AACT_HUMAN - dbPTM
AACT_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AACT_HUMAN
UniProt AC P01011
Protein Name Alpha-1-antichymotrypsin
Gene Name SERPINA3
Organism Homo sapiens (Human).
Sequence Length 423
Subcellular Localization Secreted.
Protein Description Although its physiological function is unclear, it can inhibit neutrophil cathepsin G and mast cell chymase, both of which can convert angiotensin-1 to the active angiotensin-2..
Protein Sequence MERMLPLLALGLLAAGFCPAVLCHPNSPLDEENLTQENQDRGTHVDLGLASANVDFAFSLYKQLVLKAPDKNVIFSPLSISTALAFLSLGAHNTTLTEILKGLKFNLTETSEAEIHQSFQHLLRTLNQSSDELQLSMGNAMFVKEQLSLLDRFTEDAKRLYGSEAFATDFQDSAAAKKLINDYVKNGTRGKITDLIKDLDSQTMMVLVNYIFFKAKWEMPFDPQDTHQSRFYLSKKKWVMVPMMSLHHLTIPYFRDEELSCTVVELKYTGNASALFILPDQDKMEEVEAMLLPETLKRWRDSLEFREIGELYLPKFSISRDYNLNDILLQLGIEEAFTSKADLSGITGARNLAVSQVVHKAVLDVFEEGTEASAATAVKITLLSALVETRTIVRFNRPFLMIIVPTDTQNIFFMSKVTNPKQA
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
27PhosphorylationAVLCHPNSPLDEENL
HHHCCCCCCCCHHHC		31.1524505115
33N-linked_GlycosylationNSPLDEENLTQENQD
CCCCCHHHCCCCCCC		46.4716335952
33N-linked_GlycosylationNSPLDEENLTQENQD
CCCCCHHHCCCCCCC		46.4717623646
35PhosphorylationPLDEENLTQENQDRG
CCCHHHCCCCCCCCC		45.4826657352
93N-linked_GlycosylationFLSLGAHNTTLTEIL
HHHHCCCCCCHHHHH		33.9417623646
93N-linked_GlycosylationFLSLGAHNTTLTEIL
HHHHCCCCCCHHHHH		33.9417623646
106N-linked_GlycosylationILKGLKFNLTETSEA
HHHHCCCCCCCCCHH		44.4512754519
106N-linked_GlycosylationILKGLKFNLTETSEA
HHHHCCCCCCCCCHH		44.4518638581
127N-linked_GlycosylationQHLLRTLNQSSDELQ
HHHHHHHCCCCCHHC		38.7918638581
127N-linked_GlycosylationQHLLRTLNQSSDELQ
HHHHHHHCCCCCHHC		38.7916335952
158AcetylationDRFTEDAKRLYGSEA
HHHHHHHHHHHCCHH		56.0812438997
177AcetylationFQDSAAAKKLINDYV
CCCHHHHHHHHHHHH		43.3012439007
186N-linked_GlycosylationLINDYVKNGTRGKIT
HHHHHHHHCCCCCHH		47.2017623646
186N-linked_GlycosylationLINDYVKNGTRGKIT
HHHHHHHHCCCCCHH		47.2016335952
191AcetylationVKNGTRGKITDLIKD
HHHCCCCCHHHHHHH		38.8619814787
201PhosphorylationDLIKDLDSQTMMVLV
HHHHHCCHHHHHHHH		34.5425003641
203PhosphorylationIKDLDSQTMMVLVNY
HHHCCHHHHHHHHHH		15.9325003641
210PhosphorylationTMMVLVNYIFFKAKW
HHHHHHHHHHHHHCC		7.5128851738
226PhosphorylationMPFDPQDTHQSRFYL
CCCCCCCCCCHHEEC		19.3029083192
229PhosphorylationDPQDTHQSRFYLSKK
CCCCCCCHHEECCCC		19.4229083192
235AcetylationQSRFYLSKKKWVMVP
CHHEECCCCCEEEEE		56.6481933
236AcetylationSRFYLSKKKWVMVPM
HHEECCCCCEEEEEC		48.7981935
237AcetylationRFYLSKKKWVMVPMM
HEECCCCCEEEEECC		49.0881937
245PhosphorylationWVMVPMMSLHHLTIP
EEEEECCCCCCCCCC		20.4924505115
261S-nitrosylationFRDEELSCTVVELKY
CCCCCCCEEEEEEEE		5.3825040305
271N-linked_GlycosylationVELKYTGNASALFIL
EEEEECCCCEEEEEE		23.9516335952
271N-linked_GlycosylationVELKYTGNASALFIL
EEEEECCCCEEEEEE		23.9518638581
273PhosphorylationLKYTGNASALFILPD
EEECCCCEEEEEECC		29.51-
295PhosphorylationEAMLLPETLKRWRDS
HHHHCHHHHHHHHHH		35.3220363803
302PhosphorylationTLKRWRDSLEFREIG
HHHHHHHHHCHHHCC		22.6423911959
312PhosphorylationFREIGELYLPKFSIS
HHHCCCEECCCCEEC		19.3625690035
338PhosphorylationLGIEEAFTSKADLSG
HCCHHHHCCCCHHCC		36.04-
347PhosphorylationKADLSGITGARNLAV
CCHHCCCCCCHHHHH		28.4524505115
347O-linked_GlycosylationKADLSGITGARNLAV
CCHHCCCCCCHHHHH		28.4546286157
355PhosphorylationGARNLAVSQVVHKAV
CCHHHHHHHHHHHHH		16.2024505115
370PhosphorylationLDVFEEGTEASAATA
HHHHHHCCHHHHHHH		31.4924505115
373PhosphorylationFEEGTEASAATAVKI
HHHCCHHHHHHHHHH		16.5324505115
373O-linked_GlycosylationFEEGTEASAATAVKI
HHHCCHHHHHHHHHH		16.53OGP
381O-linked_GlycosylationAATAVKITLLSALVE
HHHHHHHHHHHHHHH		18.87OGP
381PhosphorylationAATAVKITLLSALVE
HHHHHHHHHHHHHHH		18.8724505115
384PhosphorylationAVKITLLSALVETRT
HHHHHHHHHHHHCCH		23.7524505115
389PhosphorylationLLSALVETRTIVRFN
HHHHHHHCCHHHCCC		26.1524505115
389O-linked_GlycosylationLLSALVETRTIVRFN
HHHHHHHCCHHHCCC		26.15OGP
416AcetylationQNIFFMSKVTNPKQA
CCEEEEECCCCCCCC		41.097782318
421AcetylationMSKVTNPKQA-----
EECCCCCCCC-----		62.017782318
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 AACT_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AACT_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 AACT_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RPA12_HUMANZNRD1physical
21988832
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AACT_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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-93; ASN-106; ASN-127 ANDASN-271, 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-33; ASN-93; ASN-106;ASN-127; ASN-186 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-93, 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-93 AND ASN-106.

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