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Protein

Piwi-like protein 1

Gene

Piwil1

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 repressing 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. Directly binds methylated piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements. Besides their function in transposable elements repression, piRNAs are probably involved in other processes during meiosis such as translation regulation. Probable component of some RISC complex, which mediates RNA cleavage and translational silencing. Also plays a role in the formation of chromatoid bodies and is required for some miRNAs stability.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei382 – 3821Required for binding 2'-O-methylated 3'-end of piRNAs

GO - Molecular functioni

  • mRNA binding Source: UniProtKB
  • piRNA binding Source: UniProtKB
  • protein kinase binding Source: MGI
  • single-stranded RNA binding Source: MGI

GO - Biological processi

  • gene silencing by RNA Source: UniProtKB
  • meiotic cell cycle Source: UniProtKB-KW
  • multicellular organism development Source: UniProtKB-KW
  • piRNA metabolic process Source: UniProtKB
  • regulation of translation Source: UniProtKB
  • spermatid development Source: UniProtKB
  • spermatogenesis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Meiosis, RNA-mediated gene silencing, Spermatogenesis, Translation regulation

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-5601884. PIWI-interacting RNA (piRNA) biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Piwi-like protein 1
Gene namesi
Name:Piwil1
Synonyms:Miwi
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1928897. Piwil1.

Subcellular locationi

GO - Cellular componenti

  • chromatoid body Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • dense body Source: MGI
  • nucleus Source: MGI
  • P granule Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Mice display spermatogenic arrest at the beginning of the round spermatid stage, resembling the phenotype of CREM, a master regulator of spermiogenesis; mRNAs of FHL5/activator of CREM and CREM target genes are down-regulated in testes. Female are fertile but male are completely sterile, no sperm is found in the epididimus. Chromatoid bodies from round spermatids are not fully compacted and remain as a diffuse chromatoid material.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi343 – 3431F → A: Impairs binding to 2'-O-methylated 3'-end of piRNAs. 1 Publication
Mutagenesisi382 – 3821M → A: Impairs binding to 2'-O-methylated 3'-end of piRNAs. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 862862Piwi-like protein 1PRO_0000234568Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141Omega-N-methylarginine; by PRMT5; alternate1 Publication
Modified residuei14 – 141Symmetric dimethylarginine; by PRMT5; alternate1 Publication
Modified residuei49 – 491Omega-N-methylarginine; by PRMT51 Publication
Modified residuei53 – 531Omega-N-methylarginine; alternate1 Publication
Modified residuei53 – 531Symmetric dimethylarginine; alternate1 Publication
Modified residuei371 – 3711Omega-N-methylarginine; by PRMT51 Publication

Post-translational modificationi

Arginine methylation by PRMT5 is required for the interaction with Tudor domain-containing protein (TDRD1, TDRKH/TDRD2, RNF17/TDRD4, TDRD6, TDRD7 and TDRD9) and subsequent localization to the meiotic nuage, also named P granule.5 Publications

Keywords - PTMi

Methylation

Proteomic databases

PaxDbiQ9JMB7.
PRIDEiQ9JMB7.

PTM databases

iPTMnetiQ9JMB7.
PhosphoSiteiQ9JMB7.

Expressioni

Tissue specificityi

Expressed in brain. Expressed in testis, specifically in spermatocytes (at protein level). Only detected in germ lineage cells of adult testis. Expressed in male gonads 2 weeks after birth at the initiation of spermatogenesis, but not expressed in female gonads.4 Publications

Gene expression databases

BgeeiQ9JMB7.
CleanExiMM_PIWIL1.
ExpressionAtlasiQ9JMB7. baseline and differential.
GenevisibleiQ9JMB7. MM.

Interactioni

Subunit structurei

Interacts (via Piwi domain) with DICER1, suggesting that it forms ribonucleoprotein RISC complexes; this interaction is regulated by HSP90AB1 activity (PubMed:16938833). Interacts with MAEL, KIF17, PABPC1, PRMT5 and WDR77 (PubMed:16787948, PubMed:16787967, PubMed:19020299, PubMed:19584108). Interacts (when methylated on arginine residues) with TDRD1, TDRKH/TDRD2, RNF17/TDRD4, TDRD6, TDRD7 and TDRD9 (PubMed:19584108, PubMed:19918066, PubMed:19926723, PubMed:23714778). Interacts with CLOCK (PubMed:22900038). Interacts with MOV10L1 (PubMed:20534472).10 Publications

GO - Molecular functioni

  • protein kinase binding Source: MGI

Protein-protein interaction databases

BioGridi208311. 1 interaction.
DIPiDIP-59456N.
IntActiQ9JMB7. 3 interactions.
STRINGi10090.ENSMUSP00000083222.

Structurei

Secondary structure

1
862
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi280 – 29011Combined sources
Helixi293 – 30412Combined sources
Beta strandi308 – 3114Combined sources
Turni312 – 3154Combined sources
Beta strandi316 – 3194Combined sources
Beta strandi322 – 3243Combined sources
Beta strandi335 – 3384Combined sources
Helixi343 – 3486Combined sources
Beta strandi358 – 3603Combined sources
Beta strandi362 – 3654Combined sources
Beta strandi381 – 3833Combined sources
Helixi385 – 3873Combined sources
Beta strandi388 – 3903Combined sources
Beta strandi492 – 4943Combined sources
Beta strandi498 – 5025Combined sources
Helixi503 – 5053Combined sources
Helixi506 – 51914Combined sources
Helixi521 – 5233Combined sources
Beta strandi525 – 5273Combined sources
Beta strandi531 – 5355Combined sources
Helixi539 – 54911Combined sources
Beta strandi557 – 5637Combined sources
Helixi566 – 57914Combined sources
Beta strandi584 – 5885Combined sources
Helixi589 – 5924Combined sources
Helixi595 – 60814Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XFMNMR-A276-425[»]
4P1ZX-ray2.30A/B/C/D485-612[»]
ProteinModelPortaliQ9JMB7.
SMRiQ9JMB7. Positions 107-841.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini278 – 392115PAZPROSITE-ProRule annotationAdd
BLAST
Domaini556 – 848293PiwiPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni317 – 3193Required for binding 2'-O-methylated 3'-end of piRNAs
Regioni541 – 678138RNA-bindingAdd
BLAST

Domaini

The PAZ domain specifically recognizes binds the 2'-O-methylated 3'-end of piRNAs.1 Publication

Sequence similaritiesi

Belongs to the argonaute family. Piwi subfamily.Curated
Contains 1 PAZ domain.PROSITE-ProRule annotation
Contains 1 Piwi domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1042. Eukaryota.
ENOG410XNRH. LUCA.
GeneTreeiENSGT00760000119148.
HOGENOMiHOG000254789.
HOVERGENiHBG049411.
InParanoidiQ9JMB7.
KOiK02156.
OMAiPGYIQPR.
OrthoDBiEOG712TVQ.
PhylomeDBiQ9JMB7.
TreeFamiTF354206.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
InterProiIPR014811. ArgoL1.
IPR031320. GAGE.
IPR003100. PAZ_dom.
IPR003165. Piwi.
IPR031326. PIWIL1.
IPR012337. RNaseH-like_dom.
[Graphical view]
PANTHERiPTHR22891:SF46. PTHR22891:SF46. 1 hit.
PfamiPF08699. ArgoL1. 1 hit.
PF05831. GAGE. 1 hit.
PF02170. PAZ. 1 hit.
PF02171. Piwi. 1 hit.
[Graphical view]
SMARTiSM01379. GAGE. 1 hit.
SM00949. PAZ. 1 hit.
SM00950. Piwi. 1 hit.
[Graphical view]
SUPFAMiSSF101690. SSF101690. 1 hit.
SSF53098. SSF53098. 1 hit.
PROSITEiPS50821. PAZ. 1 hit.
PS50822. PIWI. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9JMB7-1) [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
MTGRARARAR GRARGQETVQ HVGAAASQQP GYIPPRPQQS PTEGDLVGRG
60 70 80 90 100
RQRGMVVGAT SKSQELQISA GFQELSLAER GGRRRDFHDL GVNTRQNLDH
110 120 130 140 150
VKESKTGSSG IIVKLSTNHF RLTSRPQWAL YQYHIDYNPL MEARRLRSAL
160 170 180 190 200
LFQHEDLIGR CHAFDGTILF LPKRLQHKVT EVFSQTRNGE HVRITITLTN
210 220 230 240 250
ELPPTSPTCL QFYNIIFRRL LKIMNLQQIG RNYYNPSDPI DIPNHRLVIW
260 270 280 290 300
PGFTTSILQY ENNIMLCTDV SHKVLRSETV LDFMFNLYQQ TEEHKFQEQV
310 320 330 340 350
SKELIGLIVL TKYNNKTYRV DDIDWDQNPK STFKKADGSE VSFLEYYRKQ
360 370 380 390 400
YNQEITDLKQ PVLVSQPKRR RGPGGTLPGP AMLIPELCYL TGLTDKMRND
410 420 430 440 450
FNVMKDLAVH TRLTPEQRQR EVGRLIDYIH KDDNVQRELR DWGLSFDSNL
460 470 480 490 500
LSFSGRILQS EKIHQGGKTF DYNPQFADWS KETRGAPLIS VKPLDNWLLI
510 520 530 540 550
YTRRNYEAAN SLIQNLFKVT PAMGIQMKKA IMIEVDDRTE AYLRALQQKV
560 570 580 590 600
TSDTQIVVCL LSSNRKDKYD AIKKYLCTDC PTPSQCVVAR TLGKQQTVMA
610 620 630 640 650
IATKIALQMN CKMGGELWRV DMPLKLAMIV GIDCYHDTTA GRRSIAGFVA
660 670 680 690 700
SINEGMTRWF SRCVFQDRGQ ELVDGLKVCL QAALRAWSGC NEYMPSRVIV
710 720 730 740 750
YRDGVGDGQL KTLVNYEVPQ FLDCLKSVGR GYNPRLTVIV VKKRVNARFF
760 770 780 790 800
AQSGGRLQNP LPGTVIDVEV TRPEWYDFFI VSQAVRSGSV SPTHYNVIYD
810 820 830 840 850
SSGLKPDHIQ RLTYKLCHVY YNWPGVIRVP APCQYAHKLA FLVGQSIHRE
860
PNLSLSNRLY YL
Length:862
Mass (Da):98,574
Last modified:October 1, 2000 - v1
Checksum:i45588D13284CCC4C
GO
Isoform 2 (identifier: Q9JMB7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     825-862: GVIRVPAPCQYAHKLAFLVGQSIHREPNLSLSNRLYYL → VSVLLWTTYPG

Note: No experimental confirmation available.
Show »
Length:835
Mass (Da):95,484
Checksum:i3F96A55A0DEE610F
GO

Sequence cautioni

The sequence AAH66846.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti374 – 3741G → S in AAH66846 (PubMed:15489334).Curated
Sequence conflicti468 – 4681K → R in AAH66846 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei825 – 86238GVIRV…RLYYL → VSVLLWTTYPG in isoform 2. 1 PublicationVSP_036663Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB032604 mRNA. Translation: BAA93705.1.
AF438405 mRNA. Translation: AAL31014.1.
EF196092 mRNA. Translation: ABM69181.1.
BC066846 mRNA. Translation: AAH66846.1. Sequence problems.
BC129857 mRNA. Translation: AAI29858.1.
BC129858 mRNA. Translation: AAI29859.1.
CCDSiCCDS19690.1. [Q9JMB7-1]
RefSeqiNP_067286.1. NM_021311.3. [Q9JMB7-1]
XP_006504381.1. XM_006504318.1. [Q9JMB7-1]
XP_006504382.1. XM_006504319.2. [Q9JMB7-1]
UniGeneiMm.272720.

Genome annotation databases

EnsembliENSMUST00000086056; ENSMUSP00000083222; ENSMUSG00000029423. [Q9JMB7-1]
ENSMUST00000195959; ENSMUSP00000142386; ENSMUSG00000029423. [Q9JMB7-2]
GeneIDi57749.
KEGGimmu:57749.
UCSCiuc008zsi.1. mouse. [Q9JMB7-1]
uc008zsj.1. mouse. [Q9JMB7-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB032604 mRNA. Translation: BAA93705.1.
AF438405 mRNA. Translation: AAL31014.1.
EF196092 mRNA. Translation: ABM69181.1.
BC066846 mRNA. Translation: AAH66846.1. Sequence problems.
BC129857 mRNA. Translation: AAI29858.1.
BC129858 mRNA. Translation: AAI29859.1.
CCDSiCCDS19690.1. [Q9JMB7-1]
RefSeqiNP_067286.1. NM_021311.3. [Q9JMB7-1]
XP_006504381.1. XM_006504318.1. [Q9JMB7-1]
XP_006504382.1. XM_006504319.2. [Q9JMB7-1]
UniGeneiMm.272720.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XFMNMR-A276-425[»]
4P1ZX-ray2.30A/B/C/D485-612[»]
ProteinModelPortaliQ9JMB7.
SMRiQ9JMB7. Positions 107-841.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208311. 1 interaction.
DIPiDIP-59456N.
IntActiQ9JMB7. 3 interactions.
STRINGi10090.ENSMUSP00000083222.

PTM databases

iPTMnetiQ9JMB7.
PhosphoSiteiQ9JMB7.

Proteomic databases

PaxDbiQ9JMB7.
PRIDEiQ9JMB7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000086056; ENSMUSP00000083222; ENSMUSG00000029423. [Q9JMB7-1]
ENSMUST00000195959; ENSMUSP00000142386; ENSMUSG00000029423. [Q9JMB7-2]
GeneIDi57749.
KEGGimmu:57749.
UCSCiuc008zsi.1. mouse. [Q9JMB7-1]
uc008zsj.1. mouse. [Q9JMB7-2]

Organism-specific databases

CTDi9271.
MGIiMGI:1928897. Piwil1.

Phylogenomic databases

eggNOGiKOG1042. Eukaryota.
ENOG410XNRH. LUCA.
GeneTreeiENSGT00760000119148.
HOGENOMiHOG000254789.
HOVERGENiHBG049411.
InParanoidiQ9JMB7.
KOiK02156.
OMAiPGYIQPR.
OrthoDBiEOG712TVQ.
PhylomeDBiQ9JMB7.
TreeFamiTF354206.

Enzyme and pathway databases

ReactomeiR-MMU-5601884. PIWI-interacting RNA (piRNA) biogenesis.

Miscellaneous databases

PROiQ9JMB7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JMB7.
CleanExiMM_PIWIL1.
ExpressionAtlasiQ9JMB7. baseline and differential.
GenevisibleiQ9JMB7. MM.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
InterProiIPR014811. ArgoL1.
IPR031320. GAGE.
IPR003100. PAZ_dom.
IPR003165. Piwi.
IPR031326. PIWIL1.
IPR012337. RNaseH-like_dom.
[Graphical view]
PANTHERiPTHR22891:SF46. PTHR22891:SF46. 1 hit.
PfamiPF08699. ArgoL1. 1 hit.
PF05831. GAGE. 1 hit.
PF02170. PAZ. 1 hit.
PF02171. Piwi. 1 hit.
[Graphical view]
SMARTiSM01379. GAGE. 1 hit.
SM00949. PAZ. 1 hit.
SM00950. Piwi. 1 hit.
[Graphical view]
SUPFAMiSSF101690. SSF101690. 1 hit.
SSF53098. SSF53098. 1 hit.
PROSITEiPS50821. PAZ. 1 hit.
PS50822. PIWI. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION, RNA-BINDING.
    Tissue: Testis.
  2. "miwi, a murine homolog of piwi, encodes a cytoplasmic protein essential for spermatogenesis."
    Deng W., Lin H.
    Dev. Cell 2:819-830(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
  3. "The clone of Miwi and research about its effect on self-proliferation of SSCs."
    Zhang S., Li D., Li E., Lu J.
    Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: KM.
    Tissue: Testis.
  4. "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] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Egg.
  5. "A novel class of small RNAs in mouse spermatogenic cells."
    Grivna S.T., Beyret E., Wang Z., Lin H.
    Genes Dev. 20:1709-1714(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA-BINDING.
  6. "Interplay of PIWI/Argonaute protein MIWI and kinesin KIF17b in chromatoid bodies of male germ cells."
    Kotaja N., Lin H., Parvinen M., Sassone-Corsi P.
    J. Cell Sci. 119:2819-2825(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH KIF17, DISRUPTION PHENOTYPE.
  7. "A germline-specific class of small RNAs binds mammalian Piwi proteins."
    Girard A., Sachidanandam R., Hannon G.J., Carmell M.A.
    Nature 442:199-202(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA-BINDING.
  8. "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.
  9. "MIWI associates with translational machinery and PIWI-interacting RNAs (piRNAs) in regulating spermatogenesis."
    Grivna S.T., Pyhtila B., Lin H.
    Proc. Natl. Acad. Sci. U.S.A. 103:13415-13420(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, RNA-BINDING, INTERACTION WITH DICER1.
  10. "Characterization of two cytoplasmic poly(A)-binding proteins, PABPC1 and PABPC2, in mouse spermatogenic cells."
    Kimura M., Ishida K., Kashiwabara S., Baba T.
    Biol. Reprod. 80:545-554(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PABPC1.
  11. "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: METHYLATION AT ARG-14; ARG-49 AND ARG-371, SUBCELLULAR LOCATION, INTERACTION WITH TDRD1; TDRKH; TDRD6; PRMT5 AND WDR77.
  12. "Arginine methylation of Piwi proteins catalysed by dPRMT5 is required for Ago3 and Aub stability."
    Kirino Y., Kim N., de Planell-Saguer M., Khandros E., Chiorean S., Klein P.S., Rigoutsos I., Jongens T.A., Mourelatos Z.
    Nat. Cell Biol. 11:652-658(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, METHYLATION.
  13. "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: METHYLATION.
  14. "Mouse Piwi interactome identifies binding mechanism of Tdrkh Tudor domain to arginine methylated Miwi."
    Chen C., Jin J., James D.A., Adams-Cioaba M.A., Park J.G., Guo Y., Tenaglia E., Xu C., Gish G., Min J., Pawson T.
    Proc. Natl. Acad. Sci. U.S.A. 106:20336-20341(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT ARG-53, INTERACTION WITH TDRKH.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Testis.
  16. "Mouse MOV10L1 associates with Piwi proteins and is an essential component of the Piwi-interacting RNA (piRNA) pathway."
    Zheng K., Xiol J., Reuter M., Eckardt S., Leu N.A., McLaughlin K.J., Stark A., Sachidanandam R., Pillai R.S., Wang P.J.
    Proc. Natl. Acad. Sci. U.S.A. 107:11841-11846(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MOV10L1.
  17. "Arginine methylation of Aubergine mediates Tudor binding and germ plasm localization."
    Kirino Y., Vourekas A., Sayed N., de Lima Alves F., Thomson T., Lasko P., Rappsilber J., Jongens T.A., Mourelatos Z.
    RNA 16:70-78(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TDRD6, TISSUE SPECIFICITY, METHYLATION.
  18. "Circadian proteins CLOCK and BMAL1 in the chromatoid body, a RNA processing granule of male germ cells."
    Peruquetti R.L., de Mateo S., Sassone-Corsi P.
    PLoS ONE 7:E42695-E42695(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CLOCK.
  19. "Tdrkh is essential for spermatogenesis and participates in primary piRNA biogenesis in the germline."
    Saxe J.P., Chen M., Zhao H., Lin H.
    EMBO J. 32:1869-1885(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TDRKH.
  20. "Recognition of 2'-O-methylated 3'-end of piRNA by the PAZ domain of a Piwi protein."
    Simon B., Kirkpatrick J.P., Eckhardt S., Reuter M., Rocha E.A., Andrade-Navarro M.A., Sehr P., Pillai R.S., Carlomagno T.
    Structure 19:172-180(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 276-395 IN COMPLEX WITH METHYLATED SMALL RNA, DOMAIN PAZ, MUTAGENESIS OF PHE-343 AND MET-382.

Entry informationi

Entry nameiPIWL1_MOUSE
AccessioniPrimary (citable) accession number: Q9JMB7
Secondary accession number(s): A1L324, A1L325, Q6NXX0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: October 1, 2000
Last modified: June 8, 2016
This is version 109 of the entry and version 1 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.