Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Prothrombin  

UniProtKB / Swiss-Prot ID :  THRB_HUMAN

Gene Name (Synonyms) : 
F2  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Secreted, extracellular space. 

Protein Function :  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 MAHVRGLQLPGCLALAALCSLVHSQHVFLAPQQARSLLQRVRRANTFLEEVRKGNLERECVEETCSYEEA...
Predicted Secondary Structure CCCCCHHHHHHHHHHHHHHHCCCCCCEECCCHHHHHHCCCCCCCCCCCCCCCCCCEEEEEECCCCCCCCC...
Protein Variant
LocationDescription
72E -> G (in FA2D; Shanghai). VAR_055232
165T -> M (in dbSNP:rs5896). VAR_011781
200E -> K (in FA2D; prothrombin type 3). VAR_006711
314R -> C (in FA2D; Barcelona/Madrid). VAR_006712
314R -> H (in FA2D; Padua-1). VAR_006713
380M -> T (in FA2D; Himi-1). VAR_006714
386P -> T (in dbSNP:rs5897). VAR_011782
425R -> C (in FA2D; Quick-1). VAR_006715
431R -> H (in FA2D; Himi-2). VAR_006716
461R -> W (in FA2D; Tokushima). VAR_006717
509E -> A (in FA2D; Salakta/Frankfurt). VAR_006718
601G -> V (in FA2D; Quick-2). VAR_006719
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
494-carboxyglutamateNTFLEEVRK
CCCCCCCCC
50.70HPRD
Link-
494-carboxyglutamate.NTFLEEVRK
CCCCCCCCC
50.70UniProtKB
Link-
504-carboxyglutamateTFLEEVRKG
CCCCCCCCC
50.17HPRD
Link-
504-carboxyglutamate.TFLEEVRKG
CCCCCCCCC
50.17UniProtKB
Link-
574-carboxyglutamateKGNLERECV
CCCEEEEEE
50.89HPRD
Link-
574-carboxyglutamate.KGNLERECV
CCCEEEEEE
50.89UniProtKB
Link-
594-carboxyglutamateNLERECVEE
CEEEEEECC
33.27HPRD
Link-
594-carboxyglutamate.NLERECVEE
CEEEEEECC
33.27UniProtKB
Link-
624-carboxyglutamateRECVEETCS
EEEECCCCC
60.28HPRD
Link-
624-carboxyglutamate.RECVEETCS
EEEECCCCC
60.28UniProtKB
Link-
634-carboxyglutamateECVEETCSY
EEECCCCCC
34.42HPRD
Link-
634-carboxyglutamate.ECVEETCSY
EEECCCCCC
34.42UniProtKB
Link-
684-carboxyglutamateTCSYEEAFE
CCCCCCCCE
26.93HPRD
Link-
684-carboxyglutamate.TCSYEEAFE
CCCCCCCCE
26.93UniProtKB
Link-
694-carboxyglutamateCSYEEAFEA
CCCCCCCEE
50.88HPRD
Link-
694-carboxyglutamate.CSYEEAFEA
CCCCCCCEE
50.88UniProtKB
Link-
724-carboxyglutamateEEAFEALES
CCCCEEECC
60.43HPRD
Link-
724-carboxyglutamate.EEAFEALES
CCCCEEECC
60.43UniProtKB
Link-
754-carboxyglutamateFEALESSTA
CEEECCCCC
50.09HPRD
Link-
754-carboxyglutamate.FEALESSTA
CEEECCCCC
50.09UniProtKB
Link-
121N-linked (Glc...)RGHVNITRS
EEEECCCCC
25.00HPRD
Link-
121N-linked (GlcNAc...) (complex).RGHVNITRS
EEEECCCCC
25.00UniProtKB
Link-
143N-linked (Glc...)KPEINSTTH
CCCCCCCCC
31.48HPRD
Link-
143N-linked (GlcNAc...)KPEINSTTH
CCCCCCCCC
31.48SysPTM
Link-
143N-linked (GlcNAc...) (complex).KPEINSTTH
CCCCCCCCC
31.48UniProtKB
Link-
198noneAMTPRSEGS
CCCCCCCCC
37.87HPRD
Link-
314noneAIEGRTATS
CCCEEECCC
14.38HPRD
Link-
327noneFFNPRTFGS
ECCCCCCCC
43.73HPRD
Link
416N-linked (GlcNAc...)PWDKNFTEN
CCCCCCCCC
46.75SysPTM
Link-
416N-linked (GlcNAc...) (complex).PWDKNFTEN
CCCCCCCCC
46.75UniProtKB
Link-
436noneTRYERNIEK
CCCCCCCEE
40.26HPRD
Link-
539PhosphoserineVCKDSTRIR
HHHHHCCCC
12.70HPRD
Link-
539PhosphoserineVCKDSTRIR
HHHHHCCCC
12.70Phosphositeplus
Link-
540PhosphothreonineCKDSTRIRI
HHHHCCCCC
40.00HPRD
Link-
540PhosphothreonineCKDSTRIRI
HHHHCCCCC
40.00Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
ANT3_HUMANin vitroHPRD:01488HPRD3800906
11927130
7238875
F13A_HUMANin vitroHPRD:01488HPRD9546612
FIBA_HUMANin vitroHPRD:01488HPRD2133223
1587268
2742826
HEP2_HUMANin vitroHPRD:01488HPRD2760054
SPB6_HUMANin vitroHPRD:01488HPRD8415716
9851866
7548163
PAI1_HUMANin vitroHPRD:01488HPRD10543954
PROC_HUMANin vitroHPRD:01488HPRD2544585
AMBP_HUMANin vivoHPRD:01488HPRD9183005
PROS_HUMANin vitroHPRD:01488HPRD12490286
PAR1_HUMANin vivoHPRD:01488HPRD10644723
12563219
9058715
10978167
SNAT_HUMANin vitroHPRD:01488HPRD11427721
CBPB2_HUMANin vitroHPRD:01488HPRD10777524
ARK72_HUMANin vitro
in vivo
HPRD:01488HPRD9576847
HGFA_HUMANin vitroHPRD:01488HPRD8226803
F10A1_HUMANin vitroHPRD:01488HPRD11687574
OSTP_HUMANin vivoHPRD:01488HPRD11375993
PROZ_HUMANin vitroHPRD:01488HPRD2040612
1872862
UROK_HUMANin vivoHPRD:01488HPRD10996659
8428004
THRB_HUMANin vitroHPRD:01488HPRD8071320
PAR2_HUMANin vitroHPRD:01488HPRD10978167
HEP2_HUMANENSP00000308541STRING
FA9_HUMANENSP00000308541STRING
VKGC_HUMANENSP00000308541STRING
PROC_HUMANENSP00000308541STRING
VWF_HUMANENSP00000308541STRING
FA11_HUMANENSP00000308541STRING
F13A_HUMANENSP00000308541STRING
FURIN_HUMANENSP00000308541STRING
PAR3_HUMANENSP00000308541STRING
GPIX_HUMANENSP00000308541STRING
FIBB_HUMANENSP00000308541STRING
FIBA_HUMANENSP00000308541STRING
GPV_HUMANENSP00000308541STRING
PAR1_HUMANENSP00000308541STRING
GP1BA_HUMANENSP00000308541STRING
PROS_HUMANENSP00000308541STRING
FIBG_HUMANENSP00000308541STRING
SPB6_HUMANENSP00000308541STRING
SPB6_HUMANENSP00000308541STRING
FA8_HUMANENSP00000308541STRING
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Disease Reference
Kegg disease
OMIM disease
613679Factor II deficiency (FA2D)
601367Ischemic stroke (ISCHSTR)
188050Thrombophilia due to thrombin defect (THPH1)
614390Pregnancy loss, recurrent, 2 (RPRGL2)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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.
"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.
"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.
"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.
"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.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures