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Vitamin K-dependent protein S

 PROS_HUMAN              Reviewed;         676 AA.
P07225; A8KAC9; D3DN28; Q15518; Q7Z715; Q9UCZ8;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
01-APR-1988, sequence version 1.
20-DEC-2017, entry version 218.
RecName: Full=Vitamin K-dependent protein S;
Flags: Precursor;
Name=PROS1; Synonyms=PROS;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND GAMMA-CARBOXYGLUTAMATION AT GLU-47;
GLU-48; GLU-55; GLU-57; GLU-60; GLU-61; GLU-66; GLU-67; GLU-70; GLU-73
AND GLU-77.
PubMed=2820795; DOI=10.1016/0014-5793(87)80217-X;
Ploos van Amstel H.K., van der Zanden A.L., Reitsma P.H.,
Bertina R.M.;
"Human protein S cDNA encodes Phe-16 and Tyr 222 in consensus
sequences for the post-translational processing.";
FEBS Lett. 222:186-190(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3467362; DOI=10.1073/pnas.84.2.349;
Hoskins J., Norman D.K., Beckmann R.J., Long G.L.;
"Cloning and characterization of human liver cDNA encoding a protein S
precursor.";
Proc. Natl. Acad. Sci. U.S.A. 84:349-353(1987).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2148110; DOI=10.1021/bi00486a010;
Schmidel D.K., Tatro A.V., Phelps L.G., Tomczak J.A., Long G.L.;
"Organization of the human protein S genes.";
Biochemistry 29:7845-7852(1990).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Liver;
PubMed=2148111; DOI=10.1021/bi00486a011;
Ploos van Amstel H.K., Reitsma P.H., der Logt C.P., Bertina R.M.;
"Intron-exon organization of the active human protein S gene PS alpha
and its pseudogene PS beta: duplication and silencing during primate
evolution.";
Biochemistry 29:7853-7861(1990).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 27-676.
PubMed=2944113; DOI=10.1073/pnas.83.18.6716;
Lundwall A., Dackowski W., Cohen E., Shaffer M., Mahr A., Dahlback B.,
Stenflo J., Wydro R.;
"Isolation and sequence of the cDNA for human protein S, a regulator
of blood coagulation.";
Proc. Natl. Acad. Sci. U.S.A. 83:6716-6720(1986).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 500-519, AND VARIANTS THPH5
VAL-381 AND GLY-508.
PubMed=7482398;
Gomez E., Poort S.R., Bertina R.M., Reitsma P.H.;
"Identification of eight point mutations in protein S deficiency type
I -- analysis of 15 pedigrees.";
Thromb. Haemost. 73:750-755(1995).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-530.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[13]
STRUCTURE BY NMR OF 200-286, AND DISULFIDE BONDS.
PubMed=15952784; DOI=10.1021/bi050101f;
Drakenberg T., Ghasriani H., Thulin E., Thamlitz A.M., Muranyi A.,
Annila A., Stenflo J.;
"Solution structure of the Ca2+-binding EGF3-4 pair from vitamin K-
dependent protein S: identification of an unusual fold in EGF3.";
Biochemistry 44:8782-8789(2005).
[14]
VARIANT PRO-501.
PubMed=2143091;
Bertina R.M., Ploos van Amstel H.K., van Wijngaarden A., Coenen J.,
Leemhuis M.P., Deutz-Terlouw P.P., van der Linden I.K., Reitsma P.H.;
"Heerlen polymorphism of protein S, an immunologic polymorphism due to
dimorphism of residue 460.";
Blood 76:538-548(1990).
[15]
VARIANT THPH5 SER-258.
Cooper D.N.;
Unpublished observations (SEP-1993).
[16]
VARIANT THPH5 TOKUSHIMA GLU-196.
PubMed=8298131;
Hayashi T., Nishioka J., Shigekiyo T., Saito S., Suzuki K.;
"Protein S Tokushima: abnormal molecule with a substitution of Glu for
Lys-155 in the second epidermal growth factor-like domain of protein
S.";
Blood 83:683-690(1994).
[17]
VARIANTS THPH5 LEU-40; HIS-41; ALA-67; CYS-72; MET-78; HIS-90;
ASN-144; GLY-245; LYS-249; TRP-265; ARG-265 AND ASN-376, AND VARIANTS
LEU-76 AND VAL-385.
PubMed=7803790;
Gandrille S., Borgel D., Eschwege-Gufflet V., Aillaud M., Dreyfus M.,
Matheron C., Gaussem P., Abgrall J.F., Jude B., Sie P., Toulon P.,
Aiach M.;
"Identification of 15 different candidate causal point mutations and
three polymorphisms in 19 patients with protein S deficiency using a
scanning method for the analysis of the protein S active gene.";
Blood 85:130-138(1995).
[18]
VARIANTS THPH5 SER-258 AND THR-611.
PubMed=7545463;
Formstone C.J., Wacey A.I., Berg L.-P., Rahman S., Bevan D.,
Rowley M., Voke J., Bernardi F., Legnani C., Simioni P., Girolami A.,
Tuddenham E.G.D., Kakkar V.V., Cooper D.N.;
"Detection and characterization of seven novel protein S (PROS) gene
lesions: evaluation of reverse transcript-polymerase chain reaction as
a mutation screening strategy.";
Blood 86:2632-2641(1995).
[19]
VARIANTS THPH5 PRO-351; SER-552; GLN-584 AND PRO-616.
PubMed=7579449;
Mustafa S., Pabinger I., Mannhalter C.;
"Protein S deficiency type I: identification of point mutations in 9
of 10 families.";
Blood 86:3444-3451(1995).
[20]
VARIANT THPH5 SER-644.
PubMed=8977443; DOI=10.1161/01.ATV.16.12.1407;
Li M., Long G.L.;
"Identification of two novel point mutations in the human protein S
gene associated with familial protein S deficiency and thrombosis.";
Arterioscler. Thromb. Vasc. Biol. 16:1407-1415(1996).
[21]
VARIANT THPH5 CYS-515, CHARACTERIZATION OF VARIANT PROS1 DEFICIENCY
CYS-515, AND MUTAGENESIS OF ARG-515.
PubMed=8639833;
Yamazaki T., Katsumi A., Kagami K., Okamoto Y., Sugiura I.,
Hamaguchi M., Kojima T., Takamatsu J., Saito H.;
"Molecular basis of a hereditary type I protein S deficiency caused by
a substitution of Cys for Arg474.";
Blood 87:4643-4650(1996).
[22]
VARIANTS THPH5 TYR-186; THR-611 AND LEU-665.
PubMed=8781426;
Beauchamp N.J., Daly M.E., Cooper P.C., Makris M., Preston F.E.,
Peake I.R.;
"Molecular basis of protein S deficiency in three families also
showing independent inheritance of factor V Leiden.";
Blood 88:1700-1707(1996).
[23]
VARIANTS THPH5 GLU-50; ALA-67; GLU-95; TYR-186; SER-241; PRO-324;
ASP-381; SER-449 AND ARG-666, AND VARIANT PRO-501.
PubMed=8943854;
Protein S study group;
Simmonds R.E., Ireland H., Kunz G., Lane D.A.;
"Identification of 19 protein S gene mutations in patients with
phenotypic protein S deficiency and thrombosis.";
Blood 88:4195-4204(1996).
[24]
VARIANTS THPH5 SER-111; GLY-157; GLY-161; GLU-364; PRO-446; ARG-475;
ALA-501; MET-508; CYS-515; PRO-525; ALA-532; TYR-568; ARG-575 AND
ARG-666, AND VARIANT PRO-501.
PubMed=8765219; DOI=10.1016/S0022-2143(96)90015-3;
The French network on molecular abnormalities responsible for protein C and protein S deficiencies;
Borgel D., Duchemin J., Alhenc-Gelas M., Matheron C., Aiach M.,
Gandrille S.;
"Molecular basis for protein S hereditary deficiency: genetic defects
observed in 118 patients with type I and type IIa deficiencies.";
J. Lab. Clin. Med. 128:218-227(1996).
[25]
VARIANTS THPH5 PRO-300 AND ARG-666.
PubMed=8701404;
Duchemin J., Borg J.-Y., Borgel D., Vasse M., Leveque H., Aiach M.,
Gandrille S.;
"Five novel mutations of the protein S active gene (PROS 1) in 8
Norman families.";
Thromb. Haemost. 75:437-444(1996).
[26]
VARIANT THPH5 PHE-639.
PubMed=9031443;
Bustorff T.C., Freire I., Gago T., Crespo F., David D.;
"Identification of three novel mutations in hereditary protein S
deficiency.";
Thromb. Haemost. 77:21-25(1997).
[27]
VARIANTS THPH5 ASP-68; ARG-95 AND SER-336.
PubMed=9241758;
Plasma coagulation inhibitors subcommittee of the scientific and standardization committee of the international society on thrombosis and haemostasis;
Gandrille S., Borgel D., Ireland H., Lane D.A., Simmonds R.,
Reitsma P.H., Mannhalter C., Pabinger I., Saito H., Suzuki K.,
Formstone C., Cooper D.N., Espinosa Y., Sala N., Bernardi F.,
Aiach M.;
"Protein S deficiency: a database of mutations.";
Thromb. Haemost. 77:1201-1214(1997).
[28]
VARIANTS THPH5 CYS-482; CYS-485 AND GLY-561, AND VARIANTS PRO-501 AND
MET-559.
PubMed=10447256;
DOI=10.1002/(SICI)1098-1004(1999)14:1<30::AID-HUMU4>3.0.CO;2-X;
Espinosa-Parrilla Y., Morell M., Souto J.C., Tirado I.,
Fontcuberta J., Estivill X., Sala N.;
"Protein S gene analysis reveals the presence of a cosegregating
mutation in most pedigrees with type I but not type III PS
deficiency.";
Hum. Mutat. 14:30-39(1999).
[29]
VARIANTS THPH5 ALA-67; GLY-129; PHE-175; PRO-515; LEU-562 AND ASP-638,
AND VARIANTS LEU-76 AND ASP-638.
PubMed=10613647;
Hermida J., Faioni E.M., Mannucci P.M.;
"Poor relationship between phenotypes of protein S deficiency and
mutations in the protein S alpha gene.";
Thromb. Haemost. 82:1634-1638(1999).
[30]
VARIANTS THPH5 TYR-166; GLY-247; THR-611; ARG-622 AND ARG-666.
PubMed=10706858;
Makris M., Leach M., Beauchamp N.J., Daly M.E., Cooper P.C.,
Hampton K.K., Bayliss P., Peake I.R., Miller G.J., Preston F.E.;
"Genetic analysis, phenotypic diagnosis, and risk of venous thrombosis
in families with inherited deficiencies of protein S.";
Blood 95:1935-1941(2000).
[31]
VARIANTS THPH5 HIS-15; THR-640 AND LEU-667, AND VARIANTS SER-98;
LYS-233 AND MET-559.
PubMed=10790208;
DOI=10.1002/(SICI)1098-1004(200005)15:5<463::AID-HUMU8>3.3.CO;2-5;
Espinosa-Parrilla Y., Morell M., Borrell M., Souto J.C.,
Fontcuberta J., Estivill X., Sala N.;
"Optimization of a simple and rapid single-strand conformation
analysis for detection of mutations in the PROS1 gene: identification
of seven novel mutations and three novel, apparently neutral,
variants.";
Hum. Mutat. 15:463-473(2000).
[32]
VARIANTS THPH5 ASN-243 AND PRO-339.
PubMed=11372770; DOI=10.1055/s-2001-14075;
Iwaki T., Mastushita T., Kobayashi T., Yamamoto Y., Nomura Y.,
Kagami K., Nakayama T., Sugiura I., Kojima T., Takamatsu J.,
Kanayama N., Saito H.;
"DNA sequence analysis of protein S deficiency -- identification of
four point mutations in twelve Japanese subjects.";
Semin. Thromb. Hemost. 27:155-160(2001).
[33]
VARIANTS THPH5 CYS-149; ARG-383; LYS-390 AND SER-526.
PubMed=11776305;
Andersen B.D., Bisgaard M.L., Lind B., Philips M., Villoutreix B.O.,
Thorsen S.;
"Characterization and structural impact of five novel PROS1 mutations
in eleven protein S-deficient families.";
Thromb. Haemost. 86:1392-1399(2001).
[34]
VARIANTS THPH5 ASP-52 AND MET-78, AND CHARACTERIZATION OF VARIANTS
THPH5 ASP-52 AND MET-78.
PubMed=12351389; DOI=10.1182/blood-2002-03-0909;
Rezende S.M., Lane D.A., Mille-Baker B., Samama M.M., Conard J.,
Simmonds R.E.;
"Protein S Gla-domain mutations causing impaired Ca(2+)-induced
phospholipid binding and severe functional protein S deficiency.";
Blood 100:2812-2819(2002).
[35]
VARIANTS THPH5 GLU-18; CYS-90; SER-258; VAL-336 AND PRO-664, AND
CHARACTERIZATION OF VARIANTS THPH5 GLU-18; CYS-90; SER-258 VAL-336 AND
PRO-664.
PubMed=11858485;
Rezende S.M., Lane D.A., Zoeller B., Mille-Baker B., Laffan M.,
Dalhbaeck B., Simmonds R.E.;
"Genetic and phenotypic variability between families with hereditary
protein S deficiency.";
Thromb. Haemost. 87:258-265(2002).
[36]
VARIANTS THPH5 ARG-95; GLU-196; ILE-630 AND CYS-636, AND
CHARACTERIZATION OF VARIANTS THPH5 ARG-95; GLU-196; ILE-630 AND
CYS-636.
PubMed=11927129; DOI=10.1016/S0049-3848(02)00015-4;
Tsuda H., Urata M., Tsuda T., Wakiyama M., Iida H., Nakahara M.,
Kinoshita S., Hamasaki N.;
"Four missense mutations identified in the protein S gene of
thrombosis patients with protein S deficiency: effects on secretion
and anticoagulant activity of protein S.";
Thromb. Res. 105:233-239(2002).
[37]
VARIANTS THPH5 CYS-101 AND ASN-144, AND VARIANT SER-168.
PubMed=12632031; DOI=10.1097/00001721-200302000-00012;
Boinot C., Borgel D., Kitzis A., Guicheteau M., Aiach M.,
Alhenc-Gelas M.;
"Familial thrombophilia is an oligogenetic disease: involvement of the
prothrombin G20210A, PROC and PROS gene mutations.";
Blood Coagul. Fibrinolysis 14:191-196(2003).
[38]
VARIANTS THPH5 LEU-87; TYR-121; GLU-196; HIS-355 AND LEU-667.
PubMed=15238143; DOI=10.1111/j.1365-2141.2004.05026.x;
Okada H., Takagi A., Murate T., Adachi T., Yamamoto K., Matsushita T.,
Takamatsu J., Sugita K., Sugimoto M., Yoshioka A., Yamazaki T.,
Saito H., Kojima T.;
"Identification of protein Salpha gene mutations including four novel
mutations in eight unrelated patients with protein S deficiency.";
Br. J. Haematol. 126:219-225(2004).
[39]
VARIANTS THPH5 ALA-67; TYR-88; GLY-129; ASN-144; PHE-175; GLY-204;
CYS-266; SER-267; ASP-336; ARG-357; PRO-446; PRO-515; ASP-521;
LYS-611; ASP-638 AND TYR-639, VARIANTS LEU-76; PRO-501; MET-559;
LEU-562 AND HIS-583, CHARACTERIZATION OF VARIANTS PROS1 DEFICIENCY
ALA-67; TYR-88; GLY-129; PHE-175; GLY-204; CYS-266; SER-267; ASP-336;
ARG-357; PRO-446; PRO-515; ASP-521; LYS-611; ASP-638 AND TYR-639, AND
CHARACTERIZATION OF VARIANTS LEU-76; LEU-562 AND HIS-583.
PubMed=15712227; DOI=10.1002/humu.20136;
Protein S Italian team (PROSIT);
Biguzzi E., Razzari C., Lane D.A., Castaman G., Cappellari A.,
Bucciarelli P., Fontana G., Margaglione M., D'Andrea G.,
Simmonds R.E., Rezende S.M., Preston R., Prisco D., Faioni E.M.;
"Molecular diversity and thrombotic risk in protein S deficiency: the
PROSIT study.";
Hum. Mutat. 25:259-269(2005).
[40]
VARIANT [LARGE SCALE ANALYSIS] GLY-545.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[41]
CHARACTERIZATION OF VARIANTS THPH5 HIS-15 AND THR-640, AND
CHARACTERIZATION OF VARIANT LYS-233.
PubMed=18322254; DOI=10.3324/haematol.12090;
Hurtado B., Munoz X., Mulero M.C., Navarro G., Domenech P.,
Garcia de Frutos P., Perez-Riba M., Sala N.;
"Functional characterization of twelve natural PROS1 mutations
associated with anticoagulant protein S deficiency.";
Haematologica 93:574-580(2008).
[42]
VARIANT THPH6 CYS-234.
PubMed=20484936; DOI=10.1159/000298282;
Fischer D., Porto L., Stoll H., Geisen C., Schloesser R.L.;
"Intracerebral mass bleeding in a term neonate: manifestation of
hereditary protein S deficiency with a new mutation in the PROS1
gene.";
Neonatology 98:337-340(2010).
[43]
VARIANT LYS-233.
PubMed=27535533; DOI=10.1038/nature19057;
Exome Aggregation Consortium;
Lek M., Karczewski K.J., Minikel E.V., Samocha K.E., Banks E.,
Fennell T., O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B.,
Tukiainen T., Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K.,
Zhao F., Zou J., Pierce-Hoffman E., Berghout J., Cooper D.N.,
Deflaux N., DePristo M., Do R., Flannick J., Fromer M., Gauthier L.,
Goldstein J., Gupta N., Howrigan D., Kiezun A., Kurki M.I.,
Moonshine A.L., Natarajan P., Orozco L., Peloso G.M., Poplin R.,
Rivas M.A., Ruano-Rubio V., Rose S.A., Ruderfer D.M., Shakir K.,
Stenson P.D., Stevens C., Thomas B.P., Tiao G., Tusie-Luna M.T.,
Weisburd B., Won H.H., Yu D., Altshuler D.M., Ardissino D.,
Boehnke M., Danesh J., Donnelly S., Elosua R., Florez J.C.,
Gabriel S.B., Getz G., Glatt S.J., Hultman C.M., Kathiresan S.,
Laakso M., McCarroll S., McCarthy M.I., McGovern D., McPherson R.,
Neale B.M., Palotie A., Purcell S.M., Saleheen D., Scharf J.M.,
Sklar P., Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C.,
Wilson J.G., Daly M.J., MacArthur D.G.;
"Analysis of protein-coding genetic variation in 60,706 humans.";
Nature 536:285-291(2016).
-!- FUNCTION: Anticoagulant plasma protein; it is a cofactor to
activated protein C in the degradation of coagulation factors Va
and VIIIa. It helps to prevent coagulation and stimulating
fibrinolysis.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Plasma.
-!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
aspartate and asparagine is (R) stereospecific within EGF domains.
{ECO:0000250}.
-!- DISEASE: Thrombophilia due to protein S deficiency, autosomal
dominant (THPH5) [MIM:612336]: A hemostatic disorder characterized
by impaired regulation of blood coagulation and a tendency to
recurrent venous thrombosis. Based on the plasma levels of total
and free PROS1 as well as the serine protease-activated protein C
cofactor activity, three types of THPH5 have been described: type
I, characterized by reduced total and free PROS1 levels together
with reduced anticoagulant activity; type III, in which only free
PROS1 antigen and PROS1 activity levels are reduced; and the rare
type II which is characterized by normal concentrations of both
total and free PROS1 antigen, but low cofactor activity.
{ECO:0000269|PubMed:10447256, ECO:0000269|PubMed:10613647,
ECO:0000269|PubMed:10706858, ECO:0000269|PubMed:10790208,
ECO:0000269|PubMed:11372770, ECO:0000269|PubMed:11776305,
ECO:0000269|PubMed:11858485, ECO:0000269|PubMed:11927129,
ECO:0000269|PubMed:12351389, ECO:0000269|PubMed:12632031,
ECO:0000269|PubMed:15238143, ECO:0000269|PubMed:15712227,
ECO:0000269|PubMed:18322254, ECO:0000269|PubMed:7482398,
ECO:0000269|PubMed:7545463, ECO:0000269|PubMed:7579449,
ECO:0000269|PubMed:7803790, ECO:0000269|PubMed:8298131,
ECO:0000269|PubMed:8639833, ECO:0000269|PubMed:8701404,
ECO:0000269|PubMed:8765219, ECO:0000269|PubMed:8781426,
ECO:0000269|PubMed:8943854, ECO:0000269|PubMed:8977443,
ECO:0000269|PubMed:9031443, ECO:0000269|PubMed:9241758,
ECO:0000269|Ref.15}. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- DISEASE: Thrombophilia due to protein S deficiency, autosomal
recessive (THPH6) [MIM:614514]: A very rare and severe hematologic
disorder resulting in thrombosis and secondary hemorrhage usually
beginning in early infancy. Some affected individuals develop
neonatal purpura fulminans, multifocal thrombosis, or intracranial
hemorrhage. {ECO:0000269|PubMed:20484936}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=AAP45054.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/pros1/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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EMBL; Y00692; CAA68687.1; -; mRNA.
EMBL; Y00692; CAA68688.1; ALT_SEQ; mRNA.
EMBL; M15036; AAA36479.1; -; mRNA.
EMBL; M57853; AAA60357.1; -; Genomic_DNA.
EMBL; M57840; AAA60357.1; JOINED; Genomic_DNA.
EMBL; M57841; AAA60357.1; JOINED; Genomic_DNA.
EMBL; M57842; AAA60357.1; JOINED; Genomic_DNA.
EMBL; M57844; AAA60357.1; JOINED; Genomic_DNA.
EMBL; M57845; AAA60357.1; JOINED; Genomic_DNA.
EMBL; M57846; AAA60357.1; JOINED; Genomic_DNA.
EMBL; M57847; AAA60357.1; JOINED; Genomic_DNA.
EMBL; M57848; AAA60357.1; JOINED; Genomic_DNA.
EMBL; M57849; AAA60357.1; JOINED; Genomic_DNA.
EMBL; M57850; AAA60357.1; JOINED; Genomic_DNA.
EMBL; M57851; AAA60357.1; JOINED; Genomic_DNA.
EMBL; M57852; AAA60357.1; JOINED; Genomic_DNA.
EMBL; AH002948; AAA60180.1; -; Genomic_DNA.
EMBL; AK292994; BAF85683.1; -; mRNA.
EMBL; AY308744; AAP45054.1; ALT_SEQ; Genomic_DNA.
EMBL; CH471052; EAW79903.1; -; Genomic_DNA.
EMBL; CH471052; EAW79905.1; -; Genomic_DNA.
EMBL; BC015801; AAH15801.1; -; mRNA.
CCDS; CCDS2923.1; -.
PIR; A35610; KXHUS.
RefSeq; NP_000304.2; NM_000313.3.
RefSeq; NP_001301006.1; NM_001314077.1.
UniGene; Hs.64016; -.
PDB; 1Z6C; NMR; -; A=200-286.
PDBsum; 1Z6C; -.
ProteinModelPortal; P07225; -.
SMR; P07225; -.
BioGrid; 111611; 18.
IntAct; P07225; 4.
STRING; 9606.ENSP00000377783; -.
DrugBank; DB00055; Drotrecogin alfa.
DrugBank; DB00170; Menadione.
DrugBank; DB00464; Sodium Tetradecyl Sulfate.
iPTMnet; P07225; -.
PhosphoSitePlus; P07225; -.
BioMuta; PROS1; -.
DMDM; 131086; -.
EPD; P07225; -.
MaxQB; P07225; -.
PaxDb; P07225; -.
PeptideAtlas; P07225; -.
PRIDE; P07225; -.
DNASU; 5627; -.
Ensembl; ENST00000394236; ENSP00000377783; ENSG00000184500.
GeneID; 5627; -.
KEGG; hsa:5627; -.
UCSC; uc003drb.5; human.
CTD; 5627; -.
DisGeNET; 5627; -.
EuPathDB; HostDB:ENSG00000184500.14; -.
GeneCards; PROS1; -.
HGNC; HGNC:9456; PROS1.
HPA; HPA007724; -.
HPA; HPA023974; -.
MalaCards; PROS1; -.
MIM; 176880; gene.
MIM; 612336; phenotype.
MIM; 614514; phenotype.
neXtProt; NX_P07225; -.
OpenTargets; ENSG00000184500; -.
Orphanet; 743; Hereditary thrombophilia due to congenital protein S deficiency.
PharmGKB; PA33809; -.
eggNOG; ENOG410IGF6; Eukaryota.
eggNOG; ENOG410ZTGU; LUCA.
GeneTree; ENSGT00530000063339; -.
HOGENOM; HOG000065758; -.
HOVERGEN; HBG051702; -.
InParanoid; P07225; -.
KO; K03908; -.
OMA; WNMVSVE; -.
OrthoDB; EOG091G02L2; -.
PhylomeDB; P07225; -.
TreeFam; TF352157; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-140875; Common Pathway of Fibrin Clot Formation.
Reactome; R-HSA-159740; Gamma-carboxylation of protein precursors.
Reactome; R-HSA-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
Reactome; R-HSA-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-977606; Regulation of Complement cascade.
SIGNOR; P07225; -.
ChiTaRS; PROS1; human.
EvolutionaryTrace; P07225; -.
GeneWiki; Protein_S; -.
GenomeRNAi; 5627; -.
PRO; PR:P07225; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000184500; -.
CleanEx; HS_PROS1; -.
ExpressionAtlas; P07225; baseline and differential.
Genevisible; P07225; HS.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0004866; F:endopeptidase inhibitor activity; TAS:ProtInc.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:Reactome.
GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-KW.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0017187; P:peptidyl-glutamic acid carboxylation; TAS:Reactome.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
GO; GO:0006465; P:signal peptide processing; TAS:Reactome.
Gene3D; 4.10.740.10; -; 1.
InterPro; IPR017857; Coagulation_fac_subgr_Gla_dom.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR035972; GLA-like_dom_SF.
InterPro; IPR000294; GLA_domain.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR001791; Laminin_G.
InterPro; IPR033189; PROS1.
PANTHER; PTHR24040:SF0; PTHR24040:SF0; 1.
Pfam; PF00008; EGF; 1.
Pfam; PF07645; EGF_CA; 2.
Pfam; PF00594; Gla; 1.
Pfam; PF00054; Laminin_G_1; 1.
Pfam; PF02210; Laminin_G_2; 1.
PRINTS; PR00001; GLABLOOD.
SMART; SM00181; EGF; 4.
SMART; SM00179; EGF_CA; 4.
SMART; SM00069; GLA; 1.
SMART; SM00282; LamG; 2.
SUPFAM; SSF49899; SSF49899; 2.
SUPFAM; SSF57184; SSF57184; 1.
SUPFAM; SSF57630; SSF57630; 1.
PROSITE; PS00010; ASX_HYDROXYL; 4.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 3.
PROSITE; PS50026; EGF_3; 4.
PROSITE; PS01187; EGF_CA; 3.
PROSITE; PS00011; GLA_1; 1.
PROSITE; PS50998; GLA_2; 1.
PROSITE; PS50025; LAM_G_DOMAIN; 2.
1: Evidence at protein level;
3D-structure; Blood coagulation; Calcium;
Cleavage on pair of basic residues; Complete proteome;
Disease mutation; Disulfide bond; EGF-like domain; Fibrinolysis;
Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis; Hydroxylation;
Polymorphism; Reference proteome; Repeat; Secreted; Signal;
Thrombophilia; Zymogen.
SIGNAL 1 24
PROPEP 25 41
/FTId=PRO_0000022119.
CHAIN 42 676 Vitamin K-dependent protein S.
/FTId=PRO_0000022120.
DOMAIN 42 87 Gla. {ECO:0000255|PROSITE-
ProRule:PRU00463}.
DOMAIN 117 155 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 157 200 EGF-like 2; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 201 242 EGF-like 3; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 243 283 EGF-like 4; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 299 475 Laminin G-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 484 666 Laminin G-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
REGION 88 116 Thrombin-sensitive.
SITE 499 499 Not glycosylated; in variant Heerlen.
MOD_RES 47 47 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:2820795}.
MOD_RES 48 48 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:2820795}.
MOD_RES 55 55 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:2820795}.
MOD_RES 57 57 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:2820795}.
MOD_RES 60 60 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:2820795}.
MOD_RES 61 61 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:2820795}.
MOD_RES 66 66 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:2820795}.
MOD_RES 67 67 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:2820795}.
MOD_RES 70 70 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:2820795}.
MOD_RES 73 73 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:2820795}.
MOD_RES 77 77 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:2820795}.
MOD_RES 136 136 (3R)-3-hydroxyaspartate. {ECO:0000250}.
CARBOHYD 499 499 N-linked (GlcNAc...) asparagine.
CARBOHYD 509 509 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 530 530 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
DISULFID 58 63 {ECO:0000250}.
DISULFID 121 134 {ECO:0000250}.
DISULFID 126 143 {ECO:0000250}.
DISULFID 145 154 {ECO:0000250}.
DISULFID 161 175 {ECO:0000250}.
DISULFID 171 184 {ECO:0000250}.
DISULFID 186 199 {ECO:0000250}.
DISULFID 205 217 {ECO:0000269|PubMed:15952784}.
DISULFID 212 226 {ECO:0000269|PubMed:15952784}.
DISULFID 228 241 {ECO:0000269|PubMed:15952784}.
DISULFID 247 256 {ECO:0000269|PubMed:15952784}.
DISULFID 252 265 {ECO:0000269|PubMed:15952784}.
DISULFID 267 282 {ECO:0000269|PubMed:15952784}.
DISULFID 449 475 {ECO:0000250}.
DISULFID 639 666 {ECO:0000250}.
VARIANT 15 15 L -> H (in THPH5; reduced mutant protein
levels and secretion).
{ECO:0000269|PubMed:10790208,
ECO:0000269|PubMed:18322254}.
/FTId=VAR_046802.
VARIANT 18 18 V -> E (in THPH5; expresses very low/
undetectable PROS1 levels compared to
wild-type; has impaired secretion;
intracellular degradation of unsecreted
material is found).
{ECO:0000269|PubMed:11858485}.
/FTId=VAR_046803.
VARIANT 40 40 R -> L (in THPH5; dbSNP:rs7614835).
{ECO:0000269|PubMed:7803790}.
/FTId=VAR_046804.
VARIANT 41 41 R -> H (in THPH5; dbSNP:rs963668412).
{ECO:0000269|PubMed:7803790}.
/FTId=VAR_046805.
VARIANT 50 50 K -> E (in THPH5; dbSNP:rs748630360).
{ECO:0000269|PubMed:8943854}.
/FTId=VAR_046806.
VARIANT 52 52 G -> D (in THPH5; does not affect PROS1
production but results in 15.2-fold
reduced PROS1 activity; has 5.4 fold
reduced affinity for anionic phospholipid
vesicles (P < 0.0001) and decreased
affinity for an antibody specific for the
Ca(2+)-dependent conformation of the
PROS1 Gla domain).
{ECO:0000269|PubMed:12351389}.
/FTId=VAR_046807.
VARIANT 67 67 E -> A (in THPH5; dbSNP:rs766423432).
{ECO:0000269|PubMed:10613647,
ECO:0000269|PubMed:15712227,
ECO:0000269|PubMed:7803790,
ECO:0000269|PubMed:8943854}.
/FTId=VAR_046808.
VARIANT 68 68 A -> D (in THPH5).
{ECO:0000269|PubMed:9241758}.
/FTId=VAR_046809.
VARIANT 72 72 F -> C (in THPH5).
{ECO:0000269|PubMed:7803790}.
/FTId=VAR_046810.
VARIANT 76 76 P -> L (in dbSNP:rs73846070).
{ECO:0000269|PubMed:10613647,
ECO:0000269|PubMed:15712227,
ECO:0000269|PubMed:7803790}.
/FTId=VAR_046811.
VARIANT 78 78 T -> M (in THPH5; reduces expression of
PROS1 by 33.2% (P < 0.001) and activity
by 3.6-fold; has only a modest 1.5-fold
(P < 0.001) reduced affinity for
phospholipid and an antibody specific for
the Ca(2+)-dependent conformation of the
PROS1 Gla domain; dbSNP:rs6122).
{ECO:0000269|PubMed:12351389,
ECO:0000269|PubMed:7803790}.
/FTId=VAR_014666.
VARIANT 87 87 V -> L (in THPH5; dbSNP:rs557733421).
{ECO:0000269|PubMed:15238143}.
/FTId=VAR_046812.
VARIANT 88 88 C -> Y (in THPH5).
{ECO:0000269|PubMed:15712227}.
/FTId=VAR_046813.
VARIANT 90 90 R -> C (in THPH5; produces around 50% of
PROS1 levels compared to wild-type; has
impaired secretion; intracellular
degradation of unsecreted material is
found; dbSNP:rs765935815).
{ECO:0000269|PubMed:11858485}.
/FTId=VAR_046814.
VARIANT 90 90 R -> H (in THPH5; dbSNP:rs200886866).
{ECO:0000269|PubMed:7803790}.
/FTId=VAR_046815.
VARIANT 95 95 G -> E (in THPH5; dbSNP:rs144526169).
{ECO:0000269|PubMed:8943854}.
/FTId=VAR_046816.
VARIANT 95 95 G -> R (in THPH5; the activated protein
cofactor activity is inhibited by C4BPB
with a dose dependency similar to that of
wild-type PROS1).
{ECO:0000269|PubMed:11927129,
ECO:0000269|PubMed:9241758}.
/FTId=VAR_046817.
VARIANT 98 98 T -> S (in dbSNP:rs142805170).
{ECO:0000269|PubMed:10790208}.
/FTId=VAR_046818.
VARIANT 101 101 R -> C (in THPH5; dbSNP:rs778731080).
{ECO:0000269|PubMed:12632031}.
/FTId=VAR_046819.
VARIANT 111 111 R -> S (in THPH5).
{ECO:0000269|PubMed:8765219}.
/FTId=VAR_046820.
VARIANT 121 121 C -> Y (in THPH5).
{ECO:0000269|PubMed:15238143}.
/FTId=VAR_046821.
VARIANT 129 129 D -> G (in THPH5; dbSNP:rs749024073).
{ECO:0000269|PubMed:10613647,
ECO:0000269|PubMed:15712227}.
/FTId=VAR_046822.
VARIANT 144 144 T -> N (in THPH5; dbSNP:rs146366248).
{ECO:0000269|PubMed:12632031,
ECO:0000269|PubMed:15712227,
ECO:0000269|PubMed:7803790}.
/FTId=VAR_046823.
VARIANT 149 149 W -> C (in THPH5).
{ECO:0000269|PubMed:11776305}.
/FTId=VAR_046824.
VARIANT 157 157 D -> G (in THPH5; dbSNP:rs751090951).
{ECO:0000269|PubMed:8765219}.
/FTId=VAR_046825.
VARIANT 161 161 C -> G (in THPH5).
{ECO:0000269|PubMed:8765219}.
/FTId=VAR_046826.
VARIANT 166 166 N -> Y (in THPH5).
{ECO:0000269|PubMed:10706858}.
/FTId=VAR_046827.
VARIANT 168 168 N -> S (in dbSNP:rs144430063).
{ECO:0000269|PubMed:12632031}.
/FTId=VAR_046828.
VARIANT 175 175 C -> F (in THPH5).
{ECO:0000269|PubMed:10613647,
ECO:0000269|PubMed:15712227}.
/FTId=VAR_046829.
VARIANT 186 186 C -> Y (in THPH5; dbSNP:rs779391826).
{ECO:0000269|PubMed:8781426,
ECO:0000269|PubMed:8943854}.
/FTId=VAR_046830.
VARIANT 196 196 K -> E (in THPH5; Tokushima; the specific
activity decreases to 58% of that of the
wild-type PROS1; the activated protein
cofactor activity is inhibited by C4BPB
with a dose dependency similar to that of
wild-type PROS1; dbSNP:rs121918474).
{ECO:0000269|PubMed:11927129,
ECO:0000269|PubMed:15238143,
ECO:0000269|PubMed:8298131}.
/FTId=VAR_005566.
VARIANT 204 204 E -> G (in THPH5).
{ECO:0000269|PubMed:15712227}.
/FTId=VAR_046831.
VARIANT 233 233 R -> K (neutral polymorphism; does not
affect protein levels; the mutant is
normally secreted; dbSNP:rs41267007).
{ECO:0000269|PubMed:10790208,
ECO:0000269|PubMed:18322254,
ECO:0000269|PubMed:27535533}.
/FTId=VAR_046832.
VARIANT 234 234 Y -> C (in THPH6; dbSNP:rs387906675).
{ECO:0000269|PubMed:20484936}.
/FTId=VAR_067302.
VARIANT 241 241 C -> S (in THPH5).
{ECO:0000269|PubMed:8943854}.
/FTId=VAR_046833.
VARIANT 243 243 D -> N (in THPH5).
{ECO:0000269|PubMed:11372770}.
/FTId=VAR_046834.
VARIANT 245 245 D -> G (in THPH5).
{ECO:0000269|PubMed:7803790}.
/FTId=VAR_046835.
VARIANT 247 247 C -> G (in THPH5).
{ECO:0000269|PubMed:10706858}.
/FTId=VAR_046836.
VARIANT 249 249 E -> K (in THPH5).
{ECO:0000269|PubMed:7803790}.
/FTId=VAR_046837.
VARIANT 258 258 N -> S (in THPH5; produces around 30% of
PROS1 levels compared to wild-type; has
impaired secretion; intracellular
degradation of unsecreted material is
found; dbSNP:rs121918473).
{ECO:0000269|PubMed:11858485,
ECO:0000269|PubMed:7545463,
ECO:0000269|Ref.15}.
/FTId=VAR_005567.
VARIANT 265 265 C -> R (in THPH5).
{ECO:0000269|PubMed:7803790}.
/FTId=VAR_046838.
VARIANT 265 265 C -> W (in THPH5).
{ECO:0000269|PubMed:7803790}.
/FTId=VAR_046839.
VARIANT 266 266 Y -> C (in THPH5; dbSNP:rs777616039).
{ECO:0000269|PubMed:15712227}.
/FTId=VAR_046840.
VARIANT 267 267 C -> S (in THPH5).
{ECO:0000269|PubMed:15712227}.
/FTId=VAR_046841.
VARIANT 300 300 L -> P (in THPH5).
{ECO:0000269|PubMed:8701404}.
/FTId=VAR_046842.
VARIANT 324 324 S -> P (in THPH5).
{ECO:0000269|PubMed:8943854}.
/FTId=VAR_046843.
VARIANT 336 336 G -> D (in THPH5).
{ECO:0000269|PubMed:15712227}.
/FTId=VAR_046844.
VARIANT 336 336 G -> S (in THPH5).
{ECO:0000269|PubMed:9241758}.
/FTId=VAR_046845.
VARIANT 336 336 G -> V (in THPH5; expresses very low/
undetectable PROS1 levels compared to
wild-type; has impaired secretion;
intracellular degradation of unsecreted
material is found).
{ECO:0000269|PubMed:11858485}.
/FTId=VAR_046846.
VARIANT 339 339 L -> P (in THPH5).
{ECO:0000269|PubMed:11372770}.
/FTId=VAR_046847.
VARIANT 351 351 L -> P (in THPH5).
{ECO:0000269|PubMed:7579449}.
/FTId=VAR_046848.
VARIANT 355 355 R -> H (in THPH5; dbSNP:rs780863931).
{ECO:0000269|PubMed:15238143}.
/FTId=VAR_046849.
VARIANT 357 357 G -> R (in THPH5; dbSNP:rs941433523).
{ECO:0000269|PubMed:15712227}.
/FTId=VAR_046850.
VARIANT 364 364 K -> E (in THPH5).
{ECO:0000269|PubMed:8765219}.
/FTId=VAR_046851.
VARIANT 376 376 D -> N (in THPH5).
{ECO:0000269|PubMed:7803790}.
/FTId=VAR_046852.
VARIANT 381 381 G -> D (in THPH5).
{ECO:0000269|PubMed:8943854}.
/FTId=VAR_046853.
VARIANT 381 381 G -> V (in THPH5).
{ECO:0000269|PubMed:7482398}.
/FTId=VAR_046854.
VARIANT 383 383 W -> R (in THPH5).
{ECO:0000269|PubMed:11776305}.
/FTId=VAR_046855.
VARIANT 385 385 M -> V (in dbSNP:rs767653920).
{ECO:0000269|PubMed:7803790}.
/FTId=VAR_046856.
VARIANT 390 390 E -> K (in THPH5).
{ECO:0000269|PubMed:11776305}.
/FTId=VAR_046857.
VARIANT 446 446 L -> P (in THPH5).
{ECO:0000269|PubMed:15712227,
ECO:0000269|PubMed:8765219}.
/FTId=VAR_046858.
VARIANT 449 449 C -> S (in THPH5).
{ECO:0000269|PubMed:8943854}.
/FTId=VAR_046859.
VARIANT 475 475 C -> R (in THPH5).
{ECO:0000269|PubMed:8765219}.
/FTId=VAR_046860.
VARIANT 482 482 G -> C (in THPH5).
{ECO:0000269|PubMed:10447256}.
/FTId=VAR_014116.
VARIANT 485 485 Y -> C (in THPH5).
{ECO:0000269|PubMed:10447256}.
/FTId=VAR_014117.
VARIANT 501 501 S -> A (in THPH5; dbSNP:rs121918472).
{ECO:0000269|PubMed:8765219}.
/FTId=VAR_046862.
VARIANT 501 501 S -> P (variant Heerlen; could be
associated with THPH5;
dbSNP:rs121918472).
{ECO:0000269|PubMed:10447256,
ECO:0000269|PubMed:15712227,
ECO:0000269|PubMed:2143091,
ECO:0000269|PubMed:8765219,
ECO:0000269|PubMed:8943854}.
/FTId=VAR_005568.
VARIANT 508 508 V -> G (in THPH5).
{ECO:0000269|PubMed:7482398}.
/FTId=VAR_046863.
VARIANT 508 508 V -> M (in THPH5).
{ECO:0000269|PubMed:8765219}.
/FTId=VAR_046864.
VARIANT 515 515 R -> C (in THPH5; secretion of the mutant
markedly decreased compared with that of
the wild-type; intracellular degradation
and impaired secretion of the mutant;
dbSNP:rs199469500).
{ECO:0000269|PubMed:8639833,
ECO:0000269|PubMed:8765219}.
/FTId=VAR_046865.
VARIANT 515 515 R -> P (in THPH5).
{ECO:0000269|PubMed:10613647,
ECO:0000269|PubMed:15712227}.
/FTId=VAR_046866.
VARIANT 521 521 G -> D (in THPH5).
{ECO:0000269|PubMed:15712227}.
/FTId=VAR_046867.
VARIANT 525 525 A -> P (in THPH5).
{ECO:0000269|PubMed:8765219}.
/FTId=VAR_046868.
VARIANT 526 526 L -> S (in THPH5).
{ECO:0000269|PubMed:11776305}.
/FTId=VAR_046869.
VARIANT 532 532 T -> A (in THPH5; dbSNP:rs371028997).
{ECO:0000269|PubMed:8765219}.
/FTId=VAR_046870.
VARIANT 545 545 E -> G (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035981.
VARIANT 552 552 L -> S (in THPH5).
{ECO:0000269|PubMed:7579449}.
/FTId=VAR_046871.
VARIANT 559 559 I -> M (in dbSNP:rs184798444).
{ECO:0000269|PubMed:10447256,
ECO:0000269|PubMed:10790208,
ECO:0000269|PubMed:15712227}.
/FTId=VAR_014118.
VARIANT 561 561 R -> G (in THPH5; dbSNP:rs121918476).
{ECO:0000269|PubMed:10447256}.
/FTId=VAR_014119.
VARIANT 562 562 I -> L (in THPH5; unknown pathological
significance).
{ECO:0000269|PubMed:10613647,
ECO:0000269|PubMed:15712227}.
/FTId=VAR_046872.
VARIANT 568 568 C -> Y (in THPH5).
{ECO:0000269|PubMed:8765219}.
/FTId=VAR_046873.
VARIANT 575 575 L -> R (in THPH5).
{ECO:0000269|PubMed:8765219}.
/FTId=VAR_046874.
VARIANT 583 583 N -> H (in dbSNP:rs139479630).
{ECO:0000269|PubMed:15712227}.
/FTId=VAR_046875.
VARIANT 584 584 L -> Q (in THPH5).
{ECO:0000269|PubMed:7579449}.
/FTId=VAR_046876.
VARIANT 611 611 M -> K (in THPH5).
{ECO:0000269|PubMed:15712227}.
/FTId=VAR_046877.
VARIANT 611 611 M -> T (in THPH5; dbSNP:rs750531364).
{ECO:0000269|PubMed:10706858,
ECO:0000269|PubMed:7545463,
ECO:0000269|PubMed:8781426}.
/FTId=VAR_046878.
VARIANT 616 616 A -> P (in THPH5).
{ECO:0000269|PubMed:7579449}.
/FTId=VAR_046879.
VARIANT 622 622 L -> R (in THPH5).
{ECO:0000269|PubMed:10706858}.
/FTId=VAR_046880.
VARIANT 630 630 T -> I (in THPH5; the activated protein
cofactor activity is inhibited by C4BPB
with a dose dependency similar to that of
wild-type PROS1; dbSNP:rs202190731).
{ECO:0000269|PubMed:11927129}.
/FTId=VAR_046881.
VARIANT 636 636 Y -> C (in THPH5; shows intracellular
degradation and decreased secretion;
dbSNP:rs368173480).
{ECO:0000269|PubMed:11927129}.
/FTId=VAR_046882.
VARIANT 638 638 G -> D (in THPH5).
{ECO:0000269|PubMed:10613647,
ECO:0000269|PubMed:15712227}.
/FTId=VAR_046883.
VARIANT 639 639 C -> F (in THPH5).
{ECO:0000269|PubMed:9031443}.
/FTId=VAR_046884.
VARIANT 639 639 C -> Y (in THPH5).
{ECO:0000269|PubMed:15712227}.
/FTId=VAR_046885.
VARIANT 640 640 M -> T (in THPH5; does not affect protein
levels; the mutant is secreted at lower
levels compared to wild-type).
{ECO:0000269|PubMed:10790208,
ECO:0000269|PubMed:18322254}.
/FTId=VAR_046886.
VARIANT 644 644 I -> S (in THPH5).
{ECO:0000269|PubMed:8977443}.
/FTId=VAR_046887.
VARIANT 664 664 H -> P (in THPH5; expresses very low/
undetectable PROS1 levels compared to
wild-type; has impaired secretion;
intracellular degradation of unsecreted
material is found).
{ECO:0000269|PubMed:11858485}.
/FTId=VAR_046888.
VARIANT 665 665 S -> L (in THPH5; dbSNP:rs778685576).
{ECO:0000269|PubMed:8781426}.
/FTId=VAR_046889.
VARIANT 666 666 C -> R (in THPH5).
{ECO:0000269|PubMed:10706858,
ECO:0000269|PubMed:8701404,
ECO:0000269|PubMed:8765219,
ECO:0000269|PubMed:8943854}.
/FTId=VAR_046890.
VARIANT 667 667 P -> L (in THPH5).
{ECO:0000269|PubMed:10790208,
ECO:0000269|PubMed:15238143}.
/FTId=VAR_046891.
MUTAGEN 515 515 R->A,E: Markedly reduced secretion of the
mutant. {ECO:0000269|PubMed:8639833}.
MUTAGEN 515 515 R->K: No change in secretion of the
mutant. {ECO:0000269|PubMed:8639833}.
CONFLICT 11 11 L -> P (in Ref. 2; AAA36479).
{ECO:0000305}.
CONFLICT 26 26 F -> L (in Ref. 2; AAA36479).
{ECO:0000305}.
STRAND 204 212 {ECO:0000244|PDB:1Z6C}.
STRAND 227 229 {ECO:0000244|PDB:1Z6C}.
STRAND 233 235 {ECO:0000244|PDB:1Z6C}.
TURN 236 239 {ECO:0000244|PDB:1Z6C}.
STRAND 240 242 {ECO:0000244|PDB:1Z6C}.
HELIX 246 249 {ECO:0000244|PDB:1Z6C}.
STRAND 253 256 {ECO:0000244|PDB:1Z6C}.
STRAND 260 262 {ECO:0000244|PDB:1Z6C}.
STRAND 269 271 {ECO:0000244|PDB:1Z6C}.
STRAND 279 281 {ECO:0000244|PDB:1Z6C}.
SEQUENCE 676 AA; 75123 MW; 2B88A04F85403F25 CRC64;
MRVLGGRCGA LLACLLLVLP VSEANFLSKQ QASQVLVRKR RANSLLEETK QGNLERECIE
ELCNKEEARE VFENDPETDY FYPKYLVCLR SFQTGLFTAA RQSTNAYPDL RSCVNAIPDQ
CSPLPCNEDG YMSCKDGKAS FTCTCKPGWQ GEKCEFDINE CKDPSNINGG CSQICDNTPG
SYHCSCKNGF VMLSNKKDCK DVDECSLKPS ICGTAVCKNI PGDFECECPE GYRYNLKSKS
CEDIDECSEN MCAQLCVNYP GGYTCYCDGK KGFKLAQDQK SCEVVSVCLP LNLDTKYELL
YLAEQFAGVV LYLKFRLPEI SRFSAEFDFR TYDSEGVILY AESIDHSAWL LIALRGGKIE
VQLKNEHTSK ITTGGDVINN GLWNMVSVEE LEHSISIKIA KEAVMDINKP GPLFKPENGL
LETKVYFAGF PRKVESELIK PINPRLDGCI RSWNLMKQGA SGIKEIIQEK QNKHCLVTVE
KGSYYPGSGI AQFHIDYNNV SSAEGWHVNV TLNIRPSTGT GVMLALVSGN NTVPFAVSLV
DSTSEKSQDI LLSVENTVIY RIQALSLCSD QQSHLEFRVN RNNLELSTPL KIETISHEDL
QRQLAVLDKA MKAKVATYLG GLPDVPFSAT PVNAFYNGCM EVNINGVQLD LDEAISKHND
IRAHSCPSVW KKTKNS


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