EXD1_HUMAN - dbPTM
EXD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EXD1_HUMAN
UniProt AC Q8NHP7
Protein Name piRNA biogenesis protein EXD1 {ECO:0000305}
Gene Name EXD1
Organism Homo sapiens (Human).
Sequence Length 514
Subcellular Localization Cytoplasm . Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis.
Protein Description RNA-binding component of the PET complex, a multiprotein complex required for the processing of piRNAs during spermatogenesis. The piRNA metabolic process 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 transposable elements, preventing their mobilization, which is essential for the germline integrity (By similarity). The PET complex is required during the secondary piRNAs metabolic process for the PIWIL2 slicing-triggered loading of PIWIL4 piRNAs. In the PET complex, EXD1 probably acts as an RNA adapter. EXD1 is an inactive exonuclease (By similarity)..
Protein Sequence MEDSEFLAYVELLDEVEQGSVRAKASSVSLHAERTWMEKMKVEDLNVCEPASPAPEAPATSLLNDLKYSPSEEEEVTYTVINQFQQKFGAAILHIKKQNVLSVAAEGANVCRHGKLCWLQVATNCRVYLFDIFLLGSRAFHNGLQMILEDKRILKVIHDCRWLSDCLSHQYGILLNNVFDTQVADVLQFSMETGGYLPNCITTLQESLIKHLQVAPKYLSFLEKRQKLIQENPEVWFIRPVSPSLLKILALEATYLLPLRLALLDEMMSDLTTLVDGYLNTYREGSADRLGGTEPTCMELPEELLQLKDFQKQRREKAAREYRVNAQGLLIRTVLQPKKLVTETAGKEEKVKGFLFGKNFRIDKAPSFTSQDFHGDVNLLKEESLNKQATNPQHLPPTEEGETSEDSSNKLICTKSKGSEDQRITQKEHFMTPKHEFQASLSLKEETEQLLMVENKEDLKCTKQAVSMSSFPQETRVSPSDTFYPIRKTVVSTLPPCPALEKIDSWISPFLNLP
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
79UbiquitinationEEEEVTYTVINQFQQ
CCHHHHHHHHHHHHH
12.9220639865
82UbiquitinationEVTYTVINQFQQKFG
HHHHHHHHHHHHHHC
32.0722817900
102PhosphorylationIKKQNVLSVAAEGAN
EHHCCEEEEEECCCC
12.8626270265
188UbiquitinationTQVADVLQFSMETGG
HHHHHHHHHHHHCCC
28.3720639865
191UbiquitinationADVLQFSMETGGYLP
HHHHHHHHHCCCCCC
5.8822817900
207PhosphorylationCITTLQESLIKHLQV
HHHHHHHHHHHHHHH
23.5724719451
224UbiquitinationKYLSFLEKRQKLIQE
HHHHHHHHHHHHHHH
63.3820639865
227UbiquitinationSFLEKRQKLIQENPE
HHHHHHHHHHHHCCC
52.1422817900
228UbiquitinationFLEKRQKLIQENPEV
HHHHHHHHHHHCCCC
3.5520639865
231UbiquitinationKRQKLIQENPEVWFI
HHHHHHHHCCCCEEE
68.6922817900
244PhosphorylationFIRPVSPSLLKILAL
EEEECCHHHHHHHHH
38.5424719451
247UbiquitinationPVSPSLLKILALEAT
ECCHHHHHHHHHHHH
40.7520639865
250UbiquitinationPSLLKILALEATYLL
HHHHHHHHHHHHHHH
13.5622817900
259UbiquitinationEATYLLPLRLALLDE
HHHHHHHHHHHHHHH
7.6620639865
262UbiquitinationYLLPLRLALLDEMMS
HHHHHHHHHHHHHHH
10.3122817900
272PhosphorylationDEMMSDLTTLVDGYL
HHHHHHHHHHHHHHH
24.07-
282UbiquitinationVDGYLNTYREGSADR
HHHHHHHHCCCCCCC
12.9520639865
285UbiquitinationYLNTYREGSADRLGG
HHHHHCCCCCCCCCC
21.0922817900
407PhosphorylationEGETSEDSSNKLICT
CCCCCCCCCCCEEEE
31.5924260401
440PhosphorylationPKHEFQASLSLKEET
CHHHHHHCCCCHHHH
14.0124719451
442PhosphorylationHEFQASLSLKEETEQ
HHHHHCCCCHHHHHH
34.5924719451
456AcetylationQLLMVENKEDLKCTK
HHEEECCHHHHCCCC
38.8221466224
460AcetylationVENKEDLKCTKQAVS
ECCHHHHCCCCHHHH
52.7821466224
462PhosphorylationNKEDLKCTKQAVSMS
CHHHHCCCCHHHHCC
25.30-
470PhosphorylationKQAVSMSSFPQETRV
CHHHHCCCCCCCCCC
32.1028509920
475PhosphorylationMSSFPQETRVSPSDT
CCCCCCCCCCCCCCC
30.99-
478PhosphorylationFPQETRVSPSDTFYP
CCCCCCCCCCCCCCE
18.5230242111
480PhosphorylationQETRVSPSDTFYPIR
CCCCCCCCCCCCEEH
41.6030242111
482PhosphorylationTRVSPSDTFYPIRKT
CCCCCCCCCCEEHHH
29.4330242111
484PhosphorylationVSPSDTFYPIRKTVV
CCCCCCCCEEHHHHH
10.3930242111
514AcetylationISPFLNLP-------
HHHHHCCC-------
40.88-
518AcetylationLNLP-----------
HCCC-----------
-

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 EXD1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EXD1_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 EXD1_HUMAN !!

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

Oops, there are no PPI records of EXD1_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.
Regulatory Network of EXD1_HUMAN

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Related Literatures of Post-Translational Modification

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