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P12259 (FA5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 181. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Coagulation factor V
Alternative name(s):
Activated protein C cofactor
Proaccelerin, labile factor
Gene names
Name:F5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2224 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Central regulator of hemostasis. It serves as a critical cofactor for the prothrombinase activity of factor Xa that results in the activation of prothrombin to thrombin.

Enzyme regulation

Inhibited by SERPINA5. Ref.11 Ref.13 Ref.18 Ref.20

Subunit structure

Factor Va, the activated form of factor V, is composed of a heavy chain and a light chain, non-covalently bound. The interaction between the two chains is calcium-dependent. Forms heterodimer with SERPINA5.

Subcellular location

Secreted By similarity.

Tissue specificity

Plasma.

Domain

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

Post-translational modification

Thrombin activates factor V proteolytically to the active cofactor, factor Va (formation of a heavy chain at the N-terminus and a light chain at the C-terminus).

Sulfation is required for efficient thrombin cleavage and activation and for full procoagulant activity.

Activated protein C inactivates factor V and factor Va by proteolytic degradation.

Phosphorylation sites are present in the extracellular medium.

Involvement in disease

Factor V deficiency (FA5D) [MIM:227400]: A blood coagulation disorder leading to an hemorrhagic diathesis known as parahemophilia.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.35 Ref.38

Thrombophilia due to activated protein C resistance (THPH2) [MIM:188055]: A hemostatic disorder due to defective degradation of factor V by activated protein C. It is characterized by a poor anticoagulant response to activated protein C resulting in tendency to thrombosis.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.31 Ref.36 Ref.37 Ref.39 Ref.41

Budd-Chiari syndrome (BDCHS) [MIM:600880]: A syndrome caused by obstruction of hepatic venous outflow involving either the hepatic veins or the terminal segment of the inferior vena cava. Obstructions are generally caused by thrombosis and lead to hepatic congestion and ischemic necrosis. Clinical manifestations observed in the majority of patients include hepatomegaly, right upper quadrant pain and abdominal ascites. Budd-Chiari syndrome is associated with a combination of disease states including primary myeloproliferative syndromes and thrombophilia due to factor V Leiden, protein C deficiency and antithrombin III deficiency. Budd-Chiari syndrome is a rare but typical complication in patients with polycythemia vera.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

Ischemic stroke (ISCHSTR) [MIM:601367]: A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.40

Pregnancy loss, recurrent, 1 (RPRGL1) [MIM:614389]: A common complication of pregnancy, resulting in spontaneous abortion before the fetus has reached viability. The term includes all miscarriages from the time of conception until 24 weeks of gestation. Recurrent pregnancy loss is defined as 3 or more consecutive spontaneous abortions.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.19

Sequence similarities

Belongs to the multicopper oxidase family.

Contains 3 F5/8 type A domains.

Contains 2 F5/8 type C domains.

Contains 6 plastocyanin-like domains.

Sequence caution

The sequence ABD23003.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI23065.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828
Chain29 – 22242196Coagulation factor V
PRO_0000002978
Chain29 – 737709Coagulation factor V heavy chain
PRO_0000002979
Propeptide738 – 1573836Activation peptide (connecting region)
PRO_0000002980
Chain1574 – 2224651Coagulation factor V light chain
PRO_0000002981

Regions

Domain30 – 329300F5/8 type A 1
Domain30 – 193164Plastocyanin-like 1
Domain203 – 329127Plastocyanin-like 2
Domain348 – 684337F5/8 type A 2
Domain348 – 526179Plastocyanin-like 3
Domain536 – 684149Plastocyanin-like 4
Repeat895 – 911171-1
Repeat912 – 928171-2
Repeat1185 – 119392-1
Repeat1194 – 120292-2
Repeat1203 – 121192-3
Repeat1212 – 122092-4
Repeat1221 – 122992-5
Repeat1230 – 123892-6
Repeat1239 – 124792-7
Repeat1248 – 125692-8
Repeat1257 – 126592-9
Repeat1266 – 127492-10
Repeat1275 – 128392-11
Repeat1284 – 129292-12
Repeat1293 – 130192-13
Repeat1302 – 131092-14
Repeat1311 – 131992-15
Repeat1320 – 132892-16
Repeat1329 – 133792-17
Repeat1338 – 134692-18
Repeat1347 – 135592-19
Repeat1356 – 136492-20
Repeat1365 – 137392-21
Repeat1374 – 138292-22
Repeat1383 – 139192-23
Repeat1392 – 140092-24
Repeat1401 – 140992-25
Repeat1410 – 141892-26
Repeat1419 – 142792-27
Repeat1428 – 143692-28
Repeat1437 – 144592-29
Repeat1446 – 145492-30
Repeat1455 – 146392-31
Repeat1464 – 147292-32
Repeat1473 – 148192-33
Repeat1482 – 149092-34
Repeat1493 – 150192-35
Domain1578 – 1907330F5/8 type A 3
Domain1578 – 1751174Plastocyanin-like 5
Domain1761 – 1907147Plastocyanin-like 6
Domain1907 – 2061155F5/8 type C 1
Domain2066 – 2221156F5/8 type C 2
Region692 – 1573882B
Region895 – 928342 X 17 AA tandem repeats
Region1185 – 150131735 X 9 AA approximate tandem repeats of [TNP]-L-S-P-D-L-S-Q-T

Sites

Metal binding1391Calcium By similarity
Metal binding1401Calcium By similarity
Metal binding18431Copper By similarity
Metal binding18451Copper By similarity
Site334 – 3352Cleavage; by activated protein C
Site534 – 5352Cleavage; by activated protein C
Site707 – 7082Cleavage; by activated protein C
Site737 – 7382Cleavage; by thrombin
Site1022 – 10232Cleavage; by activated protein C
Site1046 – 10472Cleavage; by thrombin
Site1573 – 15742Cleavage; by thrombin

Amino acid modifications

Modified residue6401Phosphothreonine Ref.24
Modified residue6931Sulfotyrosine Potential
Modified residue7241Sulfotyrosine Potential
Modified residue7261Sulfotyrosine Potential
Modified residue15221Sulfotyrosine Potential
Modified residue15381Sulfotyrosine Potential
Modified residue15431Sulfotyrosine Potential
Modified residue15931Sulfotyrosine Potential
Glycosylation511N-linked (GlcNAc...) Potential
Glycosylation551N-linked (GlcNAc...) Potential
Glycosylation2391N-linked (GlcNAc...) Potential
Glycosylation2971N-linked (GlcNAc...) Ref.21 Ref.22
Glycosylation3821N-linked (GlcNAc...) Potential
Glycosylation4601N-linked (GlcNAc...) Ref.21
Glycosylation4681N-linked (GlcNAc...) Potential
Glycosylation5541N-linked (GlcNAc...) Potential
Glycosylation7411N-linked (GlcNAc...) Potential
Glycosylation7521N-linked (GlcNAc...) Potential
Glycosylation7601N-linked (GlcNAc...) Potential
Glycosylation7761N-linked (GlcNAc...) Potential
Glycosylation7821N-linked (GlcNAc...) Potential
Glycosylation8211N-linked (GlcNAc...) Ref.21
Glycosylation9381N-linked (GlcNAc...) Potential
Glycosylation9771N-linked (GlcNAc...) Ref.21
Glycosylation10741N-linked (GlcNAc...) Potential
Glycosylation10831N-linked (GlcNAc...) Potential
Glycosylation11031N-linked (GlcNAc...) Potential
Glycosylation11061N-linked (GlcNAc...) Potential
Glycosylation14791N-linked (GlcNAc...) Potential
Glycosylation14991N-linked (GlcNAc...) Potential
Glycosylation15591N-linked (GlcNAc...) Ref.21
Glycosylation17031N-linked (GlcNAc...) Potential
Glycosylation20101N-linked (GlcNAc...) Potential
Glycosylation22091N-linked (GlcNAc...) Potential
Disulfide bond167 ↔ 193 By similarity
Disulfide bond248 ↔ 329 By similarity
Disulfide bond500 ↔ 526 By similarity
Disulfide bond603 ↔ 684 By similarity
Disulfide bond1725 ↔ 1751 Probable
Disulfide bond1907 ↔ 2061 By similarity
Disulfide bond2066 ↔ 2221 By similarity

Natural variations

Natural variant151G → S. Ref.3
Corresponds to variant rs9332485 [ dbSNP | Ensembl ].
VAR_021297
Natural variant1071D → H. Ref.3 Ref.33
Corresponds to variant rs6019 [ dbSNP | Ensembl ].
VAR_013886
Natural variant3341R → G in Hong Kong; does not predispose to clinical thrombosis. Ref.30 Ref.32
Corresponds to variant rs118203905 [ dbSNP | Ensembl ].
VAR_013620
Natural variant3341R → T in THPH2; Cambridge. Ref.31
Corresponds to variant rs118203906 [ dbSNP | Ensembl ].
VAR_013621
Natural variant3871I → T in THPH2; Liverpool; mutant protein is expressed with an additional carbohydrate chain. Ref.39 Ref.41
VAR_032698
Natural variant4131M → T. Ref.3 Ref.33
Corresponds to variant rs6033 [ dbSNP | Ensembl ].
VAR_013887
Natural variant5131R → K. Ref.3 Ref.5 Ref.30 Ref.33
Corresponds to variant rs6020 [ dbSNP | Ensembl ].
VAR_013622
Natural variant5341R → Q in Leiden; associated with thrombophilia; associated with susceptibility to Budd-Chiari syndrome; associated with susceptibility to ischemic stroke. Ref.3 Ref.4 Ref.27 Ref.29 Ref.33 Ref.35 Ref.40
Corresponds to variant rs6025 [ dbSNP | Ensembl ].
VAR_001213
Natural variant6131C → R in THPH2; Nijkerk. Ref.36
VAR_032699
Natural variant7751S → A in a colorectal cancer sample; somatic mutation. Ref.42
VAR_035817
Natural variant7811S → R.
Corresponds to variant rs13306350 [ dbSNP | Ensembl ].
VAR_047740
Natural variant8091P → S. Ref.3 Ref.33
Corresponds to variant rs6031 [ dbSNP | Ensembl ].
VAR_013888
Natural variant8171N → T. Ref.3 Ref.33
Corresponds to variant rs6018 [ dbSNP | Ensembl ].
VAR_013889
Natural variant8581K → R. Ref.1 Ref.3 Ref.6 Ref.8 Ref.33
Corresponds to variant rs4524 [ dbSNP | Ensembl ].
VAR_001214
Natural variant8651H → R. Ref.1 Ref.3 Ref.6 Ref.8 Ref.33
Corresponds to variant rs4525 [ dbSNP | Ensembl ].
VAR_001215
Natural variant9151T → S. Ref.3
Corresponds to variant rs9332695 [ dbSNP | Ensembl ].
VAR_021298
Natural variant9251K → E. Ref.1 Ref.3 Ref.6 Ref.8 Ref.33
Corresponds to variant rs6032 [ dbSNP | Ensembl ].
VAR_013890
Natural variant9691N → S. Ref.3
Corresponds to variant rs9332604 [ dbSNP | Ensembl ].
VAR_021299
Natural variant9801R → L. Ref.3
Corresponds to variant rs9332605 [ dbSNP | Ensembl ].
VAR_021300
Natural variant11461H → Q. Ref.3 Ref.33
Corresponds to variant rs6005 [ dbSNP | Ensembl ].
VAR_013891
Natural variant12851L → I. Ref.3 Ref.6 Ref.28
Corresponds to variant rs1046712 [ dbSNP | Ensembl ].
VAR_013892
Natural variant13271H → R. Ref.28 Ref.35
Corresponds to variant rs1800595 [ dbSNP | Ensembl ].
VAR_013893
Natural variant13971L → F. Ref.1 Ref.8
Corresponds to variant rs13306334 [ dbSNP | Ensembl ].
VAR_047741
Natural variant14041P → S. Ref.3
Corresponds to variant rs9332608 [ dbSNP | Ensembl ].
VAR_021301
Natural variant15301E → A. Ref.3 Ref.33
Corresponds to variant rs6007 [ dbSNP | Ensembl ].
VAR_013894
Natural variant16851T → S. Ref.33
Corresponds to variant rs6011 [ dbSNP | Ensembl ].
VAR_013895
Natural variant17301Y → C in FA5D; Seoul 2. Ref.35 Ref.36
VAR_032700
Natural variant17491L → V. Ref.33
Corresponds to variant rs6034 [ dbSNP | Ensembl ].
VAR_013896
Natural variant17641M → V. Ref.1 Ref.26 Ref.33
Corresponds to variant rs6030 [ dbSNP | Ensembl ].
VAR_013897
Natural variant18201M → I. Ref.33
Corresponds to variant rs6026 [ dbSNP | Ensembl ].
VAR_013898
Natural variant21021R → C in FA5D; impairs both factor V secretion and activity. Ref.38
VAR_032701
Natural variant21021R → H in THPH2. Ref.37
VAR_017329
Natural variant21481M → T. Ref.3
Corresponds to variant rs9332701 [ dbSNP | Ensembl ].
VAR_021302
Natural variant21851K → R.
Corresponds to variant rs6679078 [ dbSNP | Ensembl ].
VAR_034603
Natural variant22221D → G. Ref.33
Corresponds to variant rs6027 [ dbSNP | Ensembl ].
VAR_013899

Experimental info

Sequence conflict7411N → S in ABD23003. Ref.7
Sequence conflict9081E → K in AAA52424. Ref.1
Sequence conflict9081E → K in CAC82573. Ref.8
Sequence conflict9911K → E in BAF84302. Ref.5
Sequence conflict22131A → T in AAA52424. Ref.1

Secondary structure

............................. 2224
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12259 [UniParc].

Last modified October 5, 2010. Version 4.
Checksum: 24AEF3FEA7332E37

FASTA2,224251,703
        10         20         30         40         50         60 
MFPGCPRLWV LVVLGTSWVG WGSQGTEAAQ LRQFYVAAQG ISWSYRPEPT NSSLNLSVTS 

        70         80         90        100        110        120 
FKKIVYREYE PYFKKEKPQS TISGLLGPTL YAEVGDIIKV HFKNKADKPL SIHPQGIRYS 

       130        140        150        160        170        180 
KLSEGASYLD HTFPAEKMDD AVAPGREYTY EWSISEDSGP THDDPPCLTH IYYSHENLIE 

       190        200        210        220        230        240 
DFNSGLIGPL LICKKGTLTE GGTQKTFDKQ IVLLFAVFDE SKSWSQSSSL MYTVNGYVNG 

       250        260        270        280        290        300 
TMPDITVCAH DHISWHLLGM SSGPELFSIH FNGQVLEQNH HKVSAITLVS ATSTTANMTV 

       310        320        330        340        350        360 
GPEGKWIISS LTPKHLQAGM QAYIDIKNCP KKTRNLKKIT REQRRHMKRW EYFIAAEEVI 

       370        380        390        400        410        420 
WDYAPVIPAN MDKKYRSQHL DNFSNQIGKH YKKVMYTQYE DESFTKHTVN PNMKEDGILG 

       430        440        450        460        470        480 
PIIRAQVRDT LKIVFKNMAS RPYSIYPHGV TFSPYEDEVN SSFTSGRNNT MIRAVQPGET 

       490        500        510        520        530        540 
YTYKWNILEF DEPTENDAQC LTRPYYSDVD IMRDIASGLI GLLLICKSRS LDRRGIQRAA 

       550        560        570        580        590        600 
DIEQQAVFAV FDENKSWYLE DNINKFCENP DEVKRDDPKF YESNIMSTIN GYVPESITTL 

       610        620        630        640        650        660 
GFCFDDTVQW HFCSVGTQNE ILTIHFTGHS FIYGKRHEDT LTLFPMRGES VTVTMDNVGT 

       670        680        690        700        710        720 
WMLTSMNSSP RSKKLRLKFR DVKCIPDDDE DSYEIFEPPE STVMATRKMH DRLEPEDEES 

       730        740        750        760        770        780 
DADYDYQNRL AAALGIRSFR NSSLNQEEEE FNLTALALEN GTEFVSSNTD IIVGSNYSSP 

       790        800        810        820        830        840 
SNISKFTVNN LAEPQKAPSH QQATTAGSPL RHLIGKNSVL NSSTAEHSSP YSEDPIEDPL 

       850        860        870        880        890        900 
QPDVTGIRLL SLGAGEFKSQ EHAKHKGPKV ERDQAAKHRF SWMKLLAHKV GRHLSQDTGS 

       910        920        930        940        950        960 
PSGMRPWEDL PSQDTGSPSR MRPWKDPPSD LLLLKQSNSS KILVGRWHLA SEKGSYEIIQ 

       970        980        990       1000       1010       1020 
DTDEDTAVNN WLISPQNASR AWGESTPLAN KPGKQSGHPK FPRVRHKSLQ VRQDGGKSRL 

      1030       1040       1050       1060       1070       1080 
KKSQFLIKTR KKKKEKHTHH APLSPRTFHP LRSEAYNTFS ERRLKHSLVL HKSNETSLPT 

      1090       1100       1110       1120       1130       1140 
DLNQTLPSMD FGWIASLPDH NQNSSNDTGQ ASCPPGLYQT VPPEEHYQTF PIQDPDQMHS 

      1150       1160       1170       1180       1190       1200 
TSDPSHRSSS PELSEMLEYD RSHKSFPTDI SQMSPSSEHE VWQTVISPDL SQVTLSPELS 

      1210       1220       1230       1240       1250       1260 
QTNLSPDLSH TTLSPELIQR NLSPALGQMP ISPDLSHTTL SPDLSHTTLS LDLSQTNLSP 

      1270       1280       1290       1300       1310       1320 
ELSQTNLSPA LGQMPLSPDL SHTTLSLDFS QTNLSPELSH MTLSPELSQT NLSPALGQMP 

      1330       1340       1350       1360       1370       1380 
ISPDLSHTTL SLDFSQTNLS PELSQTNLSP ALGQMPLSPD PSHTTLSLDL SQTNLSPELS 

      1390       1400       1410       1420       1430       1440 
QTNLSPDLSE MPLFADLSQI PLTPDLDQMT LSPDLGETDL SPNFGQMSLS PDLSQVTLSP 

      1450       1460       1470       1480       1490       1500 
DISDTTLLPD LSQISPPPDL DQIFYPSESS QSLLLQEFNE SFPYPDLGQM PSPSSPTLND 

      1510       1520       1530       1540       1550       1560 
TFLSKEFNPL VIVGLSKDGT DYIEIIPKEE VQSSEDDYAE IDYVPYDDPY KTDVRTNINS 

      1570       1580       1590       1600       1610       1620 
SRDPDNIAAW YLRSNNGNRR NYYIAAEEIS WDYSEFVQRE TDIEDSDDIP EDTTYKKVVF 

      1630       1640       1650       1660       1670       1680 
RKYLDSTFTK RDPRGEYEEH LGILGPIIRA EVDDVIQVRF KNLASRPYSL HAHGLSYEKS 

      1690       1700       1710       1720       1730       1740 
SEGKTYEDDS PEWFKEDNAV QPNSSYTYVW HATERSGPES PGSACRAWAY YSAVNPEKDI 

      1750       1760       1770       1780       1790       1800 
HSGLIGPLLI CQKGILHKDS NMPMDMREFV LLFMTFDEKK SWYYEKKSRS SWRLTSSEMK 

      1810       1820       1830       1840       1850       1860 
KSHEFHAING MIYSLPGLKM YEQEWVRLHL LNIGGSQDIH VVHFHGQTLL ENGNKQHQLG 

      1870       1880       1890       1900       1910       1920 
VWPLLPGSFK TLEMKASKPG WWLLNTEVGE NQRAGMQTPF LIMDRDCRMP MGLSTGIISD 

      1930       1940       1950       1960       1970       1980 
SQIKASEFLG YWEPRLARLN NGGSYNAWSV EKLAAEFASK PWIQVDMQKE VIITGIQTQG 

      1990       2000       2010       2020       2030       2040 
AKHYLKSCYT TEFYVAYSSN QINWQIFKGN STRNVMYFNG NSDASTIKEN QFDPPIVARY 

      2050       2060       2070       2080       2090       2100 
IRISPTRAYN RPTLRLELQG CEVNGCSTPL GMENGKIENK QITASSFKKS WWGDYWEPFR 

      2110       2120       2130       2140       2150       2160 
ARLNAQGRVN AWQAKANNNK QWLEIDLLKI KKITAIITQG CKSLSSEMYV KSYTIHYSEQ 

      2170       2180       2190       2200       2210       2220 
GVEWKPYRLK SSMVDKIFEG NTNTKGHVKN FFNPPIISRF IRVIPKTWNQ SIALRLELFG 


CDIY 

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References

« Hide 'large scale' references
[1]"Complete cDNA and derived amino acid sequence of human factor V."
Jenny R.J., Pittman D.D., Toole J.J., Kriz R.W., Aldape R.A., Hewick R.M., Kaufman R.J., Mann K.G.
Proc. Natl. Acad. Sci. U.S.A. 84:4846-4850(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ARG-858; ARG-865; GLU-925; PHE-1397 AND VAL-1764.
[2]"Structure of the gene for human coagulation factor V."
Cripe L.D., Moore K.D., Kane W.H.
Biochemistry 31:3777-3785(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]SeattleSNPs variation discovery resource
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEIDEN GLN-534, VARIANTS SER-15; HIS-107; THR-413; LYS-513; SER-809; THR-817; ARG-858; ARG-865; SER-915; GLU-925; SER-969; LEU-980; GLN-1146; ILE-1285; SER-1404; ALA-1530 AND THR-2148.
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , 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. expand/collapse author list , 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]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[24]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-640, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[25]"Crystal structures of the membrane-binding C2 domain of human coagulation factor V."
Macedo-Ribeiro S., Bode W., Huber R., Quinn-Allen M.A., Kim S.W., Ortel T.L., Bourenkov G.P., Bartunik H.D., Stubbs M.T., Kane W.H., Fuentes-Prior P.
Nature 402:434-439(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2065-2224.
[26]"A polymorphism in the human coagulation factor V gene."
Bayston T.A., Ireland H., Olds R.J., Thein S.L., Lane D.A.
Hum. Mol. Genet. 3:2085-2085(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VAL-1764.
[27]"Mutation in blood coagulation factor V associated with resistance to activated protein C."
Bertina R.M., Koeleman B.P.C., Koster T., Rosendaal F.R., Dirven R.J., de Ronde H., van der Velden P.A., Reitsma P.H.
Nature 369:64-67(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LEIDEN GLN-534.
[28]"Detection of new polymorphic markers in the factor V gene: association with factor V levels in plasma."
Lunghi B., Iacoviello L., Gemmati D., Dilasio M.G., Castoldi E., Pinotti M., Castaman G., Redaelli R., Mariani G., Marchetti G., Bernardi F.
Thromb. Haemost. 75:45-48(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ILE-1285 AND ARG-1327.
[29]"Prevalence of the factor V Leiden mutation in hepatic and portal vein thrombosis."
Mahmoud A.E.A., Elias E., Beauchamp N., Wilde J.T.
Gut 40:798-800(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION OF VARIANT LEIDEN GLN-534 WITH SUSCEPTIBILITY TO BUDD-CHIARI SYNDROME.
[30]"A novel mutation of Arg306 of factor V gene in Hong Kong Chinese."
Chan W.P., Lee C.K., Kwong Y.L., Lam C.K., Liang R.
Blood 91:1135-1139(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HONG KONG GLY-334, VARIANT LYS-513.
[31]"Factor V Cambridge: a new mutation (Arg306-to-Thr) associated with resistance to activated protein C."
Williamson D., Brown K., Luddington R., Baglin C., Baglin T.
Blood 91:1140-1144(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT THPH2 THR-334.
[32]"Clinical significance of Arg306 mutations of factor V gene."
Liang R., Lee C.K., Wat M.S., Kwong Y.L., Lam C.K., Liu H.W.
Blood 92:2599-2600(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HONG KONG GLY-334.
[33]"Characterization of single-nucleotide polymorphisms in coding regions of human genes."
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LEIDEN GLN-534, VARIANTS HIS-107; THR-413; LYS-513; SER-809; THR-817; ARG-858; ARG-865; GLU-925; GLN-1146; ALA-1530; SER-1685; VAL-1749; VAL-1764; ILE-1820 AND GLY-2222.
[34]Erratum
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 23:373-373(1999)
[35]"Combinations of 4 mutations (FV R506Q, FV H1299R, FV Y1702C, PT 20210G/A) affecting the prothrombinase complex in a thrombophilic family."
Castoldi E., Simioni P., Kalafatis M., Lunghi B., Tormene D., Girelli D., Girolami A., Bernardi F.
Blood 96:1443-1448(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FA5D CYS-1730, VARIANT LEIDEN GLN-534, VARIANT ARG-1327.
[36]"Five novel mutations in the gene for human blood coagulation factor V associated with type I factor V deficiency."
van Wijk R., Nieuwenhuis K., van den Berg M., Huizinga E.G., van der Meijden B.B., Kraaijenhagen R.J., van Solinge W.W.
Blood 98:358-367(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS THPH2 ARG-613 AND CYS-1730.
[37]"Novel factor V C2-domain mutation (R2074H) in two families with factor V deficiency and bleeding."
Schrijver I., Houissa-Kastally R., Jones C.D., Garcia K.C., Zehnder J.L.
Thromb. Haemost. 87:294-299(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT THPH2 HIS-2102.
[38]"Arg2074Cys missense mutation in the C2 domain of factor V causing moderately severe factor V deficiency: molecular characterization by expression of the recombinant protein."
Duga S., Montefusco M.C., Asselta R., Malcovati M., Peyvandi F., Santagostino E., Mannucci P.M., Tenchini M.L.
Blood 101:173-177(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FA5D CYS-2102, CHARACTERIZATION OF VARIANT FA5D CYS-2102.
[39]"Factor V I359T: a novel mutation associated with thrombosis and resistance to activated protein C."
Mumford A.D., McVey J.H., Morse C.V., Gomez K., Steen M., Norstrom E.A., Tuddenham E.G.D., Dahlback B., Bolton-Maggs P.H.B.
Br. J. Haematol. 123:496-501(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT THPH2 THR-387.
[40]"Meta-analysis of genetic studies in ischemic stroke: thirty-two genes involving approximately 18,000 cases and 58,000 controls."
Casas J.P., Hingorani A.D., Bautista L.E., Sharma P.
Arch. Neurol. 61:1652-1661(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION OF VARIANT GLN-534 WITH SUSCEPTIBILITY TO ISCHSTR.
[41]"Functional characterization of factor V-Ile359Thr: a novel mutation associated with thrombosis."
Steen M., Norstroem E.A., Tholander A.-L., Bolton-Maggs P.H.B., Mumford A., McVey J.H., Tuddenham E.G.D., Dahlbaeck B.
Blood 103:3381-3387(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT THPH2 THR-387.
[42]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-775.
+Additional computationally mapped references.

Web resources

Wikipedia

Factor V entry

SeattleSNPs
SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M16967 mRNA. Translation: AAA52424.1.
L32779 expand/collapse EMBL AC list , 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.
CCDSCCDS1281.1.
PIRKFHU5. A56172.
RefSeqNP_000121.2. NM_000130.4.
UniGeneHs.30054.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP12259.
SMRP12259. Positions 1575-2224.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108452. 6 interactions.
DIPDIP-47331N.
STRING9606.ENSP00000356771.

Chemistry

BindingDBP12259.
ChEMBLCHEMBL3618.
DrugBankDB00055. Drotrecogin alfa.
GuidetoPHARMACOLOGY2606.

PTM databases

PhosphoSiteP12259.

Polymorphism databases

DMDM308153653.

Proteomic databases

MaxQBP12259.
PaxDbP12259.
PRIDEP12259.

Protocols and materials databases

DNASU2153.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367796; ENSP00000356770; ENSG00000198734.
ENST00000367797; ENSP00000356771; ENSG00000198734.
GeneID2153.
KEGGhsa:2153.
UCSCuc001ggg.1. human.

Organism-specific databases

CTD2153.
GeneCardsGC01M169481.
GeneReviewsF5.
HGNCHGNC:3542. F5.
HPAHPA002036.
MIM188055. phenotype.
227400. phenotype.
600880. phenotype.
601367. phenotype.
612309. gene.
614389. phenotype.
neXtProtNX_P12259.
Orphanet131. Budd-Chiari syndrome.
329217. Cerebral sinovenous thrombosis.
326. Congenital factor V deficiency.
391320. East Texas bleeding disorder.
64738. Non rare thrombophilia.
PharmGKBPA159.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG240444.
HOVERGENHBG005631.
KOK03902.
OrthoDBEOG7ZWD1D.
PhylomeDBP12259.
TreeFamTF329807.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressP12259.
BgeeP12259.
CleanExHS_F5.
GenevestigatorP12259.

Family and domain databases

Gene3D2.60.120.260. 2 hits.
2.60.40.420. 6 hits.
InterProIPR000421. 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]
PfamPF07732. Cu-oxidase_3. 2 hits.
PF00754. F5_F8_type_C. 2 hits.
[Graphical view]
PIRSFPIRSF000354. Factors_V_VIII. 1 hit.
SMARTSM00231. FA58C. 2 hits.
[Graphical view]
SUPFAMSSF49503. SSF49503. 6 hits.
SSF49785. SSF49785. 2 hits.
PROSITEPS01285. FA58C_1. 2 hits.
PS01286. FA58C_2. 2 hits.
PS50022. FA58C_3. 2 hits.
PS00079. MULTICOPPER_OXIDASE1. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP12259.
GeneWikiFactor_V.
GenomeRNAi2153.
NextBio8701.
PROP12259.
SOURCESearch...

Entry information

Entry nameFA5_HUMAN
AccessionPrimary (citable) accession number: P12259
Secondary accession number(s): A8K6E8 expand/collapse secondary AC list , Q14285, Q2EHR5, Q5R346, Q5R347, Q6UPU6, Q8WWQ6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 5, 2010
Last modified: July 9, 2014
This is version 181 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM