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
35O-linked_GlycosylationQGDAAQKTDTSHHDQ
CCCCCCCCCCCCCCC		32.22OGP
35PhosphorylationQGDAAQKTDTSHHDQ
CCCCCCCCCCCCCCC		32.2227130503
37PhosphorylationDAAQKTDTSHHDQDH
CCCCCCCCCCCCCCC		34.8826657352
38PhosphorylationAAQKTDTSHHDQDHP
CCCCCCCCCCCCCCC		22.9526657352
60PhosphorylationNLAEFAFSLYRQLAH
CHHHHHHHHHHHHHH		22.5128857561
62NitrationAEFAFSLYRQLAHQS
HHHHHHHHHHHHHHC		8.63-
62PhosphorylationAEFAFSLYRQLAHQS
HHHHHHHHHHHHHHC		8.6328857561
70N-linked_GlycosylationRQLAHQSNSTNIFFS
HHHHHHCCCCCCCCC		46.4022171320
70N-linked_GlycosylationRQLAHQSNSTNIFFS
HHHHHHCCCCCCCCC		46.4022171320
107N-linked_GlycosylationILEGLNFNLTEIPEA
HHHHCCCCCCCCCHH		45.0019838169
107N-linked_GlycosylationILEGLNFNLTEIPEA
HHHHCCCCCCCCCHH		45.0019838169
109O-linked_GlycosylationEGLNFNLTEIPEAQI
HHCCCCCCCCCHHHH		32.73OGP
137O-linked_GlycosylationPDSQLQLTTGNGLFL
CCCCCEEECCCCEEH		21.5029351928
138O-linked_GlycosylationDSQLQLTTGNGLFLS
CCCCEEECCCCEEHH		36.9229351928
153AcetylationEGLKLVDKFLEDVKK
HHHHHHHHHHHHHHH		44.3527178108
153GlycationEGLKLVDKFLEDVKK
HHHHHHHHHHHHHHH		44.35-
159AcetylationDKFLEDVKKLYHSEA
HHHHHHHHHHHHCCC		49.7527178108
160AcetylationKFLEDVKKLYHSEAF
HHHHHHHHHHHCCCE		54.877673957
162NitrationLEDVKKLYHSEAFTV
HHHHHHHHHCCCEEE		16.51-
168O-linked_GlycosylationLYHSEAFTVNFGDTE
HHHCCCEEEECCCHH		22.91OGP
184NitrationAKKQINDYVEKGTQG
HHHHHHHHHHHCCCC		13.16-
184PhosphorylationAKKQINDYVEKGTQG
HHHHHHHHHHHCCCC		13.16-
187GlycationQINDYVEKGTQGKIV
HHHHHHHHCCCCCHH		58.16-
192GlycationVEKGTQGKIVDLVKE
HHHCCCCCHHHHHHH		29.73-
198AcetylationGKIVDLVKELDRDTV
CCHHHHHHHCCHHHH		60.9120167786
211NitrationTVFALVNYIFFKGKW
HHHHHHHHHHHCCCC		7.51-
217AcetylationNYIFFKGKWERPFEV
HHHHHCCCCCCCCCC		46.6127178108
238O-linked_GlycosylationDFHVDQVTTVKVPMM
CCCCCEEEEEECCCC		21.90OGP
239O-linked_GlycosylationFHVDQVTTVKVPMMK
CCCCEEEEEECCCCH		21.33OGP
256S-nitrosylationGMFNIQHCKKLSSWV
CCCCHHHHHHHHHHH		2.0822178444
256S-cysteinylationGMFNIQHCKKLSSWV
CCCCHHHHHHHHHHH		2.08-
256S-cysteinyl cysteineGMFNIQHCKKLSSWV
CCCCHHHHHHHHHHH		2.08-
257AcetylationMFNIQHCKKLSSWVL
CCCHHHHHHHHHHHH		55.417683323
261PhosphorylationQHCKKLSSWVLLMKY
HHHHHHHHHHHHHHH		31.47-
268NitrationSWVLLMKYLGNATAI
HHHHHHHHHCCCEEE		13.08-
271N-linked_GlycosylationLLMKYLGNATAIFFL
HHHHHHCCCEEEEEC		31.3622171320
271N-linked_GlycosylationLLMKYLGNATAIFFL
HHHHHHCCCEEEEEC		31.3622171320
307PhosphorylationLENEDRRSASLHLPK
HHCCCHHHCCCCCCC		24.0923911959
309PhosphorylationNEDRRSASLHLPKLS
CCCHHHCCCCCCCEE		19.9828857561
314AcetylationSASLHLPKLSITGTY
HCCCCCCCEEEEEEE		62.317684525
316PhosphorylationSLHLPKLSITGTYDL
CCCCCCEEEEEEEEH		25.0024719451
318O-linked_GlycosylationHLPKLSITGTYDLKS
CCCCEEEEEEEEHHH		21.79OGP
318PhosphorylationHLPKLSITGTYDLKS
CCCCEEEEEEEEHHH		21.7924719451
321NitrationKLSITGTYDLKSVLG
CEEEEEEEEHHHHHH		22.18-
321PhosphorylationKLSITGTYDLKSVLG
CEEEEEEEEHHHHHH		22.18-
325PhosphorylationTGTYDLKSVLGQLGI
EEEEEHHHHHHHHCC		29.8523911959
333PhosphorylationVLGQLGITKVFSNGA
HHHHHCCEEEECCCC		21.2520068231
333O-linked_GlycosylationVLGQLGITKVFSNGA
HHHHHCCEEEECCCC		21.25OGP
343PhosphorylationFSNGADLSGVTEEAP
ECCCCCCCCCCCCCC		31.5927251275
346O-linked_GlycosylationGADLSGVTEEAPLKL
CCCCCCCCCCCCHHH		31.47OGP
351SulfoxidationGVTEEAPLKLSKAVH
CCCCCCCHHHHHHHH		12.8910867014
354PhosphorylationEEAPLKLSKAVHKAV
CCCCHHHHHHHHHHE		19.5822673903
358SulfoxidationLKLSKAVHKAVLTID
HHHHHHHHHHEEEEC		19.7410867014
359AcetylationKLSKAVHKAVLTIDE
HHHHHHHHHEEEECC		33.3227178108
369PhosphorylationLTIDEKGTEAAGAMF
EEECCCCCHHHHCHH		33.2520068231
383PhosphorylationFLEAIPMSIPPEVKF
HHHHCCCCCCCCCCC		26.9617650587
385SulfoxidationEAIPMSIPPEVKFNK
HHCCCCCCCCCCCCC		16.2227929071
403O-linked_GlycosylationFLMIEQNTKSPLFMG
EEEEECCCCCCCCCC		32.37OGP
416PhosphorylationMGKVVNPTQK-----
CCEECCCCCC-----		43.7315498560
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
38SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot
-KUbiquitinationE3 ubiquitin ligaseAMFRQ9UKV5
PMID:16979136
-KUbiquitinationE3 ubiquitin ligaseSYVN1Q86TM6
PMID:21199683
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of A1AT_HUMAN !!
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 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.
Regulatory Network of A1AT_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.

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