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P08709 (FA7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 203. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Coagulation factor VII

EC=3.4.21.21
Alternative name(s):
Proconvertin
Serum prothrombin conversion accelerator
Short name=SPCA
INN=Eptacog alfa

Cleaved into the following 2 chains:

  1. Factor VII light chain
  2. Factor VII heavy chain
Gene names
Name:F7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis. In the presence of tissue factor and calcium ions, factor VIIa then converts factor X to factor Xa by limited proteolysis. Factor VIIa will also convert factor IX to factor IXa in the presence of tissue factor and calcium.

Catalytic activity

Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.

Subunit structure

Heterodimer of a light chain and a heavy chain linked by a disulfide bond.

Subcellular location

Secreted.

Tissue specificity

Plasma.

Post-translational modification

The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.

The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.

O- and N-glycosylated. N-glycosylation at Asn-205 occurs cotranslationally and is mediated by STT3A-containing complexes, while glycosylation at Asn-382 is post-translational and is mediated STT3B-containing complexes before folding. O-fucosylated by POFUT1 on a conserved serine or threonine residue found in the consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains, where C2 and C3 are the second and third conserved cysteines. Ref.12 Ref.13 Ref.14 Ref.15 Ref.16

Involvement in disease

Factor VII deficiency (FA7D) [MIM:227500]: A hemorrhagic disease with variable presentation. The clinical picture can be very severe, with the early occurrence of intracerebral hemorrhages or repeated hemarthroses, or, in contrast, moderate with cutaneous-mucosal hemorrhages (epistaxis, menorrhagia) or hemorrhages provoked by a surgical intervention. Finally, numerous subjects are completely asymptomatic despite very low factor VII levels.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.20 Ref.21 Ref.22 Ref.24 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.37 Ref.38 Ref.39 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45 Ref.46 Ref.47

Pharmaceutical use

Available under the names Niastase or Novoseven (Novo Nordisk). Used for the treatment of bleeding episodes in hemophilia A or B patients with antibodies to coagulation factors VIII or IX.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 2 EGF-like domains.

Contains 1 Gla (gamma-carboxy-glutamate) domain.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Biological processBlood coagulation
Hemostasis
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainEGF-like domain
Repeat
Signal
   LigandCalcium
   Molecular functionHydrolase
Protease
Serine protease
   PTMCleavage on pair of basic residues
Disulfide bond
Gamma-carboxyglutamic acid
Glycoprotein
Hydroxylation
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Pharmaceutical
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Traceable author statement. Source: Reactome

blood coagulation, extrinsic pathway

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

circadian rhythm

Inferred from electronic annotation. Source: Ensembl

organ regeneration

Inferred from electronic annotation. Source: Ensembl

peptidyl-glutamic acid carboxylation

Traceable author statement. Source: Reactome

positive regulation of blood coagulation

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell migration

Traceable author statement PubMed 18612547. Source: BHF-UCL

positive regulation of leukocyte chemotaxis

Inferred from direct assay PubMed 17991872. Source: BHF-UCL

positive regulation of platelet-derived growth factor receptor signaling pathway

Inferred from direct assay PubMed 17991872. Source: BHF-UCL

positive regulation of positive chemotaxis

Inferred from direct assay PubMed 17991872. Source: BHF-UCL

positive regulation of protein kinase B signaling

Inferred from direct assay PubMed 18612547. Source: BHF-UCL

post-translational protein modification

Traceable author statement. Source: Reactome

proteolysis

Traceable author statement. Source: Reactome

response to estrogen

Inferred from electronic annotation. Source: Ensembl

response to growth hormone

Inferred from electronic annotation. Source: Ensembl

response to vitamin K

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi lumen

Traceable author statement. Source: Reactome

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

vesicle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

glycoprotein binding

Inferred from physical interaction PubMed 3455766. Source: BHF-UCL

serine-type endopeptidase activity

Traceable author statement Ref.2. Source: ProtInc

serine-type peptidase activity

Traceable author statement Ref.2. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: P08709-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform B (identifier: P08709-2)

The sequence of this isoform differs from the canonical sequence as follows:
     22-43: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Propeptide21 – 6040
PRO_0000027729
Chain61 – 212152Factor VII light chain
PRO_0000027730
Chain213 – 466254Factor VII heavy chain
PRO_0000027731

Regions

Domain61 – 10545Gla
Domain106 – 14237EGF-like 1; calcium-binding Potential
Domain147 – 18842EGF-like 2
Domain213 – 452240Peptidase S1

Sites

Active site2531Charge relay system By similarity
Active site3021Charge relay system By similarity
Active site4041Charge relay system By similarity
Binding site3981Substrate By similarity
Site212 – 2132Cleavage; by factor Xa, factor XIIa, factor IXa, or thrombin Ref.1

Amino acid modifications

Modified residue6614-carboxyglutamate Ref.1
Modified residue6714-carboxyglutamate Ref.1
Modified residue7414-carboxyglutamate Ref.1
Modified residue7614-carboxyglutamate Ref.1
Modified residue7914-carboxyglutamate
Modified residue8014-carboxyglutamate Ref.1
Modified residue8514-carboxyglutamate Ref.1
Modified residue8614-carboxyglutamate Ref.1
Modified residue8914-carboxyglutamate Ref.1
Modified residue9514-carboxyglutamate Ref.1
Modified residue1231(3R)-3-hydroxyaspartate
Glycosylation1121O-linked (Glc...) Ref.14
CAR_000007
Glycosylation1201O-linked (Fuc) Ref.14 Ref.15
CAR_000180
Glycosylation2051N-linked (GlcNAc...) Ref.10 Ref.16
Glycosylation3821N-linked (GlcNAc...) Ref.16
Disulfide bond77 ↔ 82
Disulfide bond110 ↔ 121
Disulfide bond115 ↔ 130
Disulfide bond132 ↔ 141
Disulfide bond151 ↔ 162
Disulfide bond158 ↔ 172
Disulfide bond174 ↔ 187
Disulfide bond195 ↔ 322
Disulfide bond219 ↔ 224
Disulfide bond238 ↔ 254
Disulfide bond370 ↔ 389
Disulfide bond400 ↔ 428

Natural variations

Alternative sequence22 – 4322Missing in isoform B.
VSP_005387
Natural variant131L → P in FA7D; Morioka. Ref.33
VAR_014391
Natural variant591R → RR in FA7D. Ref.46
VAR_065369
Natural variant641F → L in FA7D. Ref.39 Ref.44
VAR_015135
Natural variant731L → Q in FA7D. Ref.38 Ref.44
Corresponds to variant rs45572939 [ dbSNP | Ensembl ].
VAR_014405
Natural variant791E → Q in FA7D. Ref.38
VAR_014406
Natural variant821C → F in FA7D. Ref.44
VAR_065370
Natural variant821C → R in FA7D. Ref.43
VAR_065371
Natural variant841Missing in FA7D. Ref.44
VAR_065372
Natural variant851E → K in FA7D. Ref.41
VAR_065373
Natural variant881R → G in FA7D. Ref.44
VAR_065374
Natural variant881R → P in FA7D. Ref.44
VAR_065375
Natural variant1171N → D in FA7D; exhibits no procoagulant activity and is unable to bind tissue factor. Ref.32
VAR_065376
Natural variant1201S → P in FA7D. Ref.39 Ref.44
VAR_015136
Natural variant1211C → F in FA7D. Ref.38
VAR_014407
Natural variant1251L → P in FA7D. Ref.38
VAR_014408
Natural variant1281Y → C in FA7D. Ref.38 Ref.39 Ref.44
VAR_014409
Natural variant1381G → D in FA7D. Ref.44
VAR_065377
Natural variant1391R → K in FA7D.
VAR_006497
Natural variant1391R → Q in FA7D; Charlotte. Ref.24 Ref.44
Corresponds to variant rs150525536 [ dbSNP | Ensembl ].
VAR_006498
Natural variant1391R → W in FA7D. Ref.38
VAR_006499
Natural variant1511C → S in FA7D. Ref.38
VAR_014410
Natural variant1541E → K in FA7D. Ref.39 Ref.44
Corresponds to variant rs146795869 [ dbSNP | Ensembl ].
VAR_015137
Natural variant1561G → S in FA7D. Ref.44
VAR_065378
Natural variant1571G → C in FA7D.
VAR_006501
Natural variant1571G → S in FA7D. Ref.39 Ref.44
VAR_006500
Natural variant1571G → V in FA7D. Ref.38
VAR_014411
Natural variant1601Q → R in FA7D. Ref.38 Ref.39 Ref.44
VAR_006502
Natural variant1711S → F in FA7D. Ref.44
VAR_065379
Natural variant1771G → R in FA7D. Ref.43
VAR_065380
Natural variant1811L → P in FA7D. Ref.44
VAR_065381
Natural variant1831D → N in FA7D. Ref.44
VAR_065382
Natural variant1861S → F in FA7D. Ref.44
VAR_065383
Natural variant1891P → S in FA7D. Ref.44
VAR_065384
Natural variant1941P → L in FA7D. Ref.44
VAR_065385
Natural variant1941P → T in FA7D; Malta-I. Ref.34 Ref.44
VAR_006503
Natural variant1951C → R in FA7D. Ref.38 Ref.39 Ref.44
VAR_014412
Natural variant1971K → E in FA7D.
VAR_006504
Natural variant1981I → T in FA7D. Ref.43
VAR_065386
Natural variant2121R → Q in FA7D; Charlotte. Ref.24 Ref.39 Ref.43 Ref.44
VAR_006505
Natural variant2161G → D in FA7D. Ref.39 Ref.44
VAR_015138
Natural variant2381C → Y in FA7D. Ref.22
VAR_006506
Natural variant2401G → R in FA7D. Ref.45
VAR_065387
Natural variant2411T → N in FA7D. Ref.38 Ref.44
VAR_014413
Natural variant2501S → F in FA7D. Ref.47
VAR_065388
Natural variant2511A → P in FA7D. Ref.43
VAR_065389
Natural variant2511A → T in FA7D. Ref.44
VAR_065390
Natural variant2541C → R in FA7D. Ref.44
VAR_065391
Natural variant2541C → Y in FA7D. Ref.39 Ref.44
VAR_015139
Natural variant2641L → P in FA7D. Ref.44
VAR_065392
Natural variant2661A → T in FA7D. Ref.39 Ref.44
VAR_015140
Natural variant2721D → N in FA7D. Ref.44
VAR_065393
Natural variant2771D → N in FA7D. Ref.44
VAR_065394
Natural variant2831R → W in FA7D. Ref.29 Ref.44
VAR_006507
Natural variant2951V → D. Ref.35
Corresponds to variant rs6045 [ dbSNP | Ensembl ].
VAR_013936
Natural variant2981T → I in FA7D. Ref.44
VAR_065395
Natural variant3011H → Q in FA7D. Ref.44
VAR_065396
Natural variant3021D → H in FA7D. Ref.38 Ref.39 Ref.44
VAR_014414
Natural variant3021D → N in FA7D. Ref.38 Ref.44
VAR_014415
Natural variant3041A → T in FA7D. Ref.38 Ref.44
VAR_014416
Natural variant3041A → V in FA7D; Malta-II. Ref.31 Ref.34 Ref.38 Ref.39 Ref.44
VAR_006508
Natural variant3071R → C in FA7D. Ref.38 Ref.39 Ref.44
VAR_014417
Natural variant3071R → H in FA7D; Mie. Ref.27 Ref.44
VAR_006509
Natural variant3121V → M in FA7D. Ref.39 Ref.44
VAR_015141
Natural variant3141L → V in FA7D. Ref.46
VAR_065397
Natural variant3211L → F in FA7D. Ref.44
VAR_065398
Natural variant3231L → R in FA7D. Ref.43
VAR_065399
Natural variant3251E → K in FA7D. Ref.29 Ref.39 Ref.44
VAR_006510
Natural variant3261R → Q in FA7D. Ref.44
VAR_065400
Natural variant3321T → M in FA7D. Ref.38
VAR_014418
Natural variant3371R → C in FA7D. Ref.44
VAR_065401
Natural variant3411V → F in FA7D. Ref.39 Ref.44
VAR_015142
Natural variant3431G → S in FA7D. Ref.44 Ref.46
VAR_065402
Natural variant3441W → R in FA7D. Ref.43
VAR_065403
Natural variant3451G → S in FA7D. Ref.44
VAR_065404
Natural variant3501R → C in FA7D. Ref.44
VAR_065405
Natural variant3521A → T. Ref.6
Corresponds to variant rs3093267 [ dbSNP | Ensembl ].
VAR_013122
Natural variant3541A → V in FA7D. Ref.3 Ref.26 Ref.38 Ref.39 Ref.44
Corresponds to variant rs36209567 [ dbSNP | Ensembl ].
VAR_006511
Natural variant3581M → I in FA7D. Ref.11 Ref.38 Ref.39 Ref.44
VAR_006512
Natural variant3581M → V in FA7D. Ref.29
VAR_006513
Natural variant3601L → P in FA7D. Ref.44
VAR_065406
Natural variant3631P → H in FA7D. Ref.44
VAR_065407
Natural variant3631P → R in FA7D. Ref.39 Ref.44
VAR_015143
Natural variant3641R → Q in FA7D; Harrow/Padua. Ref.11 Ref.20 Ref.21 Ref.29 Ref.44
Corresponds to variant rs121964926 [ dbSNP | Ensembl ].
VAR_006514
Natural variant3641R → W in FA7D. Ref.44
VAR_065408
Natural variant3671T → S. Ref.25
VAR_018671
Natural variant3701C → F in FA7D. Ref.11 Ref.21 Ref.38 Ref.39 Ref.43 Ref.44
VAR_006515
Natural variant3751R → W in FA7D. Ref.44
Corresponds to variant rs137919286 [ dbSNP | Ensembl ].
VAR_065409
Natural variant3841T → M in FA7D. Ref.43 Ref.44
VAR_065410
Natural variant3871M → T in FA7D. Ref.44
VAR_065411
Natural variant3871M → V in FA7D. Ref.44
VAR_065412
Natural variant3881F → S in FA7D; reduces tissue factor binding; impairs activation by factor Xa; abolishes amidolytic and coagulant activities. Ref.30 Ref.44
VAR_065413
Natural variant3891C → G in FA7D. Ref.37 Ref.38 Ref.46
VAR_014392
Natural variant3911G → C in FA7D. Ref.44
VAR_065414
Natural variant3911G → S in FA7D. Ref.38 Ref.44
Corresponds to variant rs190485816 [ dbSNP | Ensembl ].
VAR_014419
Natural variant3981D → E in FA7D. Ref.43
VAR_065415
Natural variant4011K → E in FA7D. Ref.44
VAR_065416
Natural variant4021G → E in FA7D. Ref.29
VAR_006517
Natural variant4021G → R in FA7D. Ref.11
VAR_006516
Natural variant4031D → H in FA7D. Ref.39 Ref.44
VAR_015144
Natural variant4041S → N in FA7D. Ref.44
VAR_065417
Natural variant4081H → Q in FA7D. Ref.41
Corresponds to variant rs121964936 [ dbSNP | Ensembl ].
VAR_065418
Natural variant4081H → R in FA7D. Ref.43
VAR_065419
Natural variant4131R → G in FA7D. Ref.44
VAR_065420
Natural variant4131R → Q May be associated with decreased susceptibility to myocardial infarction. Ref.3 Ref.6 Ref.11 Ref.29 Ref.35 Ref.40
Corresponds to variant rs6046 [ dbSNP | Ensembl ].
VAR_006518
Natural variant4141G → C in FA7D; results in severely impaired protein secretion. Ref.42
VAR_065421
Natural variant4191T → M in FA7D. Ref.28 Ref.39 Ref.44
VAR_006519
Natural variant4221V → F in FA7D. Ref.44
VAR_065422
Natural variant4251G → A in FA7D. Ref.44
VAR_065423
Natural variant4251G → C in FA7D. Ref.44
VAR_065424
Natural variant4291A → T in FA7D. Ref.44
VAR_065425
Natural variant4321G → D in FA7D. Ref.44
VAR_065426
Natural variant4351G → E in FA7D. Ref.38 Ref.44
VAR_014420
Natural variant4371Y → F in FA7D. Ref.44
VAR_065427
Natural variant4451E → K. Ref.6
Corresponds to variant rs3093248 [ dbSNP | Ensembl ].
VAR_013123

Secondary structure

............................................................................................... 466
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 9B5D501669D67B06

FASTA46651,594
        10         20         30         40         50         60 
MVSQALRLLC LLLGLQGCLA AGGVAKASGG ETRDMPWKPG PHRVFVTQEE AHGVLHRRRR 

        70         80         90        100        110        120 
ANAFLEELRP GSLERECKEE QCSFEEAREI FKDAERTKLF WISYSDGDQC ASSPCQNGGS 

       130        140        150        160        170        180 
CKDQLQSYIC FCLPAFEGRN CETHKDDQLI CVNENGGCEQ YCSDHTGTKR SCRCHEGYSL 

       190        200        210        220        230        240 
LADGVSCTPT VEYPCGKIPI LEKRNASKPQ GRIVGGKVCP KGECPWQVLL LVNGAQLCGG 

       250        260        270        280        290        300 
TLINTIWVVS AAHCFDKIKN WRNLIAVLGE HDLSEHDGDE QSRRVAQVII PSTYVPGTTN 

       310        320        330        340        350        360 
HDIALLRLHQ PVVLTDHVVP LCLPERTFSE RTLAFVRFSL VSGWGQLLDR GATALELMVL 

       370        380        390        400        410        420 
NVPRLMTQDC LQQSRKVGDS PNITEYMFCA GYSDGSKDSC KGDSGGPHAT HYRGTWYLTG 

       430        440        450        460 
IVSWGQGCAT VGHFGVYTRV SQYIEWLQKL MRSEPRPGVL LRAPFP 

« Hide

Isoform B [UniParc].

Checksum: 2E74EAFD2FADF2A4
Show »

FASTA44449,320

References

« Hide 'large scale' references
[1]"Characterization of a cDNA coding for human factor VII."
Hagen F.S., Gray C.L., O'Hara P.J., Grant F.J., Saari G.C., Woodbury R.G., Hart C.E., Insley M.Y., Kisiel W., Kurachi K., Davie E.W.
Proc. Natl. Acad. Sci. U.S.A. 83:2412-2416(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
Tissue: Liver.
[2]"Nucleotide sequence of the gene coding for human factor VII, a vitamin K-dependent protein participating in blood coagulation."
O'Hara P.J., Grant F.J., Haldeman B.A., Gray C.L., Insley M.Y., Hagen F.S., Murray M.J.
Proc. Natl. Acad. Sci. U.S.A. 84:5158-5162(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Human F7 sequence is split into three deep clades that are related to FVII plasma levels."
Sabater-Lleal M., Soria J.M., Bertranpetit J., Almasy L., Blangero J., Fontcuberta J., Calafell F.
Hum. Genet. 118:741-751(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-354 AND GLN-413.
[4]"Complete dissection of a human quantitative trait locus: allelic architecture of F7 and factor VII levels."
Soria J.M., Almasy L., Souto J.C., Sabater M., Fontcuberta J., Blangero J.
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]Masroori N., Habibi Roudkenar M., Halabian R.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[6]SeattleSNPs variation discovery resource
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-352; GLN-413 AND LYS-445.
[7]NHLBI resequencing and genotyping service (RS&G)
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]"The DNA sequence and analysis of human chromosome 13."
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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] (ISOFORM B).
[10]"Amino acid sequence and posttranslational modifications of human factor VIIa from plasma and transfected baby hamster kidney cells."
Thim L., Bjoern S., Christensen M., Nicolaisen E.M., Lund-Hansen T., Pedersen A.H., Hedner U.
Biochemistry 27:7785-7793(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 61-466, POST-TRANSLATIONAL MODIFICATIONS.
[11]"Molecular defects in CRM+ factor VII deficiencies: modelling of missense mutations in the catalytic domain of FVII."
Bernardi F., Liney D.L., Patracchini P., Gemmati D., Legnani C., Arcieri P., Pinotti M., Redaelli R., Ballerini G., Pemberton S., Wacey A.I., Mariani G., Tuddenham E.G.D., Marchetti G.
Br. J. Haematol. 86:610-618(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 354-412, VARIANTS FA7D ILE-358; GLN-364; PHE-370 AND ARG-402, VARIANT GLN-413.
[12]"Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z."
Nishimura H., Kawabata S., Kisiel W., Hase S., Ikenaka T., Takao T., Shimonishi Y., Iwanaga S.
J. Biol. Chem. 264:20320-20325(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE OF CARBOHYDRATE ON SER-112.
[13]"A new trisaccharide sugar chain linked to a serine residue in the first EGF-like domain of clotting factors VII and IX and protein Z."
Iwanaga S., Nishimura H., Kawabata S., Kisiel W., Hase S., Ikenaka T.
Adv. Exp. Med. Biol. 281:121-131(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE OF CARBOHYDRATE ON SER-112.
[14]"Human plasma and recombinant factor VII. Characterization of O-glycosylations at serine residues 52 and 60 and effects of site-directed mutagenesis of serine 52 to alanine."
Bjoern S., Foster D.C., Thim L., Wiberg F.C., Christensen M., Komiyama Y., Pedersen A.H., Kisiel W.
J. Biol. Chem. 266:11051-11057(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT SER-112 AND SER-120.
[15]"Identification of a GDP-L-fucose:polypeptide fucosyltransferase and enzymatic addition of O-linked fucose to EGF domains."
Wang Y., Lee G.F., Kelley R.F., Spellman M.W.
Glycobiology 6:837-842(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT SER-120, IDENTIFICATION BY MASS SPECTROMETRY.
[16]"Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms."
Ruiz-Canada C., Kelleher D.J., Gilmore R.
Cell 136:272-283(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-205 AND ASN-382.
[17]"The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor."
Banner D.W., D'Arcy A., Chene C., Winkler F.K., Guha A., Konigsberg W.H., Nemreson Y., Kirchhofer D.
Nature 380:41-46(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF FVIIA IN COMPLEX WITH TF.
[18]"Structure of extracellular tissue factor complexed with factor VIIa inhibited with a BPTI mutant."
Zhang E., St Charles R., Tulinsky A.
J. Mol. Biol. 285:2089-2104(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF FVIIA IN COMPLEX WITH TF.
[19]"Solution structure of the N-terminal EGF-like domain from human factor VII."
Muranyi A., Finn B.E., Gippert G.P., Forsen S., Stenflo J., Drakenberg T.
Biochemistry 37:10605-10615(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 105-145.
[20]"Purification and characterization of factor VII 304-Gln: a variant molecule with reduced activity isolated from a clinically unaffected male."
O'Brien D.P., Gale K.M., Anderson J.S., McVey J.H., Miller G.J., Meade T.W., Tuddenham E.G.D.
Blood 78:132-140(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FA7D GLN-364.
[21]"Detection of two missense mutations and characterization of a repeat polymorphism in the factor VII gene (F7)."
Marchetti G., Patracchini P., Gemmati D., Derosa V., Pinotti M., Rodorigo G., Casonato A., Girolami A., Bernardi F.
Hum. Genet. 89:497-502(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FA7D GLN-364 AND PHE-370.
[22]"A missense mutation (178Cys-->Tyr) and two neutral dimorphisms (115His and 333Ser) in the human coagulation factor VII gene."
Marchetti G., Ferrati M., Patracchini P., Redaelli R., Bernardi F.
Hum. Mol. Genet. 2:1055-1056(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FA7D TYR-238.
[23]"Detection of missense mutations by single-strand conformational polymorphism (SSCP) analysis in five dysfunctional variants of coagulation factor VII."
Takamiya O., Kemball-Cook G., Martin D.M.A., Cooper D.N., von Felten A., Meili E., Hahn I., Prangnell D.R., Lumley H., Tuddenham E.G.D., McVey J.H.
Hum. Mol. Genet. 2:1355-1359(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS.
[24]"Severe factor VII deficiency caused by mutations abolishing the cleavage site for activation and altering binding to tissue factor."
Chaing S., Clarke B., Sridhara S., Chu K., Friedman P., Vandusen W., Roberts H.R., Blajchman M., Monroe D.M., High K.A.
Blood 83:3524-3535(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FA7D GLN-139 AND GLN-212.
[25]"A common Ser/Thr polymorphism in the perforin-homologous region of human complement component C7."
Dewald G., Noethen M.M., Ruther K.
Hum. Hered. 44:301-304(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SER-367.
[26]"Topologically equivalent mutations causing dysfunctional coagulation factors VII (294Ala-->Val) and X (334Ser-->Pro)."
Bernardi F., Castaman G., Redaelli R., Pinotti M., Lunghi B., Rodeghiero F., Marchetti G.
Hum. Mol. Genet. 3:1175-1177(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FA7D VAL-354.
[27]"Factor VII Mie: homozygous asymptomatic type I deficiency caused by an amino acid substitution of His (CAC) for Arg(247) (CGC) in the catalytic domain."
Ohiwa M., Hayashi T., Wada H., Minamikawa K., Shirakawa S., Suzuki K.
Thromb. Haemost. 71:773-777(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FA7D HIS-307.
[28]"A Thr359Met mutation in factor VII of a patient with a hereditary deficiency causes defective secretion of the molecule."
Arbini A.A., Mannucci P.M., Bauer K.A.
Blood 87:5085-5094(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FA7D MET-419.
[29]"Mutation pattern in clinically asymptomatic coagulation factor VII deficiency."
Bernardi F., Castaman G., Pinotti M., Ferraresi P., di Iasio M.G., Lunghi B., Rodeghiero F., Marchetti G.
Hum. Mutat. 8:108-115(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FA7D TRP-283; LYS-325; VAL-358; GLN-364 AND GLU-402, VARIANT GLN-413.
[30]"Factor VII central. A novel mutation in the catalytic domain that reduces tissue factor binding, impairs activation by factor Xa, and abolishes amidolytic and coagulant activity."
Bharadwaj D., Iino M., Kontoyianni M., Smith K.J., Foster D.C., Kisiel W.
J. Biol. Chem. 271:30685-30691(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FA7D SER-388, CHARACTERIZATION OF VARIANT FA7D SER-388.
[31]"Ala244Val is a common, probably ancient mutation causing factor VII deficiency in Moroccan and Iranian Jews."
Tamary H., Fromovich Y., Shalmon L., Reich Z., Dym O., Lanir N., Brenner B., Paz M., Luder A.S., Blau O., Korostishevsky M., Zaizov R., Seligsohn U.
Thromb. Haemost. 76:283-291(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FA7D VAL-304.
[32]"Factor VII deficiency caused by a structural variant N57D of the first epidermal growth factor domain."
Leonard B.J., Chen Q., Blajchman M.A., Ofosu F.A., Sridhara S., Yang D., Clarke B.J.
Blood 91:142-148(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FA7D ASP-117, CHARACTERIZATION OF VARIANT FA7D ASP-117.
[33]"Factor VII Morioka (FVII L-26P): a homozygous missense mutation in the signal sequence identified in a patient with factor VII deficiency."
Ozawa T., Takikawa Y., Niiya K., Ejiri N., Suzuki K., Sato S., Sakuragawa N.
Br. J. Haematol. 101:47-49(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FA7D PRO-13.
[34]"Two new missense mutations (P134T and A244V) in the coagulation factor VII gene."
Alshinawi C., Scerri C., Galdies R., Aquilina A., Felice A.E.
Hum. Mutat. Suppl. 1:S189-S191(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FA7D THR-194 AND VAL-304.
[35]"Characterization of single-nucleotide polymorphisms in coding regions of human genes."
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ASP-295 AND GLN-413.
[36]Erratum
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 23:373-373(1999)
[37]"Two novel factor VII gene mutations in a Chinese family with factor VII deficiency."
Au W.Y., Lam C.C.K., Chan E.C., Kwong Y.L.
Br. J. Haematol. 111:143-145(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FA7D GLY-389.
[38]"Molecular analysis of the genotype-phenotype relationship in factor VII deficiency."
Millar D.S., Kemball-Cook G., McVey J.H., Tuddenham E.G.D., Mumford A.D., Attock G.B., Reverter J.C., Lanir N., Parapia L.A., Reynaud J., Meili E., von Felton A., Martinowitz U., Prangnell D.R., Krawczak M., Cooper D.N.
Hum. Genet. 107:327-342(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FA7D GLN-73; GLN-79; PHE-121; PRO-125; CYS-128; TRP-139; SER-151; VAL-157; ARG-160; ARG-195; ASN-241; HIS-302; ASN-302; THR-304; VAL-304; CYS-307; MET-332; VAL-354; ILE-358; PHE-370; GLY-389; SER-391 AND GLU-435.
[39]"Twenty two novel mutations of the factor VII gene in factor VII deficiency."
Wulff K., Herrmann F.H.
Hum. Mutat. 15:489-496(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FA7D LEU-64; PRO-120; CYS-128; LYS-154; SER-157; ARG-160; ARG-195; GLN-212; ASP-216; TYR-254; THR-266; HIS-302; VAL-304; CYS-307; MET-312; LYS-325; PHE-341; VAL-354; ILE-358; ARG-363; PHE-370; HIS-403 AND MET-419.
[40]"Polymorphisms in the factor VII gene and the risk of myocardial infarction in patients with coronary artery disease."
Girelli D., Russo C., Ferraresi P., Olivieri O., Pinotti M., Friso S., Manzato F., Mazzucco A., Bernardi F., Corrocher R.
N. Engl. J. Med. 343:774-780(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLN-413.
[41]"Two double heterozygous mutations in the F7 gene show different manifestations."
Nagaizumi K., Inaba H., Suzuki T., Hatta Y., Hagiwara T., Amano K., Arai M., Fukutake K.
Br. J. Haematol. 119:1052-1058(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FA7D LYS-85 AND GLN-408.
[42]"A patient homozygous for a Gly354Cys mutation in factor VII that results in severely impaired secretion of the molecule, but not complete deficiency."
Takamiya O., Hino K.
Br. J. Haematol. 124:336-342(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FA7D CYS-414, CHARACTERIZATION OF VARIANT FA7D CYS-414.
[43]"Phenotypic and genotypic characterization of Factor VII deficiency patients from Western India."
Mota L., Shetty S., Idicula-Thomas S., Ghosh K.
Clin. Chim. Acta 409:106-111(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FA7D ARG-82; ARG-177; THR-198; GLN-212; PRO-251; ARG-323; ARG-344; PHE-370; MET-384; GLU-398 AND ARG-408.
[44]"Factor VII deficiency: clinical manifestation of 717 subjects from Europe and Latin America with mutations in the factor 7 gene."
Herrmann F.H., Wulff K., Auerswald G., Schulman S., Astermark J., Batorova A., Kreuz W., Pollmann H., Ruiz-Saez A., De Bosch N., Salazar-Sanchez L.
Haemophilia 15:267-280(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FA7D LEU-64; GLN-73; PHE-82; PHE-84 DEL; GLY-88; PRO-88; PRO-120; CYS-128; ASP-138; GLN-139; LYS-154; SER-156; SER-157; ARG-160; PHE-171; PRO-181; ASN-183; PHE-186; SER-189; LEU-194; THR-194; ARG-195; GLN-212; ASP-216; ASN-241; THR-251; ARG-254; TYR-254; PRO-264; THR-266; ASN-272; ASN-277; TRP-283; ILE-298; GLN-301; ASN-302; HIS-302; THR-304; VAL-304; CYS-307; HIS-307; MET-312; PHE-321; LYS-325; GLN-326; CYS-337; PHE-341; SER-343; SER-345; CYS-350; VAL-354; ILE-358; PRO-360; ARG-363; HIS-363; GLN-364; TRP-364; PHE-370; TRP-375; MET-384; THR-387; VAL-387; SER-388; CYS-391; SER-391; GLU-401; HIS-403; ASN-404; GLY-413; MET-419; PHE-422; ALA-425; CYS-425; THR-429; ASP-432; GLU-435 AND PHE-437.
[45]"Familial factor VII deficiency with foetal and neonatal fatal cerebral haemorrhage associated with homozygosis to Gly180Arg mutation."
Landau D., Rosenberg N., Zivelin A., Staretz-Chacham O., Kapelushnik J.
Haemophilia 15:774-778(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FA7D ARG-240.
[46]"Recurrent mutations and genotype-phenotype correlations in hereditary factor VII deficiency in Korea."
Kwon M.J., Yoo K.Y., Lee K.O., Kim S.H., Kim H.J.
Blood Coagul. Fibrinolysis 22:102-105(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FA7D ARG-59 INS; VAL-314; SER-343 AND GLY-389.
[47]"A novel missense mutation close to the charge-stabilizing system in a patient with congenital factor VII deficiency."
Jiang M., Wang Z., Yu Z., Bai X., Su J., Cao L., Zhang W., Ruan C.
Blood Coagul. Fibrinolysis 22:264-270(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FA7D PHE-250.
+Additional computationally mapped references.

Web resources

Wikipedia

Factor VII entry

GeneReviews
SeattleSNPs
SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M13232 mRNA. Translation: AAA88040.1.
M13232 mRNA. Translation: AAA88041.1.
J02933 Genomic DNA. Translation: AAA51983.1.
DQ142911 Genomic DNA. Translation: ABD17891.1.
AY212252 Genomic DNA. Translation: AAP33841.1.
EU557239 mRNA. Translation: ACB87203.1.
AF466933 Genomic DNA. Translation: AAL66184.1.
EF445049 Genomic DNA. Translation: ACA06107.1.
EF445049 Genomic DNA. Translation: ACA06108.1.
AL137002 Genomic DNA. Translation: CAI41381.1.
AL137002 Genomic DNA. Translation: CAI41382.1.
BC130468 mRNA. Translation: AAI30469.1.
PIRKFHU7. A28322.
RefSeqNP_000122.1. NM_000131.4.
NP_062562.1. NM_019616.3.
UniGeneHs.36989.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BF9NMR-A105-145[»]
1CVWX-ray2.28H213-466[»]
L150-204[»]
1DANX-ray2.00H213-466[»]
L61-212[»]
1DVAX-ray3.00H/I213-466[»]
L/M102-202[»]
1F7ENMR-A105-147[»]
1F7MNMR-A105-147[»]
1FAKX-ray2.10H213-466[»]
L61-212[»]
1FF7NMR-A105-147[»]
1FFMNMR-A105-147[»]
1J9CX-ray2.90H213-466[»]
L108-202[»]
1JBUX-ray2.00H213-466[»]
L150-212[»]
1KLIX-ray1.69H213-466[»]
L144-212[»]
1KLJX-ray2.44H213-466[»]
L144-212[»]
1NL8model-H213-466[»]
M61-202[»]
1O5DX-ray2.05H213-466[»]
L61-212[»]
1QFKX-ray2.80H213-466[»]
L109-212[»]
1W0YX-ray2.50H213-466[»]
L61-202[»]
1W2KX-ray3.00H213-466[»]
L61-202[»]
1W7XX-ray1.80H213-466[»]
L150-204[»]
1W8BX-ray3.00H213-466[»]
L148-204[»]
1WQVX-ray2.50H213-466[»]
L61-212[»]
1WSSX-ray2.60H213-466[»]
L61-212[»]
1WTGX-ray2.20H213-466[»]
L61-212[»]
1WUNX-ray2.40H213-466[»]
L61-212[»]
1WV7X-ray2.70H213-466[»]
L61-212[»]
1YGCX-ray2.00H213-466[»]
L150-212[»]
1Z6JX-ray2.00H213-466[»]
L61-202[»]
2A2QX-ray1.80H213-466[»]
L61-212[»]
2AEIX-ray2.52H213-466[»]
L61-212[»]
2AERX-ray1.87H213-466[»]
L61-202[»]
2B7DX-ray2.24H213-466[»]
L61-212[»]
2B8OX-ray2.80H213-466[»]
L61-202[»]
2BZ6X-ray1.60H213-466[»]
L150-202[»]
2C4FX-ray1.72H213-466[»]
L61-202[»]
2EC9X-ray2.00H213-466[»]
L61-202[»]
2F9BX-ray2.54H213-466[»]
L61-212[»]
2FIRX-ray2.00H213-466[»]
L61-202[»]
2FLBX-ray1.95H213-466[»]
L61-212[»]
2FLRX-ray2.35H213-466[»]
L61-212[»]
2PUQX-ray2.05H213-466[»]
L109-202[»]
2ZP0X-ray2.70H213-466[»]
L61-212[»]
2ZWLX-ray2.20H213-466[»]
L61-212[»]
2ZZUX-ray2.50H213-466[»]
L61-212[»]
3ELAX-ray2.20H213-466[»]
L61-212[»]
3TH2X-ray1.72H213-466[»]
L61-202[»]
3TH3X-ray2.70H213-466[»]
L61-202[»]
3TH4X-ray1.80H213-466[»]
L61-202[»]
4ISHX-ray1.82H213-466[»]
L150-204[»]
4ISIX-ray1.94H213-466[»]
L150-204[»]
4JYUX-ray1.80H213-466[»]
L150-204[»]
4JYVX-ray2.19H213-466[»]
L150-204[»]
4JZDX-ray2.20H213-466[»]
L150-204[»]
4JZEX-ray1.52H213-466[»]
L150-204[»]
4JZFX-ray1.84H213-466[»]
L150-204[»]
4NA9X-ray2.24H213-466[»]
L150-204[»]
4NG9X-ray2.20H213-466[»]
L150-204[»]
4NGAX-ray2.15H213-466[»]
L150-204[»]
ProteinModelPortalP08709.
SMRP08709. Positions 68-466.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108453. 7 interactions.
DIPDIP-6135N.
IntActP08709. 10 interactions.
MINTMINT-1155299.
STRING9606.ENSP00000364731.

Chemistry

BindingDBP08709.
ChEMBLCHEMBL2111412.
DrugBankDB00100. Coagulation Factor IX.
DB00036. Coagulation factor VIIa.
DB00170. Menadione.
GuidetoPHARMACOLOGY2363.

Protein family/group databases

MEROPSS01.215.

PTM databases

UniCarbKBP08709.

Polymorphism databases

DMDM119766.

Proteomic databases

PaxDbP08709.
PRIDEP08709.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000346342; ENSP00000329546; ENSG00000057593. [P08709-2]
ENST00000375581; ENSP00000364731; ENSG00000057593. [P08709-1]
GeneID2155.
KEGGhsa:2155.
UCSCuc001vsv.4. human. [P08709-1]
uc001vsw.4. human. [P08709-2]

Organism-specific databases

CTD2155.
GeneCardsGC13P113760.
HGNCHGNC:3544. F7.
HPAHPA004826.
MIM227500. phenotype.
613878. gene.
neXtProtNX_P08709.
Orphanet327. Congenital factor VII deficiency.
PharmGKBPA160.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5640.
HOVERGENHBG013304.
InParanoidP08709.
KOK01320.
OMAGCEQYCS.
OrthoDBEOG75B84T.
PhylomeDBP08709.
TreeFamTF327329.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_24941. Circadian Clock.
REACT_604. Hemostasis.
SABIO-RKP08709.

Gene expression databases

ArrayExpressP08709.
BgeeP08709.
CleanExHS_F7.
GenevestigatorP08709.

Family and domain databases

Gene3D4.10.740.10. 1 hit.
InterProIPR017857. 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]
PfamPF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF001143. Factor_X. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTSM00181. EGF. 1 hit.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
SSF57630. SSF57630. 1 hit.
PROSITEPS00010. ASX_HYDROXYL. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
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]
ProtoNetSearch...

Other

EvolutionaryTraceP08709.
GeneWikiFactor_VII.
GenomeRNAi2155.
NextBio8705.
PMAP-CutDBP08709.
PROP08709.
SOURCESearch...

Entry information

Entry nameFA7_HUMAN
AccessionPrimary (citable) accession number: P08709
Secondary accession number(s): B0YJC8 expand/collapse secondary AC list , Q14339, Q5JVF1, Q5JVF2, Q9UD52, Q9UD53, Q9UD54
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: April 16, 2014
This is version 203 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM