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Protein Page:
factor V (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
factor V 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. Defects in F5 are the cause of factor V deficiency (FA5D); also known as Owren parahemophilia. It is an hemorrhagic diastesis. Defects in F5 are the cause of thrombophilia due to activated protein C resistance (THPH2). THPH2 is a hemostatic disorder due to defective degradation of factor Va by activated protein C. It is characterized by a poor anticoagulant response to activated protein C resulting in tendency to thrombosis. Defects in F5 are a cause of susceptibility to Budd- Chiari syndrome (BDCHS). 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. Defects in F5 may be a cause of susceptibility to ischemic stroke (ISCHSTR); also known as cerebrovascular accident or cerebral infarction. 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. Defects in F5 are associated with susceptibility to pregnancy loss, recurrent, type 1 (RPRGL1). RPRGL1 is 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. Belongs to the multicopper oxidase family. Note: This description may include information from UniProtKB.
Protein type: Secreted; Protease; Secreted, signal peptide
Cellular Component: extracellular space; membrane; plasma membrane; extracellular region
Molecular Function: protein binding; copper ion binding; serine-type endopeptidase activity
Biological Process: platelet activation; platelet degranulation; blood circulation; proteolysis; cell adhesion; blood coagulation
Reference #:  P12259 (UniProtKB)
Alt. Names/Synonyms: Activated protein C cofactor; Coagulation factor V; coagulation factor V (proaccelerin, labile factor); Coagulation factor V heavy chain; coagulation factor V jinjiang A2 domain; Coagulation factor V light chain; F5; FA5; factor V Leiden; FVL; PCCF; Proaccelerin, labile factor
Gene Symbols: F5
Molecular weight: 251,703 Da
Basal Isoelectric point: 5.68  Predict pI for various phosphorylation states
Select Structure to View Below

factor V

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 Y69 KKIVYREYEPYFKKE
0 1 S284-p EQNHHKVsAITLVSA
0 1 Y323-p LQAGMQAyIDIKNCP
0 1 S517-p DIMRDIAsGLIGLLL
0 1 S528-p GLLLICKsRSLDRRG
0 1 T640-p YGKRHEDtLTLFPMR
0 1 Y693-p PDDDEDSyEIFEPPE
0 1 T706-p PESTVMAtRKMHDRL
2 0 S720-p LEPEDEEsDADYDYQ
0 1 A797 NLAEPQKAPSHQQAt
0 1 T804-ga APSHQQAttAGSPLR
0 1 T805-ga PSHQQAttAGSPLRH
0 1 K864-ac FKSQEHAkHkGPKVE
0 1 K866-ac SQEHAkHkGPKVERD
0 1 T898-p GRHLSQDtGSPSGMR
0 2 P923 GSPSRMRPWKDPPSD
0 1 S937-p DLLLLKQsNSSKILV
0 1 S955-p HLASEKGsYEIIQDT
0 1 T1047-p HAPLSPRtFHPLRsE
0 1 S1053-p RtFHPLRsEAyNtFS
0 1 Y1056-p HPLRsEAyNtFSERR
0 1 T1058-p LRsEAyNtFSERRLK
0 1 S1148-p TSDPSHRsSsPELSE
0 2 S1150-p DPSHRsSsPELSEML
0 1 E1506 NDTFLSKEFNPLVIV
0 1 Y1623-p KKVVFRKyLDstFtK
0 1 S1626-p VFRKyLDstFtKRDP
0 1 T1627-p FRKyLDstFtKRDPR
0 1 T1629-p KyLDstFtKRDPRGE
0 1 S1676-p SLHAHGLsYEKSSEG
0 1 T1685-p EKSSEGKtYEDDsPE
0 1 S1690-p GKtYEDDsPEWFKED
0 1 S1914 CRMPMGLSTGIISDS
0 1 T1915 RMPMGLSTGIISDSQ
0 1 S2011-p WQIFKGNsTRNVMYF
0 1 T2026-p NGNSDAStIKENQFD
0 1 Y2149-p KSLSSEMyVKSYTIH
0 1 Y2153 SEMyVKSYTIHYsEQ
0 1 Y2157 VKSYTIHYsEQGVEW
0 1 S2158-p KSYTIHYsEQGVEWK
0 1 K2170 EWKPYRLKSSMVDKI
0 1 S2198-p FFNPPIIsRFIRVIP
  mouse

 
Y68 KKIVYREYEQYFKKE
S283 EQNQHKVSTVTLVSA
Y322 YQAGMQAYIDIKNCP
S515 DVTRDIASGLIGLLL
S526 GLLLICKSRSLDQRG
T638 YGRRHEDTLTLFPMR
Y692 DYDNEDSYEIYEPPA
T705 PAPTSMTTRRIHDSL
D719 LENEFGIDNEDDDYQ
T794-p NLKDFQRtLPGSGAT
T801 tLPGSGATVAGTLLR
V802 LPGSGATVAGTLLRN
K862 SGNREQDKPKTIKTG
K864 NREQDKPKTIKTGRP
N896 GRHSNPKNSYSGMKs
S903-p NSYSGMKsEEDIPSE
K917 ELIPLKQKITSKFLN
S935 RVASEKGSYEIIAAN
G1030 HSPLSPRGFDPLRGH
G1036 RGFDPLRGHNHSPFP
H1039 DPLRGHNHSPFPDRR
P1041 LRGHNHSPFPDRRLL
S1130 TTDPSYRSSPPELSQ
P1132 DPSYRSSPPELSQGL
K1466-ub NNTSLSRkFNPLVVV
Y1583 KKVVFRKYLDSTFTS
S1586 VFRKYLDSTFTSRDP
T1587 FRKYLDSTFTSRDPR
T1589 KYLDSTFTSRDPRAE
S1636 SLHAHGLSYEKSSEG
T1645 EKSSEGKTYEDESPE
S1650 GKTYEDESPEWFQED
S1873-p CKMPMGLstGVISDS
T1874-p KMPMGLstGVISDSQ
S1970 WQIFRGKSGKSVMYF
T1985 TGNSDGSTIKENRLD
Y2108 KSLSSEMYVKSYSIQ
Y2112 SEMYVKSYSIQYSDQ
Y2116 VKSYSIQYSDQGVAW
S2117 KSYSIQYSDQGVAWK
K2129-ac AWKPYRQkSSMVDKI
S2157 FFNPPIISRFIRIIP
  rat

 
Y68-p KKIVYREyEPYFKKE
S283 EQNQHKVSTVTLVSA
Y322 YQGKKPAYIDIKNCP
D511 VFLTEFSDSLCLCSH
S517 SDSLCLCSHISFIFD
T630 YGRRHEDTLTLFPMS
Y685 DDDDEDSYEIYQPLE
T698 LEPTSMTTRKIHDSV
E712 VENDFGIENEDDDYQ
T787 NLNDSQRTLSGSGAT
T794 TLSGSGATIAGILLG
I795 LSGSGATIAGILLGN
K855 SGSREQTKPKTIKTG
K857 SREQTKPKTIKTGRP
N889 GRHSNPKNTSSRMKS
S896 NTSSRMKSEEDIPSD
K910 DLLLLKQKVASKLLN
S928 HMASEKGSYEIIPAN
G1023 HSPLSPRGFYHPRRE
R1029 RGFYHPRREDHPPLL
H1032 YHPRREDHPPLLDRR
P1034 PRREDHPPLLDRRLL
S1123 TTDPSYRSSPPEPSQ
P1125 DPSYRSSPPEPSQGI
T1462 NDTSLSKTFNPLVVV
Y1579 KKVVFRKYLDSTFTS
S1582 VFRKYLDSTFTSRDP
T1583 FRKYLDSTFTSRDPQ
T1585 KYLDSTFTSRDPQGE
S1632 SLHAHGLSYEKSSEG
N1641 EKSSEGKNYEDDSPK
S1646 GKNYEDDSPKWFQED
S1868 CKMPMGLSTGAISDS
T1869 KMPMGLSTGAISDSQ
S1965 WQIFRGNSMKSVMSF
T1980 AGNSDASTIKENRFD
Y2103 KSLSSEMYVKSySIL
Y2107-p SEMYVKSySILySDQ
Y2111-p VKSySILySDQGVSW
S2112 KSySILySDQGVSWK
K2124 SWKPYRQKSSMVDKI
S2152 FFNPPIISRFIRIIP
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