KLKB1_HUMAN - dbPTM
KLKB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
109PhosphorylationKQCGHQISACHRDIY
HHHCCCCHHHCHHHH
20.4829052541
125N-linked_GlycosylationGVDMRGVNFNVSKVS
CCCCCCCCCCEECCC
26.1217623646
125N-linked_GlycosylationGVDMRGVNFNVSKVS
CCCCCCCCCCEECCC
26.12-
127N-linked_GlycosylationDMRGVNFNVSKVSSV
CCCCCCCCEECCCCH
31.7618638581
127N-linked_GlycosylationDMRGVNFNVSKVSSV
CCCCCCCCEECCCCH
31.763521732
175PhosphorylationLKYSPGGTPTAIKVL
EEECCCCCCCCEEHH
24.3123403867
177PhosphorylationYSPGGTPTAIKVLSN
ECCCCCCCCEEHHHC
40.6323403867
260PhosphorylationRNVCLLKTSESGTPS
CCEEEEEECCCCCCC
37.3830576142
261PhosphorylationNVCLLKTSESGTPSS
CEEEEEECCCCCCCC
28.3324505115
263PhosphorylationCLLKTSESGTPSSST
EEEEECCCCCCCCCC
47.9724505115
269PhosphorylationESGTPSSSTPQENTI
CCCCCCCCCCCCCCC
48.7430576142
275PhosphorylationSSTPQENTISGYSLL
CCCCCCCCCCCEEEE
18.77-
283PhosphorylationISGYSLLTCKRTLPE
CCCEEEEEEECCCCC
22.6730576142
308N-linked_GlycosylationDFGGEELNVTFVKGV
CCCCCEEEEEEEECC
33.783521732
308N-linked_GlycosylationDFGGEELNVTFVKGV
CCCCCEEEEEEEECC
33.7817623646
371PhosphorylationTQGSSGYSLRLCNTG
CCCCCCEEEEEEECC
15.5624719451
384O-linked_GlycosylationTGDNSVCTTKTSTRI
CCCCCEEEECCCCEE
29.22OGP
396N-linked_GlycosylationTRIVGGTNSSWGEWP
CEEECCCCCCCCCCC
37.003521732
396N-linked_GlycosylationTRIVGGTNSSWGEWP
CEEECCCCCCCCCCC
37.0019159218
453N-linked_GlycosylationRIYSGILNLSDITKD
HHHHCCCCHHHCCCC
35.2617623646
453N-linked_GlycosylationRIYSGILNLSDITKD
HHHHCCCCHHHCCCC
35.2618638581
494N-linked_GlycosylationIKLQAPLNYTEFQKP
EEEECCCCCCCCCCC
40.393521732
494N-linked_GlycosylationIKLQAPLNYTEFQKP
EEEECCCCCCCCCCC
40.3918638581
506PhosphorylationQKPICLPSKGDTSTI
CCCEECCCCCCCCEE
36.0024719451
510PhosphorylationCLPSKGDTSTIYTNC
ECCCCCCCCEEEECC
36.1219690332
511PhosphorylationLPSKGDTSTIYTNCW
CCCCCCCCEEEECCE
19.9719690332
514PhosphorylationKGDTSTIYTNCWVTG
CCCCCEEEECCEECC
7.6219690332
515PhosphorylationGDTSTIYTNCWVTGW
CCCCEEEECCEECCC
21.7619690332
520PhosphorylationIYTNCWVTGWGFSKE
EEECCEECCCCCCCC
11.6119690332
525PhosphorylationWVTGWGFSKEKGEIQ
EECCCCCCCCCCHHH
35.6519690332
604MethylationSWGEGCARREQPGVY
ECCCCCCCCCCCCCC
46.9024381453
605MethylationWGEGCARREQPGVYT
CCCCCCCCCCCCCCH
28.5124381461

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 KLKB1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KLKB1_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 KLKB1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KNG1_HUMANKNG1physical
7944388
GEPH_HUMANGPHNphysical
28514442
ZBTB1_HUMANZBTB1physical
28514442
CND2_HUMANNCAPHphysical
28514442
CNOT2_HUMANCNOT2physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612423Prekallikrein deficiency (PKK deficiency)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KLKB1_HUMAN

loading...

Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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].

TOP