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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Alpha-1-antitrypsin

UniprotKB/SwissProt ID: A1AT_HUMAN (P01009)

Gene Name: SERPINA1

Synonyms: AAT, PI

Organism: Homo sapiens (Human).

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: 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).

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Secreted. Endoplasmic reticulum. Note=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.

PDB :
( If your security settings prevent Jmol from running, please register http://140.138.144.145/ as a safe location in your Java settings. )

Protein disease:
Disease database Database Entry Disease information
HPRD02463PI B (Alhambra)
HPRD02463PI Christchurch
HPRD02463PI F
HPRD02463PI I
HPRD02463PI Kalsheker-Poller
HPRD02463PI M (Heerlen)
HPRD02463PI M (Malton)
HPRD02463PI M (Mineral Springs)
HPRD02463PI M (Nichinan)
HPRD02463PI M (Procida)
HPRD02463PI M1-Ala213
HPRD02463PI M2
HPRD02463PI M3
HPRD02463PI null (Bellingham)
HPRD02463PI null (Bolton)
HPRD02463PI null (Devon)
HPRD02463PI null (Granite Falls)
HPRD02463PI null (Hong Kong 1)
HPRD02463PI null (Ludwigshafen)
HPRD02463PI null (Mattawa)
HPRD02463PI null (Procida)
HPRD02463PI null (Riedenburg)
HPRD02463PI null (West)
HPRD02463PI P (Duarte)
HPRD02463PI P (Lowell)
HPRD02463PI P (St. Albans)
HPRD02463PI Pittsburgh
HPRD02463PI S
HPRD02463PI S (Iiyama)
HPRD02463PI V (Munich)
HPRD02463PI W (Bethesda)
HPRD02463PI X
HPRD02463PI Z
HPRD02463PI Z (Augsburg)
HPRD02463PI Z (Wrexham)
Network with metabolic pathway:
Kegg map ID Pathway Link
map04610Complement and coagulation cascades
Graphical Visualization of S-nitrosylation Sites:
Overview of Protein S-nitrosylation Sites with Functional and Structural Information
InterPro ID Domain
IPR000215

3D Structure Databases:
3D structure databases
EntryMethodResolution (A)ChainPositionsView
1ATU X-ray 2.70 A A45-418Link
1D5S X-ray 3.00 A A44-377Link
B378-418
1EZX X-ray 2.60 A A48-382Link
1HP7 X-ray 2.10 A A25-418Link
1IZ2 X-ray 2.20 A A25-418Link
1KCT X-ray 3.46 A A25-418Link
1OO8 X-ray 2.65 A A26-418Link
1OPH X-ray 2.30 A A26-418Link
1PSI X-ray 2.92 A A26-418Link
1QLP X-ray 2.00 A A26-418Link
1QMB X-ray 2.60 A A49-376Link
2D26 X-ray 3.30 A A26-382Link
B383-418
2QUG X-ray 2.00 A A25-418Link
3CWL X-ray 2.44 A A25-418Link
3CWM X-ray 2.51 A A25-418Link
3DRM X-ray 2.20 A A26-418Link
3DRU X-ray 3.20 A A/B/C26-418Link
3NDD X-ray 1.50 A A46-372Link
B383-418
3NDF X-ray 2.70 A A46-381Link
3NE4 X-ray 1.81 A A1-418Link
3T1P X-ray 3.90 A A48-418Link
7API X-ray 3.00 A A36-382Link
B383-418
8API X-ray 3.10 A A36-382Link
9API X-ray 3.00 A A36-382Link
B383-418

The S-nitrosylation sites of A1AT_HUMAN

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site Substrate Motifs PubMed ID Experiment
1256KRLGMFNIQH C KKLSSWVLLM CEECCEEEEE E CCCCCEEEEE 2.08%HC0222178444-
2256KRLGMFNIQH C KKLSSWVLLM CEECCEEEEE E CCCCCEEEEE 2.08%HC0225040305in vivo
3256KRLGMFNIQH C KKLSSWVLLM CEECCEEEEE E CCCCCEEEEE 2.08%HC0210673391
(Cys232)
in vitro