PIWL2_HUMAN - dbPTM
PIWL2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PIWL2_HUMAN
UniProt AC Q8TC59
Protein Name Piwi-like protein 2
Gene Name PIWIL2
Organism Homo sapiens (Human).
Sequence Length 973
Subcellular Localization Cytoplasm . 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.
Protein Description Endoribonuclease that plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity (By similarity). Plays an essential role in meiotic differentiation of spermatocytes, germ cell differentiation and in self-renewal of spermatogonial stem cells (By similarity). 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 govern the methylation and subsequent repression of transposons (By similarity). During piRNA biosynthesis, plays a key role in the piRNA amplification loop, also named ping-pong amplification cycle, by acting as a 'slicer-competent' piRNA endoribonuclease that cleaves primary piRNAs, which are then loaded onto 'slicer-incompetent' PIWIL4 (By similarity). PIWIL2 slicing produces a pre-miRNA intermediate, which is then processed in mature piRNAs, and as well as a 16 nucleotide by-product that is degraded (By similarity). Required for PIWIL4/MIWI2 nuclear localization and association with secondary piRNAs antisense (By similarity). Besides their function in transposable elements repression, piRNAs are probably involved in other processes during meiosis such as translation regulation (By similarity). Indirectly modulates expression of genes such as PDGFRB, SLC2A1, ITGA6, GJA7, THY1, CD9 and STRA8 (By similarity). When overexpressed, acts as an oncogene by inhibition of apoptosis and promotion of proliferation in tumors. [PubMed: 16377660]
Protein Sequence MDPFRPSFRGQSPIHPSQCQAVRMPGCWPQASKPLDPALGRGAPAGRGHVFGKPEEPSTQRGPAQRESVGLVSMFRGLGIETVSKTPLKREMLPSGRGILGRGLSANLVRKDREELSPTFWDPKVLAAGDSKMAETSVGWSRTLGRGSSDASLLPLGRAAGGISREVDKPPCTFSTPSRGPPQLSSPPALPQSPLHSPDRPLVLTVEHKEKELIVKQGSKGTPQSLGLNLVKIQCHNEAVYQYHVTFSPNVECKSMRFGMLKDHQAVTGNVTAFDGSILYLPVKLQQVLELKSQRKTDSAEISIKIQMTKILEPCSDLCIPFYNVVFRRVMKLLDMKLVGRNFYDPTSAMVLQQHRLQIWPGYAASIRRTDGGLFLLADVSHKVIRNDCVLDVMHAIYQQNKEHFQDECTKLLVGNIVITRYNNRTYRIDDVDWNKTPKDSFTMSDGKEITFLEYYSKNYGITVKEEDQPLLIHRPSERQDNHGMLLKGEILLLPELSFMTGIPEKMKKDFRAMKDLAQQINLSPKQHHSALECLLQRIAKNEAATNELMRWGLRLQKDVHKIEGRVLPMERINLKNTSFITSQELNWVKEVTRDPSILTIPMHFWALFYPKRAMDQARELVNMLEKIAGPIGMRMSPPAWVELKDDRIETYVRTIQSTLGAEGKIQMVVCIIMGPRDDLYGAIKKLCCVQSPVPSQVVNVRTIGQPTRLRSVAQKILLQINCKLGGELWGVDIPLKQLMVIGMDVYHDPSRGMRSVVGFVASINLTLTKWYSRVVFQMPHQEIVDSLKLCLVGSLKKFYEVNHCLPEKIVVYRDGVSDGQLKTVANYEIPQLQKCFEAFENYQPKMVVFVVQKKISTNLYLAAPQNFVTPTPGTVVDHTITSCEWVDFYLLAHHVRQGCGIPTHYVCVLNTANLSPDHMQRLTFKLCHMYWNWPGTIRVPAPCKYAHKLAFLSGHILHHEPAIQLCENLFFL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
32PhosphorylationPGCWPQASKPLDPAL
CCCCCCCCCCCCHHC
29.5624719451
47Symmetric dimethylarginineGRGAPAGRGHVFGKP
CCCCCCCCCCCCCCC
33.86-
47MethylationGRGAPAGRGHVFGKP
CCCCCCCCCCCCCCC
33.86-
76Symmetric dimethylarginineVGLVSMFRGLGIETV
HHHHHHHCCCCCEEE
30.68-
76MethylationVGLVSMFRGLGIETV
HHHHHHHCCCCCEEE
30.6819719617
97Symmetric dimethylarginineREMLPSGRGILGRGL
HHHCCCCCCCCCCCC
33.06-
97MethylationREMLPSGRGILGRGL
HHHCCCCCCCCCCCC
33.06-
102Symmetric dimethylarginineSGRGILGRGLSANLV
CCCCCCCCCCHHHHC
39.16-
102MethylationSGRGILGRGLSANLV
CCCCCCCCCCHHHHC
39.16-
105PhosphorylationGILGRGLSANLVRKD
CCCCCCCHHHHCCCC
20.2424732914
146MethylationGWSRTLGRGSSDASL
CCCCCCCCCCCCHHH
44.9530760677
148PhosphorylationSRTLGRGSSDASLLP
CCCCCCCCCCHHHHH
24.5522468782
152PhosphorylationGRGSSDASLLPLGRA
CCCCCCHHHHHHHHH
35.1122468782
158MethylationASLLPLGRAAGGISR
HHHHHHHHHCCCCCC
29.0130760683
164PhosphorylationGRAAGGISREVDKPP
HHHCCCCCCCCCCCC
26.1822468782
165MethylationRAAGGISREVDKPPC
HHCCCCCCCCCCCCC
46.14-
165Symmetric dimethylarginineRAAGGISREVDKPPC
HHCCCCCCCCCCCCC
46.14-
222PhosphorylationVKQGSKGTPQSLGLN
EECCCCCCCCCCCCE
23.14-
293PhosphorylationQQVLELKSQRKTDSA
HHHHHHHHCCCCCCC
48.0929052541
297PhosphorylationELKSQRKTDSAEISI
HHHHCCCCCCCEEEE
37.0629052541
299PhosphorylationKSQRKTDSAEISIKI
HHCCCCCCCEEEEEE
32.7929052541
303PhosphorylationKTDSAEISIKIQMTK
CCCCCEEEEEEEHHH
14.88-
309PhosphorylationISIKIQMTKILEPCS
EEEEEEHHHHCCCCC
9.88-
316PhosphorylationTKILEPCSDLCIPFY
HHHCCCCCHHHHHHH
44.31-
422PhosphorylationGNIVITRYNNRTYRI
CCEEEEEECCCEEEE
14.2428509920
426PhosphorylationITRYNNRTYRIDDVD
EEEECCCEEEECCCC
21.1928509920
460PhosphorylationLEYYSKNYGITVKEE
EEEHHHHCCCEECCC
17.4027135362
463PhosphorylationYSKNYGITVKEEDQP
HHHHCCCEECCCCCC
22.5927135362
551Symmetric dimethylarginineAATNELMRWGLRLQK
HHHHHHHHHHHHHHH
36.61-
551MethylationAATNELMRWGLRLQK
HHHHHHHHHHHHHHH
36.61-
637PhosphorylationGPIGMRMSPPAWVEL
CCCCCCCCCCCEEEE
19.84-
651PhosphorylationLKDDRIETYVRTIQS
ECCCHHHHHHHHHHH
25.5822461510
652PhosphorylationKDDRIETYVRTIQST
CCCHHHHHHHHHHHH
3.8322461510
772PhosphorylationNLTLTKWYSRVVFQM
EEEEHHHHHHEEECC
6.53-
931PhosphorylationTFKLCHMYWNWPGTI
HHHHHCHHCCCCCCE
3.3530576142

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of PIWL2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PIWL2_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PIWL2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HS90A_HUMANHSP90AA1physical
22848678

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PIWL2_HUMAN

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Related Literatures of Post-Translational Modification

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