dbPTM

HEP2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HEP2_HUMAN
UniProt AC	P05546
Protein Name	Heparin cofactor 2
Gene Name	SERPIND1
Organism	Homo sapiens (Human).
Sequence Length	499
Subcellular Localization
Protein Description	Thrombin inhibitor activated by the glycosaminoglycans, heparin or dermatan sulfate. In the presence of the latter, HC-II becomes the predominant thrombin inhibitor in place of antithrombin III (AT-III). Also inhibits chymotrypsin, but in a glycosaminoglycan-independent manner.; Peptides at the N-terminal of HC-II have chemotactic activity for both monocytes and neutrophils..
Protein Sequence	MKHSLNALLIFLIITSAWGGSKGPLDQLEKGGETAQSADPQWEQLNNKNLSMPLLPADFHKENTVTNDWIPEGEEDDDYLDLEKIFSEDDDYIDIVDSLSVSPTDSDVSAGNILQLFHGKSRIQRLNILNAKFAFNLYRVLKDQVNTFDNIFIAPVGISTAMGMISLGLKGETHEQVHSILHFKDFVNASSKYEITTIHNLFRKLTHRLFRRNFGYTLRSVNDLYIQKQFPILLDFKTKVREYYFAEAQIADFSDPAFISKTNNHIMKLTKGLIKDALENIDPATQMMILNCIYFKGSWVNKFPVEMTHNHNFRLNEREVVKVSMMQTKGNFLAANDQELDCDILQLEYVGGISMLIVVPHKMSGMKTLEAQLTPRVVERWQKSMTNRTREVLLPKFKLEKNYNLVESLKLMGIRMLFDKNGNMAGISDQRIAIDLFKHQGTITVNEEGTQATTVTTVGFMPLSTQVRFTVDRPFLFLIYEHRTSCLLFMGRVANPSRS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
21	Phosphorylation	ITSAWGGSKGPLDQL HHHHCCCCCCHHHHH	30.42	24505115
34	O-linked_Glycosylation	QLEKGGETAQSADPQ HHHHCCCCCHHCCHH	33.02	OGP
34	Phosphorylation	QLEKGGETAQSADPQ HHHHCCCCCHHCCHH	33.02	24505115
37	Phosphorylation	KGGETAQSADPQWEQ HCCCCCHHCCHHHHH	31.98	27130503
37	O-linked_Glycosylation	KGGETAQSADPQWEQ HCCCCCHHCCHHHHH	31.98	OGP
49	N-linked_Glycosylation	WEQLNNKNLSMPLLP HHHHCCCCCCCCCCC	39.20	11846800
49	N-linked_Glycosylation	WEQLNNKNLSMPLLP HHHHCCCCCCCCCCC	39.20	11846800
51	O-linked_Glycosylation	QLNNKNLSMPLLPAD HHCCCCCCCCCCCCC	27.96	OGP
64	Phosphorylation	ADFHKENTVTNDWIP CCCCCCCCCCCCCCC	29.78	22673903
66	Phosphorylation	FHKENTVTNDWIPEG CCCCCCCCCCCCCCC	25.97	22673903
79	Phosphorylation	EGEEDDDYLDLEKIF CCCCCCCCCCHHHHC	14.76	22673903
79	Sulfation	EGEEDDDYLDLEKIF CCCCCCCCCCHHHHC	14.76	-
79	Sulfation	EGEEDDDYLDLEKIF CCCCCCCCCCHHHHC	14.76	12169660
92	Sulfation	IFSEDDDYIDIVDSL HCCCCCCCEEEEHHH	13.90	12169660
92	Sulfation	IFSEDDDYIDIVDSL HCCCCCCCEEEEHHH	13.90	-
100	O-linked_Glycosylation	IDIVDSLSVSPTDSD EEEEHHHCCCCCCCC	25.22	OGP
102	O-linked_Glycosylation	IVDSLSVSPTDSDVS EEHHHCCCCCCCCCC	20.78	OGP
104	O-linked_Glycosylation	DSLSVSPTDSDVSAG HHHCCCCCCCCCCHH	40.40	OGP
138	Phosphorylation	AKFAFNLYRVLKDQV HHHHHHHHHHHHHHH	10.36	-
188	N-linked_Glycosylation	LHFKDFVNASSKYEI HCHHHHCCCCCCCCH	33.81	11846800
188	N-linked_Glycosylation	LHFKDFVNASSKYEI HCHHHHCCCCCCCCH	33.81	12169660
217	Phosphorylation	FRRNFGYTLRSVNDL HHHHCCCEEEEHHHH	18.97	24719451
328	O-linked_Glycosylation	VKVSMMQTKGNFLAA EEEEEEECCCCEEEC	24.03	31492838
374	Phosphorylation	KTLEAQLTPRVVERW CHHHHHCCHHHHHHH	9.29	29083192
387	N-linked_Glycosylation	RWQKSMTNRTREVLL HHHHHCCCCCHHHHH	34.38	11846800
387	N-linked_Glycosylation	RWQKSMTNRTREVLL HHHHHCCCCCHHHHH	34.38	11846800
444	Phosphorylation	FKHQGTITVNEEGTQ HHCCCEEEECCCCCE	19.67	22210691
450	Phosphorylation	ITVNEEGTQATTVTT EEECCCCCEEEEEEE	20.50	22210691
453	O-linked_Glycosylation	NEEGTQATTVTTVGF CCCCCEEEEEEEEEE	16.39	OGP
454	O-linked_Glycosylation	EEGTQATTVTTVGFM CCCCEEEEEEEEEEE	20.90	OGP
457	O-linked_Glycosylation	TQATTVTTVGFMPLS CEEEEEEEEEEEECC	17.81	OGP
465	Phosphorylation	VGFMPLSTQVRFTVD EEEEECCCEEEEEEC	38.47	22210691

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
37	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 HEP2_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 HEP2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
A4_HUMAN	APP	physical	21832049
VAT1L_HUMAN	VAT1L	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612356	Thrombophilia due to heparin cofactor 2 deficiency (THPH10)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00407	Ardeparin
DB06271	Sulodexide

Regulatory Network of HEP2_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-49 AND ASN-188, AND MASSSPECTROMETRY.	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-49 AND ASN-188, 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-37, TISSUE SPECIFICITY,AND MASS SPECTROMETRY.	19824718 [Abstract]