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Human Metabolome Database Version 2.5

 

Showing metabocard for Methionine sulfoxide (HMDB02005)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-05-22 15:17:31
Update Date 2010-04-26 12:47:17
Accession Number HMDB02005
Secondary Accession Numbers Not Available
Common Name Methionine sulfoxide
Description Methionine sulfoxide is an oxidation product of methionine with reactive oxygen species via 2-electron-dependent mechanism. Such oxidants can be generated from activated neutrophils; therefore, methionine sulfoxide can be regarded as a biomarker of oxidative stress in vivo. (PMID 12576054)
Synonyms
  1. DL-Methionine sulfoxide
  2. L-Methionine sulfoxide
  3. S-oxide-methionine
  4. alpha-amino-gamma-(methylsulfinyl)-Butyric acid
  5. 2-amino-4-(methylsulfinyl)-Butanoic acid
  6. 2-amino-4-(methylsulfinyl)-Butanoate
  7. L-methionine R-oxide;L-methionine (S)-S-oxide
Chemical IUPAC Name 2-amino-4-methylsulfinyl-butanoic acid
Chemical Formula C5H11NO3S
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Amino Acids
Sub Class
  • NA
Family
  • Mammalian Metabolite
Species
  • primary amine
  • primary aliphatic amine (alkylamine)
  • carboxylic acid
  • sulfoxide
  • alpha-aminoacid
Biofunction
  • Protein synthesis, amino acid biosynthesis
Application
Source
  • Endogenous
Average Molecular Weight 165.211
Monoisotopic Molecular Weight 165.045959
Isomeric SMILES CS(=O)CCC(N)C(O)=O
Canonical SMILES CS(=O)CCC(N)C(O)=O
KEGG Compound ID Not Available
BioCyc ID L-METHIONINE_SULFOXIDE Link Image
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB02005 Link Image
Metagene Link HMDB02005 Link Image
METLIN ID 6428 Link Image
PubChem Compound 847 Link Image
PubChem Substance 10487164 Link Image
ChEBI ID Not Available
CAS Registry Number 62697-73-8
InChI Identifier InChI=1/C5H11NO3S/c1-10(9)3-2-4(6)5(7)8/h4H,2-3,6H2,1H3,(H,7,8)
Synthesis Reference Not Available
Melting Point (Experimental) 232 - 234 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 54.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.40 [Predicted by ALOGPS]; -3.9 [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 Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
Biofluid Location
  • Blood
  • Urine
Tissue Location
Tissue References
Epidermis
Concentrations (Normal)
Biofluid Blood
Value 4.0 (3.0-5.0) uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Doctor's Data
Biofluid Urine
Value < 0.132 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Doctor's Data
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Methionine Metabolism SMP00033 Link Image map00270 Link Image
General References
  1. Schallreuter KU: Functioning methionine-S-sulfoxide reductases A and B are present in human skin. J Invest Dermatol. 2006 May;126(5):947-9. [PubMed Link Image]
  2. O'Donohue TL, Charlton CG, Thoa NB, Helke CJ, Moody TW, Pert A, Williams A, Miller RL, Jacobowitz DM: Release of alpha-melanocyte stimulating hormone into rat and human cerebrospinal fluid in vivo and from rat hypothalamus slices in vitro. Peptides. 1981 Spring;2(1):93-100. [PubMed Link Image]
  3. Boudier C, Cadene M, Bieth JG: Inhibition of neutrophil cathepsin G by oxidized mucus proteinase inhibitor. Effect of heparin. Biochemistry. 1999 Jun 29;38(26):8451-7. [PubMed Link Image]
  4. Mashima R, Nakanishi-Ueda T, Yamamoto Y: Simultaneous determination of methionine sulfoxide and methionine in blood plasma using gas chromatography-mass spectrometry. Anal Biochem. 2003 Feb 1;313(1):28-33. [PubMed Link Image]
Metabolic Enzymes
  1. Peptide methionine sulfoxide reductase
  2. Methionine-R-sulfoxide reductase B2, mitochondrial
  3. Methionine-R-sulfoxide reductase B3, mitochondrial
Enzyme 1 [top]
Enzyme 1 ID 5769
Enzyme 1 Name Peptide methionine sulfoxide reductase
Enzyme 1 Synonyms
  1. Peptide-methionine (S)-S-oxide reductase
  2. Peptide Met(O) reductase
  3. Protein-methionine-S-oxide reductase
  4. PMSR
Enzyme 1 Gene Name MSRA
Enzyme 1 Protein Sequence >Peptide methionine sulfoxide reductase
MLSATRRACQLLLLHSLFPVPRMGNSASNIVSPQEALPGRKEQTPVAAKHHVNGNRTVEP
FPEGTQMAVFGMGCFWGAERKFWVLKGVYSTQVGFAGGYTSNPTYKEVCSEKTGHAEVVR
VVYQPEHMSFEELLKVFWENHDPTQGMRQGNDHGTQYRSAIYPTSAKQMEAALSSKENYQ
KVLSEHGFGPITTDIREGQTFYYAEDYHQQYLSKNPNGYCGLGGTGVSCPVGIKK
Enzyme 1 Number of Residues 235
Enzyme 1 Molecular Weight 26132.4
Enzyme 1 Theoretical pI 8.21
Enzyme 1 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on a sulfur group of donors
  • oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor
Process
  • macromolecule metabolic process
  • metabolic process
  • oxidation reduction
  • protein metabolic process
Component
Enzyme 1 General Function Involved in oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor
Enzyme 1 Specific Function Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine
Enzyme 1 Pathways Not Available
Enzyme 1 Reactions
  • (1) peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin [RN:R04120]
  • (2) L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin [RN:R07606]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 6136945 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q9UJ68 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name MSRA_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >708 bp
ATGCTCTCGGCCACCCGGAGGGCTTGCCAGCTCCTCCTCCTCCACAGCCTCTTTCCCGTC
CCGAGGATGGGCAACTCGGCCTCGAACATCGTCAGCCCCCAGGAGGCCTTGCCGGGCCGG
AAGGAACAGACCCCTGTAGCGGCCAAACATCATGTCAATGGCAACAGAACAGTCGAACCT
TTCCCAGAGGGAACACAGATGGCTGTATTTGGAATGGGATGTTTCTGGGGAGCTGAAAGG
AAATTCTGGGTCTTGAAAGGAGTGTATTCAACTCAAGTTGGTTTTGCAGGAGGCTATACT
TCAAATCCTACTTATAAAGAAGTCTGCTCAGAAAAAACTGGCCATGCAGAAGTCGTCCGA
GTGGTGTACCAGCCAGAACACATGAGTTTTGAGGAACTGCTCAAGGTCTTCTGGGAGAAT
CACGACCCGACCCAAGGTATGCGCCAGGGGAACGACCATGGCACTCAGTACCGCTCGGCC
ATCTACCCGACCTCTGCCAAGCAAATGGAGGCAGCCCTGAGCTCCAAAGAGAACTACCAA
AAGGTTCTTTCAGAGCACGGCTTCGGCCCCATCACTACCGACATCCGGGAGGGACAGACT
TTCTACTATGCGGAAGACTACCACCAGCAGTACCTGAGCAAGAACCCCAATGGCTACTGC
GGCCTTGGGGGCACCGGCGTGTCCTGCCCAGTGGGTATTAAAAAATAA
Enzyme 1 GenBank Gene ID AJ242973 Link Image
Enzyme 1 GeneCard ID MSRA Link Image
Enzyme 1 GenAtlas ID MSRA Link Image
Enzyme 1 HGNC ID HGNC:7377 Link Image
Enzyme 1 Chromosome Location 8
Enzyme 1 Locus 8p23.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Kuschel L, Hansel A, Schonherr R, Weissbach H, Brot N, Hoshi T, Heinemann SH: Molecular cloning and functional expression of a human peptide methionine sulfoxide reductase (hMsrA). FEBS Lett. 1999 Jul 30;456(1):17-21. [PubMed Link Image]
  2. 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]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 14940
Enzyme 2 Name Methionine-R-sulfoxide reductase B2, mitochondrial
Enzyme 2 Synonyms
  1. MsrB2
Enzyme 2 Gene Name MSRB2
Enzyme 2 Protein Sequence >Methionine-R-sulfoxide reductase B2, mitochondrial
MARLLWLLRGLTLGTAPRRAVRGQAGGGGPGTGPGLGEAGSLATCELPLAKSEWQKKLTP
EQFYVTREKGTEPPFSGIYLNNKEAGMYHCVCCDSPLFSSEKKYCSGTGWPSFSEAHGTS
GSDESHTGILRRLDTSLGSARTEVVCKQCEAHLGHVFPDGPGPNGQRFCINSVALKFKPR
KH
Enzyme 2 Number of Residues 182
Enzyme 2 Molecular Weight 19536.1
Enzyme 2 Theoretical pI 8.76
Enzyme 2 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on a sulfur group of donors
  • oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor
  • peptide-methionine-(S)-S-oxide reductase activity
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 2 General Function Involved in peptide-methionine-(S)-S-oxide reductase activity
Enzyme 2 Specific Function Catalyzes the reduction of free and protein-bound methionine sulfoxide to methionine
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 5059062 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q9Y3D2 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name MSRB2_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >549 bp
ATGGCGCGGCTCCTCTGGTTGCTCCGGGGCCTGACCCTCGGAACTGCGCCTCGGCGGGCG
GTGCGGGGCCAAGCGGGCGGCGGCGGGCCCGGCACCGGGCCGGGACTGGGGGAGGCAGGG
TCTCTTGCAACGTGTGAGCTGCCTCTTGCCAAGAGTGAGTGGCAAAAGAAACTAACCCCG
GAGCAGTTCTACGTCACAAGAGAAAAGGGAACGGAACCGCCTTTCAGTGGGATCTACCTG
AATAACAAGGAAGCAGGAATGTATCATTGCGTGTGCTGCGACAGTCCACTCTTCAGTTCT
GAGAAAAAGTACTGCTCTGGCACTGGGTGGCCTTCGTTTTCCGAGGCTCATGGTACGTCT
GGCTCTGATGAAAGCCACACAGGGATCCTGAGACGTCTGGATACCTCGTTAGGATCAGCT
CGCACAGAGGTTGTCTGCAAGCAGTGTGAAGCTCATCTAGGTCACGTGTTTCCTGATGGA
CCTGGGCCCAATGGTCAGAGGTTTTGCATCAACAGTGTGGCTTTGAAGTTCAAACCAAGG
AAACACTGA
Enzyme 2 GenBank Gene ID AF122004 Link Image
Enzyme 2 GeneCard ID MSRB2 Link Image
Enzyme 2 GenAtlas ID MSRB2 Link Image
Enzyme 2 HGNC ID HGNC:17061 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 10p12
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Huang W, Escribano J, Sarfarazi M, Coca-Prados M: Identification, expression and chromosome localization of a human gene encoding a novel protein with similarity to the pilB family of transcriptional factors (pilin) and to bacterial peptide methionine sulfoxide reductases. Gene. 1999 Jun 11;233(1-2):233-40. [PubMed Link Image]
  2. Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W: Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. Genome Res. 2000 May;10(5):703-13. [PubMed Link Image]
  3. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [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. Marchetti MA, Pizarro GO, Sagher D, Deamicis C, Brot N, Hejtmancik JF, Weissbach H, Kantorow M: Methionine sulfoxide reductases B1, B2, and B3 are present in the human lens and confer oxidative stress resistance to lens cells. Invest Ophthalmol Vis Sci. 2005 Jun;46(6):2107-12. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 14941
Enzyme 3 Name Methionine-R-sulfoxide reductase B3, mitochondrial
Enzyme 3 Synonyms
  1. MsrB3
Enzyme 3 Gene Name MSRB3
Enzyme 3 Protein Sequence >Methionine-R-sulfoxide reductase B3, mitochondrial
MSAFNLLHLVTKSQPVALRACGLPSGSCRDKKNCKVVFSQQELRKRLTPLQYHVTQEKGT
ESAFEGEYTHHKDPGIYKCVVCGTPLFKSETKFDSGSGWPSFHDVINSEAITFTDDFSYG
MHRVETSCSQCGAHLGHIFDDGPRPTGKRYCINSAALSFTPADSSGTAEGGSGVASPAQA
DKAEL
Enzyme 3 Number of Residues 185
Enzyme 3 Molecular Weight 20010.2
Enzyme 3 Theoretical pI 7.18
Enzyme 3 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on a sulfur group of donors
  • oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor
  • peptide-methionine-(S)-S-oxide reductase activity
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 3 General Function Involved in peptide-methionine-(S)-S-oxide reductase activity
Enzyme 3 Specific Function Catalyzes the reduction of free and protein-bound methionine sulfoxide to methionine
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 158259629 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q8IXL7 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name MSRB3_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >558 bp
ATGTCTGCATTCAACCTGCTGCATTTGGTGACAAAGAGCCAGCCAGTAGCCCTTCGAGCC
TGTGGGCTTCCCTCAGGGTCGTGTAGGGATAAAAAGAACTGTAAGGTGGTCTTTTCCCAG
CAGGAACTGAGGAAGCGGCTAACACCCCTGCAGTACCATGTCACTCAGGAGAAAGGGACC
GAAAGTGCCTTTGAAGGAGAATACACACATCACAAAGATCCTGGAATATATAAATGTGTT
GTTTGTGGAACTCCATTGTTTAAGTCAGAAACCAAATTTGACTCCGGTTCAGGTTGGCCT
TCATTCCACGATGTGATCAATTCTGAGGCAATCACATTCACAGATGACTTTTCCTATGGG
ATGCACAGGGTGGAAACAAGCTGCTCTCAGTGTGGTGCTCACCTTGGGCACATTTTTGAT
GATGGGCCTCGTCCAACTGGGAAAAGATACTGCATAAATTCGGCTGCCTTGTCTTTTACA
CCTGCGGATAGCAGTGGCACCGCCGAGGGAGGCAGTGGGGTCGCCAGCCCGGCCCAGGCA
GACAAAGCGGAGCTCTAG
Enzyme 3 GenBank Gene ID AK293084 Link Image
Enzyme 3 GeneCard ID MSRB3 Link Image
Enzyme 3 GenAtlas ID MSRB3 Link Image
Enzyme 3 HGNC ID HGNC:27375 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 12q14.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. 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]
  2. 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]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
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Enzyme 3 Metabolite References Not Available