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Q96J94

- PIWL1_HUMAN

UniProt

Q96J94 - PIWL1_HUMAN

Protein

Piwi-like protein 1

Gene

PIWIL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    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 By similarity. Isoform 3 may be a negative developmental regulator.By similarity3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei381 – 3811Required for binding 2'-O-methylated 3'-end of piRNAs

    GO - Molecular functioni

    1. mRNA binding Source: UniProtKB
    2. piRNA binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. single-stranded RNA binding Source: Ensembl

    GO - Biological processi

    1. gene silencing by RNA Source: UniProtKB
    2. meiotic nuclear division Source: UniProtKB-KW
    3. multicellular organismal development Source: UniProtKB-KW
    4. piRNA metabolic process Source: Ensembl
    5. regulation of translation Source: UniProtKB-KW
    6. spermatid development Source: UniProtKB

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

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

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Piwi-like protein 1
    Gene namesi
    Name:PIWIL1
    Synonyms:HIWI
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:9007. PIWIL1.

    Subcellular locationi

    Cytoplasm By similarity
    Note: Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. Also present in chromatoid body By similarity.By similarity

    GO - Cellular componenti

    1. chromatoid body Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. mRNA cap binding complex Source: Ensembl
    4. P granule Source: UniProtKB
    5. polysome Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi379 – 3791P → H: Impairs binding to 2'-O-methylated 3'-end of piRNAs; when associated with Y-381. 1 Publication
    Mutagenesisi381 – 3811M → Y: Impairs binding to 2'-O-methylated 3'-end of piRNAs; when associated with H-379. 1 Publication

    Organism-specific databases

    PharmGKBiPA33341.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 861861Piwi-like protein 1PRO_0000234567Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei14 – 141Omega-N-methylarginine; by PRMT5; alternateBy similarity
    Modified residuei14 – 141Symmetric dimethylarginine; by PRMT5; alternateBy similarity
    Modified residuei49 – 491Omega-N-methylarginine; by PRMT5By similarity
    Modified residuei53 – 531Omega-N-methylarginineBy similarity
    Modified residuei370 – 3701Omega-N-methylarginine; by PRMT5By similarity

    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.By similarity

    Keywords - PTMi

    Methylation

    Proteomic databases

    PaxDbiQ96J94.
    PRIDEiQ96J94.

    PTM databases

    PhosphoSiteiQ96J94.

    Expressioni

    Tissue specificityi

    Expressed in spermatocytes and spermatids. Also detected in prostate cancer (at protein level). Detected in most fetal and adult tissues. Expressed in testes, specifically in germline cells; detected in spermatocytes and spermatids during spermatogenesis. Increased expression in testicular tumors originating from embryonic germ cells with retention of germ cells phenotype. No expression in testicular tumors of somatic origin, such as Sertoli cell and Leydig cell tumors. Overexpressed in gastric cancer cells. Isoform 3 is ubiquitously expressed, and specifically in CD34+ hematopoietic progenitor cells but not in more differentiated cells.4 Publications

    Inductioni

    Isoform 3 is down-regulated in CD34+ hematopoietic cells during differentiation.1 Publication

    Gene expression databases

    ArrayExpressiQ96J94.
    BgeeiQ96J94.
    CleanExiHS_PIWIL1.
    GenevestigatoriQ96J94.

    Organism-specific databases

    HPAiCAB012217.
    HPA018798.

    Interactioni

    Subunit structurei

    Interacts (via Piwi domain) with DICER1, suggesting that it forms ribonucleoprotein RISC complexes. This interaction is regulated by HSP90AB1 activity. Interacts with MAEL, KIF17, PABPC1, PRMT5 and WDR77. Interacts (when methylated on arginine residues) with TDRD1, TDRKH/TDRD2, RNF17/TDRD4, TDRD6, TDRD7 and TDRD9. Interacts with CLOCK By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DICER1Q9UPY32EBI-527417,EBI-395506

    Protein-protein interaction databases

    BioGridi114690. 5 interactions.
    DIPiDIP-33534N.
    IntActiQ96J94. 12 interactions.
    STRINGi9606.ENSP00000245255.

    Structurei

    Secondary structure

    1
    861
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi279 – 2857
    Helixi286 – 2883
    Helixi292 – 30312
    Beta strandi307 – 3104
    Turni311 – 3144
    Beta strandi316 – 3183
    Beta strandi321 – 3233
    Beta strandi331 – 3333
    Beta strandi335 – 3373
    Beta strandi339 – 3413
    Helixi342 – 3509
    Beta strandi361 – 3644
    Beta strandi370 – 3756
    Beta strandi380 – 3823
    Helixi384 – 3863
    Beta strandi387 – 3893

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2L5CNMR-A266-399[»]
    2L5DNMR-A266-399[»]
    3O3IX-ray2.80X277-399[»]
    3O6EX-ray2.90X277-399[»]
    3O7VX-ray2.10X276-399[»]
    ProteinModelPortaliQ96J94.
    SMRiQ96J94. Positions 106-840.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96J94.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini277 – 391115PAZPROSITE-ProRule annotationAdd
    BLAST
    Domaini555 – 847293PiwiPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni316 – 3183Required for binding 2'-O-methylated 3'-end of piRNAs
    Regioni540 – 677138RNA-bindingBy similarityAdd
    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

    eggNOGiNOG286051.
    HOGENOMiHOG000254789.
    HOVERGENiHBG049411.
    InParanoidiQ96J94.
    KOiK02156.
    OMAiPGYIQPR.
    OrthoDBiEOG712TVQ.
    PhylomeDBiQ96J94.
    TreeFamiTF354206.

    Family and domain databases

    Gene3Di3.30.420.10. 1 hit.
    InterProiIPR008625. GAGE.
    IPR003100. PAZ_dom.
    IPR003165. Piwi.
    IPR012337. RNaseH-like_dom.
    [Graphical view]
    PfamiPF05831. GAGE. 1 hit.
    PF02170. PAZ. 1 hit.
    PF02171. Piwi. 1 hit.
    [Graphical view]
    SMARTiSM00949. 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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96J94-1) [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

    MTGRARARAR GRARGQETAQ LVGSTASQQP GYIQPRPQPP PAEGELFGRG    50
    RQRGTAGGTA KSQGLQISAG FQELSLAERG GRRRDFHDLG VNTRQNLDHV 100
    KESKTGSSGI IVRLSTNHFR LTSRPQWALY QYHIDYNPLM EARRLRSALL 150
    FQHEDLIGKC HAFDGTILFL PKRLQQKVTE VFSKTRNGED VRITITLTNE 200
    LPPTSPTCLQ FYNIIFRRLL KIMNLQQIGR NYYNPNDPID IPSHRLVIWP 250
    GFTTSILQYE NSIMLCTDVS HKVLRSETVL DFMFNFYHQT EEHKFQEQVS 300
    KELIGLVVLT KYNNKTYRVD DIDWDQNPKS TFKKADGSEV SFLEYYRKQY 350
    NQEITDLKQP VLVSQPKRRR GPGGTLPGPA MLIPELCYLT GLTDKMRNDF 400
    NVMKDLAVHT RLTPEQRQRE VGRLIDYIHK NDNVQRELRD WGLSFDSNLL 450
    SFSGRILQTE KIHQGGKTFD YNPQFADWSK ETRGAPLISV KPLDNWLLIY 500
    TRRNYEAANS LIQNLFKVTP AMGMQMRKAI MIEVDDRTEA YLRVLQQKVT 550
    ADTQIVVCLL SSNRKDKYDA IKKYLCTDCP TPSQCVVART LGKQQTVMAI 600
    ATKIALQMNC KMGGELWRVD IPLKLVMIVG IDCYHDMTAG RRSIAGFVAS 650
    INEGMTRWFS RCIFQDRGQE LVDGLKVCLQ AALRAWNSCN EYMPSRIIVY 700
    RDGVGDGQLK TLVNYEVPQF LDCLKSIGRG YNPRLTVIVV KKRVNTRFFA 750
    QSGGRLQNPL PGTVIDVEVT RPEWYDFFIV SQAVRSGSVS PTHYNVIYDN 800
    SGLKPDHIQR LTYKLCHIYY NWPGVIRVPA PCQYAHKLAF LVGQSIHREP 850
    NLSLSNRLYY L 861
    Length:861
    Mass (Da):98,603
    Last modified:December 1, 2001 - v1
    Checksum:i58D7F6C7321DEFA4
    GO
    Isoform 2 (identifier: Q96J94-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         824-829: GVIRVP → VSASTC
         830-861: Missing.

    Show »
    Length:829
    Mass (Da):94,845
    Checksum:i03ADA415D1C159C3
    GO
    Isoform 3 (identifier: Q96J94-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-86: Missing.
         87-89: HDL → MIF

    Show »
    Length:775
    Mass (Da):89,484
    Checksum:iDF169A2E9EAFD916
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti178 – 1781V → A in BAC04068. (PubMed:14702039)Curated
    Sequence conflicti314 – 3141N → I in AAC97371. (PubMed:12037681)Curated
    Sequence conflicti339 – 3391E → G in AAC97371. (PubMed:12037681)Curated
    Sequence conflicti353 – 3531E → K in BAF49084. (PubMed:17544373)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti491 – 4911K → N.1 Publication
    Corresponds to variant rs17856812 [ dbSNP | Ensembl ].
    VAR_026288
    Natural varianti527 – 5271R → K.1 Publication
    Corresponds to variant rs1106042 [ dbSNP | Ensembl ].
    VAR_026289
    Natural varianti575 – 5751L → P.1 Publication
    Corresponds to variant rs17852568 [ dbSNP | Ensembl ].
    VAR_026290

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8686Missing in isoform 3. 1 PublicationVSP_018366Add
    BLAST
    Alternative sequencei87 – 893HDL → MIF in isoform 3. 1 PublicationVSP_018367
    Alternative sequencei824 – 8296GVIRVP → VSASTC in isoform 2. 1 PublicationVSP_018368
    Alternative sequencei830 – 86132Missing in isoform 2. 1 PublicationVSP_018369Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF264004 mRNA. Translation: AAK92281.1.
    AF104260 mRNA. Translation: AAC97371.2.
    AF387507 mRNA. Translation: AAK69348.1.
    AK093133 mRNA. Translation: BAC04068.1.
    BC028581 mRNA. Translation: AAH28581.1.
    AB274731 mRNA. Translation: BAF49084.1.
    CCDSiCCDS9268.1. [Q96J94-1]
    RefSeqiNP_001177900.1. NM_001190971.1. [Q96J94-2]
    NP_004755.2. NM_004764.4. [Q96J94-1]
    XP_005253689.1. XM_005253632.2. [Q96J94-1]
    XP_006719761.1. XM_006719698.1. [Q96J94-1]
    UniGeneiHs.405659.

    Genome annotation databases

    EnsembliENST00000245255; ENSP00000245255; ENSG00000125207. [Q96J94-1]
    GeneIDi9271.
    KEGGihsa:9271.
    UCSCiuc001uij.2. human. [Q96J94-2]
    uc001uik.3. human. [Q96J94-1]

    Polymorphism databases

    DMDMi74716803.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF264004 mRNA. Translation: AAK92281.1 .
    AF104260 mRNA. Translation: AAC97371.2 .
    AF387507 mRNA. Translation: AAK69348.1 .
    AK093133 mRNA. Translation: BAC04068.1 .
    BC028581 mRNA. Translation: AAH28581.1 .
    AB274731 mRNA. Translation: BAF49084.1 .
    CCDSi CCDS9268.1. [Q96J94-1 ]
    RefSeqi NP_001177900.1. NM_001190971.1. [Q96J94-2 ]
    NP_004755.2. NM_004764.4. [Q96J94-1 ]
    XP_005253689.1. XM_005253632.2. [Q96J94-1 ]
    XP_006719761.1. XM_006719698.1. [Q96J94-1 ]
    UniGenei Hs.405659.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2L5C NMR - A 266-399 [» ]
    2L5D NMR - A 266-399 [» ]
    3O3I X-ray 2.80 X 277-399 [» ]
    3O6E X-ray 2.90 X 277-399 [» ]
    3O7V X-ray 2.10 X 276-399 [» ]
    ProteinModelPortali Q96J94.
    SMRi Q96J94. Positions 106-840.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114690. 5 interactions.
    DIPi DIP-33534N.
    IntActi Q96J94. 12 interactions.
    STRINGi 9606.ENSP00000245255.

    PTM databases

    PhosphoSitei Q96J94.

    Polymorphism databases

    DMDMi 74716803.

    Proteomic databases

    PaxDbi Q96J94.
    PRIDEi Q96J94.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000245255 ; ENSP00000245255 ; ENSG00000125207 . [Q96J94-1 ]
    GeneIDi 9271.
    KEGGi hsa:9271.
    UCSCi uc001uij.2. human. [Q96J94-2 ]
    uc001uik.3. human. [Q96J94-1 ]

    Organism-specific databases

    CTDi 9271.
    GeneCardsi GC12P130822.
    HGNCi HGNC:9007. PIWIL1.
    HPAi CAB012217.
    HPA018798.
    MIMi 605571. gene.
    neXtProti NX_Q96J94.
    PharmGKBi PA33341.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG286051.
    HOGENOMi HOG000254789.
    HOVERGENi HBG049411.
    InParanoidi Q96J94.
    KOi K02156.
    OMAi PGYIQPR.
    OrthoDBi EOG712TVQ.
    PhylomeDBi Q96J94.
    TreeFami TF354206.

    Miscellaneous databases

    EvolutionaryTracei Q96J94.
    GeneWikii PIWIL1.
    GenomeRNAii 9271.
    NextBioi 34751.
    PROi Q96J94.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96J94.
    Bgeei Q96J94.
    CleanExi HS_PIWIL1.
    Genevestigatori Q96J94.

    Family and domain databases

    Gene3Di 3.30.420.10. 1 hit.
    InterProi IPR008625. GAGE.
    IPR003100. PAZ_dom.
    IPR003165. Piwi.
    IPR012337. RNaseH-like_dom.
    [Graphical view ]
    Pfami PF05831. GAGE. 1 hit.
    PF02170. PAZ. 1 hit.
    PF02171. Piwi. 1 hit.
    [Graphical view ]
    SMARTi SM00949. PAZ. 1 hit.
    SM00950. Piwi. 1 hit.
    [Graphical view ]
    SUPFAMi SSF101690. SSF101690. 1 hit.
    SSF53098. SSF53098. 1 hit.
    PROSITEi PS50821. PAZ. 1 hit.
    PS50822. PIWI. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human CD34+ stem cells express the hiwi gene, a human homologue of the Drosophila gene piwi."
      Sharma A.K., Nelson M.C., Brandt J.E., Wessman M., Mahmud N., Weller K.P., Hoffman R.
      Blood 97:426-434(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, INDUCTION.
      Tissue: Testis.
    2. "Molecular characterization of hiwi, a human member of the piwi gene family whose overexpression is correlated to seminomas."
      Qiao D., Zeeman A.-M., Deng W., Looijenga L.H.J., Lin H.
      Oncogene 21:3988-3999(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
      Tissue: Testis.
    3. "Cloning and identification of human piwi protein related to testis development."
      Sha J.H.
      Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Testis.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: 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] (ISOFORM 1), VARIANTS ASN-491; LYS-527 AND PRO-575.
      Tissue: Testis.
    6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-530.
    7. "Identification of eight members of the Argonaute family in the human genome."
      Sasaki T., Shiohama A., Minoshima S., Shimizu N.
      Genomics 82:323-330(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    8. "Characterization of the interactions between mammalian PAZ PIWI domain proteins and Dicer."
      Tahbaz N., Kolb F.A., Zhang H., Jaronczyk K., Filipowicz W., Hobman T.C.
      EMBO Rep. 5:189-194(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DICER1, FUNCTION.
    9. "Expression of hiwi gene in human gastric cancer was associated with proliferation of cancer cells."
      Liu X., Sun Y., Guo J., Ma H., Li J., Dong B., Jin G., Zhang J., Wu J., Meng L., Shou C.
      Int. J. Cancer 118:1922-1929(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Scanning of novel cancer/testis proteins by human testis proteomic analysis."
      Liu M., Hu Z., Qi L., Wang J., Zhou T., Guo Y., Zeng Y., Zheng B., Wu Y., Zhang P., Chen X., Tu W., Zhang T., Zhou Q., Jiang M., Guo X., Zhou Z., Sha J.
      Proteomics 13:1200-1210(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    11. "Structural basis for piRNA 2'-O-methylated 3'-end recognition by Piwi PAZ (Piwi/Argonaute/Zwille) domains."
      Tian Y., Simanshu D.K., Ma J.B., Patel D.J.
      Proc. Natl. Acad. Sci. U.S.A. 108:903-910(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 277-399 IN COMPLEX WITH METHYLATED SMALL RNA, DOMAIN PAZ, MUTAGENESIS OF PRO-379 AND MET-381.

    Entry informationi

    Entry nameiPIWL1_HUMAN
    AccessioniPrimary (citable) accession number: Q96J94
    Secondary accession number(s): A4F266
    , O95404, Q8NA60, Q8TBY5, Q96JD5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 16, 2006
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 96 of the entry and version 1 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3