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P00742

- FA10_HUMAN

UniProt

P00742 - FA10_HUMAN

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Protein

Coagulation factor X

Gene
F10
Organism
Homo sapiens (Human)
Status
Reviewed - 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. protein binding Source: UniProtKB
  4. serine-type endopeptidase activity Source: BHF-UCL

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.
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: 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) [MIM:227600]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.17 Publications
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. 1 Publication
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. 1 Publication
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 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. 1 Publication
VAR_065450
Natural varianti420 – 4201G → R in FA10D; Padua 3. 1 Publication
VAR_065451
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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131 Reviewed predictionAdd
BLAST
Propeptidei32 – 409PRO_0000027786
Chaini41 – 488448Coagulation factor XPRO_0000027787Add
BLAST
Chaini41 – 179139Factor X light chainPRO_0000027788Add
BLAST
Chaini183 – 488306Factor X heavy chainPRO_0000027789Add
BLAST
Propeptidei183 – 23452Activation peptide1 PublicationPRO_0000027790Add
BLAST
Chaini235 – 488254Activated factor Xa heavy chainPRO_0000027791Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 4614-carboxyglutamate1 Publication
Modified residuei47 – 4714-carboxyglutamate1 Publication
Modified residuei54 – 5414-carboxyglutamate1 Publication
Modified residuei56 – 5614-carboxyglutamate1 Publication
Disulfide bondi57 ↔ 62 By similarity
Modified residuei59 – 5914-carboxyglutamate1 Publication
Modified residuei60 – 6014-carboxyglutamate1 Publication
Modified residuei65 – 6514-carboxyglutamate1 Publication
Modified residuei66 – 6614-carboxyglutamate1 Publication
Modified residuei69 – 6914-carboxyglutamate1 Publication
Modified residuei72 – 7214-carboxyglutamate1 Publication
Modified residuei79 – 7914-carboxyglutamate1 Publication
Disulfide bondi90 ↔ 101
Disulfide bondi95 ↔ 110
Modified residuei103 – 1031(3R)-3-hydroxyaspartate
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.

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

ArrayExpressiP00742.
BgeeiP00742.
CleanExiHS_F10.
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 – 5711
Helixi64 – 718
Helixi74 – 818
Turni89 – 924
Beta strandi96 – 983
Beta strandi100 – 1023
Beta strandi105 – 1073
Beta strandi109 – 1113
Beta strandi116 – 1183
Beta strandi123 – 1253
Turni129 – 1313
Helixi132 – 1354
Beta strandi137 – 1437
Beta strandi146 – 1505
Beta strandi155 – 1573
Beta strandi164 – 1707
Beta strandi172 – 1743
Beta strandi236 – 2405
Turni243 – 2453
Beta strandi249 – 2535
Turni255 – 2573
Beta strandi259 – 2657
Beta strandi267 – 2737
Helixi275 – 2795
Beta strandi280 – 2834
Beta strandi285 – 2895
Beta strandi291 – 2955
Beta strandi301 – 3033
Beta strandi305 – 3106
Turni316 – 3194
Beta strandi324 – 3307
Helixi346 – 3527
Turni353 – 3553
Beta strandi356 – 3649
Beta strandi366 – 3683
Beta strandi372 – 3765
Beta strandi378 – 3858
Helixi387 – 3937
Beta strandi402 – 4065
Beta strandi408 – 4114
Turni416 – 4205
Beta strandi422 – 4276
Beta strandi430 – 43910
Beta strandi441 – 4444
Beta strandi450 – 4545
Helixi455 – 4584
Helixi459 – 4657
Beta strandi471 – 4733

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP00742.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 8545GlaAdd
BLAST
Domaini86 – 12237EGF-like 1; calcium-binding Reviewed predictionAdd
BLAST
Domaini125 – 16541EGF-like 2Add
BLAST
Domaini235 – 467233Peptidase S1Add
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.
Contains 2 EGF-like domains.

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

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MGRPLHLVLL SASLAGLLLL GESLFIRREQ ANNILARVTR ANSFLEEMKK    50
GHLERECMEE TCSYEEAREV FEDSDKTNEF WNKYKDGDQC ETSPCQNQGK 100
CKDGLGEYTC TCLEGFEGKN CELFTRKLCS LDNGDCDQFC HEEQNSVVCS 150
CARGYTLADN GKACIPTGPY PCGKQTLERR KRSVAQATSS SGEAPDSITW 200
KPYDAADLDP TENPFDLLDF NQTQPERGDN NLTRIVGGQE CKDGECPWQA 250
LLINEENEGF CGGTILSEFY ILTAAHCLYQ AKRFKVRVGD RNTEQEEGGE 300
AVHEVEVVIK HNRFTKETYD FDIAVLRLKT PITFRMNVAP ACLPERDWAE 350
STLMTQKTGI VSGFGRTHEK GRQSTRLKML EVPYVDRNSC KLSSSFIITQ 400
NMFCAGYDTK QEDACQGDSG GPHVTRFKDT YFVTGIVSWG EGCARKGKYG 450
IYTKVTAFLK WIDRSMKTRG LPKAKSHAPE VITSSPLK 488
Length:488
Mass (Da):54,732
Last modified:October 1, 1989 - v2
Checksum:iF81D5746AF4797AF
GO

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. 1 Publication
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. 1 Publication
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 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. 1 Publication
VAR_065450
Natural varianti420 – 4201G → R in FA10D; Padua 3. 1 Publication
VAR_065451
Natural varianti448 – 4481K → N in FA10D; San Giovanni Rotondo. 1 Publication
VAR_065452

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti285 – 2884KVRV → E in AAA51984. 1 Publication
Sequence conflicti285 – 2884KVRV → E in AAA52486. 1 Publication
Sequence conflicti442 – 4421G → S in AAA52490. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 databases

DMDMi119761.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Factor X entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS9530.1.
PIRi A24478. EXHU.
RefSeqi NP_000495.1. NM_000504.3.
UniGenei Hs.361463.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1C5M X-ray 1.95 D 235-488 [» ]
F 84-179 [» ]
1EZQ X-ray 2.20 A 235-488 [» ]
B 46-179 [» ]
1F0R X-ray 2.10 A 235-488 [» ]
B 46-179 [» ]
1F0S X-ray 2.10 A 235-488 [» ]
B 46-179 [» ]
1FAX X-ray 3.00 A 235-488 [» ]
L 84-179 [» ]
1FJS X-ray 1.92 A 235-468 [» ]
L 127-178 [» ]
1FXY X-ray 2.15 A 235-344 [» ]
1G2L X-ray 1.90 A 235-469 [» ]
B 86-179 [» ]
1G2M X-ray 3.02 A 235-469 [» ]
B 86-179 [» ]
1HCG X-ray 2.20 A 235-475 [» ]
B 129-179 [» ]
1IOE X-ray 2.90 A 235-469 [» ]
L 84-179 [» ]
1IQE X-ray 2.90 A 235-469 [» ]
L 84-179 [» ]
1IQF X-ray 3.20 A 235-469 [» ]
L 84-179 [» ]
1IQG X-ray 2.60 A 235-469 [» ]
L 84-179 [» ]
1IQH X-ray 3.00 A 235-469 [» ]
L 84-179 [» ]
1IQI X-ray 2.90 A 235-469 [» ]
L 84-179 [» ]
1IQJ X-ray 3.00 A 235-469 [» ]
L 84-179 [» ]
1IQK X-ray 3.20 A 235-469 [» ]
L 84-179 [» ]
1IQL X-ray 2.70 A 235-469 [» ]
L 84-179 [» ]
1IQM X-ray 2.60 A 235-469 [» ]
L 84-179 [» ]
1IQN X-ray 2.60 A 235-469 [» ]
L 84-179 [» ]
1KSN X-ray 2.10 A 235-488 [» ]
B 46-179 [» ]
1LPG X-ray 2.00 A 46-179 [» ]
B 235-488 [» ]
1LPK X-ray 2.20 A 46-179 [» ]
B 235-488 [» ]
1LPZ X-ray 2.40 A 46-179 [» ]
B 235-488 [» ]
1LQD X-ray 2.70 A 46-179 [» ]
B 235-488 [» ]
1MQ5 X-ray 2.10 A 235-467 [» ]
L 127-177 [» ]
1MQ6 X-ray 2.10 A 235-467 [» ]
L 127-177 [» ]
1MSX model - A 235-469 [» ]
1NFU X-ray 2.05 A 235-488 [» ]
B 46-240 [» ]
1NFW X-ray 2.10 A 235-488 [» ]
B 46-179 [» ]
1NFX X-ray 2.15 A 235-488 [» ]
B 46-179 [» ]
1NFY X-ray 2.10 A 235-488 [» ]
B 46-179 [» ]
1NL8 model - F 235-469 [» ]
L 41-179 [» ]
1P0S X-ray 2.80 H 235-488 [» ]
L 41-178 [» ]
1V3X X-ray 2.20 A 235-467 [» ]
B 127-178 [» ]
1WU1 X-ray 2.30 A 235-467 [» ]
B 85-179 [» ]
1XKA X-ray 2.30 C 235-469 [» ]
L 85-179 [» ]
1XKB X-ray 2.40 A/B 85-179 [» ]
C/D 235-469 [» ]
1Z6E X-ray 1.80 A 235-468 [» ]
L 127-178 [» ]
2BMG X-ray 2.70 A 126-178 [» ]
B 235-468 [» ]
2BOH X-ray 2.20 A 46-179 [» ]
B 235-488 [» ]
2BOK X-ray 1.64 A 235-475 [» ]
L 126-180 [» ]
2BQ6 X-ray 3.00 A 126-177 [» ]
B 220-468 [» ]
2BQ7 X-ray 2.20 A 126-177 [» ]
B 220-468 [» ]
2BQW X-ray 2.95 A 126-177 [» ]
B 220-468 [» ]
2CJI X-ray 2.10 A 235-488 [» ]
B 46-179 [» ]
2D1J X-ray 2.20 A 235-467 [» ]
B 125-178 [» ]
2EI6 X-ray 2.30 A 235-467 [» ]
B 125-178 [» ]
2EI7 X-ray 2.30 A 235-467 [» ]
B 125-178 [» ]
2EI8 X-ray 2.10 A 235-467 [» ]
B 125-178 [» ]
2FZZ X-ray 2.20 A 235-468 [» ]
L 127-178 [» ]
2G00 X-ray 2.10 A 235-468 [» ]
L 127-178 [» ]
2GD4 X-ray 3.30 A/L 126-182 [» ]
B/H 235-475 [» ]
2H9E X-ray 2.20 H 235-467 [» ]
L 86-234 [» ]
2J2U X-ray 1.90 A 235-488 [» ]
B 46-179 [» ]
2J34 X-ray 2.01 A 235-488 [» ]
B 46-179 [» ]
2J38 X-ray 2.10 A 235-488 [» ]
B 46-179 [» ]
2J4I X-ray 1.80 A 235-488 [» ]
B 46-179 [» ]
2J94 X-ray 2.10 A 235-488 [» ]
B 46-179 [» ]
2J95 X-ray 2.01 A 235-488 [» ]
B 46-179 [» ]
2JKH X-ray 1.25 A 235-475 [» ]
L 126-180 [» ]
2P16 X-ray 2.30 A 235-468 [» ]
L 127-178 [» ]
2P3F X-ray 3.10 H 235-469 [» ]
L 125-178 [» ]
2P3T X-ray 1.92 A 127-178 [» ]
B 235-467 [» ]
2P3U X-ray 1.62 A 127-178 [» ]
B 235-467 [» ]
2P93 X-ray 1.90 A 235-468 [» ]
L 127-178 [» ]
2P94 X-ray 1.80 A 235-468 [» ]
L 127-178 [» ]
2P95 X-ray 2.20 A 235-468 [» ]
L 127-178 [» ]
2PHB X-ray 2.30 A 235-468 [» ]
B 128-178 [» ]
2PR3 X-ray 1.50 A 235-468 [» ]
B 128-178 [» ]
2Q1J X-ray 1.90 A 235-468 [» ]
B 128-178 [» ]
2RA0 X-ray 2.30 A 235-468 [» ]
L 128-178 [» ]
2UWL X-ray 1.90 A 235-488 [» ]
B 46-179 [» ]
2UWO X-ray 1.75 A 235-488 [» ]
B 46-179 [» ]
2UWP X-ray 1.75 A 235-488 [» ]
B 46-179 [» ]
2VH0 X-ray 1.70 A 235-488 [» ]
B 46-179 [» ]
2VH6 X-ray 1.95 A 235-488 [» ]
B 46-177 [» ]
2VVC X-ray 1.95 A/B 235-475 [» ]
K/L 126-180 [» ]
2VVU X-ray 2.30 A 235-475 [» ]
L 126-180 [» ]
2VVV X-ray 1.73 A 235-475 [» ]
L 126-180 [» ]
2VWL X-ray 1.80 A 235-475 [» ]
L 126-180 [» ]
2VWM X-ray 1.96 A/B 235-475 [» ]
K/L 126-180 [» ]
2VWN X-ray 1.61 A 235-475 [» ]
L 126-180 [» ]
2VWO X-ray 1.60 A 235-475 [» ]
L 126-180 [» ]
2W26 X-ray 2.08 A 235-468 [» ]
B 129-177 [» ]
2W3I X-ray 1.90 A 235-468 [» ]
B 128-178 [» ]
2W3K X-ray 2.05 A 235-468 [» ]
B 128-178 [» ]
2WYG X-ray 1.88 A 235-487 [» ]
B 46-179 [» ]
2WYJ X-ray 2.38 A 235-488 [» ]
B 46-179 [» ]
2XBV X-ray 1.66 A 235-475 [» ]
L 126-180 [» ]
2XBW X-ray 1.72 A 235-475 [» ]
L 126-180 [» ]
2XBX X-ray 1.85 A 235-475 [» ]
L 126-180 [» ]
2XBY X-ray 2.02 A 235-475 [» ]
L 126-180 [» ]
2XC0 X-ray 2.05 A 235-475 [» ]
L 126-180 [» ]
2XC4 X-ray 1.67 A 235-475 [» ]
L 126-180 [» ]
2XC5 X-ray 1.70 A 235-475 [» ]
L 126-180 [» ]
2Y5F X-ray 1.29 A 235-468 [» ]
L 127-180 [» ]
2Y5G X-ray 1.29 A 235-468 [» ]
L 127-180 [» ]
2Y5H X-ray 1.33 A 235-468 [» ]
L 127-180 [» ]
2Y7X X-ray 1.90 A 235-488 [» ]
B 46-179 [» ]
2Y7Z X-ray 1.84 A 235-488 [» ]
B 46-179 [» ]
2Y80 X-ray 1.90 A 235-488 [» ]
B 46-179 [» ]
2Y81 X-ray 1.70 A 235-488 [» ]
B 46-179 [» ]
2Y82 X-ray 2.20 A 235-488 [» ]
B 46-179 [» ]
3CEN X-ray 1.60 A 235-468 [» ]
L 127-178 [» ]
3CS7 X-ray 2.20 A 235-468 [» ]
L 127-178 [» ]
3ENS X-ray 2.30 A/C 85-178 [» ]
B/D 235-472 [» ]
3FFG X-ray 1.54 A 235-468 [» ]
L 127-178 [» ]
3HPT X-ray 2.19 A/C 85-178 [» ]
B/D 235-472 [» ]
3IIT X-ray 1.80 A 235-467 [» ]
B 125-178 [» ]
3K9X X-ray 1.90 A/C 85-178 [» ]
B/D 235-472 [» ]
3KL6 X-ray 1.45 A 235-475 [» ]
B 126-179 [» ]
3KQB X-ray 2.25 A 235-468 [» ]
L 127-178 [» ]
3KQC X-ray 2.20 A 235-468 [» ]
L 127-178 [» ]
3KQD X-ray 2.75 A 235-468 [» ]
L 127-178 [» ]
3KQE X-ray 2.35 A 235-468 [» ]
L 127-178 [» ]
3LIW X-ray 2.22 A 235-468 [» ]
B 128-178 [» ]
3M36 X-ray 2.15 A 235-468 [» ]
L 127-178 [» ]
3M37 X-ray 1.90 A 235-468 [» ]
L 127-178 [» ]
3Q3K X-ray 2.00 A 235-467 [» ]
B 125-178 [» ]
3SW2 X-ray 2.42 A 85-178 [» ]
B 235-472 [» ]
3TK5 X-ray 2.20 A 235-467 [» ]
B 125-178 [» ]
3TK6 X-ray 1.80 A 235-467 [» ]
B 125-178 [» ]
4A7I X-ray 2.40 A 84-179 [» ]
B 235-488 [» ]
4BTI X-ray 2.30 A/E 84-179 [» ]
B/F 235-488 [» ]
4BTT X-ray 2.59 A/E 84-179 [» ]
B/F 235-488 [» ]
4BTU X-ray 2.37 A/E 84-179 [» ]
B/F 235-488 [» ]
ProteinModelPortali P00742.
SMRi P00742. Positions 43-180, 235-466.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108457. 9 interactions.
DIPi DIP-29896N.
IntActi P00742. 7 interactions.
MINTi MINT-276128.
STRINGi 9606.ENSP00000364709.

Chemistry

BindingDBi P00742.
ChEMBLi CHEMBL244.
DrugBanki DB00009. Alteplase.
DB00029. Anistreplase.
DB00025. Antihemophilic Factor.
DB00100. Coagulation Factor IX.
DB00036. Coagulation factor VIIa.
DB01225. Enoxaparin.
DB01109. Heparin.
DB00170. Menadione.
DB00015. Reteplase.
DB00031. Tenecteplase.
GuidetoPHARMACOLOGYi 2359.

Protein family/group databases

MEROPSi S01.216.

PTM databases

PhosphoSitei P00742.
UniCarbKBi P00742.

Polymorphism databases

DMDMi 119761.

Proteomic databases

MaxQBi P00742.
PaxDbi P00742.
PRIDEi P00742.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000375559 ; ENSP00000364709 ; ENSG00000126218 .
GeneIDi 2159.
KEGGi hsa:2159.
UCSCi uc001vsx.3. human.

Organism-specific databases

CTDi 2159.
GeneCardsi GC13P113777.
HGNCi HGNC:3528. F10.
MIMi 227600. phenotype.
613872. gene.
neXtProti NX_P00742.
Orphaneti 328. Congenital factor X deficiency.
PharmGKBi PA27940.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5640.
HOGENOMi HOG000251821.
HOVERGENi HBG013304.
InParanoidi P00742.
KOi K01314.
OMAi EMAHEVE.
PhylomeDBi P00742.
TreeFami TF327329.

Enzyme and pathway databases

BioCyci MetaCyc:HS05000-MONOMER.
Reactomei REACT_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-RK P00742.

Miscellaneous databases

ChiTaRSi F10. human.
EvolutionaryTracei P00742.
GeneWikii Factor_X.
GenomeRNAii 2159.
NextBioi 8723.
PMAP-CutDB P00742.
PROi P00742.
SOURCEi Search...

Gene expression databases

ArrayExpressi P00742.
Bgeei P00742.
CleanExi HS_F10.
Genevestigatori P00742.

Family and domain databases

Gene3Di 4.10.740.10. 1 hit.
InterProi IPR017857. 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 ]
Pfami PF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view ]
PIRSFi PIRSF001143. Factor_X. 1 hit.
PRINTSi PR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTi SM00181. EGF. 1 hit.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 2 hits.
SSF57630. SSF57630. 1 hit.
PROSITEi PS00010. 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 ]
ProtoNeti Search...

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. "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.
  33. "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.
  34. "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.

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: September 3, 2014
This is version 205 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

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