Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Alpha-1-antitrypsin  

UniProtKB / Swiss-Prot ID :  A1AT_HUMAN

Gene Name (Synonyms) : 
SERPINA1, AAT, PI PRO0684, PRO2209  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Secreted. Short peptide from AAT: Secreted, extracellular space, extracellular matrix. 

Protein Function :  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 (SPAAT) is a 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 MPSSVSWGILLLAGLCCLVPVSLAEDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSN...
Predicted Secondary Structure CHHHHHHHHHHHHHHHHHHCCEECCCCCCCCCCCCCCCCCCCCCHHHHHHHHHHHHHHHHHHHHHHHHCC...
Protein Variant
LocationDescription
4S -> L (in Z-Wrexham). VAR_006978
26D -> A (in V-Munich). VAR_006979
37T -> A (in dbSNP:rs11558262). VAR_051938
58A -> T (in M5-Karlsruhe). VAR_006980
63R -> C (in I; dbSNP:rs28931570). VAR_006981
65L -> P (in M-Procida; dbSNP:rs28931569). VAR_006982
69S -> F (in M6-Bonn). VAR_006983
75Missing (in M-Malton, M-Nichinan and M-Palermo; associated with very low serum
77S -> F (in S-Iiyama; dbSNP:rs55819880). VAR_006985
84A -> T (in M6-Passau). VAR_006986
91G -> E (in M-Mineral springs; causesreduced AAT secretion; dbSNP:rs28931568).
92T -> I (in QO-Lisbon; deficient AAT withvery low serum levels).
109T -> M (in Z-Bristol; deficient AA;disrupts the N-glycosylation site N-107).
112P -> T (in M5-Berlin). VAR_006989
116I -> N (in QO-Ludwigshafen;dbSNP:rs28931572).
125R -> H (in M2; associated with D-400;dbSNP:rs709932).
139G -> S (in QO-Newport; dbSNP:rs11558261). VAR_006992
172G -> R (in V and M-Nichinan). VAR_006993
172G -> W (in M2-Obernburg). VAR_006994
180Q -> E (in L-Frankfurt). VAR_006995
190QGKIVDLVK -> GFQNAILVR (in Aberrantform).
228E -> K (in X). VAR_006996
237V -> A (in M1A and Z; associated with K-366 in Z; dbSNP:rs6647).
247R -> C (in F; dbSNP:rs28929470). VAR_006998
280D -> V (in P-Duarte/P-Cardiff/P-Lowell;associated with H-415 in Y-Barcelona;
288E -> V (in S and T; dbSNP:rs17580). VAR_007000
305Missing (in Basque). VAR_009216
354S -> F (in S-Munich). VAR_007001
360A -> T (in W-Bethesda; dbSNP:rs1802959). VAR_007002
365D -> N (in P-St.Albans/P-Donauwoerth). VAR_007003
366E -> K (in Z/Z-Augsburg/Z-Tun; associatedwith A-237 in Z; dbSNP:rs28929474).
382M -> R (in Pittsburgh; has antithrombinactivity; causes fatal bleeding
386P -> H (in Sao Tome). VAR_007006
386P -> T (in L-Offenbach). VAR_007007
387E -> K (in Christchurch). VAR_007008
393P -> L (in M-Heerlen). VAR_007009
400E -> D (in M2 and M3; associated with H-125 in M2; dbSNP:rs1303).
415P -> H (in Y-Barcelona; associated withV-280).
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
24nonePVSLAEDPQ
CCEECCCCC
16.19HPRD
Link-
70N-linked (Glc...)AHQSNSTNI
HHHCCCCCE
46.40HPRD
Link
70N-linked (GlcNAc...) (complex).AHQSNSTNI
HHHCCCCCE
46.40UniProtKB
Link
107N-linked (Glc...)GLNFNLTEI
HHCCCCCCC
45.00HPRD
Link
107N-linked (GlcNAc...) (complex).GLNFNLTEI
HHCCCCCCC
45.00UniProtKB
Link
198N6-acetyllysineVDLVKELDR
CHHHCCCCH
60.91Phosphositeplus
Link
256S-cysteinyl cysteine.NIQHCKKLS
EEEEECCCC
2.08UniProtKB
Link
256S-nitrosocysteineNIQHCKKLS
EEEEECCCC
2.08dbSNO
Link
256S-nitrosocysteineNIQHCKKLS
EEEEECCCC
2.08HPRD
Link
271N-linked (Glc...)KYLGNATAI
EECCCCEEE
31.36HPRD
Link
271N-linked (GlcNAc...)KYLGNATAI
EECCCCEEE
31.36SysPTM
Link
271N-linked (GlcNAc...) (complex).KYLGNATAI
EECCCCEEE
31.36UniProtKB
Link
333PhosphothreonineQLGITKVFS
HCCCCHHHC
21.25HPRD
Link
333PhosphothreonineQLGITKVFS
HCCCCHHHC
21.25Phosphositeplus
Link
374noneEAAGAMFLE
ECCCCCEEE
4.84HPRD
Link
376noneAGAMFLEAI
CCCCEEEEE
5.74HPRD
Link
383PhosphoserineAIPMSIPPE
EEEEEECCE
26.96HPRD
Link
416PhosphothreonineVVNPTQK
ECCCCCC
43.73Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
SSRA_HUMANphysical interactionMINT-4546656MINT17380188
ELNE_HUMANdirect interactionEBI-986375
intact16321984
A1AT_HUMANphysical interactionEBI-1030075
intact11057674
CTRB1_HUMANin vitroHPRD:02463HPRD6983488
ELA1_HUMANin vitro
in vivo
HPRD:02463HPRD6191979
6153632
1079736
ELNE_HUMANin vitroHPRD:02463HPRD10867014
PRTN3_HUMANin vitroHPRD:02463HPRD12114510
TRY1_HUMANin vitroHPRD:02463HPRD11057674
A1AT_HUMANin vitroHPRD:02463HPRD2785270
6332197
6966283
6976274
6982267
6983488
CATG_HUMANin vitroHPRD:02463HPRD15131125
CATG_HUMANENSP00000348068STRING
CATG_HUMANENSP00000348068STRING
CATG_HUMANENSP00000348068STRING
CATG_HUMANENSP00000348068STRING
CATG_HUMANENSP00000348068STRING
CD79A_HUMANENSP00000348068STRING
CD79A_HUMANENSP00000348068STRING
CD79A_HUMANENSP00000348068STRING
CD79A_HUMANENSP00000348068STRING
CD79A_HUMANENSP00000348068STRING
CD79A_HUMANENSP00000348068STRING
CD79A_HUMANENSP00000348068STRING
CD79A_HUMANENSP00000348068STRING
CD79A_HUMANENSP00000348068STRING
CD79A_HUMANENSP00000348068STRING
PRTN3_HUMANENSP00000348068STRING
PRTN3_HUMANENSP00000348068STRING
PRTN3_HUMANENSP00000348068STRING
PRTN3_HUMANENSP00000348068STRING
PRTN3_HUMANENSP00000348068STRING
TTHY_HUMANENSP00000348068STRING
TTHY_HUMANENSP00000348068STRING
TTHY_HUMANENSP00000348068STRING
TTHY_HUMANENSP00000348068STRING
TTHY_HUMANENSP00000348068STRING
CALX_HUMANENSP00000348068STRING
CALX_HUMANENSP00000348068STRING
CALX_HUMANENSP00000348068STRING
CALX_HUMANENSP00000348068STRING
CALX_HUMANENSP00000348068STRING
HNF1A_HUMANENSP00000348068STRING
HNF1A_HUMANENSP00000348068STRING
HNF1A_HUMANENSP00000348068STRING
HNF1A_HUMANENSP00000348068STRING
HNF1A_HUMANENSP00000348068STRING
ELNE_HUMANENSP00000348068STRING
ELNE_HUMANENSP00000348068STRING
ELNE_HUMANENSP00000348068STRING
ELNE_HUMANENSP00000348068STRING
ELNE_HUMANENSP00000348068STRING
ELA1_HUMANENSP00000348068STRING
ELA1_HUMANENSP00000348068STRING
ELA1_HUMANENSP00000348068STRING
ELA1_HUMANENSP00000348068STRING
ELA1_HUMANENSP00000348068STRING
ALBU_HUMANENSP00000348068STRING
ALBU_HUMANENSP00000348068STRING
ALBU_HUMANENSP00000348068STRING
ALBU_HUMANENSP00000348068STRING
ALBU_HUMANENSP00000348068STRING
ALBU_HUMANENSP00000348068STRING
ALBU_HUMANENSP00000348068STRING
ALBU_HUMANENSP00000348068STRING
ALBU_HUMANENSP00000348068STRING
ALBU_HUMANENSP00000348068STRING
CTRB1_HUMANENSP00000348068STRING
CTRB1_HUMANENSP00000348068STRING
CTRB1_HUMANENSP00000348068STRING
CTRB1_HUMANENSP00000348068STRING
CTRB1_HUMANENSP00000348068STRING
A2MG_HUMANENSP00000348068STRING
A2MG_HUMANENSP00000348068STRING
A2MG_HUMANENSP00000348068STRING
A2MG_HUMANENSP00000348068STRING
A2MG_HUMANENSP00000348068STRING
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Disease Reference
Kegg disease
OMIM disease
613490Alpha-1-antitrypsin deficiency (A1ATD)
Drug Reference
There are no disease associations of PTM sites.
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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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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures