THRB_HUMAN - dbPTM
THRB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID THRB_HUMAN
UniProt AC P00734
Protein Name Prothrombin
Gene Name F2
Organism Homo sapiens (Human).
Sequence Length 622
Subcellular Localization Secreted, extracellular space.
Protein Description Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing..
Protein Sequence MAHVRGLQLPGCLALAALCSLVHSQHVFLAPQQARSLLQRVRRANTFLEEVRKGNLERECVEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHVNITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQECSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASAQAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETGDGLDEDSDRAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDQFGE
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
49Gamma-carboxyglutamic_acidRRANTFLEEVRKGNL
HHHHHHHHHHHCCCC		50.703759958
494-carboxyglutamateRRANTFLEEVRKGNL
HHHHHHHHHHHCCCC		50.70-
49Gamma-carboxyglutamic_acidRRANTFLEEVRKGNL
HHHHHHHHHHHCCCC		50.706305407
50Gamma-carboxyglutamic_acidRANTFLEEVRKGNLE
HHHHHHHHHHCCCCH		50.173759958
50Gamma-carboxyglutamic_acidRANTFLEEVRKGNLE
HHHHHHHHHHCCCCH		50.176305407
504-carboxyglutamateRANTFLEEVRKGNLE
HHHHHHHHHHCCCCH		50.17-
57Gamma-carboxyglutamic_acidEVRKGNLERECVEET
HHHCCCCHHHHHHHH		50.896305407
57Gamma-carboxyglutamic_acidEVRKGNLERECVEET
HHHCCCCHHHHHHHH		50.896305407
574-carboxyglutamateEVRKGNLERECVEET
HHHCCCCHHHHHHHH		50.89-
59Gamma-carboxyglutamic_acidRKGNLERECVEETCS
HCCCCHHHHHHHHCC		33.276305407
594-carboxyglutamateRKGNLERECVEETCS
HCCCCHHHHHHHHCC		33.27-
59Gamma-carboxyglutamic_acidRKGNLERECVEETCS
HCCCCHHHHHHHHCC		33.276305407
62Gamma-carboxyglutamic_acidNLERECVEETCSYEE
CCHHHHHHHHCCHHH		60.286305407
62Gamma-carboxyglutamic_acidNLERECVEETCSYEE
CCHHHHHHHHCCHHH		60.286305407
624-carboxyglutamateNLERECVEETCSYEE
CCHHHHHHHHCCHHH		60.28-
634-carboxyglutamateLERECVEETCSYEEA
CHHHHHHHHCCHHHH		34.42-
63Gamma-carboxyglutamic_acidLERECVEETCSYEEA
CHHHHHHHHCCHHHH		34.426305407
63Gamma-carboxyglutamic_acidLERECVEETCSYEEA
CHHHHHHHHCCHHHH		34.426305407
684-carboxyglutamateVEETCSYEEAFEALE
HHHHCCHHHHHHHHH		26.93-
68Gamma-carboxyglutamic_acidVEETCSYEEAFEALE
HHHHCCHHHHHHHHH		26.936305407
68Gamma-carboxyglutamic_acidVEETCSYEEAFEALE
HHHHCCHHHHHHHHH		26.936305407
694-carboxyglutamateEETCSYEEAFEALES
HHHCCHHHHHHHHHC		50.88-
69Gamma-carboxyglutamic_acidEETCSYEEAFEALES
HHHCCHHHHHHHHHC		50.886305407
69Gamma-carboxyglutamic_acidEETCSYEEAFEALES
HHHCCHHHHHHHHHC		50.886305407
724-carboxyglutamateCSYEEAFEALESSTA
CCHHHHHHHHHCCCH		60.43-
72Gamma-carboxyglutamic_acidCSYEEAFEALESSTA
CCHHHHHHHHHCCCH		60.436305407
72Gamma-carboxyglutamic_acidCSYEEAFEALESSTA
CCHHHHHHHHHCCCH		60.436305407
754-carboxyglutamateEEAFEALESSTATDV
HHHHHHHHCCCHHHH		50.09-
75Gamma-carboxyglutamic_acidEEAFEALESSTATDV
HHHHHHHHCCCHHHH		50.096305407
75Gamma-carboxyglutamic_acidEEAFEALESSTATDV
HHHHHHHHCCCHHHH		50.096305407
78O-linked_GlycosylationFEALESSTATDVFWA
HHHHHCCCHHHHHHH		42.74OGP
121N-linked_GlycosylationTNYRGHVNITRSGIE
CCCCCCEEEECCCEE		25.0022171320
121N-linked_GlycosylationTNYRGHVNITRSGIE
CCCCCCEEEECCCEE		25.0016335952
125PhosphorylationGHVNITRSGIECQLW
CCEEEECCCEEEEEE		35.1624505115
134PhosphorylationIECQLWRSRYPHKPE
EEEEEEHHCCCCCCC		25.2824505115
143N-linked_GlycosylationYPHKPEINSTTHPGA
CCCCCCCCCCCCCCC		31.4822171320
143N-linked_GlycosylationYPHKPEINSTTHPGA
CCCCCCCCCCCCCCC		31.4816335952
144PhosphorylationPHKPEINSTTHPGAD
CCCCCCCCCCCCCCC		40.1024505115
145O-linked_GlycosylationHKPEINSTTHPGADL
CCCCCCCCCCCCCCH		25.33OGP
192O-linked_GlycosylationVCGQDQVTVAMTPRS
CCCCCEEEEEECCCC		9.27OGP
196O-linked_GlycosylationDQVTVAMTPRSEGSS
CEEEEEECCCCCCCC		13.05OGP
199O-linked_GlycosylationTVAMTPRSEGSSVNL
EEEECCCCCCCCCCC		47.73OGP
199PhosphorylationTVAMTPRSEGSSVNL
EEEECCCCCCCCCCC		47.7324505115
202PhosphorylationMTPRSEGSSVNLSPP
ECCCCCCCCCCCCCC		27.3624505115
203PhosphorylationTPRSEGSSVNLSPPL
CCCCCCCCCCCCCCH		26.3624505115
207PhosphorylationEGSSVNLSPPLEQCV
CCCCCCCCCCHHHCC		21.1924275569
207O-linked_GlycosylationEGSSVNLSPPLEQCV
CCCCCCCCCCHHHCC		21.19OGP
315O-linked_GlycosylationDRAIEGRTATSEYQT
HHHHCCCCCCCCCCC		45.18OGP
317O-linked_GlycosylationAIEGRTATSEYQTFF
HHCCCCCCCCCCCCC		22.83OGP
317PhosphorylationAIEGRTATSEYQTFF
HHCCCCCCCCCCCCC		22.8324505115
318PhosphorylationIEGRTATSEYQTFFN
HCCCCCCCCCCCCCC		31.6624505115
320PhosphorylationGRTATSEYQTFFNPR
CCCCCCCCCCCCCCC		16.78-
331PhosphorylationFNPRTFGSGEADCGL
CCCCCCCCCCCCCCC		29.3024505115
416N-linked_GlycosylationLYPPWDKNFTENDLL
HCCCCCCCCCCCCEE		46.7518638581
434PhosphorylationGKHSRTRYERNIEKI
CCCCCCHHHHHHHHH		20.73-
539PhosphorylationERPVCKDSTRIRITD
ECCCCCCCCEEEEEC		12.7020068231
540PhosphorylationRPVCKDSTRIRITDN
CCCCCCCCEEEEECC		40.0020068231
553NitrationDNMFCAGYKPDEGKR
CCEEECCCCCCCCCC		10.79-
599AcetylationEGCDRDGKYGFYTHV
CCCCCCCCCEEEHHH		46.6330591549
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 THRB_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of THRB_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
143N-linked Glycosylation149 (6)T ⇒ R;Mrs5896
  • Intraocular pressure
29617998
143N-linked Glycosylation149 (6)T ⇒ R;Mrs5896
  • Intraocular pressure
29617998
153N-linked Glycosylation149 (4)T ⇒ R;Mrs5896
  • Intraocular pressure
29617998
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PAI1_HUMANSERPINE1physical
12709053
FIBA_HUMANFGAphysical
1587268
HEP2_HUMANSERPIND1physical
12169660
CBPB2_HUMANCPB2physical
8663147
TRBM_HUMANTHBDphysical
8663147
FA5_HUMANF5physical
9032460
IC1_HUMANSERPING1physical
11460008
F10A1_HUMANST13physical
11687574
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613679Factor II deficiency (FA2D)
601367Ischemic stroke (ISCHSTR)
188050Thrombophilia due to thrombin defect (THPH1)
614390Pregnancy loss, recurrent, 2 (RPRGL2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of THRB_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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 ASN-121 AND ASN-143, STRUCTURE OF CARBOHYDRATES, ANDMASS SPECTROMETRY.
"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-416, CARBOHYDRATESTRUCTURE, AND MASS SPECTROMETRY.
"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-416, AND MASSSPECTROMETRY.
"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-121; ASN-143 AND ASN-416,AND MASS SPECTROMETRY.
"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-121 AND ASN-143, AND MASSSPECTROMETRY.

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