UniProt ID | ANXA7_MOUSE | |
---|---|---|
UniProt AC | Q07076 | |
Protein Name | Annexin A7 | |
Gene Name | Anxa7 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 463 | |
Subcellular Localization | ||
Protein Description | Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis.. | |
Protein Sequence | MSYPGYPPTGYPPFPGYPPAGQESSFPTAGQYPYPSGFPPMGGGAYPPAPSGGYPGAGGYPAPGGYPAPGGYPGALSPGGPPAYPGGQGFGAPPGGAGFSGYPQPPAQSYGGGPAQVPVPGGFPGGQMPSQYPGGQAPYPSQPASMTQGTQGTILPASNFDAMRDAEILRKAMKGFGTDEQAIVDVVSNRSNDQRQQIKAAFKTMYGKDLIKDLKSELSGNMEELILALFMPSTYYDAWSLRKAMQGAGTQERVLIEILCTRTNQEIRDIVRCYQLEFGRDLEKDIRSDTSGHFERLLVSMCQGNRDERQSVNHQMAQEDAQRLYQAGEGRLGTDESCFNMILATRSFPQLKATMEAYSRMANRDLLSSVSREFSGYVESGLKTILQCALNRPAFFAERLYYSMKGAGTDDSTLVRIVVTRSEIDLVQIKQMFTQMYQKTLSTMIASDTSGDYRKLLLAIVGQ | |
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 |
---|---|---|---|---|---|
174 | Ubiquitination | EILRKAMKGFGTDEQ HHHHHHHCCCCCCHH | 56.82 | - | |
203 | Acetylation | QQIKAAFKTMYGKDL HHHHHHHHHHHCHHH | 27.88 | 22826441 | |
203 | Ubiquitination | QQIKAAFKTMYGKDL HHHHHHHHHHHCHHH | 27.88 | - | |
208 | Acetylation | AFKTMYGKDLIKDLK HHHHHHCHHHHHHHH | 31.69 | 22826441 | |
212 | Malonylation | MYGKDLIKDLKSELS HHCHHHHHHHHHHHC | 65.39 | 26320211 | |
212 | Ubiquitination | MYGKDLIKDLKSELS HHCHHHHHHHHHHHC | 65.39 | - | |
250 | Phosphorylation | KAMQGAGTQERVLIE HHHCCCCCCHHHHHH | 27.07 | 30635358 | |
260 | Glutathionylation | RVLIEILCTRTNQEI HHHHHHHHCCCCHHH | 2.73 | 24333276 | |
284 | Acetylation | EFGRDLEKDIRSDTS CCCCCHHHHHHCCCC | 66.79 | 22826441 | |
284 | Ubiquitination | EFGRDLEKDIRSDTS CCCCCHHHHHHCCCC | 66.79 | - | |
302 | S-palmitoylation | ERLLVSMCQGNRDER HHHHHHHHCCCHHHH | 3.50 | 26165157 | |
311 | Phosphorylation | GNRDERQSVNHQMAQ CCHHHHHHHHHHHHH | 30.98 | 25521595 | |
325 | Phosphorylation | QEDAQRLYQAGEGRL HHHHHHHHHCCCCCC | 9.86 | 25195567 | |
337 | Phosphorylation | GRLGTDESCFNMILA CCCCCCHHHHHHHHH | 27.15 | 25266776 | |
338 | S-nitrosocysteine | RLGTDESCFNMILAT CCCCCHHHHHHHHHC | 2.41 | - | |
338 | Glutathionylation | RLGTDESCFNMILAT CCCCCHHHHHHHHHC | 2.41 | 24333276 | |
338 | S-nitrosylation | RLGTDESCFNMILAT CCCCCHHHHHHHHHC | 2.41 | 22178444 | |
338 | S-palmitoylation | RLGTDESCFNMILAT CCCCCHHHHHHHHHC | 2.41 | 28526873 | |
352 | Ubiquitination | TRSFPQLKATMEAYS CCCCHHHHHHHHHHH | 36.24 | - | |
368 | Phosphorylation | MANRDLLSSVSREFS HHCHHHHHHHHHHHH | 35.67 | 29176673 | |
369 | Phosphorylation | ANRDLLSSVSREFSG HCHHHHHHHHHHHHH | 24.87 | 29176673 | |
371 | Phosphorylation | RDLLSSVSREFSGYV HHHHHHHHHHHHHHH | 28.21 | 29176673 | |
388 | S-palmitoylation | GLKTILQCALNRPAF HHHHHHHHHHCCHHH | 4.11 | 26165157 | |
405 | Malonylation | ERLYYSMKGAGTDDS HHHHHHHCCCCCCCC | 39.40 | 26320211 | |
405 | Acetylation | ERLYYSMKGAGTDDS HHHHHHHCCCCCCCC | 39.40 | 23236377 | |
405 | Ubiquitination | ERLYYSMKGAGTDDS HHHHHHHCCCCCCCC | 39.40 | - | |
430 | Acetylation | EIDLVQIKQMFTQMY HCCHHHHHHHHHHHH | 20.72 | 22826441 |
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 ANXA7_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ANXA7_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 ANXA7_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
SORCN_MOUSE | Sri | physical | 14644162 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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