Gene F10 - ENSG00000126218 | NCBI Gene ID: 2159

Details for: F10

Gene ID: 2159

Symbol: F10

Ensembl ID: ENSG00000126218

Description: coagulation factor X

Associated with

Common pathway of fibrin clot formation
(R-HSA-140875)
Defective cofactor function of fviiia variant
(R-HSA-9672396)
Defective f9 variant does not activate fx
(R-HSA-9673202)
Defective factor ix causes hemophilia b
(R-HSA-9668250)
Defective factor ix causes thrombophilia
(R-HSA-9672383)
Defective factor viii causes hemophilia a
(R-HSA-9662001)
Defects of contact activation system (cas) and kallikrein/kinin system (kks)
(R-HSA-9651496)
Disease
(R-HSA-1643685)
Diseases of hemostasis
(R-HSA-9671793)
Extrinsic pathway of fibrin clot formation
(R-HSA-140834)
Formation of fibrin clot (clotting cascade)
(R-HSA-140877)
Gamma-carboxylation, transport, and amino-terminal cleavage of proteins
(R-HSA-159854)
Gamma-carboxylation of protein precursors
(R-HSA-159740)
Gamma carboxylation, hypusinylation, hydroxylation, and arylsulfatase activation
(R-HSA-163841)
Hemostasis
(R-HSA-109582)
Intrinsic pathway of fibrin clot formation
(R-HSA-140837)
Metabolism of proteins
(R-HSA-392499)
Post-translational protein modification
(R-HSA-597592)
Removal of aminoterminal propeptides from gamma-carboxylated proteins
(R-HSA-159782)
Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the golgi apparatus
(R-HSA-159763)
Blood coagulation
(GO:0007596)
Calcium ion binding
(GO:0005509)
Endoplasmic reticulum lumen
(GO:0005788)
External side of plasma membrane
(GO:0009897)
Extracellular region
(GO:0005576)
Extracellular space
(GO:0005615)
Golgi lumen
(GO:0005796)
Phospholipid binding
(GO:0005543)
Plasma membrane
(GO:0005886)
Positive regulation of cell migration
(GO:0030335)
Positive regulation of tor signaling
(GO:0032008)
Protein binding
(GO:0005515)
Proteolysis
(GO:0006508)
Serine-type endopeptidase activity
(GO:0004252)

Cells (max top 100)

(Marker Score score is uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: enterocyte of colon (CL1000347)
Fold Change: 4.67
Marker Score: 7190
Cell Name: type A enteroendocrine cell (CL0002067)
Fold Change: 2.04
Marker Score: 821
Cell Name: fibroblast of connective tissue of nonglandular part of prostate (CL1000304)
Fold Change: 2.02
Marker Score: 1718
Cell Name: P/D1 enteroendocrine cell (CL0002268)
Fold Change: 1.92
Marker Score: 715
Cell Name: mural cell (CL0008034)
Fold Change: 1.47
Marker Score: 168930
Cell Name: hepatoblast (CL0005026)
Fold Change: 1.38
Marker Score: 4529
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: 1.33
Marker Score: 14994
Cell Name: keratocyte (CL0002363)
Fold Change: 1.25
Marker Score: 287
Cell Name: fibroblast of lung (CL0002553)
Fold Change: 1.22
Marker Score: 3200
Cell Name: fibroblast of connective tissue of glandular part of prostate (CL1000305)
Fold Change: 1.16
Marker Score: 483
Cell Name: inflammatory cell (CL0009002)
Fold Change: 1.14
Marker Score: 492
Cell Name: goblet cell (CL0000160)
Fold Change: 1.13
Marker Score: 7537.5
Cell Name: decidual cell (CL2000002)
Fold Change: 1.12
Marker Score: 4817
Cell Name: OFF retinal ganglion cell (CL4023033)
Fold Change: 1.1
Marker Score: 459
Cell Name: granulocyte monocyte progenitor cell (CL0000557)
Fold Change: 1.04
Marker Score: 658.5
Cell Name: fallopian tube secretory epithelial cell (CL4030006)
Fold Change: 1.04
Marker Score: 251792.5
Cell Name: adventitial cell (CL0002503)
Fold Change: 1.01
Marker Score: 249
Cell Name: cerebral cortex GABAergic interneuron (CL0010011)
Fold Change: 1
Marker Score: 71812
Cell Name: forebrain radial glial cell (CL0013000)
Fold Change: 1
Marker Score: 48035.5
Cell Name: absorptive cell (CL0000212)
Fold Change: 0.98
Marker Score: 30407
Cell Name: tuft cell of colon (CL0009041)
Fold Change: 0.98
Marker Score: 505
Cell Name: tracheobronchial smooth muscle cell (CL0019019)
Fold Change: 0.98
Marker Score: 287
Cell Name: BEST4+ intestinal epithelial cell, human (CL4030026)
Fold Change: 0.97
Marker Score: 459
Cell Name: PP cell (CL0000696)
Fold Change: 0.97
Marker Score: 218
Cell Name: intestinal crypt stem cell of colon (CL0009043)
Fold Change: 0.95
Marker Score: 2411
Cell Name: smooth muscle cell (CL0000192)
Fold Change: 0.94
Marker Score: 616
Cell Name: transit amplifying cell (CL0009010)
Fold Change: 0.93
Marker Score: 5318
Cell Name: intestinal epithelial cell (CL0002563)
Fold Change: 0.93
Marker Score: 1507
Cell Name: abnormal cell (CL0001061)
Fold Change: 0.91
Marker Score: 2740
Cell Name: secondary lens fiber (CL0002225)
Fold Change: 0.91
Marker Score: 534
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: 0.9
Marker Score: 324
Cell Name: transit amplifying cell of small intestine (CL0009012)
Fold Change: 0.88
Marker Score: 364.5
Cell Name: neoplastic cell (CL0001063)
Fold Change: 0.87
Marker Score: 5296
Cell Name: midzonal region hepatocyte (CL0019028)
Fold Change: 0.84
Marker Score: 3624
Cell Name: small intestine goblet cell (CL1000495)
Fold Change: 0.82
Marker Score: 330
Cell Name: ON retinal ganglion cell (CL4023032)
Fold Change: 0.79
Marker Score: 217
Cell Name: early T lineage precursor (CL0002425)
Fold Change: 0.79
Marker Score: 604
Cell Name: centrilobular region hepatocyte (CL0019029)
Fold Change: 0.78
Marker Score: 5010
Cell Name: Cajal-Retzius cell (CL0000695)
Fold Change: 0.76
Marker Score: 394
Cell Name: enterocyte of epithelium of small intestine (CL1000334)
Fold Change: 0.76
Marker Score: 3176.5
Cell Name: brush cell (CL0002204)
Fold Change: 0.75
Marker Score: 686
Cell Name: enteroendocrine cell (CL0000164)
Fold Change: 0.74
Marker Score: 385
Cell Name: endocrine cell (CL0000163)
Fold Change: 0.73
Marker Score: 380
Cell Name: precursor B cell (CL0000817)
Fold Change: 0.73
Marker Score: 484
Cell Name: interstitial cell of ovary (CL0002094)
Fold Change: 0.7
Marker Score: 4561
Cell Name: neutrophil progenitor cell (CL0000834)
Fold Change: 0.7
Marker Score: 179
Cell Name: progenitor cell of endocrine pancreas (CL0002351)
Fold Change: 0.69
Marker Score: 149
Cell Name: gut absorptive cell (CL0000677)
Fold Change: 0.68
Marker Score: 437
Cell Name: type G enteroendocrine cell (CL0000508)
Fold Change: 0.68
Marker Score: 235
Cell Name: fibroblast (CL0000057)
Fold Change: 0.68
Marker Score: 653
Cell Name: fibroblast of connective tissue of prostate (CL1000299)
Fold Change: 0.67
Marker Score: 167
Cell Name: reticular cell (CL0000432)
Fold Change: 0.67
Marker Score: 244
Cell Name: prostate stromal cell (CL0002622)
Fold Change: 0.67
Marker Score: 167
Cell Name: M cell of gut (CL0000682)
Fold Change: 0.65
Marker Score: 168
Cell Name: periportal region hepatocyte (CL0019026)
Fold Change: 0.63
Marker Score: 3398
Cell Name: type I enteroendocrine cell (CL0002277)
Fold Change: 0.62
Marker Score: 154
Cell Name: pancreatic D cell (CL0000173)
Fold Change: 0.61
Marker Score: 267
Cell Name: vascular associated smooth muscle cell (CL0000359)
Fold Change: 0.61
Marker Score: 281
Cell Name: stromal cell (CL0000499)
Fold Change: 0.6
Marker Score: 706
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: 0.59
Marker Score: 2476
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: 0.58
Marker Score: 19712
Cell Name: supporting cell (CL0000630)
Fold Change: 0.58
Marker Score: 1083
Cell Name: megakaryocyte-erythroid progenitor cell (CL0000050)
Fold Change: 0.57
Marker Score: 238
Cell Name: pericyte (CL0000669)
Fold Change: 0.57
Marker Score: 332
Cell Name: bronchial smooth muscle cell (CL0002598)
Fold Change: 0.56
Marker Score: 159
Cell Name: renal beta-intercalated cell (CL0002201)
Fold Change: 0.55
Marker Score: 175
Cell Name: intestinal enteroendocrine cell (CL1001516)
Fold Change: 0.55
Marker Score: 440
Cell Name: smooth muscle cell of prostate (CL1000487)
Fold Change: 0.53
Marker Score: 136
Cell Name: common myeloid progenitor (CL0000049)
Fold Change: 0.52
Marker Score: 139
Cell Name: hepatocyte (CL0000182)
Fold Change: 0.51
Marker Score: 345
Cell Name: pancreatic A cell (CL0000171)
Fold Change: 0.5
Marker Score: 488.5
Cell Name: mesodermal cell (CL0000222)
Fold Change: 0.49
Marker Score: 6455.5
Cell Name: pro-B cell (CL0000826)
Fold Change: 0.49
Marker Score: 472
Cell Name: mesenchymal stem cell (CL0000134)
Fold Change: 0.49
Marker Score: 751.5
Cell Name: kidney cell (CL1000497)
Fold Change: 0.48
Marker Score: 322
Cell Name: hepatic stellate cell (CL0000632)
Fold Change: 0.48
Marker Score: 180
Cell Name: lens fiber cell (CL0011004)
Fold Change: 0.45
Marker Score: 142
Cell Name: type L enteroendocrine cell (CL0002279)
Fold Change: 0.44
Marker Score: 120
Cell Name: fibroblast of breast (CL4006000)
Fold Change: 0.43
Marker Score: 248
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: 0.43
Marker Score: 197
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: 0.42
Marker Score: 6546
Cell Name: muscle precursor cell (CL0000680)
Fold Change: 0.42
Marker Score: 108
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: 0.41
Marker Score: 409
Cell Name: vascular leptomeningeal cell (CL4023051)
Fold Change: 0.41
Marker Score: 474
Cell Name: cardiac endothelial cell (CL0010008)
Fold Change: 0.41
Marker Score: 777
Cell Name: neuroendocrine cell (CL0000165)
Fold Change: 0.41
Marker Score: 158
Cell Name: theca cell (CL0000503)
Fold Change: 0.4
Marker Score: 284
Cell Name: kidney interstitial cell (CL1000500)
Fold Change: 0.39
Marker Score: 279
Cell Name: A2 amacrine cell (CL0004219)
Fold Change: 0.38
Marker Score: 121
Cell Name: mesenchymal lymphangioblast (CL0005021)
Fold Change: 0.38
Marker Score: 85
Cell Name: pancreatic stellate cell (CL0002410)
Fold Change: 0.38
Marker Score: 240
Cell Name: interstitial cell of Cajal (CL0002088)
Fold Change: 0.37
Marker Score: 127
Cell Name: fraction A pre-pro B cell (CL0002045)
Fold Change: 0.37
Marker Score: 369
Cell Name: kidney proximal straight tubule epithelial cell (CL1000839)
Fold Change: 0.35
Marker Score: 834
Cell Name: myeloid cell (CL0000763)
Fold Change: 0.34
Marker Score: 553
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: 0.34
Marker Score: 108
Cell Name: endothelial cell of pericentral hepatic sinusoid (CL0019022)
Fold Change: 0.34
Marker Score: 365
Cell Name: mast cell (CL0000097)
Fold Change: 0.34
Marker Score: 197
Cell Name: cholangiocyte (CL1000488)
Fold Change: 0.34
Marker Score: 127
Cell Name: muscle cell (CL0000187)
Fold Change: 0.34
Marker Score: 96

Hover over a box to see details here...

**Key characteristics:** * F10 is a coagulation factor that is involved in the extrinsic pathway of fibrin clot formation. * It is a glycoprotein with a molecular weight of approximately 110 kDa. * It is synthesized as a pro-protein and is processed to form the mature protein. * It is a key regulator of blood clotting and is involved in the prevention of excessive bleeding. **Pathways and functions:** * The F10 gene is involved in the formation of fibrin clots through the extrinsic pathway. * The protein is expressed in the enterocyte of the colon, where it is produced and secreted into the lumen of the colon. * It is also expressed in the fibroblasts of connective tissue of the prostate, suggesting a role in hemostasis in this tissue. * F10 also plays a role in the intrinsic pathway of fibrin clot formation, where it is expressed in the liver. * It is involved in the metabolism of proteins and is a key regulator of blood clotting. **Clinical significance:** Mutations in the F10 gene have been linked to several bleeding disorders, including hemophilia. * Hemophilia A is caused by mutations in the F10 gene, which results in a deficiency of coagulation factor VIII. * Hemophilia B is caused by mutations in the F10 gene, which results in a deficiency of coagulation factor IX. * Hemophilia IX is caused by mutations in the F10 gene, which results in a deficiency of coagulation factor IX. * These bleeding disorders can be prevented by prophylactic factor replacement therapy, which involves the administration of clotting factors to correct the deficiency.

Disclaimer: This summary is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

Coagulation factor X
Q5JVE8_HUMAN

Genular Protein ID: 3057900335

Symbol: FA10_HUMAN

Name: Coagulation factor X

UniProtKB Accession Codes:

P00742 Q14340

Database IDs:

Citations:

PubMed ID: 1902434

Title: Cloning and expression in COS-1 cells of a full-length cDNA encoding human coagulation factor X.

PubMed ID: 1902434

DOI: 10.1016/0378-1119(91)90141-w

PubMed ID: 3768336

Title: Gene for human factor X: a blood coagulation factor whose gene organization is essentially identical with that of factor IX and protein C.

PubMed ID: 3768336

DOI: 10.1021/bi00366a018

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 2582420

Title: Characterization of an almost full-length cDNA coding for human blood coagulation factor X.

PubMed ID: 2582420

DOI: 10.1073/pnas.82.11.3591

PubMed ID: 3011603

Title: Isolation and characterization of human blood-coagulation factor X cDNA.

PubMed ID: 3011603

DOI: 10.1016/0378-1119(86)90112-5

PubMed ID: 6871167

Title: Complete amino acid sequence of the light chain of human blood coagulation factor X: evidence for identification of residue 63 as beta-hydroxyaspartic acid.

PubMed ID: 6871167

DOI: 10.1021/bi00281a016

PubMed ID: 6587384

Title: Characterization of a cDNA coding for human factor X.

PubMed ID: 6587384

DOI: 10.1073/pnas.81.12.3699

PubMed ID: 8243461

Title: Identification of O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X. The role of the carbohydrate moieties in the activation of factor X.

PubMed ID: 8243461

DOI: 10.1111/j.1432-1033.1993.tb18361.x

PubMed ID: 2612918

Title: Cloning and characterization of the 5' end (exon 1) of the gene encoding human factor X.

PubMed ID: 2612918

DOI: 10.1016/0378-1119(89)90529-5

PubMed ID: 6323392

Title: Mechanism of inhibition of activated protein C by protein C inhibitor.

PubMed ID: 6323392

DOI: 10.1093/oxfordjournals.jbchem.a134583

PubMed ID: 8920993

Title: Activation of Mac-1 (CD11b/CD18)-bound factor X by released cathepsin G defines an alternative pathway of leucocyte initiation of coagulation.

PubMed ID: 8920993

DOI: 10.1042/bj3190873

PubMed ID: 20427285

Title: Basis for the specificity and activation of the serpin protein Z-dependent proteinase inhibitor (ZPI) as an inhibitor of membrane-associated factor Xa.

PubMed ID: 20427285

DOI: 10.1074/jbc.m110.112748

PubMed ID: 22171320

Title: Human urinary glycoproteomics; attachment site specific analysis of N- and O-linked glycosylations by CID and ECD.

PubMed ID: 22171320

DOI: 10.1074/mcp.m111.013649

PubMed ID: 8355279

Title: Structure of human des(1-45) factor Xa at 2.2-A resolution.

PubMed ID: 8355279

DOI: 10.1006/jmbi.1993.1441

PubMed ID: 9618463

Title: Structural basis for chemical inhibition of human blood coagulation factor Xa.

PubMed ID: 9618463

DOI: 10.1073/pnas.95.12.6630

PubMed ID: 17227710

Title: Substituted thiophene-anthranilamides as potent inhibitors of human factor Xa.

PubMed ID: 17227710

DOI: 10.1016/j.bmc.2006.12.019

PubMed ID: 2790181

Title: Molecular characterization of human factor XSan Antonio.

PubMed ID: 2790181

PubMed ID: 1973167

Title: Molecular defect (Gla+14TO: hereditary factor X deficiency (factor X 'Vorarlberg').

PubMed ID: 1973167

DOI: 10.1016/s0021-9258(19)38497-2

PubMed ID: 1985698

Title: Molecular defect in coagulation factor XFriuli results from a substitution of serine for proline at position 343.

PubMed ID: 1985698

PubMed ID: 7669671

Title: Molecular bases of CRM+ factor X deficiency: a frequent mutation (Ser334Pro) in the catalytic domain and a substitution (Glu102Lys) in the second EGF-like domain.

PubMed ID: 7669671

DOI: 10.1111/j.1365-2141.1995.tb05214.x

PubMed ID: 8529633

Title: Functional consequences of the Ser334-->Pro mutation in a human factor X variant (factor XMarseille).

PubMed ID: 8529633

DOI: 10.1111/j.1432-1033.1995.140_c.x

PubMed ID: 7860069

Title: Factor XKetchikan: a variant molecule in which Gly replaces a Gla residue at position 14 in the light chain.

PubMed ID: 7860069

DOI: 10.1007/bf00209404

PubMed ID: 8845463

Title: Factor X Stockton: a mild bleeding diathesis associated with an active site mutation in factor X.

PubMed ID: 8845463

PubMed ID: 8910490

Title: Factor XSt. Louis II. Identification of a glycine substitution at residue 7 and characterization of the recombinant protein.

PubMed ID: 8910490

DOI: 10.1074/jbc.271.45.28601

PubMed ID: 10468877

Title: A family with hereditary factor X deficiency with a point mutation Gla32 to Gln in the Gla domain (factor X Tokyo).

PubMed ID: 10468877

DOI: 10.1046/j.1365-2141.1999.01614.x

PubMed ID: 10391209

Title: Characterization of single-nucleotide polymorphisms in coding regions of human genes.

PubMed ID: 10391209

DOI: 10.1038/10290

PubMed ID: 10746568

Title: Molecular analysis of the genotype-phenotype relationship in factor X deficiency.

PubMed ID: 10746568

DOI: 10.1007/s004390051035

PubMed ID: 10739379

Title: The impact of Glu102Lys on the factor X function in a patient with a doubly homozygous factor X deficiency (Gla14Lys and Glu102Lys).

PubMed ID: 10739379

PubMed ID: 11248282

Title: A dysfunctional factor X (factor X San Giovanni Rotondo) present at homozygous and double heterozygous level: identification of a novel microdeletion (delC556) and missense mutation (Lys(408)-->Asn) in the factor X gene. A study of an Italian family.

PubMed ID: 11248282

DOI: 10.1016/s0049-3848(00)00406-0

PubMed ID: 11728527

Title: A new factor X defect (factor X Padua 3): a compound heterozygous between true deficiency (Gly(380)-->Arg) and an abnormality (Ser(334)-->Pro).

PubMed ID: 11728527

DOI: 10.1016/s0049-3848(01)00371-1

PubMed ID: 12945883

Title: A novel type I factor X variant (factor X Cys350Phe) due to loss of a disulfide bond in the catalytic domain.

PubMed ID: 12945883

DOI: 10.1097/00001721-200306000-00012

PubMed ID: 12574802

Title: Impaired prothrombinase activity of factor X Gly381Asp results in severe familial CRM+ FX deficiency.

PubMed ID: 12574802

PubMed ID: 15075089

Title: Molecular characterization of factor X deficiency associated with borderline plasma factor X level.

PubMed ID: 15075089

PubMed ID: 15650540

Title: Genetic analysis of hereditary factor X deficiency in a French patient of Sri Lankan ancestry: in vitro expression study identified Gly366Ser substitution as the molecular basis of the dysfunctional factor X.

PubMed ID: 15650540

DOI: 10.1097/00001721-200501000-00002

PubMed ID: 17393015

Title: Analysis of the novel factor X gene mutation Glu51Lys in two families with factor X-Riyadh anomaly.

PubMed ID: 17393015

DOI: 10.1160/th06-09-0532

PubMed ID: 19135706

Title: Characterization of a homozygous Gly11Val mutation in the Gla domain of coagulation factor X.

PubMed ID: 19135706

DOI: 10.1016/j.thromres.2008.11.018

PubMed ID: 25313940

Title: Molecular dynamics characterization of five pathogenic Factor X mutants associated with decreased catalytic activity.

PubMed ID: 25313940

DOI: 10.1021/bi500770p

PubMed ID: 26222694

Title: Frequency of the p.Gly262Asp mutation in congenital Factor X deficiency.

PubMed ID: 26222694

DOI: 10.1111/eci.12511

Sequence Information:

Length: 488
Mass: 54732
Checksum: F81D5746AF4797AF
Sequence:

MGRPLHLVLL SASLAGLLLL GESLFIRREQ ANNILARVTR ANSFLEEMKK GHLERECMEE 
TCSYEEAREV FEDSDKTNEF WNKYKDGDQC ETSPCQNQGK CKDGLGEYTC TCLEGFEGKN 
CELFTRKLCS LDNGDCDQFC HEEQNSVVCS CARGYTLADN GKACIPTGPY PCGKQTLERR 
KRSVAQATSS SGEAPDSITW KPYDAADLDP TENPFDLLDF NQTQPERGDN NLTRIVGGQE 
CKDGECPWQA LLINEENEGF CGGTILSEFY ILTAAHCLYQ AKRFKVRVGD RNTEQEEGGE 
AVHEVEVVIK HNRFTKETYD FDIAVLRLKT PITFRMNVAP ACLPERDWAE STLMTQKTGI 
VSGFGRTHEK GRQSTRLKML EVPYVDRNSC KLSSSFIITQ NMFCAGYDTK QEDACQGDSG 
GPHVTRFKDT YFVTGIVSWG EGCARKGKYG IYTKVTAFLK WIDRSMKTRG LPKAKSHAPE 
VITSSPLK

Genular Protein ID: 1556262470

Symbol: Q5JVE8_HUMAN

Name: N/A

UniProtKB Accession Codes:

Q5JVE8

Database IDs:

Citations:

PubMed ID: 15057823

Title: The DNA sequence and analysis of human chromosome 13.

PubMed ID: 15057823

DOI: 10.1038/nature02379

Sequence Information:

Length: 332
Mass: 37094
Checksum: 434393FC2A30A8FB
Sequence:

MGRPLHLVLL SASLAGLLLL GESLFIRREQ ANNILARVTR ANSFLEEMKK GHLERECMEE 
TCSYEEAREV FEDSDKTNEF WNKYKDGDQC ETSPCQNQGK CKDGLGEYTC TCLEGFEGKN 
CELFTRKLCS LDNGDCDQFC HEEQNSVVCS CARGYTLADN GKACIPTGPY PCGKQTLERR 
KRSVAQATSS SGEAPDSITW KPYDAADLDP TENPFDLLDF NQTQPERGDN NLTRIVGGQE 
CKDGECPWQA LLINEENEGF CGGTILSEFY ILTAAHCLYQ AKRFKGTGTR SRRRAVRRCT 
RWRWSSSTTG SQRRPMTSTS PCSGSRPPSP SA

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. For the full schema, download it here.

Details for: F10

Associated with

Cells (max top 100)

Other Information

Cloning and expression in COS-1 cells of a full-length cDNA encoding human coagulation factor X. PubMed ID: 1902434

Gene for human factor X: a blood coagulation factor whose gene organization is essentially identical with that of factor IX and protein C. PubMed ID: 3768336

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Characterization of an almost full-length cDNA coding for human blood coagulation factor X. PubMed ID: 2582420

Isolation and characterization of human blood-coagulation factor X cDNA. PubMed ID: 3011603

Complete amino acid sequence of the light chain of human blood coagulation factor X: evidence for identification of residue 63 as beta-hydroxyaspartic acid. PubMed ID: 6871167

Characterization of a cDNA coding for human factor X. PubMed ID: 6587384

Identification of O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X. The role of the carbohydrate moieties in the activation of factor X. PubMed ID: 8243461

Cloning and characterization of the 5' end (exon 1) of the gene encoding human factor X. PubMed ID: 2612918

Mechanism of inhibition of activated protein C by protein C inhibitor. PubMed ID: 6323392

Activation of Mac-1 (CD11b/CD18)-bound factor X by released cathepsin G defines an alternative pathway of leucocyte initiation of coagulation. PubMed ID: 8920993

Basis for the specificity and activation of the serpin protein Z-dependent proteinase inhibitor (ZPI) as an inhibitor of membrane-associated factor Xa. PubMed ID: 20427285

Human urinary glycoproteomics; attachment site specific analysis of N- and O-linked glycosylations by CID and ECD. PubMed ID: 22171320

Structure of human des(1-45) factor Xa at 2.2-A resolution. PubMed ID: 8355279

Structural basis for chemical inhibition of human blood coagulation factor Xa. PubMed ID: 9618463

Substituted thiophene-anthranilamides as potent inhibitors of human factor Xa. PubMed ID: 17227710

Molecular characterization of human factor XSan Antonio. PubMed ID: 2790181

Molecular defect (Gla+14TO: hereditary factor X deficiency (factor X 'Vorarlberg'). PubMed ID: 1973167

Molecular defect in coagulation factor XFriuli results from a substitution of serine for proline at position 343. PubMed ID: 1985698

Molecular bases of CRM+ factor X deficiency: a frequent mutation (Ser334Pro) in the catalytic domain and a substitution (Glu102Lys) in the second EGF-like domain. PubMed ID: 7669671

Functional consequences of the Ser334--&gt;Pro mutation in a human factor X variant (factor XMarseille). PubMed ID: 8529633

Factor XKetchikan: a variant molecule in which Gly replaces a Gla residue at position 14 in the light chain. PubMed ID: 7860069

Factor X Stockton: a mild bleeding diathesis associated with an active site mutation in factor X. PubMed ID: 8845463

Factor XSt. Louis II. Identification of a glycine substitution at residue 7 and characterization of the recombinant protein. PubMed ID: 8910490

A family with hereditary factor X deficiency with a point mutation Gla32 to Gln in the Gla domain (factor X Tokyo). PubMed ID: 10468877

Characterization of single-nucleotide polymorphisms in coding regions of human genes. PubMed ID: 10391209

Molecular analysis of the genotype-phenotype relationship in factor X deficiency. PubMed ID: 10746568

The impact of Glu102Lys on the factor X function in a patient with a doubly homozygous factor X deficiency (Gla14Lys and Glu102Lys). PubMed ID: 10739379

A dysfunctional factor X (factor X San Giovanni Rotondo) present at homozygous and double heterozygous level: identification of a novel microdeletion (delC556) and missense mutation (Lys(408)--&gt;Asn) in the factor X gene. A study of an Italian family. PubMed ID: 11248282

A new factor X defect (factor X Padua 3): a compound heterozygous between true deficiency (Gly(380)--&gt;Arg) and an abnormality (Ser(334)--&gt;Pro). PubMed ID: 11728527

A novel type I factor X variant (factor X Cys350Phe) due to loss of a disulfide bond in the catalytic domain. PubMed ID: 12945883

Impaired prothrombinase activity of factor X Gly381Asp results in severe familial CRM+ FX deficiency. PubMed ID: 12574802

Molecular characterization of factor X deficiency associated with borderline plasma factor X level. PubMed ID: 15075089

Genetic analysis of hereditary factor X deficiency in a French patient of Sri Lankan ancestry: in vitro expression study identified Gly366Ser substitution as the molecular basis of the dysfunctional factor X. PubMed ID: 15650540

Analysis of the novel factor X gene mutation Glu51Lys in two families with factor X-Riyadh anomaly. PubMed ID: 17393015

Characterization of a homozygous Gly11Val mutation in the Gla domain of coagulation factor X. PubMed ID: 19135706

Molecular dynamics characterization of five pathogenic Factor X mutants associated with decreased catalytic activity. PubMed ID: 25313940

Frequency of the p.Gly262Asp mutation in congenital Factor X deficiency. PubMed ID: 26222694

The DNA sequence and analysis of human chromosome 13. PubMed ID: 15057823