UniProt ID | ATAD3_MOUSE | |
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UniProt AC | Q925I1 | |
Protein Name | ATPase family AAA domain-containing protein 3 | |
Gene Name | Atad3 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 591 | |
Subcellular Localization |
Mitochondrion inner membrane Single-pass membrane protein. Mitochondrion matrix, mitochondrion nucleoid. In the mitochondrial inner membrane, enriched in sites with the potential to form contacts with the outer membrane. The N-terminal domain intera |
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Protein Description | Essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organism and cellular level. May play an important role in mitochondrial protein synthesis. May also participate in mitochondrial DNA replication. May bind to mitochondrial DNA D-loops and contribute to nucleoid stability. Required for enhanced channeling of cholesterol for hormone-dependent steroidogenesis (By similarity).. | |
Protein Sequence | MSWLFGIKGPKGEGTGPPLPLPPAQPGAEGGGDRGAGDRPSPKDKWSNFDPTGLERAAKAARELEHSRHAKEALSLAQMQEQTLQLEQQSKLKEYEAAVEQLKSEQIRVQAEERRKTLTEETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAIRRATVEREMELRHKNEMLRVEAEARARAKADRENADIIREQIRLKAAEHRQTILESIRTAGTLLGEGFRAFVTDWDKVTATVAGLTLLAVGVYSAKNATSVAGRYIEARLGKPSLVRETSRISVLEALRHPIQVSRRLVSRPQDALEGVILSPSLEARVRDIAIATRNTKKNKSLYRNVLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAMHKVFDWASTSRRGLLLFVDEADAFLRKRATEKISEDLRATLNAFLHRTGQHSSKFMLVLASNQPEQFDWAINDRIDEMVCFALPQREERERLVRMYFDKYVLKPATEGKQRLKVAQFDYGKKCSEVAQLTEGMSGREIAQLAVAWQAMAYSSEDGVLTEAMMDARVQDAVQQHQQKMQWLKVERPDSQTNKPPHPSLLSC | |
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 |
---|---|---|---|---|---|
2 | Acetylation | ------MSWLFGIKG ------CCCCCCCCC | 32.27 | - | |
8 | Succinylation | MSWLFGIKGPKGEGT CCCCCCCCCCCCCCC | 70.33 | 23954790 | |
41 | Phosphorylation | RGAGDRPSPKDKWSN CCCCCCCCCCCCCCC | 45.54 | 22817900 | |
45 | Malonylation | DRPSPKDKWSNFDPT CCCCCCCCCCCCCHH | 59.66 | 26320211 | |
71 | Acetylation | LEHSRHAKEALSLAQ HHHHHHHHHHHHHHH | 37.08 | 7969809 | |
134 | Acetylation | ARAQYQDKLARQRYE HHHHHHHHHHHHHHH | 28.64 | 23201123 | |
134 | Malonylation | ARAQYQDKLARQRYE HHHHHHHHHHHHHHH | 28.64 | 26320211 | |
197 | Malonylation | AEARARAKADRENAD HHHHHHHHHHHHHHH | 45.31 | 26320211 | |
320 | Phosphorylation | ALEGVILSPSLEARV HHCCCEECHHHHHHH | 11.00 | 26824392 | |
322 | Phosphorylation | EGVILSPSLEARVRD CCCEECHHHHHHHHH | 35.15 | 28066266 | |
358 | Phosphorylation | GPPGTGKTLFAKKLA CCCCCCHHHHHHHHH | 28.58 | 21454597 | |
362 | Acetylation | TGKTLFAKKLALHSG CCHHHHHHHHHHCCC | 40.77 | 23201123 | |
372 | Phosphorylation | ALHSGMDYAIMTGGD HHCCCCCEEEECCCC | 6.80 | 21149613 | |
376 | Phosphorylation | GMDYAIMTGGDVAPM CCCEEEECCCCCCCC | 31.72 | 21149613 | |
393 | Acetylation | EGVTAMHKVFDWAST CCCHHHHHHHCHHHC | 31.35 | 23201123 | |
423 | Glutarylation | LRKRATEKISEDLRA HHHHHHHHHCHHHHH | 47.37 | 24703693 | |
423 | Acetylation | LRKRATEKISEDLRA HHHHHHHHHCHHHHH | 47.37 | 23806337 | |
423 | Succinylation | LRKRATEKISEDLRA HHHHHHHHHCHHHHH | 47.37 | 23806337 | |
425 | Phosphorylation | KRATEKISEDLRATL HHHHHHHCHHHHHHH | 35.80 | 25159016 | |
471 | S-palmitoylation | DRIDEMVCFALPQRE HCCCHHHHHCCCCHH | 1.27 | 28526873 | |
490 | Succinylation | LVRMYFDKYVLKPAT HHHHHHHHHCCCCCC | 27.62 | - | |
490 | Succinylation | LVRMYFDKYVLKPAT HHHHHHHHHCCCCCC | 27.62 | 23806337 | |
490 | Acetylation | LVRMYFDKYVLKPAT HHHHHHHHHCCCCCC | 27.62 | 23576753 | |
494 | Acetylation | YFDKYVLKPATEGKQ HHHHHCCCCCCCCCH | 23.67 | 23576753 | |
494 | Succinylation | YFDKYVLKPATEGKQ HHHHHCCCCCCCCCH | 23.67 | 24315375 | |
512 | Acetylation | VAQFDYGKKCSEVAQ EEEECCCCCHHHHHH | 44.36 | 23576753 | |
512 | Succinylation | VAQFDYGKKCSEVAQ EEEECCCCCHHHHHH | 44.36 | 23954790 | |
513 | Acetylation | AQFDYGKKCSEVAQL EEECCCCCHHHHHHH | 38.33 | 2390999 | |
567 | Acetylation | AVQQHQQKMQWLKVE HHHHHHHHCCCCEEC | 26.87 | 23201123 | |
578 | Phosphorylation | LKVERPDSQTNKPPH CEECCCCCCCCCCCC | 41.40 | - | |
580 | Phosphorylation | VERPDSQTNKPPHPS ECCCCCCCCCCCCCH | 49.51 | - | |
587 | Phosphorylation | TNKPPHPSLLSC--- CCCCCCCHHCCC--- | 38.62 | 29472430 | |
590 | Phosphorylation | PPHPSLLSC------ CCCCHHCCC------ | 24.07 | 29472430 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of ATAD3_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ATAD3_MOUSE !! |
* 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 ATAD3_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of ATAD3_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-490 AND LYS-512, AND MASSSPECTROMETRY. |