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Protein

Coagulation factor X

Gene

F10

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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.

Activity regulationi

Inhibited by SERPINA5 and SERPINA10.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei276Charge relay system1
Active sitei322Charge relay system1
Active sitei419Charge relay system1

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • phospholipid binding Source: BHF-UCL
  • serine-type endopeptidase activity Source: BHF-UCL

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Protease, Serine protease
Biological processBlood coagulation, Hemostasis
LigandCalcium

Enzyme and pathway databases

BioCyciMetaCyc:HS05000-MONOMER
BRENDAi3.4.21.6 2681
ReactomeiR-HSA-140834 Extrinsic Pathway of Fibrin Clot Formation
R-HSA-140837 Intrinsic Pathway of Fibrin Clot Formation
R-HSA-140875 Common Pathway of Fibrin Clot Formation
R-HSA-159740 Gamma-carboxylation of protein precursors
R-HSA-159763 Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus
R-HSA-159782 Removal of aminoterminal propeptides from gamma-carboxylated proteins
SABIO-RKiP00742
SIGNORiP00742

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
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

EuPathDBiHostDB:ENSG00000126218.11
HGNCiHGNC:3528 F10
MIMi613872 gene
neXtProtiNX_P00742

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Factor X deficiency (FA10D)21 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)DescriptionActionsGraphical viewLength
Natural variantiVAR_06542847E → G in FA10D; St. Louis II; strongly reduced activity; not activated by factor VIIa and tissue factor. 1 PublicationCorresponds to variant dbSNP:rs121964943Ensembl.1
Natural variantiVAR_06542951G → V in FA10D. 1 PublicationCorresponds to variant dbSNP:rs751782758Ensembl.1
Natural variantiVAR_06543054E → G in FA10D; Ketchikan. 1 PublicationCorresponds to variant dbSNP:rs121964944Ensembl.1
Natural variantiVAR_06543154E → K in FA10D; Vorarlberg; converts prothrombin at a normal rate but shows decreased affinity for calcium. 2 PublicationsCorresponds to variant dbSNP:rs121964939Ensembl.1
Natural variantiVAR_06543272E → Q in FA10D; Tokyo. 1 PublicationCorresponds to variant dbSNP:rs121964945Ensembl.1
Natural variantiVAR_06543391E → K in FA10D; Riyadh. 1 Publication1
Natural variantiVAR_065434142E → K in FA10D; uncertain pathological significance; detected in patients carrying K-54 or P-374; slightly reduced activity. 3 PublicationsCorresponds to variant dbSNP:rs61753266EnsemblClinVar.1
Natural variantiVAR_065435149C → Y in FA10D. 1 Publication1
Natural variantiVAR_065436151C → Y in FA10D. 1 Publication1
Natural variantiVAR_075212176 – 186Missing in FA10D; unknown pathological significance. 1 PublicationAdd BLAST11
Natural variantiVAR_075213262G → D in FA10D; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1393705267Ensembl.1
Natural variantiVAR_065437289G → R in FA10D; may affect splicing. 1 PublicationCorresponds to variant dbSNP:rs121964946Ensembl.1
Natural variantiVAR_065438304E → K in FA10D. 1 PublicationCorresponds to variant dbSNP:rs747292771Ensembl.1
Natural variantiVAR_065439322D → N in FA10D; Stockton; 50% decrease in specific activity. 2 PublicationsCorresponds to variant dbSNP:rs121964942Ensembl.1
Natural variantiVAR_065440327R → W in FA10D. 1 PublicationCorresponds to variant dbSNP:rs770119164Ensembl.1
Natural variantiVAR_065441338V → M in FA10D. 1 PublicationCorresponds to variant dbSNP:rs121964947Ensembl.1
Natural variantiVAR_065442350E → K in FA10D. 1 PublicationCorresponds to variant dbSNP:rs372309538Ensembl.1
Natural variantiVAR_065443358T → M in FA10D; Roma. 2 PublicationsCorresponds to variant dbSNP:rs768222784Ensembl.1
Natural variantiVAR_065444363G → S in FA10D. 1 Publication1
Natural variantiVAR_065445366R → C in FA10D; San Antonio. 1 PublicationCorresponds to variant dbSNP:rs104894392EnsemblClinVar.1
Natural variantiVAR_065446374S → P in FA10D; Marseille; decreased cleavage by factor IXa; normal catalytic efficiency for prothrombin. 3 PublicationsCorresponds to variant dbSNP:rs121964941Ensembl.1
Natural variantiVAR_072751382V → A in FA10D; partial loss of activity. 2 Publications1
Natural variantiVAR_065447383P → S in FA10D; Friuli. 1 PublicationCorresponds to variant dbSNP:rs121964940Ensembl.1
Natural variantiVAR_065448390C → F in FA10D; Padua 4. 1 PublicationCorresponds to variant dbSNP:rs199778916Ensembl.1
Natural variantiVAR_065449404C → R in FA10D. 1 Publication1
Natural variantiVAR_065450406G → S in FA10D; almost complete loss of activity. 2 PublicationsCorresponds to variant dbSNP:rs376163818Ensembl.1
Natural variantiVAR_065451420G → R in FA10D; Padua 3. 1 PublicationCorresponds to variant dbSNP:rs750759634Ensembl.1
Natural variantiVAR_072752421G → D in FA10D; significant loss of activity. 2 PublicationsCorresponds to variant dbSNP:rs758726161Ensembl.1
Natural variantiVAR_065452448K → N in FA10D; San Giovanni Rotondo. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi2159
MalaCardsiF10
MIMi227600 phenotype
OpenTargetsiENSG00000126218
Orphaneti328 Congenital factor X deficiency
PharmGKBiPA27940

Chemistry databases

ChEMBLiCHEMBL244
DrugBankiDB07211 (2R)-2-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}PROPENE-1-SULFONAMIDE
DB08746 1-[[(1E)-2-(4-CHLOROPHENYL)ETHENYL]SULFONYL]-4-[[1-(4-PYRIDINYL)-4-PIPERIDINYL]METHYL]PIPERAZINE
DB07974 1-{2-[(4-CHLOROPHENYL)AMINO]-2-OXOETHYL}-N-(1-ISOPROPYLPIPERIDIN-4-YL)-1H-INDOLE-2-CARBOXAMIDE
DB07277 2-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}ETHANESULFONAMIDE
DB07278 2-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}ETHENESULFONAMIDE
DB08487 3-({4-[(6-CHLORO-1-BENZOTHIEN-2-YL)SULFONYL]-2-OXOPIPERAZIN-1-YL}METHYL)BENZENECARBOXIMIDAMIDE
DB08495 4-({4-[(6-CHLORO-1-BENZOTHIEN-2-YL)SULFONYL]-2-OXOPIPERAZIN-1-YL}METHYL)BENZENECARBOXIMIDAMIDE
DB04673 4-[(5-CHLOROINDOL-2-YL)SULFONYL]-2-(2-METHYLPROPYL)-1-[[5-(PYRIDIN-4-YL)PYRIMIDIN-2-YL]CARBONYL]PIPERAZINE
DB08745 4-[[(1E)-2-(4-CHLOROPHENYL)ETHENYL]SULFONYL]-1-[[1-(4-PYRIDINYL)-4-PIPERIDINYL]METHYL]PIPERAZINONE
DB08173 5-CHLORO-N-(2-(4-(2-OXOPYRIDIN-1(2H)-YL)BENZAMIDO)ETHYL)THIOPHENE-2-CARBOXAMIDE
DB07872 5-chloro-N-[(3R)-1-(2-{[2-fluoro-4-(2-oxopyridin-1(2H)-yl)phenyl]amino}-2-oxoethyl)pyrrolidin-3-yl]thiophene-2-carboxamide
DB07843 5-CHLORO-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}-1-BENZOTHIOPHENE-2-SULFONAMIDE
DB07847 6-CHLORO-N-{(3S)-1-[(1S)-1-METHYL-2-(4-MORPHOLINYL)-2-OXO ETHYL]-2-OXO-3-PYRROLIDINYL}-2-NAPHTHALENESULFONAMIDE
DB07844 6-CHLORO-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}-1-BENZOTHIOPHENE-2-SULFONAMIDE
DB00025 Antihemophilic Factor (Recombinant)
DB06605 Apixaban
DB00100 Coagulation Factor IX (Recombinant)
DB13150 Coagulation factor VII human
DB00036 Coagulation factor VIIa Recombinant Human
DB09075 Edoxaban
DB01225 Enoxaparin
DB00569 Fondaparinux sodium
DB03847 Gamma-Carboxy-Glutamic Acid
DB01109 Heparin
DB05713 LY-517717
DB00170 Menadione
DB07973 N-(1-ISOPROPYLPIPERIDIN-4-YL)-1-(3-METHOXYBENZYL)-1H-INDOLE-2-CARBOXAMIDE
DB07800 N-(2-(((5-CHLORO-2-PYRIDINYL)AMINO)SULFONYL)PHENYL)-4-(2-OXO-1(2H)-PYRIDINYL)BENZAMIDE
DB06228 Rivaroxaban
DB05362 SSR-126517E
GuidetoPHARMACOLOGYi2359

Polymorphism and mutation databases

BioMutaiF10
DMDMi119761

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31Sequence analysisAdd BLAST31
PropeptideiPRO_000002778632 – 401 Publication9
ChainiPRO_000002778741 – 488Coagulation factor XAdd BLAST448
ChainiPRO_000002778841 – 179Factor X light chainAdd BLAST139
ChainiPRO_0000027789183 – 488Factor X heavy chainAdd BLAST306
PropeptideiPRO_0000027790183 – 234Activation peptideAdd BLAST52
ChainiPRO_0000027791235 – 488Activated factor Xa heavy chainAdd BLAST254

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei464-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei474-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei544-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei564-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Disulfide bondi57 ↔ 62By similarity
Modified residuei594-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei604-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei654-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei664-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei694-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei724-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei794-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Disulfide bondi90 ↔ 101
Disulfide bondi95 ↔ 110
Modified residuei103(3R)-3-hydroxyaspartate1 Publication1
Disulfide bondi112 ↔ 121
Disulfide bondi129 ↔ 140
Disulfide bondi136 ↔ 149
Disulfide bondi151 ↔ 164
Disulfide bondi172 ↔ 342Interchain (between light and heavy chains)
Glycosylationi199O-linked (GalNAc...) threonine1 Publication1
Glycosylationi211O-linked (GalNAc...) threonine1 Publication1
GlycosylationiCAR_000012221N-linked (GlcNAc...) asparagine1 Publication1
GlycosylationiCAR_000013231N-linked (GlcNAc...) asparagine1 Publication1
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

PaxDbiP00742
PeptideAtlasiP00742
PRIDEiP00742
ProteomicsDBi51275

PTM databases

GlyConnecti102
iPTMnetiP00742
PhosphoSitePlusiP00742
UniCarbKBiP00742

Miscellaneous databases

PMAP-CutDBiP00742

Expressioni

Tissue specificityi

Plasma; synthesized in the liver.1 Publication

Gene expression databases

BgeeiENSG00000126218 Expressed in 127 organ(s), highest expression level in right lobe of liver
CleanExiHS_F10
ExpressionAtlasiP00742 baseline and differential
GenevisibleiP00742 HS

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 interactors
CORUMiP00742
DIPiDIP-29896N
ELMiP00742
IntActiP00742, 11 interactors
MINTiP00742
STRINGi9606.ENSP00000364709

Chemistry databases

BindingDBiP00742

Structurei

Secondary structure

1488
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP00742
SMRiP00742
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00742

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini41 – 85GlaPROSITE-ProRule annotationAdd BLAST45
Domaini86 – 122EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini125 – 165EGF-like 2PROSITE-ProRule annotationAdd BLAST41
Domaini235 – 467Peptidase S1PROSITE-ProRule annotationAdd BLAST233

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni183 – 203O-glycosylated at one siteAdd BLAST21
Regioni476 – 485O-glycosylated at one site10

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IGPV Eukaryota
COG5640 LUCA
GeneTreeiENSGT00760000118890
HOGENOMiHOG000251821
HOVERGENiHBG013304
InParanoidiP00742
KOiK01314
OMAiNFLKWID
OrthoDBiEOG091G0AH5
PhylomeDBiP00742
TreeFamiTF327329

Family and domain databases

CDDicd00190 Tryp_SPc, 1 hit
Gene3Di4.10.740.10, 1 hit
InterProiView protein in InterPro
IPR017857 Coagulation_fac-like_Gla_dom
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR000152 EGF-type_Asp/Asn_hydroxyl_site
IPR018097 EGF_Ca-bd_CS
IPR035972 GLA-like_dom_SF
IPR000294 GLA_domain
IPR012224 Pept_S1A_FX
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR001254 Trypsin_dom
IPR018114 TRYPSIN_HIS
IPR033116 TRYPSIN_SER
PfamiView protein in Pfam
PF00008 EGF, 1 hit
PF00594 Gla, 1 hit
PF00089 Trypsin, 1 hit
PIRSFiPIRSF001143 Factor_X, 1 hit
PRINTSiPR00722 CHYMOTRYPSIN
PR00001 GLABLOOD
SMARTiView protein in SMART
SM00181 EGF, 2 hits
SM00179 EGF_CA, 1 hit
SM00069 GLA, 1 hit
SM00020 Tryp_SPc, 1 hit
SUPFAMiSSF50494 SSF50494, 2 hits
SSF57630 SSF57630, 1 hit
PROSITEiView protein in PROSITE
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

Sequence (1+)i

Sequence statusi: Complete.

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

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q5JVE8Q5JVE8_HUMAN
Coagulation factor X
F10
332Annotation score:
B7ZBK1B7ZBK1_HUMAN
Coagulation factor X
F10
334Annotation score:
F8WBM7F8WBM7_HUMAN
Coagulation factor X
F10
130Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti285 – 288KVRV → E in AAA51984 (PubMed:3011603).Curated4
Sequence conflicti285 – 288KVRV → E in AAA52486 (PubMed:6587384).Curated4
Sequence conflicti442G → S in AAA52490 (PubMed:2582420).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0141627L → I1 PublicationCorresponds to variant dbSNP:rs5963Ensembl.1
Natural variantiVAR_01416330Q → H1 PublicationCorresponds to variant dbSNP:rs5961EnsemblClinVar.1
Natural variantiVAR_06542847E → G in FA10D; St. Louis II; strongly reduced activity; not activated by factor VIIa and tissue factor. 1 PublicationCorresponds to variant dbSNP:rs121964943Ensembl.1
Natural variantiVAR_06542951G → V in FA10D. 1 PublicationCorresponds to variant dbSNP:rs751782758Ensembl.1
Natural variantiVAR_06543054E → G in FA10D; Ketchikan. 1 PublicationCorresponds to variant dbSNP:rs121964944Ensembl.1
Natural variantiVAR_06543154E → K in FA10D; Vorarlberg; converts prothrombin at a normal rate but shows decreased affinity for calcium. 2 PublicationsCorresponds to variant dbSNP:rs121964939Ensembl.1
Natural variantiVAR_06543272E → Q in FA10D; Tokyo. 1 PublicationCorresponds to variant dbSNP:rs121964945Ensembl.1
Natural variantiVAR_06543391E → K in FA10D; Riyadh. 1 Publication1
Natural variantiVAR_065434142E → K in FA10D; uncertain pathological significance; detected in patients carrying K-54 or P-374; slightly reduced activity. 3 PublicationsCorresponds to variant dbSNP:rs61753266EnsemblClinVar.1
Natural variantiVAR_065435149C → Y in FA10D. 1 Publication1
Natural variantiVAR_065436151C → Y in FA10D. 1 Publication1
Natural variantiVAR_020176152A → T1 PublicationCorresponds to variant dbSNP:rs3211772Ensembl.1
Natural variantiVAR_075212176 – 186Missing in FA10D; unknown pathological significance. 1 PublicationAdd BLAST11
Natural variantiVAR_020177192G → R1 PublicationCorresponds to variant dbSNP:rs3211783EnsemblClinVar.1
Natural variantiVAR_075213262G → D in FA10D; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1393705267Ensembl.1
Natural variantiVAR_065437289G → R in FA10D; may affect splicing. 1 PublicationCorresponds to variant dbSNP:rs121964946Ensembl.1
Natural variantiVAR_065438304E → K in FA10D. 1 PublicationCorresponds to variant dbSNP:rs747292771Ensembl.1
Natural variantiVAR_065439322D → N in FA10D; Stockton; 50% decrease in specific activity. 2 PublicationsCorresponds to variant dbSNP:rs121964942Ensembl.1
Natural variantiVAR_065440327R → W in FA10D. 1 PublicationCorresponds to variant dbSNP:rs770119164Ensembl.1
Natural variantiVAR_065441338V → M in FA10D. 1 PublicationCorresponds to variant dbSNP:rs121964947Ensembl.1
Natural variantiVAR_065442350E → K in FA10D. 1 PublicationCorresponds to variant dbSNP:rs372309538Ensembl.1
Natural variantiVAR_065443358T → M in FA10D; Roma. 2 PublicationsCorresponds to variant dbSNP:rs768222784Ensembl.1
Natural variantiVAR_065444363G → S in FA10D. 1 Publication1
Natural variantiVAR_065445366R → C in FA10D; San Antonio. 1 PublicationCorresponds to variant dbSNP:rs104894392EnsemblClinVar.1
Natural variantiVAR_065446374S → P in FA10D; Marseille; decreased cleavage by factor IXa; normal catalytic efficiency for prothrombin. 3 PublicationsCorresponds to variant dbSNP:rs121964941Ensembl.1
Natural variantiVAR_072751382V → A in FA10D; partial loss of activity. 2 Publications1
Natural variantiVAR_065447383P → S in FA10D; Friuli. 1 PublicationCorresponds to variant dbSNP:rs121964940Ensembl.1
Natural variantiVAR_065448390C → F in FA10D; Padua 4. 1 PublicationCorresponds to variant dbSNP:rs199778916Ensembl.1
Natural variantiVAR_065449404C → R in FA10D. 1 Publication1
Natural variantiVAR_065450406G → S in FA10D; almost complete loss of activity. 2 PublicationsCorresponds to variant dbSNP:rs376163818Ensembl.1
Natural variantiVAR_065451420G → R in FA10D; Padua 3. 1 PublicationCorresponds to variant dbSNP:rs750759634Ensembl.1
Natural variantiVAR_072752421G → D in FA10D; significant loss of activity. 2 PublicationsCorresponds to variant dbSNP:rs758726161Ensembl.1
Natural variantiVAR_065452448K → N in FA10D; San Giovanni Rotondo. 1 Publication1

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
NP_001299603.1, NM_001312674.1
NP_001299604.1, NM_001312675.1
UniGeneiHs.361463

Genome annotation databases

EnsembliENST00000375559; ENSP00000364709; ENSG00000126218
GeneIDi2159
KEGGihsa:2159

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

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
NP_001299603.1, NM_001312674.1
NP_001299604.1, NM_001312675.1
UniGeneiHs.361463

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4Y6DX-ray1.55A235-488[»]
B46-179[»]
4Y71X-ray1.80A235-488[»]
B46-179[»]
4Y76X-ray2.00A235-488[»]
B46-179[»]
4Y79X-ray2.10A235-488[»]
B46-179[»]
4Y7AX-ray1.99A235-488[»]
B46-179[»]
4Y7BX-ray1.79A235-488[»]
B46-179[»]
4ZH8X-ray1.80A235-488[»]
B46-179[»]
4ZHAX-ray1.86A235-488[»]
B46-179[»]
5JQYX-ray1.99B86-124[»]
5JTCX-ray2.24B86-124[»]
5JZ8X-ray2.10B86-124[»]
5JZUX-ray2.50B86-111[»]
5JZZX-ray2.29B102-119[»]
5K0HX-ray2.20A235-468[»]
B128-178[»]
5VOEX-ray2.00H235-467[»]
L128-178[»]
5VOFX-ray2.25H235-467[»]
L128-178[»]
ProteinModelPortaliP00742
SMRiP00742
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108457, 9 interactors
CORUMiP00742
DIPiDIP-29896N
ELMiP00742
IntActiP00742, 11 interactors
MINTiP00742
STRINGi9606.ENSP00000364709

Chemistry databases

BindingDBiP00742
ChEMBLiCHEMBL244
DrugBankiDB07211 (2R)-2-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}PROPENE-1-SULFONAMIDE
DB08746 1-[[(1E)-2-(4-CHLOROPHENYL)ETHENYL]SULFONYL]-4-[[1-(4-PYRIDINYL)-4-PIPERIDINYL]METHYL]PIPERAZINE
DB07974 1-{2-[(4-CHLOROPHENYL)AMINO]-2-OXOETHYL}-N-(1-ISOPROPYLPIPERIDIN-4-YL)-1H-INDOLE-2-CARBOXAMIDE
DB07277 2-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}ETHANESULFONAMIDE
DB07278 2-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}ETHENESULFONAMIDE
DB08487 3-({4-[(6-CHLORO-1-BENZOTHIEN-2-YL)SULFONYL]-2-OXOPIPERAZIN-1-YL}METHYL)BENZENECARBOXIMIDAMIDE
DB08495 4-({4-[(6-CHLORO-1-BENZOTHIEN-2-YL)SULFONYL]-2-OXOPIPERAZIN-1-YL}METHYL)BENZENECARBOXIMIDAMIDE
DB04673 4-[(5-CHLOROINDOL-2-YL)SULFONYL]-2-(2-METHYLPROPYL)-1-[[5-(PYRIDIN-4-YL)PYRIMIDIN-2-YL]CARBONYL]PIPERAZINE
DB08745 4-[[(1E)-2-(4-CHLOROPHENYL)ETHENYL]SULFONYL]-1-[[1-(4-PYRIDINYL)-4-PIPERIDINYL]METHYL]PIPERAZINONE
DB08173 5-CHLORO-N-(2-(4-(2-OXOPYRIDIN-1(2H)-YL)BENZAMIDO)ETHYL)THIOPHENE-2-CARBOXAMIDE
DB07872 5-chloro-N-[(3R)-1-(2-{[2-fluoro-4-(2-oxopyridin-1(2H)-yl)phenyl]amino}-2-oxoethyl)pyrrolidin-3-yl]thiophene-2-carboxamide
DB07843 5-CHLORO-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}-1-BENZOTHIOPHENE-2-SULFONAMIDE
DB07847 6-CHLORO-N-{(3S)-1-[(1S)-1-METHYL-2-(4-MORPHOLINYL)-2-OXO ETHYL]-2-OXO-3-PYRROLIDINYL}-2-NAPHTHALENESULFONAMIDE
DB07844 6-CHLORO-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}-1-BENZOTHIOPHENE-2-SULFONAMIDE
DB00025 Antihemophilic Factor (Recombinant)
DB06605 Apixaban
DB00100 Coagulation Factor IX (Recombinant)
DB13150 Coagulation factor VII human
DB00036 Coagulation factor VIIa Recombinant Human
DB09075 Edoxaban
DB01225 Enoxaparin
DB00569 Fondaparinux sodium
DB03847 Gamma-Carboxy-Glutamic Acid
DB01109 Heparin
DB05713 LY-517717
DB00170 Menadione
DB07973 N-(1-ISOPROPYLPIPERIDIN-4-YL)-1-(3-METHOXYBENZYL)-1H-INDOLE-2-CARBOXAMIDE
DB07800 N-(2-(((5-CHLORO-2-PYRIDINYL)AMINO)SULFONYL)PHENYL)-4-(2-OXO-1(2H)-PYRIDINYL)BENZAMIDE
DB06228 Rivaroxaban
DB05362 SSR-126517E
GuidetoPHARMACOLOGYi2359

Protein family/group databases

MEROPSiS01.216

PTM databases

GlyConnecti102
iPTMnetiP00742
PhosphoSitePlusiP00742
UniCarbKBiP00742

Polymorphism and mutation databases

BioMutaiF10
DMDMi119761

Proteomic databases

PaxDbiP00742
PeptideAtlasiP00742
PRIDEiP00742
ProteomicsDBi51275

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375559; ENSP00000364709; ENSG00000126218
GeneIDi2159
KEGGihsa:2159

Organism-specific databases

CTDi2159
DisGeNETi2159
EuPathDBiHostDB:ENSG00000126218.11
GeneCardsiF10
HGNCiHGNC:3528 F10
MalaCardsiF10
MIMi227600 phenotype
613872 gene
neXtProtiNX_P00742
OpenTargetsiENSG00000126218
Orphaneti328 Congenital factor X deficiency
PharmGKBiPA27940
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IGPV Eukaryota
COG5640 LUCA
GeneTreeiENSGT00760000118890
HOGENOMiHOG000251821
HOVERGENiHBG013304
InParanoidiP00742
KOiK01314
OMAiNFLKWID
OrthoDBiEOG091G0AH5
PhylomeDBiP00742
TreeFamiTF327329

Enzyme and pathway databases

BioCyciMetaCyc:HS05000-MONOMER
BRENDAi3.4.21.6 2681
ReactomeiR-HSA-140834 Extrinsic Pathway of Fibrin Clot Formation
R-HSA-140837 Intrinsic Pathway of Fibrin Clot Formation
R-HSA-140875 Common Pathway of Fibrin Clot Formation
R-HSA-159740 Gamma-carboxylation of protein precursors
R-HSA-159763 Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus
R-HSA-159782 Removal of aminoterminal propeptides from gamma-carboxylated proteins
SABIO-RKiP00742
SIGNORiP00742

Miscellaneous databases

ChiTaRSiF10 human
EvolutionaryTraceiP00742
GeneWikiiFactor_X
GenomeRNAii2159
PMAP-CutDBiP00742
PROiPR:P00742
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000126218 Expressed in 127 organ(s), highest expression level in right lobe of liver
CleanExiHS_F10
ExpressionAtlasiP00742 baseline and differential
GenevisibleiP00742 HS

Family and domain databases

CDDicd00190 Tryp_SPc, 1 hit
Gene3Di4.10.740.10, 1 hit
InterProiView protein in InterPro
IPR017857 Coagulation_fac-like_Gla_dom
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR000152 EGF-type_Asp/Asn_hydroxyl_site
IPR018097 EGF_Ca-bd_CS
IPR035972 GLA-like_dom_SF
IPR000294 GLA_domain
IPR012224 Pept_S1A_FX
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR001254 Trypsin_dom
IPR018114 TRYPSIN_HIS
IPR033116 TRYPSIN_SER
PfamiView protein in Pfam
PF00008 EGF, 1 hit
PF00594 Gla, 1 hit
PF00089 Trypsin, 1 hit
PIRSFiPIRSF001143 Factor_X, 1 hit
PRINTSiPR00722 CHYMOTRYPSIN
PR00001 GLABLOOD
SMARTiView protein in SMART
SM00181 EGF, 2 hits
SM00179 EGF_CA, 1 hit
SM00069 GLA, 1 hit
SM00020 Tryp_SPc, 1 hit
SUPFAMiSSF50494 SSF50494, 2 hits
SSF57630 SSF57630, 1 hit
PROSITEiView protein in PROSITE
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
ProtoNetiSearch...

Entry informationi

Entry nameiFA10_HUMAN
AccessioniPrimary (citable) accession number: P00742
Secondary accession number(s): Q14340
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1989
Last modified: October 10, 2018
This is version 247 of the entry and version 2 of the sequence. See 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 entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  6. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
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