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O60231 (DHX16_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 150. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative pre-mRNA-splicing factor ATP-dependent RNA helicase DHX16

EC=3.6.4.13
Alternative name(s):
ATP-dependent RNA helicase #3
DEAH-box protein 16
Gene names
Name:DHX16
Synonyms:DBP2, DDX16, KIAA0577
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1041 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable ATP-binding RNA helicase involved in pre-mRNA splicing.

Catalytic activity

ATP + H2O = ADP + phosphate.

Subcellular location

Nucleus.

Sequence similarities

Belongs to the DEAD box helicase family. DEAH subfamily. DDX16/PRP8 sub-subfamily.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Sequence caution

The sequence BAA25503.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionHelicase
Hydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA splicing

Traceable author statement Ref.1. Source: ProtInc

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleus

Inferred from direct assay. Source: HPA

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent helicase activity

Inferred from electronic annotation. Source: InterPro

RNA helicase activity

Traceable author statement Ref.1. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10411041Putative pre-mRNA-splicing factor ATP-dependent RNA helicase DHX16
PRO_0000055151

Regions

Domain409 – 573165Helicase ATP-binding
Domain598 – 771174Helicase C-terminal
Nucleotide binding422 – 4298ATP By similarity
Motif520 – 5234DEAH box

Amino acid modifications

Modified residue1031Phosphoserine Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.14
Modified residue1061Phosphoserine Ref.8 Ref.12
Modified residue1071Phosphoserine Ref.8 Ref.12 Ref.14
Modified residue1601Phosphoserine Ref.6 Ref.12 Ref.14

Natural variations

Natural variant3521K → E.
Corresponds to variant rs17189239 [ dbSNP | Ensembl ].
VAR_057236
Natural variant5021L → F.
Corresponds to variant rs17189232 [ dbSNP | Ensembl ].
VAR_057237
Natural variant5661D → G. Ref.4
Corresponds to variant rs9262138 [ dbSNP | Ensembl ].
VAR_057238

Experimental info

Sequence conflict2231V → I in BAA25908. Ref.1
Sequence conflict6311R → P in BAA25908. Ref.1
Sequence conflict6811L → P in BAA25908. Ref.1
Sequence conflict7921A → T in BAA25908. Ref.1
Sequence conflict8991Y → C in BAA25908. Ref.1
Sequence conflict10321K → KK in AAH08825. Ref.5
Sequence conflict10321K → KK in AAH09392. Ref.5

Sequences

Sequence LengthMass (Da)Tools
O60231 [UniParc].

Last modified November 28, 2002. Version 2.
Checksum: 5CAC4DBEF21A4E6D

FASTA1,041119,264
        10         20         30         40         50         60 
MATPAGLERW VQDELHSVLG LSERHVAQFL IGTAQRCTSA EEFVQRLRDT DTLDLSGPAR 

        70         80         90        100        110        120 
DFALRLWNKV PRKAVVEKPA RAAEREARAL LEKNRSYRLL EDSEESSEET VSRAGSSLQK 

       130        140        150        160        170        180 
KRKKRKHLRK KREEEEEEEA SEKGKKKTGG SKQQTEKPES EDEWERTERE RLQDLEERDA 

       190        200        210        220        230        240 
FAERVRQRDK DRTRNVLERS DKKAYEEAQK RLKMAEEDRK AMVPELRKKS RREYLAKRER 

       250        260        270        280        290        300 
EKLEDLEAEL ADEEFLFGDV ELSRHERQEL KYKRRVRDLA REYRAAGEQE KLEATNRYHM 

       310        320        330        340        350        360 
PKETRGQPAR AVDLVEEESG APGEEQRRWE EARLGAASLK FGARDAASQE PKYQLVLEEE 

       370        380        390        400        410        420 
ETIEFVRATQ LQGDEEPSAP PTSTQAQQKE SIQAVRRSLP VFPFREELLA AIANHQVLII 

       430        440        450        460        470        480 
EGETGSGKTT QIPQYLFEEG YTNKGMKIAC TQPRRVAAMS VAARVAREMG VKLGNEVGYS 

       490        500        510        520        530        540 
IRFEDCTSER TVLRYMTDGM LLREFLSEPD LASYSVVMVD EAHERTLHTD ILFGLIKDVA 

       550        560        570        580        590        600 
RFRPELKVLV ASATMDTARF STFFDDAPVF RIPGRRFPVD IFYTKAPEAD YLEACVVSVL 

       610        620        630        640        650        660 
QIHVTQPPGD ILVFLTGQEE IEAACEMLQD RCRRLGSKIR ELLVLPIYAN LPSDMQARIF 

       670        680        690        700        710        720 
QPTPPGARKV VVATNIAETS LTIEGIIYVL DPGFCKQKSY NPRTGMESLT VTPCSKASAN 

       730        740        750        760        770        780 
QRAGRAGRVA AGKCFRLYTA WAYQHELEET TVPEIQRTSL GNVVLLLKSL GIHDLMHFDF 

       790        800        810        820        830        840 
LDPPPYETLL LALEQLYALG ALNHLGELTT SGRKMAELPV DPMLSKMILA SEKYSCSEEI 

       850        860        870        880        890        900 
LTVAAMLSVN NSIFYRPKDK VVHADNARVN FFLPGGDHLV LLNVYTQWAE SGYSSQWCYE 

       910        920        930        940        950        960 
NFVQFRSMRR ARDVREQLEG LLERVEVGLS SCQGDYIRVR KAITAGYFYH TARLTRSGYR 

       970        980        990       1000       1010       1020 
TVKQQQTVFI HPNSSLFEQQ PRWLLYHELV LTTKEFMRQV LEIESSWLLE VAPHYYKAKE 

      1030       1040 
LEDPHAKKMP KKIGKTREEL G 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of a human DEAH-box RNA helicase, a functional homolog of fission yeast Cdc28/Prp8."
Imamura O., Saiki K., Tani T., Ohshima Y., Sugawara M., Furuichi Y.
Nucleic Acids Res. 26:2063-2068(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."
Shiina S., Tamiya G., Oka A., Inoko H.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLY-566.
[5]"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: Brain.
[6]"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-103 AND SER-160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"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-103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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-103; SER-106 AND SER-107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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-103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[10]"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].
[11]"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-103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"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-103; SER-106; SER-107 AND SER-160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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].
[14]"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-103; SER-107 AND SER-160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB001601 mRNA. Translation: BAA25908.1.
BA000025 Genomic DNA. Translation: BAB63323.1.
AB011149 mRNA. Translation: BAA25503.2. Different initiation.
AL845353 Genomic DNA. Translation: CAI41883.1.
BC008825 mRNA. Translation: AAH08825.1.
BC009392 mRNA. Translation: AAH09392.1.
RefSeqNP_001157711.1. NM_001164239.1.
NP_003578.2. NM_003587.4.
UniGeneHs.485060.

3D structure databases

ProteinModelPortalO60231.
SMRO60231. Positions 392-1033.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114027. 32 interactions.
IntActO60231. 10 interactions.
MINTMINT-5003862.
STRING9606.ENSP00000390938.

PTM databases

PhosphoSiteO60231.

Proteomic databases

PaxDbO60231.
PRIDEO60231.

Protocols and materials databases

DNASU8449.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000376442; ENSP00000365625; ENSG00000204560.
ENST00000383577; ENSP00000373071; ENSG00000206486.
ENST00000417308; ENSP00000390938; ENSG00000233561.
ENST00000421095; ENSP00000396193; ENSG00000226171.
ENST00000424672; ENSP00000389862; ENSG00000233418.
ENST00000451456; ENSP00000408956; ENSG00000233049.
ENST00000458094; ENSP00000393958; ENSG00000231377.
GeneID8449.
KEGGhsa:8449.
UCSCuc003nqz.3. human.

Organism-specific databases

CTD8449.
GeneCardsGC06M030620.
GC06Mj30610.
GC06Mk30611.
GC06Ml30665.
GC06Mm30699.
GC06Mn30610.
GC06Mo30612.
HGNCHGNC:2739. DHX16.
HPAHPA051455.
MIM603405. gene.
neXtProtNX_O60231.
PharmGKBPA27205.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1643.
HOGENOMHOG000175261.
HOVERGENHBG039428.
InParanoidO60231.
KOK12813.
OMAIEIESKW.
PhylomeDBO60231.
TreeFamTF313473.

Gene expression databases

ArrayExpressO60231.
BgeeO60231.
CleanExHS_DHX16.
GenevestigatorO60231.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
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]
PfamPF00270. DEAD. 1 hit.
PF04408. HA2. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07717. OB_NTP_bind. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00847. HA2. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00690. DEAH_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiDHX16.
GenomeRNAi8449.
NextBio31614.
PROO60231.
SOURCESearch...

Entry information

Entry nameDHX16_HUMAN
AccessionPrimary (citable) accession number: O60231
Secondary accession number(s): O60322 expand/collapse secondary AC list , Q5JP45, Q969X7, Q96QC1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 28, 2002
Last modified: April 16, 2014
This is version 150 of the entry and version 2 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

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM