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Human Metabolome Database Version 2.5

 

Showing metabocard for 4-Hydroxy-L-proline (HMDB06055)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2007-04-12 22:28:41
Update Date 2009-12-14 14:59:06
Accession Number HMDB06055
Secondary Accession Numbers Not Available
Common Name 4-Hydroxy-L-proline
Description A hydroxylated form of the imino acid proline. A deficiency in ascorbic acid can result in impaired hydroxyproline formation. (PubChem CID:69248)
Synonyms
  1. L-4-hydroxy-proline
  2. L-4-Hydroxyproline
  3. L-4-allo-hydroxy-Proline
  4. 4-hydroxy-L-Proline
  5. cis-4-hydroxy-L-Proline
  6. cis-4-hydroxyproline;(2S)-4-hydroxypyrrolidine-2-carboxylic acid
  7. (4S)-4-hydroxy-L-Proline
  8. allo-4-Hydroxy-L-proline
  9. allo-4-Hydroxyproline
  10. allo-hydroxy-L-Proline
  11. L-Allohydroxyproline
Chemical IUPAC Name (2S)-4-hydroxypyrrolidine-2-carboxylic acid
Chemical Formula C5H9NO3
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
  • secondary alcohol
  • 1,2-aminoalcohol
  • secondary amine
  • secondary aliphatic amine (dialkylamine)
  • carboxylic acid
  • heterocyclic compound
  • alpha-aminoacid
Biofunction
Application
Source
  • Endogenous
Average Molecular Weight 131.130
Monoisotopic Molecular Weight 131.058243
Isomeric SMILES OC1CN[C@@H](C1)C(O)=O
Canonical SMILES OC1CNC(C1)C(O)=O
KEGG Compound ID C01015 Link Image
BioCyc ID Protein-hydroxyprolines Link Image
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB06055 Link Image
Metagene Link HMDB06055 Link Image
METLIN ID Not Available
PubChem Compound 69248 Link Image
PubChem Substance 10366583 Link Image
ChEBI ID 18240 Link Image
CAS Registry Number 30724-02-8
InChI Identifier InChI=1/C5H9NO3/c7-3-1-4(5(8)9)6-2-3/h3-4,6-7H,1-2H2,(H,8,9)/t3?,4-/m0/s1
Synthesis Reference Not Available
Melting Point (Experimental) 274 oC
Experimental Water Solubility 361 mg/mL at 25 oC [MERCK INDEX (1996)] Source: PhysProp
Predicted Water Solubility 492.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity -3.17 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP/Hydrophobicity -3.31 [Predicted by ALOGPS]; -3.4 [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 Not Available
Not Available
Predicted 13C NMR Spectrum Not Available
Not Available
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location Not Available
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location Not Available
Concentrations (Normal)
Biofluid Urine
Value 0.15 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Guo K, Li L: Differential (12)C-/(13)C-Isotope Dansylation Labeling and Fast Liquid Chromatography/Mass Spectrometry for Absolute and Relative Quantification of the Metabolome. Anal Chem. 2009 Mar 23. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 5.6 +/- 0.67 uM
Age Adult:>18 yrs old
Sex Both
Condition Alzheimer's disease
Comments Not Available
References
  • Fonteh AN, Harrington RJ, Tsai A, Liao P, Harrington MG: Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids. 2007 Feb;32(2):213-24. Epub 2006 Oct 10. [PubMed Link Image]
Biofluid CSF
Value 0.28 +/- 0.055 uM
Age Adult:>18 yrs old
Sex Both
Condition Alzheimer's disease
Comments Not Available
References
  • Fonteh AN, Harrington RJ, Tsai A, Liao P, Harrington MG: Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids. 2007 Feb;32(2):213-24. Epub 2006 Oct 10. [PubMed Link Image]
Biofluid Urine
Value 0.21 +/- 0.017 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Alzheimer's disease
Comments Not Available
References
  • Fonteh AN, Harrington RJ, Tsai A, Liao P, Harrington MG: Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids. 2007 Feb;32(2):213-24. Epub 2006 Oct 10. [PubMed Link Image]
Associated Disorders
Condition References
Alzheimer's disease
  • Fonteh AN, Harrington RJ, Tsai A, Liao P, Harrington MG: Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids. 2007 Feb;32(2):213-24. Epub 2006 Oct 10. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Arginine and Proline Metabolism SMP00020 Link Image map00330 Link Image
General References
  1. Tasanen K, Eble JA, Aumailley M, Schumann H, Baetge J, Tu H, Bruckner P, Bruckner-Tuderman L: Collagen XVII is destabilized by a glycine substitution mutation in the cell adhesion domain Col15. J Biol Chem. 2000 Feb 4;275(5):3093-9. [PubMed Link Image]
  2. Keskiaho K, Hieta R, Sormunen R, Myllyharju J: Chlamydomonas reinhardtii has multiple prolyl 4-hydroxylases, one of which is essential for proper cell wall assembly. Plant Cell. 2007 Jan;19(1):256-69. Epub 2007 Jan 12. [PubMed Link Image]
  3. Lafranconi WM, Duhamel RC, Brendel K, Huxtable RJ: Differentiation of the cardiac and pulmonary toxicity of monocrotaline, a pyrrolizidine alkaloid. Biochem Pharmacol. 1984 Jan 15;33(2):191-7. [PubMed Link Image]
  4. Sodian R, Hoerstrup SP, Sperling JS, Martin DP, Daebritz S, Mayer JE Jr, Vacanti JP: Evaluation of biodegradable, three-dimensional matrices for tissue engineering of heart valves. ASAIO J. 2000 Jan-Feb;46(1):107-10. [PubMed Link Image]
  5. ADAMS E, GOLDSTONE A, SINGH RM, ROSSO G: SUBSTRATE ACTIVITY OF 3-HYDROXYPROLINE ISOMERS FOR ENZYMES ACTIVE WITH 4-HYDROXYPROLINE. Biochim Biophys Acta. 1964 Jul 8;89:164-6. [PubMed Link Image]
  6. Last JA, Reiser KM, Tyler WS, Rucker RB: Long-term consequences of exposure to ozone. I. Lung collagen content. Toxicol Appl Pharmacol. 1984 Jan;72(1):111-8. [PubMed Link Image]
  7. Koike K, Li Y, Seo M, Sakurada I, Tezuka K, Uchikura K: Free 4-hydroxyproline content in serum of bedridden aged people is elevated due to fracture. Biol Pharm Bull. 2000 Jan;23(1):101-3. [PubMed Link Image]
  8. Burjanadze TV: New analysis of the phylogenetic change of collagen thermostability. Biopolymers. 2000 May;53(6):523-8. [PubMed Link Image]
  9. Dixon IM, Hao J, Reid NL, Roth JC: Effect of chronic AT(1) receptor blockade on cardiac Smad overexpression in hereditary cardiomyopathic hamsters. Cardiovasc Res. 2000 May;46(2):286-97. [PubMed Link Image]
  10. Turpeenniemi-Hujanen T, Myllyla R: Concomitant hydroxylation of proline and lysine residues in collagen using purified enzymes in vitro. Biochim Biophys Acta. 1984 Jul 16;800(1):59-65. [PubMed Link Image]
Metabolic Enzymes
  1. D-amino-acid oxidase
  2. Pyrroline-5-carboxylate reductase 2
  3. Proline dehydrogenase, mitochondrial
  4. cDNA FLJ75752, highly similar to Homo sapiens pyrroline-5-carboxylate reductase family, member 2
  5. Uncharacterized protein PRODH
  6. Melastatin 1 splicing variant
  7. Transient receptor potential cation channel subfamily M member 1
Enzyme 1 [top]
Enzyme 1 ID 5438
Enzyme 1 Name D-amino-acid oxidase
Enzyme 1 Synonyms
  1. DAAO
  2. DAMOX
  3. DAO
Enzyme 1 Gene Name DAO
Enzyme 1 Protein Sequence >D-amino-acid oxidase
MRVVVIGAGVIGLSTALCIHERYHSVLQPLDIKVYADRFTPLTTTDVAAGLWQPYLSDPN
NPQEADWSQQTFDYLLSHVHSPNAENLGLFLISGYNLFHEAIPDPSWKDTVLGFRKLTPR
ELDMFPDYGYGWFHTSLILEGKNYLQWLTERLTERGVKFFQRKVESFEEVAREGADVIVN
CTGVWAGALQRDPLLQPGRGQIMKVDAPWMKHFILTHDPERGIYNSPYIIPGTQTVTLGG
IFQLGNWSELNNIQDHNTIWEGCCRLEPTLKNARIIGERTGFRPVRPQIRLEREQLRTGP
SNTEVIHNYGHGGYGLTIHWGCALEAAKLFGRILEEKKLSRMPPSHL
Enzyme 1 Number of Residues 347
Enzyme 1 Molecular Weight 39473.7
Enzyme 1 Theoretical pI 6.84
Enzyme 1 GO Classification
Function
  • D-amino-acid oxidase activity
  • binding
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH2 group of donors
  • oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 1 General Function Involved in D-amino-acid oxidase activity
Enzyme 1 Specific Function Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D- amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids
Enzyme 1 Pathways
  • Arginine and Proline Metabolism (map00330 Link Image)
  • D-Arginine and D-ornithine Metabolism (map00472 Link Image)
  • Glycine, Serine and Threonine Metabolism (map00260 Link Image)
Enzyme 1 Reactions
  • a D-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2 [RN:R01340]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 30446 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P14920 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name OXDA_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1044 bp
ATGCGTGTGGTGGTGATTGGAGCAGGAGTCATCGGGCTGTCCACCGCCCTCTGCATCCAT
GAGCGCTACCACTCAGTCCTGCAGCCACTGCACATAAAGGTCTACGCGGACCGCTTCACC
CCACTCACCACCACCGACGTGGCTGCCGGCCTCTGGCAGCCCTACCTTTCTGACCCCAAC
AACCCACAGGAGGCGGACTGGAGCCAACAGACCTTTGACTATCTCCTGAGCCATGTCCAT
TCTCCCAACGCTGAAAACCTGGGCCTGTTCCTAATCTCGGGCTACAACCTCTTCCATGAA
GCCATTCCGGACCCTTCCTGGAAGGACACAGTTCTGGGATTTCGGAAGCTGACCCCCAGA
GAGCTGGATATGTTCCCAGATTACGGCTATGGCTGGTTCCACACAAGCCTAATTCTGGAG
GGAAAGAACTATCTACAGTGGCTGACTGAAAGGTTAACTGAGAGGGGAGTGAAGTTCTTC
CAGCGGAAAGTGGAGTCTTTTGAGGAGGTGGCAAGAGAAGGCGCAGACGTGATTGTCAAC
TGCACTGGGGTATGGGCTGGGGCGCTACAACGAGACCCCCTGCTGCAGCCAGGCCGGGGG
CAGATCATGAAGGTGGACGCCCCTTGGATGAAGCACTTCATTCTCACCCATGACCCAGAG
AGAGGCATCTACAATTCCCCGTACATCATCCCAGGGACCCAGACAGTTACTCTTGGAGGC
ATCTTCCAGTTGGGAAACTGGAGTGAACTAAACAATATCCAGGACCACAACACCATTTGG
GAAGGCTGCTGCAGACTGGAGCCCACACTGAAGAATGCAAGAATTATTGGTGAAGCAACT
GGCTTCCGGCCAGTACGCCCCCAGATTCGGCTAGAAAGAGAACAGCTTCGCACTGGACCT
TCAAACACAGAGGTCATCCACAACTATGGCCATGGAGGCTACGGGCTCACCATCCACTGG
GGATGTGCCCTGGAGGCAGCCAAGCTCTTTGGGAGAATCCTGGAAGAAAAGAAATTGTCC
AGAATGCCACCATCCCACCTCTGA
Enzyme 1 GenBank Gene ID X13227 Link Image
Enzyme 1 GeneCard ID DAO Link Image
Enzyme 1 GenAtlas ID DAO Link Image
Enzyme 1 HGNC ID HGNC:2671 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 12q24
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Momoi K, Fukui K, Watanabe F, Miyake Y: Molecular cloning and sequence analysis of cDNA encoding human kidney D-amino acid oxidase. FEBS Lett. 1988 Sep 26;238(1):180-4. [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. 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]
  4. Fukui K, Miyake Y: Molecular cloning and chromosomal localization of a human gene encoding D-amino-acid oxidase. J Biol Chem. 1992 Sep 15;267(26):18631-8. [PubMed Link Image]
  5. Kawazoe T, Tsuge H, Pilone MS, Fukui K: Crystal structure of human D-amino acid oxidase: context-dependent variability of the backbone conformation of the VAAGL hydrophobic stretch located at the si-face of the flavin ring. Protein Sci. 2006 Dec;15(12):2708-17. Epub 2006 Nov 6. [PubMed Link Image]
  6. Kawazoe T, Tsuge H, Imagawa T, Aki K, Kuramitsu S, Fukui K: Structural basis of D-DOPA oxidation by D-amino acid oxidase: alternative pathway for dopamine biosynthesis. Biochem Biophys Res Commun. 2007 Apr 6;355(2):385-91. Epub 2007 Feb 8. [PubMed Link Image]
  7. Sparey T, Abeywickrema P, Almond S, Brandon N, Byrne N, Campbell A, Hutson PH, Jacobson M, Jones B, Munshi S, Pascarella D, Pike A, Prasad GS, Sachs N, Sakatis M, Sardana V, Venkatraman S, Young MB: The discovery of fused pyrrole carboxylic acids as novel, potent D-amino acid oxidase (DAO) inhibitors. Bioorg Med Chem Lett. 2008 Jun 1;18(11):3386-91. Epub 2008 Apr 13. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5540
Enzyme 2 Name Pyrroline-5-carboxylate reductase 2
Enzyme 2 Synonyms
  1. P5C reductase 2
  2. P5CR 2
Enzyme 2 Gene Name PYCR2
Enzyme 2 Protein Sequence >Pyrroline-5-carboxylate reductase 2
MSVGFIGAGQLAYALARGFTAAGILSAHKIIASSPEMNLPTVSALRKMGVNLTRSNKETV
KHSDVLFLAVKPHIIPFILDEIGADVQARHIVVSCAAGVTISSVEKKLMAFQPAPKVIRC
MTNTPVVVQEGATVYATGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAY
AFMALDALADGGVKMGLPRRLAIQLGAQALLGAAKMLLDSEQHPCQLKDNVCSPGGATIH
ALHFLESGGFRSLLINAVEASCIRTRELQSMADQEKISPAALKKTLLDRVKLESPTVSTL
TPSSPGKLLTRSLALGGKKD
Enzyme 2 Number of Residues 320
Enzyme 2 Molecular Weight 33636.8
Enzyme 2 Theoretical pI 7.87
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH group of donors
  • oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
  • pyrroline-5-carboxylate reductase activity
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • glutamine family amino acid metabolic process
  • metabolic process
  • oxidation reduction
  • proline biosynthetic process
  • proline metabolic process
Component
Enzyme 2 General Function Involved in oxidoreductase activity
Enzyme 2 Specific Function L-proline + NAD(P)(+) = 1-pyrroline-5- carboxylate + NAD(P)H
Enzyme 2 Pathways
Enzyme 2 Reactions
  • L-proline + NAD(P)+ = 1-pyrroline-5-carboxylate + NAD(P)H + H+ [RN:R01248 R01251]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 33150582 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q96C36 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name P5CR2_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >963 bp
ATGAGCGTGGGCTTCATCGGGGCCGGCCAGCTGGCTAATGCTCTGGCGCGGGGCTTCACG
GCCGCAGCATTCCTGTCGGCTCACAAGATAATAGCCAGCTCCCCAGAAATGAACCTGCCC
ACGGTGTCCGCGCTCAGGAAGATGGGTGTGAACCTGACACGCAGCAACAAGGAGACGGTG
AAGCACAGCGACGTCCTGTTTCTGGCTGTGAAGCACATTATCATCCCCTTCATCCTGGAT
GAGATTGGGGCCGACGTGCAAGCCAGACACATCGTGGTCTCCTGTGCGGCTGGTGTCACC
ATCAGCTCTGTGGAGAAGAAGCTGATGGCATTCCAGCCAGCCCCCAAAGTGATTCGCTGC
ATGACCAACACACCTGTGGTAGTGCAGGAAGGCGCTACAGTGTACGCCACGGGCACCCAT
GCCCTGGTGGAGGATGGGCAGCTCCTGGAGCAGCTCATGAGCAGCGTGGGCTTCTGCACT
GAGGTGGAAGAGGACCTCATCGATGCCGTCACGGGGCTCAGTGGCAGCGGGCCTGCCTAT
GCATTCATGGCTCTGGACGCATTGGCTGATGGTGGGGTGAAGATGGGTTTGCCACGGCGC
CTGGCAATCCAACTCGGGGCCCAGGCTTTGCTGGGAGCTGCCAAGATGCTGCTGGACTCG
GAGCAGCATCCATGCCAGCTTAAGGACAATGTCTGCTCCCCTGGGGGAGCCACCATCCAC
GCCCTGCACTTTCTAGAGAGTGGGGGCTTCCGCTCTCTGCTCATCAATGCAGTTGAGGCC
TCCTGTATCCGAACACGAGAGCTACAGTCCATGGCCGACCAAGAAAAGATCTCCCCAGCT
GCCCTTAAGAAGACCCTCTTAGACAGAGTGAAGCTGGAATCCCCCACAGTCTCCACACTG
ACCCCCTCCAGCCCAGGGAAGCTCCTCACAAGAAGCCTGGCCCTGGGAGGCAAGAAGGAC
TAA
Enzyme 2 GenBank Gene ID AF087859 Link Image
Enzyme 2 GeneCard ID PYCR2 Link Image
Enzyme 2 GenAtlas ID PYCR2 Link Image
Enzyme 2 HGNC ID HGNC:30262 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 1q42.12
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. 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]
  2. 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]
  3. 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]
  4. 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]
  5. 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 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 7521
Enzyme 3 Name Proline dehydrogenase, mitochondrial
Enzyme 3 Synonyms
  1. Proline oxidase
  2. Proline oxidase 2
  3. p53-induced gene 6 protein
Enzyme 3 Gene Name PRODH
Enzyme 3 Protein Sequence >Proline dehydrogenase, mitochondrial
MLEFVMREWKKSRKLLGQRLFNKLMKMTFYGHFVAGEDQESIQPLLRHYRAFGVSAILDY
GVEEDLSPEEAEHKEMESCTSAAERDGSGTNKRDKQYQAHRAFGDRRNGVISARTYFYAN
EAKCDSHMETFLRCIEASGRVSDDGFIAIKLTALGRPQFLLQFSEVLAKWRCFFHQMAVE
QGQAGLAAMDTKLEVAVLQESVAKLGIASRAEIEDWFTAETLGVSGTMDLLDWSSLIDSR
TKLSKHLVVPNAQTGQLEPLLSRFTEEEELQMTRMLQRMDVLAKKATEMGVRLMVDAEQT
YFQPAISRLTLEMQRKFNVEKPLIFNTYQCYLKDAYDNVTLDVELARREGWCFGAKLVRG
AYLAQERARAAEIGYEDPINPTYEATNAMYHRCLDYVLEELKHNAKAKVMVASHNEDTVR
FALRRMEELGLHPADHQVYFGQLLGMCDQISFPLGQAGYPVYKYVPYGPVMEVLPYLSRR
ALENSSLMKGTHRERQLLWLELLRRLRTGNLFHRPA
Enzyme 3 Number of Residues 516
Enzyme 3 Molecular Weight 59230.4
Enzyme 3 Theoretical pI 6.88
Enzyme 3 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH group of donors
  • proline dehydrogenase activity
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • glutamate biosynthetic process
  • glutamate metabolic process
  • glutamine family amino acid metabolic process
  • metabolic process
  • oxidation reduction
  • proline catabolic process
  • proline metabolic process
Component
Enzyme 3 General Function Involved in proline dehydrogenase activity
Enzyme 3 Specific Function Converts proline to delta-1-pyrroline-5-carboxylate
Enzyme 3 Pathways
Enzyme 3 Reactions
  • L-proline + acceptor = (S)-1-pyrroline-5-carboxylate + reduced acceptor [RN:R01253]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 2677802 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID O43272 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name PROD_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1551 bp
ATGCTGGAATTTGTGATGAGAGAGTGGAAAAAATCCAGGAAACTTCTAGGACAGAGGCTA
TTCAACAAGCTCATGAAGATGACCTTCTATGGGCATTTTGTAGCCGGGGAGGACCAGGAG
TCCATCCAGCCCCTGCTTCGGCACTACAGGGCCTTCGGTGTCAGCGCCATCCTGGACTAT
GGAGTGGAGGAGGACCTGAGCCCCGAGGAGGCAGAGCACAAGGAGATGGAGTCCTGCTCC
TCGGCTGCGGAGAGGGATGGCAGTGGCACGAATAAGCGGGACAAGCAATACCAGGCCCAC
CGGGCTTTCGGGGACCGCAGGAATGGTGTCATCAGTGCCCGCACCTACTTCTACGCCAAT
GAGGCCAAGTGCGACAGCCACATGGAGACATTCTTGCGCTGCATCGAAGCCTCAGGTAGA
GTCAGCGATGACGGCTTCATAGCCATTAAGCTCACAGCACTGGGGAGACCCCAGTTTCTG
CTGCAGTTCTCAGAGGTGCTGGCCAAGTGGAGGTGCTTCTTTCACCAAATGGCTGTGGAG
CAAGGGCAGGCGGGCCTGGCTGCCATGGACACCAAGCTGGAGGTGGCGGTGCTGCAGGAA
AGTGTCGCAAAGTTGGGCATCGCATCCAGGGCTGAGATTGAGGACTGGTTCACGGCAGAG
ACCCTGGGAGTGTCTGGCACCATGGACCTGCTGGACTGGAGCAGCCTCATCGACAGCAGG
ACCAAGCTGTCCAAGCACCTGGTAGTCCCCAACGCACAGACAGGACAGCTGGAGCCCCTG
CTGTCCCGGTTCACTGAGGAGGAGGAGCTACAGATGACCAGGATGCTACAGCGGATGGAT
GTCCTGGCCAAGAAAGCCACAGAGATGGGCGTGCGGCTGATGGTGGATGCCGAGCAGACC
TACTTCCAGCCGGCCATCAGCCGCCTGACGCTGGAGATGCAGCGGAAGTTCAATGTGGAG
AAGCCGCTCATCTTCAACACATACCAGTGCTACCTCAAGGATGCCTATGACAATGTGACC
CTGGACGTGGAGCTGGCTCGCCGTGAGGGCTGGTGTTTTGGGGCCAAGCTGGTGCGGGGC
GCATACCTGGCCCAGGAGCGAGCCCGTGCGGCAGAGATCGGCTATGAGGACCCCATCAAC
CCCACGTACGAGGCCACCAACGCCATGTACCACAGGTGCCTGGACTACGTGTTGGAGGAG
CTGAAGCACAACGCCAAGGCCAAGGTGATGGTGGCCTCCCACAATGAGGACACAGTGCGC
TTCGCACTGCGCAGGATGGAGGAGCTGGGCCTGCATCCTGCTGACCACCAGGTGTACTTT
GGACAGCTGCTAGGCATGTGTGACCAGATCAGCTTCCCGCTGGGCCAGGCCGGCTACCCC
GTGTACAAGTACGTGCCCTATGGCCCCGTGATGGAGGTGCTGCCCTACTTGTCCCGCCGT
GCCCTGGAGAACAGCAGCCTCATGAAGGGCACCCATCGGGAGCGGCAGTTGCTGTGGCTG
GAGCTCTTGAGGCGGCTCCGAACTGGCAACCTCTTCCATCGCCCTGCCTAG
Enzyme 3 GenBank Gene ID U82381 Link Image
Enzyme 3 GeneCard ID PRODH Link Image
Enzyme 3 GenAtlas ID PRODH Link Image
Enzyme 3 HGNC ID HGNC:9453 Link Image
Enzyme 3 Chromosome Location 2
Enzyme 3 Locus 22q11.21
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Campbell HD, Webb GC, Young IG: A human homologue of the Drosophila melanogaster sluggish-A (proline oxidase) gene maps to 22q11.2, and is a candidate gene for type-I hyperprolinaemia. Hum Genet. 1997 Nov;101(1):69-74. [PubMed Link Image]
  2. Gogos JA, Santha M, Takacs Z, Beck KD, Luine V, Lucas LR, Nadler JV, Karayiorgou M: The gene encoding proline dehydrogenase modulates sensorimotor gating in mice. Nat Genet. 1999 Apr;21(4):434-9. [PubMed Link Image]
  3. Bender HU, Almashanu S, Steel G, Hu CA, Lin WW, Willis A, Pulver A, Valle D: Functional consequences of PRODH missense mutations. Am J Hum Genet. 2005 Mar;76(3):409-20. Epub 2005 Jan 20. [PubMed Link Image]
  4. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
  5. 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]
  6. Polyak K, Xia Y, Zweier JL, Kinzler KW, Vogelstein B: A model for p53-induced apoptosis. Nature. 1997 Sep 18;389(6648):300-5. [PubMed Link Image]
  7. Jacquet H, Raux G, Thibaut F, Hecketsweiler B, Houy E, Demilly C, Haouzir S, Allio G, Fouldrin G, Drouin V, Bou J, Petit M, Campion D, Frebourg T: PRODH mutations and hyperprolinemia in a subset of schizophrenic patients. Hum Mol Genet. 2002 Sep 15;11(19):2243-9. [PubMed Link Image]
  8. Liu H, Heath SC, Sobin C, Roos JL, Galke BL, Blundell ML, Lenane M, Robertson B, Wijsman EM, Rapoport JL, Gogos JA, Karayiorgou M: Genetic variation at the 22q11 PRODH2/DGCR6 locus presents an unusual pattern and increases susceptibility to schizophrenia. Proc Natl Acad Sci U S A. 2002 Mar 19;99(6):3717-22. Epub 2002 Mar 12. [PubMed Link Image]
  9. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
  10. Raux G, Bumsel E, Hecketsweiler B, van Amelsvoort T, Zinkstok J, Manouvrier-Hanu S, Fantini C, Breviere GM, Di Rosa G, Pustorino G, Vogels A, Swillen A, Legallic S, Bou J, Opolczynski G, Drouin-Garraud V, Lemarchand M, Philip N, Gerard-Desplanches A, Carlier M, Philippe A, Nolen MC, Heron D, Sarda P, Lacombe D, Coizet C, Alembik Y, Layet V, Afenjar A, Hannequin D, Demily C, Petit M, Thibaut F, Frebourg T, Campion D: Involvement of hyperprolinemia in cognitive and psychiatric features of the 22q11 deletion syndrome. Hum Mol Genet. 2007 Jan 1;16(1):83-91. Epub 2006 Nov 29. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 12995
Enzyme 4 Name cDNA FLJ75752, highly similar to Homo sapiens pyrroline-5-carboxylate reductase family, member 2
Enzyme 4 Synonyms
  1. PYCR2, mRNA
  2. Pyrroline-5-carboxylate reductase family, member 2, isoform CRA_b
Enzyme 4 Gene Name PYCR2
Enzyme 4 Protein Sequence >cDNA FLJ75752, highly similar to Homo sapiens pyrroline-5-carboxylate reductase family, member 2
MSVGFIGAGQLAYALARGFTAAGILSAHKIIASSPEMNLPTVSALRKMGVNLTRSNKETV
KHSDVLFLAVKPHIIPFILDEIGADVQARHIVVSCAAGVTISSVEKKLMAFQPAPKVIRC
MTNTPVVVQEGATVYATGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAY
AFMALDALADGGVKMGLPRRLAIQLGAQALLGAAKMLLDSEQHPCQLKDNVCSPGGATIH
ALHFLESGGFRSLLINAVEASCIRTRELQSMADQEKISPAALKKTLLDRVKLESPTVSTL
TPSSPGKLLTRSLALGGKKD
Enzyme 4 Number of Residues 320
Enzyme 4 Molecular Weight 33638
Enzyme 4 Theoretical pI 7.87
Enzyme 4 GO Classification Not Available
Enzyme 4 General Function Amino acid transport and metabolism
Enzyme 4 Specific Function Not Available
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function Not Available
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 158257258 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID A8K798 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name A8K798_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence Not Available
Enzyme 4 GenBank Gene ID AK291913 Link Image
Enzyme 4 GeneCard ID A8K798 Link Image
Enzyme 4 GenAtlas ID Not Available
Enzyme 4 HGNC ID Not Available
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References Not Available
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 12996
Enzyme 5 Name Uncharacterized protein PRODH
Enzyme 5 Synonyms Not Available
Enzyme 5 Gene Name PRODH
Enzyme 5 Protein Sequence >Uncharacterized protein PRODH
RHGSEARPARAAPLHSPLRPAVHGAGLPRAARSGPSGRARRWVGHGSAAAGARRGLRQRA
GGVPQPANLGAGAEPAGAALVRLARAAGAPRAAAVCFQETSRTEAIQQAHEDDLLWAFCS
RGGESIQPLLRHYRAFGVSAILDYGVEEDLSPEEAEHKEMESCTSAAERDGSGTNKRDKQ
YQAHWAFGDRRNGVISARTYFYANEAKCDSHMETFLRCIEASGRVSDDGFIAIKLTALGR
PQFLLQFSEVLAKWRCFFHQMAVEQGQAGLAAMDTKLEVAVLQESVAKLGIASRAEIEDW
FTAETLGVSGTMDLLDWSSLIDSRTKLSKHLVVPNAQTGQLEPLLSRFTEEEELQMTRML
QRMDVLAKKATEMGVRLMVDAEQTYFQPAISRLTLEMQRKFNVEKPLIFNTYQPHPADAY
DNVTLDVELARREGWCFGAKLVRGAYLAQERARAAEIGYEDPINPTYEATNAMYHRCLDY
VLEELKHNAKAKVMVASHNEDTVRFALRRMEELGLHPADHRVYFGQLLGMCDQISFPLGQ
AGYPVYKYVPYGPVMEVLPYLSRRALENSSLMKGTHRERQLLWLELLRRLRTGNLFHRPA
Enzyme 5 Number of Residues 600
Enzyme 5 Molecular Weight 66921
Enzyme 5 Theoretical pI 8.01
Enzyme 5 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH group of donors
  • proline dehydrogenase activity
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • cellular metabolism
  • glutamate biosynthesis
  • glutamate metabolism
  • glutamine family amino acid metabolism
  • metabolism
  • physiological process
  • proline catabolism
  • proline metabolism
Component
Enzyme 5 General Function Amino acid transport and metabolism
Enzyme 5 Specific Function Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein Not Available
Enzyme 5 UniProtKB/Swiss-Prot ID A6NF53 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name A6NF53_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence Not Available
Enzyme 5 GenBank Gene ID AC007326 Link Image
Enzyme 5 GeneCard ID A6NF53 Link Image
Enzyme 5 GenAtlas ID PRODH Link Image
Enzyme 5 HGNC ID HGNC:9453 Link Image
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 12997
Enzyme 6 Name Melastatin 1 splicing variant
Enzyme 6 Synonyms Not Available
Enzyme 6 Gene Name MLSN1
Enzyme 6 Protein Sequence >Melastatin 1 splicing variant
MYIRVSYDTKPDSLLHLMVKDWQLELPKLLISVHGGLQNFEMQPKLKQVFGKGLIKAAMT
TGAWIFTGGVSTGVISHVGDALKDHSSKSRGRVCAIGIAPWGIVENKEDLVGKDVTRVYQ
TMSNPLSKLSVLNNSHTHFILADNGTLGKYGAEVKLRRLLEKHISLQKINTRLGQGVPLV
GLVVEGGPNVVSIVLEYLQEEPPIPVVICDGSGRASDILSFAHKYCEEGG
Enzyme 6 Number of Residues 230
Enzyme 6 Molecular Weight 25053
Enzyme 6 Theoretical pI 8.79
Enzyme 6 GO Classification Not Available
Enzyme 6 General Function Not Available
Enzyme 6 Specific Function Not Available
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function Not Available
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 33235690 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q7Z4N3 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name Q7Z4N3_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence Not Available
Enzyme 6 GenBank Gene ID AB115500 Link Image
Enzyme 6 GeneCard ID Q7Z4N3 Link Image
Enzyme 6 GenAtlas ID TRPM1 Link Image
Enzyme 6 HGNC ID HGNC:7146 Link Image
Enzyme 6 Chromosome Location Not Available
Enzyme 6 Locus Not Available
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References Not Available
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 13791
Enzyme 7 Name Transient receptor potential cation channel subfamily M member 1
Enzyme 7 Synonyms
  1. Long transient receptor potential channel 1
  2. LTrpC1
  3. Melastatin-1
Enzyme 7 Gene Name TRPM1
Enzyme 7 Protein Sequence >Transient receptor potential cation channel subfamily M member 1
MKDSNRCCCGQFTNQHIPPLPSATPSKNEEESKQVETQPEKWSVAKHTQSYPTDSYGVLE
FQGGGYSNKAMYIRVSYDTKPDSLLHLMVKDWQLELPKLLISVHGGLQNFEMQPKLKQVF
GKGLIKAAMTTGAWIFTGGVSTGVISHVGDALKDHSSKSRGRVCAIGIAPWGIVENKEDL
VGKDVTRVYQTMSNPLSKLSVLNNSHTHFILADNGTLGKYGAEVKLRRLLEKHISLQKIN
TRLGQGVPLVGLVVEGGPNVVSIVLEYLQEEPPIPVVICDGSGRASDILSFAHKYCEEGG
IINESLREQLLVTIQKTFNYNKAQSHQLFAIIMECMKKKELVTVFRMGSEGQQDIEMAIL
TALLKGTNVSAPDQLSLALAWNRVDIARSQIFVFGPHWPPLGSLAPPTDSKATEKEKKPP
MATTKGGRGKGKGKKKGKVKEEVEEETDPRKIELLNWVNALEQAMLDALVLDRVDFVKLL
IENGVNMQHFLTIPRLEELYNTRLGPPNTLHLLVRDVKKSNLPPDYHISLIDIGLVLEYL
MGGAYRCNYTRKNFRTLYNNLFGPKRPKALKLLGMEDDEPPAKGKKKKKKKKEEEIDIDV
DDPAVSRFQYPFHELMVWAVLMKRQKMAVFLWQRGEESMAKALVACKLYKAMAHESSESD
LVDDISQDLDNNSKDFGQLALELLDQSYKHDEQIAMKLLTYELKNWSNSTCLKLAVAAKH
RDFIAHTCSQMLLTDMWMGRLRMRKNPGLKVIMGILLPPTILFLEFRTYDDFSYQTSKEN
EDGKEKEEENTDANADAGSRKGDEENEHKKQRSIPIGTKICEFYNAPIVKFWFYTISYLG
YLLLFNYVILVRMDGWPSLQEWIVISYIVSLALEKIREILMSEPGKLSQKIKVWLQEYWN
ITDLVAISTFMIGAILRLQNQPYMGYGRVIYCVDIIFWYIRVLDIFGVNKYLGPYVMMIG
KMMIDMLYFVVIMLVVLMSFGVARQAILHPEEKPSWKLARNIFYMPYWMIYGEVFADQID
LYAMEINPPCGENLYDEEGKRLPPCIPGAWLTPALMACYLLVANILLVNLLIAVFNNTFF
EVKSISNQVWKFQRYQLIMTFHDRPVLPPPMIILSHIYIIIMRLSGRCRKKREGDQEERD
RGLKLFLSDEELKRLHEFEEQCVQEHFREKEDEQQSSSDERIRVTSERVENMSMRLEEIN
ERETFMKTSLQTVDLRLAQLEELSNRMVNALENLAGIDRSDLIQARSRASSECEATYLLR
QSSINSADGYSLYRYHFNGEELLFEDTSLSTSPGTGVRKKTCSFRIKEEKDVKTHLVPEC
QNSLHLSLGTSTSATPDGSHLAVDDLKNAEESKLGPDIGISKEDDERQTDSKKEETISPS
LNKTDVIHGQDKSDVQNTQLTVETTNIEGTISYPLEETKITRYFPDETINACKTMKSRSF
VYSRGRKLVGGVNQDVEYSSITDQQLTTEWQCQVQKITRSHSTDIPYIVSEAAVQAEHKE
QFADMQDEHHVAEAIPRIPRLSLTITDRNGMENLLSVKPDQTLGFPSLRSKSLHGHPRNV
KSIQGKLDRSGHASSVSSLVIVSGMTAEEKKVKKEKASTETEC
Enzyme 7 Number of Residues 1603
Enzyme 7 Molecular Weight 182177.0
Enzyme 7 Theoretical pI 6.82
Enzyme 7 GO Classification
Function
  • ion channel activity
  • ion transmembrane transporter activity
  • substrate-specific transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • establishment of localization
  • ion transport
  • transmembrane transport
  • transport
Component
  • cell part
  • membrane
Enzyme 7 General Function Involved in ion channel activity
Enzyme 7 Specific Function Cation channel essential for the depolarizing photoresponse of retinal ON bipolar cells. It is part of the GRM6 signaling cascade. May play a role in metastasis suppression. May act as a spontaneously active, calcium-permeable plasma membrane channel
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • 525-545 746-766 831-851 853-873 898-918 929-949 962-982 1055-1075 1106-1126
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 94538366 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q7Z4N2 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name TRPM1_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >4812 bp
ATGAAAGACTCTAACAGGTGTTGCTGTGGCCAGTTCACCAACCAGCATATCCCCCCTCTG
CCAAGTGCAACACCCAGCAAAAATGAAGAGGAAAGCAAACAGGTGGAGACTCAGCCTGAG
AAATGGTCTGTTGCCAAGCACACCCAGAGCTACCCAACAGATTCCTATGGAGTTCTTGAA
TTCCAGGGTGGCGGATATTCCAATAAAGCCATGTATATCCGTGTATCCTATGACACCAAG
CCAGACTCACTGCTCCATCTCATGGTGAAAGATTGGCAGCTGGAACTCCCCAAGCTCTTA
ATATCTGTGCATGGAGGCCTCCAGAACTTTGAGATGCAGCCCAAGCTGAAACAAGTCTTT
GGGAAAGGCCTGATCAAGGCTGCTATGACCACCGGGGCCTGGATCTTCACCGGGGGTGTC
AGCACAGGTGTTATCAGCCACGTAGGGGATGCCTTGAAAGACCACTCCTCCAAGTCCAGA
GGCCGGGTTTGTGCTATAGGAATTGCTCCATGGGGCATCGTGGAGAATAAGGAAGACCTG
GTTGGAAAGGATGTAACAAGAGTGTACCAGACCATGTCCAACCCTCTAAGTAAGCTCTCT
GTGCTCAACAACTCCCACACCCACTTCATCCTGGCTGACAATGGCACCCTGGGCAAGTAT
GGCGCCGAGGTGAAGCTGCGAAGGCTGCTGGAAAAGCACATCTCCCTGCAGAAGATCAAC
ACAAGACTGGGGCAGGGCGTGCCCCTCGTGGGTCTCGTGGTGGAGGGGGGCCCTAACGTG
GTGTCCATCGTCTTGGAATACCTGCAAGAAGAGCCTCCCATCCCTGTGGTGATTTGTGAT
GGCAGCGGACGTGCCTCGGACATCCTGTCCTTTGCGCACAAGTACTGTGAAGAAGGCGGA
ATAATAAATGAGTCCCTCAGGGAGCAGCTTCTAGTTACCATTCAGAAAACATTTAATTAT
AATAAGGCACAATCACATCAGCTGTTTGCAATTATAATGGAGTGCATGAAGAAGAAAGAA
CTCGTCACTGTGTTCAGAATGGGTTCTGAGGGCCAGCAGGACATCGAGATGGCAATTTTA
ACTGCCCTGCTGAAAGGAACAAACGTATCTGCTCCAGATCAGCTGAGCTTGGCACTGGCT
TGGAACCGCGTGGACATAGCACGAAGCCAGATCTTTGTCTTTGGGCCCCACTGGCCGCCC
CTGGGAAGCCTGGCACCCCCGACGGACAGCAAAGCCACGGAGAAGGAGAAGAAGCCACCC
ATGGCCACCACCAAGGGAGGAAGAGGAAAAGGGAAAGGCAAGAAGAAAGGGAAAGTGAAA
GAGGAAGTGGAGGAAGAAACTGACCCCCGGAAGATAGAGCTGCTGAACTGGGTGAATGCT
TTGGAGCAAGCGATGCTAGATGCTTTAGTCTTAGATCGTGTCGACTTTGTGAAGCTCCTG
ATTGAAAACGGAGTGAACATGCAACACTTTCTGACCATTCCGAGGCTGGAGGAGCTTTAT
AACACAAGACTGGGTCCACCAAACACACTTCATCTGCTGGTGAGGGATGTGAAAAAGAGC
AACCTTCCGCCTGATTACCACATCAGCCTCATAGACATCGGGCTCGTGCTGGAGTACCTC
ATGGGAGGAGCCTACCGCTGCAACTACACTCGGAAAAACTTTCGGACCCTTTACAACAAC
TTGTTTGGACCAAAGAGGCCTAAAGCTCTTAAACTTCTGGGAATGGAAGATGATGAGCCT
CCAGCTAAAGGGAAGAAAAAGAAAAAGAAGAAAAAGGAGGAAGAGATCGACATTGATGTG
GACGACCCTGCCGTGAGTCGGTTCCAGTATCCCTTCCACGAGCTGATGGTGTGGGCAGTG
CTGATGAAACGCCAGAAAATGGCAGTGTTCCTCTGGCAGCGAGGGGAAGAGAGCATGGCC
AAGGCCCTGGTGGCCTGCAAGCTCTACAAGGCCATGGCCCACGAGTCCTCCGAGAGTGAT
CTGGTGGATGACATCTCCCAGGACTTGGATAACAATTCCAAAGACTTCGGCCAGCTTGCT
TTGGAGTTATTAGACCAGTCCTATAAGCATGACGAGCAGATCGCTATGAAACTCCTGACC
TACGAGCTGAAAAACTGGAGCAACTCGACCTGCCTCAAACTGGCCGTGGCAGCCAAACAC
CGGGACTTCATTGCTCACACCTGCAGCCAGATGCTGCTGACCGATATGTGGATGGGAAGA
CTGCGGATGCGGAAGAACCCCGGCCTGAAGGTTATCATGGGGATTCTTCTACCCCCCACC
ATCTTGTTTTTGGAATTTCGCACATATGATGATTTCTCGTATCAAACATCCAAGGAAAAT
GAGGATGGCAAAGAAAAAGAAGAGGAAAATACGGATGCAAATGCAGATGCTGGCTCAAGA
AAGGGGGATGAGGAGAACGAGCACAAAAAACAGAGAAGTATTCCCATCGGAACAAAGATC
TGTGAATTCTATAACGCGCCCATTGTCAAGTTCTGGTTTTACACAATATCATACTTGGGC
TACCTGCTGCTGTTTAACTACGTCATCCTGGTGCGGATGGATGGCTGGCCGTCCCTCCAG
GAGTGGATCGTCATCTCCTACATCGTGAGCCTGGCGTTAGAGAAGATACGAGAGATCCTC
ATGTCAGAACCAGGCAAACTCAGCCAGAAAATCAAAGTTTGGCTTCAGGAGTACTGGAAC
ATCACAGATCTCGTGGCCATTTCCACATTCATGATTGGAGCAATTCTTCGCCTACAGAAC
CAGCCCTACATGGGCTATGGCCGGGTGATCTACTGTGTGGATATCATCTTCTGGTACATC
CGTGTCCTGGACATCTTTGGTGTCAACAAGTATCTGGGGCCATACGTGATGATGATTGGA
AAGATGATGATCGACATGCTGTACTTTGTGGTCATCATGCTGGTCGTGCTCATGAGTTTC
GGAGTAGCCCGTCAAGCCATTCTGCATCCAGAGGAGAAGCCCTCTTGGAAACTGGCCCGA
AACATCTTCTACATGCCCTACTGGATGATCTATGGAGAGGTGTTTGCAGACCAGATAGAC
CTCTACGCCATGGAAATTAATCCTCCTTGTGGTGAGAACCTATATGATGAGGAGGGCAAG
CGGCTTCCTCCCTGTATCCCCGGCGCCTGGCTCACTCCAGCACTCATGGCGTGCTATCTA
CTGGTCGCCAACATCCTGCTGGTGAACCTGCTGATTGCTGTGTTCAACAATACCTTCTTT
GAAGTAAAATCAATATCCAACCAGGTGTGGAAGTTCCAGCGATATCAGCTGATTATGACA
TTTCATGACAGGCCAGTCCTGCCCCCACCGATGATCATTTTAAGCCACATCTACATCATC
ATTATGCGTCTCAGCGGCCGCTGCAGGAAAAAGAGAGAAGGGGACCAAGAGGAACGGGAT
CGTGGATTGAAGCTCTTCCTTAGCGACGAGGAGCTAAAGAGGCTGCATGAGTTCGAGGAG
CAGTGCGTGCAGGAGCACTTCCGGGAGAAGGAGGATGAGCAGCAGTCGTCCAGCGACGAG
CGCATCCGGGTCACTTCTGAAAGAGTTGAAAATATGTCAATGAGGTTGGAAGAAATCAAT
GAAAGAGAAACTTTTATGAAAACTTCCCTGCAGACTGTTGACCTTCGACTTGCTCAGCTA
GAAGAATTATCTAACAGAATGGTGAATGCTCTTGAAAATCTTGCGGGAATCGACAGGTCT
GACCTGATCCAGGCACGGTCCCGGGCTTCTTCTGAATGTGAGGCAACGTATCTTCTCCGG
CAAAGCAGCATCAATAGCGCTGATGGCTACAGCTTGTATCGATATCATTTTAACGGAGAA
GAGTTATTATTTGAGGATACATCTCTCTCCACGTCACCAGGGACAGGAGTCAGGAAAAAA
ACCTGTTCCTTCCGTATAAAGGAAGAGAAGGACGTGAAAACGCACCTAGTCCCAGAATGT
CAGAACAGTCTTCACCTTTCACTGGGCACAAGCACATCAGCAACCCCAGATGGCAGTCAC
CTTGCAGTAGATGACTTAAAGAACGCTGAAGAGTCAAAATTAGGTCCAGATATTGGGATT
TCAAAGGAAGATGATGAAAGACAGACAGACTCTAAAAAAGAAGAAACTATTTCCCCAAGT
TTAAATAAAACAGATGTGATACATGGACAGGACAAATCAGATGTTCAAAACACTCAGCTA
ACAGTGGAAACGACAAATATAGAAGGCACTATTTCCTATCCCCTGGAAGAAACCAAAATT
ACACGCTATTTCCCCGATGAAACGATCAATGCTTGTAAAACAATGAAGTCCAGAAGCTTC
GTCTATTCCCGGGGAAGAAAGCTGGTCGGTGGGGTTAACCAGGATGTAGAGTACAGTTCA
ATCACGGACCAGCAATTGACGACGGAATGGCAATGCCAAGTTCAAAAGATCACGCGCTCT
CATAGCACAGATATTCCTTACATTGTGTCGGAAGCTGCAGTGCAAGCTGAGCATAAAGAG
CAGTTTGCAGATATGCAAGATGAACACCATGTCGCTGAAGCAATTCCTCGAATCCCTCGC
TTGTCCCTAACCATTACTGACAGAAATGGGATGGAAAACTTACTGTCTGTGAAGCCAGAT
CAAACTTTGGGATTCCCATCTCTCAGGTCAAAAAGTTTACATGGACATCCTAGGAATGTG
AAATCCATTCAGGGAAAGTTAGACAGATCTGGACATGCCAGTAGTGTAAGCAGCTTAGTA
ATTGTGTCTGGAATGACAGCAGAAGAAAAAAAGGTTAAGAAAGAGAAAGCTTCCACAGAA
ACTGAATGCTAG
Enzyme 7 GenBank Gene ID NM_002420.4 Link Image
Enzyme 7 GeneCard ID TRPM1 Link Image
Enzyme 7 GenAtlas ID TRPM1 Link Image
Enzyme 7 HGNC ID HGNC:7146 Link Image
Enzyme 7 Chromosome Location 1
Enzyme 7 Locus 15q13.3
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Hunter JJ, Shao J, Smutko JS, Dussault BJ, Nagle DL, Woolf EA, Holmgren LM, Moore KJ, Shyjan AW: Chromosomal localization and genomic characterization of the mouse melastatin gene (Mlsn1). Genomics. 1998 Nov 15;54(1):116-23. [PubMed Link Image]
  2. Zody MC, Garber M, Sharpe T, Young SK, Rowen L, O'Neill K, Whittaker CA, Kamal M, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Kodira CD, Madan A, Qin S, Yang X, Abbasi N, Abouelleil A, Arachchi HM, Baradarani L, Birditt B, Bloom S, Bloom T, Borowsky ML, Burke J, Butler J, Cook A, DeArellano K, DeCaprio D, Dorris L 3rd, Dors M, Eichler EE, Engels R, Fahey J, Fleetwood P, Friedman C, Gearin G, Hall JL, Hensley G, Johnson E, Jones C, Kamat A, Kaur A, Locke DP, Madan A, Munson G, Jaffe DB, Lui A, Macdonald P, Mauceli E, Naylor JW, Nesbitt R, Nicol R, O'Leary SB, Ratcliffe A, Rounsley S, She X, Sneddon KM, Stewart S, Sougnez C, Stone SM, Topham K, Vincent D, Wang S, Zimmer AR, Birren BW, Hood L, Lander ES, Nusbaum C: Analysis of the DNA sequence and duplication history of human chromosome 15. Nature. 2006 Mar 30;440(7084):671-5. [PubMed Link Image]
  3. Duncan LM, Deeds J, Hunter J, Shao J, Holmgren LM, Woolf EA, Tepper RI, Shyjan AW: Down-regulation of the novel gene melastatin correlates with potential for melanoma metastasis. Cancer Res. 1998 Apr 1;58(7):1515-20. [PubMed Link Image]
  4. Fang D, Setaluri V: Expression and Up-regulation of alternatively spliced transcripts of melastatin, a melanoma metastasis-related gene, in human melanoma cells. Biochem Biophys Res Commun. 2000 Dec 9;279(1):53-61. [PubMed Link Image]
  5. Xu XZ, Moebius F, Gill DL, Montell C: Regulation of melastatin, a TRP-related protein, through interaction with a cytoplasmic isoform. Proc Natl Acad Sci U S A. 2001 Sep 11;98(19):10692-7. Epub 2001 Sep 4. [PubMed Link Image]
  6. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  7. Li Z, Sergouniotis PI, Michaelides M, Mackay DS, Wright GA, Devery S, Moore AT, Holder GE, Robson AG, Webster AR: Recessive mutations of the gene TRPM1 abrogate ON bipolar cell function and cause complete congenital stationary night blindness in humans. Am J Hum Genet. 2009 Nov;85(5):711-9. Epub 2009 Oct 29. [PubMed Link Image]
  8. van Genderen MM, Bijveld MM, Claassen YB, Florijn RJ, Pearring JN, Meire FM, McCall MA, Riemslag FC, Gregg RG, Bergen AA, Kamermans M: Mutations in TRPM1 are a common cause of complete congenital stationary night blindness. Am J Hum Genet. 2009 Nov;85(5):730-6. Epub 2009 Nov 5. [PubMed Link Image]
  9. Audo I, Kohl S, Leroy BP, Munier FL, Guillonneau X, Mohand-Said S, Bujakowska K, Nandrot EF, Lorenz B, Preising M, Kellner U, Renner AB, Bernd A, Antonio A, Moskova-Doumanova V, Lancelot ME, Poloschek CM, Drumare I, Defoort-Dhellemmes S, Wissinger B, Leveillard T, Hamel CP, Schorderet DF, De Baere E, Berger W, Jacobson SG, Zrenner E, Sahel JA, Bhattacharya SS, Zeitz C: TRPM1 is mutated in patients with autosomal-recessive complete congenital stationary night blindness. Am J Hum Genet. 2009 Nov;85(5):720-9. Epub 2009 Nov 5. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available