KNG1_HUMAN - dbPTM
KNG1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KNG1_HUMAN
UniProt AC P01042
Protein Name Kininogen-1
Gene Name KNG1
Organism Homo sapiens (Human).
Sequence Length 644
Subcellular Localization Secreted, extracellular space.
Protein Description (1) Kininogens are inhibitors of thiol proteases; (2) HMW-kininogen plays an important role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII; (3) HMW-kininogen inhibits the thrombin- and plasmin-induced aggregation of thrombocytes; (4) the active peptide bradykinin that is released from HMW-kininogen shows a variety of physiological effects: (4A) influence in smooth muscle contraction, (4B) induction of hypotension, (4C) natriuresis and diuresis, (4D) decrease in blood glucose level, (4E) it is a mediator of inflammation and causes (4E1) increase in vascular permeability, (4E2) stimulation of nociceptors (4E3) release of other mediators of inflammation (e.g. prostaglandins), (4F) it has a cardioprotective effect (directly via bradykinin action, indirectly via endothelium-derived relaxing factor action); (5) LMW-kininogen inhibits the aggregation of thrombocytes; (6) LMW-kininogen is in contrast to HMW-kininogen not involved in blood clotting..
Protein Sequence MKLITILFLCSRLLLSLTQESQSEEIDCNDKDLFKAVDAALKKYNSQNQSNNQFVLYRITEATKTVGSDTFYSFKYEIKEGDCPVQSGKTWQDCEYKDAAKAATGECTATVGKRSSTKFSVATQTCQITPAEGPVVTAQYDCLGCVHPISTQSPDLEPILRHGIQYFNNNTQHSSLFMLNEVKRAQRQVVAGLNFRITYSIVQTNCSKENFLFLTPDCKSLWNGDTGECTDNAYIDIQLRIASFSQNCDIYPGKDFVQPPTKICVGCPRDIPTNSPELEETLTHTITKLNAENNATFYFKIDNVKKARVQVVAGKKYFIDFVARETTCSKESNEELTESCETKKLGQSLDCNAEVYVVPWEKKIYPTVNCQPLGMISLMKRPPGFSPFRSSRIGEIKEETTVSPPHTSMAPAQDEERDSGKEQGHTRRHDWGHEKQRKHNLGHGHKHERDQGHGHQRGHGLGHGHEQQHGLGHGHKFKLDDDLEHQGGHVLDHGHKHKHGHGHGKHKNKGKKNGKHNGWKTEHLASSSEDSTTPSAQTQEKTEGPTPIPSLAKPGVTVTFSDFQDSDLIATMMPPISPAPIQSDDDWIPDIQIDPNGLSFNPISDFPDTTSPKCPGRPWKSVSEINPTTQMKESYYFDLTDGLS
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
5Phosphorylation---MKLITILFLCSR
---CHHHHHHHHHHH		23.2824505115
11PhosphorylationITILFLCSRLLLSLT
HHHHHHHHHHHHHHC		28.2724505115
16PhosphorylationLCSRLLLSLTQESQS
HHHHHHHHHCCHHCC		29.3724505115
18PhosphorylationSRLLLSLTQESQSEE
HHHHHHHCCHHCCCC		27.2424505115
19Pyrrolidone_carboxylic_acidRLLLSLTQESQSEEI
HHHHHHCCHHCCCCC		54.35-
19Pyrrolidone_carboxylic_acidRLLLSLTQESQSEEI
HHHHHHCCHHCCCCC		54.35-
21PhosphorylationLLSLTQESQSEEIDC
HHHHCCHHCCCCCCC		29.2324505115
23PhosphorylationSLTQESQSEEIDCND
HHCCHHCCCCCCCCH		46.6124505115
46PhosphorylationAALKKYNSQNQSNNQ
HHHHHHHCCCCCCCC		27.6724505115
48N-linked_GlycosylationLKKYNSQNQSNNQFV
HHHHHCCCCCCCCEE		47.2518638581
48N-linked_GlycosylationLKKYNSQNQSNNQFV
HHHHHCCCCCCCCEE		47.2516335952
50PhosphorylationKYNSQNQSNNQFVLY
HHHCCCCCCCCEEEE		45.3524505115
110PhosphorylationATGECTATVGKRSST
HCCCCEEEECCCCCC		16.19-
113AcetylationECTATVGKRSSTKFS
CCEEEECCCCCCEEE		44.787683337
120O-linked_GlycosylationKRSSTKFSVATQTCQ
CCCCCEEEEEEEECE		16.64OGP
129O-linked_GlycosylationATQTCQITPAEGPVV
EEEECEECCCCCCEE		7.20OGP
137O-linked_GlycosylationPAEGPVVTAQYDCLG
CCCCCEEEEEEEECC		14.31OGP
150O-linked_GlycosylationLGCVHPISTQSPDLE
CCCCCCCCCCCCCHH		25.50OGP
151O-linked_GlycosylationGCVHPISTQSPDLEP
CCCCCCCCCCCCHHH		33.51OGP
169N-linked_GlycosylationHGIQYFNNNTQHSSL
CHHHCCCCCCCCCEE		42.9217623646
169N-linked_GlycosylationHGIQYFNNNTQHSSL
CHHHCCCCCCCCCEE		42.9218638581
171PhosphorylationIQYFNNNTQHSSLFM
HHCCCCCCCCCEEEH		29.77-
174PhosphorylationFNNNTQHSSLFMLNE
CCCCCCCCEEEHHHH		20.93-
175PhosphorylationNNNTQHSSLFMLNEV
CCCCCCCEEEHHHHH		24.41-
205N-linked_GlycosylationTYSIVQTNCSKENFL
EEEEEEECCCCCCEE		15.8018638581
205N-linked_GlycosylationTYSIVQTNCSKENFL
EEEEEEECCCCCCEE		15.8017623646
261O-linked_GlycosylationKDFVQPPTKICVGCP
CCCCCCCCEEEECCC		39.46OGP
273O-linked_GlycosylationGCPRDIPTNSPELEE
CCCCCCCCCCHHHHH		48.97OGP
273PhosphorylationGCPRDIPTNSPELEE
CCCCCCCCCCHHHHH		48.9728857561
275PhosphorylationPRDIPTNSPELEETL
CCCCCCCCHHHHHHH		23.4126657352
281PhosphorylationNSPELEETLTHTITK
CCHHHHHHHHHHHHH		27.8128060719
283PhosphorylationPELEETLTHTITKLN
HHHHHHHHHHHHHCC		25.1328060719
285PhosphorylationLEETLTHTITKLNAE
HHHHHHHHHHHCCCC		25.7128060719
287PhosphorylationETLTHTITKLNAENN
HHHHHHHHHCCCCCC		30.5428060719
294N-linked_GlycosylationTKLNAENNATFYFKI
HHCCCCCCCEEEEEE		31.6817623646
294N-linked_GlycosylationTKLNAENNATFYFKI
HHCCCCCCCEEEEEE		31.6818638581
316AcetylationVQVVAGKKYFIDFVA
EEEECCCEEEEEEHH		44.4627178108
317PhosphorylationQVVAGKKYFIDFVAR
EEECCCEEEEEEHHC		14.8424505115
326PhosphorylationIDFVARETTCSKESN
EEEHHCCCCCCHHHH		27.7823911959
327PhosphorylationDFVARETTCSKESNE
EEHHCCCCCCHHHHH		15.2723911959
329PhosphorylationVARETTCSKESNEEL
HHCCCCCCHHHHHHH		37.0524972180
332PhosphorylationETTCSKESNEELTES
CCCCCHHHHHHHHHH		53.9623911959
337PhosphorylationKESNEELTESCETKK
HHHHHHHHHHHCCCC		29.1830242111
339PhosphorylationSNEELTESCETKKLG
HHHHHHHHHCCCCCC		16.4228192239
342PhosphorylationELTESCETKKLGQSL
HHHHHHCCCCCCCCC		37.4928060719
364 (in isoform 3)Phosphorylation-8.0427130503
365 (in isoform 3)Phosphorylation-11.1727130503
366 (in isoform 3)Phosphorylation-33.0927130503
370 (in isoform 3)Phosphorylation-3.7127130503
377PhosphorylationCQPLGMISLMKRPPG
CEECCEEECCCCCCC		17.3322468782
383HydroxylationISLMKRPPGFSPFRS
EECCCCCCCCCCCCC		61.573182782
386PhosphorylationMKRPPGFSPFRSSRI
CCCCCCCCCCCCCCC		29.1024719451
386 (in isoform 3)Phosphorylation-29.1027130503
390PhosphorylationPGFSPFRSSRIGEIK
CCCCCCCCCCCCCCC		25.0922817900
391PhosphorylationGFSPFRSSRIGEIKE
CCCCCCCCCCCCCCE		24.5422817900
400O-linked_GlycosylationIGEIKEETTVSPPHT
CCCCCEECCCCCCCC		33.32OGP
400 (in isoform 2)Phosphorylation-33.3227130503
401O-linked_GlycosylationGEIKEETTVSPPHTS
CCCCEECCCCCCCCC		23.434054110
401 (in isoform 2)Phosphorylation-23.4327130503
401PhosphorylationGEIKEETTVSPPHTS
CCCCEECCCCCCCCC		23.4327251275
402PhosphorylationEIKEETTVSPPHTSM
CCCEECCCCCCCCCC		12.0427251275
402 (in isoform 2)Phosphorylation-12.0427130503
406PhosphorylationETTVSPPHTSMAPAQ
ECCCCCCCCCCCCCC		33.6824719451
406 (in isoform 2)Phosphorylation-33.6827130503
407O-linked_GlycosylationTTVSPPHTSMAPAQD
CCCCCCCCCCCCCCC		26.43OGP
408O-linked_GlycosylationTVSPPHTSMAPAQDE
CCCCCCCCCCCCCCC		15.20OGP
422PhosphorylationEERDSGKEQGHTRRH
CCCCCCCCCCCCCCC		66.3827251275
422 (in isoform 2)Phosphorylation-66.3827130503
531O-linked_GlycosylationLASSSEDSTTPSAQT
HCCCCCCCCCCCCCC		30.08OGP
532O-linked_GlycosylationASSSEDSTTPSAQTQ
CCCCCCCCCCCCCCC		55.86OGP
533O-linked_GlycosylationSSSEDSTTPSAQTQE
CCCCCCCCCCCCCCC		21.144054110
542O-linked_GlycosylationSAQTQEKTEGPTPIP
CCCCCCCCCCCCCCC		45.484054110
546O-linked_GlycosylationQEKTEGPTPIPSLAK
CCCCCCCCCCCCCCC		44.714054110
550O-linked_GlycosylationEGPTPIPSLAKPGVT
CCCCCCCCCCCCCEE		41.50OGP
557O-linked_GlycosylationSLAKPGVTVTFSDFQ
CCCCCCEEEEECCCC		21.534054110
571O-linked_GlycosylationQDSDLIATMMPPISP
CCCCCEEEECCCCCC		13.654054110
577O-linked_GlycosylationATMMPPISPAPIQSD
EEECCCCCCCCCCCC		22.304054110
599O-linked_GlycosylationQIDPNGLSFNPISDF
EECCCCCCCCCCCCC		25.11OGP
604O-linked_GlycosylationGLSFNPISDFPDTTS
CCCCCCCCCCCCCCC		34.16OGP
628O-linked_GlycosylationSVSEINPTTQMKESY
CHHHCCCCCCCEEEE		25.774054110
629O-linked_GlycosylationVSEINPTTQMKESYY
HHHCCCCCCCEEEEE		28.11OGP
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
332SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
383PHydroxylation

3366244
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 KNG1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KLKB1_HUMANKLKB1physical
291905
FA11_HUMANF11physical
291905
KLKB1_HUMANKLKB1physical
7686159
FRIL_HUMANFTLphysical
12071855
KLKB1_HUMANKLKB1physical
10464316
ITB2_HUMANITGB2physical
10845911
C1QR1_HUMANCD93physical
8710908
TBB8_HUMANTUBB8physical
26186194
APC1_HUMANANAPC1physical
26186194
CAN1_HUMANCAPN1physical
26186194
CATO_HUMANCTSOphysical
26186194
SC65_HUMANP3H4physical
26186194
CATL2_HUMANCTSVphysical
26186194
APC5_HUMANANAPC5physical
26186194
PP2AA_HUMANPPP2CAphysical
26186194
P3H3_HUMANLEPREL2physical
26186194
TECT1_HUMANTCTN1physical
26186194
CPNS1_HUMANCAPNS1physical
26186194
DPB1_HUMANHLA-DPB1physical
26186194
VHL_HUMANVHLphysical
26186194
CATO_HUMANCTSOphysical
28514442
CAN1_HUMANCAPN1physical
28514442
APC1_HUMANANAPC1physical
28514442
P3H3_HUMANLEPREL2physical
28514442
CATL2_HUMANCTSVphysical
28514442
VHL_HUMANVHLphysical
28514442
2ABG_HUMANPPP2R2Cphysical
28514442
APC5_HUMANANAPC5physical
28514442
MRC2_HUMANMRC2physical
28514442
TECT1_HUMANTCTN1physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
228960High molecular weight kininogen deficiency (HMWK deficiency)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KNG1_HUMAN

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Related Literatures of Post-Translational Modification
Hydroxylation
ReferencePubMed
"Purification and identification of [hydroxyprolyl3]bradykinin inascitic fluid from a patient with gastric cancer.";
Maeda H., Matsumura Y., Kato H.;
J. Biol. Chem. 263:16051-16054(1988).
Cited for: AMINO-ACID COMPOSITION OF 381-389, AND HYDROXYLATION AT PRO-383.
"Isolation and identification of hydroxyproline analogues ofbradykinin in human urine.";
Kato H., Matsumura Y., Maeda H.;
FEBS Lett. 232:252-254(1988).
Cited for: PROTEIN SEQUENCE OF 380-389, AND HYDROXYLATION AT PRO-383.
N-linked Glycosylation
ReferencePubMed
"Enrichment of glycopeptides for glycan structure and attachment siteidentification.";
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,Brinkmalm G., Larson G.;
Nat. Methods 6:809-811(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-294, STRUCTURE OFCARBOHYDRATES, AND MASS SPECTROMETRY.
"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-169; ASN-205 AND ASN-294,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-48; ASN-169; ASN-205 ANDASN-294, AND MASS SPECTROMETRY.
"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-169 AND ASN-294, AND MASSSPECTROMETRY.
"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-294.
"Completion of the primary structure of human high-molecular-masskininogen. The amino acid sequence of the entire heavy chain andevidence for its evolution by gene triplication.";
Kellermann J., Lottspeich F., Henschen A., Muller-Esterl W.;
Eur. J. Biochem. 154:471-478(1986).
Cited for: PROTEIN SEQUENCE OF 19-380, GLYCOSYLATION AT ASN-169 AND ASN-205, ANDLACK OF GLYCOSYLATION AT ASN-48.
O-linked Glycosylation
ReferencePubMed
"The amino acid sequence of the light chain of human high-molecular-mass kininogen.";
Lottspeich F., Kellermann J., Henschen A., Foertsch B.,Mueller-Esterl W.;
Eur. J. Biochem. 152:307-314(1985).
Cited for: PROTEIN SEQUENCE OF 379-644.
Phosphorylation
ReferencePubMed
"An initial characterization of the serum phosphoproteome.";
Zhou W., Ross M.M., Tessitore A., Ornstein D., Vanmeter A.,Liotta L.A., Petricoin E.F. III;
J. Proteome Res. 8:5523-5531(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-326; THR-327; SER-329AND SER-332, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.

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