FA12_HUMAN - dbPTM
FA12_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FA12_HUMAN
UniProt AC P00748
Protein Name Coagulation factor XII
Gene Name F12
Organism Homo sapiens (Human).
Sequence Length 615
Subcellular Localization Secreted.
Protein Description Factor XII is a serum glycoprotein that participates in the initiation of blood coagulation, fibrinolysis, and the generation of bradykinin and angiotensin. Prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa and then trypsin cleaves it to beta-factor XIIa. Alpha-factor XIIa activates factor XI to factor XIa..
Protein Sequence MRALLLLGFLLVSLESTLSIPPWEAPKEHKYKAEEHTVVLTVTGEPCHFPFQYHRQLYHKCTHKGRPGPQPWCATTPNFDQDQRWGYCLEPKKVKDHCSKHSPCQKGGTCVNMPSGPHCLCPQHLTGNHCQKEKCFEPQLLRFFHKNEIWYRTEQAAVARCQCKGPDAHCQRLASQACRTNPCLHGGRCLEVEGHRLCHCPVGYTGAFCDVDTKASCYDGRGLSYRGLARTTLSGAPCQPWASEATYRNVTAEQARNWGLGGHAFCRNPDNDIRPWCFVLNRDRLSWEYCDLAQCQTPTQAAPPTPVSPRLHVPLMPAQPAPPKPQPTTRTPPQSQTPGALPAKREQPPSLTRNGPLSCGQRLRKSLSSMTRVVGGLVALRGAHPYIAALYWGHSFCAGSLIAPCWVLTAAHCLQDRPAPEDLTVVLGQERRNHSCEPCQTLAVRSYRLHEAFSPVSYQHDLALLRLQEDADGSCALLSPYVQPVCLPSGAARPSETTLCQVAGWGHQFEGAEEYASFLQEAQVPFLSLERCSAPDVHGSSILPGMLCAGFLEGGTDACQGDSGGPLVCEDQAAERRLTLQGIISWGSGCGDRNKPGVYTDVAYYLAWIREHTVS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
31PhosphorylationEAPKEHKYKAEEHTV
CCCCCCCCCCCCCEE
19.82-
43O-linked_GlycosylationHTVVLTVTGEPCHFP
CEEEEEECCCCCCCC
30.50OGP
53PhosphorylationPCHFPFQYHRQLYHK
CCCCCHHHHHHHHHH
10.19-
58PhosphorylationFQYHRQLYHKCTHKG
HHHHHHHHHHCCCCC
7.30-
109O-linked_GlycosylationSPCQKGGTCVNMPSG
CCCCCCCEEECCCCC
23.191544894
231PhosphorylationSYRGLARTTLSGAPC
CHHCEEEECCCCCCC
26.8724719451
243PhosphorylationAPCQPWASEATYRNV
CCCCCCCCCCCCCCC
24.72-
246PhosphorylationQPWASEATYRNVTAE
CCCCCCCCCCCCCHH
20.9724719451
249N-linked_GlycosylationASEATYRNVTAEQAR
CCCCCCCCCCHHHHH
25.693886654
297O-linked_GlycosylationCDLAQCQTPTQAAPP
CCHHHCCCCCCCCCC
35.61OGP
299O-linked_GlycosylationLAQCQTPTQAAPPTP
HHHCCCCCCCCCCCC
33.943886654
305O-linked_GlycosylationPTQAAPPTPVSPRLH
CCCCCCCCCCCCCCC
34.953886654
308O-linked_GlycosylationAAPPTPVSPRLHVPL
CCCCCCCCCCCCCCC
12.903886654
308PhosphorylationAAPPTPVSPRLHVPL
CCCCCCCCCCCCCCC
12.9024945436
328O-linked_GlycosylationAPPKPQPTTRTPPQS
CCCCCCCCCCCCCCC
24.543886654
329O-linked_GlycosylationPPKPQPTTRTPPQSQ
CCCCCCCCCCCCCCC
38.953886654
331O-linked_GlycosylationKPQPTTRTPPQSQTP
CCCCCCCCCCCCCCC
36.91OGP
331PhosphorylationKPQPTTRTPPQSQTP
CCCCCCCCCCCCCCC
36.91-
335O-linked_GlycosylationTTRTPPQSQTPGALP
CCCCCCCCCCCCCCC
41.62OGP
337O-linked_GlycosylationRTPPQSQTPGALPAK
CCCCCCCCCCCCCCC
29.013886654
350PhosphorylationAKREQPPSLTRNGPL
CCCCCCCCCCCCCCC
49.4024505115
366PhosphorylationCGQRLRKSLSSMTRV
HHHHHHHHHHHHHHH
27.35-
368PhosphorylationQRLRKSLSSMTRVVG
HHHHHHHHHHHHHHH
25.75-
371PhosphorylationRKSLSSMTRVVGGLV
HHHHHHHHHHHHHHH
23.43-
433N-linked_GlycosylationVLGQERRNHSCEPCQ
EECCCCCCCCCCCCC
37.3317623646
433N-linked_GlycosylationVLGQERRNHSCEPCQ
EECCCCCCCCCCCCC
37.3316335952
466MethylationQHDLALLRLQEDADG
HHHHHHHEECCCCCC
34.86-

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 FA12_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FA12_HUMAN !!

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 FA12_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EPAS1_HUMANEPAS1physical
21512133
PJA1_HUMANPJA1physical
26186194
AMRA1_HUMANAMBRA1physical
26186194
NUDC1_HUMANNUDCD1physical
26186194
MRRP3_HUMANKIAA0391physical
26186194
HIF1A_HUMANHIF1Aphysical
18838541
FA12_HUMANF12physical
18838541
ANR40_HUMANANKRD40physical
28514442
HSP7C_HUMANHSPA8physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
234000Factor XII deficiency (FA12D)
610618Hereditary angioedema 3 (HAE3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FA12_HUMAN

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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-249 AND ASN-433, AND MASSSPECTROMETRY.
"Screening for N-glycosylated proteins by liquid chromatography massspectrometry.";
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
Proteomics 4:454-465(2004).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-433, AND MASSSPECTROMETRY.
"Amino acid sequence of the heavy chain of human alpha-factor XIIa(activated Hageman factor).";
McMullen B.A., Fujikawa K.;
J. Biol. Chem. 260:5328-5341(1985).
Cited for: PROTEIN SEQUENCE OF 20-379, GLYCOSYLATION AT ASN-249; THR-299;THR-305; SER-308; THR-328; THR-329 AND THR-337, AND VARIANT PRO-207.
"Characterization of human blood coagulation factor XII cDNA.Prediction of the primary structure of factor XII and the tertiarystructure of beta-factor XIIa.";
Cool D.E., Edgell C.-J.S., Louie G.V., Zoller M.J., Brayer G.D.,McGillivray R.T.A.;
J. Biol. Chem. 260:13666-13676(1985).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-615, AND VARIANT PRO-207.
O-linked Glycosylation
ReferencePubMed
"O-linked fucose is present in the first epidermal growth factordomain of factor XII but not protein C.";
Harris R.J., Ling V.T., Spellman M.W.;
J. Biol. Chem. 267:5102-5107(1992).
Cited for: GLYCOSYLATION AT THR-109.
"Amino acid sequence of the heavy chain of human alpha-factor XIIa(activated Hageman factor).";
McMullen B.A., Fujikawa K.;
J. Biol. Chem. 260:5328-5341(1985).
Cited for: PROTEIN SEQUENCE OF 20-379, GLYCOSYLATION AT ASN-249; THR-299;THR-305; SER-308; THR-328; THR-329 AND THR-337, AND VARIANT PRO-207.

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