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Protein

Kininogen-1

Gene

KNG1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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: UniProtKB
  2. heparin binding Source: UniProtKB
  3. receptor binding Source: UniProtKB
  4. 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: UniProtKB
  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
Complete GO annotation...

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: UniProtKB
  2. extracellular region Source: UniProtKB
  3. extracellular space Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProtKB
  5. plasma membrane Source: Reactome
  6. platelet alpha granule lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

High molecular weight kininogen deficiency

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAutosomal recessive coagulation defect. Patients with HWMK deficiency do not have a hemorrhagic tendency, but they exhibit abnormal surface-mediated activation of fibrinolysis.

See also OMIM:228960

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)PROSITE-ProRule annotation1 Publication
Glycosylationi48 – 481N-linked (GlcNAc...) (complex)2 Publications
Disulfide bondi83 ↔ 94PROSITE-ProRule annotation1 Publication
Disulfide bondi107 ↔ 126PROSITE-ProRule annotation1 Publication
Disulfide bondi142 ↔ 145PROSITE-ProRule annotation1 Publication
Glycosylationi169 – 1691N-linked (GlcNAc...)4 Publications
Glycosylationi205 – 2051N-linked (GlcNAc...) (complex)4 Publications
Disulfide bondi206 ↔ 218PROSITE-ProRule annotation1 Publication
Disulfide bondi229 ↔ 248PROSITE-ProRule annotation1 Publication
Disulfide bondi264 ↔ 267PROSITE-ProRule annotation1 Publication
Glycosylationi294 – 2941N-linked (GlcNAc...) (complex)6 Publications
Disulfide bondi328 ↔ 340PROSITE-ProRule annotation1 Publication
Modified residuei332 – 3321Phosphoserine1 Publication
Disulfide bondi351 ↔ 370PROSITE-ProRule annotation1 Publication
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.
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

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. 28 interactions.
IntActiP01042. 11 interactions.
MINTiMINT-1512276.
STRINGi9606.ENSP00000265023.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00440000039713.
HOVERGENiHBG006224.
InParanoidiP01042.
KOiK03898.
OMAiHGHGKHK.
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. AlignAdd to basket

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

        10         20         30         40         50
MKLITILFLC SRLLLSLTQE SQSEEIDCND KDLFKAVDAA LKKYNSQNQS
60 70 80 90 100
NNQFVLYRIT EATKTVGSDT FYSFKYEIKE GDCPVQSGKT WQDCEYKDAA
110 120 130 140 150
KAATGECTAT VGKRSSTKFS VATQTCQITP AEGPVVTAQY DCLGCVHPIS
160 170 180 190 200
TQSPDLEPIL RHGIQYFNNN TQHSSLFMLN EVKRAQRQVV AGLNFRITYS
210 220 230 240 250
IVQTNCSKEN FLFLTPDCKS LWNGDTGECT DNAYIDIQLR IASFSQNCDI
260 270 280 290 300
YPGKDFVQPP TKICVGCPRD IPTNSPELEE TLTHTITKLN AENNATFYFK
310 320 330 340 350
IDNVKKARVQ VVAGKKYFID FVARETTCSK ESNEELTESC ETKKLGQSLD
360 370 380 390 400
CNAEVYVVPW EKKIYPTVNC QPLGMISLMK RPPGFSPFRS SRIGEIKEET
410 420 430 440 450
TVSPPHTSMA PAQDEERDSG KEQGHTRRHD WGHEKQRKHN LGHGHKHERD
460 470 480 490 500
QGHGHQRGHG LGHGHEQQHG LGHGHKFKLD DDLEHQGGHV LDHGHKHKHG
510 520 530 540 550
HGHGKHKNKG KKNGKHNGWK TEHLASSSED STTPSAQTQE KTEGPTPIPS
560 570 580 590 600
LAKPGVTVTF SDFQDSDLIA TMMPPISPAP IQSDDDWIPD IQIDPNGLSF
610 620 630 640
NPISDFPDTT SPKCPGRPWK SVSEINPTTQ MKESYYFDLT DGLS
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 (Ref. 5) Curated
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi110026. 28 interactions.
IntActiP01042. 11 interactions.
MINTiMINT-1512276.
STRINGi9606.ENSP00000265023.

Chemistry

BindingDBiP01042.

Protein family/group databases

MEROPSiI25.016.

PTM databases

PhosphoSiteiP01042.

Polymorphism databases

DMDMi124056474.

2D gel databases

SWISS-2DPAGEP01042.

Proteomic databases

PaxDbiP01042.
PeptideAtlasiP01042.
PRIDEiP01042.

Protocols and materials databases

DNASUi3827.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi3827.
GeneCardsiGC03P186435.
HGNCiHGNC:6383. KNG1.
HPAiCAB009809.
HPA001616.
HPA001645.
MIMi228960. phenotype.
612358. gene.
neXtProtiNX_P01042.
Orphaneti483. Congenital high-molecular-weight kininogen deficiency.
PharmGKBiPA225.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG72605.
GeneTreeiENSGT00440000039713.
HOVERGENiHBG006224.
InParanoidiP01042.
KOiK03898.
OMAiHGHGKHK.
OrthoDBiEOG7M98J9.
PhylomeDBiP01042.
TreeFamiTF351852.

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.

Miscellaneous databases

ChiTaRSiKNG1. human.
EvolutionaryTraceiP01042.
GeneWikiiKininogen_1.
GenomeRNAii3827.
NextBioi15047.
PMAP-CutDBB2RCR2.
PROiP01042.
SOURCEiSearch...

Gene expression databases

BgeeiP01042.
CleanExiHS_KNG1.
GenevestigatoriP01042.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "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.
  23. Cited for: GLYCOSYLATION AT ASN-48; ASN-205 AND ASN-294.
  24. "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.
  25. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

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: March 4, 2015
This is version 176 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.