dbPTM

ZPI_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ZPI_HUMAN
UniProt AC	Q9UK55
Protein Name	Protein Z-dependent protease inhibitor
Gene Name	SERPINA10
Organism	Homo sapiens (Human).
Sequence Length	444
Subcellular Localization	Secreted.
Protein Description	Inhibits activity of the coagulation protease factor Xa in the presence of PROZ, calcium and phospholipids. Also inhibits factor XIa in the absence of cofactors..
Protein Sequence	MKVVPSLLLSVLLAQVWLVPGLAPSPQSPETPAPQNQTSRVVQAPKEEEEDEQEASEEKASEEEKAWLMASRQQLAKETSNFGFSLLRKISMRHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQALKPTKPGLLPSLFKGLRETLSRNLELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFDEINPETKLILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNATMLVVLMEKMGDHLALEDYLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSATGRNLQVSRVLQRTVIEVDERGTEAVAGILSEITAYSMPPVIKVDRPFHFMIYEETSGMLLFLGRVVNPTLL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
36	N-linked_Glycosylation	PETPAPQNQTSRVVQ CCCCCCCCCCCCEEE	46.14	19159218
56	Phosphorylation	EEDEQEASEEKASEE HHHHHHHHHHHHCHH	45.60	10460162
61	Phosphorylation	EASEEKASEEEKAWL HHHHHHHCHHHHHHH	57.52	23911959
79	Phosphorylation	RQQLAKETSNFGFSL HHHHHHHHCCCCHHH	28.41	23403867
80	Phosphorylation	QQLAKETSNFGFSLL HHHHHHHCCCCHHHH	31.11	23403867
85	Phosphorylation	ETSNFGFSLLRKISM HHCCCCHHHHHHHHC	27.20	23403867
91	Phosphorylation	FSLLRKISMRHDGNM HHHHHHHHCCCCCCE	16.88	24719451
101	Phosphorylation	HDGNMVFSPFGMSLA CCCCEEECCCHHHHH	14.12	24275569
106	Phosphorylation	VFSPFGMSLAMTGLM EECCCHHHHHHHHHH	17.23	24275569
143	Phosphorylation	TKPGLLPSLFKGLRE CCCCCHHHHHHHHHH	46.54	24719451
180	N-linked_Glycosylation	DVKETFFNLSKRYFD CHHHHHHEHHHHHCC	38.93	16335952
180	N-linked_Glycosylation	DVKETFFNLSKRYFD CHHHHHHEHHHHHCC	38.93	17623646
197	N-linked_Glycosylation	CVPMNFRNASQAKRL CCCCCCCCHHHHHHH	39.54	20427285
235	Phosphorylation	TKLILVDYILFKGKW CCEEEEEEEECCCCC	7.64	23917254
292	Phosphorylation	CHVLKLPYQGNATML EEEEECCCCCCEEEE	39.22	19835603
295	N-linked_Glycosylation	LKLPYQGNATMLVVL EECCCCCCEEEEEEE	19.40	16335952
297	Phosphorylation	LPYQGNATMLVVLME CCCCCCEEEEEEEHH	18.29	19835603

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
56	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ZPI_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 ZPI_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PSB7_HUMAN	PSMB7	physical	18768472
TPA_HUMAN	PLAT	physical	28514442
TGO1_HUMAN	MIA3	physical	28514442
CTGE5_HUMAN	CTAGE5	physical	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 ZPI_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"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-36, AND MASS SPECTROMETRY.	19159218 [Abstract]
"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-180 AND ASN-295, AND MASSSPECTROMETRY.	16335952 [Abstract]
Phosphorylation
Reference	PubMed
"An initial characterization of the serum phosphoproteome."; Zhou W., Ross M.M., Tessitore A., Ornstein D., Vanmeter A.,Liotta L.A., Petricoin E.F. III; J. Proteome Res. 8:5523-5531(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56 AND SER-61, TISSUESPECIFICITY, AND MASS SPECTROMETRY.	19824718 [Abstract]