TFPI1_HUMAN - dbPTM
TFPI1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TFPI1_HUMAN
UniProt AC P10646
Protein Name Tissue factor pathway inhibitor
Gene Name TFPI
Organism Homo sapiens (Human).
Sequence Length 304
Subcellular Localization Isoform Alpha: Secreted.
Isoform Beta: Microsome membrane
Lipid-anchor, GPI-anchor .
Protein Description Inhibits factor X (X(a)) directly and, in a Xa-dependent way, inhibits VIIa/tissue factor activity, presumably by forming a quaternary Xa/LACI/VIIa/TF complex. It possesses an antithrombotic action and also the ability to associate with lipoproteins in plasma..
Protein Sequence MIYTMKKVHALWASVCLLLNLAPAPLNADSEEDEEHTIITDTELPPLKLMHSFCAFKADDGPCKAIMKRFFFNIFTRQCEEFIYGGCEGNQNRFESLEECKKMCTRDNANRIIKTTLQQEKPDFCFLEEDPGICRGYITRYFYNNQTKQCERFKYGGCLGNMNNFETLEECKNICEDGPNGFQVDNYGTQLNAVNNSLTPQSTKVPSLFEFHGPSWCLTPADRGLCRANENRFYYNSVIGKCRPFKYSGCGGNENNFTSKQECLRACKKGFIQRISKGGLIKTKRKRKKQRVKIAYEEIFVKNM
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
30PhosphorylationPAPLNADSEEDEEHT
CCCCCCCCCCCCCCE		40.2426657352
42O-linked_GlycosylationEHTIITDTELPPLKL
CCEECCCCCCCCCHH		30.6719017259
52PhosphorylationPPLKLMHSFCAFKAD
CCCHHHHHHHHEECC		14.1926434776
101AcetylationFESLEECKKMCTRDN
CCCHHHHHHHHCHHC		46.9927452117
115O-linked_GlycosylationNANRIIKTTLQQEKP
CHHHHHHHHHHHCCC		23.4855830519
116O-linked_GlycosylationANRIIKTTLQQEKPD
HHHHHHHHHHHCCCC		19.9855830523
121UbiquitinationKTTLQQEKPDFCFLE
HHHHHHCCCCEEEEE		45.6229967540
139PhosphorylationGICRGYITRYFYNNQ
CCCHHHHHHHHCCCC		15.7229507054
141PhosphorylationCRGYITRYFYNNQTK
CHHHHHHHHCCCCCC		11.1929507054
143PhosphorylationGYITRYFYNNQTKQC
HHHHHHHCCCCCCEE		12.3129507054
145N-linked_GlycosylationITRYFYNNQTKQCER
HHHHHCCCCCCEEEE		39.2519017259
145N-linked_GlycosylationITRYFYNNQTKQCER
HHHHHCCCCCCEEEE		39.2519017259
195N-linked_GlycosylationGTQLNAVNNSLTPQS
HHCHHHCCCCCCCCC		29.9319017259
195N-linked_GlycosylationGTQLNAVNNSLTPQS
HHCHHHCCCCCCCCC		29.9319017259
197 (in isoform 2)Phosphorylation-28.5422210691
202O-linked_GlycosylationNNSLTPQSTKVPSLF
CCCCCCCCCCCCCCE		31.2519017259
202 (in isoform 2)Phosphorylation-31.2522210691
202O-linked_GlycosylationNNSLTPQSTKVPSLF
CCCCCCCCCCCCCCE		31.2519017259
203O-linked_GlycosylationNSLTPQSTKVPSLFE
CCCCCCCCCCCCCEE		30.7119017259
203O-linked_GlycosylationNSLTPQSTKVPSLFE
CCCCCCCCCCCCCEE		30.7119017259
207 (in isoform 2)Phosphorylation-48.9922210691
215PhosphorylationLFEFHGPSWCLTPAD
CEEECCCCEECCHHH		34.7125002506
219PhosphorylationHGPSWCLTPADRGLC
CCCCEECCHHHCCCC		17.1925002506
260UbiquitinationNENNFTSKQECLRAC
CCCCCCCHHHHHHHH		47.2429967540
268AcetylationQECLRACKKGFIQRI
HHHHHHHHHCHHHHH		55.7520167786
269SumoylationECLRACKKGFIQRIS
HHHHHHHHCHHHHHH		59.96-
269SumoylationECLRACKKGFIQRIS
HHHHHHHHCHHHHHH		59.96-
269AcetylationECLRACKKGFIQRIS
HHHHHHHHCHHHHHH		59.9620167786
293SumoylationKRKKQRVKIAYEEIF
HHHHHHHEEEEEEHH		24.65-
293SumoylationKRKKQRVKIAYEEIF
HHHHHHHEEEEEEHH		24.65-
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
30SPhosphorylationKinaseCSNK2A1P68400
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TFPI1_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 TFPI1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TSP1_HUMANTHBS1physical
10922378
A4_HUMANAPPphysical
21832049
KCIP4_HUMANKCNIP4physical
28514442
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 TFPI1_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-145, AND MASSSPECTROMETRY.
"Amino acid sequence and carbohydrate structure of a recombinant humantissue factor pathway inhibitor expressed in Chinese hamster ovarycells: one N- and two O-linked carbohydrate chains are located betweenKunitz domains 2 and 3 and one N-linked carbohydrate chain is inKunitz domain 2.";
Nakahara Y., Miyata T., Hamuro T., Funatsu A., Miyagi M.,Tsunasawa S., Kato H.;
Biochemistry 35:6450-6459(1996).
Cited for: GLYCOSYLATION AT ASN-145; ASN-195; SER-202 AND THR-203.
"Biochemical characterization of plasma-derived tissue factor pathwayinhibitor: post-translational modification of free, full-length formwith particular reference to the sugar chain.";
Mori Y., Hamuro T., Nakashima T., Hamamoto T., Natsuka S., Hase S.,Iwanaga S.;
J. Thromb. Haemost. 7:111-120(2009).
Cited for: PROTEIN SEQUENCE OF 29-304, MASS SPECTROMETRY, AND GLYCOSYLATION ATTHR-42; ASN-145; ASN-195; SER-202 AND THR-203.
O-linked Glycosylation
ReferencePubMed
"Amino acid sequence and carbohydrate structure of a recombinant humantissue factor pathway inhibitor expressed in Chinese hamster ovarycells: one N- and two O-linked carbohydrate chains are located betweenKunitz domains 2 and 3 and one N-linked carbohydrate chain is inKunitz domain 2.";
Nakahara Y., Miyata T., Hamuro T., Funatsu A., Miyagi M.,Tsunasawa S., Kato H.;
Biochemistry 35:6450-6459(1996).
Cited for: GLYCOSYLATION AT ASN-145; ASN-195; SER-202 AND THR-203.
"Biochemical characterization of plasma-derived tissue factor pathwayinhibitor: post-translational modification of free, full-length formwith particular reference to the sugar chain.";
Mori Y., Hamuro T., Nakashima T., Hamamoto T., Natsuka S., Hase S.,Iwanaga S.;
J. Thromb. Haemost. 7:111-120(2009).
Cited for: PROTEIN SEQUENCE OF 29-304, MASS SPECTROMETRY, AND GLYCOSYLATION ATTHR-42; ASN-145; ASN-195; SER-202 AND THR-203.

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