PIWL1_HUMAN - dbPTM
PIWL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PIWL1_HUMAN
UniProt AC Q96J94
Protein Name Piwi-like protein 1
Gene Name PIWIL1
Organism Homo sapiens (Human).
Sequence Length 861
Subcellular Localization Cytoplasm . 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.
Protein Description Endoribonuclease that plays a central role in postnatal germ cells 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. Strongly prefers a uridine in the first position of their guide (g1U preference, also named 1U-bias). Not involved in the piRNA amplification loop, also named ping-pong amplification cycle. Acts as an endoribonuclease that cleaves transposon messenger RNAs. 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. Required to sequester RNF8 in the cytoplasm until late spermatogenesis; RNF8 being released upon ubiquitination and degradation of PIWIL1.; Isoform 3: May be a negative developmental regulator. [PubMed: 12037681]
Protein Sequence MTGRARARARGRARGQETAQLVGSTASQQPGYIQPRPQPPPAEGELFGRGRQRGTAGGTAKSQGLQISAGFQELSLAERGGRRRDFHDLGVNTRQNLDHVKESKTGSSGIIVRLSTNHFRLTSRPQWALYQYHIDYNPLMEARRLRSALLFQHEDLIGKCHAFDGTILFLPKRLQQKVTEVFSKTRNGEDVRITITLTNELPPTSPTCLQFYNIIFRRLLKIMNLQQIGRNYYNPNDPIDIPSHRLVIWPGFTTSILQYENSIMLCTDVSHKVLRSETVLDFMFNFYHQTEEHKFQEQVSKELIGLVVLTKYNNKTYRVDDIDWDQNPKSTFKKADGSEVSFLEYYRKQYNQEITDLKQPVLVSQPKRRRGPGGTLPGPAMLIPELCYLTGLTDKMRNDFNVMKDLAVHTRLTPEQRQREVGRLIDYIHKNDNVQRELRDWGLSFDSNLLSFSGRILQTEKIHQGGKTFDYNPQFADWSKETRGAPLISVKPLDNWLLIYTRRNYEAANSLIQNLFKVTPAMGMQMRKAIMIEVDDRTEAYLRVLQQKVTADTQIVVCLLSSNRKDKYDAIKKYLCTDCPTPSQCVVARTLGKQQTVMAIATKIALQMNCKMGGELWRVDIPLKLVMIVGIDCYHDMTAGRRSIAGFVASINEGMTRWFSRCIFQDRGQELVDGLKVCLQAALRAWNSCNEYMPSRIIVYRDGVGDGQLKTLVNYEVPQFLDCLKSIGRGYNPRLTVIVVKKRVNTRFFAQSGGRLQNPLPGTVIDVEVTRPEWYDFFIVSQAVRSGSVSPTHYNVIYDNSGLKPDHIQRLTYKLCHIYYNWPGVIRVPAPCQYAHKLAFLVGQSIHREPNLSLSNRLYYL
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
14Symmetric dimethylarginineARARGRARGQETAQL
HHHHHHHCCHHHHHH
46.06-
14MethylationARARGRARGQETAQL
HHHHHHHCCHHHHHH
46.06-
18PhosphorylationGRARGQETAQLVGST
HHHCCHHHHHHHCCC
16.3029978859
24PhosphorylationETAQLVGSTASQQPG
HHHHHHCCCCCCCCC
17.2029978859
25PhosphorylationTAQLVGSTASQQPGY
HHHHHCCCCCCCCCC
25.1329978859
27PhosphorylationQLVGSTASQQPGYIQ
HHHCCCCCCCCCCCC
29.4529978859
32PhosphorylationTASQQPGYIQPRPQP
CCCCCCCCCCCCCCC
11.7629978859
49MethylationAEGELFGRGRQRGTA
CCCCCCCCCCCCCCC
29.77-
53MethylationLFGRGRQRGTAGGTA
CCCCCCCCCCCCCCC
42.97-
55PhosphorylationGRGRQRGTAGGTAKS
CCCCCCCCCCCCCHH
25.0722210691
107PhosphorylationVKESKTGSSGIIVRL
CHHCCCCCCCEEEEE
30.53-
122PhosphorylationSTNHFRLTSRPQWAL
ECCCEEECCCCCEEE
20.59-
123PhosphorylationTNHFRLTSRPQWALY
CCCEEECCCCCEEEE
46.70-
183PhosphorylationQKVTEVFSKTRNGED
HHHHHHHHHCCCCCE
37.9924505115
185PhosphorylationVTEVFSKTRNGEDVR
HHHHHHHCCCCCEEE
28.3324505115
338PhosphorylationTFKKADGSEVSFLEY
CCCCCCCCCCHHHHH
35.0624719451
370MethylationVSQPKRRRGPGGTLP
ECCCCCCCCCCCCCC
60.74-
388PhosphorylationMLIPELCYLTGLTDK
HHHHHHHHHHCCHHH
21.6628634298
390PhosphorylationIPELCYLTGLTDKMR
HHHHHHHHCCHHHHH
12.0428634298
393PhosphorylationLCYLTGLTDKMRNDF
HHHHHCCHHHHHCCC
34.6128634298
410PhosphorylationMKDLAVHTRLTPEQR
HHHHHHHHCCCHHHH
22.3030576142
413PhosphorylationLAVHTRLTPEQRQRE
HHHHHCCCHHHHHHH
22.8430576142
489PhosphorylationTRGAPLISVKPLDNW
CCCCCEEEEEECCCE
31.6024719451
517 (in isoform 3)Ubiquitination-48.6521906983
519PhosphorylationIQNLFKVTPAMGMQM
HHHHHHCCHHCCCCC
13.1124114839
550PhosphorylationRVLQQKVTADTQIVV
HHHHHHCCCCCEEEE
26.3329507054
561PhosphorylationQIVVCLLSSNRKDKY
EEEEEEECCCCCCHH
16.7829507054
562PhosphorylationIVVCLLSSNRKDKYD
EEEEEECCCCCCHHH
40.3929507054
564MethylationVCLLSSNRKDKYDAI
EEEECCCCCCHHHHH
50.96115388099
603UbiquitinationTVMAIATKIALQMNC
HHHHHHHHHHHHHCC
19.572190698
603 (in isoform 2)Ubiquitination-19.5721906983
603 (in isoform 1)Ubiquitination-19.5721906983
643PhosphorylationDMTAGRRSIAGFVAS
CCCCCCCCHHHHHHH
18.54-
650PhosphorylationSIAGFVASINEGMTR
CHHHHHHHHCHHHHH
22.20-
736PhosphorylationRGYNPRLTVIVVKKR
CCCCCCEEEEEEECC
14.96-
781PhosphorylationWYDFFIVSQAVRSGS
HEEEEEEEHHHHCCC
13.9626074081
786PhosphorylationIVSQAVRSGSVSPTH
EEEHHHHCCCCCCCE
28.9026074081
788PhosphorylationSQAVRSGSVSPTHYN
EHHHHCCCCCCCEEE
22.2226074081
790PhosphorylationAVRSGSVSPTHYNVI
HHHCCCCCCCEEEEE
26.2726074081
792PhosphorylationRSGSVSPTHYNVIYD
HCCCCCCCEEEEEEC
29.5026074081
794PhosphorylationGSVSPTHYNVIYDNS
CCCCCCEEEEEECCC
17.3826074081
798PhosphorylationPTHYNVIYDNSGLKP
CCEEEEEECCCCCCH
12.5626074081
801PhosphorylationYNVIYDNSGLKPDHI
EEEEECCCCCCHHHH
42.4726074081
860PhosphorylationSLSNRLYYL------
CCCCCEECC------
15.5518083107

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 PIWL1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PIWL1_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 PIWL1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DICER_HUMANDICER1physical
14749716
STMN1_HUMANSTMN1physical
26317901
TBA1B_HUMANTUBA1Bphysical
26317901
TBB3_HUMANTUBB3physical
26317901

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.
Regulatory Network of PIWL1_HUMAN

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Related Literatures of Post-Translational Modification

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