| UniProt ID | KNG1_MOUSE | |
|---|---|---|
| UniProt AC | O08677 | |
| Protein Name | Kininogen-1 | |
| Gene Name | Kng1 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 661 | |
| 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 (By similarity).. | |
| Protein Sequence | MKLITTLLLCSGLLLTLTQGEEAQEIDCNDEAVFQAVDFSLKQFNPGVKSGNQYMLHRVIEGTKTDGSPTFYSFKYLIKEGNCSAQSGLAWQDCDFKDAEEAATGECTATVGKRENEFFIVTQTCKIAPSKAPILKAYFPCIGCVHAISTDSPDLEPVLKHSIEHFNNNTDHSHLFTLRKVKSAHRQVVAGLNFDITYTIVQTNCSKERFPSLHGDCVALPNGDDGECRGNLFMDINNKIANFSQSCTLYSGDDLVEALPKPCPGCPRDIPVDSPELKEVLGHSIAQLNAENDHPFYYKIDTVKKATSQVVAGTKYVIEFIARETKCSKESNTELAEDCEIKHLGQSLDCNANVYMRPWENKVVPTVKCQALDMTEMARRPPGFSPFRSVTVQETKEGRTVSPPYIAREQEERDAETEQGPTHGHGWLHEKQIKANKNHRGHKHGHDHGHWSPRRHGLGHGHQKPHGLGHGHQLKLDYLRHQREDGDDHTHTVGHGHGHGHGHGHGHGHGHGHGHGHGHGHGHGKHTNKDKNSVKQTTQRTESLASSSEYSTTSTQMQGRTEGPTLTPPRAQPTVTSSGFQDSDFIEDVVATTPPYDTGAHDDLIPDIHVQPDSLSFKLISDFPEATSPKCPGRPWKPASWEDPNTETTEFSDFDLLDALS | |
| 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 |
|---|---|---|---|---|---|
| 64 | Ubiquitination | HRVIEGTKTDGSPTF EEEEECCCCCCCCCE | 56.31 | 22790023 | |
| 65 (in isoform 2) | Phosphorylation | - | 45.49 | 24719451 | |
| 75 | Ubiquitination | SPTFYSFKYLIKEGN CCCEEEEEEEEECCC | 32.95 | 22790023 | |
| 82 | N-linked_Glycosylation | KYLIKEGNCSAQSGL EEEEECCCCCCCCCC | 20.05 | 17330941 | |
| 150 (in isoform 2) | Phosphorylation | - | 34.09 | 24719451 | |
| 168 | N-linked_Glycosylation | HSIEHFNNNTDHSHL HHHHHCCCCCCCCCE | 52.41 | 16944957 | |
| 204 | N-linked_Glycosylation | TYTIVQTNCSKERFP EEEEEECCCCCCCCC | 15.80 | 17330941 | |
| 242 | N-linked_Glycosylation | DINNKIANFSQSCTL ECCHHHHHHHCCCEE | 40.34 | 17330941 | |
| 274 | Phosphorylation | PRDIPVDSPELKEVL CCCCCCCCHHHHHHH | 22.10 | 27180971 | |
| 328 (in isoform 2) | Phosphorylation | - | 40.80 | 24719451 | |
| 331 | Phosphorylation | ETKCSKESNTELAED HHCCCCCCCCHHHHH | 53.43 | - | |
| 369 | S-palmitoylation | KVVPTVKCQALDMTE CCCCEEEEEECCHHH | 2.19 | 26165157 | |
| 385 | Phosphorylation | ARRPPGFSPFRSVTV HCCCCCCCCCCEEEE | 29.10 | - | |
| 396 | Acetylation | SVTVQETKEGRTVSP EEEEEEECCCCCCCC | 58.37 | - | |
| 400 | Phosphorylation | QETKEGRTVSPPYIA EEECCCCCCCCCCCC | 35.87 | 28059163 | |
| 405 | Phosphorylation | GRTVSPPYIAREQEE CCCCCCCCCCCHHHH | 15.59 | 28059163 | |
| 427 (in isoform 2) | Phosphorylation | - | 6.72 | 25521595 | |
| 428 (in isoform 2) | Phosphorylation | - | 4.41 | 23375375 | |
| 546 | Phosphorylation | QRTESLASSSEYSTT HHHHHHHHCCCCCCC | 39.42 | 28285833 | |
| 567 | Phosphorylation | RTEGPTLTPPRAQPT CCCCCCCCCCCCCCC | 33.45 | 27149854 |
| 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 KNG1_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KNG1_MOUSE !! | ||||||
* 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_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of KNG1_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| N-linked Glycosylation | |
| Reference | PubMed |
| "Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides."; Bernhard O.K., Kapp E.A., Simpson R.J.; J. Proteome Res. 6:987-995(2007). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-82; ASN-168; ASN-204 ANDASN-242, AND MASS SPECTROMETRY. | |
| "Proteome-wide characterization of N-glycosylation events by diagonalchromatography."; Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,Gevaert K.; J. Proteome Res. 5:2438-2447(2006). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-168, AND MASSSPECTROMETRY. | |
