UniProt ID | SPG7_MOUSE | |
---|---|---|
UniProt AC | Q3ULF4 | |
Protein Name | Paraplegin {ECO:0000303|PubMed:14722615} | |
Gene Name | Spg7 {ECO:0000312|MGI:MGI:2385906} | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 781 | |
Subcellular Localization |
Mitochondrion inner membrane Multi-pass membrane protein . |
|
Protein Description | ATP-dependent zinc metalloprotease. Plays a role in the formation and regulation of the mitochondrial permeability transition pore (mPTP) and its proteolytic activity is dispensable for this function (By similarity).. | |
Protein Sequence | MAAALLLLRGLRPGPEPRPRRLWGLLSGRGPGLSSGAGARRPYAARGTPVGPAAAGGHAPQSLLLRILTPSFEGISGLLLKQHIVPNAVRLWPLSGSTLYFNTSRMKQKNKDNDKPKGKTPEDDEEEKRRKEREDQMYRERLRTLFIIALVMSLLNSLSTSGGSISWADFVNEMLAKGEVQRVQVVPESDVVEVYLHPGAVVFGRPRLALMYRMQVANIDKFEEKLRAAEDELNIESKDRIPVSYKRTGFFGNALYALGMTAVGLAILWYVFRLAGMTGREGGFSAFNQLKMARFTIVDGKTGKGVSFQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGFSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADVLDNALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSSFYSQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTFNFEYAVERVIAGTAKKSKILSKEEQRVVAFHESGHALVGWLLEHTEAVMKVSIAPRTNAALGFSQMLPRDQYLFTKEQLFERMCMALGGRAAEAISFSRVTSGAQDDLRKVTRIAYSMVKQFGMAPSIGPVSFPEAQEGLMGIGRRPFSQGLQQMMDHEAKLLVAKAYRHTEKVLLDNLDKLQALANALLEKEVINYEDIEALIGPPPHGPKKMIAPQKWIDAEKERQASGEEEAPAP | |
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 |
---|---|---|---|---|---|
248 | Phosphorylation | IPVSYKRTGFFGNAL CCCCEECCCCHHHHH | 33.90 | 28285833 | |
270 | Phosphorylation | VGLAILWYVFRLAGM HHHHHHHHHHHHHCC | 6.05 | 28285833 | |
505 | Nitrated tyrosine | LTQPSSFYSQRLAEL CCCCCCHHHHHHHHH | 13.07 | - | |
505 | Nitration | LTQPSSFYSQRLAEL CCCCCCHHHHHHHHH | 13.07 | 16800626 | |
505 | Nitration | LTQPSSFYSQRLAEL CCCCCCHHHHHHHHH | 13.07 | 16800626 | |
517 | Phosphorylation | AELTPGFSGADIANI HHHCCCCCHHHHHHH | 38.70 | - | |
607 | Phosphorylation | TNAALGFSQMLPRDQ CCCCCCHHHCCCHHH | 16.94 | - | |
619 | Acetylation | RDQYLFTKEQLFERM HHHCCCCHHHHHHHH | 35.81 | 23954790 | |
619 | Succinylation | RDQYLFTKEQLFERM HHHCCCCHHHHHHHH | 35.81 | 23954790 | |
639 | Phosphorylation | GRAAEAISFSRVTSG CHHHHHHHHHHHCCC | 24.98 | 26160508 | |
641 | Phosphorylation | AAEAISFSRVTSGAQ HHHHHHHHHHCCCCH | 21.03 | 25266776 | |
709 | Acetylation | EAKLLVAKAYRHTEK HHHHHHHHHHHHCHH | 38.17 | 23201123 | |
716 | Acetylation | KAYRHTEKVLLDNLD HHHHHCHHHHHCCHH | 39.06 | 23201123 | |
762 | Ubiquitination | KKMIAPQKWIDAEKE CCCCCCHHHCCHHHH | 45.09 | - | |
768 | Ubiquitination | QKWIDAEKERQASGE HHHCCHHHHHHHCCC | 60.97 | - |
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 SPG7_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SPG7_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 SPG7_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of SPG7_MOUSE !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...
Nitration | |
Reference | PubMed |
"Endogenously nitrated proteins in mouse brain: links toneurodegenerative disease."; Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,Squier T.C., Bigelow D.J.; Biochemistry 45:8009-8022(2006). Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-505, AND MASS SPECTROMETRY. |