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Protein

Coagulation factor X

Gene

F10

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting.

Catalytic activityi

Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.

Enzyme regulationi

Inhibited by SERPINA5 and SERPINA10.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei276 – 2761Charge relay system
Active sitei322 – 3221Charge relay system
Active sitei419 – 4191Charge relay system

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. phospholipid binding Source: BHF-UCL
  3. serine-type endopeptidase activity Source: UniProtKB

GO - Biological processi

  1. blood coagulation Source: BHF-UCL
  2. blood coagulation, extrinsic pathway Source: Reactome
  3. blood coagulation, intrinsic pathway Source: Reactome
  4. cellular protein metabolic process Source: Reactome
  5. peptidyl-glutamic acid carboxylation Source: Reactome
  6. positive regulation of cell migration Source: BHF-UCL
  7. positive regulation of protein kinase B signaling Source: BHF-UCL
  8. post-translational protein modification Source: Reactome
  9. proteolysis Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium

Enzyme and pathway databases

BioCyciMetaCyc:HS05000-MONOMER.
BRENDAi3.4.21.6. 2681.
ReactomeiREACT_1050. Gamma-carboxylation of protein precursors.
REACT_1439. Common Pathway.
REACT_1573. Extrinsic Pathway.
REACT_1906. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
REACT_326. Intrinsic Pathway.
REACT_733. Removal of aminoterminal propeptides from gamma-carboxylated proteins.
SABIO-RKP00742.

Protein family/group databases

MEROPSiS01.216.

Names & Taxonomyi

Protein namesi
Recommended name:
Coagulation factor X (EC:3.4.21.6)
Alternative name(s):
Stuart factor
Stuart-Prower factor
Cleaved into the following 3 chains:
Gene namesi
Name:F10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:3528. F10.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: Reactome
  2. extracellular region Source: UniProtKB
  3. Golgi lumen Source: Reactome
  4. intrinsic component of external side of plasma membrane Source: BHF-UCL
  5. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Factor X deficiency (FA10D)19 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA hemorrhagic disease with variable presentation. Affected individuals can manifest prolonged nasal and mucosal hemorrhage, menorrhagia, hematuria, and occasionally hemarthrosis. Some patients do not have clinical bleeding diathesis.

See also OMIM:227600
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti47 – 471E → G in FA10D; St. Louis II; strongly reduced activity; not activated by factor VIIa and tissue factor. 1 Publication
VAR_065428
Natural varianti51 – 511G → V in FA10D. 1 Publication
VAR_065429
Natural varianti54 – 541E → G in FA10D; Ketchikan. 1 Publication
VAR_065430
Natural varianti54 – 541E → K in FA10D; Vorarlberg; converts prothrombin at a normal rate but shows decreased affinity for calcium. 2 Publications
VAR_065431
Natural varianti72 – 721E → Q in FA10D; Tokyo. 1 Publication
VAR_065432
Natural varianti91 – 911E → K in FA10D; Riyadh. 1 Publication
VAR_065433
Natural varianti142 – 1421E → K in FA10D; uncertain pathological significance; detected in patients carrying K-54 or P-374; slightly reduced activity. 3 Publications
Corresponds to variant rs61753266 [ dbSNP | Ensembl ].
VAR_065434
Natural varianti149 – 1491C → Y in FA10D. 1 Publication
VAR_065435
Natural varianti151 – 1511C → Y in FA10D. 1 Publication
VAR_065436
Natural varianti289 – 2891G → R in FA10D; may affect splicing. 1 Publication
VAR_065437
Natural varianti304 – 3041E → K in FA10D. 1 Publication
VAR_065438
Natural varianti322 – 3221D → N in FA10D; Stockton; 50% decrease in specific activity; decrease in protein flexibility. 2 Publications
VAR_065439
Natural varianti327 – 3271R → W in FA10D. 1 Publication
VAR_065440
Natural varianti338 – 3381V → M in FA10D. 1 Publication
VAR_065441
Natural varianti350 – 3501E → K in FA10D. 1 Publication
VAR_065442
Natural varianti358 – 3581T → M in FA10D; Roma; decrease in protein flexibilty. 2 Publications
VAR_065443
Natural varianti363 – 3631G → S in FA10D. 1 Publication
VAR_065444
Natural varianti366 – 3661R → C in FA10D; San Antonio. 1 Publication
VAR_065445
Natural varianti374 – 3741S → P in FA10D; Marseille; decreased cleavage by factor IXa; normal catalytic efficiency for prothrombin. 3 Publications
VAR_065446
Natural varianti382 – 3821V → A in FA10D; partial loss of activity; decrease in protein flexibilty. 2 Publications
VAR_072751
Natural varianti383 – 3831P → S in FA10D; Friuli. 1 Publication
VAR_065447
Natural varianti390 – 3901C → F in FA10D; Padua 4. 1 Publication
Corresponds to variant rs199778916 [ dbSNP | Ensembl ].
VAR_065448
Natural varianti404 – 4041C → R in FA10D. 1 Publication
VAR_065449
Natural varianti406 – 4061G → S in FA10D; almost complete loss of activity; decrease in protein flexibilty. 2 Publications
VAR_065450
Natural varianti420 – 4201G → R in FA10D; Padua 3. 1 Publication
VAR_065451
Natural varianti421 – 4211G → D in FA10D; significant loss of activity; no change in protein flexibilty. 2 Publications
VAR_072752
Natural varianti448 – 4481K → N in FA10D; San Giovanni Rotondo. 1 Publication
VAR_065452

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi227600. phenotype.
Orphaneti328. Congenital factor X deficiency.
PharmGKBiPA27940.

Chemistry

DrugBankiDB00025. Antihemophilic Factor.
DB06605. Apixaban.
DB00100. Coagulation Factor IX.
DB00036. Coagulation factor VIIa.
DB01225. Enoxaparin.
DB00569. Fondaparinux sodium.
DB01109. Heparin.
DB00170. Menadione.
DB06228. Rivaroxaban.

Polymorphism and mutation databases

BioMutaiF10.
DMDMi119761.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Sequence AnalysisAdd
BLAST
Propeptidei32 – 4091 PublicationPRO_0000027786
Chaini41 – 488448Coagulation factor XPRO_0000027787Add
BLAST
Chaini41 – 179139Factor X light chainPRO_0000027788Add
BLAST
Chaini183 – 488306Factor X heavy chainPRO_0000027789Add
BLAST
Propeptidei183 – 23452Activation peptidePRO_0000027790Add
BLAST
Chaini235 – 488254Activated factor Xa heavy chainPRO_0000027791Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 4614-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei47 – 4714-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei54 – 5414-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei56 – 5614-carboxyglutamatePROSITE-ProRule annotation1 Publication
Disulfide bondi57 ↔ 62By similarity
Modified residuei59 – 5914-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei60 – 6014-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei65 – 6514-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei66 – 6614-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei69 – 6914-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei72 – 7214-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei79 – 7914-carboxyglutamatePROSITE-ProRule annotation1 Publication
Disulfide bondi90 ↔ 101
Disulfide bondi95 ↔ 110
Modified residuei103 – 1031(3R)-3-hydroxyaspartate1 Publication
Disulfide bondi112 ↔ 121
Disulfide bondi129 ↔ 140
Disulfide bondi136 ↔ 149
Disulfide bondi151 ↔ 164
Disulfide bondi172 ↔ 342Interchain (between light and heavy chains)
Glycosylationi199 – 1991O-linked (GalNAc...)1 Publication
Glycosylationi211 – 2111O-linked (GalNAc...)1 Publication
Glycosylationi221 – 2211N-linked (GlcNAc...)1 PublicationCAR_000012
Glycosylationi231 – 2311N-linked (GlcNAc...)1 PublicationCAR_000013
Disulfide bondi241 ↔ 246
Disulfide bondi261 ↔ 277
Disulfide bondi390 ↔ 404
Disulfide bondi415 ↔ 443

Post-translational modificationi

The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.
N- and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans.2 Publications
The activation peptide is cleaved by factor IXa (in the intrinsic pathway), or by factor VIIa (in the extrinsic pathway).
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Gamma-carboxyglutamic acid, Glycoprotein, Hydroxylation, Zymogen

Proteomic databases

MaxQBiP00742.
PaxDbiP00742.
PRIDEiP00742.

PTM databases

PhosphoSiteiP00742.
UniCarbKBiP00742.

Miscellaneous databases

PMAP-CutDBP00742.

Expressioni

Tissue specificityi

Plasma; synthesized in the liver.1 Publication

Gene expression databases

BgeeiP00742.
CleanExiHS_F10.
ExpressionAtlasiP00742. baseline and differential.
GenevestigatoriP00742.

Interactioni

Subunit structurei

The two chains are formed from a single-chain precursor by the excision of two Arg residues and are held together by 1 or more disulfide bonds. Forms a heterodimer with SERPINA5.

Protein-protein interaction databases

BioGridi108457. 9 interactions.
DIPiDIP-29896N.
IntActiP00742. 7 interactions.
MINTiMINT-276128.
STRINGi9606.ENSP00000364709.

Structurei

Secondary structure

1
488
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi47 – 5711Combined sources
Helixi64 – 718Combined sources
Helixi74 – 818Combined sources
Turni89 – 924Combined sources
Beta strandi96 – 983Combined sources
Beta strandi100 – 1023Combined sources
Beta strandi105 – 1073Combined sources
Beta strandi109 – 1113Combined sources
Beta strandi116 – 1183Combined sources
Beta strandi123 – 1253Combined sources
Turni129 – 1313Combined sources
Helixi132 – 1354Combined sources
Beta strandi137 – 1437Combined sources
Beta strandi146 – 1505Combined sources
Beta strandi155 – 1573Combined sources
Beta strandi164 – 1707Combined sources
Beta strandi172 – 1743Combined sources
Beta strandi236 – 2405Combined sources
Turni243 – 2453Combined sources
Beta strandi249 – 2535Combined sources
Turni255 – 2573Combined sources
Beta strandi259 – 2657Combined sources
Beta strandi267 – 2737Combined sources
Helixi275 – 2795Combined sources
Beta strandi280 – 2834Combined sources
Beta strandi285 – 2895Combined sources
Beta strandi291 – 2955Combined sources
Beta strandi301 – 3033Combined sources
Beta strandi305 – 3106Combined sources
Turni316 – 3194Combined sources
Beta strandi324 – 3307Combined sources
Helixi346 – 3527Combined sources
Turni353 – 3553Combined sources
Beta strandi356 – 3649Combined sources
Beta strandi366 – 3683Combined sources
Beta strandi372 – 3765Combined sources
Beta strandi378 – 3858Combined sources
Helixi387 – 3937Combined sources
Beta strandi402 – 4065Combined sources
Beta strandi408 – 4114Combined sources
Turni416 – 4205Combined sources
Beta strandi422 – 4276Combined sources
Beta strandi430 – 43910Combined sources
Beta strandi441 – 4444Combined sources
Beta strandi450 – 4545Combined sources
Helixi455 – 4584Combined sources
Helixi459 – 4657Combined sources
Beta strandi471 – 4733Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C5MX-ray1.95D235-488[»]
F84-179[»]
1EZQX-ray2.20A235-488[»]
B46-179[»]
1F0RX-ray2.10A235-488[»]
B46-179[»]
1F0SX-ray2.10A235-488[»]
B46-179[»]
1FAXX-ray3.00A235-488[»]
L84-179[»]
1FJSX-ray1.92A235-468[»]
L127-178[»]
1FXYX-ray2.15A235-344[»]
1G2LX-ray1.90A235-469[»]
B86-179[»]
1G2MX-ray3.02A235-469[»]
B86-179[»]
1HCGX-ray2.20A235-475[»]
B129-179[»]
1IOEX-ray2.90A235-469[»]
L84-179[»]
1IQEX-ray2.90A235-469[»]
L84-179[»]
1IQFX-ray3.20A235-469[»]
L84-179[»]
1IQGX-ray2.60A235-469[»]
L84-179[»]
1IQHX-ray3.00A235-469[»]
L84-179[»]
1IQIX-ray2.90A235-469[»]
L84-179[»]
1IQJX-ray3.00A235-469[»]
L84-179[»]
1IQKX-ray3.20A235-469[»]
L84-179[»]
1IQLX-ray2.70A235-469[»]
L84-179[»]
1IQMX-ray2.60A235-469[»]
L84-179[»]
1IQNX-ray2.60A235-469[»]
L84-179[»]
1KSNX-ray2.10A235-488[»]
B46-179[»]
1LPGX-ray2.00A46-179[»]
B235-488[»]
1LPKX-ray2.20A46-179[»]
B235-488[»]
1LPZX-ray2.40A46-179[»]
B235-488[»]
1LQDX-ray2.70A46-179[»]
B235-488[»]
1MQ5X-ray2.10A235-467[»]
L127-177[»]
1MQ6X-ray2.10A235-467[»]
L127-177[»]
1MSXmodel-A235-469[»]
1NFUX-ray2.05A235-488[»]
B46-240[»]
1NFWX-ray2.10A235-488[»]
B46-179[»]
1NFXX-ray2.15A235-488[»]
B46-179[»]
1NFYX-ray2.10A235-488[»]
B46-179[»]
1NL8model-F235-469[»]
L41-179[»]
1P0SX-ray2.80H235-488[»]
L41-178[»]
1V3XX-ray2.20A235-467[»]
B127-178[»]
1WU1X-ray2.30A235-467[»]
B85-179[»]
1XKAX-ray2.30C235-469[»]
L85-179[»]
1XKBX-ray2.40A/B85-179[»]
C/D235-469[»]
1Z6EX-ray1.80A235-468[»]
L127-178[»]
2BMGX-ray2.70A126-178[»]
B235-468[»]
2BOHX-ray2.20A46-179[»]
B235-488[»]
2BOKX-ray1.64A235-475[»]
L126-180[»]
2BQ6X-ray3.00A126-177[»]
B220-468[»]
2BQ7X-ray2.20A126-177[»]
B220-468[»]
2BQWX-ray2.95A126-177[»]
B220-468[»]
2CJIX-ray2.10A235-488[»]
B46-179[»]
2D1JX-ray2.20A235-467[»]
B125-178[»]
2EI6X-ray2.30A235-467[»]
B125-178[»]
2EI7X-ray2.30A235-467[»]
B125-178[»]
2EI8X-ray2.10A235-467[»]
B125-178[»]
2FZZX-ray2.20A235-468[»]
L127-178[»]
2G00X-ray2.10A235-468[»]
L127-178[»]
2GD4X-ray3.30A/L126-182[»]
B/H235-475[»]
2H9EX-ray2.20H235-467[»]
L86-234[»]
2J2UX-ray1.90A235-488[»]
B46-179[»]
2J34X-ray2.01A235-488[»]
B46-179[»]
2J38X-ray2.10A235-488[»]
B46-179[»]
2J4IX-ray1.80A235-488[»]
B46-179[»]
2J94X-ray2.10A235-488[»]
B46-179[»]
2J95X-ray2.01A235-488[»]
B46-179[»]
2JKHX-ray1.25A235-475[»]
L126-180[»]
2P16X-ray2.30A235-468[»]
L127-178[»]
2P3FX-ray3.10H235-469[»]
L125-178[»]
2P3TX-ray1.92A127-178[»]
B235-467[»]
2P3UX-ray1.62A127-178[»]
B235-467[»]
2P93X-ray1.90A235-468[»]
L127-178[»]
2P94X-ray1.80A235-468[»]
L127-178[»]
2P95X-ray2.20A235-468[»]
L127-178[»]
2PHBX-ray2.30A235-468[»]
B128-178[»]
2PR3X-ray1.50A235-468[»]
B128-178[»]
2Q1JX-ray1.90A235-468[»]
B128-178[»]
2RA0X-ray2.30A235-468[»]
L128-178[»]
2UWLX-ray1.90A235-488[»]
B46-179[»]
2UWOX-ray1.75A235-488[»]
B46-179[»]
2UWPX-ray1.75A235-488[»]
B46-179[»]
2VH0X-ray1.70A235-488[»]
B46-179[»]
2VH6X-ray1.95A235-488[»]
B46-177[»]
2VVCX-ray1.95A/B235-475[»]
K/L126-180[»]
2VVUX-ray2.30A235-475[»]
L126-180[»]
2VVVX-ray1.73A235-475[»]
L126-180[»]
2VWLX-ray1.80A235-475[»]
L126-180[»]
2VWMX-ray1.96A/B235-475[»]
K/L126-180[»]
2VWNX-ray1.61A235-475[»]
L126-180[»]
2VWOX-ray1.60A235-475[»]
L126-180[»]
2W26X-ray2.08A235-468[»]
B129-177[»]
2W3IX-ray1.90A235-468[»]
B128-178[»]
2W3KX-ray2.05A235-468[»]
B128-178[»]
2WYGX-ray1.88A235-487[»]
B46-179[»]
2WYJX-ray2.38A235-488[»]
B46-179[»]
2XBVX-ray1.66A235-475[»]
L126-180[»]
2XBWX-ray1.72A235-475[»]
L126-180[»]
2XBXX-ray1.85A235-475[»]
L126-180[»]
2XBYX-ray2.02A235-475[»]
L126-180[»]
2XC0X-ray2.05A235-475[»]
L126-180[»]
2XC4X-ray1.67A235-475[»]
L126-180[»]
2XC5X-ray1.70A235-475[»]
L126-180[»]
2Y5FX-ray1.29A235-468[»]
L127-180[»]
2Y5GX-ray1.29A235-468[»]
L127-180[»]
2Y5HX-ray1.33A235-468[»]
L127-180[»]
2Y7XX-ray1.90A235-488[»]
B46-179[»]
2Y7ZX-ray1.84A235-488[»]
B46-179[»]
2Y80X-ray1.90A235-488[»]
B46-179[»]
2Y81X-ray1.70A235-488[»]
B46-179[»]
2Y82X-ray2.20A235-488[»]
B46-179[»]
3CENX-ray1.60A235-468[»]
L127-178[»]
3CS7X-ray2.20A235-468[»]
L127-178[»]
3ENSX-ray2.30A/C85-178[»]
B/D235-472[»]
3FFGX-ray1.54A235-468[»]
L127-178[»]
3HPTX-ray2.19A/C85-178[»]
B/D235-472[»]
3IITX-ray1.80A235-467[»]
B125-178[»]
3K9XX-ray1.90A/C85-178[»]
B/D235-472[»]
3KL6X-ray1.45A235-475[»]
B126-179[»]
3KQBX-ray2.25A235-468[»]
L127-178[»]
3KQCX-ray2.20A235-468[»]
L127-178[»]
3KQDX-ray2.75A235-468[»]
L127-178[»]
3KQEX-ray2.35A235-468[»]
L127-178[»]
3LIWX-ray2.22A235-468[»]
B128-178[»]
3M36X-ray2.15A235-468[»]
L127-178[»]
3M37X-ray1.90A235-468[»]
L127-178[»]
3Q3KX-ray2.00A235-467[»]
B125-178[»]
3SW2X-ray2.42A85-178[»]
B235-472[»]
3TK5X-ray2.20A235-467[»]
B125-178[»]
3TK6X-ray1.80A235-467[»]
B125-178[»]
4A7IX-ray2.40A84-179[»]
B235-488[»]
4BTIX-ray2.30A/E84-179[»]
B/F235-488[»]
4BTTX-ray2.59A/E84-179[»]
B/F235-488[»]
4BTUX-ray2.37A/E84-179[»]
B/F235-488[»]
ProteinModelPortaliP00742.
SMRiP00742. Positions 43-180, 235-466.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00742.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 8545GlaPROSITE-ProRule annotationAdd
BLAST
Domaini86 – 12237EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini125 – 16541EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini235 – 467233Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni183 – 20321O-glycosylated at one siteAdd
BLAST
Regioni476 – 48510O-glycosylated at one site

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 2 EGF-like domains.PROSITE-ProRule annotation
Contains 1 Gla (gamma-carboxy-glutamate) domain.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiCOG5640.
HOGENOMiHOG000251821.
HOVERGENiHBG013304.
InParanoidiP00742.
KOiK01314.
OMAiEMAHEVE.
PhylomeDBiP00742.
TreeFamiTF327329.

Family and domain databases

Gene3Di4.10.740.10. 1 hit.
InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001143. Factor_X. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTiSM00181. EGF. 1 hit.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 2 hits.
SSF57630. SSF57630. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 1 hit.
PS01187. EGF_CA. 1 hit.
PS00011. GLA_1. 1 hit.
PS50998. GLA_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00742-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRPLHLVLL SASLAGLLLL GESLFIRREQ ANNILARVTR ANSFLEEMKK
60 70 80 90 100
GHLERECMEE TCSYEEAREV FEDSDKTNEF WNKYKDGDQC ETSPCQNQGK
110 120 130 140 150
CKDGLGEYTC TCLEGFEGKN CELFTRKLCS LDNGDCDQFC HEEQNSVVCS
160 170 180 190 200
CARGYTLADN GKACIPTGPY PCGKQTLERR KRSVAQATSS SGEAPDSITW
210 220 230 240 250
KPYDAADLDP TENPFDLLDF NQTQPERGDN NLTRIVGGQE CKDGECPWQA
260 270 280 290 300
LLINEENEGF CGGTILSEFY ILTAAHCLYQ AKRFKVRVGD RNTEQEEGGE
310 320 330 340 350
AVHEVEVVIK HNRFTKETYD FDIAVLRLKT PITFRMNVAP ACLPERDWAE
360 370 380 390 400
STLMTQKTGI VSGFGRTHEK GRQSTRLKML EVPYVDRNSC KLSSSFIITQ
410 420 430 440 450
NMFCAGYDTK QEDACQGDSG GPHVTRFKDT YFVTGIVSWG EGCARKGKYG
460 470 480
IYTKVTAFLK WIDRSMKTRG LPKAKSHAPE VITSSPLK
Length:488
Mass (Da):54,732
Last modified:October 1, 1989 - v2
Checksum:iF81D5746AF4797AF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti285 – 2884KVRV → E in AAA51984 (PubMed:3011603).Curated
Sequence conflicti285 – 2884KVRV → E in AAA52486 (PubMed:6587384).Curated
Sequence conflicti442 – 4421G → S in AAA52490 (PubMed:2582420).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti7 – 71L → I.1 Publication
Corresponds to variant rs5963 [ dbSNP | Ensembl ].
VAR_014162
Natural varianti30 – 301Q → H.1 Publication
Corresponds to variant rs5961 [ dbSNP | Ensembl ].
VAR_014163
Natural varianti47 – 471E → G in FA10D; St. Louis II; strongly reduced activity; not activated by factor VIIa and tissue factor. 1 Publication
VAR_065428
Natural varianti51 – 511G → V in FA10D. 1 Publication
VAR_065429
Natural varianti54 – 541E → G in FA10D; Ketchikan. 1 Publication
VAR_065430
Natural varianti54 – 541E → K in FA10D; Vorarlberg; converts prothrombin at a normal rate but shows decreased affinity for calcium. 2 Publications
VAR_065431
Natural varianti72 – 721E → Q in FA10D; Tokyo. 1 Publication
VAR_065432
Natural varianti91 – 911E → K in FA10D; Riyadh. 1 Publication
VAR_065433
Natural varianti142 – 1421E → K in FA10D; uncertain pathological significance; detected in patients carrying K-54 or P-374; slightly reduced activity. 3 Publications
Corresponds to variant rs61753266 [ dbSNP | Ensembl ].
VAR_065434
Natural varianti149 – 1491C → Y in FA10D. 1 Publication
VAR_065435
Natural varianti151 – 1511C → Y in FA10D. 1 Publication
VAR_065436
Natural varianti152 – 1521A → T.1 Publication
Corresponds to variant rs3211772 [ dbSNP | Ensembl ].
VAR_020176
Natural varianti192 – 1921G → R.1 Publication
Corresponds to variant rs3211783 [ dbSNP | Ensembl ].
VAR_020177
Natural varianti289 – 2891G → R in FA10D; may affect splicing. 1 Publication
VAR_065437
Natural varianti304 – 3041E → K in FA10D. 1 Publication
VAR_065438
Natural varianti322 – 3221D → N in FA10D; Stockton; 50% decrease in specific activity; decrease in protein flexibility. 2 Publications
VAR_065439
Natural varianti327 – 3271R → W in FA10D. 1 Publication
VAR_065440
Natural varianti338 – 3381V → M in FA10D. 1 Publication
VAR_065441
Natural varianti350 – 3501E → K in FA10D. 1 Publication
VAR_065442
Natural varianti358 – 3581T → M in FA10D; Roma; decrease in protein flexibilty. 2 Publications
VAR_065443
Natural varianti363 – 3631G → S in FA10D. 1 Publication
VAR_065444
Natural varianti366 – 3661R → C in FA10D; San Antonio. 1 Publication
VAR_065445
Natural varianti374 – 3741S → P in FA10D; Marseille; decreased cleavage by factor IXa; normal catalytic efficiency for prothrombin. 3 Publications
VAR_065446
Natural varianti382 – 3821V → A in FA10D; partial loss of activity; decrease in protein flexibilty. 2 Publications
VAR_072751
Natural varianti383 – 3831P → S in FA10D; Friuli. 1 Publication
VAR_065447
Natural varianti390 – 3901C → F in FA10D; Padua 4. 1 Publication
Corresponds to variant rs199778916 [ dbSNP | Ensembl ].
VAR_065448
Natural varianti404 – 4041C → R in FA10D. 1 Publication
VAR_065449
Natural varianti406 – 4061G → S in FA10D; almost complete loss of activity; decrease in protein flexibilty. 2 Publications
VAR_065450
Natural varianti420 – 4201G → R in FA10D; Padua 3. 1 Publication
VAR_065451
Natural varianti421 – 4211G → D in FA10D; significant loss of activity; no change in protein flexibilty. 2 Publications
VAR_072752
Natural varianti448 – 4481K → N in FA10D; San Giovanni Rotondo. 1 Publication
VAR_065452

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K03194 mRNA. Translation: AAA52490.1.
M57285 mRNA. Translation: AAA52421.1.
AF503510 Genomic DNA. Translation: AAM19347.1.
BC046125 mRNA. Translation: AAH46125.1.
N00045
, L00390, L00391, L00392, L00393, L00394, L00395, L00396 Genomic DNA. Translation: AAA52764.1.
M22613 mRNA. Translation: AAA51984.1.
K01886 mRNA. Translation: AAA52486.1.
M33297 Genomic DNA. Translation: AAA52636.1.
CCDSiCCDS9530.1.
PIRiA24478. EXHU.
RefSeqiNP_000495.1. NM_000504.3.
UniGeneiHs.361463.

Genome annotation databases

EnsembliENST00000375559; ENSP00000364709; ENSG00000126218.
GeneIDi2159.
KEGGihsa:2159.
UCSCiuc001vsx.3. human.

Polymorphism and mutation databases

BioMutaiF10.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Factor X entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K03194 mRNA. Translation: AAA52490.1.
M57285 mRNA. Translation: AAA52421.1.
AF503510 Genomic DNA. Translation: AAM19347.1.
BC046125 mRNA. Translation: AAH46125.1.
N00045
, L00390, L00391, L00392, L00393, L00394, L00395, L00396 Genomic DNA. Translation: AAA52764.1.
M22613 mRNA. Translation: AAA51984.1.
K01886 mRNA. Translation: AAA52486.1.
M33297 Genomic DNA. Translation: AAA52636.1.
CCDSiCCDS9530.1.
PIRiA24478. EXHU.
RefSeqiNP_000495.1. NM_000504.3.
UniGeneiHs.361463.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C5MX-ray1.95D235-488[»]
F84-179[»]
1EZQX-ray2.20A235-488[»]
B46-179[»]
1F0RX-ray2.10A235-488[»]
B46-179[»]
1F0SX-ray2.10A235-488[»]
B46-179[»]
1FAXX-ray3.00A235-488[»]
L84-179[»]
1FJSX-ray1.92A235-468[»]
L127-178[»]
1FXYX-ray2.15A235-344[»]
1G2LX-ray1.90A235-469[»]
B86-179[»]
1G2MX-ray3.02A235-469[»]
B86-179[»]
1HCGX-ray2.20A235-475[»]
B129-179[»]
1IOEX-ray2.90A235-469[»]
L84-179[»]
1IQEX-ray2.90A235-469[»]
L84-179[»]
1IQFX-ray3.20A235-469[»]
L84-179[»]
1IQGX-ray2.60A235-469[»]
L84-179[»]
1IQHX-ray3.00A235-469[»]
L84-179[»]
1IQIX-ray2.90A235-469[»]
L84-179[»]
1IQJX-ray3.00A235-469[»]
L84-179[»]
1IQKX-ray3.20A235-469[»]
L84-179[»]
1IQLX-ray2.70A235-469[»]
L84-179[»]
1IQMX-ray2.60A235-469[»]
L84-179[»]
1IQNX-ray2.60A235-469[»]
L84-179[»]
1KSNX-ray2.10A235-488[»]
B46-179[»]
1LPGX-ray2.00A46-179[»]
B235-488[»]
1LPKX-ray2.20A46-179[»]
B235-488[»]
1LPZX-ray2.40A46-179[»]
B235-488[»]
1LQDX-ray2.70A46-179[»]
B235-488[»]
1MQ5X-ray2.10A235-467[»]
L127-177[»]
1MQ6X-ray2.10A235-467[»]
L127-177[»]
1MSXmodel-A235-469[»]
1NFUX-ray2.05A235-488[»]
B46-240[»]
1NFWX-ray2.10A235-488[»]
B46-179[»]
1NFXX-ray2.15A235-488[»]
B46-179[»]
1NFYX-ray2.10A235-488[»]
B46-179[»]
1NL8model-F235-469[»]
L41-179[»]
1P0SX-ray2.80H235-488[»]
L41-178[»]
1V3XX-ray2.20A235-467[»]
B127-178[»]
1WU1X-ray2.30A235-467[»]
B85-179[»]
1XKAX-ray2.30C235-469[»]
L85-179[»]
1XKBX-ray2.40A/B85-179[»]
C/D235-469[»]
1Z6EX-ray1.80A235-468[»]
L127-178[»]
2BMGX-ray2.70A126-178[»]
B235-468[»]
2BOHX-ray2.20A46-179[»]
B235-488[»]
2BOKX-ray1.64A235-475[»]
L126-180[»]
2BQ6X-ray3.00A126-177[»]
B220-468[»]
2BQ7X-ray2.20A126-177[»]
B220-468[»]
2BQWX-ray2.95A126-177[»]
B220-468[»]
2CJIX-ray2.10A235-488[»]
B46-179[»]
2D1JX-ray2.20A235-467[»]
B125-178[»]
2EI6X-ray2.30A235-467[»]
B125-178[»]
2EI7X-ray2.30A235-467[»]
B125-178[»]
2EI8X-ray2.10A235-467[»]
B125-178[»]
2FZZX-ray2.20A235-468[»]
L127-178[»]
2G00X-ray2.10A235-468[»]
L127-178[»]
2GD4X-ray3.30A/L126-182[»]
B/H235-475[»]
2H9EX-ray2.20H235-467[»]
L86-234[»]
2J2UX-ray1.90A235-488[»]
B46-179[»]
2J34X-ray2.01A235-488[»]
B46-179[»]
2J38X-ray2.10A235-488[»]
B46-179[»]
2J4IX-ray1.80A235-488[»]
B46-179[»]
2J94X-ray2.10A235-488[»]
B46-179[»]
2J95X-ray2.01A235-488[»]
B46-179[»]
2JKHX-ray1.25A235-475[»]
L126-180[»]
2P16X-ray2.30A235-468[»]
L127-178[»]
2P3FX-ray3.10H235-469[»]
L125-178[»]
2P3TX-ray1.92A127-178[»]
B235-467[»]
2P3UX-ray1.62A127-178[»]
B235-467[»]
2P93X-ray1.90A235-468[»]
L127-178[»]
2P94X-ray1.80A235-468[»]
L127-178[»]
2P95X-ray2.20A235-468[»]
L127-178[»]
2PHBX-ray2.30A235-468[»]
B128-178[»]
2PR3X-ray1.50A235-468[»]
B128-178[»]
2Q1JX-ray1.90A235-468[»]
B128-178[»]
2RA0X-ray2.30A235-468[»]
L128-178[»]
2UWLX-ray1.90A235-488[»]
B46-179[»]
2UWOX-ray1.75A235-488[»]
B46-179[»]
2UWPX-ray1.75A235-488[»]
B46-179[»]
2VH0X-ray1.70A235-488[»]
B46-179[»]
2VH6X-ray1.95A235-488[»]
B46-177[»]
2VVCX-ray1.95A/B235-475[»]
K/L126-180[»]
2VVUX-ray2.30A235-475[»]
L126-180[»]
2VVVX-ray1.73A235-475[»]
L126-180[»]
2VWLX-ray1.80A235-475[»]
L126-180[»]
2VWMX-ray1.96A/B235-475[»]
K/L126-180[»]
2VWNX-ray1.61A235-475[»]
L126-180[»]
2VWOX-ray1.60A235-475[»]
L126-180[»]
2W26X-ray2.08A235-468[»]
B129-177[»]
2W3IX-ray1.90A235-468[»]
B128-178[»]
2W3KX-ray2.05A235-468[»]
B128-178[»]
2WYGX-ray1.88A235-487[»]
B46-179[»]
2WYJX-ray2.38A235-488[»]
B46-179[»]
2XBVX-ray1.66A235-475[»]
L126-180[»]
2XBWX-ray1.72A235-475[»]
L126-180[»]
2XBXX-ray1.85A235-475[»]
L126-180[»]
2XBYX-ray2.02A235-475[»]
L126-180[»]
2XC0X-ray2.05A235-475[»]
L126-180[»]
2XC4X-ray1.67A235-475[»]
L126-180[»]
2XC5X-ray1.70A235-475[»]
L126-180[»]
2Y5FX-ray1.29A235-468[»]
L127-180[»]
2Y5GX-ray1.29A235-468[»]
L127-180[»]
2Y5HX-ray1.33A235-468[»]
L127-180[»]
2Y7XX-ray1.90A235-488[»]
B46-179[»]
2Y7ZX-ray1.84A235-488[»]
B46-179[»]
2Y80X-ray1.90A235-488[»]
B46-179[»]
2Y81X-ray1.70A235-488[»]
B46-179[»]
2Y82X-ray2.20A235-488[»]
B46-179[»]
3CENX-ray1.60A235-468[»]
L127-178[»]
3CS7X-ray2.20A235-468[»]
L127-178[»]
3ENSX-ray2.30A/C85-178[»]
B/D235-472[»]
3FFGX-ray1.54A235-468[»]
L127-178[»]
3HPTX-ray2.19A/C85-178[»]
B/D235-472[»]
3IITX-ray1.80A235-467[»]
B125-178[»]
3K9XX-ray1.90A/C85-178[»]
B/D235-472[»]
3KL6X-ray1.45A235-475[»]
B126-179[»]
3KQBX-ray2.25A235-468[»]
L127-178[»]
3KQCX-ray2.20A235-468[»]
L127-178[»]
3KQDX-ray2.75A235-468[»]
L127-178[»]
3KQEX-ray2.35A235-468[»]
L127-178[»]
3LIWX-ray2.22A235-468[»]
B128-178[»]
3M36X-ray2.15A235-468[»]
L127-178[»]
3M37X-ray1.90A235-468[»]
L127-178[»]
3Q3KX-ray2.00A235-467[»]
B125-178[»]
3SW2X-ray2.42A85-178[»]
B235-472[»]
3TK5X-ray2.20A235-467[»]
B125-178[»]
3TK6X-ray1.80A235-467[»]
B125-178[»]
4A7IX-ray2.40A84-179[»]
B235-488[»]
4BTIX-ray2.30A/E84-179[»]
B/F235-488[»]
4BTTX-ray2.59A/E84-179[»]
B/F235-488[»]
4BTUX-ray2.37A/E84-179[»]
B/F235-488[»]
ProteinModelPortaliP00742.
SMRiP00742. Positions 43-180, 235-466.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108457. 9 interactions.
DIPiDIP-29896N.
IntActiP00742. 7 interactions.
MINTiMINT-276128.
STRINGi9606.ENSP00000364709.

Chemistry

BindingDBiP00742.
ChEMBLiCHEMBL2111419.
DrugBankiDB00025. Antihemophilic Factor.
DB06605. Apixaban.
DB00100. Coagulation Factor IX.
DB00036. Coagulation factor VIIa.
DB01225. Enoxaparin.
DB00569. Fondaparinux sodium.
DB01109. Heparin.
DB00170. Menadione.
DB06228. Rivaroxaban.
GuidetoPHARMACOLOGYi2359.

Protein family/group databases

MEROPSiS01.216.

PTM databases

PhosphoSiteiP00742.
UniCarbKBiP00742.

Polymorphism and mutation databases

BioMutaiF10.
DMDMi119761.

Proteomic databases

MaxQBiP00742.
PaxDbiP00742.
PRIDEiP00742.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375559; ENSP00000364709; ENSG00000126218.
GeneIDi2159.
KEGGihsa:2159.
UCSCiuc001vsx.3. human.

Organism-specific databases

CTDi2159.
GeneCardsiGC13P113777.
HGNCiHGNC:3528. F10.
MIMi227600. phenotype.
613872. gene.
neXtProtiNX_P00742.
Orphaneti328. Congenital factor X deficiency.
PharmGKBiPA27940.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5640.
HOGENOMiHOG000251821.
HOVERGENiHBG013304.
InParanoidiP00742.
KOiK01314.
OMAiEMAHEVE.
PhylomeDBiP00742.
TreeFamiTF327329.

Enzyme and pathway databases

BioCyciMetaCyc:HS05000-MONOMER.
BRENDAi3.4.21.6. 2681.
ReactomeiREACT_1050. Gamma-carboxylation of protein precursors.
REACT_1439. Common Pathway.
REACT_1573. Extrinsic Pathway.
REACT_1906. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
REACT_326. Intrinsic Pathway.
REACT_733. Removal of aminoterminal propeptides from gamma-carboxylated proteins.
SABIO-RKP00742.

Miscellaneous databases

ChiTaRSiF10. human.
EvolutionaryTraceiP00742.
GeneWikiiFactor_X.
GenomeRNAii2159.
NextBioi8723.
PMAP-CutDBP00742.
PROiP00742.
SOURCEiSearch...

Gene expression databases

BgeeiP00742.
CleanExiHS_F10.
ExpressionAtlasiP00742. baseline and differential.
GenevestigatoriP00742.

Family and domain databases

Gene3Di4.10.740.10. 1 hit.
InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001143. Factor_X. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTiSM00181. EGF. 1 hit.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 2 hits.
SSF57630. SSF57630. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 1 hit.
PS01187. EGF_CA. 1 hit.
PS00011. GLA_1. 1 hit.
PS50998. GLA_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression in COS-1 cells of a full-length cDNA encoding human coagulation factor X."
    Messier T.L., Pittman D.D., Long G.L., Kaufman R.J., Church W.R.
    Gene 99:291-294(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Gene for human factor X: a blood coagulation factor whose gene organization is essentially identical with that of factor IX and protein C."
    Leytus S.P., Foster D.C., Kurachi K., Davie E.W.
    Biochemistry 25:5098-5102(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. SeattleSNPs variation discovery resource
    Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-152 AND ARG-192.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Ovary.
  5. "Characterization of an almost full-length cDNA coding for human blood coagulation factor X."
    Fung M.R., Hay C.W., McGillivray R.T.A.
    Proc. Natl. Acad. Sci. U.S.A. 82:3591-3595(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-488.
  6. "Isolation and characterization of human blood-coagulation factor X cDNA."
    Kaul R.K., Hildebrand B., Roberts S., Jagadeeswaran P.
    Gene 41:311-314(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 19-488.
    Tissue: Liver.
  7. "Complete amino acid sequence of the light chain of human blood coagulation factor X: evidence for identification of residue 63 as beta-hydroxyaspartic acid."
    McMullen B.A., Fujikawa K., Kisiel W., Sasagawa T., Howald W.N., Kwa E.Y., Weinstein B.
    Biochemistry 22:2875-2884(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 41-179, HYDROXYLATION AT ASP-103, GAMMA-CARBOXYGLUTAMATION AT GLU-46; GLU-47; GLU-54; GLU-56; GLU-59; GLU-60; GLU-65; GLU-66; GLU-69; GLU-72 AND GLU-79.
  8. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 115-488, TISSUE SPECIFICITY.
    Tissue: Liver.
  9. "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."
    Inoue K., Morita T.
    Eur. J. Biochem. 218:153-163(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 183-234, GLYCOSYLATION AT THR-199; THR-211; ASN-221 AND ASN-231.
  10. "Cloning and characterization of the 5' end (exon 1) of the gene encoding human factor X."
    Jagadeeswaran P., Reddy S.V., Rao K.J., Hamsabhushanam K., Lyman G.
    Gene 84:517-519(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
  11. "Mechanism of inhibition of activated protein C by protein C inhibitor."
    Suzuki K., Nishioka J., Kusumoto H., Hashimoto S.
    J. Biochem. 95:187-195(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, HETERODIMER WITH SERPINA5.
  12. "Basis for the specificity and activation of the serpin protein Z-dependent proteinase inhibitor (ZPI) as an inhibitor of membrane-associated factor Xa."
    Huang X., Dementiev A., Olson S.T., Gettins P.G.
    J. Biol. Chem. 285:20399-20409(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  13. "Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
    Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
    Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
  14. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 86-179 AND 235-278.
  15. "Structural basis for chemical inhibition of human blood coagulation factor Xa."
    Kamata K., Kawamoto H., Honma T., Iwama T., Kim S.H.
    Proc. Natl. Acad. Sci. U.S.A. 95:6630-6635(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 86-179 AND 235-278.
  16. Cited for: X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS) OF 127-467.
  17. "Molecular characterization of human factor XSan Antonio."
    Reddy S.V., Zhou Z.Q., Rao K.J., Scott J.P., Watzke H., High K.A., Jagadeeswaran P.
    Blood 74:1486-1490(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FA10D CYS-366.
  18. "Molecular defect (Gla+14TO: hereditary factor X deficiency (factor X 'Vorarlberg')."
    Watzke H.H., Lechner K., Roberts H.R., Reddy S.V., Welsch D.J., Friedman P., Mahr G., Jagadeeswaran P., Monroe D.M., High K.A.
    J. Biol. Chem. 265:11982-11989(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS FA10D LYS-54 AND LYS-142, CHARACTERIZATION OF VARIANT FA10D LYS-54.
  19. "Molecular defect in coagulation factor XFriuli results from a substitution of serine for proline at position 343."
    James H.L., Girolami A., Fair D.S.
    Blood 77:317-323(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FA10D SER-383.
  20. "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."
    Marchetti G., Castaman G., Pinotti M., Lunghi B., Di Iasio M.G., Ruggieri M., Rodeghiero F., Bernardi F.
    Br. J. Haematol. 90:910-915(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS FA10D LYS-142 AND PRO-374.
  21. "Functional consequences of the Ser334-->Pro mutation in a human factor X variant (factor XMarseille)."
    Bezeaud A., Miyata T., Helley D., Zeng Y.Z., Kato H., Aillaud M.F., Juhan-Vague I., Guillin M.C.
    Eur. J. Biochem. 234:140-147(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FA10D PRO-374, CHARACTERIZATION OF VARIANT FA10D PRO-374.
  22. "Factor XKetchikan: a variant molecule in which Gly replaces a Gla residue at position 14 in the light chain."
    Kim D.J., Thompson A.R., James H.L.
    Hum. Genet. 95:212-214(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FA10D GLY-54.
  23. "Factor X Stockton: a mild bleeding diathesis associated with an active site mutation in factor X."
    Messier T.L., Wong C.Y., Bovill E.G., Long G.L., Church W.R.
    Blood Coagul. Fibrinolysis 7:5-14(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FA10D ASN-322, CHARACTERIZATION OF VARIANT FA10D ASN-322.
  24. "Factor XSt. Louis II. Identification of a glycine substitution at residue 7 and characterization of the recombinant protein."
    Rudolph A.E., Mullane M.P., Porche-Sorbet R., Tsuda S., Miletich J.P.
    J. Biol. Chem. 271:28601-28606(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FA10D GLY-47.
  25. "A family with hereditary factor X deficiency with a point mutation Gla32 to Gln in the Gla domain (factor X Tokyo)."
    Zama T., Murata M., Watanabe R., Yokoyama K., Moriki T., Ambo H., Murakami H., Kikuchi M., Ikeda Y.
    Br. J. Haematol. 106:809-811(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FA10D GLN-72.
  26. Cited for: VARIANTS ILE-7 AND HIS-30.
  27. Cited for: VARIANTS FA10D LYS-54; TYR-149; TYR-151; ARG-289; LYS-304; TRP-327; MET-338; LYS-350; MET-358; SER-363 AND ARG-404.
  28. "The impact of Glu102Lys on the factor X function in a patient with a doubly homozygous factor X deficiency (Gla14Lys and Glu102Lys)."
    Forberg E., Huhmann I., Jimenez-Boj E., Watzke H.H.
    Thromb. Haemost. 83:234-238(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT FA10D LYS-142.
  29. "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."
    Simioni P., Vianello F., Kalafatis M., Barzon L., Ladogana S., Paolucci P., Carotenuto M., Dal Bello F., Palu G., Girolami A.
    Thromb. Res. 101:219-230(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FA10D ASN-448.
  30. "A new factor X defect (factor X Padua 3): a compound heterozygous between true deficiency (Gly(380)-->Arg) and an abnormality (Ser(334)-->Pro)."
    Vianello F., Lombardi A.M., Boldrin C., Luni S., Girolami A.
    Thromb. Res. 104:257-264(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS FA10D PRO-374 AND ARG-420.
  31. "A novel type I factor X variant (factor X Cys350Phe) due to loss of a disulfide bond in the catalytic domain."
    Vianello F., Lombardi A.M., Bello F.D., Palu G., Zanon E., Girolami A.
    Blood Coagul. Fibrinolysis 14:401-405(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FA10D PHE-390.
  32. "Impaired prothrombinase activity of factor X Gly381Asp results in severe familial CRM+ FX deficiency."
    Pinotti M., Camire R.M., Baroni M., Rajab A., Marchetti G., Bernardi F.
    Thromb. Haemost. 89:243-248(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FA10D ASP-421, CHARACTERIZATION OF VARIANT FA10D ASP-421.
  33. "Molecular characterization of factor X deficiency associated with borderline plasma factor X level."
    Pinotti M., Monti M., Baroni M., Marchetti G., Bernardi F.
    Haematologica 89:501-502(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FA10D ALA-382, CHARACTERIZATION OF VARIANT FA10D ALA-382.
  34. "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."
    Isshiki I., Favier R., Moriki T., Uchida T., Ishihara H., Van Dreden P., Murata M., Ikeda Y.
    Blood Coagul. Fibrinolysis 16:9-16(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FA10D SER-406, CHARACTERIZATION OF VARIANT FA10D SER-406.
  35. "Analysis of the novel factor X gene mutation Glu51Lys in two families with factor X-Riyadh anomaly."
    Al-Hilali A., Wulff K., Abdel-Razeq H., Saud K.A., Al-Gaili F., Herrmann F.H.
    Thromb. Haemost. 97:542-545(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FA10D LYS-91.
  36. "Characterization of a homozygous Gly11Val mutation in the Gla domain of coagulation factor X."
    Chafa O., Tagzirt M., Tapon-Bretaudiere J., Reghis A., Fischer A.M., LeBonniec B.F.
    Thromb. Res. 124:144-148(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FA10D VAL-51.
  37. "Molecular dynamics characterization of five pathogenic Factor X mutants associated with decreased catalytic activity."
    Abdel-Azeim S., Oliva R., Chermak E., De Cristofaro R., Cavallo L.
    Biochemistry 53:6992-7001(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS FA10D ASN-322; MET-358; ALA-382; SER-406 AND ASP-421, CHARACTERIZATION OF VARIANTS FA10D ASN-322; MET-358; ALA-382; SER-406 AND ASP-421.

Entry informationi

Entry nameiFA10_HUMAN
AccessioniPrimary (citable) accession number: P00742
Secondary accession number(s): Q14340
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1989
Last modified: April 29, 2015
This is version 212 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.