dbPTM

IPSP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IPSP_HUMAN
UniProt AC	P05154
Protein Name	Plasma serine protease inhibitor
Gene Name	SERPINA5
Organism	Homo sapiens (Human).
Sequence Length	406
Subcellular Localization	Secreted, extracellular space . Localized on the plasma membrane overlying the acrosomal head of spermatozoa of ependymal spermatozoa and ejaculated sperm. Localized at the equatorial segment of acrosome-reacted spematozoa. Localized in alpha granule
Protein Description	Heparin-dependent serine protease inhibitor acting in body fluids and secretions. Inactivates serine proteases by binding irreversibly to their serine activation site. Involved in the regulation of intravascular and extravascular proteolytic activities. Plays hemostatic roles in the blood plasma. Acts as a procoagulant and proinflammatory factor by inhibiting the anticoagulant activated protein C factor as well as the generation of activated protein C factor by the thrombin/thrombomodulin complex. Acts as an anticoagulant factor by inhibiting blood coagulation factors like prothrombin, factor XI, factor Xa, plasma kallikrein and fibrinolytic enzymes such as tissue- and urinary-type plasminogen activators. In seminal plasma, inactivates several serine proteases implicated in the reproductive system. Inhibits the serpin acrosin; indirectly protects component of the male genital tract from being degraded by excessive released acrosin. Inhibits tissue-and urinary-type plasminogen activator, prostate-specific antigen and kallikrein activities; has a control on the sperm motility and fertilization. Inhibits the activated protein C-catalyzed degradation of SEMG1 and SEMG2; regulates the degradation of semenogelin during the process of transfer of spermatozoa from the male reproductive tract into the female tract. In urine, inhibits urinary-type plasminogen activator and kallikrein activities. Inactivates membrane-anchored serine proteases activities such as MPRSS7 and TMPRSS11E. Inhibits urinary-type plasminogen activator-dependent tumor cell invasion and metastasis. May also play a non-inhibitory role in seminal plasma and urine as a hydrophobic hormone carrier by its binding to retinoic acid..
Protein Sequence	MQLFLLLCLVLLSPQGASLHRHHPREMKKRVEDLHVGATVAPSSRRDFTFDLYRALASAAPSQSIFFSPVSISMSLAMLSLGAGSSTKMQILEGLGLNLQKSSEKELHRGFQQLLQELNQPRDGFQLSLGNALFTDLVVDLQDTFVSAMKTLYLADTFPTNFRDSAGAMKQINDYVAKQTKGKIVDLLKNLDSNAVVIMVNYIFFKAKWETSFNHKGTQEQDFYVTSETVVRVPMMSREDQYHYLLDRNLSCRVVGVPYQGNATALFILPSEGKMQQVENGLSEKTLRKWLKMFKKRQLELYLPKFSIEGSYQLEKVLPSLGISNVFTSHADLSGISNHSNIQVSEMVHKAVVEVDESGTRAAAATGTIFTFRSARLNSQRLVFNRPFLMFIVDNNILFLGKVNRP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
13	Phosphorylation	LLCLVLLSPQGASLH HHHHHHHCCCCHHHH	15.83	24719451
18	Phosphorylation	LLSPQGASLHRHHPR HHCCCCHHHHHCCCH	31.37	24719451
39	O-linked_Glycosylation	EDLHVGATVAPSSRR HHCCCCCEECCCCCC	15.98	22171320
44	O-linked_Glycosylation	GATVAPSSRRDFTFD CCEECCCCCCCCHHH	30.21	OGP
218	Phosphorylation	TSFNHKGTQEQDFYV ECCCCCCCCEEEEEE	33.46	-
242	Phosphorylation	MMSREDQYHYLLDRN CCCCHHHHHHHHCCC	12.54	26657352
249	N-linked_Glycosylation	YHYLLDRNLSCRVVG HHHHHCCCCCEEEEE	35.65	11583740
249	N-linked_Glycosylation	YHYLLDRNLSCRVVG HHHHHCCCCCEEEEE	35.65	11583740
251	Phosphorylation	YLLDRNLSCRVVGVP HHHCCCCCEEEEEEE	11.92	26657352
259	Phosphorylation	CRVVGVPYQGNATAL EEEEEEECCCCEEEE	27.01	26657352
262	N-linked_Glycosylation	VGVPYQGNATALFIL EEEECCCCEEEEEEE	20.70	11583740
262	N-linked_Glycosylation	VGVPYQGNATALFIL EEEECCCCEEEEEEE	20.70	11583740
338	N-linked_Glycosylation	ADLSGISNHSNIQVS HHHCCCCCCCCCCHH	40.46	16335952
338	N-linked_Glycosylation	ADLSGISNHSNIQVS HHHCCCCCCCCCCHH	40.46	11583740
366	O-linked_Glycosylation	GTRAAAATGTIFTFR CCHHCCCCCCEEEEE	30.08	OGP
368	O-linked_Glycosylation	RAAAATGTIFTFRSA HHCCCCCCEEEEECH	14.46	OGP
371	O-linked_Glycosylation	AATGTIFTFRSARLN CCCCCEEEEECHHCC	17.81	OGP

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 IPSP_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CSN6_HUMAN	COPS6	physical	16169070
ACRO_HUMAN	ACR	physical	7521127
KLKB1_HUMAN	KLKB1	physical	2551064
PROC_HUMAN	PROC	physical	2551064
UROK_HUMAN	PLAU	physical	2551064
TPA_HUMAN	PLAT	physical	2551064
FA11_HUMAN	F11	physical	2551064
KLK3_HUMAN	KLK3	physical	7509746
WWOX_HUMAN	WWOX	physical	28514442
FURIN_HUMAN	FURIN	physical	28514442
HGFA_HUMAN	HGFAC	physical	28514442
CTGE5_HUMAN	CTAGE5	physical	28514442
ZZEF1_HUMAN	ZZEF1	physical	28514442
TGO1_HUMAN	MIA3	physical	28514442
HECD3_HUMAN	HECTD3	physical	28514442
CALX_HUMAN	CANX	physical	28514442
FBX2_HUMAN	FBXO2	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
DB00055	Drotrecogin alfa
DB00013	Urokinase

Regulatory Network of IPSP_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Crystal structure of protein C inhibitor provides insights intohormone binding and heparin activation."; Huntington J.A., Kjellberg M., Stenflo J.; Structure 11:205-215(2003). Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 30-406, AND GLYCOSYLATION ATASN-262.	12575940 [Abstract]
"N-glycans and the N terminus of protein C inhibitor affect thecofactor-enhanced rates of thrombin inhibition."; Sun W., Parry S., Panico M., Morris H.R., Kjellberg M., Engstrom A.,Dell A., Schedin-Weiss S.; J. Biol. Chem. 283:18601-18611(2008). Cited for: FUNCTION, PROTEOLYTIC CLEAVAGE, GLYCOSYLATION AT ASN-249; ASN-262 ANDASN-338, STRUCTURE OF CARBOHYDRATES, SUBCELLULAR LOCATION, TISSUESPECIFICITY, AND MASS SPECTROMETRY.	18467335 [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-262 AND ASN-338, AND MASSSPECTROMETRY.	16335952 [Abstract]
"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-249, AND MASSSPECTROMETRY.	14760718 [Abstract]
O-linked Glycosylation
Reference	PubMed
"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 THR-39, STRUCTURE OF CARBOHYDRATES, AND MASSSPECTROMETRY.	22171320 [Abstract]
"Further insight into the roles of the glycans attached to human bloodprotein C inhibitor."; Sun W., Parry S., Ubhayasekera W., Engstrom A., Dell A.,Schedin-Weiss S.; Biochem. Biophys. Res. Commun. 403:198-202(2010). Cited for: GLYCOSYLATION AT THR-39, AND MASS SPECTROMETRY.	21056543 [Abstract]