PIWL4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PIWL4_HUMAN
• UniProt AC: Q7Z3Z4
• Protein Name: Piwi-like protein 4
• Gene Name: PIWIL4
• Organism: Homo sapiens (Human).
• Sequence Length: 852
• Subcellular Localization: Nucleus . Cytoplasm . Probable component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. PIWIL2/MILI is required for nuclear localization (By similarity).
• Protein Description: Plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity (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 governs the methylation and subsequent repression of transposons (By similarity). 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 (By similarity). Associates with secondary piRNAs antisense and PIWIL2/MILI is required for such association (By similarity). The piRNA process acts upstream of known mediators of DNA methylation (By similarity). Does not show endonuclease activity (By similarity). Plays a key role in the piRNA amplification loop, also named ping-pong amplification cycle, by acting as a 'slicer-incompetent' component that loads cleaved piRNAs from the 'slicer-competent' component PIWIL2 and target them on genomic transposon loci in the nucleus (By similarity). May be involved in the chromatin-modifying pathway by inducing 'Lys-9' methylation of histone H3 at some loci. [PubMed: 17544373]
• Protein Sequence: MSGRARVKARGIARSPSATEVGRIQASPLPRSVDLSNNEASSSNGFLGTSRISTNDKYGISSGDAGSTFMERGVKNKQDFMDLSICTREKLAHVRNCKTGSSGIPVKLVTNLFNLDFPQDWQLYQYHVTYIPDLASRRLRIALLYSHSELSNKAKAFDGAILFLSQKLEEKVTELSSETQRGETIKMTITLKRELPSSSPVCIQVFNIIFRKILKKLSMYQIGRNFYNPSEPMEIPQHKLSLWPGFAISVSYFERKLLFSADVSYKVLRNETVLEFMTALCQRTGLSCFTQTCEKQLIGLIVLTRYNNRTYSIDDIDWSVKPTHTFQKRDGTEITYVDYYKQQYDITVSDLNQPMLVSLLKKKRNDNSEAQLAHLIPELCFLTGLTDQATSDFQLMKAVAEKTRLSPSGRQQRLARLVDNIQRNTNARFELETWGLHFGSQISLTGRIVPSEKILMQDHICQPVSAADWSKDIRTCKILNAQSLNTWLILCSDRTEYVAESFLNCLRRVAGSMGFNVDYPKIIKVQENPAAFVRAIQQYVDPDVQLVMCILPSNQKTYYDSIKKYLSSDCPVPSQCVLARTLNKQGMMMSIATKIAMQMTCKLGGELWAVEIPLKSLMVVGIDVCKDALSKDVMVVGCVASVNPRITRWFSRCILQRTMTDVADCLKVFMTGALNKWYKYNHDLPARIIVYRAGVGDGQLKTLIEYEVPQLLSSVAESSSNTSSRLSVIVVRKKCMPRFFTEMNRTVQNPPLGTVVDSEATRNEWYDFYLISQVACRGTVSPTYYNVIYDDNGLKPDHMQRLTFKLCHLYYNWPGIVSVPAPCQYAHKLTFLVAQSIHKEPSLELANHLFYL

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
17	Phosphorylation	RGIARSPSATEVGRI CCCCCCCCCCCCCEE	49.41	20393185
27	Phosphorylation	EVGRIQASPLPRSVD CCCEEECCCCCCEEE	15.59	24719451
61	Phosphorylation	TNDKYGISSGDAGST CCCCCCCCCCCCCHH	24.73	-
62	Phosphorylation	NDKYGISSGDAGSTF CCCCCCCCCCCCHHH	38.48	-
84	Phosphorylation	KQDFMDLSICTREKL HHHCCCHHHHCHHHH	16.02	-
102	Phosphorylation	RNCKTGSSGIPVKLV HCCCCCCCCCCCEEE	41.93	24719451
252	Phosphorylation	GFAISVSYFERKLLF CEEEEEEHHHHHHHC	13.80	-
260	Phosphorylation	FERKLLFSADVSYKV HHHHHHCCCCCHHHH	24.43	30576142
264	Phosphorylation	LLFSADVSYKVLRNE HHCCCCCHHHHHCCH	21.56	30576142
265	Phosphorylation	LFSADVSYKVLRNET HCCCCCHHHHHCCHH	12.64	30576142
266	Ubiquitination	FSADVSYKVLRNETV CCCCCHHHHHCCHHH	27.56	-
306	Phosphorylation	GLIVLTRYNNRTYSI EEEEEEEECCCEEEE	16.14	26074081
310	Phosphorylation	LTRYNNRTYSIDDID EEEECCCEEEECCCC	24.60	26074081
311	Phosphorylation	TRYNNRTYSIDDIDW EEECCCEEEECCCCC	10.61	26074081
319	Phosphorylation	SIDDIDWSVKPTHTF EECCCCCCCCCCCEE	19.26	26074081
339	Phosphorylation	TEITYVDYYKQQYDI CEEEEEEEEECEEEE	11.52	-
340	Phosphorylation	EITYVDYYKQQYDIT EEEEEEEEECEEEEE	9.62	-
358	Phosphorylation	LNQPMLVSLLKKKRN CCCHHHHHHHHHHCC	24.83	24719451
443	Phosphorylation	LHFGSQISLTGRIVP EECCCEEEECCEECC	16.55	24945436
667	Acetylation	TDVADCLKVFMTGAL CHHHHHHHHHHHHHH	39.49	7364291
676	Ubiquitination	FMTGALNKWYKYNHD HHHHHHHHHHHCCCC	53.39	21890473
676 (in isoform 1)	Ubiquitination	-	53.39	21890473
679	Ubiquitination	GALNKWYKYNHDLPA HHHHHHHHCCCCCCC	38.16	21890473
679 (in isoform 1)	Ubiquitination	-	38.16	21890473
722	Phosphorylation	VAESSSNTSSRLSVI HHHCCCCCCCCEEEE	29.99	22210691
727	Phosphorylation	SNTSSRLSVIVVRKK CCCCCCEEEEEEECC	14.53	22210691

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of PIWL4_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PIWL4_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of PIWL4_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of PIWL4_HUMAN !!

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.