dbPTM

FA11_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FA11_HUMAN
UniProt AC	P03951
Protein Name	Coagulation factor XI
Gene Name	F11
Organism	Homo sapiens (Human).
Sequence Length	625
Subcellular Localization	Secreted.
Protein Description	Factor XI triggers the middle phase of the intrinsic pathway of blood coagulation by activating factor IX..
Protein Sequence	MIFLYQVVHFILFTSVSGECVTQLLKDTCFEGGDITTVFTPSAKYCQVVCTYHPRCLLFTFTAESPSEDPTRWFTCVLKDSVTETLPRVNRTAAISGYSFKQCSHQISACNKDIYVDLDMKGINYNSSVAKSAQECQERCTDDVHCHFFTYATRQFPSLEHRNICLLKHTQTGTPTRITKLDKVVSGFSLKSCALSNLACIRDIFPNTVFADSNIDSVMAPDAFVCGRICTHHPGCLFFTFFSQEWPKESQRNLCLLKTSESGLPSTRIKKSKALSGFSLQSCRHSIPVFCHSSFYHDTDFLGEELDIVAAKSHEACQKLCTNAVRCQFFTYTPAQASCNEGKGKCYLKLSSNGSPTKILHGRGGISGYTLRLCKMDNECTTKIKPRIVGGTASVRGEWPWQVTLHTTSPTQRHLCGGSIIGNQWILTAAHCFYGVESPKILRVYSGILNQSEIKEDTSFFGVQEIIIHDQYKMAESGYDIALLKLETTVNYTDSQRPICLPSKGDRNVIYTDCWVTGWGYRKLRDKIQNTLQKAKIPLVTNEECQKRYRGHKITHKMICAGYREGGKDACKGDSGGPLSCKHNEVWHLVGITSWGEGCAQRERPGVYTNVVEYVDWILEKTQAV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MIFLYQVVHFIL ---CCHHHHHHHHHH	6.63	24043423
14	Phosphorylation	VVHFILFTSVSGECV HHHHHHHHCCCCHHH	25.44	24043423
15	Phosphorylation	VHFILFTSVSGECVT HHHHHHHCCCCHHHH	13.62	24043423
17	Phosphorylation	FILFTSVSGECVTQL HHHHHCCCCHHHHHH	28.74	22817900
22	Phosphorylation	SVSGECVTQLLKDTC CCCCHHHHHHHHHHC	25.76	22817900
75	Phosphorylation	EDPTRWFTCVLKDSV CCCCCEEEEEEECCH	8.51	23532336
81	Phosphorylation	FTCVLKDSVTETLPR EEEEEECCHHHCCCC	29.38	23532336
90	N-linked_Glycosylation	TETLPRVNRTAAISG HHCCCCCCCCHHHCC	36.54	25092234
104 (in isoform 2)	Phosphorylation	-	18.88	28450419
108 (in isoform 2)	Phosphorylation	-	21.87	28450419
115	Phosphorylation	SACNKDIYVDLDMKG HCCCCCEEEEEECCC	9.69	18491316
125	Phosphorylation	LDMKGINYNSSVAKS EECCCCCCCHHHHHH	17.94	18491316
126	N-linked_Glycosylation	DMKGINYNSSVAKSA ECCCCCCCHHHHHHH	24.26	17623646
126	N-linked_Glycosylation	DMKGINYNSSVAKSA ECCCCCCCHHHHHHH	24.26	25092234
128	Phosphorylation	KGINYNSSVAKSAQE CCCCCCHHHHHHHHH	23.58	18491316
163	N-linked_Glycosylation	FPSLEHRNICLLKHT CCCCCCCCEEEEEEC	31.09	25092234
180	Acetylation	GTPTRITKLDKVVSG CCCCEEEHHHHHHCC	52.93	7396797
186	Phosphorylation	TKLDKVVSGFSLKSC EHHHHHHCCCCHHHH	36.79	-
347	Phosphorylation	NEGKGKCYLKLSSNG CCCCCEEEEEECCCC	15.45	28270605
351	Phosphorylation	GKCYLKLSSNGSPTK CEEEEEECCCCCCCE	21.85	28270605
352	Phosphorylation	KCYLKLSSNGSPTKI EEEEEECCCCCCCEE	56.50	28270605
353	N-linked_Glycosylation	CYLKLSSNGSPTKIL EEEEECCCCCCCEEE	52.14	UniProtKB CARBOHYD
355	Phosphorylation	LKLSSNGSPTKILHG EEECCCCCCCEEEEC	33.38	28270605
357	Phosphorylation	LSSNGSPTKILHGRG ECCCCCCCEEEECCC	32.20	28270605
370	Phosphorylation	RGGISGYTLRLCKMD CCCCCCEEEEEEECC	14.66	24719451
394	Phosphorylation	RIVGGTASVRGEWPW EEECCCEEECCCCCC	16.51	-
450	N-linked_Glycosylation	RVYSGILNQSEIKED HEEECCCCHHHHCCC	41.22	19159218
488	Phosphorylation	IALLKLETTVNYTDS EEEEEEEEEECCCCC	46.62	29978859
489	Phosphorylation	ALLKLETTVNYTDSQ EEEEEEEEECCCCCC	9.44	29978859
491	N-linked_Glycosylation	LKLETTVNYTDSQRP EEEEEEECCCCCCCC	31.71	1998667
492	Phosphorylation	KLETTVNYTDSQRPI EEEEEECCCCCCCCE	13.95	29978859
493	Phosphorylation	LETTVNYTDSQRPIC EEEEECCCCCCCCEE	24.78	29978859
495	Phosphorylation	TTVNYTDSQRPICLP EEECCCCCCCCEECC	21.93	29978859
503	Phosphorylation	QRPICLPSKGDRNVI CCCEECCCCCCCCEE	36.00	24719451
517	Phosphorylation	IYTDCWVTGWGYRKL EEEECEECCCHHHHH	11.61	-
521	Phosphorylation	CWVTGWGYRKLRDKI CEECCCHHHHHHHHH	9.69	-
531	Phosphorylation	LRDKIQNTLQKAKIP HHHHHHHHHHHCCCC	17.75	26699800
608	Phosphorylation	QRERPGVYTNVVEYV CCCCCCCEEHHHHHH	9.86	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of FA11_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
163	N	Glycosylation		25092234
Glycosylation at Asn-163 uses a rare non-canonical Asn-X-Cys glycosite.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of FA11_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	28514442
CREL2_HUMAN	CRELD2	physical	28514442
N42L2_HUMAN	N4BP2L2	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612416	Factor XI deficiency (FA11D)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of FA11_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"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.	19159218 [Abstract]
"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.	16335952 [Abstract]
"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.	1998667 [Abstract]
Phosphorylation
Reference	PubMed
"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.	18187866 [Abstract]

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