A2AP_HUMAN - dbPTM
A2AP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID A2AP_HUMAN
UniProt AC P08697
Protein Name Alpha-2-antiplasmin
Gene Name SERPINF2
Organism Homo sapiens (Human).
Sequence Length 491
Subcellular Localization Secreted.
Protein Description Serine protease inhibitor. The major targets of this inhibitor are plasmin and trypsin, but it also inactivates matriptase-3/TMPRSS7 and chymotrypsin..
Protein Sequence MALLWGLLVLSWSCLQGPCSVFSPVSAMEPLGRQLTSGPNQEQVSPLTLLKLGNQEPGGQTALKSPPGVCSRDPTPEQTHRLARAMMAFTADLFSLVAQTSTCPNLILSPLSVALALSHLALGAQNHTLQRLQQVLHAGSGPCLPHLLSRLCQDLGPGAFRLAARMYLQKGFPIKEDFLEQSEQLFGAKPVSLTGKQEDDLANINQWVKEATEGKIQEFLSGLPEDTVLLLLNAIHFQGFWRNKFDPSLTQRDSFHLDEQFTVPVEMMQARTYPLRWFLLEQPEIQVAHFPFKNNMSFVVLVPTHFEWNVSQVLANLSWDTLHPPLVWERPTKVRLPKLYLKHQMDLVATLSQLGLQELFQAPDLRGISEQSLVVSGVQHQSTLELSEVGVEAAAATSIAMSRMSLSSFSVNRPFLFFIFEDTTGLPLFVGSVRNPNPSAPRELKEQQDSPGNKDFLQSLKGFPRGDKLFGPDLKLVPPMEEDYPQFGSPK
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
36O-linked_GlycosylationEPLGRQLTSGPNQEQ
CCCCCCCCCCCCHHH
24.25OGP
36PhosphorylationEPLGRQLTSGPNQEQ
CCCCCCCCCCCCHHH
24.2528509920
37PhosphorylationPLGRQLTSGPNQEQV
CCCCCCCCCCCHHHC
61.9328509920
37O-linked_GlycosylationPLGRQLTSGPNQEQV
CCCCCCCCCCCHHHC
61.93OGP
45O-linked_GlycosylationGPNQEQVSPLTLLKL
CCCHHHCCCEEEEEC
17.56OGP
48PhosphorylationQEQVSPLTLLKLGNQ
HHHCCCEEEEECCCC
33.1728509920
48O-linked_GlycosylationQEQVSPLTLLKLGNQ
HHHCCCEEEEECCCC
33.17OGP
126N-linked_GlycosylationHLALGAQNHTLQRLQ
HHHHHCCCHHHHHHH
29.58UniProtKB CARBOHYD
126N-linked_GlycosylationHLALGAQNHTLQRLQ
HHHHHCCCHHHHHHH
29.5816335952
250PhosphorylationNKFDPSLTQRDSFHL
CCCCCCCCCCCCCCC
26.3720068231
295N-linked_GlycosylationAHFPFKNNMSFVVLV
EECCCCCCEEEEEEE
28.24UniProtKB CARBOHYD
295N-linked_GlycosylationAHFPFKNNMSFVVLV
EECCCCCCEEEEEEE
28.2416335952
309N-linked_GlycosylationVPTHFEWNVSQVLAN
EECCCCCCHHHHHHH
19.16UniProtKB CARBOHYD
309N-linked_GlycosylationVPTHFEWNVSQVLAN
EECCCCCCHHHHHHH
19.1616335952
316N-linked_GlycosylationNVSQVLANLSWDTLH
CHHHHHHHCCCCCCC
30.37UniProtKB CARBOHYD
316N-linked_GlycosylationNVSQVLANLSWDTLH
CHHHHHHHCCCCCCC
30.372440681
390UbiquitinationTLELSEVGVEAAAAT
EEEHHHHHHHHHHHH
13.9029967540
397O-linked_GlycosylationGVEAAAATSIAMSRM
HHHHHHHHHHHHHHC
18.88OGP
397PhosphorylationGVEAAAATSIAMSRM
HHHHHHHHHHHHHHC
18.88-
398PhosphorylationVEAAAATSIAMSRMS
HHHHHHHHHHHHHCC
12.01-
405PhosphorylationSIAMSRMSLSSFSVN
HHHHHHCCHHHCCCC
24.80-
407PhosphorylationAMSRMSLSSFSVNRP
HHHHCCHHHCCCCCC
23.25-
410PhosphorylationRMSLSSFSVNRPFLF
HCCHHHCCCCCCEEE
22.04-
450PhosphorylationELKEQQDSPGNKDFL
HHHHCCCCCCCHHHH
30.3024505115
454UbiquitinationQQDSPGNKDFLQSLK
CCCCCCCHHHHHHHC
56.6329967540
459PhosphorylationGNKDFLQSLKGFPRG
CCHHHHHHHCCCCCC
33.9124972180
459O-linked_GlycosylationGNKDFLQSLKGFPRG
CCHHHHHHHCCCCCC
33.91OGP
484PhosphorylationVPPMEEDYPQFGSPK
CCCCCCCCCCCCCCC
11.382434496
484SulfationVPPMEEDYPQFGSPK
CCCCCCCCCCCCCCC
11.38-
484SulfationVPPMEEDYPQFGSPK
CCCCCCCCCCCCCCC
11.382434496
489PhosphorylationEDYPQFGSPK-----
CCCCCCCCCC-----
30.7024719451
489O-linked_GlycosylationEDYPQFGSPK-----
CCCCCCCCCC-----
30.70OGP

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 A2AP_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of A2AP_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 A2AP_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CFAD_HUMANCFDphysical
12080056
SSRA_HUMANSSR1physical
21988832

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
262850Alpha-2-plasmin inhibitor deficiency (APLID)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of A2AP_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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-126; ASN-295 AND ASN-309,AND MASS SPECTROMETRY.

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