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Q8TC59

- PIWL2_HUMAN

UniProt

Q8TC59 - PIWL2_HUMAN

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Protein
Piwi-like protein 2
Gene
PIWIL2, HILI
Organism
Homo sapiens (Human)
Status
Reviewed - 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. Plays an essential role in meiotic differentiation of spermatocytes, germ cell differentiation and in self-renewal of spermatogonial stem cells. Its presence in oocytes suggests that it may participate in similar functions during oogenesis in females. 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 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. Associates with primary piRNAs in the cytoplasm and is required for PIWIL4/MIWI2 nuclear localization and association with secondary piRNAs antisense. The piRNA process acts upstream of known mediators of DNA methylation. Participates in a piRNA amplification loop. Besides their function in transposable elements repression, piRNAs are probably involved in other processes during meiosis such as translation regulation. Indirectly modulate expression of genes such as PDGFRB, SLC2A1, ITGA6, GJA7, THY1, CD9 and STRA8. Inhibits tumor cell growth when repressed. When overexpressed, acts as an oncogene by inhibition of apoptosis and promotion of proliferation in tumors By similarity.1 Publication

GO - Molecular functioni

  1. mRNA binding Source: Ensembl
  2. piRNA binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. DNA methylation involved in gamete generation Source: UniProtKB
  2. RNA 5'-end processing Source: UniProtKB
  3. gene silencing by RNA Source: UniProtKB
  4. germ-line stem cell maintenance Source: UniProtKB
  5. meiotic nuclear division Source: UniProtKB-KW
  6. multicellular organismal development Source: UniProtKB-KW
  7. oogenesis Source: UniProtKB
  8. piRNA metabolic process Source: UniProtKB
  9. positive regulation of meiosis I Source: Ensembl
  10. positive regulation of translation Source: UniProtKB
  11. spermatogenesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

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

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Piwi-like protein 2
Alternative name(s):
Cancer/testis antigen 80
Short name:
CT80
Gene namesi
Name:PIWIL2
Synonyms:HILI
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:17644. PIWIL2.

Subcellular locationi

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

GO - Cellular componenti

  1. P granule Source: UniProtKB
  2. chromatoid body Source: UniProtKB
  3. cytoplasm Source: UniProtKB
  4. pi-body Source: UniProtKB
  5. polysome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38461.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 973973Piwi-like protein 2
PRO_0000234569Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei47 – 471Symmetric dimethylarginine By similarity
Modified residuei76 – 761Omega-N-methylarginine; by PRMT5; alternate By similarity
Modified residuei76 – 761Symmetric dimethylarginine; by PRMT5; alternate By similarity
Modified residuei97 – 971Omega-N-methylarginine; by PRMT5; alternate By similarity
Modified residuei97 – 971Symmetric dimethylarginine; alternate By similarity
Modified residuei102 – 1021Omega-N-methylarginine; alternate By similarity
Modified residuei102 – 1021Symmetric dimethylarginine; by PRMT5; alternate By similarity
Modified residuei165 – 1651Symmetric dimethylarginine; by PRMT5 By similarity
Modified residuei551 – 5511Symmetric dimethylarginine; by PRMT5 By similarity

Post-translational modificationi

Arginine methylation by PRMT5 is required for the interaction with Tudor domain-containing protein TDRD1 and subsequent localization to the meiotic nuage, also named P granule By similarity.

Keywords - PTMi

Methylation

Proteomic databases

PaxDbiQ8TC59.
PRIDEiQ8TC59.

PTM databases

PhosphoSiteiQ8TC59.

Expressioni

Tissue specificityi

Expressed in adult testis and in most tumors.1 Publication

Gene expression databases

BgeeiQ8TC59.
CleanExiHS_PIWIL2.
GenevestigatoriQ8TC59.

Organism-specific databases

HPAiHPA029345.

Interactioni

Subunit structurei

Interacts with DDX4, MAEL, EIF3A, EIF4E, EIF4G, PRMT5 and WDR77. Associates with EIF4E- and EIF4G-containing m7G cap-binding complexes. Interacts (when methylated on arginine residues) with TDRD1 and TDRKH/TDRD2. Interacts with TDRD12 By similarity.

Protein-protein interaction databases

BioGridi120431. 2 interactions.
STRINGi9606.ENSP00000349208.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi390 – 41324
Beta strandi417 – 4204
Turni421 – 4233
Beta strandi426 – 4283
Beta strandi431 – 4333
Beta strandi440 – 4434
Beta strandi449 – 4513
Helixi452 – 4609
Beta strandi471 – 4744
Beta strandi477 – 4804
Beta strandi482 – 4854
Beta strandi491 – 4933
Helixi495 – 4973

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3O7XX-ray2.92A/B/C/D387-525[»]
3QIRX-ray2.45A/B/C/D386-533[»]
ProteinModelPortaliQ8TC59.
SMRiQ8TC59. Positions 218-962.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini384 – 496113PAZ
Add
BLAST
Domaini668 – 959292Piwi
Add
BLAST

Sequence similaritiesi

Contains 1 PAZ domain.
Contains 1 Piwi domain.

Phylogenomic databases

eggNOGiNOG286051.
HOVERGENiHBG049411.
InParanoidiQ8TC59.
KOiK02156.
OMAiQELNWIK.
OrthoDBiEOG712TVQ.
PhylomeDBiQ8TC59.
TreeFamiTF354206.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
InterProiIPR003100. PAZ_dom.
IPR003165. Piwi.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamiPF02170. 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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8TC59-1) [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

MDPFRPSFRG QSPIHPSQCQ AVRMPGCWPQ ASKPLDPALG RGAPAGRGHV    50
FGKPEEPSTQ RGPAQRESVG LVSMFRGLGI ETVSKTPLKR EMLPSGRGIL 100
GRGLSANLVR KDREELSPTF WDPKVLAAGD SKMAETSVGW SRTLGRGSSD 150
ASLLPLGRAA GGISREVDKP PCTFSTPSRG PPQLSSPPAL PQSPLHSPDR 200
PLVLTVEHKE KELIVKQGSK GTPQSLGLNL VKIQCHNEAV YQYHVTFSPN 250
VECKSMRFGM LKDHQAVTGN VTAFDGSILY LPVKLQQVLE LKSQRKTDSA 300
EISIKIQMTK ILEPCSDLCI PFYNVVFRRV MKLLDMKLVG RNFYDPTSAM 350
VLQQHRLQIW PGYAASIRRT DGGLFLLADV SHKVIRNDCV LDVMHAIYQQ 400
NKEHFQDECT KLLVGNIVIT RYNNRTYRID DVDWNKTPKD SFTMSDGKEI 450
TFLEYYSKNY GITVKEEDQP LLIHRPSERQ DNHGMLLKGE ILLLPELSFM 500
TGIPEKMKKD FRAMKDLAQQ INLSPKQHHS ALECLLQRIA KNEAATNELM 550
RWGLRLQKDV HKIEGRVLPM ERINLKNTSF ITSQELNWVK EVTRDPSILT 600
IPMHFWALFY PKRAMDQARE LVNMLEKIAG PIGMRMSPPA WVELKDDRIE 650
TYVRTIQSTL GAEGKIQMVV CIIMGPRDDL YGAIKKLCCV QSPVPSQVVN 700
VRTIGQPTRL RSVAQKILLQ INCKLGGELW GVDIPLKQLM VIGMDVYHDP 750
SRGMRSVVGF VASINLTLTK WYSRVVFQMP HQEIVDSLKL CLVGSLKKFY 800
EVNHCLPEKI VVYRDGVSDG QLKTVANYEI PQLQKCFEAF ENYQPKMVVF 850
VVQKKISTNL YLAAPQNFVT PTPGTVVDHT ITSCEWVDFY LLAHHVRQGC 900
GIPTHYVCVL NTANLSPDHM QRLTFKLCHM YWNWPGTIRV PAPCKYAHKL 950
AFLSGHILHH EPAIQLCENL FFL 973
Length:973
Mass (Da):109,849
Last modified:June 1, 2002 - v1
Checksum:iC44398136B144CA0
GO
Isoform 2 (identifier: Q8TC59-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     887-922: Missing.

Show »
Length:937
Mass (Da):105,760
Checksum:i5888D266DD32416C
GO

Sequence cautioni

The sequence BAA91558.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAB55155.1 differs from that shown. Reason: Erroneous termination at position 421. Translated as Arg.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei887 – 92236Missing in isoform 2.
VSP_036664Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181Q → R in BAG61134. 1 Publication
Sequence conflicti581 – 5811I → T in BAF98721. 1 Publication
Sequence conflicti685 – 6851K → N in BAA91558. 1 Publication
Sequence conflicti720 – 7201Q → R in BAF98724. 1 Publication
Sequence conflicti887 – 8871V → G in BAF83727. 1 Publication
Sequence conflicti961 – 9611E → G in BAB55155. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB079367 mRNA. Translation: BAC81342.1.
HQ651229 mRNA. Translation: ADV17663.1.
AK001213 mRNA. Translation: BAA91558.1. Different initiation.
AK027497 mRNA. Translation: BAB55155.1. Sequence problems.
AK291038 mRNA. Translation: BAF83727.1.
AK292440 mRNA. Translation: BAF85129.1.
AK299068 mRNA. Translation: BAG61134.1.
AK315830 mRNA. Translation: BAF98721.1.
AK315833 mRNA. Translation: BAF98724.1.
BC025995 mRNA. Translation: AAH25995.1.
BC111751 mRNA. Translation: AAI11752.1.
CCDSiCCDS6029.1. [Q8TC59-1]
RefSeqiNP_001129193.1. NM_001135721.1. [Q8TC59-1]
NP_060538.2. NM_018068.3. [Q8TC59-1]
XP_005273607.1. XM_005273550.2. [Q8TC59-2]
UniGeneiHs.614809.

Genome annotation databases

EnsembliENST00000356766; ENSP00000349208; ENSG00000197181. [Q8TC59-1]
ENST00000454009; ENSP00000406956; ENSG00000197181. [Q8TC59-1]
ENST00000521356; ENSP00000428267; ENSG00000197181. [Q8TC59-2]
GeneIDi55124.
KEGGihsa:55124.
UCSCiuc003xbn.2. human. [Q8TC59-1]
uc011kzf.1. human. [Q8TC59-2]

Polymorphism databases

DMDMi74730558.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB079367 mRNA. Translation: BAC81342.1 .
HQ651229 mRNA. Translation: ADV17663.1 .
AK001213 mRNA. Translation: BAA91558.1 . Different initiation.
AK027497 mRNA. Translation: BAB55155.1 . Sequence problems.
AK291038 mRNA. Translation: BAF83727.1 .
AK292440 mRNA. Translation: BAF85129.1 .
AK299068 mRNA. Translation: BAG61134.1 .
AK315830 mRNA. Translation: BAF98721.1 .
AK315833 mRNA. Translation: BAF98724.1 .
BC025995 mRNA. Translation: AAH25995.1 .
BC111751 mRNA. Translation: AAI11752.1 .
CCDSi CCDS6029.1. [Q8TC59-1 ]
RefSeqi NP_001129193.1. NM_001135721.1. [Q8TC59-1 ]
NP_060538.2. NM_018068.3. [Q8TC59-1 ]
XP_005273607.1. XM_005273550.2. [Q8TC59-2 ]
UniGenei Hs.614809.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3O7X X-ray 2.92 A/B/C/D 387-525 [» ]
3QIR X-ray 2.45 A/B/C/D 386-533 [» ]
ProteinModelPortali Q8TC59.
SMRi Q8TC59. Positions 218-962.
ModBasei Search...

Protein-protein interaction databases

BioGridi 120431. 2 interactions.
STRINGi 9606.ENSP00000349208.

PTM databases

PhosphoSitei Q8TC59.

Polymorphism databases

DMDMi 74730558.

Proteomic databases

PaxDbi Q8TC59.
PRIDEi Q8TC59.

Protocols and materials databases

DNASUi 55124.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000356766 ; ENSP00000349208 ; ENSG00000197181 . [Q8TC59-1 ]
ENST00000454009 ; ENSP00000406956 ; ENSG00000197181 . [Q8TC59-1 ]
ENST00000521356 ; ENSP00000428267 ; ENSG00000197181 . [Q8TC59-2 ]
GeneIDi 55124.
KEGGi hsa:55124.
UCSCi uc003xbn.2. human. [Q8TC59-1 ]
uc011kzf.1. human. [Q8TC59-2 ]

Organism-specific databases

CTDi 55124.
GeneCardsi GC08P022132.
HGNCi HGNC:17644. PIWIL2.
HPAi HPA029345.
MIMi 610312. gene.
neXtProti NX_Q8TC59.
PharmGKBi PA38461.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG286051.
HOVERGENi HBG049411.
InParanoidi Q8TC59.
KOi K02156.
OMAi QELNWIK.
OrthoDBi EOG712TVQ.
PhylomeDBi Q8TC59.
TreeFami TF354206.

Miscellaneous databases

GenomeRNAii 55124.
NextBioi 58776.
PROi Q8TC59.
SOURCEi Search...

Gene expression databases

Bgeei Q8TC59.
CleanExi HS_PIWIL2.
Genevestigatori Q8TC59.

Family and domain databases

Gene3Di 3.30.420.10. 1 hit.
InterProi IPR003100. PAZ_dom.
IPR003165. Piwi.
IPR012337. RNaseH-like_dom.
[Graphical view ]
Pfami 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

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Identification of piwil2-like (PL2L106) protein in HeLa cells."
    Zhang K., Lu Y., Li C.
    Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  3. "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] (ISOFORMS 1 AND 2).
    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] (ISOFORM 1).
    Tissue: Testis.
  5. "Stem-cell protein Piwil2 is widely expressed in tumors and inhibits apoptosis through activation of Stat3/Bcl-XL pathway."
    Lee J.H., Schutte D., Wulf G., Fuzesi L., Radzun H.-J., Schweyer S., Engel W., Nayernia K.
    Hum. Mol. Genet. 15:201-211(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  6. "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 (2.92 ANGSTROMS) OF 387-525, RNA-BINDING.

Entry informationi

Entry nameiPIWL2_HUMAN
AccessioniPrimary (citable) accession number: Q8TC59
Secondary accession number(s): A8K4S3
, A8K8S5, B0AZN9, B0AZP2, B4DR22, E7ECA4, Q96SW6, Q9NW28
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: June 1, 2002
Last modified: July 9, 2014
This is version 101 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 8
    Human chromosome 8: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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