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P01042

- KNG1_HUMAN

UniProt

P01042 - KNG1_HUMAN

Protein

Kininogen-1

Gene

KNG1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 172 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei48 – 481Not glycosylated
    Sitei379 – 3802Cleavage; by kallikrein
    Sitei389 – 3902Cleavage; by kallikrein

    GO - Molecular functioni

    1. cysteine-type endopeptidase inhibitor activity Source: UniProt
    2. heparin binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. receptor binding Source: UniProtKB
    5. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. blood coagulation, intrinsic pathway Source: Reactome
    3. inflammatory response Source: UniProtKB
    4. negative regulation of blood coagulation Source: UniProtKB
    5. negative regulation of cell adhesion Source: UniProtKB
    6. negative regulation of endopeptidase activity Source: GOC
    7. negative regulation of proteolysis Source: UniProt
    8. platelet activation Source: Reactome
    9. platelet degranulation Source: Reactome
    10. positive regulation of apoptotic process Source: UniProtKB
    11. positive regulation of cytosolic calcium ion concentration Source: UniProtKB
    12. positive regulation of renal sodium excretion Source: UniProtKB
    13. positive regulation of urine volume Source: UniProtKB
    14. smooth muscle contraction Source: UniProtKB
    15. vasodilation Source: UniProtKB-KW

    Keywords - Molecular functioni

    Protease inhibitor, Thiol protease inhibitor, Vasoactive, Vasodilator

    Keywords - Biological processi

    Blood coagulation, Hemostasis, Inflammatory response

    Enzyme and pathway databases

    ReactomeiREACT_14819. Peptide ligand-binding receptors.
    REACT_18283. G alpha (q) signalling events.
    REACT_19231. G alpha (i) signalling events.
    REACT_326. Intrinsic Pathway.

    Protein family/group databases

    MEROPSiI25.016.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Kininogen-1
    Alternative name(s):
    Alpha-2-thiol proteinase inhibitor
    Fitzgerald factor
    High molecular weight kininogen
    Short name:
    HMWK
    Williams-Fitzgerald-Flaujeac factor
    Cleaved into the following 6 chains:
    Alternative name(s):
    Ile-Ser-Bradykinin
    Alternative name(s):
    Kallidin I
    Alternative name(s):
    Kallidin II
    Gene namesi
    Name:KNG1
    Synonyms:BDK, KNG
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:6383. KNG1.

    Subcellular locationi

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. extracellular region Source: UniProtKB
    3. extracellular space Source: UniProt
    4. extracellular vesicular exosome Source: UniProt
    5. plasma membrane Source: Reactome
    6. platelet alpha granule lumen Source: Reactome

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    High molecular weight kininogen deficiency (HMWK deficiency) [MIM:228960]: Autosomal recessive coagulation defect. Patients with HWMK deficiency do not have a hemorrhagic tendency, but they exhibit abnormal surface-mediated activation of fibrinolysis.
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi228960. phenotype.
    Orphaneti483. Congenital high-molecular-weight kininogen deficiency.
    PharmGKBiPA225.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 18182 PublicationsAdd
    BLAST
    Chaini19 – 644626Kininogen-1PRO_0000006685Add
    BLAST
    Chaini19 – 380362Kininogen-1 heavy chainPRO_0000006686Add
    BLAST
    Peptidei376 – 38914T-kininPRO_0000372485Add
    BLAST
    Peptidei380 – 38910Lysyl-bradykininPRO_0000006687
    Peptidei381 – 3899BradykininPRO_0000006688
    Chaini390 – 644255Kininogen-1 light chainPRO_0000006689Add
    BLAST
    Peptidei431 – 4344Low molecular weight growth-promoting factorPRO_0000006690

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei19 – 191Pyrrolidone carboxylic acid; in mature formBy similarity
    Disulfide bondi28 ↔ 614Interchain (between heavy and light chains)1 PublicationPROSITE-ProRule annotation
    Glycosylationi48 – 481N-linked (GlcNAc...) (complex)2 Publications
    Disulfide bondi83 ↔ 941 PublicationPROSITE-ProRule annotation
    Disulfide bondi107 ↔ 1261 PublicationPROSITE-ProRule annotation
    Disulfide bondi142 ↔ 1451 PublicationPROSITE-ProRule annotation
    Glycosylationi169 – 1691N-linked (GlcNAc...)4 Publications
    Glycosylationi205 – 2051N-linked (GlcNAc...) (complex)4 Publications
    Disulfide bondi206 ↔ 2181 PublicationPROSITE-ProRule annotation
    Disulfide bondi229 ↔ 2481 PublicationPROSITE-ProRule annotation
    Disulfide bondi264 ↔ 2671 PublicationPROSITE-ProRule annotation
    Glycosylationi294 – 2941N-linked (GlcNAc...) (complex)6 Publications
    Disulfide bondi328 ↔ 3401 PublicationPROSITE-ProRule annotation
    Modified residuei332 – 3321Phosphoserine1 Publication
    Disulfide bondi351 ↔ 3701 PublicationPROSITE-ProRule annotation
    Modified residuei383 – 38314-hydroxyproline; partial2 Publications
    Glycosylationi401 – 4011O-linked (GalNAc...)
    Glycosylationi533 – 5331O-linked (GalNAc...)1 Publication
    Glycosylationi542 – 5421O-linked (GalNAc...)
    Glycosylationi546 – 5461O-linked (GalNAc...)1 Publication
    Glycosylationi557 – 5571O-linked (GalNAc...)
    Glycosylationi571 – 5711O-linked (GalNAc...)
    Glycosylationi577 – 5771O-linked (GalNAc...)
    Glycosylationi628 – 6281O-linked (GalNAc...)

    Post-translational modificationi

    Bradykinin is released from kininogen by plasma kallikrein.
    Hydroxylation of Pro-383 occurs prior to the release of bradykinin.2 Publications
    Phosphorylation sites are present in the extracellular medium.1 Publication
    N- and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans.7 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation, Phosphoprotein, Pyrrolidone carboxylic acid

    Proteomic databases

    PaxDbiP01042.
    PeptideAtlasiP01042.
    PRIDEiP01042.

    2D gel databases

    SWISS-2DPAGEP01042.

    PTM databases

    PhosphoSiteiP01042.

    Miscellaneous databases

    PMAP-CutDBB2RCR2.

    Expressioni

    Tissue specificityi

    Secreted in plasma. T-kinin is detected in malignant ovarian, colon and breast carcinomas, but not in benign tumors.1 Publication

    Gene expression databases

    ArrayExpressiP01042.
    BgeeiP01042.
    CleanExiHS_KNG1.
    GenevestigatoriP01042.

    Organism-specific databases

    HPAiCAB009809.
    HPA001616.
    HPA001645.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AnceQ107142EBI-6378713,EBI-115736From a different organism.
    BDKRB1P466632EBI-6623250,EBI-6623218
    BDKRB2P304112EBI-6623273,EBI-6623386
    C1QBPQ070214EBI-6378713,EBI-347528

    Protein-protein interaction databases

    BioGridi110026. 13 interactions.
    IntActiP01042. 11 interactions.
    MINTiMINT-1512276.
    STRINGi9606.ENSP00000265023.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WOKX-ray1.70B381-389[»]
    4ASQX-ray1.99P381-389[»]
    4ASRX-ray1.90P381-389[»]
    4ECBX-ray2.20A/B498-507[»]
    4ECCX-ray2.20A498-510[»]
    ProteinModelPortaliP01042.
    SMRiP01042. Positions 266-364.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP01042.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini28 – 132105Cystatin kininogen-type 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini151 – 254104Cystatin kininogen-type 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini273 – 376104Cystatin kininogen-type 3PROSITE-ProRule annotationAdd
    BLAST
    Repeati420 – 44930Add
    BLAST
    Repeati450 – 47930Add
    BLAST
    Repeati480 – 51031Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni120 – 15334O-glycosylated at one site onlyAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi420 – 51091His-richAdd
    BLAST

    Sequence similaritiesi

    Contains 3 cystatin kininogen-type domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG72605.
    HOVERGENiHBG006224.
    InParanoidiP01042.
    KOiK03898.
    OMAiWIPDIQI.
    OrthoDBiEOG7M98J9.
    PhylomeDBiP01042.
    TreeFamiTF351852.

    Family and domain databases

    InterProiIPR002395. Kininogen.
    IPR027358. Kininogen-type_cystatin_dom.
    IPR000010. Prot_inh_cystat.
    IPR018073. Prot_inh_cystat_CS.
    [Graphical view]
    PfamiPF00031. Cystatin. 3 hits.
    [Graphical view]
    PRINTSiPR00334. KININOGEN.
    SMARTiSM00043. CY. 3 hits.
    [Graphical view]
    PROSITEiPS00287. CYSTATIN. 2 hits.
    PS51647. CYSTATIN_KININOGEN. 3 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform HMW (identifier: P01042-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MKLITILFLC SRLLLSLTQE SQSEEIDCND KDLFKAVDAA LKKYNSQNQS    50
    NNQFVLYRIT EATKTVGSDT FYSFKYEIKE GDCPVQSGKT WQDCEYKDAA 100
    KAATGECTAT VGKRSSTKFS VATQTCQITP AEGPVVTAQY DCLGCVHPIS 150
    TQSPDLEPIL RHGIQYFNNN TQHSSLFMLN EVKRAQRQVV AGLNFRITYS 200
    IVQTNCSKEN FLFLTPDCKS LWNGDTGECT DNAYIDIQLR IASFSQNCDI 250
    YPGKDFVQPP TKICVGCPRD IPTNSPELEE TLTHTITKLN AENNATFYFK 300
    IDNVKKARVQ VVAGKKYFID FVARETTCSK ESNEELTESC ETKKLGQSLD 350
    CNAEVYVVPW EKKIYPTVNC QPLGMISLMK RPPGFSPFRS SRIGEIKEET 400
    TVSPPHTSMA PAQDEERDSG KEQGHTRRHD WGHEKQRKHN LGHGHKHERD 450
    QGHGHQRGHG LGHGHEQQHG LGHGHKFKLD DDLEHQGGHV LDHGHKHKHG 500
    HGHGKHKNKG KKNGKHNGWK TEHLASSSED STTPSAQTQE KTEGPTPIPS 550
    LAKPGVTVTF SDFQDSDLIA TMMPPISPAP IQSDDDWIPD IQIDPNGLSF 600
    NPISDFPDTT SPKCPGRPWK SVSEINPTTQ MKESYYFDLT DGLS 644
    Length:644
    Mass (Da):71,957
    Last modified:January 23, 2007 - v2
    Checksum:i3132B4DF2954C24E
    GO
    Isoform LMW (identifier: P01042-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         402-427: VSPPHTSMAPAQDEERDSGKEQGHTR → SHLRSCEYKGRPPKAGAEPASEREVS
         428-644: Missing.

    Show »
    Length:427
    Mass (Da):47,883
    Checksum:iC8B398F00BE38BE9
    GO
    Isoform 3 (identifier: P01042-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         189-224: Missing.
         402-643: VSPPHTSMAP...SYYFDLTDGL → SHLRSCEYKGRPPKAGAEPASEREV

    Note: Gene prediction based on EST data.

    Show »
    Length:391
    Mass (Da):43,822
    Checksum:iE2126218B3462290
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti33 – 331L → F in BAF83528. (PubMed:14702039)Curated
    Sequence conflicti311 – 3111V → A in BAF83528. (PubMed:14702039)Curated
    Sequence conflicti593 – 5931I → T in AAO61092. 1 PublicationCurated
    Sequence conflicti593 – 5931I → T AA sequence (PubMed:4054110)Curated

    Polymorphismi

    The T-kinin peptide is missing residues 378 to 380, probably as a result of a naturally occurring variant. The complete sequence of the T-kinin peptide is therefore ISRPPGFSPFR. This peptide is associated with malignant tumors but not with benign ones.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti163 – 1631G → S.1 Publication
    Corresponds to variant rs5030015 [ dbSNP | Ensembl ].
    VAR_019277
    Natural varianti178 – 1781M → T.3 Publications
    Corresponds to variant rs1656922 [ dbSNP | Ensembl ].
    VAR_019278
    Natural varianti197 – 1971I → M.1 Publication
    Corresponds to variant rs2304456 [ dbSNP | Ensembl ].
    VAR_028937
    Natural varianti212 – 2121L → P.1 Publication
    Corresponds to variant rs5030024 [ dbSNP | Ensembl ].
    VAR_019279
    Natural varianti378 – 3803Missing in T-kinin peptide. 2 Publications
    VAR_055233
    Natural varianti430 – 4301D → E.
    Corresponds to variant rs5030084 [ dbSNP | Ensembl ].
    VAR_048853
    Natural varianti581 – 5811I → T.
    Corresponds to variant rs710446 [ dbSNP | Ensembl ].
    VAR_048854
    Natural varianti642 – 6421G → A.
    Corresponds to variant rs5030087 [ dbSNP | Ensembl ].
    VAR_048855

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei189 – 22436Missing in isoform 3. CuratedVSP_047307Add
    BLAST
    Alternative sequencei402 – 643242VSPPH…LTDGL → SHLRSCEYKGRPPKAGAEPA SEREV in isoform 3. CuratedVSP_047308Add
    BLAST
    Alternative sequencei402 – 42726VSPPH…QGHTR → SHLRSCEYKGRPPKAGAEPA SEREVS in isoform LMW. 4 PublicationsVSP_001261Add
    BLAST
    Alternative sequencei428 – 644217Missing in isoform LMW. 4 PublicationsVSP_001262Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02566 mRNA. Translation: AAA35497.1.
    M11437
    , M11438, M11521, M11522, M11523, M11524, M11525, M11526, M11527, M11528 Genomic DNA. Translation: AAB59550.1.
    M11437
    , M11438, M11521, M11522, M11523, M11524, M11525, M11526, M11527, M11528 Genomic DNA. Translation: AAB59551.1.
    AK315230 mRNA. Translation: BAG37659.1.
    AK290839 mRNA. Translation: BAF83528.1.
    AK223589 mRNA. Translation: BAD97309.1.
    AY248697 Genomic DNA. Translation: AAO61092.1.
    AC109780 Genomic DNA. No translation available.
    AC112907 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW78179.1.
    BC060039 mRNA. Translation: AAH60039.1.
    CCDSiCCDS3281.1. [P01042-2]
    CCDS43183.1. [P01042-1]
    CCDS54695.1. [P01042-3]
    PIRiA01279. KGHUH1.
    A01280. KGHUL1.
    S13279.
    RefSeqiNP_000884.1. NM_000893.3. [P01042-2]
    NP_001095886.1. NM_001102416.2. [P01042-1]
    NP_001159923.1. NM_001166451.1. [P01042-3]
    UniGeneiHs.77741.

    Genome annotation databases

    EnsembliENST00000265023; ENSP00000265023; ENSG00000113889. [P01042-1]
    ENST00000287611; ENSP00000287611; ENSG00000113889. [P01042-2]
    ENST00000447445; ENSP00000396025; ENSG00000113889. [P01042-3]
    GeneIDi3827.
    KEGGihsa:3827.
    UCSCiuc003fqr.3. human. [P01042-2]
    uc011bsa.2. human. [P01042-1]

    Polymorphism databases

    DMDMi124056474.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    High molecular weight kininogen entry

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02566 mRNA. Translation: AAA35497.1 .
    M11437
    , M11438 , M11521 , M11522 , M11523 , M11524 , M11525 , M11526 , M11527 , M11528 Genomic DNA. Translation: AAB59550.1 .
    M11437
    , M11438 , M11521 , M11522 , M11523 , M11524 , M11525 , M11526 , M11527 , M11528 Genomic DNA. Translation: AAB59551.1 .
    AK315230 mRNA. Translation: BAG37659.1 .
    AK290839 mRNA. Translation: BAF83528.1 .
    AK223589 mRNA. Translation: BAD97309.1 .
    AY248697 Genomic DNA. Translation: AAO61092.1 .
    AC109780 Genomic DNA. No translation available.
    AC112907 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW78179.1 .
    BC060039 mRNA. Translation: AAH60039.1 .
    CCDSi CCDS3281.1. [P01042-2 ]
    CCDS43183.1. [P01042-1 ]
    CCDS54695.1. [P01042-3 ]
    PIRi A01279. KGHUH1.
    A01280. KGHUL1.
    S13279.
    RefSeqi NP_000884.1. NM_000893.3. [P01042-2 ]
    NP_001095886.1. NM_001102416.2. [P01042-1 ]
    NP_001159923.1. NM_001166451.1. [P01042-3 ]
    UniGenei Hs.77741.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2WOK X-ray 1.70 B 381-389 [» ]
    4ASQ X-ray 1.99 P 381-389 [» ]
    4ASR X-ray 1.90 P 381-389 [» ]
    4ECB X-ray 2.20 A/B 498-507 [» ]
    4ECC X-ray 2.20 A 498-510 [» ]
    ProteinModelPortali P01042.
    SMRi P01042. Positions 266-364.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110026. 13 interactions.
    IntActi P01042. 11 interactions.
    MINTi MINT-1512276.
    STRINGi 9606.ENSP00000265023.

    Chemistry

    DrugBanki DB01092. Ouabain.

    Protein family/group databases

    MEROPSi I25.016.

    PTM databases

    PhosphoSitei P01042.

    Polymorphism databases

    DMDMi 124056474.

    2D gel databases

    SWISS-2DPAGE P01042.

    Proteomic databases

    PaxDbi P01042.
    PeptideAtlasi P01042.
    PRIDEi P01042.

    Protocols and materials databases

    DNASUi 3827.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265023 ; ENSP00000265023 ; ENSG00000113889 . [P01042-1 ]
    ENST00000287611 ; ENSP00000287611 ; ENSG00000113889 . [P01042-2 ]
    ENST00000447445 ; ENSP00000396025 ; ENSG00000113889 . [P01042-3 ]
    GeneIDi 3827.
    KEGGi hsa:3827.
    UCSCi uc003fqr.3. human. [P01042-2 ]
    uc011bsa.2. human. [P01042-1 ]

    Organism-specific databases

    CTDi 3827.
    GeneCardsi GC03P186435.
    HGNCi HGNC:6383. KNG1.
    HPAi CAB009809.
    HPA001616.
    HPA001645.
    MIMi 228960. phenotype.
    612358. gene.
    neXtProti NX_P01042.
    Orphaneti 483. Congenital high-molecular-weight kininogen deficiency.
    PharmGKBi PA225.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG72605.
    HOVERGENi HBG006224.
    InParanoidi P01042.
    KOi K03898.
    OMAi WIPDIQI.
    OrthoDBi EOG7M98J9.
    PhylomeDBi P01042.
    TreeFami TF351852.

    Enzyme and pathway databases

    Reactomei REACT_14819. Peptide ligand-binding receptors.
    REACT_18283. G alpha (q) signalling events.
    REACT_19231. G alpha (i) signalling events.
    REACT_326. Intrinsic Pathway.

    Miscellaneous databases

    ChiTaRSi KNG1. human.
    EvolutionaryTracei P01042.
    GeneWikii Kininogen_1.
    GenomeRNAii 3827.
    NextBioi 15047.
    PMAP-CutDB B2RCR2.
    PROi P01042.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P01042.
    Bgeei P01042.
    CleanExi HS_KNG1.
    Genevestigatori P01042.

    Family and domain databases

    InterProi IPR002395. Kininogen.
    IPR027358. Kininogen-type_cystatin_dom.
    IPR000010. Prot_inh_cystat.
    IPR018073. Prot_inh_cystat_CS.
    [Graphical view ]
    Pfami PF00031. Cystatin. 3 hits.
    [Graphical view ]
    PRINTSi PR00334. KININOGEN.
    SMARTi SM00043. CY. 3 hits.
    [Graphical view ]
    PROSITEi PS00287. CYSTATIN. 2 hits.
    PS51647. CYSTATIN_KININOGEN. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation of a human cDNA for alpha 2-thiol proteinase inhibitor and its identity with low molecular weight kininogen."
      Ohkubo I., Kurachi K., Takasawa T., Shiokawa H., Sasaki M.
      Biochemistry 23:5691-5697(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LMW).
    2. "Cloning and sequence analysis of cDNAs for human high molecular weight and low molecular weight prekininogens. Primary structures of two human prekininogens."
      Takagaki Y., Kitamura N., Nakanishi S.
      J. Biol. Chem. 260:8601-8609(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS HMW AND LMW).
      Tissue: Liver.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LMW).
      Tissue: Liver.
    4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LMW), VARIANT THR-178.
      Tissue: Kidney.
    5. SeattleSNPs variation discovery resource
      Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-163; THR-178 AND PRO-212.
    6. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT THR-178.
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LMW), VARIANT MET-197.
      Tissue: Kidney.
    9. "Completion of the primary structure of human high-molecular-mass kininogen. The amino acid sequence of the entire heavy chain and evidence for its evolution by gene triplication."
      Kellermann J., Lottspeich F., Henschen A., Muller-Esterl W.
      Eur. J. Biochem. 154:471-478(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-380, GLYCOSYLATION AT ASN-169 AND ASN-205, LACK OF GLYCOSYLATION AT ASN-48.
    10. "Human Ile-Ser-bradykinin, identical with rat T-kinin, is a major permeability factor in ovarian carcinoma ascites."
      Wunderer G., Walter I., Mueller E., Henschen A.
      Biol. Chem. Hoppe-Seyler 367:1231-1234(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 376-389 (T-KININ), VARIANT 378-LEU--LYS-380 DEL.
      Tissue: Ascites.
    11. "Ile-Ser-bradykinin is an aberrant permeability factor in various human malignant effusions."
      Wunderer G., Walter I., Eschenbacher B., Lang M., Kellermann J., Kindermann G.
      Biol. Chem. Hoppe-Seyler 371:977-981(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 376-389 (T-KININ), TISSUE SPECIFICITY, VARIANT 378-LEU--LYS-380 DEL.
    12. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 379-644.
    13. "Isolation and identification of hydroxyproline analogues of bradykinin in human urine."
      Kato H., Matsumura Y., Maeda H.
      FEBS Lett. 232:252-254(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 380-389, HYDROXYLATION AT PRO-383.
    14. "Structural features of plasma kinins and kininogens."
      Pierce J.V.
      Fed. Proc. 27:52-57(1968) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 381-389.
    15. "Purification from human plasma of a tetrapeptide that potentiates insulin-like growth factor-I activity in chick embryo cartilage."
      Straczek J., Maachi F., Le Nguyen D., Becchi M., Heulin M.H., Nabet P., Belleville F.
      FEBS Lett. 373:207-211(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 431-434, IDENTIFICATION BY MASS SPECTROMETRY.
    16. "Disulfide bonds in bovine HMW kininogens."
      Sueyoshi T., Miyata T., Kato H., Iwanaga S.
      Seikagaku 56:808-808(1984)
      Cited for: DISULFIDE BONDS.
    17. "Structural organization of the human kininogen gene and a model for its evolution."
      Kitamura N., Kitagawa H., Fukushima D., Takagaki Y., Miyata T., Nakanishi S.
      J. Biol. Chem. 260:8610-8617(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE STRUCTURE.
    18. "Purification and identification of [hydroxyprolyl3]bradykinin in ascitic fluid from a patient with gastric cancer."
      Maeda H., Matsumura Y., Kato H.
      J. Biol. Chem. 263:16051-16054(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: AMINO-ACID COMPOSITION OF 381-389, HYDROXYLATION AT PRO-383.
    19. "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
      Zhang H., Li X.-J., Martin D.B., Aebersold R.
      Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-294.
    20. "Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
      Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
      Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-169 AND ASN-294.
      Tissue: Plasma.
    21. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-48; ASN-169; ASN-205 AND ASN-294.
      Tissue: Plasma.
    22. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Serum.
    23. "Glycoproteomics analysis of human liver tissue by combination of multiple 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) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-169; ASN-205 AND ASN-294.
      Tissue: Liver.
    24. Cited for: GLYCOSYLATION AT ASN-48; ASN-205 AND ASN-294.
    25. "Enrichment of glycopeptides for glycan structure and attachment site identification."
      Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
      Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-294, STRUCTURE OF CARBOHYDRATES.
      Tissue: Cerebrospinal fluid.

    Entry informationi

    Entry nameiKNG1_HUMAN
    AccessioniPrimary (citable) accession number: P01042
    Secondary accession number(s): A8K474
    , B2RCR2, C9JEX1, P01043, Q53EQ0, Q6PAU9, Q7M4P1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 172 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3