UniProt ID | A1AT1_MOUSE | |
---|---|---|
UniProt AC | P07758 | |
Protein Name | Alpha-1-antitrypsin 1-1 | |
Gene Name | Serpina1a | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 413 | |
Subcellular Localization | Secreted . | |
Protein Description | Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin.. | |
Protein Sequence | MTPSISWGLLLLAGLCCLVPSFLAEDVQETDTSQKDQSPASHEIATNLGDFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEADIHKSFQHLLQTLNRPDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVKKLDQDTVFALANYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNATAVFLLPDDGKMQHLEQTLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEENAPLKLSQAVHKAVLTIDETGTEAAAVTVLQMVPMSMPPILRFDHPFLFIIFEEHTQSPIFLGKVVDPTHK | |
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 |
---|---|---|---|---|---|
38 | Phosphorylation | DTSQKDQSPASHEIA CCCCCCCCCHHHHHH | 32.35 | 23984901 | |
41 | Phosphorylation | QKDQSPASHEIATNL CCCCCCHHHHHHHHH | 25.66 | 27180971 | |
46 | Phosphorylation | PASHEIATNLGDFAI CHHHHHHHHHHHHHH | 36.32 | 23984901 | |
64 | N-linked_Glycosylation | RELVHQSNTSNIFFS HHHHHHCCCCCCCCC | 40.74 | 17330941 | |
101 | N-linked_Glycosylation | ILEGLQFNLTQTSEA HHHHCEECCCCCCHH | 29.26 | 17330941 | |
147 | Ubiquitination | NDLKLVEKFLEEAKN CCHHHHHHHHHHHHH | 48.01 | 22790023 | |
147 | Acetylation | NDLKLVEKFLEEAKN CCHHHHHHHHHHHHH | 48.01 | 23954790 | |
173 | Ubiquitination | AESEEAKKVINDFVE CCCHHHHHHHHHHHH | 56.23 | 22790023 | |
181 | Acetylation | VINDFVEKGTQGKIA HHHHHHHHCCCCHHH | 63.05 | 23954790 | |
181 | Ubiquitination | VINDFVEKGTQGKIA HHHHHHHHCCCCHHH | 63.05 | - | |
181 | Succinylation | VINDFVEKGTQGKIA HHHHHHHHCCCCHHH | 63.05 | 23954790 | |
186 | Ubiquitination | VEKGTQGKIAEAVKK HHHCCCCHHHHHHHH | 29.00 | 27667366 | |
209 | Ubiquitination | LANYILFKGKWKKPF HHHHHHHCCCCCCCC | 57.02 | 27667366 | |
214 | Acetylation | LFKGKWKKPFDPENT HHCCCCCCCCCCCCC | 50.21 | 21728379 | |
265 | N-linked_Glycosylation | LLMDYAGNATAVFLL HHECCCCCEEEEEEC | 26.41 | - | |
287 | Ubiquitination | HLEQTLSKELISKFL HHHHHHCHHHHHHHH | 60.70 | 22790023 | |
292 | Malonylation | LSKELISKFLLNRRR HCHHHHHHHHHHHHH | 32.79 | 25418362 | |
292 | Ubiquitination | LSKELISKFLLNRRR HCHHHHHHHHHHHHH | 32.79 | 27667366 | |
292 | Acetylation | LSKELISKFLLNRRR HCHHHHHHHHHHHHH | 32.79 | 23864654 | |
315 | Ubiquitination | RLSISGEYNLKTLMS CCEECCCCCHHHHCC | 29.35 | 27667366 | |
318 | Ubiquitination | ISGEYNLKTLMSPLG ECCCCCHHHHCCCCC | 35.65 | 22790023 | |
347 | Ubiquitination | TEENAPLKLSQAVHK CCCCCCHHHHHHHHH | 45.06 | 22790023 | |
370 | Ubiquitination | GTEAAAVTVLQMVPM CCHHHHEEEECCCCC | 15.69 | 27667366 |
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 A1AT1_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of A1AT1_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 A1AT1_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
CELA1_MOUSE | Cela1 | physical | 11961105 | |
ELNE_MOUSE | Elane | physical | 11961105 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...
N-linked Glycosylation | |
Reference | PubMed |
"Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides."; Bernhard O.K., Kapp E.A., Simpson R.J.; J. Proteome Res. 6:987-995(2007). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-64 AND ASN-101, AND MASSSPECTROMETRY. |