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Protein S

May 07, 2024

Protein S (also known as PROS) is a vitamin K-dependent plasma glycoprotein synthesized in the liver. In the circulation, Protein S exists in two forms: a free form and a complex form bound to complement protein C4b-binding protein (C4BP). In humans, protein S is encoded by the PROS1 gene.[5][6] Protein S plays a role in coagulation.

PROS1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesPROS1, PROS, PS21, PS22, PS23, PS24, PS25, PSA, THPH5, THPH6, protein S (alpha), protein S
External IDsOMIM: 176880 MGI: 1095733 HomoloGene: 264 GeneCards: PROS1
Orthologs
SpeciesHumanMouse
Entrez

5627

19128

Ensembl

ENSG00000184500

ENSMUSG00000022912

UniProt

P07225

Q08761

RefSeq (mRNA)

NM_000313
NM_001314077

NM_011173

RefSeq (protein)

NP_000304
NP_001301006

NP_035303

Location (UCSC)Chr 3: 93.87 – 93.98 MbChr 16: 62.67 – 62.75 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

History edit

Protein S is named for Seattle, Washington, where it was originally discovered and purified[7] by Earl Davie's group in 1977.[8]

Structure edit

Protein S is partly homologous to other vitamin K-dependent plasma coagulation proteins, such as protein C and factors VII, IX, and X. Similar to them, it has a Gla domain and several EGF-like domains (four rather than two), but no serine protease domain. Instead, there is a large C-terminus domain that is homologous to plasma steroid hormone-binding proteins such as sex hormone-binding globulin and corticosteroid-binding globulin. It may play a role in the protein functions as either a cofactor for activated protein C (APC) or in binding C4BP.[9][10]

Additionally, protein S has a peptide between the Gla domain and the EGF-like domain, that is cleaved by thrombin. The Gla and EGF-like domains stay connected after the cleavage by a disulfide bond. However, protein S loses its function as an APC cofactor following either this cleavage or binding C4BP.[11]

Function edit

The best characterized function of Protein S is its role in the anti coagulation pathway, where it functions as a cofactor to Protein C in the inactivation of Factors Va and VIIIa. Only the free form has cofactor activity.[12]

Protein S binds to negatively charged phospholipids via the carboxylated Gla domain. This property allows Protein S to facilitate the removal of cells that are undergoing apoptosis, a form of structured cell death used by the body to remove unwanted or damaged cells. In healthy cells, an ATP (adenosine triphosphate)-dependent enzyme removes negatively charged phospholipids such as phosphatidyl serine from the outer leaflet of the cell membrane. An apoptotic cell (that is, one undergoing apoptosis) no longer actively manages the distribution of phospholipids in its outer membrane and hence begins to display negatively charged phospholipids on its exterior surface. These negatively charged phospholipids are recognized by phagocytes such as macrophages. Protein S binds to the negatively charged phospholipids and functions as a bridge between the apoptotic cell and the phagocyte. This bridging expedites phagocytosis and allows the cell to be removed without giving rise to inflammation or other signs of tissue damage.

Protein S does not bind to the nascent complement complex C5,6,7 to prevents it from inserting into a membrane. This is a different complement protein S AKA vitronectin made by the VTN gene, not to be confused with the coagulation protein S made by the PROS gene which this wiki page concerns.

Pathology edit

Mutations in the PROS1 gene can lead to Protein S deficiency which is a rare blood disorder which can lead to an increased risk of thrombosis.[13][14]

Interactions edit

Protein S has been shown to interact with Factor V.[15][16]

See also edit

References edit

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000184500 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000022912 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Lundwall A, Dackowski W, Cohen E, Shaffer M, Mahr A, Dahlbäck B, Stenflo J, Wydro R (September 1986). "Isolation and sequence of the cDNA for human protein S, a regulator of blood coagulation". Proc. Natl. Acad. Sci. U.S.A. 83 (18): 6716–20. Bibcode:1986PNAS...83.6716L. doi:10.1073/pnas.83.18.6716. PMC 386580. PMID 2944113.
  6. ^ Long GL, Marshall A, Gardner JC, Naylor SL (January 1988). "Genes for human vitamin K-dependent plasma proteins C and S are located on chromosomes 2 and 3, respectively". Somat. Cell Mol. Genet. 14 (1): 93–8. doi:10.1007/BF01535052. PMID 2829367. S2CID 31236887.
  7. ^ "Protein S deficiency". UpToDate. Retrieved May 10, 2017.
  8. ^ Kaushansky K, Lichtman M, Prchal J, Levi M, Press O, Burns L, Caligiuri M (2015). Williams Hematology. McGraw-Hill. p. 1926.
  9. ^ Stenflo J (1999). "Contributions of Gla and EGF-like domains to the function of vitamin K-dependent coagulation factors". Critical Reviews in Eukaryotic Gene Expression. 9 (1): 59–88. doi:10.1615/CritRevEukaryotGeneExpr.v9.i1.50. PMID 10200912.
  10. ^ Rosner W (Dec 1991). "Plasma steroid-binding proteins". Endocrinology and Metabolism Clinics of North America. 20 (4): 697–720. doi:10.1016/S0889-8529(18)30240-8. PMID 1778174.
  11. ^ Dahlbäck B, Lundwall A, Stenflo J (Jun 1986). "Primary structure of bovine vitamin K-dependent protein S". Proceedings of the National Academy of Sciences. 83 (12): 4199–203. Bibcode:1986PNAS...83.4199D. doi:10.1073/pnas.83.12.4199. PMC 323699. PMID 2940598.
  12. ^ Castoldi E, Hackeng TM (September 2008). "Regulation of coagulation by protein S". Curr. Opin. Hematol. 15 (5): 529–36. doi:10.1097/MOH.0b013e328309ec97. PMID 18695379. S2CID 11522770.
  13. ^ Beauchamp NJ, Dykes AC, Parikh N, Campbell Tait R, Daly ME (June 2004). "The prevalence of, and molecular defects underlying, inherited protein S deficiency in the general population". Br. J. Haematol. 125 (5): 647–54. doi:10.1111/j.1365-2141.2004.04961.x. PMID 15147381. S2CID 705661.
  14. ^ García de Frutos P, Fuentes-Prior P, Hurtado B, Sala N (September 2007). "Molecular basis of protein S deficiency". Thromb. Haemost. 98 (3): 543–56. doi:10.1160/th07-03-0199. PMID 17849042. S2CID 17274778.
  15. ^ Heeb MJ, Kojima Y, Rosing J, Tans G, Griffin J H (Dec 1999). "C-terminal residues 621-635 of protein S are essential for binding to factor Va". J. Biol. Chem. 274 (51). UNITED STATES: 36187–92. doi:10.1074/jbc.274.51.36187. ISSN 0021-9258. PMID 10593904. S2CID 45995946.
  16. ^ Heeb MJ, Mesters R M, Tans G, Rosing J, Griffin J H (Feb 1993). "Binding of protein S to factor Va associated with inhibition of prothrombinase that is independent of activated protein C". J. Biol. Chem. 268 (4). UNITED STATES: 2872–7. doi:10.1016/S0021-9258(18)53854-0. ISSN 0021-9258. PMID 8428962.

Further reading edit

  • Dahlbäck B (1991). "Protein S and C4b-binding protein: components involved in the regulation of the protein C anticoagulant system". Thromb. Haemost. 66 (1): 49–61. doi:10.1055/s-0038-1646373. PMID 1833851. S2CID 24929072.
  • Witt I (2002). "Molekularbiologische Grundlagen und Diagnostik der hereditären Defekte von Antithrombin III, Protein C und Protein S" [Molecular biological basis and diagnosis of hereditary defect of antithrombin III, protein c and protein S]. Hamostaseologie (in German). 22 (2): 57–66. doi:10.1055/s-0037-1619540. PMID 12193972. S2CID 58077740.
  • Rezende SM, Simmonds RE, Lane DA (2004). "Coagulation, inflammation, and apoptosis: different roles for protein S and the protein S-C4b binding protein complex". Blood. 103 (4): 1192–201. doi:10.1182/blood-2003-05-1551. PMID 12907438. S2CID 133028.
  • Dahlbäck B (2007). "The tale of protein S and C4b-binding protein, a story of affection". Thromb. Haemost. 98 (1): 90–6. doi:10.1160/th07-04-0269. PMID 17597997. S2CID 18823655.
  • García de Frutos P, Fuentes-Prior P, Hurtado B, Sala N (2007). "Molecular basis of protein S deficiency". Thromb. Haemost. 98 (3): 543–56. doi:10.1160/th07-03-0199. PMID 17849042. S2CID 17274778.
  • Maillard C, Berruyer M, Serre CM, et al. (1992). "Protein-S, a vitamin K-dependent protein, is a bone matrix component synthesized and secreted by osteoblasts". Endocrinology. 130 (3): 1599–604. doi:10.1210/endo.130.3.1531628. PMID 1531628.
  • Griffin JH, Gruber A, Fernández JA (1992). "Reevaluation of total, free, and bound protein S and C4b-binding protein levels in plasma anticoagulated with citrate or hirudin". Blood. 79 (12): 3203–11. doi:10.1182/blood.V79.12.3203.bloodjournal79123203 (inactive 2024-04-10). PMID 1534488.{{cite journal}}: CS1 maint: DOI inactive as of April 2024 (link)
  • Guglielmone HA, Vides MA (1992). "A novel functional assay of protein C in human plasma and its comparison with amidolytic and anticoagulant assays". Thromb. Haemost. 67 (1): 46–9. doi:10.1055/s-0038-1648377. PMID 1615482. S2CID 27769717.
  • Bertina RM, Ploos van Amstel HK, van Wijngaarden A, et al. (1990). "Heerlen polymorphism of protein S, an immunologic polymorphism due to dimorphism of residue 460". Blood. 76 (3): 538–48. doi:10.1182/blood.V76.3.538.538. PMID 2143091.
  • Schmidel DK, Tatro AV, Phelps LG, et al. (1991). "Organization of the human protein S genes". Biochemistry. 29 (34): 7845–52. doi:10.1021/bi00486a010. PMID 2148110.
  • Ploos van Amstel HK, Reitsma PH, van der Logt CP, Bertina RM (1991). "Intron-exon organization of the active human protein S gene PS alpha and its pseudogene PS beta: duplication and silencing during primate evolution". Biochemistry. 29 (34): 7853–61. doi:10.1021/bi00486a011. PMID 2148111.
  • Allaart CF, Aronson DC, Ruys T, et al. (1991). "Hereditary protein S deficiency in young adults with arterial occlusive disease". Thromb. Haemost. 64 (2): 206–10. PMID 2148653.
  • Ohlin AK, Landes G, Bourdon P, et al. (1989). "Beta-hydroxyaspartic acid in the first epidermal growth factor-like domain of protein C. Its role in Ca2+ binding and biological activity". J. Biol. Chem. 263 (35): 19240–8. doi:10.1016/S0021-9258(18)37415-5. PMID 2461936.
  • Schwarz HP, Heeb MJ, Lottenberg R, et al. (1989). "Familial protein S deficiency with a variant protein S molecule in plasma and platelets". Blood. 74 (1): 213–21. doi:10.1182/blood.V74.1.213.213. PMID 2526663.
  • Ploos van Amstel HK, van der Zanden AL, Reitsma PH, Bertina RM (1987). "Human protein S cDNA encodes Phe-16 and Tyr 222 in consensus sequences for the post-translational processing". FEBS Lett. 222 (1): 186–90. doi:10.1016/0014-5793(87)80217-X. PMID 2820795. S2CID 46365357.
  • Dahlbäck B, Lundwall A, Stenflo J (1986). "Primary structure of bovine vitamin K-dependent protein S". Proc. Natl. Acad. Sci. U.S.A. 83 (12): 4199–203. Bibcode:1986PNAS...83.4199D. doi:10.1073/pnas.83.12.4199. PMC 323699. PMID 2940598.
  • Lundwall A, Dackowski W, Cohen E, et al. (1986). "Isolation and sequence of the cDNA for human protein S, a regulator of blood coagulation". Proc. Natl. Acad. Sci. U.S.A. 83 (18): 6716–20. Bibcode:1986PNAS...83.6716L. doi:10.1073/pnas.83.18.6716. PMC 386580. PMID 2944113.
  • Engesser L, Broekmans AW, Briët E, et al. (1987). "Hereditary protein S deficiency: clinical manifestations". Ann. Intern. Med. 106 (5): 677–82. doi:10.7326/0003-4819-106-5-677. PMID 2952034.
  • Watkins PC, Eddy R, Fukushima Y, et al. (1988). "The gene for protein S maps near the centromere of human chromosome 3". Blood. 71 (1): 238–41. doi:10.1182/blood.V71.1.238.238. PMID 2961379.

May 07, 2024
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This article includes a list of general references but it lacks sufficient corresponding inline citations Please help to improve this article by introducing more precise citations August 2013 Learn how and when to remove this message Protein S also known as PROS is a vitamin K dependent plasma glycoprotein synthesized in the liver In the circulation Protein S exists in two forms a free form and a complex form bound to complement protein C4b binding protein C4BP In humans protein S is encoded by the PROS1 gene 5 6 Protein S plays a role in coagulation PROS1Available structuresPDBOrtholog search PDBe RCSBList of PDB id codes1Z6CIdentifiersAliasesPROS1 PROS PS21 PS22 PS23 PS24 PS25 PSA THPH5 THPH6 protein S alpha protein SExternal IDsOMIM 176880 MGI 1095733 HomoloGene 264 GeneCards PROS1Gene location Human Chr Chromosome 3 human 1 Band3q11 1Start93 873 051 bp 1 End93 980 003 bp 1 Gene location Mouse Chr Chromosome 16 mouse 2 Band16 16 C1 3Start62 674 670 bp 2 End62 749 709 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inbronchial epithelial cellsynovial jointgerminal epitheliumparietal pleurapericardiumlivervisceral pleuraspinal gangliatrigeminal ganglionright lobe of liverTop expressed incumulus cellaortic valveiriscalvarialeft lung lobesciatic nervespermatocyteascending aortaright lungadrenal glandMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functioncalcium ion binding endopeptidase inhibitor activityCellular componentblood microparticle endoplasmic reticulum membrane Golgi membrane plasma membrane extracellular region Golgi lumen extracellular exosome platelet alpha granule lumen extracellular spaceBiological processhemostasis fibrinolysis platelet degranulation blood coagulation endoplasmic reticulum to Golgi vesicle mediated transport signal peptide processing peptidyl glutamic acid carboxylation regulation of complement activation leukocyte migration negative regulation of endopeptidase activity negative regulation of blood coagulationSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez562719128EnsemblENSG00000184500ENSMUSG00000022912UniProtP07225Q08761RefSeq mRNA NM 000313NM 001314077NM 011173RefSeq protein NP 000304NP 001301006NP 035303Location UCSC Chr 3 93 87 93 98 MbChr 16 62 67 62 75 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse Contents 1 History 2 Structure 3 Function 4 Pathology 5 Interactions 6 See also 7 References 8 Further readingHistory editProtein S is named for Seattle Washington where it was originally discovered and purified 7 by Earl Davie s group in 1977 8 Structure editProtein S is partly homologous to other vitamin K dependent plasma coagulation proteins such as protein C and factors VII IX and X Similar to them it has a Gla domain and several EGF like domains four rather than two but no serine protease domain Instead there is a large C terminus domain that is homologous to plasma steroid hormone binding proteins such as sex hormone binding globulin and corticosteroid binding globulin It may play a role in the protein functions as either a cofactor for activated protein C APC or in binding C4BP 9 10 Additionally protein S has a peptide between the Gla domain and the EGF like domain that is cleaved by thrombin The Gla and EGF like domains stay connected after the cleavage by a disulfide bond However protein S loses its function as an APC cofactor following either this cleavage or binding C4BP 11 Function editThe best characterized function of Protein S is its role in the anti coagulation pathway where it functions as a cofactor to Protein C in the inactivation of Factors Va and VIIIa Only the free form has cofactor activity 12 Protein S binds to negatively charged phospholipids via the carboxylated Gla domain This property allows Protein S to facilitate the removal of cells that are undergoing apoptosis a form of structured cell death used by the body to remove unwanted or damaged cells In healthy cells an ATP adenosine triphosphate dependent enzyme removes negatively charged phospholipids such as phosphatidyl serine from the outer leaflet of the cell membrane An apoptotic cell that is one undergoing apoptosis no longer actively manages the distribution of phospholipids in its outer membrane and hence begins to display negatively charged phospholipids on its exterior surface These negatively charged phospholipids are recognized by phagocytes such as macrophages Protein S binds to the negatively charged phospholipids and functions as a bridge between the apoptotic cell and the phagocyte This bridging expedites phagocytosis and allows the cell to be removed without giving rise to inflammation or other signs of tissue damage Protein S does not bind to the nascent complement complex C5 6 7 to prevents it from inserting into a membrane This is a different complement protein S AKA vitronectin made by the VTN gene not to be confused with the coagulation protein S made by the PROS gene which this wiki page concerns Pathology editMutations in the PROS1 gene can lead to Protein S deficiency which is a rare blood disorder which can lead to an increased risk of thrombosis 13 14 Interactions editProtein S has been shown to interact with Factor V 15 16 See also editHemostasisReferences edit a b c GRCh38 Ensembl release 89 ENSG00000184500 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000022912 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Lundwall A Dackowski W Cohen E Shaffer M Mahr A Dahlback B Stenflo J Wydro R September 1986 Isolation and sequence of the cDNA for human protein S a regulator of blood coagulation Proc Natl Acad Sci U S A 83 18 6716 20 Bibcode 1986PNAS 83 6716L doi 10 1073 pnas 83 18 6716 PMC 386580 PMID 2944113 Long GL Marshall A Gardner JC Naylor SL January 1988 Genes for human vitamin K dependent plasma proteins C and S are located on chromosomes 2 and 3 respectively Somat Cell Mol Genet 14 1 93 8 doi 10 1007 BF01535052 PMID 2829367 S2CID 31236887 Protein S deficiency UpToDate Retrieved May 10 2017 Kaushansky K Lichtman M Prchal J Levi M Press O Burns L Caligiuri M 2015 Williams Hematology McGraw Hill p 1926 Stenflo J 1999 Contributions of Gla and EGF like domains to the function of vitamin K dependent coagulation factors Critical Reviews in Eukaryotic Gene Expression 9 1 59 88 doi 10 1615 CritRevEukaryotGeneExpr v9 i1 50 PMID 10200912 Rosner W Dec 1991 Plasma steroid binding proteins Endocrinology and Metabolism Clinics of North America 20 4 697 720 doi 10 1016 S0889 8529 18 30240 8 PMID 1778174 Dahlback B Lundwall A Stenflo J Jun 1986 Primary structure of bovine vitamin K dependent protein S Proceedings of the National Academy of Sciences 83 12 4199 203 Bibcode 1986PNAS 83 4199D doi 10 1073 pnas 83 12 4199 PMC 323699 PMID 2940598 Castoldi E Hackeng TM September 2008 Regulation of coagulation by protein S Curr Opin Hematol 15 5 529 36 doi 10 1097 MOH 0b013e328309ec97 PMID 18695379 S2CID 11522770 Beauchamp NJ Dykes AC Parikh N Campbell Tait R Daly ME June 2004 The prevalence of and molecular defects underlying inherited protein S deficiency in the general population Br J Haematol 125 5 647 54 doi 10 1111 j 1365 2141 2004 04961 x PMID 15147381 S2CID 705661 Garcia de Frutos P Fuentes Prior P Hurtado B Sala N September 2007 Molecular basis of protein S deficiency Thromb Haemost 98 3 543 56 doi 10 1160 th07 03 0199 PMID 17849042 S2CID 17274778 Heeb MJ Kojima Y Rosing J Tans G Griffin J H Dec 1999 C terminal residues 621 635 of protein S are essential for binding to factor Va J Biol Chem 274 51 UNITED STATES 36187 92 doi 10 1074 jbc 274 51 36187 ISSN 0021 9258 PMID 10593904 S2CID 45995946 Heeb MJ Mesters R M Tans G Rosing J Griffin J H Feb 1993 Binding of protein S to factor Va associated with inhibition of prothrombinase that is independent of activated protein C J Biol Chem 268 4 UNITED STATES 2872 7 doi 10 1016 S0021 9258 18 53854 0 ISSN 0021 9258 PMID 8428962 Further reading editDahlback B 1991 Protein S and C4b binding protein components involved in the regulation of the protein C anticoagulant system Thromb Haemost 66 1 49 61 doi 10 1055 s 0038 1646373 PMID 1833851 S2CID 24929072 Witt I 2002 Molekularbiologische Grundlagen und Diagnostik der hereditaren Defekte von Antithrombin III Protein C und Protein S Molecular biological basis and diagnosis of hereditary defect of antithrombin III protein c and protein S Hamostaseologie in German 22 2 57 66 doi 10 1055 s 0037 1619540 PMID 12193972 S2CID 58077740 Rezende SM Simmonds RE Lane DA 2004 Coagulation inflammation and apoptosis different roles for protein S and the protein S C4b binding protein complex Blood 103 4 1192 201 doi 10 1182 blood 2003 05 1551 PMID 12907438 S2CID 133028 Dahlback B 2007 The tale of protein S and C4b binding protein a story of affection Thromb Haemost 98 1 90 6 doi 10 1160 th07 04 0269 PMID 17597997 S2CID 18823655 Garcia de Frutos P Fuentes Prior P Hurtado B Sala N 2007 Molecular basis of protein S deficiency Thromb Haemost 98 3 543 56 doi 10 1160 th07 03 0199 PMID 17849042 S2CID 17274778 Maillard C Berruyer M Serre CM et al 1992 Protein S a vitamin K dependent protein is a bone matrix component synthesized and secreted by osteoblasts Endocrinology 130 3 1599 604 doi 10 1210 endo 130 3 1531628 PMID 1531628 Griffin JH Gruber A Fernandez JA 1992 Reevaluation of total free and bound protein S and C4b binding protein levels in plasma anticoagulated with citrate or hirudin Blood 79 12 3203 11 doi 10 1182 blood V79 12 3203 bloodjournal79123203 inactive 2024 04 10 PMID 1534488 a href Template Cite journal html title Template Cite journal cite journal a CS1 maint DOI inactive as of April 2024 link Guglielmone HA Vides MA 1992 A novel functional assay of protein C in human plasma and its comparison with amidolytic and anticoagulant assays Thromb Haemost 67 1 46 9 doi 10 1055 s 0038 1648377 PMID 1615482 S2CID 27769717 Bertina RM Ploos van Amstel HK van Wijngaarden A et al 1990 Heerlen polymorphism of protein S an immunologic polymorphism due to dimorphism of residue 460 Blood 76 3 538 48 doi 10 1182 blood V76 3 538 538 PMID 2143091 Schmidel DK Tatro AV Phelps LG et al 1991 Organization of the human protein S genes Biochemistry 29 34 7845 52 doi 10 1021 bi00486a010 PMID 2148110 Ploos van Amstel HK Reitsma PH van der Logt CP Bertina RM 1991 Intron exon organization of the active human protein S gene PS alpha and its pseudogene PS beta duplication and silencing during primate evolution Biochemistry 29 34 7853 61 doi 10 1021 bi00486a011 PMID 2148111 Allaart CF Aronson DC Ruys T et al 1991 Hereditary protein S deficiency in young adults with arterial occlusive disease Thromb Haemost 64 2 206 10 PMID 2148653 Ohlin AK Landes G Bourdon P et al 1989 Beta hydroxyaspartic acid in the first epidermal growth factor like domain of protein C Its role in Ca2 binding and biological activity J Biol Chem 263 35 19240 8 doi 10 1016 S0021 9258 18 37415 5 PMID 2461936 Schwarz HP Heeb MJ Lottenberg R et al 1989 Familial protein S deficiency with a variant protein S molecule in plasma and platelets Blood 74 1 213 21 doi 10 1182 blood V74 1 213 213 PMID 2526663 Ploos van Amstel HK van der Zanden AL Reitsma PH Bertina RM 1987 Human protein S cDNA encodes Phe 16 and Tyr 222 in consensus sequences for the post translational processing FEBS Lett 222 1 186 90 doi 10 1016 0014 5793 87 80217 X PMID 2820795 S2CID 46365357 Dahlback B Lundwall A Stenflo J 1986 Primary structure of bovine vitamin K dependent protein S Proc Natl Acad Sci U S A 83 12 4199 203 Bibcode 1986PNAS 83 4199D doi 10 1073 pnas 83 12 4199 PMC 323699 PMID 2940598 Lundwall A Dackowski W Cohen E et al 1986 Isolation and sequence of the cDNA for human protein S a regulator of blood coagulation Proc Natl Acad Sci U S A 83 18 6716 20 Bibcode 1986PNAS 83 6716L doi 10 1073 pnas 83 18 6716 PMC 386580 PMID 2944113 Engesser L Broekmans AW Briet E et al 1987 Hereditary protein S deficiency clinical manifestations Ann Intern Med 106 5 677 82 doi 10 7326 0003 4819 106 5 677 PMID 2952034 Watkins PC Eddy R Fukushima Y et al 1988 The gene for protein S maps near the centromere of human chromosome 3 Blood 71 1 238 41 doi 10 1182 blood V71 1 238 238 PMID 2961379 Retrieved from https en wikipedia org w index php title Protein S amp oldid 1218260201, wikipedia, wiki, book, books, library,

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