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Human Metabolome Database Version 2.5

 

Showing metabocard for Bradykinin (HMDB04246)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-08-13 16:11:32
Update Date 2009-05-26 17:04:16
Accession Number HMDB04246
Secondary Accession Numbers Not Available
Common Name Bradykinin
Description Bradykinin is a vasoactive kinin that is liberated from its substrate kininogen by the action of kallikrein, and is known to be involved in a wide range of biologic processes. It may play an important role in blood pressure regulation and the maintenance of normal blood flow. Moreover, in various pathologic states of the cardiovascular system, it appears to provide protective actions against ischemic injury, ventricular hypertrophy, congestive heart failure, and thrombosis. Bradykinin is a potent vasodilator that acts through endothelial B2 kinin receptors to stimulate the release of nitric oxide and endothelium-derived hyperpolarizing factor. Bradykinin deficiency states may play a role in some forms of hypertension, and a relative deficiency in bradykinin may be a contributing factor to worsening heart failure. Experimental studies revealed that mice lacking the B2 receptor gene were more likely to develop hypertension, cardiac hypertrophy, and myocardial damage. Kinins exert several biologic actions. They are involved in nociception, inflammation, capillary permeability, reactive hyperemia, and stimulation of cellular glucose uptake. Bradykinin is a polypeptide that circulates in the plasma in very low concentrations in comparison with the amount of bradykinin found in various body tissues. Kininogens ([alpha] 2 globulins) are synthesized in the liver and circulate at high concentrations in the plasma. There are two kininogenases that convert kininogens into bradykinin: plasma kallikrein, also known as Fletcher factor, and glandular kallikrein, also known as tissue kallikrein. (PMID: 11975815)
Synonyms
  1. Callidin I
  2. Kallidin 9
  3. Kallidin I
  4. L-arginyl-L-prolyl-L-prolylglycyl-L-phenylalanyl-L-seryl-L-prolyl-L-phenylalanyl-L-Arginine
  5. L-Bradykinin
Chemical IUPAC Name (2S)-2-[[(2S)-2-[[(2S)-1-[(2S)-2-[[(2S)-2-[[2-[[(2S)-1-[(2S)-1-[(2S)-2-amino-5-(diaminomethylideneamino)pentanoyl]pyrrolidine-2-carbonyl]pyrrolidine-2-carbonyl]amino]acetyl]amino]-3-phenylpropanoyl]amino]-3-hydroxypropanoyl]pyrrolidine-2-carbonyl]amino]-3-phenylpropanoyl]amino]-5-(diaminomethylideneamino)pentanoic acid
Chemical Formula C50H73N15O11
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Polypeptides
Sub Class
  • Polypeptides
Family
  • Mammalian Metabolite
Species
  • primary alcohol
  • primary amine
  • primary aliphatic amine (alkylamine)
  • carboxylic acid
  • secondary carboxylic acid amide
  • tertiary carboxylic acid amide
  • guanidine
  • aromatic compound
  • heterocyclic compound
Biofunction
Application
Source
  • Endogenous
Average Molecular Weight 1060.208
Monoisotopic Molecular Weight 1059.561401
Isomeric SMILES N[C@@H](CCCNC(N)=N)C(=O)N1CCC[C@H]1C(=O)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CO)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O
Canonical SMILES NC(CCCNC(N)=N)C(=O)N1CCCC1C(=O)N1CCCC1C(=O)NCC(=O)NC(CC1=CC=CC=C1)C(=O)NC(CO)C(=O)N1CCCC1C(=O)NC(CC1=CC=CC=C1)C(=O)NC(CCCNC(N)=N)C(O)=O
KEGG Compound ID C00306 Link Image
BioCyc ID Not Available
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB04246 Link Image
Metagene Link HMDB04246 Link Image
METLIN ID Not Available
PubChem Compound 439201 Link Image
PubChem Substance 3600 Link Image
ChEBI ID Not Available
CAS Registry Number 58-82-2
InChI Identifier InChI=1/C50H73N15O11/c51-32(16-7-21-56-49(52)53)45(72)65-25-11-20-39(65)47(74)64-24-9-18-37(64)43(70)58-28-40(67)59-34(26-30-12-3-1-4-13-30)41(68)62-36(29-66)46(73)63-23-10-19-38(63)44(71)61-35(27-31-14-5-2-6-15-31)42(69)60-33(48(75)76)17-8-22-57-50(54)55/h1-6,12-15,32-39,66H,7-11,16-29,51H2,(H,58,70)(H,59,67)(H,60,69)(H,61,71)(H,62,68)(H,75,76)(H4,52,53,56)(H4,54,55,57)/t32-,33-,34-,35-,36-,37-,38-,39-/m0/s1
Synthesis Reference Postnov, V. N. Some aspects of the synthesis of organic functional groups on inorganic matrices. Napravl. Sintez Tverd. Veshchestv (1987), (2), 109-20.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 0.056599997 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.14 [Predicted by ALOGPS]; -4.9 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location Not Available
Biofluid Location
  • Prostate Tissue
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal)
Biofluid Prostate Tissue
Value 0.5 (0.0-1.0) umol/gr tissue
Age Adult:>18 yrs old
Sex Both
Condition Prostate cancer
Comments Estimated concentration
References
  • Sreekumar A, Poisson LM, Rajendiran TM, Khan AP, Cao Q, Yu J, Laxman B, Mehra R, Lonigro RJ, Li Y, Nyati MK, Ahsan A, Kalyana-Sundaram S, Han B, Cao X, Byun J, Omenn GS, Ghosh D, Pennathur S, Alexander DC, Berger A, Shuster JR, Wei JT, Varambally S, Beecher C, Chinnaiyan AM: Metabolomic profiles delineate potential role for sarcosine in prostate cancer progression. Nature. 2009 Feb 12;457(7231):910-4. [PubMed Link Image]
Associated Disorders
Condition References
Prostate cancer
  • Sreekumar A, Poisson LM, Rajendiran TM, Khan AP, Cao Q, Yu J, Laxman B, Mehra R, Lonigro RJ, Li Y, Nyati MK, Ahsan A, Kalyana-Sundaram S, Han B, Cao X, Byun J, Omenn GS, Ghosh D, Pennathur S, Alexander DC, Berger A, Shuster JR, Wei JT, Varambally S, Beecher C, Chinnaiyan AM: Metabolomic profiles delineate potential role for sarcosine in prostate cancer progression. Nature. 2009 Feb 12;457(7231):910-4. [PubMed Link Image]
OMIM ID
Pathways Not Available
General References Not Available
Metabolic Enzymes
  1. Angiotensin-converting enzyme
  2. Coagulation factor XII
  3. Kininogen-1
  4. Plasma kallikrein
  5. Type-1 angiotensin II receptor
  6. B2 bradykinin receptor
  7. Protein MRVI1
  8. Relaxin-3 receptor 2
  9. Endoplasmic reticulum aminopeptidase 1
  10. Neurolysin, mitochondrial
  11. B1 bradykinin receptor
  12. cDNA FLJ75760, highly similar to Homo sapiens bradykinin receptor B1 (BDKRB1), mRNA
  13. cDNA FLJ55307, highly similar to B2 bradykinin receptor
  14. Bradykinin B1 receptor
  15. B2 bradykinin receptor basal promoter, allele BP-58-T
  16. B2 bradykinin receptor basal promoter, allele BP-58-C
  17. Putative uncharacterized protein DKFZp686O088
Enzyme 1 [top]
Enzyme 1 ID 7050
Enzyme 1 Name Angiotensin-converting enzyme
Enzyme 1 Synonyms
  1. ACE
  2. Dipeptidyl carboxypeptidase I
  3. Kininase II
  4. CD143 antigen
  5. Angiotensin-converting enzyme, soluble form
Enzyme 1 Gene Name ACE
Enzyme 1 Protein Sequence >Angiotensin-converting enzyme
MGAASGRRGPGLLLPLPLLLLLPPQPALALDPGLQPGNFSADEAGAQLFAQSYNSSAEQV
LFQSVAASWAHDTNITAENARRQEEAALLSQEFAEAWGQKAKELYEPIWQNFTDPQLRRI
IGAVRTLGSANLPLAKRQQYNALLSNMSRIYSTAKVCLPNKTATCWSLDPDLTNILASSR
SYAMLLFAWEGWHNAAGIPLKPLYEDFTALSNEAYKQDGFTDTGAYWRSWYNSPTFEDDL
EHLYQQLEPLYLNLHAFVRRALHRRYGDRYINLRGPIPAHLLGDMWAQSWENIYDMVVPF
PDKPNLDVTSTMLQQGWNATHMFRVAEEFFTSLELSPMPPEFWEGSMLEKPADGREVVCH
ASAWDFYNRKDFRIKQCTRVTMDQLSTVHHEMGHIQYYLQYKDLPVSLRRGANPGFHEAI
GDVLALSVSTPEHLHKIGLLDRVTNDTESDINYLLKMALEKIAFLPFGYLVDQWRWGVFS
GRTPPSRYNFDWWYLRTKYQGICPPVTRNETHFDAGAKFHVPNVTPYIRYFVSFVLQFQF
HEALCKEAGYEGPLHQCDIYRSTKAGAKLRKVLQAGSSRPWQEVLKDMVGLDALDAQPLL
KYFQPVTQWLQEQNQQNGEVLGWPEYQWHPPLPDNYPEGIDLVTDEAEASKFVEEYDRTS
QVVWNEYAEANWNYNTNITTETSKILLQKNMQIANHTLKYGTQARKFDVNQLQNTTIKRI
IKKVQDLERAALPAQELEEYNKILLDMETTYSVATVCHPNGSCLQLEPDLTNVMATSRKY
EDLLWAWEGWRDKAGRAILQFYPKYVELINQAARLNGYVDAGDSWRSMYETPSLEQDLER
LFQELQPLYLNLHAYVRRALHRHYGAQHINLEGPIPAHLLGNMWAQTWSNIYDLVVPFPS
APSMDTTEAMLKQGWTPRRMFKEADDFFTSLGLLPVPPEFWNKSMLEKPTDGREVVCHAS
AWDFYNGKDFRIKQCTTVNLEDLVVAHHEMGHIQYFMQYKDLPVALREGANPGFHEAIGD
VLALSVSTPKHLHSLNLLSSEGGSDEHDINFLMKMALDKIAFIPFSYLVDQWRWRVFDGS
ITKENYNQEWWSLRLKYQGLCPPVPRTQGDFDPGAKFHIPSSVPYIRYFVSFIIQFQFHE
ALCQAAGHTGPLHKCDIYQSKEAGQRLATAMKLGFSRPWPEAMQLITGQPNMSASAMLSY
FKPLLDWLRTENELHGEKLGWPQYNWTPNSARSEGPLPDSGRVSFLGLDLDAQQARVGQW
LLLFLGIALLVATLGLSQRLFSIRHRSLHRHSHGPQFGSEVELRHS
Enzyme 1 Number of Residues 1306
Enzyme 1 Molecular Weight 149713.7
Enzyme 1 Theoretical pI 6.36
Enzyme 1 GO Classification
Function
  • catalytic activity
  • exopeptidase activity
  • hydrolase activity
  • metallopeptidase activity
  • peptidase activity
  • peptidase activity, acting on L-amino acid peptides
  • peptidyl-dipeptidase activity
Process
  • macromolecule metabolic process
  • metabolic process
  • protein metabolic process
  • proteolysis
Component
  • cell part
  • membrane
Enzyme 1 General Function Involved in metallopeptidase activity
Enzyme 1 Specific Function Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety
Enzyme 1 Pathways Not Available
Enzyme 1 Reactions
  • Release of a C-terminal dipeptide, oligopeptide!Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II, with increase in vasoconstrictor activity, but no action on angiotensin II COFACTOR Zinc [CPD:C00038] INHIBITOR (S)-N-[3-(3,4-Methylenedioxyphenyl)-2-(mercaptomethyl)-1-oxoprolyl]g lycine [CPD:C01313]
  • (S)-N-[3-(3,4-Methylenedioxyphenyl)-2-(mercaptomethyl)-1-oxoprolyl]- (S)-alanine [CPD:C01314]
  • (S)-N-[3-(3,4-Methylenedioxyphenyl)-2-(acetylthio)methyl-1-oxoprolyl ]glycine benzyl ester [CPD:C01315]
  • (S)-N-[3-(3,4-Methylenedioxyphenyl)-2-(acetylthio)methyl-1-oxoprolyl ]-(S)-alanine benzyl ester [CPD:C01316]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-29
Enzyme 1 Transmembrane Regions
  • 1257-1277
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein Not Available
Enzyme 1 UniProtKB/Swiss-Prot ID P12821 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ACE_HUMAN Link Image
Enzyme 1 PDB ID 1UZF Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >3921 bp
ATGGGGGCCGCCTCGGGCCGCCGGGGGCCGGGGCTGCTGCTGCCGCTGCCGCTGCTGTTG
CTGCTGCCGCCGCAGCCCGCCCTGGCGTTGGACCCCGGGCTGCAGCCCGGCAACTTTTCT
GCTGACGAGGCCGGGGCGCAGCTCTTCGCGCAGAGCTACAACTCCAGCGCCGAACAGGTG
CTGTTCCAGAGCGTGGCCGCCAGCTGGGCGCACGACACCAACATCACCGCGGAGAATGCA
AGGCGCCAGGAGGAAGCAGCCCTGCTCAGCCAGGAGTTTGCGGAGGCCTGGGGCCAGAAG
GCCAAGGAGCTGTATGAACCGATCTGGCAGAACTTCACGGACCCGCAGCTGCGCAGGATC
ATCGGAGCTGTGCGAACCCTGGGCTCTGCCAACCTGCCCCTGGCTAAGCGGCAGCAGTAC
AACGCCCTGCTAAGCAACATGAGCAGGATCTACTCCACCGCCAAGGTCTGCCTCCCCAAC
AAGACTGCCACCTGCTGGTCCCTGGACCCAGATCTCACCAACATCCTGGCTTCCTCGCGA
AGCTACGCCATGCTCCTGTTTGCCTGGGAGGGCTGGCACAACGCTGCGGGCATCCCGCTG
AAACCGCTGTACGAGGATTTCACTGCCCTCAGCAATGAAGCCTACAAGCAGGACGGCTTC
ACAGACACGGGGGCCTACTGGCGCTCCTGGTACAACTCCCCCACCTTCGAGGACGATCTG
GAACACCTCTACCAACAGCTAGAGCCCCTCTACCTGAACCTCCATGCCTTCGTCCGCCGC
GCACTGCATCGCCGATACGGAGACAGATACATCAACCTCAGGGGACCCATCCCTGCTCAT
CTGCTGGGAGACATGTGGGCCCAGAGCTGGGAAAACATCTACGACATGGTGGTGCCTTTC
CCAGACAAGCCCAACCTCGATGTCACCAGTACTATGCTGCAGCAGGGCTGGAACGCCACG
CACATGTTCCGGGTGGCAGAGGAGTTCTTCACCTCCCTGGAGCTCTCCCCCATGCCTCCC
GAGTTCTGGGAAGGGTCGATGCTGGAGAAGCCGGCCGACGGGCGGGAAGTGGTGTGCCAC
GCCTCGGCTTGGGACTTCTACAACAGGAAAGACTTCAGGATCAAGCAGTGCACACGGGTC
ACGATGGACCAGCTCTCCACAGTGCACCATGAGATGGGCCATATACAGTACTACCTGCAG
TACAAGGATCTGCCCGTCTCCCTGCGTCGGGGGGCCAACCCCGGCTTCCATGAGGCCATT
GGGGACGTGCTGGCGCTCTCGGTCTCCACTCCTGAACATCTGCACAAAATCGGCCTGCTG
GACCGTGTCACCAATGACACGGAAAGTGACATCAATTACTTGCTAAAAATGGCACTGGAA
AAAATTGCCTTCCTGCCCTTTGGCTACTTGGTGGACCAGTGGCGCTGGGGGGTCTTTAGT
GGGCGTACCCCCCCTTCCCGCTACAACTTCGACTGGTGGTATCTTCGAACCAAGTATCAG
GGGATCTGTCCTCCTGTTACCCGAAACGAAACCCACTTTGATGCTGGAGCTAAGTTTCAT
GTTCCAAATGTGACACCATACATCAGGTACTTTGTGAGTTTTGTCCTGCAGTTCCAGTTC
CATGAAGCCCTGTGCAAGGAGGCAGGCTATGAGGGCCCACTGCACCAGTGTGACATCTAC
CGGTCCACCAAGGCAGGGGCCAAGCTCCGGAAGGTGCTGCAGGCTGGCTCCTCCAGGCCC
TGGCAGGAGGTGCTGAAGGACATGGTCGGCTTAGATGCCCTGGATGCCCAGCCGCTGCTC
AAGTACTTCCAGCCAGTCACCCAGTGGCTGCAGGAGCAGAACCAGCAGAACGGCGAGGTC
CTGGGCTGGCCCGAGTACCAGTGGCACCCGCCGTTGCCTGACAACTACCCGGAGGGCATA
GACCTGGTGACTGATGAGGCTGAGGCCAGCAAGTTTGTGGAGGAATATGACCGGACATCC
CAGGTGGTGTGGAACGAGTATGCCGAGGCCAACTGGAACTACAACACCAACATCACCACA
GAGACCAGCAAGATTCTGCTGCAGAAGAACATGCAAATAGCCAACCACACCCTGAAGTAC
GGCACCCAGGCCAGGAAGTTTGATGTGAACCAGTTGCAGAACACCACTATCAAGCGGATC
ATAAAGAAGGTTCAGGACCTAGAACGGGCAGCGCTGCCTGCCCAGGAGCTGGAGGAGTAC
AACAAGATCCTGTTGGATATGGAAACCACCTACAGCGTGGCCACTGTGTGCCACCCGAAT
GGCAGCTGCCTGCAGCTCGAGCCAGATCTGACGAATGTGATGGCCACATCCCGGAAATAT
GAAGACCTGTTATGGGCATGGGAGGGCTGGCGAGACAAGGCGGGGAGAGCCATCCTCCAG
TTTTACCCGAAATACGTGGAACTCATCAACCAGGCTGCCCGGCTCAATGGCTATGTAGAT
GCAGGGGACTCGTGGAGGTCTATGTACGAGACACCATCCCTGGAGCAAGACCTGGAGCGG
CTCTTCCAGGAGCTGCAGCCACTCTACCTCAACCTGCATGCCTACGTGCGCCGGGCCCTG
CACCGTCACTACGGGGCCCAGCACATCAACCTGGAGGGGCCCATTCCTGCTCACCTGCTG
GGGAACATGTGGGCGCAGACCTGGTCCAACATCTATGACTTGGTGGTGCCCTTCCCTTCA
GCCCCCTCGATGGACACCACAGAGGCTATGCTAAAGCAGGGCTGGACGCCCAGGAGGATG
TTTAAGGAGGCTGATGATTTCTTCACCTCCCTGGGGCTGCTGCCCGTGCCTCCTGAGTTC
TGGAACAAGTCGATGCTGGAGAAGCCAACCGACGGGCGGGAGGTGGTCTGCCACGCCTCG
GCCTGGGACTTCTACAACGGCAAGGACTTCCGGATCAAGCAGTGCACCACCGTGAACTTG
GAGGACCTGGTGGTGGCCCACCACGAAATGGGCCACATCCAGTATTTCATGCAGTACAAA
GACTTACCTGTGGCCTTGAGGGAGGGTGCCAACCCCGGCTTCCATGAGGCCATTGGGGAC
GTGCTAGCCCTCTCAGTGTCTACGCCCAAGCACCTGCACAGTCTCAACCTGCTGAGCAGT
GAGGGTGGCAGCGACGAGCATGACATCAACTTTCTGATGAAGATGGCCCTTGACAAGATC
GCCTTTATCCCCTTCAGCTACCTCGTCGATCAGTGGCGCTGGAGGGTATTTGATGGAAGC
ATCACCAAGGAGAACTATAACCAGGAGTGGTGGAGCCTCAGGCTGAAGTACCAGGGCCTC
TGCCCCCCAGTGCCCAGGACTCAAGGTGACTTTGACCCAGGGGCCAAGTTCCACATTCCT
TCTAGCGTGCCTTACATCAGGTACTTTGTCAGCTTCATCATCCAGTTCCAGTTCCACGAG
GCACTGTGCCAGGCAGCTGGCCACACGGGCCCCCTGCACAAGTGTGACATCTACCAGTCC
AAGGAGGCCGGGCAGCGCCTGGCGACCGCCATGAAGCTGGGCTTCAGTAGGCCGTGGCCG
GAAGCCATGCAGCTGATCACGGGCCAGCCCAACATGAGCGCCTCGGCCATGTTGAGCTAC
TTCAAGCCGCTGCTGGACTGGCTCCGCACGGAGAACGAGCTGCATGGGGAGAAGCTGGGC
TGGCCGCAGTACAACTGGACGCCGAACTCCGCTCGCTCAGAAGGGCCCCTCCCAGACAGC
GGCCGCGTCAGCTTCCTGGGCCTGGACCTGGATGCGCAGCAGGCCCGCGTGGGCCAGTGG
CTGCTGCTCTTCCTGGGCATCGCCCTGCTGGTAGCCACCCTGGGCCTCAGCCAGCGGCTC
TTCAGCATCCGCCACCGCAGCCTCCACCGGCACTCCCACGGGCCCCAGTTCGGCTCCGAG
GTGGAGCTGAGACACTCCTGA
Enzyme 1 GenBank Gene ID J04144 Link Image
Enzyme 1 GeneCard ID ACE Link Image
Enzyme 1 GenAtlas ID ACE Link Image
Enzyme 1 HGNC ID HGNC:2707 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 17q23.3
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Soubrier F, Alhenc-Gelas F, Hubert C, Allegrini J, John M, Tregear G, Corvol P: Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning. Proc Natl Acad Sci U S A. 1988 Dec;85(24):9386-90. [PubMed Link Image]
  2. Lattion AL, Soubrier F, Allegrini J, Hubert C, Corvol P, Alhenc-Gelas F: The testicular transcript of the angiotensin I-converting enzyme encodes for the ancestral, non-duplicated form of the enzyme. FEBS Lett. 1989 Jul 31;252(1-2):99-104. [PubMed Link Image]
  3. Ehlers MR, Fox EA, Strydom DJ, Riordan JF: Molecular cloning of human testicular angiotensin-converting enzyme: the testis isozyme is identical to the C-terminal half of endothelial angiotensin-converting enzyme. Proc Natl Acad Sci U S A. 1989 Oct;86(20):7741-5. [PubMed Link Image]
  4. Rieder MJ, Taylor SL, Clark AG, Nickerson DA: Sequence variation in the human angiotensin converting enzyme. Nat Genet. 1999 May;22(1):59-62. [PubMed Link Image]
  5. Takeuchi K, Shimizu T, Ohishi N, Seyama Y, Takaku F, Yotsumoto H: Purification of human lung angiotensin-converting enzyme by high-performance liquid chromatography: properties and N-terminal amino acid sequence. J Biochem (Tokyo). 1989 Sep;106(3):442-5. [PubMed Link Image]
  6. Sugimura K, Tian XL, Hoffmann S, Ganten D, Bader M: Alternative splicing of the mRNA coding for the human endothelial angiotensin-converting enzyme: a new mechanism for solubilization. Biochem Biophys Res Commun. 1998 Jun 18;247(2):466-72. [PubMed Link Image]
  7. Ehlers MR, Riordan JF: Angiotensin-converting enzyme: zinc- and inhibitor-binding stoichiometries of the somatic and testis isozymes. Biochemistry. 1991 Jul 23;30(29):7118-26. [PubMed Link Image]
  8. Sturrock ED, Yu XC, Wu Z, Biemann K, Riordan JF: Assignment of free and disulfide-bonded cysteine residues in testis angiotensin-converting enzyme: functional implications. Biochemistry. 1996 Jul 23;35(29):9560-6. [PubMed Link Image]
  9. Yu XC, Sturrock ED, Wu Z, Biemann K, Ehlers MR, Riordan JF: Identification of N-linked glycosylation sites in human testis angiotensin-converting enzyme and expression of an active deglycosylated form. J Biol Chem. 1997 Feb 7;272(6):3511-9. [PubMed Link Image]
  10. Woodman ZL, Oppong SY, Cook S, Hooper NM, Schwager SL, Brandt WF, Ehlers MR, Sturrock ED: Shedding of somatic angiotensin-converting enzyme (ACE) is inefficient compared with testis ACE despite cleavage at identical stalk sites. Biochem J. 2000 May 1;347 Pt 3:711-8. [PubMed Link Image]
  11. Donoghue M, Hsieh F, Baronas E, Godbout K, Gosselin M, Stagliano N, Donovan M, Woolf B, Robison K, Jeyaseelan R, Breitbart RE, Acton S: A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9. Circ Res. 2000 Sep 1;87(5):E1-9. [PubMed Link Image]
  12. Tipnis SR, Hooper NM, Hyde R, Karran E, Christie G, Turner AJ: A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidase. J Biol Chem. 2000 Oct 27;275(43):33238-43. [PubMed Link Image]
  13. Eyries M, Michaud A, Deinum J, Agrapart M, Chomilier J, Kramers C, Soubrier F: Increased shedding of angiotensin-converting enzyme by a mutation identified in the stalk region. J Biol Chem. 2001 Feb 23;276(8):5525-32. Epub 2000 Nov 13. [PubMed Link Image]
  14. Kohlstedt K, Shoghi F, Muller-Esterl W, Busse R, Fleming I: CK2 phosphorylates the angiotensin-converting enzyme and regulates its retention in the endothelial cell plasma membrane. Circ Res. 2002 Oct 18;91(8):749-56. [PubMed Link Image]
  15. Harmer D, Gilbert M, Borman R, Clark KL: Quantitative mRNA expression profiling of ACE 2, a novel homologue of angiotensin converting enzyme. FEBS Lett. 2002 Dec 4;532(1-2):107-10. [PubMed Link Image]
  16. Gordon K, Redelinghuys P, Schwager SL, Ehlers MR, Papageorgiou AC, Natesh R, Acharya KR, Sturrock ED: Deglycosylation, processing and crystallization of human testis angiotensin-converting enzyme. Biochem J. 2003 Apr 15;371(Pt 2):437-42. [PubMed Link Image]
  17. Goulter AB, Goddard MJ, Allen JC, Clark KL: ACE2 gene expression is up-regulated in the human failing heart. BMC Med. 2004 May 19;2:19. [PubMed Link Image]
  18. Burrell LM, Risvanis J, Kubota E, Dean RG, MacDonald PS, Lu S, Tikellis C, Grant SL, Lew RA, Smith AI, Cooper ME, Johnston CI: Myocardial infarction increases ACE2 expression in rat and humans. Eur Heart J. 2005 Feb;26(4):369-75; discussion 322-4. Epub 2005 Jan 25. [PubMed Link Image]
  19. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed Link Image]
  20. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed Link Image]
  21. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  22. Natesh R, Schwager SL, Sturrock ED, Acharya KR: Crystal structure of the human angiotensin-converting enzyme-lisinopril complex. Nature. 2003 Jan 30;421(6922):551-4. Epub 2003 Jan 19. [PubMed Link Image]
  23. Natesh R, Schwager SL, Evans HR, Sturrock ED, Acharya KR: Structural details on the binding of antihypertensive drugs captopril and enalaprilat to human testicular angiotensin I-converting enzyme. Biochemistry. 2004 Jul 13;43(27):8718-24. [PubMed Link Image]
  24. Corradi HR, Schwager SL, Nchinda AT, Sturrock ED, Acharya KR: Crystal structure of the N domain of human somatic angiotensin I-converting enzyme provides a structural basis for domain-specific inhibitor design. J Mol Biol. 2006 Mar 31;357(3):964-74. Epub 2006 Jan 31. [PubMed Link Image]
  25. Vleming LJ, van der Pijl JW, Lemkes HH, Westendorp RG, Maassen JA, Daha MR, van Es LA, van Kooten C: The DD genotype of the ACE gene polymorphism is associated with progression of diabetic nephropathy to end stage renal failure in IDDM. Clin Nephrol. 1999 Mar;51(3):133-40. [PubMed Link Image]
  26. Halushka MK, Fan JB, Bentley K, Hsie L, Shen N, Weder A, Cooper R, Lipshutz R, Chakravarti A: Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis. Nat Genet. 1999 Jul;22(3):239-47. [PubMed Link Image]
  27. Kramers C, Danilov SM, Deinum J, Balyasnikova IV, Scharenborg N, Looman M, Boomsma F, de Keijzer MH, van Duijn C, Martin S, Soubrier F, Adema GJ: Point mutation in the stalk of angiotensin-converting enzyme causes a dramatic increase in serum angiotensin-converting enzyme but no cardiovascular disease. Circulation. 2001 Sep 11;104(11):1236-40. [PubMed Link Image]
  28. Linnebank M, Kesper K, Jeub M, Urbach H, Wullner U, Klockgether T, Schmidt S: Hereditary elevation of angiotensin converting enzyme suggesting neurosarcoidosis. Neurology. 2003 Dec 23;61(12):1819-20. [PubMed Link Image]
  29. Casas JP, Hingorani AD, Bautista LE, Sharma P: Meta-analysis of genetic studies in ischemic stroke: thirty-two genes involving approximately 18,000 cases and 58,000 controls. Arch Neurol. 2004 Nov;61(11):1652-61. [PubMed Link Image]
  30. Slowik A, Turaj W, Dziedzic T, Haefele A, Pera J, Malecki MT, Glodzik-Sobanska L, Szermer P, Figlewicz DA, Szczudlik A: DD genotype of ACE gene is a risk factor for intracerebral hemorrhage. Neurology. 2004 Jul 27;63(2):359-61. [PubMed Link Image]
  31. Gribouval O, Gonzales M, Neuhaus T, Aziza J, Bieth E, Laurent N, Bouton JM, Feuillet F, Makni S, Ben Amar H, Laube G, Delezoide AL, Bouvier R, Dijoud F, Ollagnon-Roman E, Roume J, Joubert M, Antignac C, Gubler MC: Mutations in genes in the renin-angiotensin system are associated with autosomal recessive renal tubular dysgenesis. Nat Genet. 2005 Sep;37(9):964-8. Epub 2005 Aug 14. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 7533
Enzyme 2 Name Coagulation factor XII
Enzyme 2 Synonyms
  1. Hageman factor
  2. HAF
  3. Coagulation factor XIIa heavy chain
  4. Beta-factor XIIa part 1
  5. Beta-factor XIIa part 2
  6. Coagulation factor XIIa light chain
Enzyme 2 Gene Name F12
Enzyme 2 Protein Sequence >Coagulation factor XII
MRALLLLGFLLVSLESTLSIPPWEAPKEHKYKAEEHTVVLTVTGEPCHFPFQYHRQLYHK
CTHKGRPGPQPWCATTPNFDQDQRWGYCLEPKKVKDHCSKHSPCQKGGTCVNMPSGPHCL
CPQHLTGNHCQKEKCFEPQLLRFFHKNEIWYRTEQAAVARCQCKGPDAHCQRLASQACRT
NPCLHGGRCLEVEGHRLCHCPVGYTGPFCDVDTKASCYDGRGLSYRGLARTTLSGAPCQP
WASEATYRNVTAEQARNWGLGGHAFCRNPDNDIRPWCFVLNRDRLSWEYCDLAQCQTPTQ
AAPPTPVSPRLHVPLMPAQPAPPKPQPTTRTPPQSQTPGALPAKREQPPSLTRNGPLSCG
QRLRKSLSSMTRVVGGLVALRGAHPYIAALYWGHSFCAGSLIAPCWVLTAAHCLQDRPAP
EDLTVVLGQERRNHSCEPCQTLAVRSYRLHEAFSPVSYQHDLALLRLQEDADGSCALLSP
YVQPVCLPSGAARPSETTLCQVAGWGHQFEGAEEYASFLQEAQVPFLSLERCSAPDVHGS
SILPGMLCAGFLEGGTDACQGDSGGPLVCEDQAAERRLTLQGIISWGSGCGDRNKPGVYT
DVAYYLAWIREHTVS
Enzyme 2 Number of Residues 615
Enzyme 2 Molecular Weight 67817.6
Enzyme 2 Theoretical pI 7.76
Enzyme 2 GO Classification
Function
  • catalytic activity
  • endopeptidase activity
  • hydrolase activity
  • peptidase activity
  • peptidase activity, acting on L-amino acid peptides
  • serine-type endopeptidase activity
Process
  • macromolecule metabolic process
  • metabolic process
  • protein metabolic process
  • proteolysis
Component
  • extracellular region
  • extracellular region part
  • extracellular space
Enzyme 2 General Function Involved in serine-type endopeptidase activity
Enzyme 2 Specific Function Factor XII is a serum glycoprotein that participates in the initiation of blood coagulation, fibrinolysis, and the generation of bradykinin and angiotensin. Prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa and then trypsin cleaves it to beta- factor XIIa. Alpha-factor XIIa activates factor XI to factor XIa
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions
  • Selective cleavage of Arg!Ile bonds in factor VII to form factor VIIa and factor XI to form factor XIa
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-19
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 22532477 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P00748 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name FA12_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1848 bp
ATGAGGGCTCTGCTGCTCCTGGGGTTCCTGCTGGTGAGCTTGGAGTCAACACTTTCGATT
CCACCTTGGGAAGCCCCCAAGGAGCATAAGTACAAAGCTGAAGAGCACACAGTCGTTCTC
ACTGTCACCGGGGAGCCCTGCCACTTCCCCTTCCAGTACCACCGGCAGCTGTACCACAAA
TGTACCCACAAGGGCCGGCCAGGCCCTCAGCCCTGGTGTGCTACCACCCCCAACTTTGAT
CAGGACCAGCGATGGGGATACTGTTTGGAGCCCAAGAAAGTGAAAGACCACTGCAGCAAA
CACAGCCCCTGCCAGAAAGGAGGGACCTGTGTGAACATGCCAAGCGGCCCCCACTGTCTC
TGTCCACAACACCTCACTGGAAACCACTGCCAGAAAGAGAAGTGCTTTGAGCCTCAGCTT
CTCCGGTTTTTCCACAAGAATGAGATATGGTATAGAACTGAGCAAGCAGCTGTGGCCAGA
TGCCAGTGCAAGGGTCCTGATGCCCACTGCCAGCGGCTGGCCAGCCAGGCCTGCCGCACC
AACCCGTGCCTCCATGGGGGTCGCTGCCTAGAGGTGGAGGGCCACCGCCTGTGCCACTGC
CCGGTGGGCTACACCGGACCCTTCTGCGACGTGGACACCAAGGCAAGCTGCTATGATGGC
CGCGGGCTCAGCTACCGCGGCCTGGCCAGGACCACGCTCTCGGGTGCGCCCTGTCAGCCG
TGGGCCTCGGAGGCCACCTACCGGAACGTGACTGCCGAGCAAGCGCGGAACTGGGGACTG
GGCGGCCACGCCTTCTGCCGGAACCCGGACAACGACATCCGCCCGTGGTGCTTCGTGCTG
AACCGCGACCGGCTGAGCTGGGAGTACTGCGACCTGGCACAGTGCCAGACCCCAACCCAG
GCGGCGCCTCCGACCCCGGTGTCCCCTAGGCTTCATGTCCCACTCATGCCCGCGCAGCCG
GCACCGCCGAAGCCTCAGCCCACGACCCGGACCCCGCCTCAGTCCCAGACCCCGGGAGCC
TTGCCGGCGAAGCGGGAGCAGCCGCCTTCCCTGACCAGGAACGGCCCACTGAGCTGCGGG
CAGCGGCTCCGCAAGAGTCTGTCTTCGATGACCCGCGTCGTTGGCGGGCTGGTGGCGCTA
CGCGGGGCGCACCCCTACATCGCCGCGCTGTACTGGGGCCACAGTTTCTGCGCCGGCAGC
CTCATCGCCCCCTGCTGGGTGCTGACGGCCGCTCACTGCCTGCAGGACCGGCCCGCACCC
GAGGATCTGACGGTGGTGCTCGGCCAGGAACGCCGTAACCACAGCTGTGAGCCGTGCCAG
ACGTTGGCCGTGCGCTCCTACCGCTTGCACGAGGCCTTCTCGCCCGTCAGCTACCAGCAC
GACCTGGCTCTGTTGCGCCTTCAGGAGGATGCGGACGGCAGCTGCGCGCTCCTGTCGCCT
TACGTTCAGCCGGTGTGCCTGCCAAGCGGCGCCGCGCGACCCTCCGAGACCACGCTCTGC
CAGGTGGCCGGCTGGGGCCACCAGTTCGAGGGGGCGGAGGAATATGCCAGCTTCCTGCAG
GAGGCGCAGGTACCGTTCCTCTCCCTGGAGCGCTGCTCAGCCCCGGACGTGCACGGATCC
TCCATCCTCCCCGGCATGCTCTGCGCAGGGTTCCTCGAGGGCGGCACCGATGCGTGCCAG
GGTGATTCCGGAGGCCCGCTGGTGTGTGAGGACCAAGCTGCAGAGCGCCGGCTCACCCTG
CAAGGCATCATCAGCTGGGGATCGGGCTGTGGTGACCGCAACAAGCCAGGCGTCTACACC
GATGTGGCCTACTACCTGGCCTGGATCCGGGAGCACACCGTTTCCTGA
Enzyme 2 GenBank Gene ID AF538691 Link Image
Enzyme 2 GeneCard ID F12 Link Image
Enzyme 2 GenAtlas ID F12 Link Image
Enzyme 2 HGNC ID HGNC:3530 Link Image
Enzyme 2 Chromosome Location 5
Enzyme 2 Locus 5q33-qter
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Cool DE, MacGillivray RT: Characterization of the human blood coagulation factor XII gene. Intron/exon gene organization and analysis of the 5'-flanking region. J Biol Chem. 1987 Oct 5;262(28):13662-73. [PubMed Link Image]
  2. Tripodi M, Citarella F, Guida S, Galeffi P, Fantoni A, Cortese R: cDNA sequence coding for human coagulation factor XII (Hageman). Nucleic Acids Res. 1986 Apr 11;14(7):3146. [PubMed Link Image]
  3. Cool DE, Edgell CJ, Louie GV, Zoller MJ, Brayer GD, MacGillivray RT: Characterization of human blood coagulation factor XII cDNA. Prediction of the primary structure of factor XII and the tertiary structure of beta-factor XIIa. J Biol Chem. 1985 Nov 5;260(25):13666-76. [PubMed Link Image]
  4. Que BG, Davie EW: Characterization of a cDNA coding for human factor XII (Hageman factor). Biochemistry. 1986 Apr 8;25(7):1525-8. [PubMed Link Image]
  5. McMullen BA, Fujikawa K: Amino acid sequence of the heavy chain of human alpha-factor XIIa (activated Hageman factor). J Biol Chem. 1985 May 10;260(9):5328-41. [PubMed Link Image]
  6. Fujikawa K, McMullen BA: Amino acid sequence of human beta-factor XIIa. J Biol Chem. 1983 Sep 25;258(18):10924-33. [PubMed Link Image]
  7. Schloesser M, Hofferbert S, Bartz U, Lutze G, Lammle B, Engel W: The novel acceptor splice site mutation 11396(G-->A) in the factor XII gene causes a truncated transcript in cross-reacting material negative patients. Hum Mol Genet. 1995 Jul;4(7):1235-7. [PubMed Link Image]
  8. Harris RJ, Ling VT, Spellman MW: O-linked fucose is present in the first epidermal growth factor domain of factor XII but not protein C. J Biol Chem. 1992 Mar 15;267(8):5102-7. [PubMed Link Image]
  9. Bunkenborg J, Pilch BJ, Podtelejnikov AV, Wisniewski JR: Screening for N-glycosylated proteins by liquid chromatography mass spectrometry. Proteomics. 2004 Feb;4(2):454-65. [PubMed Link Image]
  10. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed Link Image]
  11. Bernardi F, Marchetti G, Patracchini P, del Senno L, Tripodi M, Fantoni A, Bartolai S, Vannini F, Felloni L, Rossi L, et al.: Factor XII gene alteration in Hageman trait detected by TaqI restriction enzyme. Blood. 1987 May;69(5):1421-4. [PubMed Link Image]
  12. Miyata T, Kawabata S, Iwanaga S, Takahashi I, Alving B, Saito H: Coagulation factor XII (Hageman factor) Washington D.C.: inactive factor XIIa results from Cys-571----Ser substitution. Proc Natl Acad Sci U S A. 1989 Nov;86(21):8319-22. [PubMed Link Image]
  13. Hovinga JK, Schaller J, Stricker H, Wuillemin WA, Furlan M, Lammle B: Coagulation factor XII Locarno: the functional defect is caused by the amino acid substitution Arg 353-->Pro leading to loss of a kallikrein cleavage site. Blood. 1994 Aug 15;84(4):1173-81. [PubMed Link Image]
  14. Schloesser M, Zeerleder S, Lutze G, Halbmayer WM, Hofferbert S, Hinney B, Koestering H, Lammle B, Pindur G, Thies K, Kohler M, Engel W: Mutations in the human factor XII gene. Blood. 1997 Nov 15;90(10):3967-77. [PubMed Link Image]
  15. Kondo S, Tokunaga F, Kawano S, Oono Y, Kumagai S, Koide T: Factor XII Tenri, a novel cross-reacting material negative factor XII deficiency, occurs through a proteasome-mediated degradation. Blood. 1999 Jun 15;93(12):4300-8. [PubMed Link Image]
  16. Kanaji T, Kanaji S, Osaki K, Kuroiwa M, Sakaguchi M, Mihara K, Niho Y, Okamura T: Identification and characterization of two novel mutations (Q421 K and R123P) in congenital factor XII deficiency. Thromb Haemost. 2001 Dec;86(6):1409-15. [PubMed Link Image]
  17. Ishii K, Oguchi S, Moriki T, Yatabe Y, Takeshita E, Murata M, Ikeda Y, Watanabe K: Genetic analyses and expression studies identified a novel mutation (W486C) as a molecular basis of congenital coagulation factor XII deficiency. Blood Coagul Fibrinolysis. 2004 Jul;15(5):367-73. [PubMed Link Image]
  18. Oguchi S, Ishii K, Moriki T, Takeshita E, Murata M, Ikeda Y, Watanabe K: Factor XII Shizuoka, a novel mutation (Ala392Thr) identified and characterized in a patient with congenital coagulation factor XII deficiency. Thromb Res. 2005;115(3):191-7. [PubMed Link Image]
  19. Dewald G, Bork K: Missense mutations in the coagulation factor XII (Hageman factor) gene in hereditary angioedema with normal C1 inhibitor. Biochem Biophys Res Commun. 2006 May 19;343(4):1286-9. [PubMed Link Image]
  20. Cichon S, Martin L, Hennies HC, Muller F, Van Driessche K, Karpushova A, Stevens W, Colombo R, Renne T, Drouet C, Bork K, Nothen MM: Increased activity of coagulation factor XII (Hageman factor) causes hereditary angioedema type III. Am J Hum Genet. 2006 Dec;79(6):1098-104. Epub 2006 Oct 18. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 7542
Enzyme 3 Name Kininogen-1
Enzyme 3 Synonyms
  1. Alpha-2-thiol proteinase inhibitor
  2. Fitzgerald factor
  3. High molecular weight kininogen
  4. HMWK
  5. Williams-Fitzgerald-Flaujeac factor
  6. Kininogen-1 heavy chain
  7. T-kinin
  8. Ile-Ser-Bradykinin
  9. Bradykinin
  10. Kallidin I
  11. Lysyl-bradykinin
  12. Kallidin II
  13. Kininogen-1 light chain
  14. Low molecular weight growth-promoting factor
Enzyme 3 Gene Name KNG1
Enzyme 3 Protein Sequence >Kininogen-1
MKLITILFLCSRLLLSLTQESQSEEIDCNDKDLFKAVDAALKKYNSQNQSNNQFVLYRIT
EATKTVGSDTFYSFKYEIKEGDCPVQSGKTWQDCEYKDAAKAATGECTATVGKRSSTKFS
VATQTCQITPAEGPVVTAQYDCLGCVHPISTQSPDLEPILRHGIQYFNNNTQHSSLFMLN
EVKRAQRQVVAGLNFRITYSIVQTNCSKENFLFLTPDCKSLWNGDTGECTDNAYIDIQLR
IASFSQNCDIYPGKDFVQPPTKICVGCPRDIPTNSPELEETLTHTITKLNAENNATFYFK
IDNVKKARVQVVAGKKYFIDFVARETTCSKESNEELTESCETKKLGQSLDCNAEVYVVPW
EKKIYPTVNCQPLGMISLMKRPPGFSPFRSSRIGEIKEETTVSPPHTSMAPAQDEERDSG
KEQGHTRRHDWGHEKQRKHNLGHGHKHERDQGHGHQRGHGLGHGHEQQHGLGHGHKFKLD
DDLEHQGGHVLDHGHKHKHGHGHGKHKNKGKKNGKHNGWKTEHLASSSEDSTTPSAQTQE
KTEGPTPIPSLAKPGVTVTFSDFQDSDLIATMMPPISPAPIQSDDDWIPDIQIDPNGLSF
NPISDFPDTTSPKCPGRPWKSVSEINPTTQMKESYYFDLTDGLS
Enzyme 3 Number of Residues 644
Enzyme 3 Molecular Weight 71957.0
Enzyme 3 Theoretical pI 6.80
Enzyme 3 GO Classification
Function
  • cysteine-type endopeptidase inhibitor activity
  • endopeptidase inhibitor activity
  • enzyme inhibitor activity
  • enzyme regulator activity
  • peptidase inhibitor activity
Process
Component
Enzyme 3 General Function Involved in cysteine-type endopeptidase inhibitor activity
Enzyme 3 Specific 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
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-18
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 156231037 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P01042 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name KNG1_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1935 bp
ATGAAACTAATTACCATCCTTTTCCTCTGCTCCAGGCTGCTACTAAGTTTAACCCAGGAA
TCACAGTCCGAGGAAATTGACTGCAATGACAAGGATTTATTTAAAGCTGTGGATGCTGCT
CTGAAGAAATATAACAGTCAAAACCAAAGTAACAACCAGTTTGTATTGTACCGCATAACT
GAAGCCACTAAGACGGTTGGCTCTGACACGTTTTATTCCTTCAAGTACGAAATCAAGGAG
GGGGATTGTCCTGTTCAAAGTGGCAAAACCTGGCAGGACTGTGAGTACAAGGATGCTGCA
AAAGCAGCCACTGGAGAATGCACGGCAACCGTGGGGAAGAGGAGCAGTACGAAATTCTCC
GTGGCTACCCAGACCTGCCAGATTACTCCAGCCGAGGGCCCTGTGGTGACAGCCCAGTAC
GACTGCCTCGGCTGTGTGCATCCTATATCAACGCAGAGCCCAGACCTGGAGCCCATTCTG
AGACACGGCATTCAGTACTTTAACAACAACACTCAACATTCCTCCCTCTTCATGCTTAAT
GAAGTAAAACGGGCCCAAAGACAGGTGGTGGCTGGATTGAACTTTCGAATTACCTACTCA
ATTGTGCAAACGAATTGTTCCAAAGAGAATTTTCTGTTCTTAACTCCAGACTGCAAGTCC
CTTTGGAATGGTGATACCGGTGAATGTACAGATAATGCATACATCGATATTCAGCTACGA
ATTGCTTCCTTCTCACAGAACTGTGACATTTATCCAGGGAAGGATTTTGTACAACCACCT
ACCAAGATTTGCGTGGGCTGCCCCAGAGATATACCCACCAACAGCCCAGAGCTGGAGGAG
ACACTGACTCACACCATCACAAAGCTTAATGCAGAGAATAACGCAACTTTCTATTTCAAG
ATTGACAATGTGAAAAAAGCAAGAGTACAGGTGGTGGCTGGCAAGAAATATTTTATTGAC
TTCGTGGCCAGGGAAACCACATGTTCCAAGGAAAGTAATGAAGAGTTGACCGAAAGCTGT
GAGACCAAAAAACTTGGCCAAAGCCTAGATTGCAACGCTGAAGTTTATGTGGTACCCTGG
GAGAAAAAAATTTACCCTACTGTCAACTGTCAACCACTGGGAATGATCTCACTGATGAAA
AGGCCTCCAGGTTTTTCACCTTTCCGATCATCACGAATAGGGGAAATAAAAGAAGAAACA
ACTGTAAGTCCACCCCACACTTCCATGGCACCTGCACAAGATGAAGAGCGGGATTCAGGA
AAAGAACAAGGGCATACTCGTAGACATGACTGGGGCCATGAAAAACAAAGAAAACATAAT
CTTGGCCATGGCCATAAACATGAACGTGACCAAGGGCATGGGCACCAAAGAGGACATGGC
CTTGGCCATGGACACGAACAACAGCATGGTCTTGGTCATGGACATAAGTTCAAACTTGAT
GATGATCTTGAACACCAAGGGGGCCATGTCCTTGACCATGGACATAAGCATAAGCATGGT
CATGGCCACGGAAAACATAAAAATAAAGGCAAAAAGAATGGAAAGCACAATGGTTGGAAA
ACAGAGCATTTGGCAAGCTCTTCTGAAGACAGTACTACACCTTCTGCACAGACACAAGAG
AAGACAGAAGGGCCAACACCCATCCCTTCCCTAGCCAAGCCAGGTGTAACAGTTACCTTT
TCTGACTTTCAGGACTCTGATCTCATTGCAACTATGATGCCTCCTATATCACCAGCTCCC
ATACAGAGTGATGACGATTGGATCCCTGATATCCAGATAGACCCAAATGGCCTTTCATTT
AACCCAATATCAGATTTTCCAGACACGACCTCCCCAAAATGTCCTGGACGCCCCTGGAAG
TCAGTTAGTGAAATTAATCCAACCACACAAATGAAAGAATCTTATTATTTCGATCTCACT
GATGGCCTTTCTTAA
Enzyme 3 GenBank Gene ID NM_001102416.2 Link Image
Enzyme 3 GeneCard ID KNG1 Link Image
Enzyme 3 GenAtlas ID KNG1 Link Image
Enzyme 3 HGNC ID HGNC:6383 Link Image
Enzyme 3 Chromosome Location 3
Enzyme 3 Locus 3q27
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Ohkubo I, Kurachi K, Takasawa T, Shiokawa H, Sasaki M: Isolation of a human cDNA for alpha 2-thiol proteinase inhibitor and its identity with low molecular weight kininogen. Biochemistry. 1984 Nov 20;23(24):5691-7. [PubMed Link Image]
  2. Takagaki Y, Kitamura N, Nakanishi S: Cloning and sequence analysis of cDNAs for human high molecular weight and low molecular weight prekininogens. Primary structures of two human prekininogens. J Biol Chem. 1985 Jul 15;260(14):8601-9. [PubMed Link Image]
  3. 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 TO, 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: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Kellermann J, Lottspeich F, Henschen A, Muller-Esterl W: 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. Eur J Biochem. 1986 Jan 15;154(2):471-8. [PubMed Link Image]
  6. Wunderer G, Walter I, Muller E, Henschen A: Human Ile-Ser-bradykinin, identical with rat T-kinin, is a major permeability factor in ovarian carcinoma ascites. Biol Chem Hoppe Seyler. 1986 Dec;367(12):1231-4. [PubMed Link Image]
  7. Wunderer G, Walter I, Eschenbacher B, Lang M, Kellermann J, Kindermann G: Ile-Ser-bradykinin is an aberrant permeability factor in various human malignant effusions. Biol Chem Hoppe Seyler. 1990 Oct;371(10):977-81. [PubMed Link Image]
  8. Lottspeich F, Kellermann J, Henschen A, Foertsch B, Muller-Esterl W: The amino acid sequence of the light chain of human high-molecular-mass kininogen. Eur J Biochem. 1985 Oct 15;152(2):307-14. [PubMed Link Image]
  9. Kato H, Matsumura Y, Maeda H: Isolation and identification of hydroxyproline analogues of bradykinin in human urine. FEBS Lett. 1988 May 9;232(1):252-4. [PubMed Link Image]
  10. Pierce JV: Structural features of plasma kinins and kininogens. Fed Proc. 1968 Jan-Feb;27(1):52-7. [PubMed Link Image]
  11. Straczek J, Maachi F, Le Nguyen D, Becchi M, Heulin MH, Nabet P, Belleville F: Purification from human plasma of a tetrapeptide that potentiates insulin-like growth factor-I activity in chick embryo cartilage. FEBS Lett. 1995 Oct 16;373(3):207-11. [PubMed Link Image]
  12. Kitamura N, Kitagawa H, Fukushima D, Takagaki Y, Miyata T, Nakanishi S: Structural organization of the human kininogen gene and a model for its evolution. J Biol Chem. 1985 Jul 15;260(14):8610-7. [PubMed Link Image]
  13. Maeda H, Matsumura Y, Kato H: Purification and identification of [hydroxyprolyl3]bradykinin in ascitic fluid from a patient with gastric cancer. J Biol Chem. 1988 Nov 5;263(31):16051-4. [PubMed Link Image]
  14. Zhang H, Li XJ, Martin DB, Aebersold R: Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol. 2003 Jun;21(6):660-6. Epub 2003 May 18. [PubMed Link Image]
  15. Bunkenborg J, Pilch BJ, Podtelejnikov AV, Wisniewski JR: Screening for N-glycosylated proteins by liquid chromatography mass spectrometry. Proteomics. 2004 Feb;4(2):454-65. [PubMed Link Image]
  16. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed Link Image]
  17. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  18. Zhou W, Ross MM, Tessitore A, Ornstein D, Vanmeter A, Liotta LA, Petricoin EF 3rd: An initial characterization of the serum phosphoproteome. J Proteome Res. 2009 Dec;8(12):5523-31. [PubMed Link Image]
  19. Nilsson J, Ruetschi U, Halim A, Hesse C, Carlsohn E, Brinkmalm G, Larson G: Enrichment of glycopeptides for glycan structure and attachment site identification. Nat Methods. 2009 Nov;6(11):809-11. Epub 2009 Oct 18. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 7561
Enzyme 4 Name Plasma kallikrein
Enzyme 4 Synonyms
  1. Fletcher factor
  2. Kininogenin
  3. Plasma prekallikrein
  4. Plasma kallikrein heavy chain
  5. Plasma kallikrein light chain
Enzyme 4 Gene Name KLKB1
Enzyme 4 Protein Sequence >Plasma kallikrein
MILFKQATYFISLFATVSCGCLTQLYENAFFRGGDVASMYTPNAQYCQMRCTFHPRCLLF
SFLPASSINDMEKRFGCFLKDSVTGTLPKVHRTGAVSGHSLKQCGHQISACHRDIYKGVD
MRGVNFNVSKVSSVEECQKRCTNNIRCQFFSYATQTFHKAEYRNNCLLKYSPGGTPTAIK
VLSNVESGFSLKPCALSEIGCHMNIFQHLAFSDVDVARVLTPDAFVCRTICTYHPNCLFF
TFYTNVWKIESQRNVCLLKTSESGTPSSSTPQENTISGYSLLTCKRTLPEPCHSKIYPGV
DFGGEELNVTFVKGVNVCQETCTKMIRCQFFTYSLLPEDCKEEKCKCFLRLSMDGSPTRI
AYGTQGSSGYSLRLCNTGDNSVCTTKTSTRIVGGTNSSWGEWPWQVSLQVKLTAQRHLCG
GSLIGHQWVLTAAHCFDGLPLQDVWRIYSGILNLSDITKDTPFSQIKEIIIHQNYKVSEG
NHDIALIKLQAPLNYTEFQKPICLPSKGDTSTIYTNCWVTGWGFSKEKGEIQNILQKVNI
PLVTNEECQKRYQDYKITQRMVCAGYKEGGKDACKGDSGGPLVCKHNGMWRLVGITSWGE
GCARREQPGVYTKVAEYMDWILEKTQSSDGKAQMQSPA
Enzyme 4 Number of Residues 638
Enzyme 4 Molecular Weight 71369.2
Enzyme 4 Theoretical pI 8.26
Enzyme 4 GO Classification
Function
  • catalytic activity
  • endopeptidase activity
  • hydrolase activity
  • peptidase activity
  • peptidase activity, acting on L-amino acid peptides
  • serine-type endopeptidase activity
Process
  • blood coagulation
  • hemostasis
  • macromolecule metabolic process
  • metabolic process
  • multicellular organismal process
  • protein metabolic process
  • proteolysis
  • regulation of body fluid levels
Component
  • extracellular region
Enzyme 4 General Function Involved in serine-type endopeptidase activity
Enzyme 4 Specific Function The enzyme cleaves Lys-Arg and Arg-Ser bonds. It activates, in a reciprocal reaction, factor XII after its binding to a negatively charged surface. It also releases bradykinin from HMW kininogen and may also play a role in the renin-angiotensin system by converting prorenin into renin
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions
  • Selective cleavage of some Arg! and Lys! bonds, including Lys!Arg and Arg!Ser in (human) kininogen to release bradykinin
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • 1-19
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein Not Available
Enzyme 4 UniProtKB/Swiss-Prot ID P03952 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name KLKB1_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1917 bp
ATGATTTTATTCAAGCAAGCAACTTATTTCATTTCCTTGTTTGCTACAGTTTCCTGTGGA
TGTCTGACTCAACTCTATGAAAACGCCTTCTTCAGAGGTGGGGATGTAGCTTCCATGTAC
ACCCCAAATGCCCAATACTGCCAGATGAGGTGCACATTCCACCCAAGGTGTTTGCTATTC
AGTTTTCTTCCAGCAAGTTCAATCAATGACATGGAGAAAAGGTTTGGTTGCTTCTTGAAA
GATAGTGTTACAGGAACCCTGCCAAAAGTACATCGAACAGGTGCAGTTTCTGGACATTCC
TTGAAGCAATGTGGTCATCAAATAAGTGCTTGCCATCGAGACATTTATAAAGGAGTTGAT
ATGAGAGGAGTCAATTTTAATGTGTCTAAGGTTAGCAGTGTTGAAGAATGCCAAAAAAGG
TGCACCAATAACATTCGCTGCCAGTTTTTTTCATATGCCACGCAAACATTTCACAAGGCA
GAGTACCGGAACAATTGCCTATTAAAGTACAGTCCCGGAGGAACACCTACCGCTATAAAG
GTGCTGAGTAACGTGGAATCTGGATTCTCACTGAAGCCCTGTGCCCTTTCAGAAATTGGT
TGCCACATGAACATCTTCCAGCATCTTGCGTTCTCAGATGTGGATGTTGCCAGGGTTCTC
ACTCCAGATGCTTTTGTGTGTCGGACCATCTGCACCTATCACCCCAACTGCCTCTTCTTT
ACATTCTATACAAATGTATGGAAAATCGAGTCACAAAGAAATGTTTGTCTTCTTAAAACA
TCTGAAAGTGGCACACCAAGTTCCTCTACTCCTCAAGAAAACACCATATCTGGATATAGC
CTTTTAACCTGCAAAAGAACTTTACCTGAACCCTGCCATTCTAAAATTTACCCGGGAGTT
GACTTTGGAGGAGAAGAATTGAATGTGACTTTTGTTAAAGGAGTGAATGTTTGCCAAGAG
ACTTGCACAAAGATGATTCGCTGTCAGTTTTTCACTTATTCTTTACTCCCAGAAGACTGT
AAGGAAGAGAAGTGTAAGTGTTTCTTAAGATTATCTATGGATGGTTCTCCAACTAGGATT
GCGTATGGGACACAAGGGAGCTCTGGTTACTCTTTGAGATTGTGTAACACTGGGGACAAC
TCTGTCTGCACAACAAAAACAAGCACACGCATTGTTGGAGGAACAAACTCTTCTTGGGGA
GAGTGGCCCTGGCAGGTGAGCCTGCAGGTGAAGCTGACAGCTCAGAGGCACCTGTGTGGA
GGGTCACTCATAGGACACCAGTGGGTCCTCACTGCTGCCCACTGCTTTGATGGGCTTCCC
CTGCAGGATGTTTGGCGCATCTATAGTGGCATTTTAAATCTGTCAGACATTACAAAAGAT
ACACCTTTCTCACAAATAAAAGAGATTATTATTCACCAAAACTATAAAGTCTCAGAAGGG
AATCATGATATCGCCTTGATAAAACTCCAGGCTCCTTTGAATTACACTGAATTCCAAAAA
CCAATATGCCTACCTTCCAAAGGTGACACAAGCACAATTTATACCAACTGTTGGGTAACC
GGATGGGGCTTCTCGAAGGAGAAAGGTGAAATCCAAAATATTCTACAAAAGGTAAATATT
CCTTTGGTAACAAATGAAGAATGCCAGAAAAGATATCAAGATTATAAAATAACCCAACGG
ATGGTCTGTGCTGGCTATAAAGAAGGGGGAAAAGATGCTTGTAAGGGAGATTCAGGTGGT
CCCTTAGTTTGCAAACACAACGGAATGTGGCGTTTGGTGGGCATCACAAGCTGGGGTGAA
GGCTGTGCCCGCAGGGAGCAACCTGGTGTCTACACCAAAGTCGCTGAGTACATGGACTGG
ATTTTAGAGAAAACACAGAGCAGTGATGGAAAAGCTCAGATGCAGTCACCAGCATGA
Enzyme 4 GenBank Gene ID M13143 Link Image
Enzyme 4 GeneCard ID KLKB1 Link Image
Enzyme 4 GenAtlas ID KLKB1 Link Image
Enzyme 4 HGNC ID HGNC:6371 Link Image
Enzyme 4 Chromosome Location 4
Enzyme 4 Locus 4q35
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Chung DW, Fujikawa K, McMullen BA, Davie EW: Human plasma prekallikrein, a zymogen to a serine protease that contains four tandem repeats. Biochemistry. 1986 May 6;25(9):2410-7. [PubMed Link Image]
  2. Yu H, Anderson PJ, Freedman BI, Rich SS, Bowden DW: Genomic structure of the human plasma prekallikrein gene, identification of allelic variants, and analysis in end-stage renal disease. Genomics. 2000 Oct 15;69(2):225-34. [PubMed Link Image]
  3. 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 TO, 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: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. McMullen BA, Fujikawa K, Davie EW: Location of the disulfide bonds in human plasma prekallikrein: the presence of four novel apple domains in the amino-terminal portion of the molecule. Biochemistry. 1991 Feb 26;30(8):2050-6. [PubMed Link Image]
  6. Zhang H, Li XJ, Martin DB, Aebersold R: Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol. 2003 Jun;21(6):660-6. Epub 2003 May 18. [PubMed Link Image]
  7. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed Link Image]
  8. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  9. Lombardi AM, Sartori MT, Cabrio L, Fadin M, Zanon E, Girolami A: Severe prekallikrein (Fletcher factor) deficiency due to a compound heterozygosis (383Trp stop codon and Cys529Tyr). Thromb Haemost. 2003 Dec;90(6):1040-5. [PubMed Link Image]
  10. Katsuda I, Maruyama F, Ezaki K, Sawamura T, Ichihara Y: A new type of plasma prekallikrein deficiency associated with homozygosity for Gly104Arg and Asn124Ser in apple domain 2 of the heavy-chain region. Eur J Haematol. 2007 Jul;79(1):59-68. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 7648
Enzyme 5 Name Type-1 angiotensin II receptor
Enzyme 5 Synonyms
  1. AT1AR
  2. AT1BR
  3. Angiotensin II type-1 receptor
  4. AT1
Enzyme 5 Gene Name AGTR1
Enzyme 5 Protein Sequence >Type-1 angiotensin II receptor
MILNSSTEDGIKRIQDDCPKAGRHNYIFVMIPTLYSIIFVVGIFGNSLVVIVIYFYMKLK
TVASVFLLNLALADLCFLLTLPLWAVYTAMEYRWPFGNYLCKIASASVSFNLYASVFLLT
CLSIDRYLAIVHPMKSRLRRTMLVAKVTCIIIWLLAGLASLPAIIHRNVFFIENTNITVC
AFHYESQNSTLPIGLGLTKNILGFLFPFLIILTSYTLIWKALKKAYEIQKNKPRNDDIFK
IIMAIVLFFFFSWIPHQIFTFLDVLIQLGIIRDCRIADIVDTAMPITICIAYFNNCLNPL
FYGFLGKKFKRYFLQLLKYIPPKAKSHSNLSTKMSTLSYRPSDNVSSSTKKPAPCFEVE
Enzyme 5 Number of Residues 359
Enzyme 5 Molecular Weight 41060.5
Enzyme 5 Theoretical pI 9.71
Enzyme 5 GO Classification
Function
  • angiotensin receptor activity
  • angiotensin type II receptor activity
  • molecular transducer activity
  • peptide receptor activity
  • peptide receptor activity, G-protein coupled
  • receptor activity
  • signal transducer activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 5 General Function Involved in G-protein coupled receptor protein signaling pathway
Enzyme 5 Specific Function Receptor for angiotensin II. Mediates its action by association with G proteins that activate a phosphatidylinositol- calcium second messenger system
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • 28-52 65-87 103-124 143-162 193-214 241-262 276-296
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein Not Available
Enzyme 5 UniProtKB/Swiss-Prot ID P30556 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name AGTR1_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1080 bp
ATGATTCTCAACTCTTCTACTGAAGATGGTATTAAAAGAATCCAAGATGATTGTCCCAAA
GCTGGAAGGCATAATTACATATTTGTCATGATTCCTACTTTATACAGTATCATCTTTGTG
GTGGGAATATTTGGAAACAGCTTGGTGGTGATAGTCATTTACTTTTATATGAAGCTGAAG
ACTGTGGCCAGTGTTTTTCTTTTGAATTTAGCACTGGCTGACTTATGCTTTTTACTGACT
TTGCCACTATGGGCTGTCTACACAGCTATGGAATACCGCTGGCCCTTTGGCAATTACCTA
TGTAAGATTGCTTCAGCCAGCGTCAGTTTCAACCTGTACGCTAGTGTGTTTCTACTCACG
TGTCTCAGCATTGATCGATACCTGGCTATTGTTCACCCAATGAAGTCCCGCCTTCGACGC
ACAATGCTTGTAGCCAAAGTCACCTGCATCATCATTTGGCTGCTGGCAGGCTTGGCCAGT
TTGCCAGCTATAATCCATCGAAATGTATTTTTCATTGAGAACACCAATATTACAGTTTGT
GCTTTCCATTATGAGTCCCAAAATTCAACCCTTCCGATAGGGCTGGGCCTGACCAAAAAT
ATACTGGGTTTCCTGTTTCCTTTTCTGATCATTCTTACAAGTTATACTCTTATTTGGAAG
GCCCTAAAGAAGGCTTATGAAATTCAGAAGAACAAACCAAGAAATGATGATATTTTTAAG
ATAATTATGGCAATTGTGCTTTTCTTTTTCTTTTCCTGGATTCCCCACCAAATATTCACT
TTTCTGGATGTATTGATTCAACTAGGCATCATACGTGACTGTAGAATTGCAGATATTGTG
GACACGGCCATGCCTATCACCATTTGTATAGCTTATTTTAACAATTGCCTGAATCCTCTT
TTTTATGGCTTTCTGGGGAAAAAATTTAAAAGATATTTTCTCCAGCTTCTAAAATATATT
CCCCCAAAAGCCAAATCCCACTCAAACCTTTCAACAAAAATGAGCACGCTTTCCTACCGC
CCCTCAGATAATGTAAGCTCATCCACCAAGAAGCCTGCACCATGTTTTGAGGTTGAGTGA
Enzyme 5 GenBank Gene ID M87290 Link Image
Enzyme 5 GeneCard ID AGTR1 Link Image
Enzyme 5 GenAtlas ID AGTR1 Link Image
Enzyme 5 HGNC ID HGNC:336 Link Image
Enzyme 5 Chromosome Location 3
Enzyme 5 Locus 3q24
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Mauzy CA, Hwang O, Egloff AM, Wu LH, Chung FZ: Cloning, expression, and characterization of a gene encoding the human angiotensin II type 1A receptor. Biochem Biophys Res Commun. 1992 Jul 15;186(1):277-84. [PubMed Link Image]
  2. Furuta H, Guo DF, Inagami T: Molecular cloning and sequencing of the gene encoding human angiotensin II type 1 receptor. Biochem Biophys Res Commun. 1992 Feb 28;183(1):8-13. [PubMed Link Image]
  3. Bergsma DJ, Ellis C, Kumar C, Nuthulaganti P, Kersten H, Elshourbagy N, Griffin E, Stadel JM, Aiyar N: Cloning and characterization of a human angiotensin II type 1 receptor. Biochem Biophys Res Commun. 1992 Mar 31;183(3):989-95. [PubMed Link Image]
  4. Takayanagi R, Ohnaka K, Sakai Y, Nakao R, Yanase T, Haji M, Inagami T, Furuta H, Gou DF, Nakamuta M, et al.: Molecular cloning, sequence analysis and expression of a cDNA encoding human type-1 angiotensin II receptor. Biochem Biophys Res Commun. 1992 Mar 16;183(2):910-6. [PubMed Link Image]
  5. Curnow KM, Pascoe L, White PC: Genetic analysis of the human type-1 angiotensin II receptor. Mol Endocrinol. 1992 Jul;6(7):1113-8. [PubMed Link Image]
  6. Konishi H, Kuroda S, Inada Y, Fujisawa Y: Novel subtype of human angiotensin II type 1 receptor: cDNA cloning and expression. Biochem Biophys Res Commun. 1994 Mar 15;199(2):467-74. [PubMed Link Image]
  7. Nawata H, Takayanagi R, Ohnaka K, Sakai Y, Imasaki K, Yanase T, Ikuyama S, Tanaka S, Ohe K: Type 1 angiotensin II receptors of adrenal tumors. Steroids. 1995 Jan;60(1):28-34. [PubMed Link Image]
  8. Kostenis E, Milligan G, Christopoulos A, Sanchez-Ferrer CF, Heringer-Walther S, Sexton PM, Gembardt F, Kellett E, Martini L, Vanderheyden P, Schultheiss HP, Walther T: G-protein-coupled receptor Mas is a physiological antagonist of the angiotensin II type 1 receptor. Circulation. 2005 Apr 12;111(14):1806-13. Epub 2005 Apr 4. [PubMed Link Image]
  9. Gribouval O, Gonzales M, Neuhaus T, Aziza J, Bieth E, Laurent N, Bouton JM, Feuillet F, Makni S, Ben Amar H, Laube G, Delezoide AL, Bouvier R, Dijoud F, Ollagnon-Roman E, Roume J, Joubert M, Antignac C, Gubler MC: Mutations in genes in the renin-angiotensin system are associated with autosomal recessive renal tubular dysgenesis. Nat Genet. 2005 Sep;37(9):964-8. Epub 2005 Aug 14. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 13179
Enzyme 6 Name B2 bradykinin receptor
Enzyme 6 Synonyms
  1. B2R
  2. BK-2 receptor
Enzyme 6 Gene Name BDKRB2
Enzyme 6 Protein Sequence >B2 bradykinin receptor
MFSPWKISMFLSVREDSVPTTASFSADMLNVTLQGPTLNGTFAQSKCPQVEWLGWLNTIQ
PPFLWVLFVLATLENIFVLSVFCLHKSSCTVAEIYLGNLAAADLILACGLPFWAITISNN
FDWLFGETLCRVVNAIISMNLYSSICFLMLVSIDRYLALVKTMSMGRMRGVRWAKLYSLV
IWGCTLLLSSPMLVFRTMKEYSDEGHNVTACVISYPSLIWEVFTNMLLNVVGFLLPLSVI
TFCTMQIMQVLRNNEMQKFKEIQTERRATVLVLVVLLLFIICWLPFQISTFLDTLHRLGI
LSSCQDERIIDVITQIASFMAYSNSCLNPLVYVIVGKRFRKKSWEVYQGVCQKGGCRSEP
IQMENSMGTLRTSISVERQIHKLQDWAGSRQ
Enzyme 6 Number of Residues 391
Enzyme 6 Molecular Weight 44460.2
Enzyme 6 Theoretical pI 8.20
Enzyme 6 GO Classification
Function
  • bradykinin receptor activity
  • molecular transducer activity
  • peptide receptor activity
  • peptide receptor activity, G-protein coupled
  • receptor activity
  • signal transducer activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 6 General Function Involved in G-protein coupled receptor protein signaling pathway
Enzyme 6 Specific Function Receptor for bradykinin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • 61-84 94-118 132-153 176-198 222-248 268-292 312-335
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 14194396 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P30411 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name BKRB2_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1176 bp
ATGTTCTCTCCCTGGAAGATATCAATGTTTCTGTCTGTTCGTGAGGACTCCGTGCCCACC
ACGGCCTCTTTCAGCGCCGACATGCTCAATGTCACCTTGCAAGGGCCCACTCTTAACGGG
ACCTTTGCCCAGAGCAAATGCCCCCAAGTGGAGTGGCTGGGCTGGCTCAACACCATCCAG
CCCCCCTTCCTCTGGGTGCTGTTCGTGCTGGCCACCCTAGAGAACATCTTTGTCCTCAGC
GTCTTCTGCCTGCACAAGAGCAGCTGCACGGTGGCAGAGATCTACCTGGGGAACCTGGCC
GCAGCAGACCTGATCCTGGCCTGCGGGCTGCCCTTCTGGGCCATCACCATCTCCAACAAC
TTCGACTGGCTCTTTGGGGAGACGCTCTGCCGCGTGGTGAATGCCATTATCTCCATGAAC
CTGTACAGCAGCATCTGTTTCCTGATGCTGGTGAGCATCGACCGCTACCTGGCCCTGGTG
AAAACCATGTCCATGGGCCGGATGCGCGGCGTGCGCTGGGCCAAGCTCTACAGCTTGGTG
ATCTGGGGGTGTACGCTGCTCCTGAGCTCACCCATGCTGGTGTTCCGGACCATGAAGGAG
TACAGCGATGAGGGCCACAACGTCACCGCTTGTGTCATCAGCTACCCATCCCTCATCTGG
GAAGTGTTCACCAACATGCTCCTGAATGTCGTGGGCTTCCTGCTGCCCCTGAGTGTCATC
ACCTTCTGCACGATGCAGATCATGCAGGTGCTGCGGAACAACGAGATGCAGAAGTTCAAG
GAGATCCAGACGGAGAGGAGGGCCACGGTGCTAGTCCTGGTTGTGCTGCTGCTATTCATC
ATCTGCTGGCTGCCCTTCCAGATCAGCACCTTCCTGGATACGCTGCATCGCCTCGGCATC
CTCTCCAGCTGCCAGGACGAGCGCATCATCGATGTAATCACACAGATCGCCTCCTTCATG
GCCTACAGCAACAGCTGCCTCAACCCACTGGTGTACGTGATCGTGGGCAAGCGCTTCCGA
AAGAAGTCTTGGGAGGTGTACCAGGGAGTGTGCCAGAAAGGGGGCTGCAGGTCAGAACCC
ATTCAGATGGAGAACTCCATGGGCACACTGCGGACCTCCATCTCCGTGGAACGCCAGATT
CACAAACTGCAGGACTGGGCAGGGAGCAGACAGTGA
Enzyme 6 GenBank Gene ID AF378542 Link Image
Enzyme 6 GeneCard ID BDKRB2 Link Image
Enzyme 6 GenAtlas ID BDKRB2 Link Image
Enzyme 6 HGNC ID HGNC:1030 Link Image
Enzyme 6 Chromosome Location 1
Enzyme 6 Locus 14q32.1-q32.2
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Hess JF, Borkowski JA, Young GS, Strader CD, Ransom RW: Cloning and pharmacological characterization of a human bradykinin (BK-2) receptor. Biochem Biophys Res Commun. 1992 Apr 15;184(1):260-8. [PubMed Link Image]
  2. Powell SJ, Slynn G, Thomas C, Hopkins B, Briggs I, Graham A: Human bradykinin B2 receptor: nucleotide sequence analysis and assignment to chromosome 14. Genomics. 1993 Feb;15(2):435-8. [PubMed Link Image]
  3. McIntyre P, Phillips E, Skidmore E, Brown M, Webb M: Cloned murine bradykinin receptor exhibits a mixed B1 and B2 pharmacological selectivity. Mol Pharmacol. 1993 Aug;44(2):346-55. [PubMed Link Image]
  4. Eggerickx D, Raspe E, Bertrand D, Vassart G, Parmentier M: Molecular cloning, functional expression and pharmacological characterization of a human bradykinin B2 receptor gene. Biochem Biophys Res Commun. 1992 Sep 30;187(3):1306-13. [PubMed Link Image]
  5. Ma JX, Wang DZ, Ward DC, Chen L, Dessai T, Chao J, Chao L: Structure and chromosomal localization of the gene (BDKRB2) encoding human bradykinin B2 receptor. Genomics. 1994 Sep 15;23(2):362-9. [PubMed Link Image]
  6. Braun A, Kammerer S, Bohme E, Muller B, Roscher AA: Identification of polymorphic sites of the human bradykinin B2 receptor gene. Biochem Biophys Res Commun. 1995 Jun 6;211(1):234-40. [PubMed Link Image]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  8. AbdAlla S, Godovac-Zimmermann J, Braun A, Roscher AA, Muller-Esterl W, Quitterer U: Structure of the bradykinin B2 receptors' amino terminus. Biochemistry. 1996 Jun 11;35(23):7514-9. [PubMed Link Image]
  9. Yeh JC, Otte LA, Frangos JA: Regulation of G protein-coupled receptor activities by the platelet-endothelial cell adhesion molecule, PECAM-1. Biochemistry. 2008 Aug 26;47(34):9029-39. Epub 2008 Aug 2. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 13527
Enzyme 7 Name Protein MRVI1
Enzyme 7 Synonyms
  1. Inositol 1,4,5-triphosphate receptor-associated cGMP kinase substrate
  2. JAW1-related protein MRVI1
Enzyme 7 Gene Name MRVI1
Enzyme 7 Protein Sequence >Protein MRVI1
MGMDLTCPFGISPACGAQASWSIFGADAAEVPGTRGHSQQEAAMPHIPEDEEPPGEPQAA
QSPAGQGPPAAGVSCSPTPTIVLTGDATSPEGETDKNLANRVHSPHKRLSHRHLKVSTAS
LTSVDPAGHIIDLVNDQLPDISISEEDKKKNLALLEEAKLVSERFLTRRGRKSRSSPGDS
PSAVSPNLSPSASPTSSRSNSLTVPTPPDGDEADVSSPHPGEPNVPKGLADRKQNDQRKV
SQGRLAPRPPPVEKSKEIAIEQKENFDPLQYPETTPKGLAPVTNSSGKMALNSPQPGPVE
SELGKQLLKTGWEGSPLPRSPTQDAAGVGPPASQGRGPAGEPMGPEAGSKAELPPTVSRP
PLLRGLSWDSGPEEPGPRLQKVLAKLPLAEEEKRFAGKAGGKLAKAPGLKDFQIQVQPVR
MQKLTKLREEHILMRNQNLVGLKLPDLSEAAEQEKGLPSELSPAIEEEESKSGLDVMPNI
SDVLLRKLRVHRSLPGSAPPLTEKEVENVFVQLSLAFRNDSYTLESRINQAERERNLTEE
NTEKELENFKASITSSASLWHHCEHRETYQKLLEDIAVLHRLAARLSSRAEVVGAVRQEK
RMSKATEVMMQYVENLKRTYEKDHAELMEFKKLANQNSSRSCGPSEDGVPRTARSMSLTL
GKNMPRRRVSVAVVPKFNALNLPGQTPSSSSIPSLPALSESPNGKGSLPVTSALPALLEN
GKTNGDPDCEASAPALTLSCLEELSQETKARMEEEAYSKGFQEGLKKTKELQDLKEEEEE
QKSESPEEPEEVEETEEEEKGPRSSKLEELVHFLQVMYPKLCQHWQVIWMMAAVMLVLTV
VLGLYNSYNSCAEQADGPLGRSTCSAAQRDSWWSSGLQHEQPTEQ
Enzyme 7 Number of Residues 885
Enzyme 7 Molecular Weight 96144.2
Enzyme 7 Theoretical pI 5.29
Enzyme 7 GO Classification Not Available
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function Play a role as NO/PRKG1-dependent regulator of IP3- induced calcium release; its phosphorylation by PRKG1 inhibits bradykinin and IP3-induced calcium release from intracellular stores. Recruits PRKG1 to the endoplasmic reticulum and may mediate the assembly of PRKG1 and ITPR1 in a macrocomplex. Involved in PRKG1 signaling cascade leading to inhibition of platelet activation and aggregation. Mediates also NO-dependent inhibition of calcium signaling in gastrointestinal smooth muscle contributing to NO-dependent relaxation
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • 825-845
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 148728182 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q9Y6F6 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name MRVI1_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >2466 bp
CTGACTGGGGATGCCACTTCACCAGAAGGAGAAACCGACAAAAACCTGGCCAACAGAGTT
CACAGTCCCCACAAGAGGCTTTCTCACCGACACTTGAAGGTGTCCACTGCCTCCCTGACA
TCTGTGGACCCCGCGGGGCACATCATTGACCTGGTGAATGACCAGCTGCCAGACATCAGC
ATCTCAGAGGAGGACAAGAAGAAAAACCTGGCGCTGCTGGAAGAAGCCAAGTTGGTGAGT
GAGCGATTCCTGACCCGCCGTGGGAGGAAGTCCAGGAGCAGCCCCGGAGACTCCCCATCA
GCTGTTTCCCCGAACCTCAGCCCCAGCGCTTCTCCTACATCCTCTCGGAGCAACTCACTT
ACAGTCCCCACCCCGCCAGGTTTGGATGTGTGCAGTGGCCCGCCATCCCCTCTGCCTGGA
GCACCACCACAGAAGGGGGATGAGGCCGACGTCTCTTCACCTCACCCTGGCGAGCCTAAC
GTCCCCAAAGGGCTAGCTGACAGGAAGCAGAATGACCAGAGGAAAGTGTCTCAGGGCAGG
CTGGCTCCTCGTCCTCCTCCAGTTGAGAAGTCCAAAGAGATTGCAATAGAACAAAAGGAA
AACTTCGATCCCCTCCAGTACCCCGAGACCACACCCAAAGGCCTAGCTCCTGTTACAAAC
AGCAGTGGGAAAATGGCCCTGAACAGCCCTCAGCCTGGCCCCGTGGAGAGCGAGCTGGGG
AAGCAGCTCTTGAAAACGGGCTGGGAGGGCAGCCCTCTGCCGAGAAGTCCAACCCAGGAT
GCGGCAGGAGTGGGTCCCCCAGCCTCCCAGGGGAGAGGCCCAGCTGGAGAGCCGATGGGG
CCCGAGGCTGGCTCCAAAGCTGAGCTTCCACCCACTGTGTCCCGGCCCCCGCTGCTGCGA
GGGCTCTCCTGGGACAGTGGCCCTGAAGAACCTGGCCCCCGGCTGCAGAAAGTGCTTGCC
AAGCTGCCACTGGCAGAGGAAGAAAAGCGTTTTGCAGGCAAGGCCGGCGGCAAGCTGGCC
AAGGCCCCTGGTCTCAAAGACTTTCAGATACAAGTGCAGCCCGTGCGGATGCAGAAACTG
ACCAAGCTCCGAGAGGAGCACATCCTGATGAGAAATCAGAACTTAGTGGGGCTCAAGCTT
CCAGACCTTAGTGAAGCAGCTGAGCAGGAAAAAGGGCTTCCTTCTGAACTCTCCCCAGCT
ATTGAGGAAGAAGAGTCAAAGAGTGGCTTAGATGTCATGCCTAATATTTCTGATGTGCTG
CTGCGCAAACTGCGGGTCCACAGGAGTCTCCCTGGAAGTGCCCCTCCACTCACTGAAAAG
GAAGTTGAGAACGTGTTTGTGCAACTGTCCTTGGCCTTTAGAAATGACAGCTACACTCTG
GAATCTAGAATTAACCAGGCTGAAAGGGAACGCAACCTGACAGAGGAGAACACTGAGAAA
GAACTGGAAAACTTCAAAGCTTCCATTACGTCCTCAGCTTCACTCTGGCACCACTGTGAG
CACCGGGAAACCTACCAGAAGTTGCTGGAGGACATCGCTGTCCTGCACCGCCTGGCTGCC
CGCCTCTCCAGCCGAGCTGAGGTGGTAGGCGCCGTCCGCCAGGAAAAGCGCATGTCGAAA
GCAACGGAAGTGATGATGCAGTATGTGGAGAATCTAAAGAGGACGTATGAGAAGGACCAT
GCGGAGCTCATGGAGTTTAAAAAGCTTGCAAATCAGAATTCAAGCCGCAGCTGTGGCCCC
TCTGAAGATGGGGTCCCTCGCACGGCACGGTCCATGTCCCTCACGCTGGGAAAGAATATG
CCTCGCCGGAGGGTCAGCGTTGCTGTGGTTCCTAAGTTTAATGCCCTGAATCTGCCTGGC
CAAACTCCCAGCTCATCATCCATTCCCTCCTTACCAGCCTTGTCGGAATCACCCAATGGG
AAAGGCAGCCTACCTGTCACTTCAGCACTGCCTGCACTTTTGGAAAATGGAAAGACAAAT
GGGGACCCAGATTGTGAAGCCTCTGCTCCTGCGCTGACCCTGAGCTGCCTGGAGGAGCTT
AGTCAGGAGACCAAGGCCAGGATGGAGGAAGAAGCCTACAGCAAGGGATTCCAAGAAGGT
CTAAAGAAGACCAAAGAACTTCAAGACCTGAAGGAGGAGGAGGAAGAACAGAAGAGTGAG
AGTCCTGAGGAACCTGAAGAGGTAGAAGAAACTGAGGAAGAGGAAAAGGGCCCAAGAAGC
AGCAAACTTGAAGAATTGGTCCATTTCTTACAAGTCATGTATCCCAAACTGTGTCAGCAC
TGGCAAGTGATCTGGATGATGGCTGCAGTGATGCTGGTCTTGACTGTTGTGCTGGGGCTC
TACAATTCCTATAACTCTTGTGCAGAGCAGGCTGATGGGCCCCTTGGAAGATCCACTTGC
TCGGCAGCCCAGAGGGACTCCTGGTGGAGCTCAGGACTCCAGCATGAGCAGCCTACAGAG
CAGTAG
Enzyme 7 GenBank Gene ID Not Available
Enzyme 7 GeneCard ID MRVI1 Link Image
Enzyme 7 GenAtlas ID MRVI1 Link Image
Enzyme 7 HGNC ID HGNC:7237 Link Image
Enzyme 7 Chromosome Location 1
Enzyme 7 Locus 11p15
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Shaughnessy JD Jr, Largaespada DA, Tian E, Fletcher CF, Cho BC, Vyas P, Jenkins NA, Copeland NG: Mrvi1, a common MRV integration site in BXH2 myeloid leukemias, encodes a protein with homology to a lymphoid-restricted membrane protein Jaw1. Oncogene. 1999 Mar 25;18(12):2069-84. [PubMed Link Image]
  2. Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [PubMed Link Image]
  3. 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 TO, 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: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Fritsch RM, Saur D, Kurjak M, Oesterle D, Schlossmann J, Geiselhoringer A, Hofmann F, Allescher HD: InsP3R-associated cGMP kinase substrate (IRAG) is essential for nitric oxide-induced inhibition of calcium signaling in human colonic smooth muscle. J Biol Chem. 2004 Mar 26;279(13):12551-9. Epub 2004 Jan 18. [PubMed Link Image]
  5. Antl M, von Bruhl ML, Eiglsperger C, Werner M, Konrad I, Kocher T, Wilm M, Hofmann F, Massberg S, Schlossmann J: IRAG mediates NO/cGMP-dependent inhibition of platelet aggregation and thrombus formation. Blood. 2007 Jan 15;109(2):552-9. Epub 2006 Sep 21. [PubMed Link Image]
  6. Kusumawidjaja G, Kayed H, Giese N, Bauer A, Erkan M, Giese T, Hoheise JD, Friess H, Kleeff J: Basic transcription factor 3 (BTF3) regulates transcription of tumor-associated genes in pancreatic cancer cells. Cancer Biol Ther. 2007 Mar;6(3):367-76. Epub 2007 Mar 13. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 13879
Enzyme 8 Name Relaxin-3 receptor 2
Enzyme 8 Synonyms
  1. RLN3 receptor 2
  2. G-protein coupled receptor 100
  3. G-protein coupled receptor GPCR142
  4. Insulin-like peptide INSL5 receptor
  5. Relaxin family peptide receptor 4
Enzyme 8 Gene Name RXFP4
Enzyme 8 Protein Sequence >Relaxin-3 receptor 2
MPTLNTSASPPTFFWANASGGSVLSADDAPMPVKFLALRLMVALAYGLVGAIGLLGNLAV
LWVLSNCARRAPGPPSDTFVFNLALADLGLALTLPFWAAESALDFHWPFGGALCKMVLTA
TVLNVYASIFLITALSVARYWVVAMAAGPGTHLSLFWARIATLAVWAAAALVTVPTAVFG
VEGEVCGVRLCLLRFPSRYWLGAYQLQRVVLAFMVPLGVITTSYLLLLAFLQRRQRRRQD
SRVVARSVRILVASFFLCWFPNHVVTLWGVLVKFDLVPWNSTFYTIQTYVFPVTTCLAHS
NSCLNPVLYCLLRREPRQALAGTFRDLRLRLWPQGGGWVQQVALKQVGRRWVASNPRESR
PSTLLTNLDRGTPG
Enzyme 8 Number of Residues 374
Enzyme 8 Molecular Weight 41141.0
Enzyme 8 Theoretical pI 10.65
Enzyme 8 GO Classification
Function
  • angiotensin receptor activity
  • angiotensin type II receptor activity
  • molecular transducer activity
  • peptide receptor activity
  • peptide receptor activity, G-protein coupled
  • receptor activity
  • signal transducer activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 8 General Function Involved in G-protein coupled receptor protein signaling pathway
Enzyme 8 Specific Function High affinity receptor for INSL5. Also acts as receptor for RLN3/relaxin-3, as well as bradykinin and kallidin. Binding of the ligand inhibit cAMP accumulation
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • 44-64 79-99 117-137 155-175 210-230 250-270 282-302
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 20152250 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q8TDU9 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name RL3R2_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1125 bp
ATGCCCACACTCAATACTTCTGCCTCTCCACCCACATTCTTCTGGGCCAATGCCTCCGGA
GGCAGTGTGCTGAGTGCTGATGATGCTCCGATGCCTGTCAAATTCCTAGCCCTGAGGCTC
ATGGTTGCCCTGGCCTATGGGCTTGTGGGGGCCATTGGCTTGCTGGGAAATTTGGCGGTG
CTGTGGGTACTGAGTAACTGTGCCCGGAGAGCCCCTGGCCCACCTTCAGACACCTTCGTC
TTCAACCTGGCTCTGGCGGACCTGGGACTGGCACTCACTCTCCCCTTTTGGGCAGCCGAG
TCGGCACTGGACTTTCACTGGCCCTTCGGAGGTGCCCTCTGCAAGATGGTTCTGACGGCC
ACTGTCCTCAACGTCTATGCCAGCATCTTCCTCATCACAGCGCTGAGCGTTGCTCGCTAC
TGGGTGGTGGCCATGGCTGCGGGGCCAGGCACCCACCTCTCACTCTTCTGGGCCCGAATA
GCCACCCTGGCAGTGTGGGCGGCGGCTGCCCTGGTGACGGTGCCCACAGCTGTCTTCGGG
GTGGAGGGTGAGGTGTGTGGTGTGCGCCTTTGCCTGCTGCGTTTCCCCAGCAGGTACTGG
CTGGGGGCCTACCAGCTGCAGAGGGTGGTGCTGGCTTTCATGGTGCCCTTGGGCGTCATC
ACCACCAGCTACCTGCTGCTGCTGGCCTTCCTGCAGCGGCGGCAACGGCGGCGGCAGGAC
AGCAGGGTCGTGGCCCGCTCTGTCCGCATCCTGGTGGCTTCCTTCTTCCTCTGCTGGTTT
CCCAACCATGTGGTCACTCTCTGGGGTGTCCTGGTGAAGTTTGACCTGGTGCCCTGGAAC
AGTACTTTCTATACTATCCAGACGTATGTCTTCCCTGTCACTACTTGCTTGGCACACAGC
AATAGCTGCCTCAACCCTGTGCTGTACTGTCTCCTGAGGCGGGAGCCCCGGCAGGCTCTG
GCAGGCACCTTCAGGGATCTGCGGTTGAGGCTGTGGCCCCAGGGCGGAGGCTGGGTGCAA
CAGGTGGCCCTAAAGCAGGTAGGCAGGCGGTGGGTCGCAAGCAACCCCCGGGAGAGCCGC
CCTTCTACCCTGCTCACCAACCTGGACAGAGGGACACCCGGGTGA
Enzyme 8 GenBank Gene ID AB083593 Link Image
Enzyme 8 GeneCard ID RXFP4 Link Image
Enzyme 8 GenAtlas ID RXFP4 Link Image
Enzyme 8 HGNC ID HGNC:14666 Link Image
Enzyme 8 Chromosome Location 1
Enzyme 8 Locus 1q22
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Liu C, Chen J, Sutton S, Roland B, Kuei C, Farmer N, Sillard R, Lovenberg TW: Identification of relaxin-3/INSL7 as a ligand for GPCR142. J Biol Chem. 2003 Dec 12;278(50):50765-70. Epub 2003 Sep 30. [PubMed Link Image]
  2. Fredriksson R, Hoglund PJ, Gloriam DE, Lagerstrom MC, Schioth HB: Seven evolutionarily conserved human rhodopsin G protein-coupled receptors lacking close relatives. FEBS Lett. 2003 Nov 20;554(3):381-8. [PubMed Link Image]
  3. Boels K, Schaller HC: Identification and characterisation of GPR100 as a novel human G-protein-coupled bradykinin receptor. Br J Pharmacol. 2003 Nov;140(5):932-8. Epub 2003 Oct 6. [PubMed Link Image]
  4. Takeda S, Kadowaki S, Haga T, Takaesu H, Mitaku S: Identification of G protein-coupled receptor genes from the human genome sequence. FEBS Lett. 2002 Jun 5;520(1-3):97-101. [PubMed Link Image]
  5. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Liu C, Kuei C, Sutton S, Chen J, Bonaventure P, Wu J, Nepomuceno D, Kamme F, Tran DT, Zhu J, Wilkinson T, Bathgate R, Eriste E, Sillard R, Lovenberg TW: INSL5 is a high affinity specific agonist for GPCR142 (GPR100). J Biol Chem. 2005 Jan 7;280(1):292-300. Epub 2004 Nov 2. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 15002
Enzyme 9 Name Endoplasmic reticulum aminopeptidase 1
Enzyme 9 Synonyms
  1. ARTS-1
  2. Adipocyte-derived leucine aminopeptidase
  3. A-LAP
  4. Aminopeptidase PILS
  5. Puromycin-insensitive leucyl-specific aminopeptidase
  6. PILS-AP
  7. Type 1 tumor necrosis factor receptor shedding aminopeptidase regulator
Enzyme 9 Gene Name ERAP1
Enzyme 9 Protein Sequence >Endoplasmic reticulum aminopeptidase 1
MVFLPLKWSLATMSFLLSSLLALLTVSTPSWCQSTEASPKRSDGTPFPWNKIRLPEYVIP
VHYDLLIHANLTTLTFWGTTKVEITASQPTSTIILHSHHLQISRATLRKGAGERLSEEPL
QVLEHPRQEQIALLAPEPLLVGLPYTVVIHYAGNLSETFHGFYKSTYRTKEGELRILAST
QFEPTAARMAFPCFDEPAFKASFSIKIRREPRHLAISNMPLVKSVTVAEGLIEDHFDVTV
KMSTYLVAFIISDFESVSKITKSGVKVSVYAVPDKINQADYALDAAVTLLEFYEDYFSIP
YPLPKQDLAAIPDFQSGAMENWGLTTYRESALLFDAEKSSASSKLGITMTVAHELAHQWF
GNLVTMEWWNDLWLNEGFAKFMEFVSVSVTHPELKVGDYFFGKCFDAMEVDALNSSHPVS
TPVENPAQIREMFDDVSYDKGACILNMLREYLSADAFKSGIVQYLQKHSYKNTKNEDLWD
SMASICPTDGVKGMDGFCSRSQHSSSSSHWHQEGVDVKTMMNTWTLQKGFPLITITVRGR
NVHMKQEHYMKGSDGAPDTGYLWHVPLTFITSKSDMVHRFLLKTKTDVLILPEEVEWIKF
NVGMNGYYIVHYEDDGWDSLTGLLKGTHTAVSSNDRASLINNAFQLVSIGKLSIEKALDL
SLYLKHETEIMPVFQGLNELIPMYKLMEKRDMNEVETQFKAFLIRLLRDLIDKQTWTDEG
SVSERMLRSQLLLLACVHNYQPCVQRAEGYFRKWKESNGNLSLPVDVTLAVFAVGAQSTE
GWDFLYSKYQFSLSSTEKSQIEFALCRTQNKEKLQWLLDESFKGDKIKTQEFPQILTLIG
RNPVGYPLAWQFLRKNWNKLVQKFELGSSSIAHMVMGTTNQFSTRTRLEEVKGFFSSLKE
NGSQLRCVQQTIETIEENIGWMDKNFDKIRVWLQSEKLERM
Enzyme 9 Number of Residues 941
Enzyme 9 Molecular Weight 107233.9
Enzyme 9 Theoretical pI 6.43
Enzyme 9 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • ion binding
  • metal ion binding
  • metallopeptidase activity
  • peptidase activity
  • peptidase activity, acting on L-amino acid peptides
  • transition metal ion binding
  • zinc ion binding
Process
  • macromolecule metabolic process
  • metabolic process
  • protein metabolic process
  • proteolysis
Component
Enzyme 9 General Function Involved in proteolysis
Enzyme 9 Specific Function Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I- binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • 2-21
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 94818891 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q9NZ08 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name ERAP1_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >2826 bp
ATGGTGTTTCTGCCCCTCAAATGGTCCCTTGCAACCATGTCATTTCTACTTTCCTCACTG
TTGGCTCTCTTAACTGTGTCCACTCCTTCATGGTGTCAGAGCACTGAAGCATCTCCAAAA
CGTAGTGATGGGACACCATTTCCTTGGAATAAAATACGACTTCCTGAGTACGTCATCCCA
GTTCATTATGATCTCTTGATCCATGCAAACCTTACCACGCTGACCTTCTGGGGAACCACG
AAAGTAGAAATCACAGCCAGTCAGCCCACCAGCACCATCATCCTGCATAGTCACCACCTG
CAGATATCTAGGGCCACCCTCAGGAAGGGAGCTGGAGAGAGGCTATCGGAAGAACCCCTG
CAGGTCCTGGAACACCCCCGTCAGGAGCAAATTGCACTGCTGGCTCCCGAGCCCCTCCTT
GTCGGGCTCCCGTACACAGTTGTCATTCACTATGCTGGCAATCTTTCGGAGACTTTCCAC
GGATTTTACAAAAGCACCTACAGAACCAAGGAAGGGGAACTGAGGATACTAGCATCAACA
CAATTTGAACCCACTGCAGCTAGAATGGCCTTTCCCTGCTTTGATGAACCTGCCTTCAAA
GCAAGTTTCTCAATCAAAATTAGAAGAGAGCCAAGGCACCTAGCCATCTCCAATATGCCA
TTGGTGAAATCTGTGACTGTTGCTGAAGGACTCATAGAAGACCATTTTGATGTCACTGTG
AAGATGAGCACCTATCTGGTGGCCTTCATCATTTCAGATTTTGAGTCTGTCAGCAAGATA
ACCAAGAGTGGAGTCAAGGTTTCTGTTTATGCTGTGCCAGACAAGATAAATCAAGCAGAT
TATGCACTGGATGCTGCGGTGACTCTTCTAGAATTTTATGAGGATTATTTCAGCATACCG
TATCCCCTACCCAAACAAGATCTTGCTGCTATTCCCGACTTTCAGTCTGGTGCTATGGAA
AACTGGGGACTGACAACATATAGAGAATCTGCTCTGTTGTTTGATGCAGAAAAGTCTTCT
GCATCAAGTAAGCTTGGCATCACAATGACTGTGGCCCATGAACTGGCTCACCAGTGGTTT
GGGAACCTGGTCACTATGGAATGGTGGAATGATCTTTGGCTAAATGAAGGATTTGCCAAA
TTTATGGAGTTTGTGTCTGTCAGTGTGACCCATCCTGAACTGAAAGTTGGAGATTATTTC
TTTGGCAAATGTTTTGACGCAATGGAGGTAGATGCTTTAAATTCCTCACACCCTGTGTCT
ACACCTGTGGAAAATCCTGCTCAGATCCGGGAGATGTTTGATGATGTTTCTTATGATAAG
GGAGCTTGTATTCTGAATATGCTAAGGGAGTATCTTAGTGCTGACGCATTTAAAAGTGGT
ATTGTACAGTATCTCCAGAAGCATAGCTATAAAAATACAAAAAACGAGGACCTGTGGGAT
AGTATGGCAAGTATTTGCCCTACAGATGGTGTAAAAGGGATGGATGGCTTTTGCTCTAGA
AGTCAACATTCATCTTCATCCTCACATTGGCATCAGGAAGGGGTGGATGTGAAAACCATG
ATGAACACTTGGACACTGCAGAAGGGTTTTCCCCTAATAACCATCACAGTGAGGGGGAGG
AATGTACACATGAAGCAAGAGCACTACATGAAGGGCTCTGACGGCGCCCCGGACACTGGG
TACCTGTGGCATGTTCCATTGACATTCATCACCAGCAAATCCGACATGGTCCATCGATTT
TTGCTAAAAACAAAAACAGATGTGCTCATCCTCCCAGAAGAGGTGGAATGGATCAAATTT
AATGTGGGCATGAATGGCTATTACATTGTGCATTACGAGGATGATGGATGGGACTCTTTG
ACTGGCCTTTTAAAAGGAACACACACAGCAGTCAGCAGTAATGATCGGGCGAGTCTCATT
AACAATGCATTTCAGCTCGTCAGCATTGGGAAGCTGTCCATTGAAAAGGCCTTGGATTTA
TCCCTGTACTTGAAACATGAAACTGAAATTATGCCCGTGTTTCAAGGTTTGAATGAGCTG
ATTCCTATGTATAAGTTAATGGAGAAAAGAGATATGAATGAAGTGGAAACTCAATTCAAG
GCCTTCCTCATCAGGCTGCTAAGGGACCTCATTGATAAGCAGACATGGACAGACGAGGGC
TCAGTCTCAGAGCGAATGCTGCGGAGTCAACTACTACTCCTCGCCTGTGTGCACAACTAT
CAGCCGTGCGTACAGAGGGCAGAAGGCTATTTCAGAAAGTGGAAGGAATCCAATGGAAAC
TTGAGCCTGCCTGTCGACGTGACCTTGGCAGTGTTTGCTGTGGGGGCCCAGAGCACAGAA
GGCTGGGATTTTCTTTATAGTAAATATCAGTTTTCTTTGTCCAGTACTGAGAAAAGCCAA
ATTGAATTTGCCCTCTGCAGAACCCAAAATAAGGAAAAGCTTCAATGGCTACTAGATGAA
AGCTTTAAGGGAGATAAAATAAAAACTCAGGAGTTTCCACAAATTCTTACACTCATTGGC
AGGAACCCAGTAGGATACCCACTGGCCTGGCAATTTCTGAGGAAAAACTGGAACAAACTT
GTACAAAAGTTTGAACTTGGCTCATCTTCCATAGCCCACATGGTAATGGGTACAACAAAT
CAATTCTCCACAAGAACACGGCTTGAAGAGGTAAAAGGATTCTTCAGCTCTTTGAAAGAA
AATGGTTCTCAGCTCCGTTGTGTCCAACAGACAATTGAAACCATTGAAGAAAACATCGGT
TGGATGGATAAGAATTTTGATAAAATCAGAGTGTGGCTGCAAAGTGAAAAGCTTGAACGT
ATGTAA
Enzyme 9 GenBank Gene ID NM_001040458.1 Link Image
Enzyme 9 GeneCard ID ERAP1 Link Image
Enzyme 9 GenAtlas ID ERAP1 Link Image
Enzyme 9 HGNC ID HGNC:18173 Link Image
Enzyme 9 Chromosome Location 5
Enzyme 9 Locus 5q15
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Hattori A, Matsumoto H, Mizutani S, Tsujimoto M: Molecular cloning of adipocyte-derived leucine aminopeptidase highly related to placental leucine aminopeptidase/oxytocinase. J Biochem. 1999 May;125(5):931-8. [PubMed Link Image]
  2. Hattori A, Matsumoto K, Mizutani S, Tsujimoto M: Genomic organization of the human adipocyte-derived leucine aminopeptidase gene and its relationship to the placental leucine aminopeptidase/oxytocinase gene. J Biochem. 2001 Aug;130(2):235-41. [PubMed Link Image]
  3. Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [PubMed Link Image]
  4. Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed Link Image]
  5. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Hattori A, Kitatani K, Matsumoto H, Miyazawa S, Rogi T, Tsuruoka N, Mizutani S, Natori Y, Tsujimoto M: Characterization of recombinant human adipocyte-derived leucine aminopeptidase expressed in Chinese hamster ovary cells. J Biochem. 2000 Nov;128(5):755-62. [PubMed Link Image]
  8. Saveanu L, Carroll O, Lindo V, Del Val M, Lopez D, Lepelletier Y, Greer F, Schomburg L, Fruci D, Niedermann G, van Endert PM: Concerted peptide trimming by human ERAP1 and ERAP2 aminopeptidase complexes in the endoplasmic reticulum. Nat Immunol. 2005 Jul;6(7):689-97. Epub 2005 May 22. [PubMed Link Image]
  9. Chang SC, Momburg F, Bhutani N, Goldberg AL: The ER aminopeptidase, ERAP1, trims precursors to lengths of MHC class I peptides by a "molecular ruler" mechanism. Proc Natl Acad Sci U S A. 2005 Nov 22;102(47):17107-12. Epub 2005 Nov 14. [PubMed Link Image]
  10. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 15003
Enzyme 10 Name Neurolysin, mitochondrial
Enzyme 10 Synonyms
  1. Angiotensin-binding protein
  2. Microsomal endopeptidase
  3. MEP
  4. Mitochondrial oligopeptidase M
  5. Neurotensin endopeptidase
Enzyme 10 Gene Name NLN
Enzyme 10 Protein Sequence >Neurolysin, mitochondrial
MIARCLLAVRSLRRVGGSRILLRMTLGREVMSPLQAMSSYTVAGRNVLRWDLSPEQIKTR
TEELIVQTKQVYDAVGMLGIEEVTYENCLQALADVEVKYIVERTMLDFPQHVSSDKEVRA
ASTEADKRLSRFDIEMSMRGDIFERIVHLQETCDLGKIKPEARRYLEKSIKMGKRNGLHL
PEQVQNEIKSMKKRMSELCIDFNKNLNEDDTFLVFSKAELGALPDDFIDSLEKTDDDKYK
ITLKYPHYFPVMKKCCIPETRRRMEMAFNTRCKEENTIILQQLLPLRTKVAKLLGYSTHA
DFVLEMNTAKSTSRVTAFLDDLSQKLKPLGEAEREFILNLKKKECKDRGFEYDGKINAWD
LYYYMTQTEELKYSIDQEFLKEYFPIEVVTEGLLNTYQELLGLSFEQMTDAHVWNKSVTL
YTVKDKATGEVLGQFYLDLYPREGKYNHAACFGLQPGCLLPDGSRMMAVAALVVNFSQPV
AGRPSLLRHDEVRTYFHEFGHVMHQICAQTDFARFSGTNVETDFVEVPSQMLENWVWDVD
SLRRLSKHYKDGSPIADDLLEKLVASRLVNTGLLTLRQIVLSKVDQSLHTNTSLDAASEY
AKYCSEILGVAATPGTNMPATFGHLAGGYDGQYYGYLWSEVFSMDMFYSCFKKEGIMNPE
VGMKYRNLILKPGGSLDGMDMLHNFLKREPNQKAFLMSRGLHAP
Enzyme 10 Number of Residues 704
Enzyme 10 Molecular Weight 80651.1
Enzyme 10 Theoretical pI 6.62
Enzyme 10 GO Classification
Function
  • catalytic activity
  • endopeptidase activity
  • hydrolase activity
  • metalloendopeptidase activity
  • peptidase activity
  • peptidase activity, acting on L-amino acid peptides
Process
  • macromolecule metabolic process
  • metabolic process
  • protein metabolic process
  • proteolysis
Component
Enzyme 10 General Function Involved in metalloendopeptidase activity
Enzyme 10 Specific Function Hydrolyzes oligopeptides such as neurotensin, bradykinin and dynorphin A
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions
  • Preferential cleavage in neurotensin: Pro10!Tyr COFACTOR Zinc [CPD:C00038]
  • Metal [CPD:C00050]
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 20521802 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q9BYT8 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name NEUL_HUMAN Link Image
Enzyme 10 PDB ID 1I1I Link Image
Enzyme 10 PDB File Show
Enzyme 10 3D Structure
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >2115 bp
ATGATCGCCCGGTGCCTTTTGGCTGTGCGAAGCCTCCGCAGAGTTGGTGGTTCCAGGATT
TTACTCAGAATGACGTTAGGAAGAGAAGTGATGTCTCCTCTTCAGGCAATGTCTTCCTAT
ACTGTGGCTGGCAGAAATGTTTTAAGATGGGATCTTTCACCAGAGCAAATTAAAACAAGA
ACTGAGGAGCTCATTGTGCAGACCAAACAGGTGTACGATGCTGTTGGAATGCTCGGTATT
GAGGAAGTAACTTACGAGAACTGTCTGCAGGCACTGGCAGATGTAGAAGTAAAGTATATA
GTGGAAAGGACCATGCTAGACTTTCCCCAGCATGTATCCTCTGACAAAGAAGTACGAGCA
GCAAGTACAGAAGCAGACAAAAGACTTTCTCGTTTTGATATTGAGATGAGCATGAGAGGA
GATATATTTGAGAGAATTGTTCATTTACAGGAAACCTGTGATCTGGGGAAGATAAAACCT
GAGGCCAGACGATACTTGGAAAAGTCAATTAAAATGGGGAAAAGAAATGGGCTCCATCTT
CCTGAACAAGTACAGAATGAAATCAAATCAATGAAGAAAAGAATGAGTGAGCTATGTATT
GATTTTAACAAAAACCTCAATGAGGATGATACCTTCCTTGTATTTTCCAAGGCTGAACTT
GGTGCTCTTCCTGATGATTTCATTGACAGTTTAGAAAAGACAGATGATGACAAGTATAAA
ATTACCTTAAAATATCCACACTATTTCCCTGTCATGAAGAAATGTTGTATCCCTGAAACC
AGAAGAAGGATGGAAATGGCTTTTAATACAAGGTGCAAAGAGGAAAACACCATAATTTTG
CAGCAGCTACTCCCACTGCGAACCAAGGTGGCCAAACTACTCGGTTATAGCACACATGCT
GACTTCGTCCTTGAAATGAACACTGCAAAGAGCACAAGCCGCGTAACAGCCTTTCTAGAT
GATTTAAGCCAGAAGTTAAAACCCTTGGGTGAAGCAGAACGAGAGTTTATTTTGAATTTG
AAGAAAAAGGAATGCAAAGACAGGGGTTTTGAATATGATGGGAAAATCAATGCCTGGGAT
CTATATTACTACATGACTCAGACAGAGGAACTCAAGTATTCCATAGACCAAGAGTTCCTC
AAGGAATACTTCCCAATTGAGGTGGTCACTGAAGGCTTGCTGAACACCTACCAGGAGTTG
TTGGGACTTTCATTTGAACAAATGACAGATGCTCATGTTTGGAACAAGAGTGTTACACTT
TATACTGTGAAGGATAAAGCTACAGGAGAAGTATTGGGACAGTTCTATTTGGACCTCTAT
CCAAGGGAAGGAAAATACAATCATGCGGCCTGCTTCGGTCTCCAGCCTGGCTGCCTTCTG
CCTGATGGAAGCCGGATGATGGCAGTGGCTGCCCTCGTGGTGAACTTCTCACAGCCAGTG
GCAGGTCGTCCCTCTCTCCTGAGACACGACGAGGTGAGGACTTACTTTCATGAGTTTGGT
CACGTGATGCATCAGATTTGTGCACAGACTGATTTTGCACGATTTAGCGGAACAAATGTG
GAAACTGACTTTGTAGAGGTGCCATCGCAAATGCTTGAAAATTGGGTGTGGGACGTCGAT
TCCCTCCGAAGATTGTCAAAACATTATAAAGATGGAAGCCCTATTGCAGACGATCTGCTT
GAAAAACTTGTTGCTTCTAGGCTGGTCAACACAGGTCTTCTGACCCTGCGCCAGATTGTT
TTGAGCAAAGTTGATCAGTCTCTTCATACCAACACATCGCTGGATGCTGCAAGTGAATAT
GCCAAATACTGCTCAGAAATATTAGGAGTTGCAGCTACTCCAGGCACAAATATGCCAGCT
ACCTTTGGACATTTGGCAGGGGGATACGATGGCCAATATTATGGATATCTTTGGAGTGAA
GTATTTTCCATGGATATGTTTTACAGCTGTTTTAAAAAAGAAGGGATAATGAATCCAGAG
GTTGGAATGAAATACAGAAACCTAATCCTGAAACCTGGGGGATCTCTGGACGGCATGGAC
ATGCTCCACAATTTCTTGAAACGTGAGCCAAACCAAAAAGCGTTCCTAATGAGTAGAGGC
CTGCATGCTCCGTGA
Enzyme 10 GenBank Gene ID AB033052 Link Image
Enzyme 10 GeneCard ID NLN Link Image
Enzyme 10 GenAtlas ID NLN Link Image
Enzyme 10 HGNC ID HGNC:16058 Link Image
Enzyme 10 Chromosome Location 5
Enzyme 10 Locus 5q12.3
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Nagase T, Ishikawa K, Kikuno R, Hirosawa M, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Oct 29;6(5):337-45. [PubMed Link Image]
  2. Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed Link Image]
  3. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  4. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 17088
Enzyme 11 Name B1 bradykinin receptor
Enzyme 11 Synonyms
  1. B1R
  2. BK-1 receptor
Enzyme 11 Gene Name BDKRB1
Enzyme 11 Protein Sequence >B1 bradykinin receptor
MASSWPPLELQSSNQSQLFPQNATACDNAPEAWDLLHRVLPTFIISICFFGLLGNLFVLL
VFLLPRRQLNVAEIYLANLAASDLVFVLGLPFWAENIWNQFNWPFGALLCRVINGVIKAN
LFISIFLVVAISQDRYRVLVHPMASRRQQRRRQARVTCVLIWVVGGLLSIPTFLLRSIQA
VPDLNITACILLLPHEAWHFARIVELNILGFLLPLAAIVFFNYHILASLRTREEVSRTRC
GGRKDSKTTALILTLVVAFLVCWAPYHFFAFLEFLFQVQAVRGCFWEDFIDLGLQLANFF
AFTNSSLNPVIYVFVGRLFRTKVWELYKQCTPKSLAPISSSHRKEIFQLFWRN
Enzyme 11 Number of Residues 353
Enzyme 11 Molecular Weight 40494.3
Enzyme 11 Theoretical pI 9.57
Enzyme 11 GO Classification
Function
  • bradykinin receptor activity
  • molecular transducer activity
  • peptide receptor activity
  • peptide receptor activity, G-protein coupled
  • receptor activity
  • signal transducer activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 11 General Function Involved in G-protein coupled receptor protein signaling pathway
Enzyme 11 Specific Function This is a receptor for bradykinin. Could be a factor in chronic pain and inflammation
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions Not Available
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • 41-64 74-98 112-133 156-178 200-226 248-272 292-314
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 21929054 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID P46663 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name BKRB1_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >1062 bp
ATGGCATCATCCTGGCCCCCTCTAGAGCTCCAATCCTCCAACCAGAGCCAGCTCTTCCCT
CAAAATGCTACGGCCTGTGACAATGCTCCAGAAGCCTGGGACCTGCTGCACAGAGTGCTG
CCAACATTTATCATCTCCATCTGTTTCTTCGGCCTCCTAGGGAACCTTTTTGTCCTGTTG
GTCTTCCTCCTGCCCCGGCGGCAACTGAACGTGGCAGAAATCTACCTGGCCAACCTGGCA
GCCTCTGATCTGGTGTTTGTCTTGGGCTTGCCCTTCTGGGCAGAGAATATCTGGAACCAG
TTTAACTGGCCTTTCGGAGCCCTCCTCTGCCGTGTCATCAACGGGGTCATCAAGGCCAAT
TTGTTCATCAGCATCTTCCTGGTGGTGGCCATCAGCCAGGACCGCTACCGCGTGCTGGTG
CACCCTATGGCCAGCCGGAGGCAGCAGCGGCGGAGGCAGGCCCGGGTCACCTGCGTGCTC
ATCTGGGTTGTGGGGGGCCTCTTGAGCATCCCCACATTCCTGCTGCGATCCATCCAAGCC
GTCCCAGATCTGAACATCACCGCCTGCATCCTGCTCCTCCCCCATGAGGCCTGGCACTTT
GCAAGGATTGTGGAGTTAAATATTCTGGGTTTCCTCCTACCACTGGCTGCGATCGTCTTC
TTCAACTACCACATCCTGGCCTCCCTGCGAACGCGGGAGGAGGTCAGCAGGACAAGGTGC
GGGGGCCGCAAGGATAGCAAGACCACAGCGCTGATCCTCACGCTCGTGGTTGCCTTCCTG
GTCTGCTGGGCCCCTTACCACTTCTTTGCCTTCCTGGAATTCTTATTCCAGGTGCAAGCA
GTCCGAGGCTGCTTTTGGGAGGACTTCATTGACCTGGGCCTGCAATTGGCCAACTTCTTT
GCCTTCACTAACAGCTCCCTGAATCCAGTAATTTATGTCTTTGTGGGCCGGCTCTTCAGG
ACCAAGGTCTGGGAACTTTATAAACAATGCACCCCTAAAAGTCTTGCTCCAATATCTTCA
TCCCATAGGAAAGAAATCTTCCAACTTTTCTGGCGGAATTAA
Enzyme 11 GenBank Gene ID AB065896 Link Image
Enzyme 11 GeneCard ID BDKRB1 Link Image
Enzyme 11 GenAtlas ID BDKRB1 Link Image
Enzyme 11 HGNC ID HGNC:1029 Link Image
Enzyme 11 Chromosome Location 1
Enzyme 11 Locus 14q32.1-q32.2
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Menke JG, Borkowski JA, Bierilo KK, MacNeil T, Derrick AW, Schneck KA, Ransom RW, Strader CD, Linemeyer DL, Hess JF: Expression cloning of a human B1 bradykinin receptor. J Biol Chem. 1994 Aug 26;269(34):21583-6. [PubMed Link Image]
  2. Yang X, Polgar P: Genomic structure of the human bradykinin B1 receptor gene and preliminary characterization of its regulatory regions. Biochem Biophys Res Commun. 1996 May 24;222(3):718-25. [PubMed Link Image]
  3. Bachvarov DR, Hess JF, Menke JG, Larrivee JF, Marceau F: Structure and genomic organization of the human B1 receptor gene for kinins (BDKRB1). Genomics. 1996 May 1;33(3):374-81. [PubMed Link Image]
  4. Jones C, Phillips E, Davis C, Arbuckle J, Yaqoob M, Burgess GM, Docherty RJ, Webb M, Bevan SJ, McIntyre P: Molecular characterisation of cloned bradykinin B1 receptors from rat and human. Eur J Pharmacol. 1999 Jun 25;374(3):423-33. [PubMed Link Image]
  5. 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 TO, 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: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 17089
Enzyme 12 Name cDNA FLJ75760, highly similar to Homo sapiens bradykinin receptor B1 (BDKRB1), mRNA
Enzyme 12 Synonyms
  1. SubName: Bradykinin receptor B1
Enzyme 12 Gene Name BDKRB1
Enzyme 12 Protein Sequence >cDNA FLJ75760, highly similar to Homo sapiens bradykinin receptor B1 (BDKRB1), mRNA
MASSWPPLELQSSNQSQLFPQNATACDNAPEAWDLLHRVLPTFIISICFFGLLGNLFVLL
VFLLPRRQLNVAEIYLANLAASDLVFVLGLPFWAENIWNQFNWPFGALLCRVINGVIKAN
LFISIFLVVAISQDRYRVLVHPMASRRQQRRRQARVTCVLIWVVGGLLSIPTFLLRSIQA
VPDLNITACILLLPHEAWHFARIVELNILGFLLPLAAIVFFNYHILASLRTREEVSRTRC
GGRKDSKTTALILTLVVAFLVCWAPYHFFAFLEFLFQVQAVRGCFWEDFIDLGLQLANFF
AFTNSSLNPVIYVFVGRLFRTKVWELYKQCTPKSLAPISSSHRKEIFQLFWRN
Enzyme 12 Number of Residues 353
Enzyme 12 Molecular Weight 40495
Enzyme 12 Theoretical pI 9.57
Enzyme 12 GO Classification
Function
  • G-protein coupled receptor activity
  • bradykinin receptor activity
  • peptide receptor activity, G-protein coupled
  • receptor activity
  • rhodopsin-like receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • signal transduction
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 12 General Function Not Available
Enzyme 12 Specific Function Not Available
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions Not Available
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein Not Available
Enzyme 12 UniProtKB/Swiss-Prot ID A8K7F5 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name A8K7F5_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence Not Available
Enzyme 12 GenBank Gene ID AK291970 Link Image
Enzyme 12 GeneCard ID A8K7F5 Link Image
Enzyme 12 GenAtlas ID Not Available
Enzyme 12 HGNC ID Not Available
Enzyme 12 Chromosome Location 14
Enzyme 12 Locus 14q32.1-q32.2
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References Not Available
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 17090
Enzyme 13 Name cDNA FLJ55307, highly similar to B2 bradykinin receptor
Enzyme 13 Synonyms Not Available
Enzyme 13 Gene Name Not Available
Enzyme 13 Protein Sequence >cDNA FLJ55307, highly similar to B2 bradykinin receptor
MLNVTLQGPTLNGTFAQSKCPQVEWLGWLNTIQPPFLWVLFVLATLENIFVLSVFCLHKS
SCTVAEIYLGNLAAADLILACGLPFWAITISNNFDWLFGETLCRVVNAIISMNLYSSICF
LMLVSIDRYLALVKTMSMGRMRGVRWAKLYSLVIWGCTLLLSSPMLVFRTMKEYSDEGHN
VTACVISYPSLIWEVFTNMLLNVVGFLLPLSVITFCTMQIMQVLRNNEMQKFKEIQTERR
ATVLVLVVLLLFIICWLPFQISTFLDTLHRLGILSSCQDERIIDVITQIASFMAYSNSCL
NPLVYVIVGKRFRKKSWEVYQGVCQKGGCRSEPIQMENSMGTLRTPISVERQIHKLQDWA
GSRQ
Enzyme 13 Number of Residues 364
Enzyme 13 Molecular Weight 41450.8
Enzyme 13 Theoretical pI 8.32
Enzyme 13 GO Classification
Function
  • bradykinin receptor activity
  • molecular transducer activity
  • peptide receptor activity
  • peptide receptor activity, G-protein coupled
  • receptor activity
  • signal transducer activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 13 General Function Involved in G-protein coupled receptor protein signaling pathway
Enzyme 13 Specific Function Not Available
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions Not Available
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 194387826 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID B4DRL4 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name B4DRL4_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1095 bp
ATGCTCAATGTCACCTTGCAAGGGCCCACTCTTAACGGGACCTTTGCCCAGAGCAAATGC
CCCCAAGTGGAGTGGCTGGGCTGGCTCAACACCATCCAGCCCCCCTTCCTCTGGGTGCTG
TTCGTGCTGGCCACCCTAGAGAACATCTTTGTCCTCAGCGTCTTCTGCCTGCACAAGAGC
AGCTGCACGGTGGCAGAGATCTACCTGGGGAACCTGGCCGCAGCAGACCTGATCCTGGCC
TGCGGGCTGCCCTTCTGGGCCATCACCATCTCCAACAACTTCGACTGGCTCTTTGGGGAG
ACGCTCTGCCGCGTGGTGAATGCCATTATCTCCATGAACCTGTACAGCAGCATCTGTTTC
CTGATGCTGGTGAGCATCGACCGCTACCTGGCCCTGGTGAAAACCATGTCCATGGGCCGG
ATGCGCGGCGTGCGCTGGGCCAAGCTCTACAGCTTGGTGATCTGGGGGTGTACGCTGCTC
CTGAGCTCACCCATGCTGGTGTTCCGGACCATGAAGGAGTACAGCGATGAGGGCCACAAC
GTCACCGCTTGTGTCATCAGCTACCCATCCCTCATCTGGGAAGTGTTCACCAACATGCTC
CTGAATGTCGTGGGCTTCCTGCTGCCCCTGAGTGTCATCACCTTCTGCACGATGCAGATC
ATGCAGGTGCTGCGGAACAACGAGATGCAGAAGTTCAAGGAGATCCAGACGGAGAGGAGG
GCCACGGTGCTAGTCCTGGTTGTGCTGCTGCTATTCATCATCTGCTGGCTGCCCTTCCAG
ATCAGCACCTTCCTGGATACGCTGCATCGCCTCGGCATCCTCTCCAGCTGCCAGGACGAG
CGCATCATCGATGTAATCACACAGATCGCCTCCTTCATGGCCTACAGCAACAGCTGCCTC
AACCCACTGGTGTACGTGATCGTGGGCAAGCGCTTCCGAAAGAAGTCTTGGGAGGTGTAC
CAGGGAGTGTGCCAGAAAGGGGGCTGCAGGTCAGAACCCATTCAGATGGAGAACTCCATG
GGCACACTGCGGACCCCCATCTCCGTGGAACGCCAGATTCACAAACTGCAGGACTGGGCA
GGGAGCAGACAGTGA
Enzyme 13 GenBank Gene ID AK299316 Link Image
Enzyme 13 GeneCard ID Not Available
Enzyme 13 GenAtlas ID Not Available
Enzyme 13 HGNC ID HGNC:1030 Link Image
Enzyme 13 Chromosome Location Not Available
Enzyme 13 Locus Not Available
Enzyme 13 SNPs Not Available
Enzyme 13 General References Not Available
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 17091
Enzyme 14 Name Bradykinin B1 receptor
Enzyme 14 Synonyms Not Available
Enzyme 14 Gene Name Not Available
Enzyme 14 Protein Sequence >Bradykinin B1 receptor
APISSSHRKEIFQLFWRN
Enzyme 14 Number of Residues 18
Enzyme 14 Molecular Weight 2216.5
Enzyme 14 Theoretical pI 11.48
Enzyme 14 GO Classification Not Available
Enzyme 14 General Function Involved in receptor activity
Enzyme 14 Specific Function Not Available
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions Not Available
Enzyme 14 Pfam Domain Function Not Available
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein Not Available
Enzyme 14 UniProtKB/Swiss-Prot ID Q71U72 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name Q71U72_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >57 bp
GCTCCAATATCTTCATCCCATAGGAAAGAAATCTTCCAACTTTTCTGGCGGAATTAA
Enzyme 14 GenBank Gene ID AF117819 Link Image
Enzyme 14 GeneCard ID Not Available
Enzyme 14 GenAtlas ID Not Available
Enzyme 14 HGNC ID Not Available
Enzyme 14 Chromosome Location Not Available
Enzyme 14 Locus Not Available
Enzyme 14 SNPs Not Available
Enzyme 14 General References
  1. Zhou X, Prado GN, Chai M, Yang X, Taylor L, Polgar P: Posttranscriptional destabilization of the bradykinin B1 receptor messenger RNA: cloning and functional characterization of the 3'-untranslated region. Mol Cell Biol Res Commun. 1999 Apr;1(1):29-35. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 17092
Enzyme 15 Name B2 bradykinin receptor basal promoter, allele BP-58-T
Enzyme 15 Synonyms Not Available
Enzyme 15 Gene Name Not Available
Enzyme 15 Protein Sequence >B2 bradykinin receptor basal promoter, allele BP-58-T
QSSAGGGGGSAQEADDIITQPLKDELFPPPLQLWLLGSEE
Enzyme 15 Number of Residues 40
Enzyme 15 Molecular Weight 4152.5
Enzyme 15 Theoretical pI 3.47
Enzyme 15 GO Classification Not Available
Enzyme 15 General Function Involved in receptor activity
Enzyme 15 Specific Function Not Available
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions Not Available
Enzyme 15 Pfam Domain Function Not Available
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 1216155 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID Q13833 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name Q13833_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >122 bp
GCAGAGCTCAGCTGGAGGCGGAGGGGGAAGTGCCCAGGAGGCTGATGACATCATTACCCA
GCCCTTGAAAGATGAGCTGTTCCCGCCGCCACTCCAGCTCTGGCTTCTGGGCTCCGAGGA
GG
Enzyme 15 GenBank Gene ID X91664 Link Image
Enzyme 15 GeneCard ID Not Available
Enzyme 15 GenAtlas ID Not Available
Enzyme 15 HGNC ID Not Available
Enzyme 15 Chromosome Location Not Available
Enzyme 15 Locus Not Available
Enzyme 15 SNPs Not Available
Enzyme 15 General References
  1. Braun A, Maier E, Kammerer S, Muller B, Roscher AA: A novel sequence polymorphism in the promoter region of the human B2-bradykinin receptor gene. Hum Genet. 1996 May;97(5):688-9. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 17093
Enzyme 16 Name B2 bradykinin receptor basal promoter, allele BP-58-C
Enzyme 16 Synonyms Not Available
Enzyme 16 Gene Name Not Available
Enzyme 16 Protein Sequence >B2 bradykinin receptor basal promoter, allele BP-58-C
QSSAGGGGGSAQEADDITTQPLKDELFPPPLQLWLLGSEE
Enzyme 16 Number of Residues 40
Enzyme 16 Molecular Weight 4140.4
Enzyme 16 Theoretical pI 3.47
Enzyme 16 GO Classification Not Available
Enzyme 16 General Function Involved in receptor activity
Enzyme 16 Specific Function Not Available
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions Not Available
Enzyme 16 Pfam Domain Function Not Available
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 1216153 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID Q13832 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name Q13832_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >122 bp
GCAGAGCTCAGCTGGAGGCGGAGGGGGAAGTGCCCAGGAGGCTGATGACATCACTACCCA
GCCCTTGAAAGATGAGCTGTTCCCGCCGCCACTCCAGCTCTGGCTTCTGGGCTCCGAGGA
GG
Enzyme 16 GenBank Gene ID X91663 Link Image
Enzyme 16 GeneCard ID Not Available
Enzyme 16 GenAtlas ID Not Available
Enzyme 16 HGNC ID Not Available
Enzyme 16 Chromosome Location Not Available
Enzyme 16 Locus Not Available
Enzyme 16 SNPs Not Available
Enzyme 16 General References
  1. Braun A, Maier E, Kammerer S, Muller B, Roscher AA: A novel sequence polymorphism in the promoter region of the human B2-bradykinin receptor gene. Hum Genet. 1996 May;97(5):688-9. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 17094
Enzyme 17 Name Putative uncharacterized protein DKFZp686O088
Enzyme 17 Synonyms Not Available
Enzyme 17 Gene Name DKFZp686O088
Enzyme 17 Protein Sequence >Putative uncharacterized protein DKFZp686O088
MLNVTLQGPTLNGTFAQSKCPQVEWLGWLNTIQPPFLWVLFVLATLENIFVLSVFCLHKS
SCTVAEIYLGNLAAADLILACGLPFWAITISNNFDWLFGETLCRVVNAIISMNLYSSICF
LMLVSIDRYLALVKTMSMGRMRGVRWAKLYSLVIWGCTLLLSSPMLVFRTMKEYSDEGHN
VTARVISYPSLIWEVFTNMLLNVVGFLLPLSVITFCTMQIMQVLRNNEMQKFKEIQTERR
ATVLVLVVLLLFIICWLPFQISTFLDTLHRLGILSSCQDERIIDVITQIASFMAYSNSCL
NPLVYVIVGKRFRKKSWEVYQGVCQKGGCRSEPIQMENSMGTLRTSISVERQIHKLQDWA
GSRQ
Enzyme 17 Number of Residues 364
Enzyme 17 Molecular Weight 41493.8
Enzyme 17 Theoretical pI 8.48
Enzyme 17 GO Classification
Function
  • bradykinin receptor activity
  • molecular transducer activity
  • peptide receptor activity
  • peptide receptor activity, G-protein coupled
  • receptor activity
  • signal transducer activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 17 General Function Involved in G-protein coupled receptor protein signaling pathway
Enzyme 17 Specific Function Not Available
Enzyme 17 Pathways Not Available
Enzyme 17 Reactions Not Available
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 51476404 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID Q68DM8 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name Q68DM8_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >1095 bp
ATGCTCAATGTCACCTTGCAAGGGCCCACTCTTAACGGGACCTTTGCCCAGAGCAAATGC
CCCCAAGTGGAGTGGCTGGGCTGGCTCAACACCATCCAGCCCCCCTTCCTCTGGGTGCTG
TTCGTGCTGGCCACCCTAGAGAACATCTTTGTCCTCAGCGTCTTCTGCCTGCACAAGAGC
AGCTGCACGGTGGCAGAGATCTACCTGGGGAACCTGGCCGCAGCAGACCTGATCCTGGCC
TGCGGGCTGCCCTTCTGGGCCATCACCATCTCCAACAACTTCGACTGGCTCTTTGGGGAG
ACGCTCTGCCGCGTGGTGAATGCCATTATCTCCATGAACCTGTACAGCAGCATCTGTTTC
CTGATGCTGGTGAGCATCGACCGCTACCTGGCCCTGGTGAAAACCATGTCCATGGGCCGG
ATGCGCGGCGTGCGCTGGGCCAAGCTCTACAGCTTGGTGATCTGGGGGTGTACGCTGCTC
CTGAGCTCACCCATGCTGGTGTTCCGGACCATGAAGGAGTACAGCGATGAGGGCCACAAC
GTCACCGCTCGTGTCATCAGCTACCCATCCCTCATCTGGGAAGTGTTCACCAACATGCTC
CTGAATGTCGTGGGCTTCCTGCTGCCCCTGAGTGTCATCACCTTCTGCACGATGCAGATC
ATGCAGGTGCTGCGGAACAACGAGATGCAGAAGTTCAAGGAGATCCAGACGGAGAGGAGG
GCCACGGTGCTAGTCCTGGTTGTGCTGCTGCTATTCATCATCTGCTGGCTGCCCTTCCAG
ATCAGCACCTTCCTGGATACGCTGCATCGCCTCGGCATCCTCTCCAGCTGCCAGGACGAG
CGCATCATCGATGTAATCACACAGATCGCCTCCTTCATGGCCTACAGCAACAGCTGCCTC
AACCCACTGGTGTACGTGATCGTGGGCAAGCGCTTCCGAAAGAAGTCTTGGGAGGTGTAC
CAGGGAGTGTGCCAGAAAGGGGGCTGCAGGTCAGAACCCATTCAGATGGAGAACTCCATG
GGCACACTGCGGACCTCCATCTCCGTGGAACGCCAGATTCACAAACTGCAGGACTGGGCA
GGGAGCAGACAGTGA
Enzyme 17 GenBank Gene ID CR749338 Link Image
Enzyme 17 GeneCard ID DKFZp686O088 Link Image
Enzyme 17 GenAtlas ID DKFZp686O088 Link Image
Enzyme 17 HGNC ID HGNC:1030 Link Image
Enzyme 17 Chromosome Location Not Available
Enzyme 17 Locus Not Available
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References Not Available
Enzyme 17 Metabolite References Not Available