dbPTM

ANT3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ANT3_HUMAN
UniProt AC	P01008
Protein Name	Antithrombin-III
Gene Name	SERPINC1
Organism	Homo sapiens (Human).
Sequence Length	464
Subcellular Localization	Secreted, extracellular space.
Protein Description	Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade. AT-III inhibits thrombin, matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa. Its inhibitory activity is greatly enhanced in the presence of heparin..
Protein Sequence	MYSNVIGTVTSGKRKVYLLSLLLIGFWDCVTCHGSPVDICTAKPRDIPMNPMCIYRSPEKKATEDEGSEQKIPEATNRRVWELSKANSRFATTFYQHLADSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKTSDQIHFFFAKLNCRLYRKANKSSKLVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKENAEQSRAAINKWVSNKTEGRITDVIPSEAINELTVLVLVNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFRYRRVAEGTQVLELPFKGDDITMVLILPKPEKSLAKVEKELTPEVLQEWLDELEEMMLVVHMPRFRIEDGFSLKEQLQDMGLVDLFSPEKSKLPGIVAEGRDDLYVSDAFHKAFLEVNEEGSEAAASTAVVIAGRSLNPNRVTFKANRPFLVFIREVPLNTIIFMGRVANPCVK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Phosphorylation	SNVIGTVTSGKRKVY CCCCEECCCCCHHHH	31.44	-
35	O-linked_Glycosylation	DCVTCHGSPVDICTA HHHCCCCCCCCCCCC	9.70	11570846
35	Phosphorylation	DCVTCHGSPVDICTA HHHCCCCCCCCCCCC	9.70	24505115
41	O-linked_Glycosylation	GSPVDICTAKPRDIP CCCCCCCCCCCCCCC	37.74	11570846
57	Phosphorylation	NPMCIYRSPEKKATE CCEEEEECCCCCCCC	22.05	-
63	Phosphorylation	RSPEKKATEDEGSEQ ECCCCCCCCCCCCCC	53.50	23927012
68	Phosphorylation	KATEDEGSEQKIPEA CCCCCCCCCCCCCHH	34.50	7832187
128	N-linked_Glycosylation	MTKLGACNDTLQQLM HHHHCCCCHHHHHHH	44.78	14760718
128	N-linked_Glycosylation	MTKLGACNDTLQQLM HHHHCCCCHHHHHHH	44.78	17623646
167	N-linked_Glycosylation	CRLYRKANKSSKLVS HHHHHHCCCCCCCEE	48.02	7599134
167	N-linked_Glycosylation	CRLYRKANKSSKLVS HHHHHHCCCCCCCEE	48.02	7599134
174	Phosphorylation	NKSSKLVSANRLFGD CCCCCCEECCHHHCC	30.20	20068231
187	N-linked_Glycosylation	GDKSLTFNETYQDIS CCCCCCCCCHHHHHH	35.15	15084671
187	N-linked_Glycosylation	GDKSLTFNETYQDIS CCCCCCCCCHHHHHH	35.15	15084671
214	Phosphorylation	FKENAEQSRAAINKW HHHCHHHHHHHHHHH	18.52	-
223	Phosphorylation	AAINKWVSNKTEGRI HHHHHHHCCCCCCCC	31.34	22468782
224	N-linked_Glycosylation	AINKWVSNKTEGRIT HHHHHHCCCCCCCCC	45.72	7599134
224	N-linked_Glycosylation	AINKWVSNKTEGRIT HHHHHHCCCCCCCCC	45.72	16263699
226	Phosphorylation	NKWVSNKTEGRITDV HHHHCCCCCCCCCEE	48.17	22468782
236	Phosphorylation	RITDVIPSEAINELT CCCEECCHHHHHHHH	28.65	22468782
272	Phosphorylation	NTRKELFYKADGESC CHHCCEEEECCCCCC	20.21	-
278	Phosphorylation	FYKADGESCSASMMY EEECCCCCCCEECCE	20.92	24505115
280	Phosphorylation	KADGESCSASMMYQE ECCCCCCCEECCEEC	32.43	24505115
418	O-linked_Glycosylation	GSEAAASTAVVIAGR HCHHHHEEEEEEECC	20.81	OGP
426	Phosphorylation	AVVIAGRSLNPNRVT EEEEECCCCCCCCEE	31.42	28258704
433	Phosphorylation	SLNPNRVTFKANRPF CCCCCCEEEEECCCE	19.04	28258704

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
63	T	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot
68	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 ANT3_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 ANT3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TBB8_HUMAN	TUBB8	physical	26186194
TBB1_HUMAN	TUBB1	physical	26186194
TEX15_HUMAN	TEX15	physical	26186194
OS9_HUMAN	OS9	physical	26186194
ISCA2_HUMAN	ISCA2	physical	26186194
SUCA_HUMAN	SUCLG1	physical	26186194
BTD_HUMAN	BTD	physical	26186194
PUR4_HUMAN	PFAS	physical	26344197
TBB1_HUMAN	TUBB1	physical	28514442
TEX15_HUMAN	TEX15	physical	28514442
BTD_HUMAN	BTD	physical	28514442
SUCA_HUMAN	SUCLG1	physical	28514442
OS9_HUMAN	OS9	physical	28514442
CBWD1_HUMAN	CBWD1	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613118	Antithrombin III deficiency (AT3D)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ANT3_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Enrichment of glycopeptides for glycan structure and attachment siteidentification."; Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,Brinkmalm G., Larson G.; Nat. Methods 6:809-811(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-187, STRUCTURE OFCARBOHYDRATES, AND MASS SPECTROMETRY.	19838169 [Abstract]
"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-128 AND ASN-187, AND MASSSPECTROMETRY.	19159218 [Abstract]
"Elucidation of N-glycosylation sites on human platelet proteins: aglycoproteomic approach."; Lewandrowski U., Moebius J., Walter U., Sickmann A.; Mol. Cell. Proteomics 5:226-233(2006). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-224, AND MASSSPECTROMETRY.	16263699 [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-128; ASN-187 AND ASN-224,AND MASS SPECTROMETRY.	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-128 AND ASN-187, AND MASSSPECTROMETRY.	14760718 [Abstract]
"A proteomic analysis of human bile."; Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H.,Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.; Mol. Cell. Proteomics 3:715-728(2004). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-187, AND MASSSPECTROMETRY.	15084671 [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-68, TISSUE SPECIFICITY,AND MASS SPECTROMETRY.	19824718 [Abstract]