A1AT2_MOUSE - dbPTM
A1AT2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID A1AT2_MOUSE
UniProt AC P22599
Protein Name Alpha-1-antitrypsin 1-2
Gene Name Serpina1b
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 MTPSISWGLLLLAGLCCMVPSFLAEDVQETDTSQKDQSPASHEIATNLGDFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEADIHKSFQHLLQTLNRPDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIVEAVKELDQDTVFALANYILFKGKWKKPFDPENTEEAEFHVDKSTTVKVPMMMLSGMLDVHHCSILSSWVLLMDYAGNASAVFLLPEDGKMQHLEQTLNKELISKILLNRRRRLVQIHIPRLSISGDYNLKTLMSPLGITRIFNNGADLSGITEENAPLKLSKAVHKAVLTIDETGTEAAAATVFEAVPMSMPPILRFDHPFLFIIFEEHTQSPIFVGKVVDPTHK
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
38PhosphorylationDTSQKDQSPASHEIA
CCCCCCCCCHHHHHH
32.3523984901
41PhosphorylationQKDQSPASHEIATNL
CCCCCCHHHHHHHHH
25.6627180971
46PhosphorylationPASHEIATNLGDFAI
CHHHHHHHHHHHHHH
36.3223984901
64N-linked_GlycosylationRELVHQSNTSNIFFS
HHHHHHCCCCCCCCC
40.74-
101N-linked_GlycosylationILEGLQFNLTQTSEA
HHHHCEECCCCCCHH
29.2616944957
147UbiquitinationNDLKLVEKFLEEAKN
CCHHHHHHHHHHHHH
48.01-
147AcetylationNDLKLVEKFLEEAKN
CCHHHHHHHHHHHHH
48.01-
173UbiquitinationAESEEAKKVINDFVE
CCCHHHHHHHHHHHH
56.23-
181AcetylationVINDFVEKGTQGKIV
HHHHHHHHCCCCCHH
63.05-
181UbiquitinationVINDFVEKGTQGKIV
HHHHHHHHCCCCCHH
63.05-
186UbiquitinationVEKGTQGKIVEAVKE
HHHCCCCCHHHHHHH
33.4927667366
214AcetylationLFKGKWKKPFDPENT
HHCCCCCCCCCCCCC
50.2155170063
265N-linked_GlycosylationLLMDYAGNASAVFLL
HHHHHCCCCEEEEEE
23.6616944957
287UbiquitinationHLEQTLNKELISKIL
HHHHHHCHHHHHHHH
57.9422790023
292AcetylationLNKELISKILLNRRR
HCHHHHHHHHHHCCH
30.3123864654
292UbiquitinationLNKELISKILLNRRR
HCHHHHHHHHHHCCH
30.3122790023
318UbiquitinationISGDYNLKTLMSPLG
ECCCCCHHHHCCCCC
35.6522790023
347UbiquitinationTEENAPLKLSKAVHK
CCCCCCHHHHHHHHH
50.0522790023

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 A1AT2_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of A1AT2_MOUSE !!

Disease-associated PTM Sites based on SAP

* 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 A1AT2_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of A1AT2_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of A1AT2_MOUSE

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Proteome-wide characterization of N-glycosylation events by diagonalchromatography.";
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,Gevaert K.;
J. Proteome Res. 5:2438-2447(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-101 AND ASN-265, AND MASSSPECTROMETRY.

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