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Q9HCE1

- MOV10_HUMAN

UniProt

Q9HCE1 - MOV10_HUMAN

Protein

Putative helicase MOV-10

Gene

MOV10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (01 Nov 2002)
      Previous versions | rss
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    Functioni

    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.4 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi524 – 5318ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. helicase activity Source: UniProtKB-KW
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. epidermal growth factor receptor signaling pathway Source: Reactome
    2. Fc-epsilon receptor signaling pathway Source: Reactome
    3. fibroblast growth factor receptor signaling pathway Source: Reactome
    4. innate immune response Source: Reactome
    5. mRNA cleavage involved in gene silencing by miRNA Source: UniProtKB
    6. neurotrophin TRK receptor signaling pathway Source: Reactome
    7. Notch signaling pathway Source: Reactome
    8. phosphatidylinositol-mediated signaling Source: Reactome
    9. regulation of transcription, DNA-templated Source: UniProtKB-KW
    10. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    RNA-mediated gene silencing, Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding, RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_118568. Pre-NOTCH Transcription and Translation.
    REACT_169325. Oncogene Induced Senescence.
    REACT_169436. Oxidative Stress Induced Senescence.
    REACT_172761. Ca2+ pathway.
    REACT_75829. PIP3 activates AKT signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Putative helicase MOV-10 (EC:3.6.4.13)
    Alternative name(s):
    Moloney leukemia virus 10 protein
    Gene namesi
    Name:MOV10
    Synonyms:KIAA1631
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:7200. MOV10.

    Subcellular locationi

    CytoplasmP-body 1 Publication

    GO - Cellular componenti

    1. cytoplasmic mRNA processing body Source: UniProtKB
    2. cytosol Source: Reactome
    3. extracellular space Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30908.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10031003Putative helicase MOV-10PRO_0000080704Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei148 – 1481N6-acetyllysine1 Publication
    Modified residuei160 – 1601Phosphothreonine1 Publication
    Modified residuei254 – 2541Phosphothreonine2 Publications
    Modified residuei969 – 9691Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9HCE1.
    PaxDbiQ9HCE1.
    PRIDEiQ9HCE1.

    PTM databases

    PhosphoSiteiQ9HCE1.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9HCE1.
    BgeeiQ9HCE1.
    CleanExiHS_MOV10.
    GenevestigatoriQ9HCE1.

    Interactioni

    Subunit structurei

    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.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EIF2AK2P195252EBI-1055820,EBI-640775

    Protein-protein interaction databases

    BioGridi110484. 51 interactions.
    DIPiDIP-44158N.
    IntActiQ9HCE1. 23 interactions.
    MINTiMINT-4539786.
    STRINGi9606.ENSP00000350028.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9HCE1.
    SMRiQ9HCE1. Positions 500-940.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni921 – 96545Interaction with AGO2 and APOBEC3GAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi645 – 6484DEAG box

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1112.
    HOGENOMiHOG000239755.
    HOVERGENiHBG052500.
    InParanoidiQ9HCE1.
    OMAiWFPEKRR.
    OrthoDBiEOG74J96Z.
    PhylomeDBiQ9HCE1.
    TreeFamiTF323999.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR026122. MOV-10.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR10887:SF326. PTHR10887:SF326. 1 hit.
    SUPFAMiSSF52540. SSF52540. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9HCE1-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MPSKFSCRQL REAGQCFESF LVVRGLDMET DRERLRTIYN RDFKISFGTP     50
    APGFSSMLYG MKIANLAYVT KTRVRFFRLD RWADVRFPEK RRMKLGSDIS 100
    KHHKSLLAKI FYDRAEYLHG KHGVDVEVQG PHEARDGQLL IRLDLNRKEV 150
    LTLRLRNGGT QSVTLTHLFP LCRTPQFAFY NEDQELPCPL GPGECYELHV 200
    HCKTSFVGYF PATVLWELLG PGESGSEGAG TFYIARFLAA VAHSPLAAQL 250
    KPMTPFKRTR ITGNPVVTNR IEEGERPDRA KGYDLELSMA LGTYYPPPRL 300
    RQLLPMLLQG TSIFTAPKEI AEIKAQLETA LKWRNYEVKL RLLLHLEELQ 350
    MEHDIRHYDL ESVPMTWDPV DQNPRLLTLE VPGVTESRPS VLRGDHLFAL 400
    LSSETHQEDP ITYKGFVHKV ELDRVKLSFS MSLLSRFVDG LTFKVNFTFN 450
    RQPLRVQHRA LELTGRWLLW PMLFPVAPRD VPLLPSDVKL KLYDRSLESN 500
    PEQLQAMRHI VTGTTRPAPY IIFGPPGTGK TVTLVEAIKQ VVKHLPKAHI 550
    LACAPSNSGA DLLCQRLRVH LPSSIYRLLA PSRDIRMVPE DIKPCCNWDA 600
    KKGEYVFPAK KKLQEYRVLI TTLITAGRLV SAQFPIDHFT HIFIDEAGHC 650
    MEPESLVAIA GLMEVKETGD PGGQLVLAGD PRQLGPVLRS PLTQKHGLGY 700
    SLLERLLTYN SLYKKGPDGY DPQFITKLLR NYRSHPTILD IPNQLYYEGE 750
    LQACADVVDR ERFCRWAGLP RQGFPIIFHG VMGKDEREGN SPSFFNPEEA 800
    ATVTSYLKLL LAPSSKKGKA RLSPRSVGVI SPYRKQVEKI RYCITKLDRE 850
    LRGLDDIKDL KVGSVEEFQG QERSVILIST VRSSQSFVQL DLDFNLGFLK 900
    NPKRFNVAVT RAKALLIIVG NPLLLGHDPD WKVFLEFCKE NGGYTGCPFP 950
    AKLDLQQGQN LLQGLSKLSP STSGPHSHDY LPQEREGEGG LSLQVEPEWR 1000
    NEL 1003
    Length:1,003
    Mass (Da):113,671
    Last modified:November 1, 2002 - v2
    Checksum:i28A8B3BF9B5B54FC
    GO
    Isoform 2 (identifier: Q9HCE1-2) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:900
    Mass (Da):101,598
    Checksum:i0CF3733285C48342
    GO
    Isoform 3 (identifier: Q9HCE1-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:56
    Mass (Da):6,546
    Checksum:i5FAEB3C0DC2A00F6
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti98 – 981D → N in AL833353. (PubMed:17974005)Curated
    Sequence conflicti248 – 2481A → T in AL833353. (PubMed:17974005)Curated
    Sequence conflicti814 – 8141S → T in AL833353. (PubMed:17974005)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei47 – 5610FGTPAPGFSS → LASSKSILQS in isoform 3. 1 PublicationVSP_037305
    Alternative sequencei57 – 1003947Missing in isoform 3. 1 PublicationVSP_037306Add
    BLAST
    Alternative sequencei838 – 90063EKIRY…LGFLK → RSSVTSKGGAPPPDGTSLIS RPLGRGSRSLGLCWLRISEE HQGQLPPPFVPQLPGLLPGS LLH in isoform 2. 1 PublicationVSP_010943Add
    BLAST
    Alternative sequencei901 – 1003103Missing in isoform 2. 1 PublicationVSP_010944Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS853.1. [Q9HCE1-1]
    RefSeqiNP_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]
    UniGeneiHs.514941.

    Genome annotation databases

    EnsembliENST00000357443; ENSP00000350028; ENSG00000155363. [Q9HCE1-1]
    ENST00000369645; ENSP00000358659; ENSG00000155363. [Q9HCE1-1]
    ENST00000413052; ENSP00000399797; ENSG00000155363. [Q9HCE1-1]
    GeneIDi4343.
    KEGGihsa:4343.
    UCSCiuc001eck.3. human. [Q9HCE1-1]

    Polymorphism databases

    DMDMi24638063.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS853.1. [Q9HCE1-1 ]
    RefSeqi NP_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 ]
    UniGenei Hs.514941.

    3D structure databases

    ProteinModelPortali Q9HCE1.
    SMRi Q9HCE1. Positions 500-940.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110484. 51 interactions.
    DIPi DIP-44158N.
    IntActi Q9HCE1. 23 interactions.
    MINTi MINT-4539786.
    STRINGi 9606.ENSP00000350028.

    PTM databases

    PhosphoSitei Q9HCE1.

    Polymorphism databases

    DMDMi 24638063.

    Proteomic databases

    MaxQBi Q9HCE1.
    PaxDbi Q9HCE1.
    PRIDEi Q9HCE1.

    Protocols and materials databases

    DNASUi 4343.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000357443 ; ENSP00000350028 ; ENSG00000155363 . [Q9HCE1-1 ]
    ENST00000369645 ; ENSP00000358659 ; ENSG00000155363 . [Q9HCE1-1 ]
    ENST00000413052 ; ENSP00000399797 ; ENSG00000155363 . [Q9HCE1-1 ]
    GeneIDi 4343.
    KEGGi hsa:4343.
    UCSCi uc001eck.3. human. [Q9HCE1-1 ]

    Organism-specific databases

    CTDi 4343.
    GeneCardsi GC01P113215.
    HGNCi HGNC:7200. MOV10.
    MIMi 610742. gene.
    neXtProti NX_Q9HCE1.
    PharmGKBi PA30908.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1112.
    HOGENOMi HOG000239755.
    HOVERGENi HBG052500.
    InParanoidi Q9HCE1.
    OMAi WFPEKRR.
    OrthoDBi EOG74J96Z.
    PhylomeDBi Q9HCE1.
    TreeFami TF323999.

    Enzyme and pathway databases

    Reactomei REACT_118568. Pre-NOTCH Transcription and Translation.
    REACT_169325. Oncogene Induced Senescence.
    REACT_169436. Oxidative Stress Induced Senescence.
    REACT_172761. Ca2+ pathway.
    REACT_75829. PIP3 activates AKT signaling.

    Miscellaneous databases

    ChiTaRSi MOV10. human.
    GeneWikii MOV10.
    GenomeRNAii 4343.
    NextBioi 17098.
    PROi Q9HCE1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9HCE1.
    Bgeei Q9HCE1.
    CleanExi HS_MOV10.
    Genevestigatori Q9HCE1.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR026122. MOV-10.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    PANTHERi PTHR10887:SF326. PTHR10887:SF326. 1 hit.
    SUPFAMi SSF52540. SSF52540. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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. 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.
      , 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH AGO1 AND AGO2, SUBCELLULAR LOCATION.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH DICER1; AGO2; EIF6 AND TARBP2, ASSOCIATION WITH THE 60S RIBOSOME.
    9. 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. 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. 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.

    Entry informationi

    Entry nameiMOV10_HUMAN
    AccessioniPrimary (citable) accession number: Q9HCE1
    Secondary accession number(s): Q5JR03
    , Q8TEF0, Q9BSY3, Q9BUJ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 2002
    Last sequence update: November 1, 2002
    Last modified: October 1, 2014
    This is version 118 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 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3