F11
entrez
2160
canonical
uniprot
P03951
canonical
ensembl
ENSG00000088926
resolver
ensp
ENSP00000384957
resolver
ensp
ENSP00000424479
resolver
ensp
ENSP00000556400
resolver
ensp
ENSP00000556401
resolver
ensp
ENSP00000556403
resolver
ensp
ENSP00000556416
resolver
ensp
ENSP00000556417
resolver
ensp
ENSP00000645479
resolver
ensp
ENSP00000645480
resolver
enst
ENST00000492972
resolver
genesymbol
F11
resolver
hgnc
HGNC:3529
resolver
uniprot
D3DP64
resolver
uniprot
D6RB32
resolver
uniprot
Q4W5C2
resolver
uniprot
Q9Y495
resolver
uniprot_entry
D6RB32_HUMAN
resolver
uniprot_entry
FA11_HUMAN
resolver
uniprot_sec
D3DP64
resolver
uniprot_sec
Q4W5C2
resolver
uniprot_sec
Q9Y495
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by SERPINA5. {ECO:0000269|PubMed:2844223}.
uniprot
proteins
amino_acid_sequence
MIFLYQVVHFILFTSVSGECVTQLLKDTCFEGGDITTVFTPSAKYCQVVCTYHPRCLLFTFTAESPSEDPTRWFTCVLKDSVTETLPRVNRTAAISGYSFKQCSHQISACNKDIYVDLDMKGINYNSSVAKSAQECQERCTDDVHCHFFTYATRQFPSLEHRNICLLKHTQTGTPTRITKLDKVVSGFSLKSCALSNLACIRDIFPNTVFADSNIDSVMAPDAFVCGRICTHHPGCLFFTFFSQEWPKESQRNLCLLKTSESGLPSTRIKKSKALSGFSLQSCRHSIPVFCHSSFYHDTDFLGEELDIVAAKSHEACQKLCTNAVRCQFFTYTPAQASCNEGKGKCYLKLSSNGSPTKILHGRGGISGYTLRLCKMDNECTTKIKPRIVGGTASVRGEWPWQVTLHTTSPTQRHLCGGSIIGNQWILTAAHCFYGVESPKILRVYSGILNQSEIKEDTSFFGVQEIIIHDQYKMAESGYDIALLKLETTVNYTDSQRPICLPSKGDRNVIYTDCWVTGWGYRKLRDKIQNTLQKAKIPLVTNEECQKRYRGHKITHKMICAGYREGGKDACKGDSGGPLSCKHNEVWHLVGITSWGEGCAQRERPGVYTNVVEYVDWILEKTQAV
uniprot
proteins
disease_involvement
DISEASE: Factor XI deficiency (FA11D) [MIM:612416]: A hemorrhagic disease characterized by reduced levels and activity of factor XI resulting in moderate bleeding symptoms, usually occurring after trauma or surgery. Patients usually do not present spontaneous bleeding but women can present with menorrhagia. Hemorrhages are usually moderate. {ECO:0000269|PubMed:10027710, ECO:0000269|PubMed:10606881, ECO:0000269|PubMed:11895778, ECO:0000269|PubMed:15026311, ECO:0000269|PubMed:15180874, ECO:0000269|PubMed:1547342, ECO:0000269|PubMed:15953011, ECO:0000269|PubMed:16607084, ECO:0000269|PubMed:18005151, ECO:0000269|PubMed:21457405, ECO:0000269|PubMed:21668437, ECO:0000269|PubMed:21999818, ECO:0000269|PubMed:22016685, ECO:0000269|PubMed:22159456, ECO:0000269|PubMed:22322133, ECO:0000269|PubMed:25158988, ECO:0000269|PubMed:2813350, ECO:0000269|PubMed:7669672, ECO:0000269|PubMed:7888672, ECO:0000269|PubMed:9401068, ECO:0000269|PubMed:9787168}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.4.21.27
uniprot
proteins
function
FUNCTION: Factor XI triggers the middle phase of the intrinsic pathway of blood coagulation by activating factor IX. {ECO:0000269|PubMed:22961984}.
uniprot
proteins
mass_dalton
70109
uniprot
proteins
mutagenesis
MUTAGEN 302; /note="L->A: Reduces dimerization. Abolishes dimerization; when associated with A-308."; /evidence="ECO:0000269|PubMed:19548906"; MUTAGEN 308; /note="I->A: Reduces dimerization. Abolishes dimerization; when associated with A-302."; /evidence="ECO:0000269|PubMed:19548906"; MUTAGEN 344; /note="G->C: Abolishes dimerization."; /evidence="ECO:0000269|PubMed:19548906"; MUTAGEN 347; /note="Y->A: Reduces dimerization."; /evidence="ECO:0000269|PubMed:19548906
uniprot
proteins
post_translational_modification
PTM: N-glycosylated on both chains. N-glycosylated sites mainly consist of nonfucosylated sialylated biantennary (in high abundance) and/or triantennary (in low abundance) complex structures. Glycosylation at Asn-163 uses a rare non-canonical Asn-X-Cys glycosite. {ECO:0000269|PubMed:25092234}.; PTM: Activated by factor XIIa (or XII), which cleaves each polypeptide after Arg-387 into the light chain, which contains the active site, and the heavy chain, which associates with high molecular weight (HMW) kininogen. Activated by F12 (activated); the presence of negatively charged surfaces accelerates activation (PubMed:2019570, PubMed:8427954). Activated by F2 (thrombin); the presence of negatively charged surfaces, such as polyphosphate and dextran sulfate, strongly accelerates activation (PubMed:2019570, PubMed:21976677). Autoactivated; the presence of negatively charged surfaces, such as polyphosphate and dextran sulfate, accelerates autoactivation and autolysis (PubMed:2019570, PubMed:21976677). {ECO:0000269|PubMed:2019570, ECO:0000269|PubMed:21976677, ECO:0000269|PubMed:8427954}.
uniprot
proteins
protein_family
Peptidase S1 family
uniprot
proteins
protein_family
Plasma kallikrein subfamily
uniprot
proteins
pubmed
10027710
uniprot
proteins
pubmed
10391209
uniprot
proteins
pubmed
10606881
uniprot
proteins
pubmed
11412111
uniprot
proteins
pubmed
11895778
uniprot
proteins
pubmed
15026311
uniprot
proteins
pubmed
15180874
uniprot
proteins
pubmed
1547342
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
15953011
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
16607084
uniprot
proteins
pubmed
18005151
uniprot
proteins
pubmed
18510371
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19548906
uniprot
proteins
pubmed
1998667
uniprot
proteins
pubmed
2019570
uniprot
proteins
pubmed
21457405
uniprot
proteins
pubmed
21668437
uniprot
proteins
pubmed
21976677
uniprot
proteins
pubmed
21999818
uniprot
proteins
pubmed
22016685
uniprot
proteins
pubmed
22159456
uniprot
proteins
pubmed
22322133
uniprot
proteins
pubmed
22961984
uniprot
proteins
pubmed
25092234
uniprot
proteins
pubmed
25158988
uniprot
proteins
pubmed
2813350
uniprot
proteins
pubmed
2827746
uniprot
proteins
pubmed
2844223
uniprot
proteins
pubmed
35460690
uniprot
proteins
pubmed
3636155
uniprot
proteins
pubmed
37469515
uniprot
proteins
pubmed
7669672
uniprot
proteins
pubmed
7888672
uniprot
proteins
pubmed
8427954
uniprot
proteins
pubmed
9401068
uniprot
proteins
pubmed
9593722
uniprot
proteins
pubmed
9787168
uniprot
proteins
sequence_length
625
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted.
uniprot
proteins