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P12259

- FA5_HUMAN

UniProt

P12259 - FA5_HUMAN

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Protein
Coagulation factor V
Gene
F5
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 regulationi

Inhibited by SERPINA5.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi139 – 1391Calcium By similarity
Metal bindingi140 – 1401Calcium By similarity
Sitei334 – 3352Cleavage; by activated protein C
Sitei534 – 5352Cleavage; by activated protein C
Sitei707 – 7082Cleavage; by activated protein C
Sitei737 – 7382Cleavage; by thrombin
Sitei1022 – 10232Cleavage; by activated protein C
Sitei1046 – 10472Cleavage; by thrombin
Sitei1573 – 15742Cleavage; by thrombin
Metal bindingi1843 – 18431Copper By similarity
Metal bindingi1845 – 18451Copper By similarity

GO - Molecular functioni

  1. copper ion binding Source: InterPro
  2. protein binding Source: UniProtKB
  3. serine-type endopeptidase activity Source: Ensembl

GO - Biological processi

  1. blood circulation Source: Ensembl
  2. blood coagulation Source: Reactome
  3. cell adhesion Source: InterPro
  4. platelet activation Source: Reactome
  5. platelet degranulation Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium, Copper, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_1439. Common Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Coagulation factor V
Alternative name(s):
Activated protein C cofactor
Proaccelerin, labile factor
Cleaved into the following 2 chains:
Gene namesi
Name:F5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:3542. F5.

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
  2. extracellular space Source: Ensembl
  3. plasma membrane Source: Reactome
  4. platelet alpha granule lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

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.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1730 – 17301Y → C in FA5D; Seoul 2. 2 Publications
VAR_032700
Natural varianti2102 – 21021R → C in FA5D; impairs both factor V secretion and activity. 1 Publication
VAR_032701
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.5 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti334 – 3341R → T in THPH2; Cambridge. 1 Publication
Corresponds to variant rs118203906 [ dbSNP | Ensembl ].
VAR_013621
Natural varianti387 – 3871I → T in THPH2; Liverpool; mutant protein is expressed with an additional carbohydrate chain. 2 Publications
VAR_032698
Natural varianti613 – 6131C → R in THPH2; Nijkerk. 1 Publication
VAR_032699
Natural varianti2102 – 21021R → H in THPH2. 1 Publication
VAR_017329
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.1 Publication
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.1 Publication

Keywords - Diseasei

Disease mutation, Thrombophilia

Organism-specific databases

MIMi188055. phenotype.
227400. phenotype.
600880. phenotype.
601367. phenotype.
614389. phenotype.
Orphaneti131. Budd-Chiari syndrome.
329217. Cerebral sinovenous thrombosis.
326. Congenital factor V deficiency.
391320. East Texas bleeding disorder.
64738. Non rare thrombophilia.
PharmGKBiPA159.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828
Add
BLAST
Chaini29 – 22242196Coagulation factor V
PRO_0000002978Add
BLAST
Chaini29 – 737709Coagulation factor V heavy chain
PRO_0000002979Add
BLAST
Propeptidei738 – 1573836Activation peptide (connecting region)
PRO_0000002980Add
BLAST
Chaini1574 – 2224651Coagulation factor V light chain
PRO_0000002981Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi51 – 511N-linked (GlcNAc...) Reviewed prediction
Glycosylationi55 – 551N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi167 ↔ 193 By similarity
Glycosylationi239 – 2391N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi248 ↔ 329 By similarity
Glycosylationi297 – 2971N-linked (GlcNAc...)2 Publications
Glycosylationi382 – 3821N-linked (GlcNAc...) Reviewed prediction
Glycosylationi460 – 4601N-linked (GlcNAc...)1 Publication
Glycosylationi468 – 4681N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi500 ↔ 526 By similarity
Glycosylationi554 – 5541N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi603 ↔ 684 By similarity
Modified residuei640 – 6401Phosphothreonine1 Publication
Modified residuei693 – 6931Sulfotyrosine Reviewed prediction
Modified residuei724 – 7241Sulfotyrosine Reviewed prediction
Modified residuei726 – 7261Sulfotyrosine Reviewed prediction
Glycosylationi741 – 7411N-linked (GlcNAc...) Reviewed prediction
Glycosylationi752 – 7521N-linked (GlcNAc...) Reviewed prediction
Glycosylationi760 – 7601N-linked (GlcNAc...) Reviewed prediction
Glycosylationi776 – 7761N-linked (GlcNAc...) Reviewed prediction
Glycosylationi782 – 7821N-linked (GlcNAc...) Reviewed prediction
Glycosylationi821 – 8211N-linked (GlcNAc...)1 Publication
Glycosylationi938 – 9381N-linked (GlcNAc...) Reviewed prediction
Glycosylationi977 – 9771N-linked (GlcNAc...)1 Publication
Glycosylationi1074 – 10741N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1083 – 10831N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1103 – 11031N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1106 – 11061N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1479 – 14791N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1499 – 14991N-linked (GlcNAc...) Reviewed prediction
Modified residuei1522 – 15221Sulfotyrosine Reviewed prediction
Modified residuei1538 – 15381Sulfotyrosine Reviewed prediction
Modified residuei1543 – 15431Sulfotyrosine Reviewed prediction
Glycosylationi1559 – 15591N-linked (GlcNAc...)1 Publication
Modified residuei1593 – 15931Sulfotyrosine Reviewed prediction
Glycosylationi1703 – 17031N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1725 ↔ 1751 Inferred
Disulfide bondi1907 ↔ 2061 By similarity
Glycosylationi2010 – 20101N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2066 ↔ 2221 By similarity
Glycosylationi2209 – 22091N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

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.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation, Zymogen

Proteomic databases

MaxQBiP12259.
PaxDbiP12259.
PRIDEiP12259.

PTM databases

PhosphoSiteiP12259.

Expressioni

Tissue specificityi

Plasma.

Gene expression databases

ArrayExpressiP12259.
BgeeiP12259.
CleanExiHS_F5.
GenevestigatoriP12259.

Organism-specific databases

HPAiHPA002036.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

BioGridi108452. 6 interactions.
DIPiDIP-47331N.
STRINGi9606.ENSP00000356771.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni1569 – 15713
Turni2072 – 20743
Beta strandi2075 – 20773
Helixi2079 – 20813
Beta strandi2082 – 20854
Beta strandi2093 – 20953
Helixi2098 – 21003
Beta strandi2107 – 21093
Beta strandi2111 – 21133
Beta strandi2123 – 213917
Beta strandi2141 – 21433
Beta strandi2146 – 216318
Beta strandi2182 – 21854
Beta strandi2188 – 221124
Beta strandi2213 – 222210

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CZSX-ray1.90A2065-2224[»]
1CZTX-ray1.87A2065-2224[»]
1CZVX-ray2.40A/B2065-2224[»]
1FV4model-H29-691[»]
L1574-2224[»]
1Y61model-H29-737[»]
L1574-2224[»]
3P6ZX-ray1.70C/I685-737[»]
3P70X-ray2.55M/N/O/P685-737[»]
3S9CX-ray1.80B1561-1574[»]
ProteinModelPortaliP12259.
SMRiP12259. Positions 1575-2224.

Miscellaneous databases

EvolutionaryTraceiP12259.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 329300F5/8 type A 1
Add
BLAST
Domaini30 – 193164Plastocyanin-like 1
Add
BLAST
Domaini203 – 329127Plastocyanin-like 2
Add
BLAST
Domaini348 – 684337F5/8 type A 2
Add
BLAST
Domaini348 – 526179Plastocyanin-like 3
Add
BLAST
Domaini536 – 684149Plastocyanin-like 4
Add
BLAST
Repeati895 – 911171-1
Add
BLAST
Repeati912 – 928171-2
Add
BLAST
Repeati1185 – 119392-1
Repeati1194 – 120292-2
Repeati1203 – 121192-3
Repeati1212 – 122092-4
Repeati1221 – 122992-5
Repeati1230 – 123892-6
Repeati1239 – 124792-7
Repeati1248 – 125692-8
Repeati1257 – 126592-9
Repeati1266 – 127492-10
Repeati1275 – 128392-11
Repeati1284 – 129292-12
Repeati1293 – 130192-13
Repeati1302 – 131092-14
Repeati1311 – 131992-15
Repeati1320 – 132892-16
Repeati1329 – 133792-17
Repeati1338 – 134692-18
Repeati1347 – 135592-19
Repeati1356 – 136492-20
Repeati1365 – 137392-21
Repeati1374 – 138292-22
Repeati1383 – 139192-23
Repeati1392 – 140092-24
Repeati1401 – 140992-25
Repeati1410 – 141892-26
Repeati1419 – 142792-27
Repeati1428 – 143692-28
Repeati1437 – 144592-29
Repeati1446 – 145492-30
Repeati1455 – 146392-31
Repeati1464 – 147292-32
Repeati1473 – 148192-33
Repeati1482 – 149092-34
Repeati1493 – 150192-35
Domaini1578 – 1907330F5/8 type A 3
Add
BLAST
Domaini1578 – 1751174Plastocyanin-like 5
Add
BLAST
Domaini1761 – 1907147Plastocyanin-like 6
Add
BLAST
Domaini1907 – 2061155F5/8 type C 1
Add
BLAST
Domaini2066 – 2221156F5/8 type C 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni692 – 1573882B
Add
BLAST
Regioni895 – 928342 X 17 AA tandem repeats
Add
BLAST
Regioni1185 – 150131735 X 9 AA approximate tandem repeats of [TNP]-L-S-P-D-L-S-Q-T
Add
BLAST

Domaini

Domain B contains 35 x 9 AA tandem repeats, and 2 x 17 AA repeats.

Sequence similaritiesi

Contains 3 F5/8 type A domains.
Contains 2 F5/8 type C domains.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG240444.
HOVERGENiHBG005631.
KOiK03902.
OrthoDBiEOG7ZWD1D.
PhylomeDBiP12259.
TreeFamiTF329807.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
2.60.40.420. 6 hits.
InterProiIPR000421. 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]
PfamiPF07732. Cu-oxidase_3. 2 hits.
PF00754. F5_F8_type_C. 2 hits.
[Graphical view]
PIRSFiPIRSF000354. Factors_V_VIII. 1 hit.
SMARTiSM00231. FA58C. 2 hits.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 6 hits.
SSF49785. SSF49785. 2 hits.
PROSITEiPS01285. FA58C_1. 2 hits.
PS01286. FA58C_2. 2 hits.
PS50022. FA58C_3. 2 hits.
PS00079. MULTICOPPER_OXIDASE1. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P12259-1 [UniParc]FASTAAdd to Basket

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MFPGCPRLWV LVVLGTSWVG WGSQGTEAAQ LRQFYVAAQG ISWSYRPEPT     50
NSSLNLSVTS FKKIVYREYE PYFKKEKPQS TISGLLGPTL YAEVGDIIKV 100
HFKNKADKPL SIHPQGIRYS KLSEGASYLD HTFPAEKMDD AVAPGREYTY 150
EWSISEDSGP THDDPPCLTH IYYSHENLIE DFNSGLIGPL LICKKGTLTE 200
GGTQKTFDKQ IVLLFAVFDE SKSWSQSSSL MYTVNGYVNG TMPDITVCAH 250
DHISWHLLGM SSGPELFSIH FNGQVLEQNH HKVSAITLVS ATSTTANMTV 300
GPEGKWIISS LTPKHLQAGM QAYIDIKNCP KKTRNLKKIT REQRRHMKRW 350
EYFIAAEEVI WDYAPVIPAN MDKKYRSQHL DNFSNQIGKH YKKVMYTQYE 400
DESFTKHTVN PNMKEDGILG PIIRAQVRDT LKIVFKNMAS RPYSIYPHGV 450
TFSPYEDEVN SSFTSGRNNT MIRAVQPGET YTYKWNILEF DEPTENDAQC 500
LTRPYYSDVD IMRDIASGLI GLLLICKSRS LDRRGIQRAA DIEQQAVFAV 550
FDENKSWYLE DNINKFCENP DEVKRDDPKF YESNIMSTIN GYVPESITTL 600
GFCFDDTVQW HFCSVGTQNE ILTIHFTGHS FIYGKRHEDT LTLFPMRGES 650
VTVTMDNVGT WMLTSMNSSP RSKKLRLKFR DVKCIPDDDE DSYEIFEPPE 700
STVMATRKMH DRLEPEDEES DADYDYQNRL AAALGIRSFR NSSLNQEEEE 750
FNLTALALEN GTEFVSSNTD IIVGSNYSSP SNISKFTVNN LAEPQKAPSH 800
QQATTAGSPL RHLIGKNSVL NSSTAEHSSP YSEDPIEDPL QPDVTGIRLL 850
SLGAGEFKSQ EHAKHKGPKV ERDQAAKHRF SWMKLLAHKV GRHLSQDTGS 900
PSGMRPWEDL PSQDTGSPSR MRPWKDPPSD LLLLKQSNSS KILVGRWHLA 950
SEKGSYEIIQ DTDEDTAVNN WLISPQNASR AWGESTPLAN KPGKQSGHPK 1000
FPRVRHKSLQ VRQDGGKSRL KKSQFLIKTR KKKKEKHTHH APLSPRTFHP 1050
LRSEAYNTFS ERRLKHSLVL HKSNETSLPT DLNQTLPSMD FGWIASLPDH 1100
NQNSSNDTGQ ASCPPGLYQT VPPEEHYQTF PIQDPDQMHS TSDPSHRSSS 1150
PELSEMLEYD RSHKSFPTDI SQMSPSSEHE VWQTVISPDL SQVTLSPELS 1200
QTNLSPDLSH TTLSPELIQR NLSPALGQMP ISPDLSHTTL SPDLSHTTLS 1250
LDLSQTNLSP ELSQTNLSPA LGQMPLSPDL SHTTLSLDFS QTNLSPELSH 1300
MTLSPELSQT NLSPALGQMP ISPDLSHTTL SLDFSQTNLS PELSQTNLSP 1350
ALGQMPLSPD PSHTTLSLDL SQTNLSPELS QTNLSPDLSE MPLFADLSQI 1400
PLTPDLDQMT LSPDLGETDL SPNFGQMSLS PDLSQVTLSP DISDTTLLPD 1450
LSQISPPPDL DQIFYPSESS QSLLLQEFNE SFPYPDLGQM PSPSSPTLND 1500
TFLSKEFNPL VIVGLSKDGT DYIEIIPKEE VQSSEDDYAE IDYVPYDDPY 1550
KTDVRTNINS SRDPDNIAAW YLRSNNGNRR NYYIAAEEIS WDYSEFVQRE 1600
TDIEDSDDIP EDTTYKKVVF RKYLDSTFTK RDPRGEYEEH LGILGPIIRA 1650
EVDDVIQVRF KNLASRPYSL HAHGLSYEKS SEGKTYEDDS PEWFKEDNAV 1700
QPNSSYTYVW HATERSGPES PGSACRAWAY YSAVNPEKDI HSGLIGPLLI 1750
CQKGILHKDS NMPMDMREFV LLFMTFDEKK SWYYEKKSRS SWRLTSSEMK 1800
KSHEFHAING MIYSLPGLKM YEQEWVRLHL LNIGGSQDIH VVHFHGQTLL 1850
ENGNKQHQLG VWPLLPGSFK TLEMKASKPG WWLLNTEVGE NQRAGMQTPF 1900
LIMDRDCRMP MGLSTGIISD SQIKASEFLG YWEPRLARLN NGGSYNAWSV 1950
EKLAAEFASK PWIQVDMQKE VIITGIQTQG AKHYLKSCYT TEFYVAYSSN 2000
QINWQIFKGN STRNVMYFNG NSDASTIKEN QFDPPIVARY IRISPTRAYN 2050
RPTLRLELQG CEVNGCSTPL GMENGKIENK QITASSFKKS WWGDYWEPFR 2100
ARLNAQGRVN AWQAKANNNK QWLEIDLLKI KKITAIITQG CKSLSSEMYV 2150
KSYTIHYSEQ GVEWKPYRLK SSMVDKIFEG NTNTKGHVKN FFNPPIISRF 2200
IRVIPKTWNQ SIALRLELFG CDIY 2224
Length:2,224
Mass (Da):251,703
Last modified:October 5, 2010 - v4
Checksum:i24AEF3FEA7332E37
GO

Sequence cautioni

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti15 – 151G → S.1 Publication
Corresponds to variant rs9332485 [ dbSNP | Ensembl ].
VAR_021297
Natural varianti107 – 1071D → H.2 Publications
Corresponds to variant rs6019 [ dbSNP | Ensembl ].
VAR_013886
Natural varianti334 – 3341R → G in Hong Kong; does not predispose to clinical thrombosis. 2 Publications
Corresponds to variant rs118203905 [ dbSNP | Ensembl ].
VAR_013620
Natural varianti334 – 3341R → T in THPH2; Cambridge. 1 Publication
Corresponds to variant rs118203906 [ dbSNP | Ensembl ].
VAR_013621
Natural varianti387 – 3871I → T in THPH2; Liverpool; mutant protein is expressed with an additional carbohydrate chain. 2 Publications
VAR_032698
Natural varianti413 – 4131M → T.2 Publications
Corresponds to variant rs6033 [ dbSNP | Ensembl ].
VAR_013887
Natural varianti513 – 5131R → K.4 Publications
Corresponds to variant rs6020 [ dbSNP | Ensembl ].
VAR_013622
Natural varianti534 – 5341R → Q in Leiden; associated with thrombophilia; associated with susceptibility to Budd-Chiari syndrome; associated with susceptibility to ischemic stroke. 7 Publications
Corresponds to variant rs6025 [ dbSNP | Ensembl ].
VAR_001213
Natural varianti613 – 6131C → R in THPH2; Nijkerk. 1 Publication
VAR_032699
Natural varianti775 – 7751S → A in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035817
Natural varianti781 – 7811S → R.
Corresponds to variant rs13306350 [ dbSNP | Ensembl ].
VAR_047740
Natural varianti809 – 8091P → S.2 Publications
Corresponds to variant rs6031 [ dbSNP | Ensembl ].
VAR_013888
Natural varianti817 – 8171N → T.2 Publications
Corresponds to variant rs6018 [ dbSNP | Ensembl ].
VAR_013889
Natural varianti858 – 8581K → R.5 Publications
Corresponds to variant rs4524 [ dbSNP | Ensembl ].
VAR_001214
Natural varianti865 – 8651H → R.5 Publications
Corresponds to variant rs4525 [ dbSNP | Ensembl ].
VAR_001215
Natural varianti915 – 9151T → S.1 Publication
Corresponds to variant rs9332695 [ dbSNP | Ensembl ].
VAR_021298
Natural varianti925 – 9251K → E.5 Publications
Corresponds to variant rs6032 [ dbSNP | Ensembl ].
VAR_013890
Natural varianti969 – 9691N → S.1 Publication
Corresponds to variant rs9332604 [ dbSNP | Ensembl ].
VAR_021299
Natural varianti980 – 9801R → L.1 Publication
Corresponds to variant rs9332605 [ dbSNP | Ensembl ].
VAR_021300
Natural varianti1146 – 11461H → Q.2 Publications
Corresponds to variant rs6005 [ dbSNP | Ensembl ].
VAR_013891
Natural varianti1285 – 12851L → I.3 Publications
Corresponds to variant rs1046712 [ dbSNP | Ensembl ].
VAR_013892
Natural varianti1327 – 13271H → R.2 Publications
Corresponds to variant rs1800595 [ dbSNP | Ensembl ].
VAR_013893
Natural varianti1397 – 13971L → F.2 Publications
Corresponds to variant rs13306334 [ dbSNP | Ensembl ].
VAR_047741
Natural varianti1404 – 14041P → S.1 Publication
Corresponds to variant rs9332608 [ dbSNP | Ensembl ].
VAR_021301
Natural varianti1530 – 15301E → A.2 Publications
Corresponds to variant rs6007 [ dbSNP | Ensembl ].
VAR_013894
Natural varianti1685 – 16851T → S.1 Publication
Corresponds to variant rs6011 [ dbSNP | Ensembl ].
VAR_013895
Natural varianti1730 – 17301Y → C in FA5D; Seoul 2. 2 Publications
VAR_032700
Natural varianti1749 – 17491L → V.1 Publication
Corresponds to variant rs6034 [ dbSNP | Ensembl ].
VAR_013896
Natural varianti1764 – 17641M → V.3 Publications
Corresponds to variant rs6030 [ dbSNP | Ensembl ].
VAR_013897
Natural varianti1820 – 18201M → I.1 Publication
Corresponds to variant rs6026 [ dbSNP | Ensembl ].
VAR_013898
Natural varianti2102 – 21021R → C in FA5D; impairs both factor V secretion and activity. 1 Publication
VAR_032701
Natural varianti2102 – 21021R → H in THPH2. 1 Publication
VAR_017329
Natural varianti2148 – 21481M → T.1 Publication
Corresponds to variant rs9332701 [ dbSNP | Ensembl ].
VAR_021302
Natural varianti2185 – 21851K → R.
Corresponds to variant rs6679078 [ dbSNP | Ensembl ].
VAR_034603
Natural varianti2222 – 22221D → G.1 Publication
Corresponds to variant rs6027 [ dbSNP | Ensembl ].
VAR_013899

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti741 – 7411N → S in ABD23003. 1 Publication
Sequence conflicti908 – 9081E → K in AAA52424. 1 Publication
Sequence conflicti908 – 9081E → K in CAC82573. 1 Publication
Sequence conflicti991 – 9911K → E in BAF84302. 1 Publication
Sequence conflicti2213 – 22131A → T in AAA52424. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS1281.1.
PIRiA56172. KFHU5.
RefSeqiNP_000121.2. NM_000130.4.
UniGeneiHs.30054.

Genome annotation databases

EnsembliENST00000367796; ENSP00000356770; ENSG00000198734.
ENST00000367797; ENSP00000356771; ENSG00000198734.
GeneIDi2153.
KEGGihsa:2153.
UCSCiuc001ggg.1. human.

Polymorphism databases

DMDMi308153653.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Factor V entry

SeattleSNPs
SHMPD

The Singapore human mutation and polymorphism database

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS1281.1.
PIRi A56172. KFHU5.
RefSeqi NP_000121.2. NM_000130.4.
UniGenei Hs.30054.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P12259.
SMRi P12259. Positions 1575-2224.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108452. 6 interactions.
DIPi DIP-47331N.
STRINGi 9606.ENSP00000356771.

Chemistry

BindingDBi P12259.
ChEMBLi CHEMBL3618.
DrugBanki DB00055. Drotrecogin alfa.
GuidetoPHARMACOLOGYi 2606.

PTM databases

PhosphoSitei P12259.

Polymorphism databases

DMDMi 308153653.

Proteomic databases

MaxQBi P12259.
PaxDbi P12259.
PRIDEi P12259.

Protocols and materials databases

DNASUi 2153.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000367796 ; ENSP00000356770 ; ENSG00000198734 .
ENST00000367797 ; ENSP00000356771 ; ENSG00000198734 .
GeneIDi 2153.
KEGGi hsa:2153.
UCSCi uc001ggg.1. human.

Organism-specific databases

CTDi 2153.
GeneCardsi GC01M169481.
GeneReviewsi F5.
HGNCi HGNC:3542. F5.
HPAi HPA002036.
MIMi 188055. phenotype.
227400. phenotype.
600880. phenotype.
601367. phenotype.
612309. gene.
614389. phenotype.
neXtProti NX_P12259.
Orphaneti 131. Budd-Chiari syndrome.
329217. Cerebral sinovenous thrombosis.
326. Congenital factor V deficiency.
391320. East Texas bleeding disorder.
64738. Non rare thrombophilia.
PharmGKBi PA159.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG240444.
HOVERGENi HBG005631.
KOi K03902.
OrthoDBi EOG7ZWD1D.
PhylomeDBi P12259.
TreeFami TF329807.

Enzyme and pathway databases

Reactomei REACT_1439. Common Pathway.

Miscellaneous databases

EvolutionaryTracei P12259.
GeneWikii Factor_V.
GenomeRNAii 2153.
NextBioi 8701.
PROi P12259.
SOURCEi Search...

Gene expression databases

ArrayExpressi P12259.
Bgeei P12259.
CleanExi HS_F5.
Genevestigatori P12259.

Family and domain databases

Gene3Di 2.60.120.260. 2 hits.
2.60.40.420. 6 hits.
InterProi 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 ]
Pfami PF07732. Cu-oxidase_3. 2 hits.
PF00754. F5_F8_type_C. 2 hits.
[Graphical view ]
PIRSFi PIRSF000354. Factors_V_VIII. 1 hit.
SMARTi SM00231. FA58C. 2 hits.
[Graphical view ]
SUPFAMi SSF49503. SSF49503. 6 hits.
SSF49785. SSF49785. 2 hits.
PROSITEi PS01285. FA58C_1. 2 hits.
PS01286. FA58C_2. 2 hits.
PS50022. FA58C_3. 2 hits.
PS00079. MULTICOPPER_OXIDASE1. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    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.
    Tissue: Platelet.
  23. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  25. 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. 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. "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.
  35. "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.
  36. "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.
  37. "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.
  38. "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.
  39. "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.
  40. "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.
  41. Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-775.

Entry informationi

Entry nameiFA5_HUMAN
AccessioniPrimary (citable) accession number: P12259
Secondary accession number(s): A8K6E8
, Q14285, Q2EHR5, Q5R346, Q5R347, Q6UPU6, Q8WWQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 5, 2010
Last modified: September 3, 2014
This is version 182 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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