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P01042 (KNG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 170. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. Kininogen-1 heavy chain
  2. T-kinin
    Alternative name(s):
    Ile-Ser-Bradykinin
  3. Bradykinin
    Alternative name(s):
    Kallidin I
  4. Lysyl-bradykinin
    Alternative name(s):
    Kallidin II
  5. Kininogen-1 light chain
  6. Low molecular weight growth-promoting factor
Gene names
Name:KNG1
Synonyms:BDK, KNG
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length644 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subcellular location

Secretedextracellular space.

Tissue specificity

Secreted in plasma. T-kinin is detected in malignant ovarian, colon and breast carcinomas, but not in benign tumors. Ref.11

Post-translational modification

Bradykinin is released from kininogen by plasma kallikrein.

Hydroxylation of Pro-383 occurs prior to the release of bradykinin.

Phosphorylation sites are present in the extracellular medium.

N- and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans. Ref.9 Ref.19 Ref.24

Polymorphism

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.

Involvement in disease

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.

Sequence similarities

Contains 3 cystatin kininogen-type domains.

Ontologies

Keywords
   Biological processBlood coagulation
Hemostasis
Inflammatory response
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Signal
   Molecular functionProtease inhibitor
Thiol protease inhibitor
Vasoactive
Vasodilator
   PTMDisulfide bond
Glycoprotein
Hydroxylation
Phosphoprotein
Pyrrolidone carboxylic acid
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Traceable author statement. Source: Reactome

blood coagulation, intrinsic pathway

Traceable author statement. Source: Reactome

inflammatory response

Traceable author statement PubMed 11385996. Source: UniProtKB

negative regulation of blood coagulation

Inferred from direct assay PubMed 11970955. Source: UniProtKB

negative regulation of cell adhesion

Inferred from direct assay PubMed 11970955. Source: UniProtKB

negative regulation of endopeptidase activity

Inferred from direct assay PubMed 3488317. Source: GOC

negative regulation of proteolysis

Inferred from direct assay PubMed 3488317. Source: UniProt

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

positive regulation of apoptotic process

Non-traceable author statement PubMed 12715893. Source: UniProtKB

positive regulation of cytosolic calcium ion concentration

Inferred from direct assay PubMed 16014619. Source: UniProtKB

positive regulation of renal sodium excretion

Traceable author statement PubMed 11385996. Source: UniProtKB

positive regulation of urine volume

Traceable author statement PubMed 11385996. Source: UniProtKB

smooth muscle contraction

Traceable author statement PubMed 11385996. Source: UniProtKB

vasodilation

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentblood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

extracellular region

Non-traceable author statement PubMed 14718574. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 3488317PubMed 16502470. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

plasma membrane

Traceable author statement. Source: Reactome

platelet alpha granule lumen

Traceable author statement. Source: Reactome

   Molecular_functioncysteine-type endopeptidase inhibitor activity

Inferred from direct assay PubMed 3488317. Source: UniProt

heparin binding

Non-traceable author statement PubMed 12911595. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 23082758PubMed 8710908PubMed 23597562PubMed 23597562. Source: IntAct

receptor binding

Inferred from physical interaction PubMed 11290596. Source: UniProtKB

zinc ion binding

Non-traceable author statement PubMed 12911595. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform HMW (identifier: P01042-1)

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.
Isoform LMW (identifier: P01042-2)

The sequence of this isoform differs from the canonical sequence as follows:
     402-427: VSPPHTSMAPAQDEERDSGKEQGHTR → SHLRSCEYKGRPPKAGAEPASEREVS
     428-644: Missing.
Isoform 3 (identifier: P01042-3)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.2 Ref.9
Chain19 – 644626Kininogen-1
PRO_0000006685
Chain19 – 380362Kininogen-1 heavy chain
PRO_0000006686
Peptide376 – 38914T-kinin Ref.10 Ref.11
PRO_0000372485
Peptide380 – 38910Lysyl-bradykinin Ref.13
PRO_0000006687
Peptide381 – 3899Bradykinin Ref.14
PRO_0000006688
Chain390 – 644255Kininogen-1 light chain
PRO_0000006689
Peptide431 – 4344Low molecular weight growth-promoting factor Ref.15
PRO_0000006690

Regions

Domain28 – 132105Cystatin kininogen-type 1
Domain151 – 254104Cystatin kininogen-type 2
Domain273 – 376104Cystatin kininogen-type 3
Repeat420 – 44930
Repeat450 – 47930
Repeat480 – 51031
Region120 – 15334O-glycosylated at one site only
Compositional bias420 – 51091His-rich

Sites

Site481Not glycosylated
Site379 – 3802Cleavage; by kallikrein
Site389 – 3902Cleavage; by kallikrein

Amino acid modifications

Modified residue191Pyrrolidone carboxylic acid; in mature form By similarity
Modified residue3321Phosphoserine Ref.22
Modified residue38314-hydroxyproline; partial Ref.13 Ref.18
Glycosylation481N-linked (GlcNAc...) (complex) Ref.9 Ref.21 Ref.24
Glycosylation1691N-linked (GlcNAc...) Ref.9 Ref.20 Ref.21 Ref.23
Glycosylation2051N-linked (GlcNAc...) (complex) Ref.9 Ref.21 Ref.23 Ref.24
Glycosylation2941N-linked (GlcNAc...) (complex) Ref.19 Ref.20 Ref.21 Ref.23 Ref.24 Ref.25
Glycosylation4011O-linked (GalNAc...)
Glycosylation5331O-linked (GalNAc...) Ref.12
Glycosylation5421O-linked (GalNAc...)
Glycosylation5461O-linked (GalNAc...) Ref.12
Glycosylation5571O-linked (GalNAc...)
Glycosylation5711O-linked (GalNAc...)
Glycosylation5771O-linked (GalNAc...)
Glycosylation6281O-linked (GalNAc...)
Disulfide bond28 ↔ 614Interchain (between heavy and light chains) Ref.16
Disulfide bond83 ↔ 94 Ref.16
Disulfide bond107 ↔ 126 Ref.16
Disulfide bond142 ↔ 145 Ref.16
Disulfide bond206 ↔ 218 Ref.16
Disulfide bond229 ↔ 248 Ref.16
Disulfide bond264 ↔ 267 Ref.16
Disulfide bond328 ↔ 340 Ref.16
Disulfide bond351 ↔ 370 Ref.16

Natural variations

Alternative sequence189 – 22436Missing in isoform 3.
VSP_047307
Alternative sequence402 – 643242VSPPH…LTDGL → SHLRSCEYKGRPPKAGAEPA SEREV in isoform 3.
VSP_047308
Alternative sequence402 – 42726VSPPH…QGHTR → SHLRSCEYKGRPPKAGAEPA SEREVS in isoform LMW.
VSP_001261
Alternative sequence428 – 644217Missing in isoform LMW.
VSP_001262
Natural variant1631G → S. Ref.5
Corresponds to variant rs5030015 [ dbSNP | Ensembl ].
VAR_019277
Natural variant1781M → T. Ref.4 Ref.5 Ref.7
Corresponds to variant rs1656922 [ dbSNP | Ensembl ].
VAR_019278
Natural variant1971I → M. Ref.8
Corresponds to variant rs2304456 [ dbSNP | Ensembl ].
VAR_028937
Natural variant2121L → P. Ref.5
Corresponds to variant rs5030024 [ dbSNP | Ensembl ].
VAR_019279
Natural variant378 – 3803Missing in T-kinin peptide.
VAR_055233
Natural variant4301D → E.
Corresponds to variant rs5030084 [ dbSNP | Ensembl ].
VAR_048853
Natural variant5811I → T.
Corresponds to variant rs710446 [ dbSNP | Ensembl ].
VAR_048854
Natural variant6421G → A.
Corresponds to variant rs5030087 [ dbSNP | Ensembl ].
VAR_048855

Experimental info

Sequence conflict331L → F in BAF83528. Ref.3
Sequence conflict3111V → A in BAF83528. Ref.3
Sequence conflict5931I → T in AAO61092. Ref.5
Sequence conflict5931I → T AA sequence Ref.12

Sequences

Sequence LengthMass (Da)Tools
Isoform HMW [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 3132B4DF2954C24E

FASTA64471,957
        10         20         30         40         50         60 
MKLITILFLC SRLLLSLTQE SQSEEIDCND KDLFKAVDAA LKKYNSQNQS NNQFVLYRIT 

        70         80         90        100        110        120 
EATKTVGSDT FYSFKYEIKE GDCPVQSGKT WQDCEYKDAA KAATGECTAT VGKRSSTKFS 

       130        140        150        160        170        180 
VATQTCQITP AEGPVVTAQY DCLGCVHPIS TQSPDLEPIL RHGIQYFNNN TQHSSLFMLN 

       190        200        210        220        230        240 
EVKRAQRQVV AGLNFRITYS IVQTNCSKEN FLFLTPDCKS LWNGDTGECT DNAYIDIQLR 

       250        260        270        280        290        300 
IASFSQNCDI YPGKDFVQPP TKICVGCPRD IPTNSPELEE TLTHTITKLN AENNATFYFK 

       310        320        330        340        350        360 
IDNVKKARVQ VVAGKKYFID FVARETTCSK ESNEELTESC ETKKLGQSLD CNAEVYVVPW 

       370        380        390        400        410        420 
EKKIYPTVNC QPLGMISLMK RPPGFSPFRS SRIGEIKEET TVSPPHTSMA PAQDEERDSG 

       430        440        450        460        470        480 
KEQGHTRRHD WGHEKQRKHN LGHGHKHERD QGHGHQRGHG LGHGHEQQHG LGHGHKFKLD 

       490        500        510        520        530        540 
DDLEHQGGHV LDHGHKHKHG HGHGKHKNKG KKNGKHNGWK TEHLASSSED STTPSAQTQE 

       550        560        570        580        590        600 
KTEGPTPIPS LAKPGVTVTF SDFQDSDLIA TMMPPISPAP IQSDDDWIPD IQIDPNGLSF 

       610        620        630        640 
NPISDFPDTT SPKCPGRPWK SVSEINPTTQ MKESYYFDLT DGLS 

« Hide

Isoform LMW [UniParc].

Checksum: C8B398F00BE38BE9
Show »

FASTA42747,883
Isoform 3 [UniParc].

Checksum: E2126218B3462290
Show »

FASTA39143,822

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"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) [PubMed] [Europe PMC] [Abstract]
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]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Wikipedia

High molecular weight kininogen entry

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K02566 mRNA. Translation: AAA35497.1.
M11437 expand/collapse EMBL AC list , M11438, M11521, M11522, M11523, M11524, M11525, M11526, M11527, M11528 Genomic DNA. Translation: AAB59550.1.
M11437 expand/collapse EMBL AC list , 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.
CCDSCCDS3281.1. [P01042-2]
CCDS43183.1. [P01042-1]
CCDS54695.1. [P01042-3]
PIRKGHUH1. A01279.
KGHUL1. A01280.
S13279.
RefSeqNP_000884.1. NM_000893.3. [P01042-2]
NP_001095886.1. NM_001102416.2. [P01042-1]
NP_001159923.1. NM_001166451.1. [P01042-3]
UniGeneHs.77741.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2WOKX-ray1.70B381-389[»]
4ASQX-ray1.99P381-389[»]
4ASRX-ray1.90P381-389[»]
4ECBX-ray2.20A/B498-507[»]
4ECCX-ray2.20A498-510[»]
ProteinModelPortalP01042.
SMRP01042. Positions 266-364.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110026. 13 interactions.
IntActP01042. 11 interactions.
MINTMINT-1512276.
STRING9606.ENSP00000265023.

Chemistry

DrugBankDB01092. Ouabain.

Protein family/group databases

MEROPSI25.016.

PTM databases

PhosphoSiteP01042.

Polymorphism databases

DMDM124056474.

2D gel databases

SWISS-2DPAGEP01042.

Proteomic databases

PaxDbP01042.
PeptideAtlasP01042.
PRIDEP01042.

Protocols and materials databases

DNASU3827.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265023; ENSP00000265023; ENSG00000113889. [P01042-1]
ENST00000287611; ENSP00000287611; ENSG00000113889. [P01042-2]
ENST00000447445; ENSP00000396025; ENSG00000113889. [P01042-3]
GeneID3827.
KEGGhsa:3827.
UCSCuc003fqr.3. human. [P01042-2]
uc011bsa.2. human. [P01042-1]

Organism-specific databases

CTD3827.
GeneCardsGC03P186435.
HGNCHGNC:6383. KNG1.
HPACAB009809.
HPA001616.
HPA001645.
MIM228960. phenotype.
612358. gene.
neXtProtNX_P01042.
Orphanet483. Congenital high-molecular-weight kininogen deficiency.
PharmGKBPA225.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG72605.
HOVERGENHBG006224.
InParanoidP01042.
KOK03898.
OMAWIPDIQI.
OrthoDBEOG7M98J9.
PhylomeDBP01042.
TreeFamTF351852.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP01042.
BgeeP01042.
CleanExHS_KNG1.
GenevestigatorP01042.

Family and domain databases

InterProIPR002395. Kininogen.
IPR027358. Kininogen-type_cystatin_dom.
IPR000010. Prot_inh_cystat.
IPR018073. Prot_inh_cystat_CS.
[Graphical view]
PfamPF00031. Cystatin. 3 hits.
[Graphical view]
PRINTSPR00334. KININOGEN.
SMARTSM00043. CY. 3 hits.
[Graphical view]
PROSITEPS00287. CYSTATIN. 2 hits.
PS51647. CYSTATIN_KININOGEN. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKNG1. human.
EvolutionaryTraceP01042.
GeneWikiKininogen_1.
GenomeRNAi3827.
NextBio15047.
PMAP-CutDBB2RCR2.
PROP01042.
SOURCESearch...

Entry information

Entry nameKNG1_HUMAN
AccessionPrimary (citable) accession number: P01042
Secondary accession number(s): A8K474 expand/collapse secondary AC list , B2RCR2, C9JEX1, P01043, Q53EQ0, Q6PAU9, Q7M4P1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 170 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM