F9
entrez
2158
canonical
uniprot
P00740
canonical
ensembl
ENSG00000101981
resolver
ensp
ENSP00000218099
resolver
ensp
ENSP00000377650
resolver
genesymbol
F9
resolver
hgnc
HGNC:3551
resolver
uniprot
A8K9N4
resolver
uniprot
F2RM36
resolver
uniprot
Q5FBE1
resolver
uniprot
Q5JYJ8
resolver
uniprot_entry
FA9_HUMAN
resolver
uniprot_sec
A8K9N4
resolver
uniprot_sec
F2RM36
resolver
uniprot_sec
Q5FBE1
resolver
uniprot_sec
Q5JYJ8
resolver
amino_acid_sequence
MQRVNMIMAESPGLITICLLGYLLSAECTVFLDHENANKILNRPKRYNSGKLEEFVQGNLERECMEEKCSFEEAREVFENTERTTEFWKQYVDGDQCESNPCLNGGSCKDDINSYECWCPFGFEGKNCELDVTCNIKNGRCEQFCKNSADNKVVCSCTEGYRLAENQKSCEPAVPFPCGRVSVSQTSKLTRAETVFPDVDYVNSTEAETILDNITQSTQSFNDFTRVVGGEDAKPGQFPWQVVLNGKVDAFCGGSIVNEKWIVTAAHCVETGVKITVVAGEHNIEETEHTEQKRNVIRIIPHHNYNAAINKYNHDIALLELDEPLVLNSYVTPICIADKEYTNIFLKFGSGYVSGWGRVFHKGRSALVLQYLRVPLVDRATCLRSTKFTIYNNMFCAGFHEGGRDSCQGDSGGPHVTEVEGTSFLTGIISWGEECAMKGKYGIYTKVSRYVNWIKEKTKLT
uniprot
proteins
disease_involvement
DISEASE: Hemophilia B (HEMB) [MIM:306900]: An X-linked blood coagulation disorder characterized by a permanent tendency to hemorrhage, due to factor IX deficiency. It is phenotypically similar to hemophilia A, but patients present with fewer symptoms. Many patients are asymptomatic until the hemostatic system is stressed by surgery or trauma. {ECO:0000269|PubMed:10094553, ECO:0000269|PubMed:10698280, ECO:0000269|PubMed:11122099, ECO:0000269|PubMed:12588353, ECO:0000269|PubMed:12604421, ECO:0000269|PubMed:1346077, ECO:0000269|PubMed:1346975, ECO:0000269|PubMed:1615485, ECO:0000269|PubMed:1680287, ECO:0000269|PubMed:1902289, ECO:0000269|PubMed:1958666, ECO:0000269|PubMed:2162822, ECO:0000269|PubMed:2306516, ECO:0000269|PubMed:2339358, ECO:0000269|PubMed:2372509, ECO:0000269|PubMed:2472424, ECO:0000269|PubMed:25251685, ECO:0000269|PubMed:25470321, ECO:0000269|PubMed:2592373, ECO:0000269|PubMed:2713493, ECO:0000269|PubMed:2714791, ECO:0000269|PubMed:2738071, ECO:0000269|PubMed:2753873, ECO:0000269|PubMed:2773937, ECO:0000269|PubMed:2775660, ECO:0000269|PubMed:3009023, ECO:0000269|PubMed:3243764, ECO:0000269|PubMed:3401602, ECO:0000269|PubMed:3790720, ECO:0000269|PubMed:6603618, ECO:0000269|PubMed:7937052, ECO:0000269|PubMed:7981722, ECO:0000269|PubMed:8076946, ECO:0000269|PubMed:8199596, ECO:0000269|PubMed:8257988, ECO:0000269|PubMed:8295821, ECO:0000269|PubMed:8680410, ECO:0000269|PubMed:9169594, ECO:0000269|PubMed:9222764, ECO:0000269|PubMed:9452115, ECO:0000269|PubMed:9590153, ECO:0000269|PubMed:9600455}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Note=Mutations in position 43 (Oxford-3, San Dimas) and 46 (Cambridge) prevents cleavage of the propeptide (PubMed:12588353, PubMed:25251685, PubMed:2738071, PubMed:3009023, PubMed:8295821, PubMed:9169594, PubMed:9600455). Mutation in position 93 (Alabama) probably fails to bind to cell membranes (PubMed:3790720). Mutation in position 191 (Chapel-Hill) or in position 226 (Nagoya or Hilo) prevent cleavage of the activation peptide (PubMed:12588353, PubMed:2162822, PubMed:25251685, PubMed:2713493, PubMed:6603618, PubMed:8076946). {ECO:0000269|PubMed:12588353, ECO:0000269|PubMed:2162822, ECO:0000269|PubMed:25251685, ECO:0000269|PubMed:2713493, ECO:0000269|PubMed:2738071, ECO:0000269|PubMed:3009023, ECO:0000269|PubMed:3790720, ECO:0000269|PubMed:6603618, ECO:0000269|PubMed:8076946, ECO:0000269|PubMed:8295821, ECO:0000269|PubMed:9169594, ECO:0000269|PubMed:9600455}.; DISEASE: Thrombophilia, X-linked, due to factor IX defect (THPH8) [MIM:300807]: A hemostatic disorder characterized by a tendency to thrombosis. {ECO:0000269|PubMed:19846852}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Warfarin sensitivity, X-linked (WARFS) [MIM:301052]: A condition characterized by sensitivity to warfarin, a drugs used as anti-coagulants for the prevention of thromboembolic diseases in subjects with deep vein thrombosis, atrial fibrillation, or mechanical heart valve replacement. Warfarin sensitive individuals develop bleeding complications when they are given warfarin within the therapeutic ranges. {ECO:0000269|PubMed:29450643, ECO:0000269|PubMed:8833911, ECO:0000269|PubMed:9233593}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.4.21.22
uniprot
proteins
function
FUNCTION: Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa (PubMed:8295821, PubMed:2592373, PubMed:20121197, PubMed:20121198, PubMed:1730085, PubMed:19846852, PubMed:39880037). {ECO:0000269|PubMed:1730085, ECO:0000269|PubMed:19846852, ECO:0000269|PubMed:20121197, ECO:0000269|PubMed:20121198, ECO:0000269|PubMed:2592373, ECO:0000269|PubMed:39880037, ECO:0000269|PubMed:8295821}.
uniprot
proteins
mass_dalton
51778
uniprot
proteins
mutagenesis
MUTAGEN 305; /note="Y->F: Strongly increases enzyme activity with a synthetic peptide substrate; when associated with T-311; A-365 and T-391."; /evidence="ECO:0000269|PubMed:12444082"; MUTAGEN 311; /note="K->T: Strongly increases enzyme activity with a synthetic peptide substrate; when associated with F-305; A-365 and T-391."; /evidence="ECO:0000269|PubMed:12444082"; MUTAGEN 312; /note="Y->A: Strongly decreases enzyme activity with a synthetic peptide substrate."; /evidence="ECO:0000269|PubMed:12444082"; MUTAGEN 391; /note="Y->T: Strongly increases enzyme activity with a synthetic peptide substrate; when associated with F-305; T-311 and A-365."; /evidence="ECO:0000269|PubMed:12444082
uniprot
proteins
post_translational_modification
PTM: Activated by factor XIa, which excises the activation peptide (PubMed:1730085, PubMed:9169594, PubMed:22961984). The propeptide can also be removed by snake venom protease (PubMed:20004170, PubMed:20080729). Activated by coagulation factor VIIa-tissue factor (F7-F3) complex in calcium-dependent manner (PubMed:271951). {ECO:0000269|PubMed:1730085, ECO:0000269|PubMed:20004170, ECO:0000269|PubMed:20080729, ECO:0000269|PubMed:22961984, ECO:0000269|PubMed:2592373, ECO:0000269|PubMed:271951, ECO:0000269|PubMed:8295821, ECO:0000269|PubMed:9169594}.; PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000269|PubMed:6688526}.; PTM: Predominantly O-glucosylated at Ser-99 by POGLUT1 in vitro. {ECO:0000269|PubMed:2129367, ECO:0000269|PubMed:2511201, ECO:0000269|PubMed:25456591}.; PTM: Carboxylated by vitamin K-dependent GGCX to form gamma-carboxyglutamate; these residues are essential for the binding of calcium. {ECO:0000269|PubMed:39880037}.
uniprot
proteins
protein_family
Peptidase S1 family
uniprot
proteins
pubmed
10094553
uniprot
proteins
pubmed
10391209
uniprot
proteins
pubmed
10467148
uniprot
proteins
pubmed
10692472
uniprot
proteins
pubmed
10698280
uniprot
proteins
pubmed
11122099
uniprot
proteins
pubmed
11133752
uniprot
proteins
pubmed
12444082
uniprot
proteins
pubmed
12588353
uniprot
proteins
pubmed
12604421
uniprot
proteins
pubmed
1304885
uniprot
proteins
pubmed
1346077
uniprot
proteins
pubmed
1346975
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14722079
uniprot
proteins
pubmed
1517205
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
1615485
uniprot
proteins
pubmed
1634040
uniprot
proteins
pubmed
1680287
uniprot
proteins
pubmed
1730085
uniprot
proteins
pubmed
1854745
uniprot
proteins
pubmed
1902289
uniprot
proteins
pubmed
1958666
uniprot
proteins
pubmed
19846852
uniprot
proteins
pubmed
20004170
uniprot
proteins
pubmed
20080729
uniprot
proteins
pubmed
20121197
uniprot
proteins
pubmed
20121198
uniprot
proteins
pubmed
2129367
uniprot
proteins
pubmed
2162822
uniprot
proteins
pubmed
22961984
uniprot
proteins
pubmed
2306516
uniprot
proteins
pubmed
2339358
uniprot
proteins
pubmed
2372509
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
2472424
uniprot
proteins
pubmed
2511201
uniprot
proteins
pubmed
25251685
uniprot
proteins
pubmed
25456591
uniprot
proteins
pubmed
25470321
uniprot
proteins
pubmed
2592373
uniprot
proteins
pubmed
2713493
uniprot
proteins
pubmed
2714791
uniprot
proteins
pubmed
271951
uniprot
proteins
pubmed
2738071
uniprot
proteins
pubmed
2743975
uniprot
proteins
pubmed
2753873
uniprot
proteins
pubmed
2773937
uniprot
proteins
pubmed
2775660
uniprot
proteins
pubmed
29450643
uniprot
proteins
pubmed
2994716
uniprot
proteins
pubmed
3009023
uniprot
proteins
pubmed
3243764
uniprot
proteins
pubmed
3340835
uniprot
proteins
pubmed
3401602
uniprot
proteins
pubmed
34502392
uniprot
proteins
pubmed
3790720
uniprot
proteins
pubmed
3857619
uniprot
proteins
pubmed
39362926
uniprot
proteins
pubmed
39880037
uniprot
proteins
pubmed
6089357
uniprot
proteins
pubmed
6329734
uniprot
proteins
pubmed
6425296
uniprot
proteins
pubmed
659613
uniprot
proteins
pubmed
6603618
uniprot
proteins
pubmed
6687940
uniprot
proteins
pubmed
6688526
uniprot
proteins
pubmed
6959130
uniprot
proteins
pubmed
7547952
uniprot
proteins
pubmed
7606779
uniprot
proteins
pubmed
7713897
uniprot
proteins
pubmed
7937052
uniprot
proteins
pubmed
7981722
uniprot
proteins
pubmed
8076946
uniprot
proteins
pubmed
8172892
uniprot
proteins
pubmed
8199596
uniprot
proteins
pubmed
8236150
uniprot
proteins
pubmed
8257988
uniprot
proteins
pubmed
8295821
uniprot
proteins
pubmed
8392713
uniprot
proteins
pubmed
8663165
uniprot
proteins
pubmed
8680410
uniprot
proteins
pubmed
8833911
uniprot
proteins
pubmed
9047312
uniprot
proteins
pubmed
9169594
uniprot
proteins
pubmed
9222764
uniprot
proteins
pubmed
9233593
uniprot
proteins
pubmed
9452115
uniprot
proteins
pubmed
9590153
uniprot
proteins
pubmed
9600455
uniprot
proteins
sequence_length
461
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19846852, ECO:0000269|PubMed:2592373, ECO:0000269|PubMed:3857619, ECO:0000269|PubMed:8295821, ECO:0000269|PubMed:9169594}.
uniprot
proteins