[8]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, MASS SPECTROMETRY.
Tissue: Liver.
[9]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-94; SER-287 AND SER-295, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[10]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17 AND LYS-71, MASS SPECTROMETRY.
[11]"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-82, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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-82, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF214731 mRNA. Translation: AAG02169.1.
AL136886 mRNA. Translation: CAB66820.1.
AK025162 mRNA. Translation: BAB15079.1.
BC008847 mRNA. Translation: AAH08847.1.
BC009406 mRNA. Translation: AAH09406.1.
IPIIPI00006987.
RefSeqNP_065147.1. NM_020414.3.
UniGeneHs.510328.

3D structure databases

ProteinModelPortalQ9GZR7.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-47301N.
IntActQ9GZR7. 35 interactions.
MINTMINT-1378437.
STRING9606.ENSP00000328690.

PTM databases

PhosphoSiteQ9GZR7.

Polymorphism databases

DMDM18202929.

2D gel databases

SWISS-2DPAGEQ9GZR7.

Proteomic databases

PaxDbQ9GZR7.
PeptideAtlasQ9GZR7.
PRIDEQ9GZR7.

Protocols and materials databases

DNASU57062.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000330836; ENSP00000328690; ENSG00000089737.
GeneID57062.
KEGGhsa:57062.
UCSCuc001ycj.3. human.

Organism-specific databases

CTD57062.
GeneCardsGC14M094517.
HGNCHGNC:13266. DDX24.
HPAHPA002554.
MIM606181. gene.
neXtProtNX_Q9GZR7.
PharmGKBPA27211.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0513.
HOGENOMHOG000290702.
HOVERGENHBG104200.
InParanoidQ9GZR7.
KOK14805.
OMADQQEERR.
PhylomeDBQ9GZR7.

Gene expression databases

ArrayExpressQ9GZR7.
BgeeQ9GZR7.
CleanExHS_DDX24.
GenevestigatorQ9GZR7.
GermOnlineENSG00000089737. Homo sapiens.

Family and domain databases

InterProIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
PROSITEPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDDX24. human.
GenomeRNAi57062.
NextBio62861.
SOURCESearch...

Entry information

Entry nameDDX24_HUMAN
AccessionPrimary (citable) accession number: Q9GZR7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: March 1, 2001
Last modified: May 29, 2013
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families