Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Coagulation factor XI  

UniProtKB / Swiss-Prot ID :  FA11_HUMAN

Gene Name (Synonyms) : 
F11  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Secreted. 

Protein Function :  Factor XI triggers the middle phase of the intrinsic pathway of blood coagulation by activating factor IX. 

Protein Sequence MIFLYQVVHFILFTSVSGECVTQLLKDTCFEGGDITTVFTPSAKYCQVVCTYHPRCLLFTFTAESPSEDP...
Predicted Secondary Structure CHHHHHHHHHHHHHHCCHHHHHHHHHHHHCCCCCEEEEECCCCCEEEEEECCCCCEEEEEEECCCCCCCC...
Protein Variant
LocationDescription
32G -> R (in FA11D). VAR_067929
34D -> H (in FA11D). VAR_012085
43A -> T (in FA11D; dominant-negativemutation that results in severely
46C -> F (in FA11D). VAR_054894
51T -> I (in FA11D). VAR_067931
51T -> P (in FA11D). VAR_067932
53H -> Q (in FA11D). VAR_067933
56C -> R (in FA11D; secretion of the mutantprotein is impaired; dbSNP:rs121965069).
63A -> V (in FA11D). VAR_067934
66P -> L (in dbSNP:rs5968). VAR_011774
101K -> R (in FA11D). VAR_054896
140C -> Y (in FA11D). VAR_067935
151Y -> C (in FA11D). VAR_054897
222D -> Y (in FA11D). VAR_067936
228R -> Q (in FA11D). VAR_067937
241F -> L (in FA11D; dominant-negativemutation that results in severely
244Q -> R (found in a patient with factor XIdeficiency that also carries mutation N-
246W -> C (in FA11D). VAR_012086
252R -> T (in FA11D). VAR_067939
255C -> Y (in FA11D; secretion of the mutantprotein is impaired).
263G -> E (in FA11D). VAR_054899
266S -> N (in FA11D; dbSNP:rs145168351). VAR_012087
270K -> I (in FA11D; although the mutantprotein is synthesized the secretion is
276S -> C (in FA11D). VAR_067940
277G -> D (in FA11D). VAR_067941
301F -> L (in FA11D; dbSNP:rs121965064). VAR_006622
308I -> F (in dbSNP:rs5972). VAR_011776
315E -> K (in FA11D). VAR_067942
320L -> P (in FA11D). VAR_012088
322T -> I (in FA11D). VAR_012089
326R -> C (in FA11D; dbSNP:rs28934608). VAR_012090
331T -> I (in FA11D). VAR_067943
339C -> F (in dbSNP:rs5967). VAR_011777
341E -> K (in FA11D). VAR_012091
360L -> P (in FA11D). VAR_067944
399W -> R (in dbSNP:rs1800439). VAR_011778
401W -> R (in FA11D). VAR_067945
403V -> M (in FA11D; dominant-negativemutation that results in severely
404T -> N (in FA11D; dbSNP:rs121965067). VAR_012092
418G -> V (in FA11D; mutant is not secretedby transfected fibroblasts; dominant-
430A -> V (in FA11D; dbSNP:rs121965068). VAR_012093
454I -> K (in FA11D). VAR_067947
460F -> V (in FA11D; dbSNP:rs121965065). VAR_012094
481I -> S (in FA11D). VAR_067948
493T -> I (in FA11D). VAR_012095
503S -> P (in FA11D). VAR_067949
506D -> G (in FA11D; mild phenotype). VAR_067950
511Y -> H (in FA11D; transfected cellscontain reduced amount of mutant protein
514C -> F (in FA11D). VAR_067951
526D -> E (in FA11D). VAR_067952
538P -> L (in FA11D; dbSNP:rs139695003). VAR_054903
565E -> K (in FA11D). VAR_054904
575S -> L (in FA11D). VAR_067953
587W -> S (in FA11D; mutant is not secretedby transfected fibroblasts; dominant-
594S -> R (in FA11D; dbSNP:rs28934609). VAR_012096
597E -> K (in FA11D). VAR_067954
608Y -> H (in FA11D). VAR_067955
618I -> S (in FA11D). VAR_054906
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
17PhosphoserineFTSVSGECV
HHHCCHHHH
28.74Phosphositeplus
Link-
17Phosphoserine.FTSVSGECV
HHHCCHHHH
28.74UniProtKB
Link-
22PhosphothreonineGECVTQLLK
HHHHHHHHH
25.76Phosphositeplus
Link-
22Phosphothreonine.GECVTQLLK
HHHHHHHHH
25.76UniProtKB
Link-
90N-linked (GlcNAc...).LPRVNRTAA
CCCEEEEEE
36.54UniProtKB
Link-
115PhosphotyrosineNKDIYVDLD
CHHHHCCCC
9.69HPRD
Link-
115PhosphotyrosineNKDIYVDLD
CHHHHCCCC
9.69Phosphositeplus
Link-
115PhosphotyrosineNKDIYVDLD
CHHHHCCCC
9.69SysPTM
Link-
125PhosphotyrosineKGINYNSSV
ECCCCCHHH
17.94HPRD
Link-
125PhosphotyrosineKGINYNSSV
ECCCCCHHH
17.94Phosphositeplus
Link-
125PhosphotyrosineKGINYNSSV
ECCCCCHHH
17.94SysPTM
Link-
126N-linked (Glc...)GINYNSSVA
CCCCCHHHH
24.26HPRD
Link-
126N-linked (GlcNAc...).GINYNSSVA
CCCCCHHHH
24.26UniProtKB
Link-
128PhosphoserineNYNSSVAKS
CCCHHHHHH
23.58HPRD
Link-
128PhosphoserineNYNSSVAKS
CCCHHHHHH
23.58Phosphositeplus
Link-
128PhosphoserineNYNSSVAKS
CCCHHHHHH
23.58SysPTM
Link-
136S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)SAQECQERC
HHHHHHHHC
3.19HPRD
Link-
140S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)CQERCTDDV
HHHHCCCCC
4.88HPRD
Link-
146S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)DDVHCHFFT
CCCEEEEEE
2.77HPRD
Link-
165S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)HRNICLLKH
HCCEEEEEE
4.09HPRD
Link-
353N-linked (GlcNAc...).KLSSNGSPT
EECCCCCCC
52.14UniProtKB
Link-
380S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)MDNECTTKI
CCCCCCCCC
8.00HPRD
Link-
416S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)QRHLCGGSI
CEEEEEEEE
4.79HPRD
Link
432S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)TAAHCFYGV
EEEEECCCC
2.11HPRD
Link
450N-linked (GlcNAc...).SGILNQSEI
EEEEECCCC
41.22UniProtKB
Link
491N-linked (GlcNAc...).ETTVNYTDS
CCCCCCCCC
31.71UniProtKB
Link-
500S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)QRPICLPSK
EEEEECCCC
5.18HPRD
Link
514S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)IYTDCWVTG
CCCEEEEEE
2.13HPRD
Link
545S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)TNEECQKRY
CHHHHHHHC
4.75HPRD
Link
560S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)HKMICAGYR
CCEEEEECC
1.84HPRD
Link
571S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)GKDACKGDS
CCCCCCCCC
7.89HPRD
Link-
581S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)GPLSCKHNE
CCEEECCCC
7.38HPRD
Link
599S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)WGEGCAQRE
ECCCCCCCC
2.25HPRD
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
HGF_HUMANin vitroHPRD:07524HPRD12372819
10962009
THRB_HUMANin vitroHPRD:07524HPRD1652157
KNG1_HUMANin vitroHPRD:07524HPRD1652157
3936495
GP1BA_HUMANin vitroHPRD:07524HPRD11696542
A2AP_HUMANin vivoHPRD:07524HPRD8703832
IPSP_HUMANin vitroHPRD:07524HPRD2551064
FA11_HUMANin vitroHPRD:07524HPRD1998667
FA9_HUMANENSP00000264691STRING
TS101_HUMANENSP00000264691STRING
FA12_HUMANENSP00000264691STRING
VPS4A_HUMANENSP00000264691STRING
ZFHX3_HUMANENSP00000264691STRING
VPS28_HUMANENSP00000264691STRING
GPIX_HUMANENSP00000264691STRING
THRB_HUMANENSP00000264691STRING
GPV_HUMANENSP00000264691STRING
GP1BA_HUMANENSP00000264691STRING
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Disease Reference
Kegg disease
OMIM disease
612416Factor XI deficiency (FA11D)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-126; ASN-450 AND ASN-491,AND MASS SPECTROMETRY.
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-450 AND ASN-491, AND MASSSPECTROMETRY.
"Location of the disulfide bonds in human coagulation factor XI: thepresence of tandem apple domains.";
McMullen B.A., Fujikawa K., Davie E.W.;
Biochemistry 30:2056-2060(1991).
Cited for: PARTIAL PROTEIN SEQUENCE, AND DISULFIDE BONDS.
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND THR-22, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures