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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
79 | Ubiquitination | EEEEVTYTVINQFQQ CCHHHHHHHHHHHHH | 12.92 | 20639865 | |
82 | Ubiquitination | EVTYTVINQFQQKFG HHHHHHHHHHHHHHC | 32.07 | 22817900 | |
102 | Phosphorylation | IKKQNVLSVAAEGAN EHHCCEEEEEECCCC | 12.86 | 26270265 | |
188 | Ubiquitination | TQVADVLQFSMETGG HHHHHHHHHHHHCCC | 28.37 | 20639865 | |
191 | Ubiquitination | ADVLQFSMETGGYLP HHHHHHHHHCCCCCC | 5.88 | 22817900 | |
207 | Phosphorylation | CITTLQESLIKHLQV HHHHHHHHHHHHHHH | 23.57 | 24719451 | |
224 | Ubiquitination | KYLSFLEKRQKLIQE HHHHHHHHHHHHHHH | 63.38 | 20639865 | |
227 | Ubiquitination | SFLEKRQKLIQENPE HHHHHHHHHHHHCCC | 52.14 | 22817900 | |
228 | Ubiquitination | FLEKRQKLIQENPEV HHHHHHHHHHHCCCC | 3.55 | 20639865 | |
231 | Ubiquitination | KRQKLIQENPEVWFI HHHHHHHHCCCCEEE | 68.69 | 22817900 | |
244 | Phosphorylation | FIRPVSPSLLKILAL EEEECCHHHHHHHHH | 38.54 | 24719451 | |
247 | Ubiquitination | PVSPSLLKILALEAT ECCHHHHHHHHHHHH | 40.75 | 20639865 | |
250 | Ubiquitination | PSLLKILALEATYLL HHHHHHHHHHHHHHH | 13.56 | 22817900 | |
259 | Ubiquitination | EATYLLPLRLALLDE HHHHHHHHHHHHHHH | 7.66 | 20639865 | |
262 | Ubiquitination | YLLPLRLALLDEMMS HHHHHHHHHHHHHHH | 10.31 | 22817900 | |
272 | Phosphorylation | DEMMSDLTTLVDGYL HHHHHHHHHHHHHHH | 24.07 | - | |
282 | Ubiquitination | VDGYLNTYREGSADR HHHHHHHHCCCCCCC | 12.95 | 20639865 | |
285 | Ubiquitination | YLNTYREGSADRLGG HHHHHCCCCCCCCCC | 21.09 | 22817900 | |
407 | Phosphorylation | EGETSEDSSNKLICT CCCCCCCCCCCEEEE | 31.59 | 24260401 | |
440 | Phosphorylation | PKHEFQASLSLKEET CHHHHHHCCCCHHHH | 14.01 | 24719451 | |
442 | Phosphorylation | HEFQASLSLKEETEQ HHHHHCCCCHHHHHH | 34.59 | 24719451 | |
456 | Acetylation | QLLMVENKEDLKCTK HHEEECCHHHHCCCC | 38.82 | 21466224 | |
460 | Acetylation | VENKEDLKCTKQAVS ECCHHHHCCCCHHHH | 52.78 | 21466224 | |
462 | Phosphorylation | NKEDLKCTKQAVSMS CHHHHCCCCHHHHCC | 25.30 | - | |
470 | Phosphorylation | KQAVSMSSFPQETRV CHHHHCCCCCCCCCC | 32.10 | 28509920 | |
475 | Phosphorylation | MSSFPQETRVSPSDT CCCCCCCCCCCCCCC | 30.99 | - | |
478 | Phosphorylation | FPQETRVSPSDTFYP CCCCCCCCCCCCCCE | 18.52 | 30242111 | |
480 | Phosphorylation | QETRVSPSDTFYPIR CCCCCCCCCCCCEEH | 41.60 | 30242111 | |
482 | Phosphorylation | TRVSPSDTFYPIRKT CCCCCCCCCCEEHHH | 29.43 | 30242111 | |
484 | Phosphorylation | VSPSDTFYPIRKTVV CCCCCCCCEEHHHHH | 10.39 | 30242111 | |
514 | Acetylation | ISPFLNLP------- HHHHHCCC------- | 40.88 | - | |
518 | Acetylation | LNLP----------- HCCC----------- | - |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of EXD1_HUMAN !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of EXD1_HUMAN !! |
Kegg Disease | ||||||
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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. |
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