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UniProtKB - P12259 (FA5_HUMAN)

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Protein

Coagulation factor V

Gene

F5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Metal bindingi139CalciumBy similarity1
Metal bindingi140CalciumBy similarity1
Metal bindingi1843CopperBy similarity1
Metal bindingi1845CopperBy similarity1

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Biological processBlood coagulation, Hemostasis
LigandCalcium, Copper, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-114608 Platelet degranulation
R-HSA-140875 Common Pathway of Fibrin Clot Formation
R-HSA-204005 COPII-mediated vesicle transport
R-HSA-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-HSA-5694530 Cargo concentration in the ER
R-HSA-8957275 Post-translational protein phosphorylation
SIGNORiP12259

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:
Coagulation factor V heavy chain
Coagulation factor V light chain
Gene namesi
Name:F5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000198734.10
HGNCiHGNC:3542 F5
MIMi612309 gene
neXtProtiNX_P12259

Subcellular locationi

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

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Factor V deficiency (FA5D)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA blood coagulation disorder leading to a hemorrhagic diathesis known as parahemophilia.
See also OMIM:227400
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0327001730Y → C in FA5D; Seoul 2. 2 PublicationsCorresponds to variant dbSNP:rs118203907EnsemblClinVar.1
Natural variantiVAR_0327012102R → C in FA5D; impairs both factor V secretion and activity. 1 PublicationCorresponds to variant dbSNP:rs118203910EnsemblClinVar.1
Thrombophilia due to activated protein C resistance (THPH2)9 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:188055
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_013621334R → T in THPH2; Cambridge. 1 PublicationCorresponds to variant dbSNP:rs118203906EnsemblClinVar.1
Natural variantiVAR_032698387I → T in THPH2; Liverpool; mutant protein is expressed with an additional carbohydrate chain. 2 PublicationsCorresponds to variant dbSNP:rs118203911EnsemblClinVar.1
Natural variantiVAR_001213534R → Q in THPH2; factor V Leiden; associated with susceptibility to Budd-Chiari syndrome; associated with susceptibility to ischemic stroke. 5 PublicationsCorresponds to variant dbSNP:rs6025EnsemblClinVar.1
Natural variantiVAR_032699613C → R in THPH2; Nijkerk. 1 Publication1
Natural variantiVAR_0173292102R → H in THPH2. 1 Publication1
Budd-Chiari syndrome (BDCHS)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:600880
Ischemic stroke (ISCHSTR)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:601367
Pregnancy loss, recurrent, 1 (RPRGL1)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:614389

Keywords - Diseasei

Disease mutation, Thrombophilia

Organism-specific databases

DisGeNETi2153
GeneReviewsiF5
MalaCardsiF5
MIMi188055 phenotype
227400 phenotype
600880 phenotype
601367 phenotype
614389 phenotype
OpenTargetsiENSG00000198734
Orphaneti131 Budd-Chiari syndrome
329217 Cerebral sinovenous thrombosis
326 Congenital factor V deficiency
391320 East Texas bleeding disorder
64738 Non rare thrombophilia
PharmGKBiPA159

Chemistry databases

ChEMBLiCHEMBL3618
DrugBankiDB00055 Drotrecogin alfa
DB05777 Thrombomodulin Alfa

Polymorphism and mutation databases

BioMutaiF5
DMDMi308153653

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Add BLAST28
ChainiPRO_000000297829 – 2224Coagulation factor VAdd BLAST2196
ChainiPRO_000000297929 – 737Coagulation factor V heavy chainAdd BLAST709
PropeptideiPRO_0000002980738 – 1573Activation peptide (connecting region)Add BLAST836
ChainiPRO_00000029811574 – 2224Coagulation factor V light chainAdd BLAST651

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi51N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi55N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi167 ↔ 193PROSITE-ProRule annotation
Glycosylationi239N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi248 ↔ 329PROSITE-ProRule annotation
Glycosylationi297N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi382N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi460N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi468N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi500 ↔ 526PROSITE-ProRule annotation
Glycosylationi554N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi603 ↔ 684PROSITE-ProRule annotation
Modified residuei640PhosphothreonineCombined sources1
Modified residuei693SulfotyrosineSequence analysis1
Modified residuei724SulfotyrosineSequence analysis1
Modified residuei726SulfotyrosineSequence analysis1
Glycosylationi741N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi752N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi760N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi776N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi782N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi821N-linked (GlcNAc...) asparagine1 Publication1
Modified residuei859Phosphoserine; by FAM20C1 Publication1
Glycosylationi938N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi977N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi1074N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1083N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1103N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1106N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1479N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1499N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei1522SulfotyrosineSequence analysis1
Modified residuei1538SulfotyrosineSequence analysis1
Modified residuei1543SulfotyrosineSequence analysis1
Glycosylationi1559N-linked (GlcNAc...) asparagine1 Publication1
Modified residuei1593SulfotyrosineSequence analysis1
Glycosylationi1703N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1725 ↔ 1751Curated
Disulfide bondi1907 ↔ 2061PROSITE-ProRule annotation
Glycosylationi2010N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2066 ↔ 2221PROSITE-ProRule annotation
Glycosylationi2209N-linked (GlcNAc...) asparagineSequence analysis1

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.1 Publication
Phosphorylated by FAM20C in the extracellular medium.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei334 – 335Cleavage; by activated protein C1 Publication2
Sitei534 – 535Cleavage; by activated protein C1 Publication2
Sitei707 – 708Cleavage; by activated protein C1 Publication2
Sitei737 – 738Cleavage; by thrombin1 Publication2
Sitei1022 – 1023Cleavage; by activated protein C1 Publication2
Sitei1046 – 1047Cleavage; by thrombin1 Publication2
Sitei1573 – 1574Cleavage; by thrombin1 Publication2

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation, Zymogen

Proteomic databases

MaxQBiP12259
PaxDbiP12259
PeptideAtlasiP12259
PRIDEiP12259
ProteomicsDBi52838

PTM databases

CarbonylDBiP12259
iPTMnetiP12259
PhosphoSitePlusiP12259

Expressioni

Tissue specificityi

Plasma.

Gene expression databases

BgeeiENSG00000198734
CleanExiHS_F5
ExpressionAtlasiP12259 baseline and differential
GenevisibleiP12259 HS

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, 13 interactors
DIPiDIP-47331N
IntActiP12259, 3 interactors
MINTiP12259
STRINGi9606.ENSP00000356771

Chemistry databases

BindingDBiP12259

Structurei

Secondary structure

12224
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni1569 – 1571Combined sources3
Turni2072 – 2074Combined sources3
Beta strandi2075 – 2077Combined sources3
Helixi2079 – 2081Combined sources3
Beta strandi2082 – 2085Combined sources4
Beta strandi2093 – 2095Combined sources3
Helixi2098 – 2100Combined sources3
Beta strandi2107 – 2109Combined sources3
Beta strandi2111 – 2113Combined sources3
Beta strandi2123 – 2139Combined sources17
Beta strandi2141 – 2143Combined sources3
Beta strandi2146 – 2163Combined sources18
Beta strandi2182 – 2185Combined sources4
Beta strandi2188 – 2211Combined sources24
Beta strandi2213 – 2222Combined sources10

3D structure databases

ProteinModelPortaliP12259
SMRiP12259
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12259

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini30 – 329F5/8 type A 1Add BLAST300
Domaini30 – 193Plastocyanin-like 1Add BLAST164
Domaini203 – 329Plastocyanin-like 2Add BLAST127
Domaini348 – 684F5/8 type A 2Add BLAST337
Domaini348 – 526Plastocyanin-like 3Add BLAST179
Domaini536 – 684Plastocyanin-like 4Add BLAST149
Repeati895 – 9111-1Add BLAST17
Repeati912 – 9281-2Add BLAST17
Repeati1185 – 11932-19
Repeati1194 – 12022-29
Repeati1203 – 12112-39
Repeati1212 – 12202-49
Repeati1221 – 12292-59
Repeati1230 – 12382-69
Repeati1239 – 12472-79
Repeati1248 – 12562-89
Repeati1257 – 12652-99
Repeati1266 – 12742-109
Repeati1275 – 12832-119
Repeati1284 – 12922-129
Repeati1293 – 13012-139
Repeati1302 – 13102-149
Repeati1311 – 13192-159
Repeati1320 – 13282-169
Repeati1329 – 13372-179
Repeati1338 – 13462-189
Repeati1347 – 13552-199
Repeati1356 – 13642-209
Repeati1365 – 13732-219
Repeati1374 – 13822-229
Repeati1383 – 13912-239
Repeati1392 – 14002-249
Repeati1401 – 14092-259
Repeati1410 – 14182-269
Repeati1419 – 14272-279
Repeati1428 – 14362-289
Repeati1437 – 14452-299
Repeati1446 – 14542-309
Repeati1455 – 14632-319
Repeati1464 – 14722-329
Repeati1473 – 14812-339
Repeati1482 – 14902-349
Repeati1493 – 15012-359
Domaini1578 – 1907F5/8 type A 3Add BLAST330
Domaini1578 – 1751Plastocyanin-like 5Add BLAST174
Domaini1761 – 1907Plastocyanin-like 6Add BLAST147
Domaini1907 – 2061F5/8 type C 1PROSITE-ProRule annotationAdd BLAST155
Domaini2066 – 2221F5/8 type C 2PROSITE-ProRule annotationAdd BLAST156

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni692 – 1573BAdd BLAST882
Regioni895 – 9282 X 17 AA tandem repeatsAdd BLAST34
Regioni1185 – 150135 X 9 AA approximate tandem repeats of [TNP]-L-S-P-D-L-S-Q-TAdd BLAST317

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

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IJ6Y Eukaryota
ENOG4111F6G LUCA
GeneTreeiENSGT00910000143988
HOVERGENiHBG005631
InParanoidiP12259
KOiK03902
PhylomeDBiP12259
TreeFamiTF329807

Family and domain databases

Gene3Di2.60.120.260, 2 hits
2.60.40.420, 5 hits
InterProiView protein in InterPro
IPR011707 Cu-oxidase_3
IPR033138 Cu_oxidase_CS
IPR008972 Cupredoxin
IPR000421 FA58C
IPR024715 Factor_5/8_like
IPR008979 Galactose-bd-like_sf
PfamiView protein in Pfam
PF07732 Cu-oxidase_3, 2 hits
PF00754 F5_F8_type_C, 2 hits
PIRSFiPIRSF000354 Factors_V_VIII, 1 hit
SMARTiView protein in SMART
SM00231 FA58C, 2 hits
SUPFAMiSSF49503 SSF49503, 6 hits
SSF49785 SSF49785, 2 hits
PROSITEiView protein in PROSITE
PS01285 FA58C_1, 2 hits
PS01286 FA58C_2, 2 hits
PS50022 FA58C_3, 2 hits
PS00079 MULTICOPPER_OXIDASE1, 2 hits

Sequencei

Sequence statusi: Complete.

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

P12259-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFPGCPRLWV LVVLGTSWVG WGSQGTEAAQ LRQFYVAAQG ISWSYRPEPT 
        60         70         80         90        100
NSSLNLSVTS FKKIVYREYE PYFKKEKPQS TISGLLGPTL YAEVGDIIKV 
       110        120        130        140        150
HFKNKADKPL SIHPQGIRYS KLSEGASYLD HTFPAEKMDD AVAPGREYTY 
       160        170        180        190        200
EWSISEDSGP THDDPPCLTH IYYSHENLIE DFNSGLIGPL LICKKGTLTE 
       210        220        230        240        250
GGTQKTFDKQ IVLLFAVFDE SKSWSQSSSL MYTVNGYVNG TMPDITVCAH 
       260        270        280        290        300
DHISWHLLGM SSGPELFSIH FNGQVLEQNH HKVSAITLVS ATSTTANMTV 
       310        320        330        340        350
GPEGKWIISS LTPKHLQAGM QAYIDIKNCP KKTRNLKKIT REQRRHMKRW 
       360        370        380        390        400
EYFIAAEEVI WDYAPVIPAN MDKKYRSQHL DNFSNQIGKH YKKVMYTQYE 
       410        420        430        440        450
DESFTKHTVN PNMKEDGILG PIIRAQVRDT LKIVFKNMAS RPYSIYPHGV 
       460        470        480        490        500
TFSPYEDEVN SSFTSGRNNT MIRAVQPGET YTYKWNILEF DEPTENDAQC 
       510        520        530        540        550
LTRPYYSDVD IMRDIASGLI GLLLICKSRS LDRRGIQRAA DIEQQAVFAV 
       560        570        580        590        600
FDENKSWYLE DNINKFCENP DEVKRDDPKF YESNIMSTIN GYVPESITTL 
       610        620        630        640        650
GFCFDDTVQW HFCSVGTQNE ILTIHFTGHS FIYGKRHEDT LTLFPMRGES 
       660        670        680        690        700
VTVTMDNVGT WMLTSMNSSP RSKKLRLKFR DVKCIPDDDE DSYEIFEPPE 
       710        720        730        740        750
STVMATRKMH DRLEPEDEES DADYDYQNRL AAALGIRSFR NSSLNQEEEE 
       760        770        780        790        800
FNLTALALEN GTEFVSSNTD IIVGSNYSSP SNISKFTVNN LAEPQKAPSH 
       810        820        830        840        850
QQATTAGSPL RHLIGKNSVL NSSTAEHSSP YSEDPIEDPL QPDVTGIRLL 
       860        870        880        890        900
SLGAGEFKSQ EHAKHKGPKV ERDQAAKHRF SWMKLLAHKV GRHLSQDTGS 
       910        920        930        940        950
PSGMRPWEDL PSQDTGSPSR MRPWKDPPSD LLLLKQSNSS KILVGRWHLA 
       960        970        980        990       1000
SEKGSYEIIQ DTDEDTAVNN WLISPQNASR AWGESTPLAN KPGKQSGHPK 
      1010       1020       1030       1040       1050
FPRVRHKSLQ VRQDGGKSRL KKSQFLIKTR KKKKEKHTHH APLSPRTFHP 
      1060       1070       1080       1090       1100
LRSEAYNTFS ERRLKHSLVL HKSNETSLPT DLNQTLPSMD FGWIASLPDH 
      1110       1120       1130       1140       1150
NQNSSNDTGQ ASCPPGLYQT VPPEEHYQTF PIQDPDQMHS TSDPSHRSSS 
      1160       1170       1180       1190       1200
PELSEMLEYD RSHKSFPTDI SQMSPSSEHE VWQTVISPDL SQVTLSPELS 
      1210       1220       1230       1240       1250
QTNLSPDLSH TTLSPELIQR NLSPALGQMP ISPDLSHTTL SPDLSHTTLS 
      1260       1270       1280       1290       1300
LDLSQTNLSP ELSQTNLSPA LGQMPLSPDL SHTTLSLDFS QTNLSPELSH 
      1310       1320       1330       1340       1350
MTLSPELSQT NLSPALGQMP ISPDLSHTTL SLDFSQTNLS PELSQTNLSP 
      1360       1370       1380       1390       1400
ALGQMPLSPD PSHTTLSLDL SQTNLSPELS QTNLSPDLSE MPLFADLSQI 
      1410       1420       1430       1440       1450
PLTPDLDQMT LSPDLGETDL SPNFGQMSLS PDLSQVTLSP DISDTTLLPD 
      1460       1470       1480       1490       1500
LSQISPPPDL DQIFYPSESS QSLLLQEFNE SFPYPDLGQM PSPSSPTLND 
      1510       1520       1530       1540       1550
TFLSKEFNPL VIVGLSKDGT DYIEIIPKEE VQSSEDDYAE IDYVPYDDPY 
      1560       1570       1580       1590       1600
KTDVRTNINS SRDPDNIAAW YLRSNNGNRR NYYIAAEEIS WDYSEFVQRE 
      1610       1620       1630       1640       1650
TDIEDSDDIP EDTTYKKVVF RKYLDSTFTK RDPRGEYEEH LGILGPIIRA 
      1660       1670       1680       1690       1700
EVDDVIQVRF KNLASRPYSL HAHGLSYEKS SEGKTYEDDS PEWFKEDNAV 
      1710       1720       1730       1740       1750
QPNSSYTYVW HATERSGPES PGSACRAWAY YSAVNPEKDI HSGLIGPLLI 
      1760       1770       1780       1790       1800
CQKGILHKDS NMPMDMREFV LLFMTFDEKK SWYYEKKSRS SWRLTSSEMK 
      1810       1820       1830       1840       1850
KSHEFHAING MIYSLPGLKM YEQEWVRLHL LNIGGSQDIH VVHFHGQTLL 
      1860       1870       1880       1890       1900
ENGNKQHQLG VWPLLPGSFK TLEMKASKPG WWLLNTEVGE NQRAGMQTPF 
      1910       1920       1930       1940       1950
LIMDRDCRMP MGLSTGIISD SQIKASEFLG YWEPRLARLN NGGSYNAWSV 
      1960       1970       1980       1990       2000
EKLAAEFASK PWIQVDMQKE VIITGIQTQG AKHYLKSCYT TEFYVAYSSN 
      2010       2020       2030       2040       2050
QINWQIFKGN STRNVMYFNG NSDASTIKEN QFDPPIVARY IRISPTRAYN 
      2060       2070       2080       2090       2100
RPTLRLELQG CEVNGCSTPL GMENGKIENK QITASSFKKS WWGDYWEPFR 
      2110       2120       2130       2140       2150
ARLNAQGRVN AWQAKANNNK QWLEIDLLKI KKITAIITQG CKSLSSEMYV 
      2160       2170       2180       2190       2200
KSYTIHYSEQ GVEWKPYRLK SSMVDKIFEG NTNTKGHVKN FFNPPIISRF 
      2210       2220 
IRVIPKTWNQ SIALRLELFG CDIY
Length:2,224
Mass (Da):251,703
Last modified:October 5, 2010 - v4
Checksum:i24AEF3FEA7332E37
GO

Sequence cautioni

The sequence ABD23003 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAI23065 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti741N → S in ABD23003 (Ref. 7) Curated1
Sequence conflicti908E → K in AAA52424 (PubMed:3110773).Curated1
Sequence conflicti908E → K in CAC82573 (PubMed:11758222).Curated1
Sequence conflicti991K → E in BAF84302 (PubMed:14702039).Curated1
Sequence conflicti2213A → T in AAA52424 (PubMed:3110773).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02129715G → S1 PublicationCorresponds to variant dbSNP:rs9332485EnsemblClinVar.1
Natural variantiVAR_013886107D → H2 PublicationsCorresponds to variant dbSNP:rs6019EnsemblClinVar.1
Natural variantiVAR_013620334R → G in Hong Kong; does not predispose to clinical thrombosis. 2 PublicationsCorresponds to variant dbSNP:rs118203905EnsemblClinVar.1
Natural variantiVAR_013621334R → T in THPH2; Cambridge. 1 PublicationCorresponds to variant dbSNP:rs118203906EnsemblClinVar.1
Natural variantiVAR_032698387I → T in THPH2; Liverpool; mutant protein is expressed with an additional carbohydrate chain. 2 PublicationsCorresponds to variant dbSNP:rs118203911EnsemblClinVar.1
Natural variantiVAR_013887413M → T2 PublicationsCorresponds to variant dbSNP:rs6033EnsemblClinVar.1
Natural variantiVAR_013622513R → K4 PublicationsCorresponds to variant dbSNP:rs6020EnsemblClinVar.1
Natural variantiVAR_001213534R → Q in THPH2; factor V Leiden; associated with susceptibility to Budd-Chiari syndrome; associated with susceptibility to ischemic stroke. 5 PublicationsCorresponds to variant dbSNP:rs6025EnsemblClinVar.1
Natural variantiVAR_032699613C → R in THPH2; Nijkerk. 1 Publication1
Natural variantiVAR_035817775S → A in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_047740781S → R. Corresponds to variant dbSNP:rs13306350Ensembl.1
Natural variantiVAR_013888809P → S2 PublicationsCorresponds to variant dbSNP:rs6031EnsemblClinVar.1
Natural variantiVAR_013889817N → T2 PublicationsCorresponds to variant dbSNP:rs6018EnsemblClinVar.1
Natural variantiVAR_001214858K → R5 PublicationsCorresponds to variant dbSNP:rs4524EnsemblClinVar.1
Natural variantiVAR_001215865H → R5 PublicationsCorresponds to variant dbSNP:rs4525EnsemblClinVar.1
Natural variantiVAR_021298915T → S1 PublicationCorresponds to variant dbSNP:rs9332695EnsemblClinVar.1
Natural variantiVAR_013890925K → E5 PublicationsCorresponds to variant dbSNP:rs6032EnsemblClinVar.1
Natural variantiVAR_021299969N → S1 PublicationCorresponds to variant dbSNP:rs9332604EnsemblClinVar.1
Natural variantiVAR_021300980R → L1 PublicationCorresponds to variant dbSNP:rs9332605Ensembl.1
Natural variantiVAR_0138911146H → Q2 PublicationsCorresponds to variant dbSNP:rs6005EnsemblClinVar.1
Natural variantiVAR_0138921285L → I3 PublicationsCorresponds to variant dbSNP:rs1046712EnsemblClinVar.1
Natural variantiVAR_0138931327H → R2 PublicationsCorresponds to variant dbSNP:rs1800595EnsemblClinVar.1
Natural variantiVAR_0477411397L → F2 PublicationsCorresponds to variant dbSNP:rs13306334EnsemblClinVar.1
Natural variantiVAR_0213011404P → S1 PublicationCorresponds to variant dbSNP:rs9332608EnsemblClinVar.1
Natural variantiVAR_0138941530E → A2 PublicationsCorresponds to variant dbSNP:rs6007Ensembl.1
Natural variantiVAR_0138951685T → S1 PublicationCorresponds to variant dbSNP:rs6011EnsemblClinVar.1
Natural variantiVAR_0327001730Y → C in FA5D; Seoul 2. 2 PublicationsCorresponds to variant dbSNP:rs118203907EnsemblClinVar.1
Natural variantiVAR_0138961749L → V1 PublicationCorresponds to variant dbSNP:rs6034Ensembl.1
Natural variantiVAR_0138971764M → V3 PublicationsCorresponds to variant dbSNP:rs6030EnsemblClinVar.1
Natural variantiVAR_0138981820M → I1 PublicationCorresponds to variant dbSNP:rs6026EnsemblClinVar.1
Natural variantiVAR_0327012102R → C in FA5D; impairs both factor V secretion and activity. 1 PublicationCorresponds to variant dbSNP:rs118203910EnsemblClinVar.1
Natural variantiVAR_0173292102R → H in THPH2. 1 Publication1
Natural variantiVAR_0213022148M → T1 PublicationCorresponds to variant dbSNP:rs9332701EnsemblClinVar.1
Natural variantiVAR_0346032185K → R. Corresponds to variant dbSNP:rs6679078Ensembl.1
Natural variantiVAR_0138992222D → G1 PublicationCorresponds to variant dbSNP:rs6027EnsemblClinVar.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

EnsembliENST00000367797; ENSP00000356771; ENSG00000198734
GeneIDi2153
KEGGihsa:2153
UCSCiuc001ggg.2 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiFA5_HUMAN
AccessioniPrimary (citable) accession number: P12259
Secondary accession number(s): A8K6E8
, Q14285, Q2EHR5, Q5R346, Q5R347, Q6UPU6, Q8WWQ6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 5, 2010
Last modified: June 20, 2018
This is version 219 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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

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