P12259 (FA5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Coagulation factor V

Alternative name(s):
Activated protein C cofactor
Proaccelerin, labile factor

Cleaved into the following 2 chains:

1. Coagulation factor V heavy chain
2. Coagulation factor V light chain

Gene names

Name:

F5

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2224 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Central regulator of hemostasis. It serves as a critical cofactor for the prothrombinase activity of factor Xa that results in the activation of prothrombin to thrombin.
Enzyme regulation	Inhibited by SERPINA5. Ref.11 Ref.13 Ref.18 Ref.20
Subunit structure	Factor Va, the activated form of factor V, is composed of a heavy chain and a light chain, non-covalently bound. The interaction between the two chains is calcium-dependent. Forms heterodimer with SERPINA5.
Subcellular location	Secreted By similarity.
Tissue specificity	Plasma.
Domain	Domain B contains 35 x 9 AA tandem repeats, and 2 x 17 AA repeats.
Post-translational modification	Thrombin activates factor V proteolytically to the active cofactor, factor Va (formation of a heavy chain at the N-terminus and a light chain at the C-terminus). Sulfation is required for efficient thrombin cleavage and activation and for full procoagulant activity. Activated protein C inactivates factor V and factor Va by proteolytic degradation. Phosphorylation sites are present in the extracellular medium.
Involvement in disease	Factor V deficiency (FA5D) [MIM:227400]: A blood coagulation disorder leading to an hemorrhagic diathesis known as parahemophilia. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.35 Ref.38 Thrombophilia due to activated protein C resistance (THPH2) [MIM:188055]: A hemostatic disorder due to defective degradation of factor V by activated protein C. It is characterized by a poor anticoagulant response to activated protein C resulting in tendency to thrombosis. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.31 Ref.36 Ref.37 Ref.39 Ref.41 Budd-Chiari syndrome (BDCHS) [MIM:600880]: A syndrome caused by obstruction of hepatic venous outflow involving either the hepatic veins or the terminal segment of the inferior vena cava. Obstructions are generally caused by thrombosis and lead to hepatic congestion and ischemic necrosis. Clinical manifestations observed in the majority of patients include hepatomegaly, right upper quadrant pain and abdominal ascites. Budd-Chiari syndrome is associated with a combination of disease states including primary myeloproliferative syndromes and thrombophilia due to factor V Leiden, protein C deficiency and antithrombin III deficiency. Budd-Chiari syndrome is a rare but typical complication in patients with polycythemia vera. Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ischemic stroke (ISCHSTR) [MIM:601367]: A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors. Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.40 Pregnancy loss, recurrent, 1 (RPRGL1) [MIM:614389]: A common complication of pregnancy, resulting in spontaneous abortion before the fetus has reached viability. The term includes all miscarriages from the time of conception until 24 weeks of gestation. Recurrent pregnancy loss is defined as 3 or more consecutive spontaneous abortions. Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.19
Sequence similarities	Belongs to the multicopper oxidase family. Contains 3 F5/8 type A domains. Contains 2 F5/8 type C domains. Contains 6 plastocyanin-like domains.
Sequence caution	The sequence ABD23003.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI23065.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Blood coagulation Hemostasis
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Disease	Disease mutation Thrombophilia
Domain	Repeat Signal
Ligand	Calcium Copper Metal-binding
PTM	Disulfide bond Glycoprotein Phosphoprotein Sulfation Zymogen
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	blood circulation Inferred from electronic annotation. Source: Compara cell adhesion Inferred from electronic annotation. Source: InterPro platelet activation Traceable author statement. Source: Reactome platelet degranulation Traceable author statement. Source: Reactome
Cellular_component	extracellular region Non-traceable author statement PubMed 14718574. Source: UniProtKB extracellular space Inferred from electronic annotation. Source: Compara plasma membrane Traceable author statement. Source: Reactome platelet alpha granule lumen Traceable author statement. Source: Reactome
Molecular_function	copper ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 28

28

Chain

29 – 2224

2196

Coagulation factor V

PRO_0000002978

Chain

29 – 737

709

Coagulation factor V heavy chain

PRO_0000002979

Propeptide

738 – 1573

836

Activation peptide (connecting region)

PRO_0000002980

Chain

1574 – 2224

651

Coagulation factor V light chain

PRO_0000002981

Regions

Domain

30 – 329

300

F5/8 type A 1

Domain

30 – 193

164

Plastocyanin-like 1

Domain

203 – 329

127

Plastocyanin-like 2

Domain

348 – 684

337

F5/8 type A 2

Domain

348 – 526

179

Plastocyanin-like 3

Domain

536 – 684

149

Plastocyanin-like 4

Repeat

895 – 911

17

1-1

Repeat

912 – 928

17

1-2

Repeat

1185 – 1193

9

2-1

Repeat

1194 – 1202

9

2-2

Repeat

1203 – 1211

9

2-3

Repeat

1212 – 1220

9

2-4

Repeat

1221 – 1229

9

2-5

Repeat

1230 – 1238

9

2-6

Repeat

1239 – 1247

9

2-7

Repeat

1248 – 1256

9

2-8

Repeat

1257 – 1265

9

2-9

Repeat

1266 – 1274

9

2-10

Repeat

1275 – 1283

9

2-11

Repeat

1284 – 1292

9

2-12

Repeat

1293 – 1301

9

2-13

Repeat

1302 – 1310

9

2-14

Repeat

1311 – 1319

9

2-15

Repeat

1320 – 1328

9

2-16

Repeat

1329 – 1337

9

2-17

Repeat

1338 – 1346

9

2-18

Repeat

1347 – 1355

9

2-19

Repeat

1356 – 1364

9

2-20

Repeat

1365 – 1373

9

2-21

Repeat

1374 – 1382

9

2-22

Repeat

1383 – 1391

9

2-23

Repeat

1392 – 1400

9

2-24

Repeat

1401 – 1409

9

2-25

Repeat

1410 – 1418

9

2-26

Repeat

1419 – 1427

9

2-27

Repeat

1428 – 1436

9

2-28

Repeat

1437 – 1445

9

2-29

Repeat

1446 – 1454

9

2-30

Repeat

1455 – 1463

9

2-31

Repeat

1464 – 1472

9

2-32

Repeat

1473 – 1481

9

2-33

Repeat

1482 – 1490

9

2-34

Repeat

1493 – 1501

9

2-35

Domain

1578 – 1907

330

F5/8 type A 3

Domain

1578 – 1751

174

Plastocyanin-like 5

Domain

1761 – 1907

147

Plastocyanin-like 6

Domain

1907 – 2061

155

F5/8 type C 1

Domain

2066 – 2221

156

F5/8 type C 2

Region

692 – 1573

882

B

Region

895 – 928

34

2 X 17 AA tandem repeats

Region

1185 – 1501

317

35 X 9 AA approximate tandem repeats of [TNP]-L-S-P-D-L-S-Q-T

Sites

Metal binding

139

1

Calcium By similarity

Metal binding

140

1

Calcium By similarity

Metal binding

1843

1

Copper By similarity

Metal binding

1845

1

Copper By similarity

Site

334 – 335

2

Cleavage; by activated protein C

Site

534 – 535

2

Cleavage; by activated protein C

Site

707 – 708

2

Cleavage; by activated protein C

Site

737 – 738

2

Cleavage; by thrombin

Site

1022 – 1023

2

Cleavage; by activated protein C

Site

1046 – 1047

2

Cleavage; by thrombin

Site

1573 – 1574

2

Cleavage; by thrombin

Amino acid modifications

Modified residue

640

1

Phosphothreonine Ref.24

Modified residue

693

1

Sulfotyrosine Potential

Modified residue

724

1

Sulfotyrosine Potential

Modified residue

726

1

Sulfotyrosine Potential

Modified residue

1522

1

Sulfotyrosine Potential

Modified residue

1538

1

Sulfotyrosine Potential

Modified residue

1543

1

Sulfotyrosine Potential

Modified residue

1593

1

Sulfotyrosine Potential

Glycosylation

51

1

N-linked (GlcNAc...) Potential

Glycosylation

55

1

N-linked (GlcNAc...) Potential

Glycosylation

239

1

N-linked (GlcNAc...) Potential

Glycosylation

297

1

N-linked (GlcNAc...) Ref.21 Ref.22

Glycosylation

382

1

N-linked (GlcNAc...) Potential

Glycosylation

460

1

N-linked (GlcNAc...) Ref.21

Glycosylation

468

1

N-linked (GlcNAc...) Potential

Glycosylation

554

1

N-linked (GlcNAc...) Potential

Glycosylation

741

1

N-linked (GlcNAc...) Potential

Glycosylation

752

1

N-linked (GlcNAc...) Potential

Glycosylation

760

1

N-linked (GlcNAc...) Potential

Glycosylation

776

1

N-linked (GlcNAc...) Potential

Glycosylation

782

1

N-linked (GlcNAc...) Potential

Glycosylation

821

1

N-linked (GlcNAc...) Ref.21

Glycosylation

938

1

N-linked (GlcNAc...) Potential

Glycosylation

977

1

N-linked (GlcNAc...) Ref.21

Glycosylation

1074

1

N-linked (GlcNAc...) Potential

Glycosylation

1083

1

N-linked (GlcNAc...) Potential

Glycosylation

1103

1

N-linked (GlcNAc...) Potential

Glycosylation

1106

1

N-linked (GlcNAc...) Potential

Glycosylation

1479

1

N-linked (GlcNAc...) Potential

Glycosylation

1499

1

N-linked (GlcNAc...) Potential

Glycosylation

1559

1

N-linked (GlcNAc...) Ref.21

Glycosylation

1703

1

N-linked (GlcNAc...) Potential

Glycosylation

2010

1

N-linked (GlcNAc...) Potential

Glycosylation

2209

1

N-linked (GlcNAc...) Potential

Disulfide bond

167 ↔ 193

By similarity

Disulfide bond

248 ↔ 329

By similarity

Disulfide bond

500 ↔ 526

By similarity

Disulfide bond

603 ↔ 684

By similarity

Disulfide bond

1725 ↔ 1751

Probable

Disulfide bond

1907 ↔ 2061

By similarity

Disulfide bond

2066 ↔ 2221

By similarity

Natural variations

Natural variant

15

1

G → S. Ref.3
Corresponds to variant rs9332485 [ dbSNP | Ensembl ].

VAR_021297

Natural variant

107

1

D → H. Ref.3 Ref.33
Corresponds to variant rs6019 [ dbSNP | Ensembl ].

VAR_013886

Natural variant

334

1

R → G in Hong Kong; does not predispose to clinical thrombosis. Ref.30 Ref.32

VAR_013620

Natural variant

334

1

R → T in THPH2; Cambridge. Ref.31

VAR_013621

Natural variant

387

1

I → T in THPH2; Liverpool; mutant protein is expressed with an additional carbohydrate chain. Ref.39 Ref.41

VAR_032698

Natural variant

413

1

M → T. Ref.3 Ref.33
Corresponds to variant rs6033 [ dbSNP | Ensembl ].

VAR_013887

Natural variant

513

1

R → K. Ref.3 Ref.5 Ref.30 Ref.33
Corresponds to variant rs6020 [ dbSNP | Ensembl ].

VAR_013622

Natural variant

534

1

R → Q in Leiden; associated with thrombophilia; associated with susceptibility to Budd-Chiari syndrome; associated with susceptibility to ischemic stroke. Ref.3 Ref.4 Ref.27 Ref.29 Ref.33 Ref.35 Ref.40
Corresponds to variant rs6025 [ dbSNP | Ensembl ].

VAR_001213

Natural variant

613

1

C → R in THPH2; Nijkerk. Ref.36

VAR_032699

Natural variant

775

1

S → A in a colorectal cancer sample; somatic mutation. Ref.42

VAR_035817

Natural variant

781

1

S → R.
Corresponds to variant rs13306350 [ dbSNP | Ensembl ].

VAR_047740

Natural variant

809

1

P → S. Ref.3 Ref.33
Corresponds to variant rs6031 [ dbSNP | Ensembl ].

VAR_013888

Natural variant

817

1

N → T. Ref.3 Ref.33
Corresponds to variant rs6018 [ dbSNP | Ensembl ].

VAR_013889

Natural variant

858

1

K → R. Ref.1 Ref.3 Ref.6 Ref.8 Ref.33
Corresponds to variant rs4524 [ dbSNP | Ensembl ].

VAR_001214

Natural variant

865

1

H → R. Ref.1 Ref.3 Ref.6 Ref.8 Ref.33
Corresponds to variant rs4525 [ dbSNP | Ensembl ].

VAR_001215

Natural variant

915

1

T → S. Ref.3
Corresponds to variant rs9332695 [ dbSNP | Ensembl ].

VAR_021298

Natural variant

925

1

K → E. Ref.1 Ref.3 Ref.6 Ref.8 Ref.33
Corresponds to variant rs6032 [ dbSNP | Ensembl ].

VAR_013890

Natural variant

969

1

N → S. Ref.3
Corresponds to variant rs9332604 [ dbSNP | Ensembl ].

VAR_021299

Natural variant

980

1

R → L. Ref.3
Corresponds to variant rs9332605 [ dbSNP | Ensembl ].

VAR_021300

Natural variant

1146

1

H → Q. Ref.3 Ref.33
Corresponds to variant rs6005 [ dbSNP | Ensembl ].

VAR_013891

Natural variant

1285

1

L → I. Ref.3 Ref.6 Ref.28
Corresponds to variant rs1046712 [ dbSNP | Ensembl ].

VAR_013892

Natural variant

1327

1

H → R. Ref.28 Ref.35
Corresponds to variant rs1800595 [ dbSNP | Ensembl ].

VAR_013893

Natural variant

1397

1

L → F. Ref.1 Ref.8
Corresponds to variant rs13306334 [ dbSNP | Ensembl ].

VAR_047741

Natural variant

1404

1

P → S. Ref.3
Corresponds to variant rs9332608 [ dbSNP | Ensembl ].

VAR_021301

Natural variant

1530

1

E → A. Ref.3 Ref.33
Corresponds to variant rs6007 [ dbSNP | Ensembl ].

VAR_013894

Natural variant

1685

1

T → S. Ref.33
Corresponds to variant rs6011 [ dbSNP | Ensembl ].

VAR_013895

Natural variant

1730

1

Y → C in FA5D; Seoul 2. Ref.35 Ref.36

VAR_032700

Natural variant

1749

1

L → V. Ref.33
Corresponds to variant rs6034 [ dbSNP | Ensembl ].

VAR_013896

Natural variant

1764

1

M → V. Ref.1 Ref.26 Ref.33
Corresponds to variant rs6030 [ dbSNP | Ensembl ].

VAR_013897

Natural variant

1820

1

M → I. Ref.33
Corresponds to variant rs6026 [ dbSNP | Ensembl ].

VAR_013898

Natural variant

2102

1

R → C in FA5D; impairs both factor V secretion and activity. Ref.38

VAR_032701

Natural variant

2102

1

R → H in THPH2. Ref.37

VAR_017329

Natural variant

2148

1

M → T. Ref.3
Corresponds to variant rs9332701 [ dbSNP | Ensembl ].

VAR_021302

Natural variant

2185

1

K → R.
Corresponds to variant rs6679078 [ dbSNP | Ensembl ].

VAR_034603

Natural variant

2222

1

D → G. Ref.33
Corresponds to variant rs6027 [ dbSNP | Ensembl ].

VAR_013899

Experimental info

Sequence conflict

741

1

N → S in ABD23003. Ref.7

Sequence conflict

908

1

E → K in AAA52424. Ref.1

Sequence conflict

908

1

E → K in CAC82573. Ref.8

Sequence conflict

991

1

K → E in BAF84302. Ref.5

Sequence conflict

2213

1

A → T in AAA52424. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

2224

Helix Strand Turn

Details...

Turn

1569 – 1571

3

Turn

2072 – 2074

3

Beta strand

2075 – 2077

3

Helix

2079 – 2081

3

Beta strand

2082 – 2085

4

Beta strand

2093 – 2095

3

Helix

2098 – 2100

3

Beta strand

2107 – 2109

3

Beta strand

2111 – 2113

3

Beta strand

2123 – 2139

17

Beta strand

2141 – 2143

3

Beta strand

2146 – 2163

18

Beta strand

2182 – 2185

4

Beta strand

2188 – 2211

24

Beta strand

2213 – 2222

10

Sequences

	Sequence		Length	Mass (Da)
	P12259 [UniParc]. Last modified October 5, 2010. Version 4. Checksum: 24AEF3FEA7332E37	FASTA	2,224	251,703
	10 20 30 40 50 60 MFPGCPRLWV LVVLGTSWVG WGSQGTEAAQ LRQFYVAAQG ISWSYRPEPT NSSLNLSVTS 70 80 90 100 110 120 FKKIVYREYE PYFKKEKPQS TISGLLGPTL YAEVGDIIKV HFKNKADKPL SIHPQGIRYS 130 140 150 160 170 180 KLSEGASYLD HTFPAEKMDD AVAPGREYTY EWSISEDSGP THDDPPCLTH IYYSHENLIE 190 200 210 220 230 240 DFNSGLIGPL LICKKGTLTE GGTQKTFDKQ IVLLFAVFDE SKSWSQSSSL MYTVNGYVNG 250 260 270 280 290 300 TMPDITVCAH DHISWHLLGM SSGPELFSIH FNGQVLEQNH HKVSAITLVS ATSTTANMTV 310 320 330 340 350 360 GPEGKWIISS LTPKHLQAGM QAYIDIKNCP KKTRNLKKIT REQRRHMKRW EYFIAAEEVI 370 380 390 400 410 420 WDYAPVIPAN MDKKYRSQHL DNFSNQIGKH YKKVMYTQYE DESFTKHTVN PNMKEDGILG 430 440 450 460 470 480 PIIRAQVRDT LKIVFKNMAS RPYSIYPHGV TFSPYEDEVN SSFTSGRNNT MIRAVQPGET 490 500 510 520 530 540 YTYKWNILEF DEPTENDAQC LTRPYYSDVD IMRDIASGLI GLLLICKSRS LDRRGIQRAA 550 560 570 580 590 600 DIEQQAVFAV FDENKSWYLE DNINKFCENP DEVKRDDPKF YESNIMSTIN GYVPESITTL 610 620 630 640 650 660 GFCFDDTVQW HFCSVGTQNE ILTIHFTGHS FIYGKRHEDT LTLFPMRGES VTVTMDNVGT 670 680 690 700 710 720 WMLTSMNSSP RSKKLRLKFR DVKCIPDDDE DSYEIFEPPE STVMATRKMH DRLEPEDEES 730 740 750 760 770 780 DADYDYQNRL AAALGIRSFR NSSLNQEEEE FNLTALALEN GTEFVSSNTD IIVGSNYSSP 790 800 810 820 830 840 SNISKFTVNN LAEPQKAPSH QQATTAGSPL RHLIGKNSVL NSSTAEHSSP YSEDPIEDPL 850 860 870 880 890 900 QPDVTGIRLL SLGAGEFKSQ EHAKHKGPKV ERDQAAKHRF SWMKLLAHKV GRHLSQDTGS 910 920 930 940 950 960 PSGMRPWEDL PSQDTGSPSR MRPWKDPPSD LLLLKQSNSS KILVGRWHLA SEKGSYEIIQ 970 980 990 1000 1010 1020 DTDEDTAVNN WLISPQNASR AWGESTPLAN KPGKQSGHPK FPRVRHKSLQ VRQDGGKSRL 1030 1040 1050 1060 1070 1080 KKSQFLIKTR KKKKEKHTHH APLSPRTFHP LRSEAYNTFS ERRLKHSLVL HKSNETSLPT 1090 1100 1110 1120 1130 1140 DLNQTLPSMD FGWIASLPDH NQNSSNDTGQ ASCPPGLYQT VPPEEHYQTF PIQDPDQMHS 1150 1160 1170 1180 1190 1200 TSDPSHRSSS PELSEMLEYD RSHKSFPTDI SQMSPSSEHE VWQTVISPDL SQVTLSPELS 1210 1220 1230 1240 1250 1260 QTNLSPDLSH TTLSPELIQR NLSPALGQMP ISPDLSHTTL SPDLSHTTLS LDLSQTNLSP 1270 1280 1290 1300 1310 1320 ELSQTNLSPA LGQMPLSPDL SHTTLSLDFS QTNLSPELSH MTLSPELSQT NLSPALGQMP 1330 1340 1350 1360 1370 1380 ISPDLSHTTL SLDFSQTNLS PELSQTNLSP ALGQMPLSPD PSHTTLSLDL SQTNLSPELS 1390 1400 1410 1420 1430 1440 QTNLSPDLSE MPLFADLSQI PLTPDLDQMT LSPDLGETDL SPNFGQMSLS PDLSQVTLSP 1450 1460 1470 1480 1490 1500 DISDTTLLPD LSQISPPPDL DQIFYPSESS QSLLLQEFNE SFPYPDLGQM PSPSSPTLND 1510 1520 1530 1540 1550 1560 TFLSKEFNPL VIVGLSKDGT DYIEIIPKEE VQSSEDDYAE IDYVPYDDPY KTDVRTNINS 1570 1580 1590 1600 1610 1620 SRDPDNIAAW YLRSNNGNRR NYYIAAEEIS WDYSEFVQRE TDIEDSDDIP EDTTYKKVVF 1630 1640 1650 1660 1670 1680 RKYLDSTFTK RDPRGEYEEH LGILGPIIRA EVDDVIQVRF KNLASRPYSL HAHGLSYEKS 1690 1700 1710 1720 1730 1740 SEGKTYEDDS PEWFKEDNAV QPNSSYTYVW HATERSGPES PGSACRAWAY YSAVNPEKDI 1750 1760 1770 1780 1790 1800 HSGLIGPLLI CQKGILHKDS NMPMDMREFV LLFMTFDEKK SWYYEKKSRS SWRLTSSEMK 1810 1820 1830 1840 1850 1860 KSHEFHAING MIYSLPGLKM YEQEWVRLHL LNIGGSQDIH VVHFHGQTLL ENGNKQHQLG 1870 1880 1890 1900 1910 1920 VWPLLPGSFK TLEMKASKPG WWLLNTEVGE NQRAGMQTPF LIMDRDCRMP MGLSTGIISD 1930 1940 1950 1960 1970 1980 SQIKASEFLG YWEPRLARLN NGGSYNAWSV EKLAAEFASK PWIQVDMQKE VIITGIQTQG 1990 2000 2010 2020 2030 2040 AKHYLKSCYT TEFYVAYSSN QINWQIFKGN STRNVMYFNG NSDASTIKEN QFDPPIVARY 2050 2060 2070 2080 2090 2100 IRISPTRAYN RPTLRLELQG CEVNGCSTPL GMENGKIENK QITASSFKKS WWGDYWEPFR 2110 2120 2130 2140 2150 2160 ARLNAQGRVN AWQAKANNNK QWLEIDLLKI KKITAIITQG CKSLSSEMYV KSYTIHYSEQ 2170 2180 2190 2200 2210 2220 GVEWKPYRLK SSMVDKIFEG NTNTKGHVKN FFNPPIISRF IRVIPKTWNQ SIALRLELFG CDIY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete cDNA and derived amino acid sequence of human factor V." Jenny R.J., Pittman D.D., Toole J.J., Kriz R.W., Aldape R.A., Hewick R.M., Kaufman R.J., Mann K.G. Proc. Natl. Acad. Sci. U.S.A. 84:4846-4850(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ARG-858; ARG-865; GLU-925; PHE-1397 AND VAL-1764.
[2]	"Structure of the gene for human coagulation factor V." Cripe L.D., Moore K.D., Kane W.H. Biochemistry 31:3777-3785(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	SeattleSNPs variation discovery resource Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEIDEN GLN-534, VARIANTS SER-15; HIS-107; THR-413; LYS-513; SER-809; THR-817; ARG-858; ARG-865; SER-915; GLU-925; SER-969; LEU-980; GLN-1146; ILE-1285; SER-1404; ALA-1530 AND THR-2148.
[4]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LEIDEN GLN-534.
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1030, VARIANT LYS-513. Tissue: Placenta.
[6]	"Cloning of cDNAs coding for the heavy chain region and connecting region of human factor V, a blood coagulation factor with four types of internal repeats." Kane W.H., Ichinose A., Hagen F.S., Davie E.W. Biochemistry 26:6508-6514(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1600, VARIANTS ARG-858; ARG-865; GLU-925 AND ILE-1285.
[7]	"Human coagulation factor V, exon 13, missense mutation Asn713Ser." Kostka H. Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 658-1598.
[8]	"Studies on hereditary deficiency of coagulation factor V." Xie F., Cheng F., Zhu X. Zhonghua Xue Ye Xue Za Zhi 22:453-456(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 660-1598, VARIANTS ARG-858; ARG-865; GLU-925 AND PHE-1397.
[9]	"Cloning of a cDNA coding for human factor V, a blood coagulation factor homologous to factor VIII and ceruloplasmin." Kane W.H., Davie E.W. Proc. Natl. Acad. Sci. U.S.A. 83:6800-6804(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1188-1215 AND 1315-2224.
[10]	"The serine protease cofactor factor V is synthesized by lymphocytes." Shen N.L.L., Fan S.-T., Pyati J., Graff R., Lapolla R.J., Edgington T.S. J. Immunol. 150:2992-3001(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fibroblast.
[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]	"Coagulation Factor V contains copper ion." Mann K.G., Lawler C.M., Vehar G.A., Church W.R. J. Biol. Chem. 259:12949-12951(1984) [PubMed] [Europe PMC] [Abstract] Cited for: COPPER-BINDING.
[13]	"Inactivation of human plasma kallikrein and factor XIa by protein C inhibitor." Meijers J.C., Kanters D.H., Vlooswijk R.A., van Erp H.E., Hessing M., Bouma B.N. Biochemistry 27:4231-4237(1988) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION, HETERODIMER WITH SERPINA5.
[14]	"Posttranslational sulfation of factor V is required for efficient thrombin cleavage and activation and for full procoagulant activity." Pittman D.D., Tomkinson K.N., Michnick D., Selighsohn U., Kaufman R.J. Biochemistry 33:6952-6959(1994) [PubMed] [Europe PMC] [Abstract] Cited for: SULFATION.
[15]	"Sulfation of tyrosine residues in coagulation factor V." Hortin G.L. Blood 76:946-952(1990) [PubMed] [Europe PMC] [Abstract] Cited for: SULFATION.
[16]	"The mechanism of inactivation of human factor V and human factor Va by activated protein C." Kalafatis M., Rand M.D., Mann K.G. J. Biol. Chem. 269:31869-31880(1994) [PubMed] [Europe PMC] [Abstract] Cited for: CLEAVAGE AT ARG-334; ARG-534; ARG-707 AND LYS-1022 BY ACTIVATED PROTEIN C.
[17]	"Characterization of semenogelin II and its molecular interaction with prostate-specific antigen and protein C inhibitor." Kise H., Nishioka J., Kawamura J., Suzuki K. Eur. J. Biochem. 238:88-96(1996) [PubMed] [Europe PMC] [Abstract] Cited for: HETERODIMER WITH SERPINA5.
[18]	"Protein C inhibitor secreted from activated platelets efficiently inhibits activated protein C on phosphatidylethanolamine of platelet membrane and microvesicles." Nishioka J., Ning M., Hayashi T., Suzuki K. J. Biol. Chem. 273:11281-11287(1998) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION, HETERODIMER WITH SERPINA5.
[19]	"Mutations in coagulation factors in women with unexplained late fetal loss." Martinelli I., Taioli E., Cetin I., Marinoni A., Gerosa S., Villa M.V., Bozzo M., Mannucci P.M. N. Engl. J. Med. 343:1015-1018(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN RPRGL1 SUSCEPTIBILITY.
[20]	"Characterization of a novel human protein C inhibitor (PCI) gene transgenic mouse useful for studying the role of PCI in physiological and pathological conditions." Hayashi T., Nishioka J., Kamada H., Asanuma K., Kondo H., Gabazza E.C., Ido M., Suzuki K. J. Thromb. Haemost. 2:949-961(2004) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION, HETERODIMER WITH SERPINA5.
[21]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-297; ASN-460; ASN-821; ASN-977 AND ASN-1559, MASS SPECTROMETRY. Tissue: Plasma.
[22]	"Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach." Lewandrowski U., Moebius J., Walter U., Sickmann A. Mol. Cell. Proteomics 5:226-233(2006) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-297, MASS SPECTROMETRY. Tissue: Platelet.
[23]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Platelet.
[24]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-640, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[25]	"Crystal structures of the membrane-binding C2 domain of human coagulation factor V." Macedo-Ribeiro S., Bode W., Huber R., Quinn-Allen M.A., Kim S.W., Ortel T.L., Bourenkov G.P., Bartunik H.D., Stubbs M.T., Kane W.H., Fuentes-Prior P. Nature 402:434-439(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2065-2224.
[26]	"A polymorphism in the human coagulation factor V gene." Bayston T.A., Ireland H., Olds R.J., Thein S.L., Lane D.A. Hum. Mol. Genet. 3:2085-2085(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT VAL-1764.
[27]	"Mutation in blood coagulation factor V associated with resistance to activated protein C." Bertina R.M., Koeleman B.P.C., Koster T., Rosendaal F.R., Dirven R.J., de Ronde H., van der Velden P.A., Reitsma P.H. Nature 369:64-67(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT LEIDEN GLN-534.
[28]	"Detection of new polymorphic markers in the factor V gene: association with factor V levels in plasma." Lunghi B., Iacoviello L., Gemmati D., Dilasio M.G., Castoldi E., Pinotti M., Castaman G., Redaelli R., Mariani G., Marchetti G., Bernardi F. Thromb. Haemost. 75:45-48(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ILE-1285 AND ARG-1327.
[29]	"Prevalence of the factor V Leiden mutation in hepatic and portal vein thrombosis." Mahmoud A.E.A., Elias E., Beauchamp N., Wilde J.T. Gut 40:798-800(1997) [PubMed] [Europe PMC] [Abstract] Cited for: ASSOCIATION OF VARIANT LEIDEN GLN-534 WITH SUSCEPTIBILITY TO BUDD-CHIARI SYNDROME.
[30]	"A novel mutation of Arg306 of factor V gene in Hong Kong Chinese." Chan W.P., Lee C.K., Kwong Y.L., Lam C.K., Liang R. Blood 91:1135-1139(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HONG KONG GLY-334, VARIANT LYS-513.
[31]	"Factor V Cambridge: a new mutation (Arg306-to-Thr) associated with resistance to activated protein C." Williamson D., Brown K., Luddington R., Baglin C., Baglin T. Blood 91:1140-1144(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT THPH2 THR-334.
[32]	"Clinical significance of Arg306 mutations of factor V gene." Liang R., Lee C.K., Wat M.S., Kwong Y.L., Lam C.K., Liu H.W. Blood 92:2599-2600(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HONG KONG GLY-334.
[33]	"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: VARIANT LEIDEN GLN-534, VARIANTS HIS-107; THR-413; LYS-513; SER-809; THR-817; ARG-858; ARG-865; GLU-925; GLN-1146; ALA-1530; SER-1685; VAL-1749; VAL-1764; ILE-1820 AND GLY-2222.
[34]	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)
[35]	"Combinations of 4 mutations (FV R506Q, FV H1299R, FV Y1702C, PT 20210G/A) affecting the prothrombinase complex in a thrombophilic family." Castoldi E., Simioni P., Kalafatis M., Lunghi B., Tormene D., Girelli D., Girolami A., Bernardi F. Blood 96:1443-1448(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FA5D CYS-1730, VARIANT LEIDEN GLN-534, VARIANT ARG-1327.
[36]	"Five novel mutations in the gene for human blood coagulation factor V associated with type I factor V deficiency." van Wijk R., Nieuwenhuis K., van den Berg M., Huizinga E.G., van der Meijden B.B., Kraaijenhagen R.J., van Solinge W.W. Blood 98:358-367(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS THPH2 ARG-613 AND CYS-1730.
[37]	"Novel factor V C2-domain mutation (R2074H) in two families with factor V deficiency and bleeding." Schrijver I., Houissa-Kastally R., Jones C.D., Garcia K.C., Zehnder J.L. Thromb. Haemost. 87:294-299(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT THPH2 HIS-2102.
[38]	"Arg2074Cys missense mutation in the C2 domain of factor V causing moderately severe factor V deficiency: molecular characterization by expression of the recombinant protein." Duga S., Montefusco M.C., Asselta R., Malcovati M., Peyvandi F., Santagostino E., Mannucci P.M., Tenchini M.L. Blood 101:173-177(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FA5D CYS-2102, CHARACTERIZATION OF VARIANT FA5D CYS-2102.
[39]	"Factor V I359T: a novel mutation associated with thrombosis and resistance to activated protein C." Mumford A.D., McVey J.H., Morse C.V., Gomez K., Steen M., Norstrom E.A., Tuddenham E.G.D., Dahlback B., Bolton-Maggs P.H.B. Br. J. Haematol. 123:496-501(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT THPH2 THR-387.
[40]	"Meta-analysis of genetic studies in ischemic stroke: thirty-two genes involving approximately 18,000 cases and 58,000 controls." Casas J.P., Hingorani A.D., Bautista L.E., Sharma P. Arch. Neurol. 61:1652-1661(2004) [PubMed] [Europe PMC] [Abstract] Cited for: ASSOCIATION OF VARIANT GLN-534 WITH SUSCEPTIBILITY TO ISCHSTR.
[41]	"Functional characterization of factor V-Ile359Thr: a novel mutation associated with thrombosis." Steen M., Norstroem E.A., Tholander A.-L., Bolton-Maggs P.H.B., Mumford A., McVey J.H., Tuddenham E.G.D., Dahlbaeck B. Blood 103:3381-3387(2004) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANT THPH2 THR-387.
[42]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-775.
+	Additional computationally mapped references.

Web resources

Wikipedia

Factor V entry

GeneReviews

SeattleSNPs

SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M16967 mRNA. Translation: AAA52424.1.
L32779 , L32755, L32756, L32757, L32758, L32759, L32760, L32761, L32762, L32763, L32764, L32765, L32766, L32767, L32768, L32769, L32770, L32771, L32772, L32773, L32774, L32775, L32776, L32777, L32778 Genomic DNA. Translation: AAB59401.1.
AY364535 Genomic DNA. Translation: AAQ55063.1.
Z99572 Genomic DNA. Translation: CAB16748.1.
Z99572 Genomic DNA. Translation: CAI23065.1. Sequence problems.
AK291613 mRNA. Translation: BAF84302.1.
M14335 mRNA. Translation: AAB59532.1.
DQ377944 Genomic DNA. Translation: ABD23003.1. Sequence problems.
AJ297255 mRNA. Translation: CAC82573.1.

IPI

IPI00478809.

PIR

KFHU5. A56172.

RefSeq

NP_000121.2. NM_000130.4.

UniGene

Hs.30054.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CZS	X-ray	1.90	A	2065-2224	[»]
1CZT	X-ray	1.87	A	2065-2224	[»]
1CZV	X-ray	2.40	A/B	2065-2224	[»]
1FV4	model	-	H	29-691	[»]
			L	1574-2224	[»]
1Y61	model	-	H	29-737	[»]
			L	1574-2224	[»]
3P6Z	X-ray	1.70	C/I	685-737	[»]
3P70	X-ray	2.55	M/N/O/P	685-737	[»]
3S9C	X-ray	1.80	B	1561-1574	[»]

ProteinModelPortal

P12259.

SMR

P12259. Positions 32-684, 1575-2224.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-47331N.

STRING

9606.ENSP00000356771.

PTM databases

PhosphoSite

P12259.

Polymorphism databases

DMDM

308153653.

Proteomic databases

PaxDb

P12259.

PRIDE

P12259.

Protocols and materials databases

DNASU

2153.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000367796; ENSP00000356770; ENSG00000198734.
ENST00000367797; ENSP00000356771; ENSG00000198734.

GeneID

2153.

KEGG

hsa:2153.

UCSC

uc001ggg.1. human.

Organism-specific databases

CTD

2153.

GeneCards

GC01M169481.

HGNC

HGNC:3542. F5.

HPA

HPA002036.

MIM

188055. phenotype.
227400. phenotype.
600880. phenotype.
601367. phenotype.
612309. gene.
614389. phenotype.

neXtProt

NX_P12259.

Orphanet

131. Budd-Chiari syndrome.
326. Congenital factor V deficiency.
64738. Non rare thrombophilia.

PharmGKB

PA159.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG240444.

HOVERGEN

HBG005631.

KO

K03902.

OrthoDB

EOG41RPT3.

Enzyme and pathway databases

Reactome

REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P12259.

Bgee

P12259.

CleanEx

HS_F5.

Genevestigator

P12259.

GermOnline

ENSG00000198734. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.420. 6 hits.

InterPro

IPR000421. Coagulation_fac_5/8-C_type_dom.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
IPR024715. Factor_5/8.
IPR008979. Galactose-bd-like.
[Graphical view]

Pfam

PF07732. Cu-oxidase_3. 2 hits.
PF00754. F5_F8_type_C. 2 hits.
[Graphical view]

PIRSF

PIRSF000354. Factors_V_VIII. 1 hit.

SMART

SM00231. FA58C. 2 hits.
[Graphical view]

SUPFAM

SSF49503. Cupredoxin. 6 hits.
SSF49785. Gal_bind_like. 2 hits.

PROSITE

PS01285. FA58C_1. 2 hits.
PS01286. FA58C_2. 2 hits.
PS50022. FA58C_3. 2 hits.
PS00079. MULTICOPPER_OXIDASE1. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P12259.

ChEMBL

CHEMBL3618.

DrugBank

DB00055. Drotrecogin alfa.

EvolutionaryTrace

P12259.

GenomeRNAi

2153.

NextBio

8701.

SOURCE

Search...

Entry information

Entry name

FA5_HUMAN

Accession

Primary (citable) accession number: P12259
Secondary accession number(s): A8K6E8 , Q14285, Q2EHR5, Q5R346, Q5R347, Q6UPU6, Q8WWQ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 5, 2010
Last modified:	May 1, 2013
This is version 167 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.