A1AT_HUMAN - dbPTM
A1AT_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID A1AT_HUMAN
UniProt AC P01009
Protein Name Alpha-1-antitrypsin
Gene Name SERPINA1
Organism Homo sapiens (Human).
Sequence Length 418
Subcellular Localization Secreted. Endoplasmic reticulum. The S and Z allele are not secreted effectively and accumulate intracellularly in the endoplasmic reticulum.
Short peptide from AAT: Secreted, extracellular space, extracellular matrix.
Protein Description Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin.; Short peptide from AAT: reversible chymotrypsin inhibitor. It also inhibits elastase, but not trypsin. Its major physiological function is the protection of the lower respiratory tract against proteolytic destruction by human leukocyte elastase (HLE)..
Protein Sequence MPSSVSWGILLLAGLCCLVPVSLAEDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK
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
38PhosphoserineAAQKTDTSHHDQDHP
CCCCCCCCCCCCCCC
22.9526091039
70N-linked (GlcNAc)RQLAHQSNSTNIFFS
HHHHHHCCCCCCCCC
46.4012754519
14760718
15084671
16263699
16335952
16622833
19159218
19838169
22171320
70N-linked GlycosylationRQLAHQSNSTNIFFS
HHHHHHCCCCCCCCC
46.4012754519
107N-linked (GlcNAc)ILEGLNFNLTEIPEA
HHHHCCCCCCCCCHH
45.0016335952
16622833
19139490
19159218
19838169
107N-linked GlycosylationILEGLNFNLTEIPEA
HHHHCCCCCCCCCHH
45.0012626422
153N6-acetyllysineEGLKLVDKFLEDVKK
HHHHHHHHHHHHHHH
44.3527178108
159N6-acetyllysineDKFLEDVKKLYHSEA
HHHHHHHHHHHHCCC
49.7527178108
160 N-acetyllysineKFLEDVKKLYHSEAF
HHHHHHHHHHHCCCE
54.877673957
184PhosphotyrosineAKKQINDYVEKGTQG
HHHHHHHHHHHCCCC
13.1622135298
198N6-acetyllysineGKIVDLVKELDRDTV
CCHHHHHHHCCHHHH
60.9120167786
217N6-acetyllysineNYIFFKGKWERPFEV
HHHHHCCCCCCCCCC
46.6127178108
256 S-nitrosocysteineGMFNIQHCKKLSSWV
CCCCHHHHHHHHHHH
2.0822178444
25040305
10673391
257 N-acetyllysineMFNIQHCKKLSSWVL
CCCHHHHHHHHHHHH
55.417683323
261PhosphoserineQHCKKLSSWVLLMKY
HHHHHHHHHHHHHHH
31.4722135298
271N-linked (GlcNAc)LLMKYLGNATAIFFL
HHHHHHCCCEEEEEC
31.3612754519
14760718
15084671
16335952
16622833
19139490
19159218
19838169
22171320
271N-linked GlycosylationLLMKYLGNATAIFFL
HHHHHHCCCEEEEEC
31.3617660510
18514042
18638581
314 N-acetyllysineSASLHLPKLSITGTY
HCCCCCCCEEEEEEE
62.317684525
321PhosphotyrosineKLSITGTYDLKSVLG
CEEEEEEEEHHHHHH
22.1822135298
333PhosphothreonineVLGQLGITKVFSNGA
HHHHHCCEEEECCCC
21.2520068231
359N6-acetyllysineKLSKAVHKAVLTIDE
HHHHHHHHHEEEECC
33.3227178108
383PhosphoserineFLEAIPMSIPPEVKF
HHHHCCCCCCCCCCC
26.9620068231
416PhosphothreonineMGKVVNPTQK-----
CCEECCCCCC-----
43.7315498560
16381945
23193290
22135298

Disease-associated PTM Sites based on nsSNP

* Distance = the distance between SNP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SNP Related Disease Reference

Oops, there are no SNP-PTM records of A1AT_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
OS9_HUMANOS9physical
18264092
ERLEC_HUMANERLEC1physical
18264092
DERL1_HUMANDERL1physical
23867461
DERL2_HUMANDERL2physical
23867461
SMAD4_HUMANSMAD4physical
21988832
SYVN1_HUMANSYVN1physical
28121484
SQSTM_HUMANSQSTM1physical
28121484
SRP54_HUMANSRP54physical
26565908
DERL1_HUMANDERL1physical
26565908
DERL2_HUMANDERL2physical
26565908
DERL3_HUMANDERL3physical
26565908

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613490Alpha-1-antitrypsin deficiency (A1ATD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Comprehensive glyco-proteomic analysis of human alpha1-antitrypsinand its charge isoforms.";
Kolarich D., Weber A., Turecek P.L., Schwarz H.P., Altmann F.;
Proteomics 6:3369-3380(2006).
Cited for: PROTEIN SEQUENCE OF 30-48 AND 248-257 (ISOFORMS 1/2/3), GLYCOSYLATIONAT ASN-70; ASN-107 AND ASN-271, STRUCTURE OF CARBOHYDRATES,CYSTEINE-BINDING, AND MASS SPECTROMETRY.
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry.";
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
Nat. Biotechnol. 21:660-666(2003).
Cited for: GLYCOSYLATION AT ASN-70 AND ASN-271.
"A proteomic analysis of human bile.";
Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H.,Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.;
Mol. Cell. Proteomics 3:715-728(2004).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70 AND ASN-271, AND MASSSPECTROMETRY.
"Screening for N-glycosylated proteins by liquid chromatography massspectrometry.";
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
Proteomics 4:454-465(2004).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70 AND ASN-271, AND MASSSPECTROMETRY.
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70; ASN-107 AND ASN-271,AND MASS SPECTROMETRY.
"Elucidation of N-glycosylation sites on human platelet proteins: aglycoproteomic approach.";
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
Mol. Cell. Proteomics 5:226-233(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70, AND MASS SPECTROMETRY.
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70; ASN-107 AND ASN-271,AND MASS SPECTROMETRY.
"Enrichment of glycopeptides for glycan structure and attachment siteidentification.";
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,Brinkmalm G., Larson G.;
Nat. Methods 6:809-811(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70; ASN-107 AND ASN-271,STRUCTURE OF CARBOHYDRATES, AND MASS SPECTROMETRY.
"Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD.";
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
Mol. Cell. Proteomics 0:0-0(2011).
Cited for: GLYCOSYLATION AT ASN-70 AND ASN-271, STRUCTURE OF CARBOHYDRATES, ANDMASS SPECTROMETRY.

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