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P23249

- MOV10_MOUSE

UniProt

P23249 - MOV10_MOUSE

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Protein

Putative helicase MOV-10

Gene
Mov10, Gb110
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 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 By similarity.

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi525 – 5328ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. helicase activity Source: UniProtKB-KW
  3. RNA binding Source: UniProtKB-KW

GO - Biological processi

  1. mRNA cleavage involved in gene silencing by miRNA Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

RNA-mediated gene silencing

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

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:Gb110
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:97054. Mov10.

Subcellular locationi

CytoplasmP-body By similarity

GO - Cellular componenti

  1. cytoplasmic mRNA processing body Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10041004Putative helicase MOV-10PRO_0000080705Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei148 – 1481N6-acetyllysine By similarity
Modified residuei254 – 2541Phosphothreonine By similarity
Modified residuei970 – 9701Phosphoserine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP23249.
PaxDbiP23249.
PRIDEiP23249.

PTM databases

PhosphoSiteiP23249.

Expressioni

Gene expression databases

ArrayExpressiP23249.
BgeeiP23249.
GenevestigatoriP23249.

Interactioni

Subunit structurei

Interacts with DICER1, AGO1, AGO2, EIF6 and TARBP2. Associates with the 60S ribosome By similarity. Interacts with APOBEC3G in an RNA-dependent manner By similarity.

Protein-protein interaction databases

BioGridi201471. 3 interactions.
DIPiDIP-48575N.
IntActiP23249. 2 interactions.
MINTiMINT-4102260.

Structurei

3D structure databases

ProteinModelPortaliP23249.
SMRiP23249. Positions 501-941.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni922 – 96645Interaction with AGO2 and APOBEC3G By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi646 – 6494DEAG box

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1112.
GeneTreeiENSGT00550000074391.
HOVERGENiHBG052500.
OrthoDBiEOG74J96Z.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR026122. MOV-10.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10887:SF326. PTHR10887:SF326. 1 hit.
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequencei

Sequence statusi: Complete.

P23249-1 [UniParc]FASTAAdd to Basket

« Hide

MPSKFSCRKL RETGQRFESF LAERGLDLET DRERLRTIYN HDFKPSYGTP     50
APGFSSMLYG MKIANLAFVT KTRVRFFKLD RWADVQLPEK RRIKPGSNIS 100
KQHRSLLARI FHDRAEYLHG KHGVDVEVQG PHEARDGQLL IHLDLNRKEV 150
LTLRLRNGGS KPVTLTHLFP LCWTPQFVFY HGEQDLPCPL GPGESYELHI 200
YCKTSIVGYF PATVLWELLG PGESGAEGAE TFYIARFLAA VAHSPLAAQL 250
KPTTPFKRPP RLTRNSVLTN RIEEGERPDR AKGYELELSL ALGTYYPPIL 300
LRQLLPTLLQ GPSIFTAPKE VAEIKAQLET TLKSRNYEVK LRLLLHLEEL 350
QMEHDIRHYD LDSVPMTWDP VDQNPRLLTL EVPGVAESRP SVLRGDHLFA 400
LLSSETQQDD PVTYKGFVHK VELDRVKLSF STSLLSRFVD GLTFKVNFTF 450
NRQPLRVQHR ALELTGRWVL WPMLFPVASR GVSLLPSDVK FKLYDRSLES 500
NPEQLQAMKH IVRGTTRPAP YIIFGPPGTG KTVTLVEAIK QVVKHLPKAH 550
ILACAPSNSG ADLLCQRLRV HLPSSIYRLL APSRDIRMVP EDIKTCCNWD 600
AKKGEYVYPA KKHLQQYRVL ITTLITASRL VSAQFPIDHF THIFIDEAGH 650
CMEPESLVAI AGLMDVKETG NPGGQLVLAG DPRQLGPVLR SPLALKHGLG 700
YSLLERLLAY NSLYKKGPNG YDPQFITKLL RNYRSHPTIL DIPNQLYYDG 750
ELQACADVVD RERFCRWEGL PQQGFPIIFH GVMGKDEREG NSPSFFNPEE 800
AATVTSYLKQ LLAPSSKKGK ARLSPRNVGV ISPYRKQVEK IRYCITKLDR 850
ELRGLDDIKD LKVGSVEEFQ GQERSVILIS TVRSSQSFVQ LDLDFNLGFL 900
KNPKRFNVAV TRAKALLIVV GNPLLLGHDP DWKTFLEFCK ENGGYTGCPF 950
PAKLDLQQGQ DLLQGLSKLS PSTSGPRRHQ NLPQEREGEG GLPLQVEPEW 1000
RNEL 1004
Length:1,004
Mass (Da):113,583
Last modified:July 19, 2004 - v2
Checksum:i8B2522AAB35B6F2B
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti142 – 1421H → R in CAA36803. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X52574 mRNA. Translation: CAA36803.1.
AK004542 mRNA. Translation: BAB23358.1.
BC053743 mRNA. Translation: AAH53743.1.
X75819 Genomic DNA. Translation: CAA53453.1.
CCDSiCCDS38579.1.
PIRiA39611.
RefSeqiNP_001156912.1. NM_001163440.1.
NP_001156913.1. NM_001163441.1.
NP_032645.2. NM_008619.2.
XP_006501163.1. XM_006501100.1.
XP_006501164.1. XM_006501101.1.
UniGeneiMm.1597.

Genome annotation databases

EnsembliENSMUST00000168015; ENSMUSP00000128246; ENSMUSG00000002227.
GeneIDi17454.
KEGGimmu:17454.
UCSCiuc008qum.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X52574 mRNA. Translation: CAA36803.1 .
AK004542 mRNA. Translation: BAB23358.1 .
BC053743 mRNA. Translation: AAH53743.1 .
X75819 Genomic DNA. Translation: CAA53453.1 .
CCDSi CCDS38579.1.
PIRi A39611.
RefSeqi NP_001156912.1. NM_001163440.1.
NP_001156913.1. NM_001163441.1.
NP_032645.2. NM_008619.2.
XP_006501163.1. XM_006501100.1.
XP_006501164.1. XM_006501101.1.
UniGenei Mm.1597.

3D structure databases

ProteinModelPortali P23249.
SMRi P23249. Positions 501-941.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201471. 3 interactions.
DIPi DIP-48575N.
IntActi P23249. 2 interactions.
MINTi MINT-4102260.

PTM databases

PhosphoSitei P23249.

Proteomic databases

MaxQBi P23249.
PaxDbi P23249.
PRIDEi P23249.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000168015 ; ENSMUSP00000128246 ; ENSMUSG00000002227 .
GeneIDi 17454.
KEGGi mmu:17454.
UCSCi uc008qum.3. mouse.

Organism-specific databases

CTDi 4343.
MGIi MGI:97054. Mov10.

Phylogenomic databases

eggNOGi COG1112.
GeneTreei ENSGT00550000074391.
HOVERGENi HBG052500.
OrthoDBi EOG74J96Z.

Miscellaneous databases

NextBioi 292100.
PROi P23249.
SOURCEi Search...

Gene expression databases

ArrayExpressi P23249.
Bgeei P23249.
Genevestigatori P23249.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR003593. AAA+_ATPase.
IPR026122. MOV-10.
IPR027417. P-loop_NTPase.
[Graphical view ]
PANTHERi PTHR10887:SF326. PTHR10887:SF326. 1 hit.
SMARTi SM00382. AAA. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and expression of a gene encoding a putative GTP-binding protein identified by provirus integration in a transgenic mouse strain."
    Mooslehner K., Mueller U., Karls U., Hamann L., Harbers K.
    Mol. Cell. Biol. 11:886-893(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Lung.
  3. "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: Limb.
  4. "Interaction of several related GC-box- and GT-box-binding proteins with the intronic enhancer is required for differential expression of the gb110 gene in embryonal carcinoma cells."
    Hamann L., Bayer K.-U., Jensen K., Harbers K.
    Mol. Cell. Biol. 14:5786-5793(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
    Strain: BALB/c.
  5. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMOV10_MOUSE
AccessioniPrimary (citable) accession number: P23249
Secondary accession number(s): Q9DC64
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: July 19, 2004
Last modified: July 9, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi