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Q9HCE1

- MOV10_HUMAN

UniProt

Q9HCE1 - MOV10_HUMAN

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Protein

Putative helicase MOV-10

Gene

MOV10

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

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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ9HCE1.
CleanExiHS_MOV10.
ExpressionAtlasiQ9HCE1. baseline and differential.
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. 60 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.
GeneTreeiENSGT00550000074391.
HOGENOMiHOG000239755.
HOVERGENiHBG052500.
InParanoidiQ9HCE1.
KOiK18422.
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

        10         20         30         40         50
MPSKFSCRQL REAGQCFESF LVVRGLDMET DRERLRTIYN RDFKISFGTP
60 70 80 90 100
APGFSSMLYG MKIANLAYVT KTRVRFFRLD RWADVRFPEK RRMKLGSDIS
110 120 130 140 150
KHHKSLLAKI FYDRAEYLHG KHGVDVEVQG PHEARDGQLL IRLDLNRKEV
160 170 180 190 200
LTLRLRNGGT QSVTLTHLFP LCRTPQFAFY NEDQELPCPL GPGECYELHV
210 220 230 240 250
HCKTSFVGYF PATVLWELLG PGESGSEGAG TFYIARFLAA VAHSPLAAQL
260 270 280 290 300
KPMTPFKRTR ITGNPVVTNR IEEGERPDRA KGYDLELSMA LGTYYPPPRL
310 320 330 340 350
RQLLPMLLQG TSIFTAPKEI AEIKAQLETA LKWRNYEVKL RLLLHLEELQ
360 370 380 390 400
MEHDIRHYDL ESVPMTWDPV DQNPRLLTLE VPGVTESRPS VLRGDHLFAL
410 420 430 440 450
LSSETHQEDP ITYKGFVHKV ELDRVKLSFS MSLLSRFVDG LTFKVNFTFN
460 470 480 490 500
RQPLRVQHRA LELTGRWLLW PMLFPVAPRD VPLLPSDVKL KLYDRSLESN
510 520 530 540 550
PEQLQAMRHI VTGTTRPAPY IIFGPPGTGK TVTLVEAIKQ VVKHLPKAHI
560 570 580 590 600
LACAPSNSGA DLLCQRLRVH LPSSIYRLLA PSRDIRMVPE DIKPCCNWDA
610 620 630 640 650
KKGEYVFPAK KKLQEYRVLI TTLITAGRLV SAQFPIDHFT HIFIDEAGHC
660 670 680 690 700
MEPESLVAIA GLMEVKETGD PGGQLVLAGD PRQLGPVLRS PLTQKHGLGY
710 720 730 740 750
SLLERLLTYN SLYKKGPDGY DPQFITKLLR NYRSHPTILD IPNQLYYEGE
760 770 780 790 800
LQACADVVDR ERFCRWAGLP RQGFPIIFHG VMGKDEREGN SPSFFNPEEA
810 820 830 840 850
ATVTSYLKLL LAPSSKKGKA RLSPRSVGVI SPYRKQVEKI RYCITKLDRE
860 870 880 890 900
LRGLDDIKDL KVGSVEEFQG QERSVILIST VRSSQSFVQL DLDFNLGFLK
910 920 930 940 950
NPKRFNVAVT RAKALLIIVG NPLLLGHDPD WKVFLEFCKE NGGYTGCPFP
960 970 980 990 1000
AKLDLQQGQN LLQGLSKLSP STSGPHSHDY LPQEREGEGG LSLQVEPEWR

NEL
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.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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. 60 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.
GeneTreei ENSGT00550000074391.
HOGENOMi HOG000239755.
HOVERGENi HBG052500.
InParanoidi Q9HCE1.
KOi K18422.
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

Bgeei Q9HCE1.
CleanExi HS_MOV10.
ExpressionAtlasi Q9HCE1. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 119 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