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Protein

Tudor domain-containing protein 1

Gene

Tdrd1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Required for the localization of Piwi proteins to the meiotic nuage. Involved in the piRNA metabolic process by ensuring the entry of correct transcripts into the normal piRNA pool and limiting the entry of cellular transcripts into the piRNA pathway. May act by allowing the recruitment of piRNA biogenesis or loading factors that ensure the correct entry of transcripts and piRNAs into Piwi proteins.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri163 – 19937MYND-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • DNA methylation involved in gamete generation Source: UniProtKB
  • gene silencing by RNA Source: UniProtKB
  • germ cell development Source: UniProtKB
  • meiotic cell cycle Source: UniProtKB-KW
  • multicellular organism development Source: UniProtKB-KW
  • piRNA metabolic process Source: UniProtKB
  • spermatogenesis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Meiosis, RNA-mediated gene silencing, Spermatogenesis

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Tudor domain-containing protein 1
Gene namesi
Name:Tdrd1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1933218. Tdrd1.

Subcellular locationi

GO - Cellular componenti

  • chromatoid body Source: MGI
  • cytoplasm Source: MGI
  • cytosol Source: Reactome
  • intracellular ribonucleoprotein complex Source: MGI
  • P granule Source: UniProtKB
  • pi-body Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Male sterility because of postnatal spermatogenic defects due to demethylation and subsequent derepression of transposable elements. Piwi-associated small RNA profiles are altered, piRNPs accepting the entry of abundant cellular transcripts into the piRNA pathway and accumulating piRNAs with a profile that is drastically different from wild-type. Piwi proteins are delocalized from the nucleus to the cytoplasm.3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi325 – 3251N → Y: Strongly enhanced binding to symmetric dimethylarginines. 1 Publication
Mutagenesisi774 – 7741Y → N: Strongly reduced binding to symmetric dimethylarginines. 1 Publication
Mutagenesisi796 – 7961N → A: Significantly reduced binding to symmetric dimethylarginines. 1 Publication
Mutagenesisi1019 – 10191Y → N: Abolishes localization to meiotic nuage; when associated with K-1023. 1 Publication
Mutagenesisi1023 – 10231E → K: Abolishes localization to meiotic nuage; when associated with N-1019. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11721172Tudor domain-containing protein 1PRO_0000183162Add
BLAST

Proteomic databases

PaxDbiQ99MV1.
PRIDEiQ99MV1.

PTM databases

PhosphoSiteiQ99MV1.

Expressioni

Tissue specificityi

Testis and ovary specific. Present in germ-line cells and is most abundant in fetal prospermatogonia and postnatal primary spermatocytes (at protein level).1 Publication

Gene expression databases

BgeeiQ99MV1.
CleanExiMM_TDRD1.
GenevisibleiQ99MV1. MM.

Interactioni

Subunit structurei

Found in a mRNP complex, at least composed of TDRD1, TDRD6, TDRD7 and DDX4. Interacts with MAEL. Interacts with PIWIL1, PIWIL2 and PIWIL4 (when methylated on arginine residues). Interacts with TDRD12.7 Publications

Protein-protein interaction databases

BioGridi219947. 1 interaction.
DIPiDIP-48523N.
IntActiQ99MV1. 1 interaction.
STRINGi10090.ENSMUSP00000077785.

Structurei

Secondary structure

1
1172
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi709 – 71911Combined sources
Beta strandi722 – 7276Combined sources
Helixi732 – 74817Combined sources
Beta strandi749 – 7513Combined sources
Beta strandi762 – 7665Combined sources
Turni768 – 7703Combined sources
Beta strandi773 – 7819Combined sources
Beta strandi787 – 7915Combined sources
Turni792 – 7943Combined sources
Beta strandi797 – 8004Combined sources
Helixi802 – 8043Combined sources
Beta strandi805 – 8073Combined sources
Helixi810 – 8134Combined sources
Beta strandi820 – 8289Combined sources
Beta strandi830 – 8334Combined sources
Helixi836 – 84611Combined sources
Beta strandi851 – 8599Combined sources
Beta strandi862 – 8698Combined sources
Beta strandi871 – 8744Combined sources
Helixi878 – 8847Combined sources
Beta strandi887 – 8904Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4B9WX-ray2.10A/B692-892[»]
4B9XX-ray2.80A692-917[»]
ProteinModelPortaliQ99MV1.
SMRiQ99MV1. Positions 697-892.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini307 – 36761Tudor 1PROSITE-ProRule annotationAdd
BLAST
Domaini536 – 59560Tudor 2PROSITE-ProRule annotationAdd
BLAST
Domaini756 – 81560Tudor 3PROSITE-ProRule annotationAdd
BLAST
Domaini982 – 104059Tudor 4PROSITE-ProRule annotationAdd
BLAST

Domaini

Tudor domains 2 and 3 have higher affinity for arginine-methylated peptides, tudor domain 1 is a poor binder due to an impaired aromatic cage.

Sequence similaritiesi

Belongs to the TDRD1 family.Curated
Contains 1 MYND-type zinc finger.PROSITE-ProRule annotation
Contains 4 Tudor domains.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri163 – 19937MYND-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IPR3. Eukaryota.
ENOG410ZWZX. LUCA.
GeneTreeiENSGT00730000110295.
HOGENOMiHOG000081819.
HOVERGENiHBG108555.
InParanoidiQ99MV1.
KOiK18405.
OMAiCVAKYTV.
OrthoDBiEOG7VX8VC.
PhylomeDBiQ99MV1.

Family and domain databases

InterProiIPR002999. Tudor.
IPR002893. Znf_MYND.
[Graphical view]
PfamiPF00567. TUDOR. 4 hits.
PF01753. zf-MYND. 1 hit.
[Graphical view]
SMARTiSM00333. TUDOR. 4 hits.
[Graphical view]
PROSITEiPS50304. TUDOR. 4 hits.
PS01360. ZF_MYND_1. 1 hit.
PS50865. ZF_MYND_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99MV1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMPRNNLEAS TCKMAEPFNF EKKESKPPPQ DPLRSPVAQH NHPTFRLKSP
60 70 80 90 100
ENGNTKNNFL LCEQNKQYLA SQEDSSVVSS NPAVVNGEVG GSKGDRKPPP
110 120 130 140 150
TGNPVSPLSL GNSSPPNQVK TKPSSNVTPE KSKKSHKLFE NALSVNNPAL
160 170 180 190 200
FNSLGPPLRS TTCHRCGLFG SLRCSQCKQT YYCSTACQRR DWSSHSTICR
210 220 230 240 250
PVQQSLNKLE DNKSPFETKA IEVKSEVDCP PGVTKEITAG AERVMFSDLR
260 270 280 290 300
SLQLKKTMEI KGTVTEFKHP SNFYIQLYSS EVLENMNQLS TSLKETYANV
310 320 330 340 350
VPEDGYLPVK GEVCVAKYTV DQTWNRAIVQ AVDVLQRKAH VLYIDYGNEE
360 370 380 390 400
MIPIDSVHPL SRGLDLFPPS AIKCCVSGVI PTAGEWSEGC VAAVKALLFE
410 420 430 440 450
QFCSVKVMDI LEEEVLTCAV DLVLQSSGKQ LDHVLVEMGY GVKPGEQSST
460 470 480 490 500
EQSVDHSALE DVGRVTVESK IVTDRNALIP KVLTLNVGDE FCGVVAHIQT
510 520 530 540 550
PEDFFCQQLQ SGHKLAELQE SLSEYCGHVI PRSDFYPTIG DVCCAQFSED
560 570 580 590 600
DQWYRASVLA YASEESVLVG YVDYGNFEIL SLKRLCPIIP KLLDLPMQAL
610 620 630 640 650
NCVLAGVKPS LGIWTPEAVC VMKEMVQNRM VTVRVVGMLG TRALVELIDK
660 670 680 690 700
SVAPHVSASK ALIDSGFAIK EKDVADKGSS MHTASVPLAI EGPAEALEWT
710 720 730 740 750
WVEFTVDETV DVVVCMMYSP GEFYCHFLKD DALEKLDDLN QSLADYCAQK
760 770 780 790 800
PPNGFKAEIG RPCCAFFSGD GNWYRALVKE ILPSGNVKVH FVDYGNVEEV
810 820 830 840 850
TTDQLQAILP QFLLLPFQGM QCWLVDIQPP NKHWTKEATA RFQACVVGLK
860 870 880 890 900
LQARVVEITA NGVGVELTDL STPYPKIISD VLIREQLVLR CGSPQDSLMS
910 920 930 940 950
RPANQHKQID SHRVQASPSA EQWKTMELPV NKTIAANVLE IISPALFYAI
960 970 980 990 1000
PSEMSENQEK LCVLAAELLE HCNAQKGQPA YRPRTGDACC AKYTNDDFWY
1010 1020 1030 1040 1050
RAIVLETSES DVKVLYADYG NIETLPLSRV QPIPASHLEL PFQIIRCSLE
1060 1070 1080 1090 1100
GPMELNGSCS QLVMELLRNA MLNQSVVLSV KAISKNVHAV SVEKCSENGM
1110 1120 1130 1140 1150
INIAENLVMC GLAENLTSKR KSASTKEIPH SRDCCCTELQ KQIEKHEQIL
1160 1170
LFLLNNPTNQ SKFTEMKKLL RS
Length:1,172
Mass (Da):129,696
Last modified:March 24, 2009 - v2
Checksum:iEF42786CAD71933D
GO

Sequence cautioni

The sequence AAI29955.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAI29956.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAK31970.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAD27578.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti903 – 9031A → G in BAC26625 (PubMed:16141072).Curated
Sequence conflicti1128 – 11281I → T in AAI29956 (PubMed:15489334).Curated
Sequence conflicti1128 – 11281I → T in AAI29955 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB067571 mRNA. Translation: BAC02433.1.
AB183526 mRNA. Translation: BAD27575.1.
AB183527 mRNA. Translation: BAD27576.1.
AB183528 mRNA. Translation: BAD27577.1.
AB183529 mRNA. Translation: BAD27578.1. Different initiation.
AK029806 mRNA. Translation: BAC26625.1.
AF285591 mRNA. Translation: AAK31970.1. Different initiation.
BC129954 mRNA. Translation: AAI29955.1. Different initiation.
BC129955 mRNA. Translation: AAI29956.1. Different initiation.
CCDSiCCDS29922.1.
RefSeqiNP_001002238.1. NM_001002238.2.
NP_001002240.1. NM_001002240.2.
NP_001002241.1. NM_001002241.2.
NP_113564.2. NM_031387.3.
UniGeneiMm.247541.

Genome annotation databases

EnsembliENSMUST00000078723; ENSMUSP00000077785; ENSMUSG00000025081.
ENSMUST00000111604; ENSMUSP00000107231; ENSMUSG00000025081.
ENSMUST00000111606; ENSMUSP00000107233; ENSMUSG00000025081.
ENSMUST00000121249; ENSMUSP00000112786; ENSMUSG00000025081.
GeneIDi83561.
KEGGimmu:83561.
UCSCiuc008hzi.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB067571 mRNA. Translation: BAC02433.1.
AB183526 mRNA. Translation: BAD27575.1.
AB183527 mRNA. Translation: BAD27576.1.
AB183528 mRNA. Translation: BAD27577.1.
AB183529 mRNA. Translation: BAD27578.1. Different initiation.
AK029806 mRNA. Translation: BAC26625.1.
AF285591 mRNA. Translation: AAK31970.1. Different initiation.
BC129954 mRNA. Translation: AAI29955.1. Different initiation.
BC129955 mRNA. Translation: AAI29956.1. Different initiation.
CCDSiCCDS29922.1.
RefSeqiNP_001002238.1. NM_001002238.2.
NP_001002240.1. NM_001002240.2.
NP_001002241.1. NM_001002241.2.
NP_113564.2. NM_031387.3.
UniGeneiMm.247541.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4B9WX-ray2.10A/B692-892[»]
4B9XX-ray2.80A692-917[»]
ProteinModelPortaliQ99MV1.
SMRiQ99MV1. Positions 697-892.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi219947. 1 interaction.
DIPiDIP-48523N.
IntActiQ99MV1. 1 interaction.
STRINGi10090.ENSMUSP00000077785.

PTM databases

PhosphoSiteiQ99MV1.

Proteomic databases

PaxDbiQ99MV1.
PRIDEiQ99MV1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000078723; ENSMUSP00000077785; ENSMUSG00000025081.
ENSMUST00000111604; ENSMUSP00000107231; ENSMUSG00000025081.
ENSMUST00000111606; ENSMUSP00000107233; ENSMUSG00000025081.
ENSMUST00000121249; ENSMUSP00000112786; ENSMUSG00000025081.
GeneIDi83561.
KEGGimmu:83561.
UCSCiuc008hzi.1. mouse.

Organism-specific databases

CTDi56165.
MGIiMGI:1933218. Tdrd1.

Phylogenomic databases

eggNOGiENOG410IPR3. Eukaryota.
ENOG410ZWZX. LUCA.
GeneTreeiENSGT00730000110295.
HOGENOMiHOG000081819.
HOVERGENiHBG108555.
InParanoidiQ99MV1.
KOiK18405.
OMAiCVAKYTV.
OrthoDBiEOG7VX8VC.
PhylomeDBiQ99MV1.

Miscellaneous databases

ChiTaRSiTdrd1. mouse.
NextBioi350650.
PROiQ99MV1.
SOURCEiSearch...

Gene expression databases

BgeeiQ99MV1.
CleanExiMM_TDRD1.
GenevisibleiQ99MV1. MM.

Family and domain databases

InterProiIPR002999. Tudor.
IPR002893. Znf_MYND.
[Graphical view]
PfamiPF00567. TUDOR. 4 hits.
PF01753. zf-MYND. 1 hit.
[Graphical view]
SMARTiSM00333. TUDOR. 4 hits.
[Graphical view]
PROSITEiPS50304. TUDOR. 4 hits.
PS01360. ZF_MYND_1. 1 hit.
PS50865. ZF_MYND_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse Tudor Repeat-1 (MTR-1) is a novel component of chromatoid bodies/nuages in male germ cells and forms a complex with snRNPs."
    Chuma S., Hiyoshi M., Yamamoto A., Hosokawa M., Takamune K., Nakatsuji N.
    Mech. Dev. 120:979-990(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: ICR.
    Tissue: Fetal gonad and Testis.
  2. "Tdrd1/Mtr-1, a tudor-related gene, is essential for male germ-cell differentiation and nuage/germinal granule formation in mice."
    Chuma S., Hosokawa M., Kitamura K., Kasai S., Fujioka M., Hiyoshi M., Takamune K., Noce T., Nakatsuji N.
    Proc. Natl. Acad. Sci. U.S.A. 103:15894-15899(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
    Strain: ICR.
    Tissue: Testis.
  3. "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: Testis.
  4. "An abundance of X-linked genes expressed in spermatogonia."
    Wang P.J., McCarrey J.R., Yang F., Page D.C.
    Nat. Genet. 27:422-426(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 27-1172.
    Tissue: Ovary and Testis.
  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] OF 220-1172.
  6. "Mouse MAELSTROM: the link between meiotic silencing of unsynapsed chromatin and microRNA pathway?"
    Costa Y., Speed R.M., Gautier P., Semple C.A., Maratou K., Turner J.M.A., Cooke H.J.
    Hum. Mol. Genet. 15:2324-2334(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAEL.
  7. "Tudor-related proteins TDRD1/MTR-1, TDRD6 and TDRD7/TRAP: domain composition, intracellular localization, and function in male germ cells in mice."
    Hosokawa M., Shoji M., Kitamura K., Tanaka T., Noce T., Chuma S., Nakatsuji N.
    Dev. Biol. 301:38-52(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-1019 AND GLU-1023.
  8. "Mili interacts with tudor domain-containing protein 1 in regulating spermatogenesis."
    Wang J., Saxe J.P., Tanaka T., Chuma S., Lin H.
    Curr. Biol. 19:640-644(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PIWIL2.
  9. "Proteomic analysis of murine Piwi proteins reveals a role for arginine methylation in specifying interaction with Tudor family members."
    Vagin V.V., Wohlschlegel J., Qu J., Jonsson Z., Huang X., Chuma S., Girard A., Sachidanandam R., Hannon G.J., Aravin A.A.
    Genes Dev. 23:1749-1762(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, INTERACTION WITH PIWIL1; PIWIL2 AND PIWIL4.
  10. "Loss of the Mili-interacting Tudor domain-containing protein-1 activates transposons and alters the Mili-associated small RNA profile."
    Reuter M., Chuma S., Tanaka T., Franz T., Stark A., Pillai R.S.
    Nat. Struct. Mol. Biol. 16:639-646(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PIWIL2, DISRUPTION PHENOTYPE.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Testis.
  12. Cited for: SUBCELLULAR LOCATION.
  13. "Tudor domain containing 12 (TDRD12) is essential for secondary PIWI interacting RNA biogenesis in mice."
    Pandey R.R., Tokuzawa Y., Yang Z., Hayashi E., Ichisaka T., Kajita S., Asano Y., Kunieda T., Sachidanandam R., Chuma S., Yamanaka S., Pillai R.S.
    Proc. Natl. Acad. Sci. U.S.A. 110:16492-16497(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TDRD12.
  14. "The multiple Tudor domain-containing protein TDRD1 is a molecular scaffold for mouse Piwi proteins and piRNA biogenesis factors."
    Mathioudakis N., Palencia A., Kadlec J., Round A., Tripsianes K., Sattler M., Pillai R.S., Cusack S.
    RNA 18:2056-2072(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 692-892 ALONE AND IN COMPLEX WITH METHYLATED PEPTIDE, TUDOR DOMAINS, MUTAGENESIS OF ASN-325; TYR-774 AND ASN-796, SUBUNIT, INTERACTION WITH PIWIL2.

Entry informationi

Entry nameiTDRD1_MOUSE
AccessioniPrimary (citable) accession number: Q99MV1
Secondary accession number(s): A2VDG6
, Q6F3G0, Q8CDN7, Q8K1G3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: March 24, 2009
Last modified: May 11, 2016
This is version 108 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

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.