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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
31 | Phosphorylation | EAPKEHKYKAEEHTV CCCCCCCCCCCCCEE | 19.82 | - | |
43 | O-linked_Glycosylation | HTVVLTVTGEPCHFP CEEEEEECCCCCCCC | 30.50 | OGP | |
53 | Phosphorylation | PCHFPFQYHRQLYHK CCCCCHHHHHHHHHH | 10.19 | - | |
58 | Phosphorylation | FQYHRQLYHKCTHKG HHHHHHHHHHCCCCC | 7.30 | - | |
109 | O-linked_Glycosylation | SPCQKGGTCVNMPSG CCCCCCCEEECCCCC | 23.19 | 1544894 | |
231 | Phosphorylation | SYRGLARTTLSGAPC CHHCEEEECCCCCCC | 26.87 | 24719451 | |
243 | Phosphorylation | APCQPWASEATYRNV CCCCCCCCCCCCCCC | 24.72 | - | |
246 | Phosphorylation | QPWASEATYRNVTAE CCCCCCCCCCCCCHH | 20.97 | 24719451 | |
249 | N-linked_Glycosylation | ASEATYRNVTAEQAR CCCCCCCCCCHHHHH | 25.69 | 3886654 | |
297 | O-linked_Glycosylation | CDLAQCQTPTQAAPP CCHHHCCCCCCCCCC | 35.61 | OGP | |
299 | O-linked_Glycosylation | LAQCQTPTQAAPPTP HHHCCCCCCCCCCCC | 33.94 | 3886654 | |
305 | O-linked_Glycosylation | PTQAAPPTPVSPRLH CCCCCCCCCCCCCCC | 34.95 | 3886654 | |
308 | O-linked_Glycosylation | AAPPTPVSPRLHVPL CCCCCCCCCCCCCCC | 12.90 | 3886654 | |
308 | Phosphorylation | AAPPTPVSPRLHVPL CCCCCCCCCCCCCCC | 12.90 | 24945436 | |
328 | O-linked_Glycosylation | APPKPQPTTRTPPQS CCCCCCCCCCCCCCC | 24.54 | 3886654 | |
329 | O-linked_Glycosylation | PPKPQPTTRTPPQSQ CCCCCCCCCCCCCCC | 38.95 | 3886654 | |
331 | O-linked_Glycosylation | KPQPTTRTPPQSQTP CCCCCCCCCCCCCCC | 36.91 | OGP | |
331 | Phosphorylation | KPQPTTRTPPQSQTP CCCCCCCCCCCCCCC | 36.91 | - | |
335 | O-linked_Glycosylation | TTRTPPQSQTPGALP CCCCCCCCCCCCCCC | 41.62 | OGP | |
337 | O-linked_Glycosylation | RTPPQSQTPGALPAK CCCCCCCCCCCCCCC | 29.01 | 3886654 | |
350 | Phosphorylation | AKREQPPSLTRNGPL CCCCCCCCCCCCCCC | 49.40 | 24505115 | |
366 | Phosphorylation | CGQRLRKSLSSMTRV HHHHHHHHHHHHHHH | 27.35 | - | |
368 | Phosphorylation | QRLRKSLSSMTRVVG HHHHHHHHHHHHHHH | 25.75 | - | |
371 | Phosphorylation | RKSLSSMTRVVGGLV HHHHHHHHHHHHHHH | 23.43 | - | |
433 | N-linked_Glycosylation | VLGQERRNHSCEPCQ EECCCCCCCCCCCCC | 37.33 | 17623646 | |
433 | N-linked_Glycosylation | VLGQERRNHSCEPCQ EECCCCCCCCCCCCC | 37.33 | 16335952 | |
466 | Methylation | QHDLALLRLQEDADG HHHHHHHEECCCCCC | 34.86 | - |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of FA12_HUMAN !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
EPAS1_HUMAN | EPAS1 | physical | 21512133 | |
PJA1_HUMAN | PJA1 | physical | 26186194 | |
AMRA1_HUMAN | AMBRA1 | physical | 26186194 | |
NUDC1_HUMAN | NUDCD1 | physical | 26186194 | |
MRRP3_HUMAN | KIAA0391 | physical | 26186194 | |
HIF1A_HUMAN | HIF1A | physical | 18838541 | |
FA12_HUMAN | F12 | physical | 18838541 | |
ANR40_HUMAN | ANKRD40 | physical | 28514442 | |
HSP7C_HUMAN | HSPA8 | physical | 28514442 |
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N-linked Glycosylation | |
Reference | PubMed |
"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 | |
Reference | PubMed |
"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. |