UniProt ID | KLKB1_HUMAN | |
---|---|---|
UniProt AC | P03952 | |
Protein Name | Plasma kallikrein | |
Gene Name | KLKB1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 638 | |
Subcellular Localization | Secreted. | |
Protein Description | The enzyme cleaves Lys-Arg and Arg-Ser bonds. It activates, in a reciprocal reaction, factor XII after its binding to a negatively charged surface. It also releases bradykinin from HMW kininogen and may also play a role in the renin-angiotensin system by converting prorenin into renin.. | |
Protein Sequence | MILFKQATYFISLFATVSCGCLTQLYENAFFRGGDVASMYTPNAQYCQMRCTFHPRCLLFSFLPASSINDMEKRFGCFLKDSVTGTLPKVHRTGAVSGHSLKQCGHQISACHRDIYKGVDMRGVNFNVSKVSSVEECQKRCTNNIRCQFFSYATQTFHKAEYRNNCLLKYSPGGTPTAIKVLSNVESGFSLKPCALSEIGCHMNIFQHLAFSDVDVARVLTPDAFVCRTICTYHPNCLFFTFYTNVWKIESQRNVCLLKTSESGTPSSSTPQENTISGYSLLTCKRTLPEPCHSKIYPGVDFGGEELNVTFVKGVNVCQETCTKMIRCQFFTYSLLPEDCKEEKCKCFLRLSMDGSPTRIAYGTQGSSGYSLRLCNTGDNSVCTTKTSTRIVGGTNSSWGEWPWQVSLQVKLTAQRHLCGGSLIGHQWVLTAAHCFDGLPLQDVWRIYSGILNLSDITKDTPFSQIKEIIIHQNYKVSEGNHDIALIKLQAPLNYTEFQKPICLPSKGDTSTIYTNCWVTGWGFSKEKGEIQNILQKVNIPLVTNEECQKRYQDYKITQRMVCAGYKEGGKDACKGDSGGPLVCKHNGMWRLVGITSWGEGCARREQPGVYTKVAEYMDWILEKTQSSDGKAQMQSPA | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
109 | Phosphorylation | KQCGHQISACHRDIY HHHCCCCHHHCHHHH | 20.48 | 29052541 | |
125 | N-linked_Glycosylation | GVDMRGVNFNVSKVS CCCCCCCCCCEECCC | 26.12 | 17623646 | |
125 | N-linked_Glycosylation | GVDMRGVNFNVSKVS CCCCCCCCCCEECCC | 26.12 | - | |
127 | N-linked_Glycosylation | DMRGVNFNVSKVSSV CCCCCCCCEECCCCH | 31.76 | 18638581 | |
127 | N-linked_Glycosylation | DMRGVNFNVSKVSSV CCCCCCCCEECCCCH | 31.76 | 3521732 | |
175 | Phosphorylation | LKYSPGGTPTAIKVL EEECCCCCCCCEEHH | 24.31 | 23403867 | |
177 | Phosphorylation | YSPGGTPTAIKVLSN ECCCCCCCCEEHHHC | 40.63 | 23403867 | |
260 | Phosphorylation | RNVCLLKTSESGTPS CCEEEEEECCCCCCC | 37.38 | 30576142 | |
261 | Phosphorylation | NVCLLKTSESGTPSS CEEEEEECCCCCCCC | 28.33 | 24505115 | |
263 | Phosphorylation | CLLKTSESGTPSSST EEEEECCCCCCCCCC | 47.97 | 24505115 | |
269 | Phosphorylation | ESGTPSSSTPQENTI CCCCCCCCCCCCCCC | 48.74 | 30576142 | |
275 | Phosphorylation | SSTPQENTISGYSLL CCCCCCCCCCCEEEE | 18.77 | - | |
283 | Phosphorylation | ISGYSLLTCKRTLPE CCCEEEEEEECCCCC | 22.67 | 30576142 | |
308 | N-linked_Glycosylation | DFGGEELNVTFVKGV CCCCCEEEEEEEECC | 33.78 | 3521732 | |
308 | N-linked_Glycosylation | DFGGEELNVTFVKGV CCCCCEEEEEEEECC | 33.78 | 17623646 | |
371 | Phosphorylation | TQGSSGYSLRLCNTG CCCCCCEEEEEEECC | 15.56 | 24719451 | |
384 | O-linked_Glycosylation | TGDNSVCTTKTSTRI CCCCCEEEECCCCEE | 29.22 | OGP | |
396 | N-linked_Glycosylation | TRIVGGTNSSWGEWP CEEECCCCCCCCCCC | 37.00 | 3521732 | |
396 | N-linked_Glycosylation | TRIVGGTNSSWGEWP CEEECCCCCCCCCCC | 37.00 | 19159218 | |
453 | N-linked_Glycosylation | RIYSGILNLSDITKD HHHHCCCCHHHCCCC | 35.26 | 17623646 | |
453 | N-linked_Glycosylation | RIYSGILNLSDITKD HHHHCCCCHHHCCCC | 35.26 | 18638581 | |
494 | N-linked_Glycosylation | IKLQAPLNYTEFQKP EEEECCCCCCCCCCC | 40.39 | 3521732 | |
494 | N-linked_Glycosylation | IKLQAPLNYTEFQKP EEEECCCCCCCCCCC | 40.39 | 18638581 | |
506 | Phosphorylation | QKPICLPSKGDTSTI CCCEECCCCCCCCEE | 36.00 | 24719451 | |
510 | Phosphorylation | CLPSKGDTSTIYTNC ECCCCCCCCEEEECC | 36.12 | 19690332 | |
511 | Phosphorylation | LPSKGDTSTIYTNCW CCCCCCCCEEEECCE | 19.97 | 19690332 | |
514 | Phosphorylation | KGDTSTIYTNCWVTG CCCCCEEEECCEECC | 7.62 | 19690332 | |
515 | Phosphorylation | GDTSTIYTNCWVTGW CCCCEEEECCEECCC | 21.76 | 19690332 | |
520 | Phosphorylation | IYTNCWVTGWGFSKE EEECCEECCCCCCCC | 11.61 | 19690332 | |
525 | Phosphorylation | WVTGWGFSKEKGEIQ EECCCCCCCCCCHHH | 35.65 | 19690332 | |
604 | Methylation | SWGEGCARREQPGVY ECCCCCCCCCCCCCC | 46.90 | 24381453 | |
605 | Methylation | WGEGCARREQPGVYT CCCCCCCCCCCCCCH | 28.51 | 24381461 |
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 KLKB1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KLKB1_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 KLKB1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
KNG1_HUMAN | KNG1 | physical | 7944388 | |
GEPH_HUMAN | GPHN | physical | 28514442 | |
ZBTB1_HUMAN | ZBTB1 | physical | 28514442 | |
CND2_HUMAN | NCAPH | physical | 28514442 | |
CNOT2_HUMAN | CNOT2 | physical | 28514442 |
Kegg Disease | ||||||
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There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
612423 | Prekallikrein deficiency (PKK deficiency) | |||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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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-308; ASN-396; ASN-453 ANDASN-494, AND MASS SPECTROMETRY. | |
"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-127; ASN-308; ASN-396;ASN-453 AND ASN-494, AND MASS SPECTROMETRY. | |
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry."; Zhang H., Li X.-J., Martin D.B., Aebersold R.; Nat. Biotechnol. 21:660-666(2003). Cited for: GLYCOSYLATION AT ASN-453. | |
"Human plasma prekallikrein, a zymogen to a serine protease thatcontains four tandem repeats."; Chung D.W., Fujikawa K., McMullen B.A., Davie E.W.; Biochemistry 25:2410-2417(1986). Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |