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P12259

- FA5_HUMAN

UniProt

P12259 - FA5_HUMAN

Protein

Coagulation factor V

Gene

F5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 183 (01 Oct 2014)
      Sequence version 4 (05 Oct 2010)
      Previous versions | rss
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    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 – 1391CalciumBy similarity
    Metal bindingi140 – 1401CalciumBy 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 – 18431CopperBy similarity
    Metal bindingi1845 – 18451CopperBy 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

    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. membrane Source: UniProtKB
    4. plasma membrane Source: Reactome
    5. platelet alpha granule lumen Source: Reactome

    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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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. 1 Publication
    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.1 Publication
    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.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    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.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

    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 – 2828Add
    BLAST
    Chaini29 – 22242196Coagulation factor VPRO_0000002978Add
    BLAST
    Chaini29 – 737709Coagulation factor V heavy chainPRO_0000002979Add
    BLAST
    Propeptidei738 – 1573836Activation peptide (connecting region)PRO_0000002980Add
    BLAST
    Chaini1574 – 2224651Coagulation factor V light chainPRO_0000002981Add
    BLAST

    Amino acid modifications

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

    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.3 Publications
    Activated protein C inactivates factor V and factor Va by proteolytic degradation.
    Phosphorylation sites are present in the extracellular medium.1 Publication

    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.
    IntActiP12259. 1 interaction.
    STRINGi9606.ENSP00000356771.

    Structurei

    Secondary structure

    1
    2224
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12259.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini30 – 329300F5/8 type A 1Add
    BLAST
    Domaini30 – 193164Plastocyanin-like 1Add
    BLAST
    Domaini203 – 329127Plastocyanin-like 2Add
    BLAST
    Domaini348 – 684337F5/8 type A 2Add
    BLAST
    Domaini348 – 526179Plastocyanin-like 3Add
    BLAST
    Domaini536 – 684149Plastocyanin-like 4Add
    BLAST
    Repeati895 – 911171-1Add
    BLAST
    Repeati912 – 928171-2Add
    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 3Add
    BLAST
    Domaini1578 – 1751174Plastocyanin-like 5Add
    BLAST
    Domaini1761 – 1907147Plastocyanin-like 6Add
    BLAST
    Domaini1907 – 2061155F5/8 type C 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini2066 – 2221156F5/8 type C 2PROSITE-ProRule annotationAdd
    BLAST

    Region

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

    Domaini

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

    Sequence similaritiesi

    Belongs to the multicopper oxidase family.Curated
    Contains 3 F5/8 type A domains.Curated
    Contains 2 F5/8 type C domains.PROSITE-ProRule annotation
    Contains 6 plastocyanin-like domains.Curated

    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

    « Hide

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti741 – 7411N → S in ABD23003. 1 PublicationCurated
    Sequence conflicti908 – 9081E → K in AAA52424. (PubMed:3110773)Curated
    Sequence conflicti908 – 9081E → K in CAC82573. (PubMed:11758222)Curated
    Sequence conflicti991 – 9911K → E in BAF84302. (PubMed:14702039)Curated
    Sequence conflicti2213 – 22131A → T in AAA52424. (PubMed:3110773)Curated

    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. 1 Publication
    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. 5 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 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.
    IntActi P12259. 1 interaction.
    STRINGi 9606.ENSP00000356771.

    Chemistry

    BindingDBi P12259.
    ChEMBLi CHEMBL3618.
    DrugBanki DB05777. ART-123.
    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

    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: October 1, 2014
    This is version 183 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