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Q9HCE1 (MOV10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative helicase MOV-10

EC=3.6.4.13
Alternative name(s):
Moloney leukemia virus 10 protein
Gene names
Name:MOV10
Synonyms:KIAA1631
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1003 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable RNA helicase. Required for RNA-mediated gene silencing by the RNA-induced silencing complex (RISC). Required for both miRNA-mediated translational repression and miRNA-mediated cleavage of complementary mRNAs by RISC. Also required for RNA-directed transcription and replication of the human hepatitis delta virus (HDV). Interacts with small capped HDV RNAs derived from genomic hairpin structures that mark the initiation sites of RNA-dependent HDV RNA transcription. Ref.7 Ref.8 Ref.10 Ref.15

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

Interacts with DICER1, AGO1, AGO2, EIF6 and TARBP2. Associates with the 60S ribosome. Interacts with the human hepatitis delta virus (HDV) antigen HDAg. Interacts with APOBEC3G in an RNA-dependent manner. Ref.7 Ref.8 Ref.15

Subcellular location

CytoplasmP-body Ref.7.

Sequence similarities

Belongs to the DNA2/NAM7 helicase family. SDE3 subfamily.

Sequence caution

The sequence BAB13457.1 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.

The sequence BAB85000.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processRNA-mediated gene silencing
Transcription
Transcription regulation
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
RNA-binding
   Molecular functionHelicase
Hydrolase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

Notch signaling pathway

Traceable author statement. Source: Reactome

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

mRNA cleavage involved in gene silencing by miRNA

Inferred from direct assay Ref.7. Source: UniProtKB

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

phosphatidylinositol-mediated signaling

Traceable author statement. Source: Reactome

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasmic mRNA processing body

Inferred from direct assay Ref.7. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 22664934. Source: UniProt

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

helicase activity

Inferred from electronic annotation. Source: UniProtKB-KW

poly(A) RNA binding

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

protein binding

Inferred from physical interaction Ref.7. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

EIF2AK2P195252EBI-1055820,EBI-640775

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9HCE1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9HCE1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     838-900: EKIRYCITKL...DLDFNLGFLK → RSSVTSKGGA...PGLLPGSLLH
     901-1003: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9HCE1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     47-56: FGTPAPGFSS → LASSKSILQS
     57-1003: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10031003Putative helicase MOV-10
PRO_0000080704

Regions

Nucleotide binding524 – 5318ATP By similarity
Region921 – 96545Interaction with AGO2 and APOBEC3G
Motif645 – 6484DEAG box

Amino acid modifications

Modified residue1481N6-acetyllysine Ref.12
Modified residue1601Phosphothreonine Ref.9
Modified residue2541Phosphothreonine Ref.11 Ref.13
Modified residue9691Phosphoserine Ref.13

Natural variations

Alternative sequence47 – 5610FGTPAPGFSS → LASSKSILQS in isoform 3.
VSP_037305
Alternative sequence57 – 1003947Missing in isoform 3.
VSP_037306
Alternative sequence838 – 90063EKIRY…LGFLK → RSSVTSKGGAPPPDGTSLIS RPLGRGSRSLGLCWLRISEE HQGQLPPPFVPQLPGLLPGS LLH in isoform 2.
VSP_010943
Alternative sequence901 – 1003103Missing in isoform 2.
VSP_010944

Experimental info

Sequence conflict981D → N in AL833353. Ref.4
Sequence conflict2481A → T in AL833353. Ref.4
Sequence conflict8141S → T in AL833353. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 2002. Version 2.
Checksum: 28A8B3BF9B5B54FC

FASTA1,003113,671
        10         20         30         40         50         60 
MPSKFSCRQL REAGQCFESF LVVRGLDMET DRERLRTIYN RDFKISFGTP APGFSSMLYG 

        70         80         90        100        110        120 
MKIANLAYVT KTRVRFFRLD RWADVRFPEK RRMKLGSDIS KHHKSLLAKI FYDRAEYLHG 

       130        140        150        160        170        180 
KHGVDVEVQG PHEARDGQLL IRLDLNRKEV LTLRLRNGGT QSVTLTHLFP LCRTPQFAFY 

       190        200        210        220        230        240 
NEDQELPCPL GPGECYELHV HCKTSFVGYF PATVLWELLG PGESGSEGAG TFYIARFLAA 

       250        260        270        280        290        300 
VAHSPLAAQL KPMTPFKRTR ITGNPVVTNR IEEGERPDRA KGYDLELSMA LGTYYPPPRL 

       310        320        330        340        350        360 
RQLLPMLLQG TSIFTAPKEI AEIKAQLETA LKWRNYEVKL RLLLHLEELQ MEHDIRHYDL 

       370        380        390        400        410        420 
ESVPMTWDPV DQNPRLLTLE VPGVTESRPS VLRGDHLFAL LSSETHQEDP ITYKGFVHKV 

       430        440        450        460        470        480 
ELDRVKLSFS MSLLSRFVDG LTFKVNFTFN RQPLRVQHRA LELTGRWLLW PMLFPVAPRD 

       490        500        510        520        530        540 
VPLLPSDVKL KLYDRSLESN PEQLQAMRHI VTGTTRPAPY IIFGPPGTGK TVTLVEAIKQ 

       550        560        570        580        590        600 
VVKHLPKAHI LACAPSNSGA DLLCQRLRVH LPSSIYRLLA PSRDIRMVPE DIKPCCNWDA 

       610        620        630        640        650        660 
KKGEYVFPAK KKLQEYRVLI TTLITAGRLV SAQFPIDHFT HIFIDEAGHC MEPESLVAIA 

       670        680        690        700        710        720 
GLMEVKETGD PGGQLVLAGD PRQLGPVLRS PLTQKHGLGY SLLERLLTYN SLYKKGPDGY 

       730        740        750        760        770        780 
DPQFITKLLR NYRSHPTILD IPNQLYYEGE LQACADVVDR ERFCRWAGLP RQGFPIIFHG 

       790        800        810        820        830        840 
VMGKDEREGN SPSFFNPEEA ATVTSYLKLL LAPSSKKGKA RLSPRSVGVI SPYRKQVEKI 

       850        860        870        880        890        900 
RYCITKLDRE LRGLDDIKDL KVGSVEEFQG QERSVILIST VRSSQSFVQL DLDFNLGFLK 

       910        920        930        940        950        960 
NPKRFNVAVT RAKALLIIVG NPLLLGHDPD WKVFLEFCKE NGGYTGCPFP AKLDLQQGQN 

       970        980        990       1000 
LLQGLSKLSP STSGPHSHDY LPQEREGEGG LSLQVEPEWR NEL 

« Hide

Isoform 2 [UniParc].

Checksum: 0CF3733285C48342
Show »

FASTA900101,598
Isoform 3 [UniParc].

Checksum: 5FAEB3C0DC2A00F6
Show »

FASTA566,546

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.
DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Brain.
[2]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[3]"The nucleotide sequence of a long cDNA clone isolated from human spleen."
Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Spleen.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Testis.
[5]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORM 1).
Tissue: Muscle, Placenta and Skin.
[7]"Identification of novel argonaute-associated proteins."
Meister G., Landthaler M., Peters L., Chen P.Y., Urlaub H., Luehrmann R., Tuschl T.
Curr. Biol. 15:2149-2155(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH AGO1 AND AGO2, SUBCELLULAR LOCATION.
[8]"MicroRNA silencing through RISC recruitment of eIF6."
Chendrimada T.P., Finn K.J., Ji X., Baillat D., Gregory R.I., Liebhaber S.A., Pasquinelli A.E., Shiekhattar R.
Nature 447:823-828(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH DICER1; AGO2; EIF6 AND TARBP2, ASSOCIATION WITH THE 60S RIBOSOME.
[9]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[10]"Capped small RNAs and MOV10 in human hepatitis delta virus replication."
Haussecker D., Cao D., Huang Y., Parameswaran P., Fire A.Z., Kay M.A.
Nat. Struct. Mol. Biol. 15:714-721(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, RNA-BINDING.
[11]"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 THR-254, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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-148, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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 THR-254 AND SER-969, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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].
[15]"APOBEC3G inhibits microRNA-mediated repression of translation by interfering with the interaction between Argonaute-2 and MOV10."
Liu C., Zhang X., Huang F., Yang B., Li J., Liu B., Luo H., Zhang P., Zhang H.
J. Biol. Chem. 287:29373-29383(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH APOBEC3G AND AGO2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB046851 mRNA. Translation: BAB13457.1. Sequence problems.
AK074174 mRNA. Translation: BAB85000.1. Different initiation.
AL833353 mRNA. No translation available.
AL603832 Genomic DNA. Translation: CAI14055.1.
BC002548 mRNA. Translation: AAH02548.1.
BC004499 mRNA. Translation: AAH04499.2.
BC009312 mRNA. Translation: AAH09312.1.
CCDSCCDS853.1. [Q9HCE1-1]
RefSeqNP_001123551.1. NM_001130079.2. [Q9HCE1-1]
NP_001273001.1. NM_001286072.1.
NP_066014.1. NM_020963.4. [Q9HCE1-1]
XP_005270925.1. XM_005270868.2. [Q9HCE1-1]
UniGeneHs.514941.

3D structure databases

ProteinModelPortalQ9HCE1.
SMRQ9HCE1. Positions 500-940.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110484. 48 interactions.
DIPDIP-44158N.
IntActQ9HCE1. 23 interactions.
MINTMINT-4539786.
STRING9606.ENSP00000350028.

PTM databases

PhosphoSiteQ9HCE1.

Polymorphism databases

DMDM24638063.

Proteomic databases

MaxQBQ9HCE1.
PaxDbQ9HCE1.
PRIDEQ9HCE1.

Protocols and materials databases

DNASU4343.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000357443; ENSP00000350028; ENSG00000155363. [Q9HCE1-1]
ENST00000369645; ENSP00000358659; ENSG00000155363. [Q9HCE1-1]
ENST00000413052; ENSP00000399797; ENSG00000155363. [Q9HCE1-1]
ENST00000544796; ENSP00000439533; ENSG00000155363. [Q9HCE1-3]
GeneID4343.
KEGGhsa:4343.
UCSCuc001eck.3. human. [Q9HCE1-1]

Organism-specific databases

CTD4343.
GeneCardsGC01P113215.
HGNCHGNC:7200. MOV10.
MIM610742. gene.
neXtProtNX_Q9HCE1.
PharmGKBPA30908.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1112.
HOGENOMHOG000239755.
HOVERGENHBG052500.
InParanoidQ9HCE1.
OMAWFPEKRR.
OrthoDBEOG74J96Z.
PhylomeDBQ9HCE1.
TreeFamTF323999.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_120956. Cellular responses to stress.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressQ9HCE1.
BgeeQ9HCE1.
CleanExHS_MOV10.
GenevestigatorQ9HCE1.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR026122. MOV-10.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR10887:SF326. PTHR10887:SF326. 1 hit.
SUPFAMSSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

ChiTaRSMOV10. human.
GeneWikiMOV10.
GenomeRNAi4343.
NextBio17098.
PROQ9HCE1.
SOURCESearch...

Entry information

Entry nameMOV10_HUMAN
AccessionPrimary (citable) accession number: Q9HCE1
Secondary accession number(s): Q5JR03 expand/collapse secondary AC list , Q8TEF0, Q9BSY3, Q9BUJ9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: November 1, 2002
Last modified: July 9, 2014
This is version 116 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 chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM