P01042 (KNG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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:

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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	644 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Secreted › extracellular space.
Tissue specificity	Secreted in plasma. T-kinin is detected in malignant ovarian, colon and breast carcinomas, but not in benign tumors. Ref.10
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.8 Ref.18
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 process	Blood coagulation Hemostasis Inflammatory response
Cellular component	Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Signal
Molecular function	Protease inhibitor Thiol protease inhibitor Vasoactive Vasodilator
PTM	Disulfide bond Glycoprotein Hydroxylation Phosphoprotein Pyrrolidone carboxylic acid
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	blood coagulation, intrinsic pathway Traceable author statement. Source: Reactome elevation of cytosolic calcium ion concentration Inferred from direct assay PubMed 16014619. Source: UniProtKB 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 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 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_component	extracellular region Non-traceable author statement PubMed 14718574. Source: UniProtKB extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Traceable author statement. Source: Reactome platelet alpha granule lumen Traceable author statement. Source: Reactome
Molecular_function	cysteine-type endopeptidase inhibitor activity Inferred from electronic annotation. Source: UniProtKB-KW heparin binding Non-traceable author statement PubMed 12911595. Source: UniProtKB zinc ion binding Non-traceable author statement PubMed 12911595. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
C1QBP	Q07021	4	EBI-6378713,EBI-347528

Alternative products

This entry describes 2 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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18	Ref.2 Ref.8
	Chain	19 – 644	626	Kininogen-1		PRO_0000006685
	Chain	19 – 380	362	Kininogen-1 heavy chain		PRO_0000006686
	Peptide	376 – 389	14	T-kinin Ref.9 Ref.10		PRO_0000372485
	Peptide	380 – 389	10	Lysyl-bradykinin Ref.12		PRO_0000006687
	Peptide	381 – 389	9	Bradykinin Ref.13		PRO_0000006688
	Chain	390 – 644	255	Kininogen-1 light chain		PRO_0000006689
	Peptide	431 – 434	4	Low molecular weight growth-promoting factor Ref.14		PRO_0000006690
Regions
	Domain	28 – 132	105	Cystatin kininogen-type 1
	Domain	151 – 254	104	Cystatin kininogen-type 2
	Domain	273 – 376	104	Cystatin kininogen-type 3
	Repeat	420 – 449	30
	Repeat	450 – 479	30
	Repeat	480 – 510	31
	Region	120 – 153	34	O-glycosylated at one site only
	Compositional bias	420 – 510	91	His-rich
Sites
	Site	48	1	Not glycosylated
	Site	379 – 380	2	Cleavage; by kallikrein
	Site	389 – 390	2	Cleavage; by kallikrein
Amino acid modifications
	Modified residue	19	1	Pyrrolidone carboxylic acid; in mature form By similarity
	Modified residue	332	1	Phosphoserine Ref.21
	Modified residue	383	1	4-hydroxyproline; partial Ref.12 Ref.17
	Glycosylation	48	1	N-linked (GlcNAc...) Ref.8 Ref.20
	Glycosylation	169	1	N-linked (GlcNAc...) Ref.8 Ref.19 Ref.20 Ref.22
	Glycosylation	205	1	N-linked (GlcNAc...) Ref.8 Ref.20 Ref.22
	Glycosylation	294	1	N-linked (GlcNAc...) (complex) Ref.18 Ref.19 Ref.20 Ref.22 Ref.23
	Glycosylation	401	1	O-linked (GalNAc...)
	Glycosylation	533	1	O-linked (GalNAc...) Ref.11
	Glycosylation	542	1	O-linked (GalNAc...)
	Glycosylation	546	1	O-linked (GalNAc...) Ref.11
	Glycosylation	557	1	O-linked (GalNAc...)
	Glycosylation	571	1	O-linked (GalNAc...)
	Glycosylation	577	1	O-linked (GalNAc...)
	Glycosylation	628	1	O-linked (GalNAc...)
	Disulfide bond	28 ↔ 614		Interchain (between heavy and light chains) Ref.15
	Disulfide bond	83 ↔ 94		Ref.15
	Disulfide bond	107 ↔ 126		Ref.15
	Disulfide bond	142 ↔ 145		Ref.15
	Disulfide bond	206 ↔ 218		Ref.15
	Disulfide bond	229 ↔ 248		Ref.15
	Disulfide bond	264 ↔ 267		Ref.15
	Disulfide bond	328 ↔ 340		Ref.15
	Disulfide bond	351 ↔ 370		Ref.15
Natural variations
	Alternative sequence	402 – 427	26	VSPPH…QGHTR → SHLRSCEYKGRPPKAGAEPA SEREVS in isoform LMW.		VSP_001261
	Alternative sequence	428 – 644	217	Missing in isoform LMW.		VSP_001262
	Natural variant	163	1	G → S. Ref.5 Corresponds to variant rs5030015 [ dbSNP | Ensembl ].		VAR_019277
	Natural variant	178	1	M → T. Ref.4 Ref.5 Ref.6 Corresponds to variant rs1656922 [ dbSNP | Ensembl ].		VAR_019278
	Natural variant	197	1	I → M. Ref.7 Corresponds to variant rs2304456 [ dbSNP | Ensembl ].		VAR_028937
	Natural variant	212	1	L → P. Ref.5 Corresponds to variant rs5030024 [ dbSNP | Ensembl ].		VAR_019279
	Natural variant	378 – 380	3	Missing in T-kinin peptide.		VAR_055233
	Natural variant	430	1	D → E. Corresponds to variant rs5030084 [ dbSNP | Ensembl ].		VAR_048853
	Natural variant	581	1	I → T. Corresponds to variant rs710446 [ dbSNP | Ensembl ].		VAR_048854
	Natural variant	642	1	G → A. Corresponds to variant rs5030087 [ dbSNP | Ensembl ].		VAR_048855
Experimental info
	Sequence conflict	33	1	L → F in BAF83528. Ref.3
	Sequence conflict	311	1	V → A in BAF83528. Ref.3
	Sequence conflict	593	1	I → T in AAO61092. Ref.5
	Sequence conflict	593	1	I → T AA sequence Ref.11

Sequences

	Sequence		Length	Mass (Da)
	Isoform HMW [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 3132B4DF2954C24E	FASTA	644	71,957
	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
	Isoform LMW [UniParc]. Checksum: C8B398F00BE38BE9	FASTA	427	47,883
	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 TSHLRSCEYK GRPPKAGAEP ASEREVS

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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, MASS SPECTROMETRY.
[15]	"Disulfide bonds in bovine HMW kininogens." Sueyoshi T., Miyata T., Kato H., Iwanaga S. Seikagaku 56:808-808(1984) Cited for: DISULFIDE BONDS.
[16]	"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.
[17]	"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.
[18]	"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.
[19]	"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, MASS SPECTROMETRY. Tissue: Plasma.
[20]	"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, MASS SPECTROMETRY. Tissue: Plasma.
[21]	"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, MASS SPECTROMETRY. Tissue: Serum.
[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, MASS SPECTROMETRY. Tissue: Liver.
[23]	"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, MASS SPECTROMETRY. 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 , 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.
AY248697 Genomic DNA. Translation: AAO61092.1.
AK290839 mRNA. Translation: BAF83528.1.
AK223589 mRNA. Translation: BAD97309.1.
CH471052 Genomic DNA. Translation: EAW78179.1.
BC060039 mRNA. Translation: AAH60039.1.

IPI

IPI00032328.
IPI00215894.

PIR

KGHUH1. A01279.
KGHUL1. A01280.
S13279.

RefSeq

NP_000884.1. NM_000893.3.
NP_001095886.1. NM_001102416.2.

UniGene

Hs.77741.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P01042.

ModBase

Search...

Protein-protein interaction databases

IntAct

P01042. 2 interactions.

STRING

9606.ENSP00000265023.

Protein family/group databases

MEROPS

I25.016.

PTM databases

PhosphoSite

P01042.

Polymorphism databases

DMDM

124056474.

2D gel databases

SWISS-2DPAGE

P01042.

Proteomic databases

PaxDb

P01042.

PeptideAtlas

P01042.

PRIDE

P01042.

Protocols and materials databases

DNASU

3827.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000265023; ENSP00000265023; ENSG00000113889.
ENST00000287611; ENSP00000287611; ENSG00000113889.

GeneID

3827.

KEGG

hsa:3827.

UCSC

uc003fqr.3. human.
uc011bsa.2. human.

Organism-specific databases

CTD

3827.

GeneCards

GC03P186435.

HGNC

HGNC:6383. KNG1.

HPA

CAB009809.
HPA001616.
HPA001645.

MIM

228960. phenotype.
612358. gene.

neXtProt

NX_P01042.

Orphanet

483. Congenital high-molecular-weight kininogen deficiency.

PharmGKB

PA225.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG72605.

HOVERGEN

HBG006224.

InParanoid

P01042.

KO

K03898.

OMA

HGKHKNK.

OrthoDB

EOG4QNMVT.

PhylomeDB

P01042.

Enzyme and pathway databases

Pathway_Interaction_DB

amb2_neutrophils_pathway. amb2 Integrin signaling.
syndecan_2_pathway. Syndecan-2-mediated signaling events.

Reactome

REACT_111102. Signal Transduction.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P01042.

Bgee

P01042.

CleanEx

HS_KNG1.

Genevestigator

P01042.

GermOnline

ENSG00000113889. Homo sapiens.

Family and domain databases

InterPro

IPR002395. Kininogen.
IPR027358. Kininogen-type_cystatin_dom.
IPR000010. Prot_inh_cystat.
IPR018073. Prot_inh_cystat_CS.
[Graphical view]

Pfam

PF00031. Cystatin. 3 hits.
[Graphical view]

PRINTS

PR00334. KININOGEN.

SMART

SM00043. CY. 3 hits.
[Graphical view]

PROSITE

PS00287. CYSTATIN. 2 hits.
PS51647. CYSTATIN_KININOGEN. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

KNG1. human.

DrugBank

DB01092. Ouabain.

EvolutionaryTrace

P01042.

GenomeRNAi

3827.

NextBio

15047.

PMAP-CutDB

B2RCR2.

SOURCE

Search...

Entry information

Entry name

KNG1_HUMAN

Accession

Primary (citable) accession number: P01042
Secondary accession number(s): A8K474 , B2RCR2, P01043, Q53EQ0, Q6PAU9, Q7M4P1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 156 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.