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Human Metabolome Database Version 2.5

 

Showing metabocard for L-Proline (HMDB00162)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-07-06 14:30:00
Accession Number HMDB00162
Secondary Accession Numbers Not Available
Common Name L-Proline
Description L-Proline is one of the twenty amino acids used in living organisms as the building blocks of proteins. Proline is sometimes called an imino acid, although the IUPAC definition of an imine requires a carbon-nitrogen double bond. Proline is a non-essential amino acid that is synthesized from glutamic acid. It is an essential component of collagen and is important for proper functioning of joints and tendons.
Synonyms
  1. (-)-(S)-Proline
  2. (-)-2-Pyrrolidinecarboxylate
  3. (-)-2-Pyrrolidinecarboxylic acid
  4. (-)-Proline
  5. (S)-(-)-Proline
  6. (S)-(-)-Pyrrolidine-2-carboxylate
  7. (S)-(-)-Pyrrolidine-2-carboxylic acid
  8. (S)-2-Carboxypyrrolidine
  9. (S)-2-Pyrralidinecarboxylate
  10. (S)-2-Pyrralidinecarboxylic acid
  11. (S)-2-Pyrrolidinecarboxylate
  12. (S)-2-Pyrrolidinecarboxylic acid
  13. (S)-Proline
  14. 2-Pyrrolidinecarboxylate
  15. 2-Pyrrolidinecarboxylic acid
  16. Proline
Chemical IUPAC Name (2S)-pyrrolidine-2-carboxylic acid
Chemical Formula C5H9NO2
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 amine
  • secondary aliphatic amine (dialkylamine)
  • carboxylic acid
  • heterocyclic compound
  • alpha-aminoacid
Biofunction
  • Component of Arginine and proline metabolism
Application
Source
  • Endogenous
Average Molecular Weight 115.131
Monoisotopic Molecular Weight 115.063332
Isomeric SMILES OC(=O)[C@@H]1CCCN1
Canonical SMILES OC(=O)C1CCCN1
KEGG Compound ID C00148 Link Image
BioCyc ID PRO Link Image
BiGG ID 34042 Link Image
Wikipedia Link L-Proline Link Image
NuGOwiki Link HMDB00162 Link Image
Metagene Link HMDB00162 Link Image
METLIN ID 29 Link Image
PubChem Compound 145742 Link Image
PubChem Substance 841800 Link Image
ChEBI ID 17203 Link Image
CAS Registry Number 147-85-3
InChI Identifier InChI=1/C5H9NO2/c7-5(8)4-2-1-3-6-4/h4,6H,1-3H2,(H,7,8)/t4-/m0/s1
Synthesis Reference Itoh, Tamio. Synthesis of L-proline from L-glutamine. Bulletin of the Chemical Society of Japan (1963), 36(1), 25-9
Melting Point (Experimental) 221 oC
Experimental Water Solubility 162.0 mg/mL [MERCK INDEX (1996)] Source: PhysProp
Predicted Water Solubility 365.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity -2.54 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP/Hydrophobicity -2.71 [Predicted by ALOGPS]; -2.4 [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 Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
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 Show Image
Show Peaklist
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm
  • endoplasmic reticulum
  • Extracellular
  • lysosome
  • mitochondria
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Saliva
  • Urine
Tissue Location
Tissue References
All Tissues
Concentrations (Normal)
Biofluid Blood
Value 168.0 (108.0-228.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Cynober LA: Plasma amino acid levels with a note on membrane transport: characteristics, regulation, and metabolic significance. Nutrition. 2002 Sep;18(9):761-6. [PubMed Link Image]
Biofluid Blood
Value 198.0 +/- 63.0 uM
Age Children:1-13 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 92. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Blood
Value 239.0 +/- 70.0 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 92. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Blood
Value 168.0 +/- 49.0 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 92. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Blood
Value 230.0 +/- 75.0 uM
Age Newborn:0-30 days old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 92. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid CSF
Value 4.0 (0 - 8.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Humbertclaude V, Rivier F, Roubertie A, Echenne B, Bellet H, Vallat C, Morin D: Is hyperprolinemia type I actually a benign trait? Report of a case with severe neurologic involvement and vigabatrin intolerance. J Child Neurol. 2001 Aug;16(8):622-3. [PubMed Link Image]
Biofluid CSF
Value 1.9 +/- 1.0 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Mandal, R. et al. (in preparation)
Biofluid Saliva
Value >10 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Silwood CJ, Lynch E, Claxson AW, Grootveld MC: 1H and (13)C NMR spectroscopic analysis of human saliva. J Dent Res. 2002 Jun;81(6):422-7. [PubMed Link Image]
Biofluid Urine
Value 2.171 (0.0658-4.276) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Doctor's Data
Biofluid Urine
Value 1.0 (0.5-2.0) umol/mmol creatinine
Age Newborn:0-30 days old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Biofluid Urine
Value 4.14 +/- 2.85 umol/mmol creatinine
Age Infant:0-1 yr old
Sex Both
Patient information Normal
Comments Not Available
References
  • Shoemaker JD, Elliott WH: Automated screening of urine samples for carbohydrates, organic and amino acids after treatment with urease. J Chromatogr. 1991 Jan 2;562(1-2):125-38. [PubMed Link Image]
Biofluid Urine
Value 0.86 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 201.0 +/- 149.5 uM
Age Adult:>18 yrs old
Sex Both
Condition Hemodialysis
Comments Conventional: for 4 h, 3 times/week
References
  • Raj DS, Ouwendyk M, Francoeur R, Pierratos A: Plasma amino acid profile on nocturnal hemodialysis. Blood Purif. 2000;18(2):97-102. [PubMed Link Image]
Biofluid Blood
Value 227.2 +/- 108.4 uM
Age Adult:>18 yrs old
Sex Both
Condition Hemodialysis
Comments Nocturnal: for 8 h during the night, 6 times/week
References
  • Raj DS, Ouwendyk M, Francoeur R, Pierratos A: Plasma amino acid profile on nocturnal hemodialysis. Blood Purif. 2000;18(2):97-102. [PubMed Link Image]
Biofluid Blood
Value 263.00 (110.00-417.00) uM
Age Adult:>18 yrs old
Sex Both
Condition Glutathione synthetase deficiency
Comments Not Available
References
Biofluid CSF
Value 0.68 +/- 0.35 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 29.6 (19.7-39.47) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Iminoglycinuria
Comments Not Available
References
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]
Glutathione synthetase deficiency
Hemodialysis
  • Raj DS, Ouwendyk M, Francoeur R, Pierratos A: Plasma amino acid profile on nocturnal hemodialysis. Blood Purif. 2000;18(2):97-102. [PubMed Link Image]
Iminoglycinuria
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Arginine and Proline Metabolism SMP00020 Link Image map00330 Link Image
Transcription/Translation SMP00019 Link Image
General References
  1. Deng C, Shang C, Hu Y, Zhang X: Rapid diagnosis of phenylketonuria and other aminoacidemias by quantitative analysis of amino acids in neonatal blood spots by gas chromatography-mass spectrometry. J Chromatogr B Analyt Technol Biomed Life Sci. 2002 Jul 25;775(1):115-20. [PubMed Link Image]
  2. Azizi M, Junot C, Ezan E, Menard J: Angiotensin I-converting enzyme and metabolism of the haematological peptide N-acetyl-seryl-aspartyl-lysyl-proline. Clin Exp Pharmacol Physiol. 2001 Dec;28(12):1066-9. [PubMed Link Image]
  3. Roesel RA, Blankenship PR, Mobley EB, Coryell ME: Increased excretion of histidyl-L-proline diketopiperazine by infants receiving Pregestimil and Nutramigen formulas. Clin Chem. 1986 May;32(5):865-7. [PubMed Link Image]
  4. Chambers ST, Kunin CM: Osmoprotective activity for Escherichia coli in mammalian renal inner medulla and urine. Correlation of glycine and proline betaines and sorbitol with response to osmotic loads. J Clin Invest. 1987 Nov;80(5):1255-60. [PubMed Link Image]
  5. Cynober LA: Plasma amino acid levels with a note on membrane transport: characteristics, regulation, and metabolic significance. Nutrition. 2002 Sep;18(9):761-6. [PubMed Link Image]
  6. Azizi M, Ezan E, Reny JL, Wdzieczak-Bakala J, Gerineau V, Menard J: Renal and metabolic clearance of N-acetyl-seryl-aspartyl-lysyl-proline (AcSDKP) during angiotensin-converting enzyme inhibition in humans. Hypertension. 1999 Mar;33(3):879-86. [PubMed Link Image]
  7. Hart W, van den Hamer CJ, van der Sluys Veer J: The use of hydroxy-DL-proline-2-(14)C in the investigation of hydroxyproline metabolism in normal subjects and in patients with renal insufficiency. Clin Nephrol. 1976 Sep;6(3):379-87. [PubMed Link Image]
  8. Kanwar YS, Krakower CA, Manaligod JR, Justice P, Wong PW: Biochemical, morphological and hybrid studies in hyperprolinemic mice. Biomedicine. 1975 May;22(3):209-16. [PubMed Link Image]
  9. Simila S: Hydroxyproline metabolism in type II hyperprolinaemia. Ann Clin Biochem. 1979 Jul;16(4):177-81. [PubMed Link Image]
  10. Lu SH, Ohshima H, Fu HM, Tian Y, Li FM, Blettner M, Wahrendorf J, Bartsch H: Urinary excretion of N-nitrosamino acids and nitrate by inhabitants of high- and low-risk areas for esophageal cancer in Northern China: endogenous formation of nitrosoproline and its inhibition by vitamin C. Cancer Res. 1986 Mar;46(3):1485-91. [PubMed Link Image]
  11. Hausmann D: [Post-traumatic imbalances of plasma amino acids--interference factors or defense mechanisms? A study of protein metabolism in severe craniocerebral trauma] Anasth Intensivther Notfallmed. 1988 Feb;23(1):14-21. [PubMed Link Image]
  12. Scriver CR, McInnes RR, Mohyuddin F: Role of epithelial architecture and intracellular metabolism in proline uptake and transtubular reclamation in PRO/re mouse kidney. Proc Natl Acad Sci U S A. 1975 Apr;72(4):1431-5. [PubMed Link Image]
  13. Boden G, Rezvani I, Owen OE: Effects of glucagon on plasma amino acids. J Clin Invest. 1984 Mar;73(3):785-93. [PubMed Link Image]
  14. Silwood CJ, Lynch E, Claxson AW, Grootveld MC: 1H and (13)C NMR spectroscopic analysis of human saliva. J Dent Res. 2002 Jun;81(6):422-7. [PubMed Link Image]
  15. Feldman JM, Plonk JW, Admiraal J, Sidbury, JB: Plasma amino acids in patients with the carcinoid syndrome. Cancer. 1976 Nov;38(5):2127-31. [PubMed Link Image]
  16. Humbertclaude V, Rivier F, Roubertie A, Echenne B, Bellet H, Vallat C, Morin D: Is hyperprolinemia type I actually a benign trait? Report of a case with severe neurologic involvement and vigabatrin intolerance. J Child Neurol. 2001 Aug;16(8):622-3. [PubMed Link Image]
  17. Wikipedia Link Image
Metabolic Enzymes
  1. Prolyl 4-hydroxylase subunit alpha-2
  2. Pyrroline-5-carboxylate reductase 1, mitochondrial
  3. Prolyl 4-hydroxylase subunit alpha-1
  4. Pyrroline-5-carboxylate reductase 2
  5. Bifunctional aminoacyl-tRNA synthetase
  6. Cytosol aminopeptidase
  7. Proline dehydrogenase, mitochondrial
  8. Pyrroline-5-carboxylate reductase 3
  9. Sodium-dependent proline transporter
  10. cDNA FLJ75752, highly similar to Homo sapiens pyrroline-5-carboxylate reductase family, member 2
  11. Uncharacterized protein PRODH
  12. Melastatin 1 splicing variant
  13. Transient receptor potential cation channel subfamily M member 1
  14. Prolyl 3-hydroxylase 1
  15. Prolyl 3-hydroxylase 2
  16. Prolyl 3-hydroxylase 3
  17. Prolyl 4-hydroxylase subunit alpha-3
  18. Egl nine homolog 1
  19. Egl nine homolog 2
  20. Egl nine homolog 3
  21. Transmembrane prolyl 4-hydroxylase
  22. cDNA FLJ75964, highly similar to Homo sapiens prolyl-tRNA synthetase (mitochondrial)(putative) (PARS2), mRNA (Prolyl-tRNA synthetase (Mitochondrial)(Putative))
  23. Probable proline racemase
  24. Peptidyl-prolyl cis-trans isomerase F, mitochondrial
  25. Peptidyl-prolyl cis-trans isomerase A
  26. Peptidyl-prolyl cis-trans isomerase B
  27. Peptidyl-prolyl cis-trans isomerase G
  28. Probable prolyl-tRNA synthetase, mitochondrial
  29. Peptidyl-prolyl cis-trans isomerase H
Enzyme 1 [top]
Enzyme 1 ID 5537
Enzyme 1 Name Prolyl 4-hydroxylase subunit alpha-2
Enzyme 1 Synonyms
  1. 4-PH alpha-2
  2. Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-2
Enzyme 1 Gene Name P4HA2
Enzyme 1 Protein Sequence >Prolyl 4-hydroxylase subunit alpha-2
MKLWVSALLMAWFGVLSCVQAEFFTSIGHMTDLIYAEKELVQSLKEYILVEEAKLSKIKS
WANKMEALTSKSAADAEGYLAHPVNAYKLVKRLNTDWPALEDLVLQDSAAGFIANLSVQR
QFFPTDEDEIGAAKALMRLQDTYRLDPGTISRGELPGTKYQAMLSVDDCFGMGRSAYNEG
DYYHTVLWMEQVLKQLDAGEEATTTKSQVLDYLSYAVFQLGDLHRALELTRRLLSLDPSH
ERAGGNLRYFEQLLEEEREKTLTNQTEAELATPEGIYERPVDYLPERDVYESLCRGEGVK
LTPRRQKRLFCRYHHGNRAPQLLIAPFKEEDEWDSPHIVRYYDVMSDEEIERIKEIAKPK
LARATVRDPKTGVLTVASYRVSKSSWLEEDDDPVVARVNRRMQHITGLTVKTAELLQVAN
YGVGGQYEPHFDFSRNDERDTFKHLGTGNRVATFLNYMSDVEAGGATVFPDLGAAIWPKK
GTAVFWYNLLRSGEGDYRTRHAACPVLVGCKWVSNKWFHERGQEFLRPCGSTEVD
Enzyme 1 Number of Residues 535
Enzyme 1 Molecular Weight 60901.4
Enzyme 1 Theoretical pI 5.43
Enzyme 1 GO Classification
Function
  • L-ascorbic acid binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
  • oxidoreductase activity, acting on single donors with incorporation of molecular oxygen
  • oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
  • peptidyl-proline dioxygenase activity
  • procollagen-proline 4-dioxygenase activity
  • procollagen-proline dioxygenase activity
  • transition metal ion binding
  • vitamin binding
Process
  • metabolic process
  • oxidation reduction
Component
  • endoplasmic reticulum
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • organelle
Enzyme 1 General Function Involved in oxidoreductase activity
Enzyme 1 Specific Function Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins
Enzyme 1 Pathways
Enzyme 1 Reactions
  • procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2 [RN:R03219]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-21
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein Not Available
Enzyme 1 UniProtKB/Swiss-Prot ID O15460 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name P4HA2_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1608 bp
ATGAAACTCTGGGTGTCTGCATTGCTGATGGCCTGGTTTGGTGTCCTGAGCTGTGTGCAG
GCCGAATTCTTCACCTCTATTGGGCACATGACTGACCTGATTTATGCAGAGAAAGAGCTG
GTGCAGTCTCTGAAAGAGTACATCCTTGTGGAGGAAGCCAAGCTTTCCAAGATTAAGAGC
TGGGCCAACAAAATGGAAGCCTTGACTAGCAAGTCAGCTGCTGATGCTGAGGGCTACCTG
GCTCACCCTGTGAATGCCTACAAACTGGTGAAGCGGCTAAACACAGACTGGCCTGCGCTG
GAGGACCTTGTCCTGCAGGACTCAGCTGCAGGTTTTATCGCCAACCTCTCTGTGCAGCGG
CAGTTCTTCCCCACTGATGAGGACGAGATAGGAGCTGCCAAAGCCCTGATGAGACTTCAG
GACACATACAGGCTGGACCCAGGCACAATTTCCAGAGGGGAACTTCCAGGAACCAAGTAC
CAGGCAATGCTGAGTGTGGATGACTGCTTTGGGATGGGCCGCTCGGCCTACAATGAAGGG
GACTATTATCATACGGTGTTGTGGATGGAGCAGGTGCTAAAGCAGCTTGATGCCGGGGAG
GAGGCCACCACAACCAAGTCACAGGTGCTGGACTACCTCAGCTATGCTGTCTTCCAGTTG
GGTGATCTGCACCGTGCCCTGGAGCTCACCCGCCGCCTGCTCTCCCTTGACCCAAGCCAC
GAACGAGCTGGAGGGAATCTGCGGTACTTTGAGCAGTTATTGGAGGAAGAGAGAGAAAAA
ACGTTAACAAATCAGACAGAAGCTGAGCTAGCAACCCCAGAAGGCATCTATGAGAGGCCT
GTGGACTACCTGCCTGAGAGGGATGTTTACGAGAGCCTCTGTCGTGGGGAGGGTGTCAAA
CTGACACCCCGTAGACAGAAGAGGCTTTTCTGTAGGTACCACCATGGCAACAGGGCCCCA
CAGCTGCTCATTGCCCCCTTCAAAGAGGAGGACGAGTGGGACAGCCCGCACATCGTCAGG
TACTACGATGTCATGTCTGATGAGGAAATCGAGAGGATCAAGGAGATCGCAAAACCTAAA
CTTGCACGAGCCACCGTTCGTGATCCCAAGACAGGAGTCCTCACTGTCGCCAGCTACCGG
GTTTCCAAAAGCTCCTGGCTAGAGGAAGATGATGACCCTGTTGTGGCCCGAGTAAATCGT
CGGATGCAGCATATCACAGGGTTAACAGTAAAGACTGCAGAATTGTTACAGGTTGCAAAT
TATGGAGTGGGAGGACAGTATGAACCGCACTTCGACTTCTCTAGGAATGATGAGCGAGAT
ACTTTCAAGCATTTAGGGACGGGGAATCGTGTGGCTACTTTCTTAAACTACATGAGTGAT
GTAGAAGCTGGTGGTGCCACCGTCTTCCCTGATCTGGGGGCTGCAATTTGGCCTAAGAAG
GGTACAGCTGTGTTCTGGTACAACCTCTTGCGGAGCGGGGAAGGTGACTACCGAACAAGA
CATGCTGCCTGCCCTGTGCTTGTGGGCTGCAAGTGGGTCTCCAATAAGTGGTTCCATGAA
CGAGGACAGGAGTTCTTGAGACCTTGTGGATCAACAGAAGTTGACTGA
Enzyme 1 GenBank Gene ID U90441 Link Image
Enzyme 1 GeneCard ID P4HA2 Link Image
Enzyme 1 GenAtlas ID P4HA2 Link Image
Enzyme 1 HGNC ID HGNC:8547 Link Image
Enzyme 1 Chromosome Location 5
Enzyme 1 Locus 5q31
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Annunen P, Helaakoski T, Myllyharju J, Veijola J, Pihlajaniemi T, Kivirikko KI: Cloning of the human prolyl 4-hydroxylase alpha subunit isoform alpha(II) and characterization of the type II enzyme tetramer. The alpha(I) and alpha(II) subunits do not form a mixed alpha(I)alpha(II)beta2 tetramer. J Biol Chem. 1997 Jul 11;272(28):17342-8. [PubMed Link Image]
  2. Nokelainen M, Nissi R, Kukkola L, Helaakoski T, Myllyharju J: Characterization of the human and mouse genes for the alpha subunit of type II prolyl 4-hydroxylase. Identification of a previously unknown alternatively spliced exon and its expression in various tissues. Eur J Biochem. 2001 Oct;268(20):5300-9. [PubMed Link Image]
  3. 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]
  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]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5538
Enzyme 2 Name Pyrroline-5-carboxylate reductase 1, mitochondrial
Enzyme 2 Synonyms
  1. P5C reductase 1
  2. P5CR 1
Enzyme 2 Gene Name PYCR1
Enzyme 2 Protein Sequence >Pyrroline-5-carboxylate reductase 1, mitochondrial
MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASSPDMDLATVSALRKMGVKLTPHNKETV
QHSDVLFLAVKPHIIPFILDEIGADIEDRHIVVSCAAGVTISSIEKKLSAFRPAPRVIRC
MTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFCTEVEEDLIDAVTGLSGSGPAY
AFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATIH
ALHVLESGGFRSLLINAVEASCIRTRELQSMADQEQVSPAAIKKTILDKVKLDSPAGTAL
SPSGHTKLLPRSLAPAGKD
Enzyme 2 Number of Residues 319
Enzyme 2 Molecular Weight 33360.3
Enzyme 2 Theoretical pI 7.69
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 Involved in the cellular response to oxidative stress
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 16306658 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P32322 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name P5CR1_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >960 bp
ATGAGCGTGGGCTTCATCGGCGCTGGCCAGCTGGCTTTTGCCCTGGCCAAGGGCTTCACA
GCAGCAGGCGTCTTGGCTGCCCACAAGATAATGGCTAGCTCCCCAGACATGGACCTGGCC
ACAGTTTCTGCTCTCAGGAAGATGGGGGTGAAGTTGACACCCCACAACAAGGAGACGGTG
CAGCACAGTGATGTGCTCTTCCTGGCTGTGAAGCCACACATCATCCCCTTCATCCTGGAT
GAAATAGGCGCCGACATTGAGGACAGACACATTGTGGTGTCCTGCGCGGCCGGCGTCACC
ATCAGCTCCATTGAGAAGAAGCTGTCAGCGTTTCGGCCAGCCCCCAGGGTCATCCGCTGC
ATGACCAACACTCCAGTCGTGGTGCGGGAGGGGGCCACCGTGTATGCCACAGGCACGCAC
GCCCAGGTGGAGGACGGGAGGCTCATGGAGCAGCTGCTGAGCAGCGTGGGCTTCTGCACG
GAGGTGGAAGAGGACCTGATTGATGCCGTCACGGGGCTCAGTGGCAGCGGCCCCGCCTAC
GCATTCACAGCCCTGGATGCCCTGGCTGATGGGGGCGTGAAGATGGGACTTCCAAGGCGC
CTGGCAGTCCGCCTCGGGGCCCAGGCCCTCCTGGGGGCTGCCAAGATGCTGCTGCACTCA
GAACAGCACCCAGGCCAGCTCAAGGACAACGTCAGCTCTCCTGGTGGGGCCACCATCCAT
GCCTTGCATGTGCTGGAGAGTGGGGGCTTCCGCTCCCTGCTCATCAACGCTGTGGAGGCC
TCCTGCATCCGCACACGGGAGCTGCAGTCCATGGCTGACCAGGAGCAGGTGTCACCAGCC
GCCATCAAGAAGACCATCCTGGACAAGGTGAAGCTGGACTCCCCTGCAGGGACCGCTCTG
TCGCCTTCTGGCCACACCAAGCTGCTCCCCCGCAGCCTGGCCCCAGCGGGCAAGGATTGA
Enzyme 2 GenBank Gene ID BC001504 Link Image
Enzyme 2 GeneCard ID PYCR1 Link Image
Enzyme 2 GenAtlas ID PYCR1 Link Image
Enzyme 2 HGNC ID HGNC:9721 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 17q25.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Dougherty KM, Brandriss MC, Valle D: Cloning human pyrroline-5-carboxylate reductase cDNA by complementation in Saccharomyces cerevisiae. J Biol Chem. 1992 Jan 15;267(2):871-5. [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]
  3. Reversade B, Escande-Beillard N, Dimopoulou A, Fischer B, Chng SC, Li Y, Shboul M, Tham PY, Kayserili H, Al-Gazali L, Shahwan M, Brancati F, Lee H, O'Connor BD, Schmidt-von Kegler M, Merriman B, Nelson SF, Masri A, Alkazaleh F, Guerra D, Ferrari P, Nanda A, Rajab A, Markie D, Gray M, Nelson J, Grix A, Sommer A, Savarirayan R, Janecke AR, Steichen E, Sillence D, Hausser I, Budde B, Nurnberg G, Nurnberg P, Seemann P, Kunkel D, Zambruno G, Dallapiccola B, Schuelke M, Robertson S, Hamamy H, Wollnik B, Van Maldergem L, Mundlos S, Kornak U: Mutations in PYCR1 cause cutis laxa with progeroid features. Nat Genet. 2009 Sep;41(9):1016-21. Epub 2009 Aug 2. [PubMed Link Image]
  4. Meng Z, Lou Z, Liu Z, Li M, Zhao X, Bartlam M, Rao Z: Crystal structure of human pyrroline-5-carboxylate reductase. J Mol Biol. 2006 Jun 23;359(5):1364-77. Epub 2006 May 11. [PubMed Link Image]
  5. Guernsey DL, Jiang H, Evans SC, Ferguson M, Matsuoka M, Nightingale M, Rideout AL, Provost S, Bedard K, Orr A, Dube MP, Ludman M, Samuels ME: Mutation in pyrroline-5-carboxylate reductase 1 gene in families with cutis laxa type 2. Am J Hum Genet. 2009 Jul;85(1):120-9. Epub 2009 Jul 2. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5539
Enzyme 3 Name Prolyl 4-hydroxylase subunit alpha-1
Enzyme 3 Synonyms
  1. 4-PH alpha-1
  2. Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-1
Enzyme 3 Gene Name P4HA1
Enzyme 3 Protein Sequence >Prolyl 4-hydroxylase subunit alpha-1
MIWYILIIGILLPQSLAHPGFFTSIGQMTDLIHTEKDLVTSLKDYIKAEEDKLEQIKKWA
EKLDRLTSTATKDPEGFVGHPVNAFKLMKRLNTEWSELENLVLKDMSDGFISNLTIQRQY
FPNDEDQVGAAKALLRLQDTYNLDTDTISKGNLPGVKHKSFLTAEDCFELGKVAYTEADY
YHTELWMEQALRQLDEGEISTIDKVSVLDYLSYAVYQQGDLDKALLLTKKLLELDPEHQR
ANGNLKYFEYIMAKEKDVNKSASDDQSDQKTTPKKKGVAVDYLPERQKYEMLCRGEGIKM
TPRRQKKLFCRYHDGNRNPKFILAPAKQEDEWDKPRIIRFHDIISDAEIEIVKDLAKPRL
RRATISNPITGDLETVHYRISKSAWLSGYENPVVSRINMRIQDLTGLDVSTAEELQVANY
GVGGQYEPHFDFARKDEPDAFKELGTGNRIATWLFYMSDVSAGGATVFPEVGASVWPKKG
TAVFWYNLFASGEGDYSTRHAACPVLVGNKWVSNKWLHERGQEFRRPCTLSELE
Enzyme 3 Number of Residues 534
Enzyme 3 Molecular Weight 61048.8
Enzyme 3 Theoretical pI 5.84
Enzyme 3 GO Classification
Function
  • L-ascorbic acid binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
  • oxidoreductase activity, acting on single donors with incorporation of molecular oxygen
  • oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
  • peptidyl-proline dioxygenase activity
  • procollagen-proline 4-dioxygenase activity
  • procollagen-proline dioxygenase activity
  • transition metal ion binding
  • vitamin binding
Process
  • metabolic process
  • oxidation reduction
Component
  • endoplasmic reticulum
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • organelle
Enzyme 3 General Function Involved in oxidoreductase activity
Enzyme 3 Specific Function Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins
Enzyme 3 Pathways
Enzyme 3 Reactions
  • procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2 [RN:R03219]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-17
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 55666281 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P13674 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name P4HA1_HUMAN Link Image
Enzyme 3 PDB ID 1TJC Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1605 bp
ATGATCTGGTATATATTAATTATAGGAATTCTGCTTCCCCAGTCTTTGGCTCATCCAGGC
TTTTTTACTTCAATTGGTCAGATGACTGATTTGATCCATACTGAGAAAGATCTGGTGACT
TCTCTGAAAGATTATATTAAGGCAGAAGAGGACAAGTTAGAACAAATAAAAAAATGGGCA
GAGAAGTTAGATCGGCTAACTAGTACAGCGACAAAAGATCCAGAAGGATTTGTTGGGCAT
CCAGTAAATGCATTCAAATTAATGAAACGTCTGAATACTGAGTGGAGTGAGTTGGAGAAT
CTGGTCCTTAAGGATATGTCAGATGGCTTTATCTCTAACCTAACCATTCAGAGACAGTAC
TTTCCTAATGATGAAGATCAGGTTGGGGCAGCCAAAGCTCTGTTACGTCTCCAGGATACC
TACAATTTGGATACAGATACCATCTCAAAGGGTAATCTTCCAGGAGTGAAACACAAATCT
TTTCTAACGGCTGAGGACTGCTTTGAGTTGGGCAAAGTGGCCTATACAGAAGCAGATTAT
TACCATACGGAACTGTGGATGGAACAAGCCCTAAGGCAACTGGATGAAGGCGAGATTTCT
ACCATAGATAAAGTCTCTGTTCTAGATTATTTGAGCTATGCGGTATATCAGCAGGGAGAC
CTGGATAAGGCACTTTTGCTCACAAAGAAGCTTCTTGAACTAGATCCTGAACATCAGAGA
GCTAATGGTAACTTAAAATATTTTGAGTATATAATGGCTAAAGAAAAAGATGTCAATAAG
TCTGCTTCAGATGACCAATCTGATCAGAAAACTACACCAAAGAAAAAAGGGGTTGCTGTG
GATTACCTGCCAGAGAGACAGAAGTACGAAATGCTGTGCCGTGGGGAGGGTATCAAAATG
ACCCCTCGGAGACAGAAAAAACTCTTTTGCCGCTACCATGATGGAAACCGTAATCCTAAA
TTTATTCTGGCTCCAGCTAAACAGGAGGATGAATGGGACAAGCCTCGTATTATTCGCTTC
CATGATATTATTTCTGATGCAGAAATTGAAATCGTCAAAGACCTAGCAAAACCAAGGCTG
AGCCGAGCTACAGTACATGACCCTGAGACTGGAAAATTGACCACAGCACAGTACAGAGTA
TCTAAGAGTGCCTGGCTCTCTGGCTATGAAAATCCTGTGGTGTCTCGAATTAATATGAGA
ATACAAGATCTAACAGGACTAGATGTTTCCACAGCAGAGGAATTACAGGTAGCAAATTAT
GGAGTTGGAGGACAGTATGAACCCCATTTTGACTTTGCACGGAAAGATGAGCCAGATGCT
TTCAAAGAGCTGGGGACAGGAAATAGAATTGCTACATGGCTGTTTTATATGAGTGATGTG
TCTGCAGGAGGAGCCACTGTTTTTCCTGAAGTTGGAGCTAGTGTTTGGCCCAAAAAAGGA
ACTGCTGTTTTCTGGTATAATCTGTTTGCCAGTGGAGAAGGAGATTATAGTACACGGCAT
GCAGCCTGTCCAGTGCTAGTTGGCAACAAATGGGTATCCAATAAATGGCTCCATGAACGT
GGACAAGAATTTCGAAGACCTTGTACGTTGTCAGAATTGGAATGA
Enzyme 3 GenBank Gene ID AL731563 Link Image
Enzyme 3 GeneCard ID P4HA1 Link Image
Enzyme 3 GenAtlas ID P4HA1 Link Image
Enzyme 3 HGNC ID HGNC:8546 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 10q21.3-q23.1
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Helaakoski T, Vuori K, Myllyla R, Kivirikko KI, Pihlajaniemi T: Molecular cloning of the alpha-subunit of human prolyl 4-hydroxylase: the complete cDNA-derived amino acid sequence and evidence for alternative splicing of RNA transcripts. Proc Natl Acad Sci U S A. 1989 Jun;86(12):4392-6. [PubMed Link Image]
  2. Helaakoski T, Veijola J, Vuori K, Rehn M, Chow LT, Taillon-Miller P, Kivirikko KI, Pihlajaniemi T: Structure and expression of the human gene for the alpha subunit of prolyl 4-hydroxylase. The two alternatively spliced types of mRNA correspond to two homologous exons the sequences of which are expressed in a variety of tissues. J Biol Chem. 1994 Nov 11;269(45):27847-54. [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. 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]
  6. Pekkala M, Hieta R, Bergmann U, Kivirikko KI, Wierenga RK, Myllyharju J: The peptide-substrate-binding domain of collagen prolyl 4-hydroxylases is a tetratricopeptide repeat domain with functional aromatic residues. J Biol Chem. 2004 Dec 10;279(50):52255-61. Epub 2004 Sep 28. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5540
Enzyme 4 Name Pyrroline-5-carboxylate reductase 2
Enzyme 4 Synonyms
  1. P5C reductase 2
  2. P5CR 2
Enzyme 4 Gene Name PYCR2
Enzyme 4 Protein Sequence >Pyrroline-5-carboxylate reductase 2
MSVGFIGAGQLAYALARGFTAAGILSAHKIIASSPEMNLPTVSALRKMGVNLTRSNKETV
KHSDVLFLAVKPHIIPFILDEIGADVQARHIVVSCAAGVTISSVEKKLMAFQPAPKVIRC
MTNTPVVVQEGATVYATGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAY
AFMALDALADGGVKMGLPRRLAIQLGAQALLGAAKMLLDSEQHPCQLKDNVCSPGGATIH
ALHFLESGGFRSLLINAVEASCIRTRELQSMADQEKISPAALKKTLLDRVKLESPTVSTL
TPSSPGKLLTRSLALGGKKD
Enzyme 4 Number of Residues 320
Enzyme 4 Molecular Weight 33636.8
Enzyme 4 Theoretical pI 7.87
Enzyme 4 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 4 General Function Involved in oxidoreductase activity
Enzyme 4 Specific Function L-proline + NAD(P)(+) = 1-pyrroline-5- carboxylate + NAD(P)H
Enzyme 4 Pathways
Enzyme 4 Reactions
  • L-proline + NAD(P)+ = 1-pyrroline-5-carboxylate + NAD(P)H + H+ [RN:R01248 R01251]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 33150582 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q96C36 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name P5CR2_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >963 bp
ATGAGCGTGGGCTTCATCGGGGCCGGCCAGCTGGCTAATGCTCTGGCGCGGGGCTTCACG
GCCGCAGCATTCCTGTCGGCTCACAAGATAATAGCCAGCTCCCCAGAAATGAACCTGCCC
ACGGTGTCCGCGCTCAGGAAGATGGGTGTGAACCTGACACGCAGCAACAAGGAGACGGTG
AAGCACAGCGACGTCCTGTTTCTGGCTGTGAAGCACATTATCATCCCCTTCATCCTGGAT
GAGATTGGGGCCGACGTGCAAGCCAGACACATCGTGGTCTCCTGTGCGGCTGGTGTCACC
ATCAGCTCTGTGGAGAAGAAGCTGATGGCATTCCAGCCAGCCCCCAAAGTGATTCGCTGC
ATGACCAACACACCTGTGGTAGTGCAGGAAGGCGCTACAGTGTACGCCACGGGCACCCAT
GCCCTGGTGGAGGATGGGCAGCTCCTGGAGCAGCTCATGAGCAGCGTGGGCTTCTGCACT
GAGGTGGAAGAGGACCTCATCGATGCCGTCACGGGGCTCAGTGGCAGCGGGCCTGCCTAT
GCATTCATGGCTCTGGACGCATTGGCTGATGGTGGGGTGAAGATGGGTTTGCCACGGCGC
CTGGCAATCCAACTCGGGGCCCAGGCTTTGCTGGGAGCTGCCAAGATGCTGCTGGACTCG
GAGCAGCATCCATGCCAGCTTAAGGACAATGTCTGCTCCCCTGGGGGAGCCACCATCCAC
GCCCTGCACTTTCTAGAGAGTGGGGGCTTCCGCTCTCTGCTCATCAATGCAGTTGAGGCC
TCCTGTATCCGAACACGAGAGCTACAGTCCATGGCCGACCAAGAAAAGATCTCCCCAGCT
GCCCTTAAGAAGACCCTCTTAGACAGAGTGAAGCTGGAATCCCCCACAGTCTCCACACTG
ACCCCCTCCAGCCCAGGGAAGCTCCTCACAAGAAGCCTGGCCCTGGGAGGCAAGAAGGAC
TAA
Enzyme 4 GenBank Gene ID AF087859 Link Image
Enzyme 4 GeneCard ID PYCR2 Link Image
Enzyme 4 GenAtlas ID PYCR2 Link Image
Enzyme 4 HGNC ID HGNC:30262 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 1q42.12
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 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 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5839
Enzyme 5 Name Bifunctional aminoacyl-tRNA synthetase
Enzyme 5 Synonyms
  1. Cell proliferation-inducing gene 32 protein
  2. Glutamyl-tRNA synthetase
  3. Glutamate--tRNA ligase
  4. GluRS
  5. Prolyl-tRNA synthetase
  6. Proline--tRNA ligase
Enzyme 5 Gene Name EPRS
Enzyme 5 Protein Sequence >Bifunctional aminoacyl-tRNA synthetase
MATLSLTVNSGDPPLGALLAVEHVKDDVSISVEEGKENILHVSENVIFTDVNSILRYLAR
VATTAGLYGSNLMEHTEIDHWLEFSATKLSSCDSFTSTINELNHCLSLRTYLVGNSLSLA
DLCVWATLKGNAAWQEQLKQKKAPVHVKRWFGFLEAQQAFQSVGTKWDVSTTKARVAPEK
KQDVGKFVELPGAEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTN
PEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMK
AEREQRIDSKHRKNPIEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMRDPTLYRCK
IQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYI
WEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGS
SRSVVNMEWDKIWAFNKKVIDPVAPRYVALLKKEVIPVNVPEAQEEMKEVAKHPKNPEVG
LKPVWYSPKVFIEGADAETFSEGEMVTFINWGNLNITKIHKNADGKIISLDAKLNLENKD
YKKTTKVTWLAETTHALPIPVICVTYEHLITKPVLGKDEDFKQYVNKNSKHEELMLGDPC
LKDLKKGDIIQLQRRGFFICDQPYEPVSPYSCKEAPCVLIYIPDGHTKEMPTSGSKEKTK
VEATKNETSAPFKERPTPSLNNNCTTSEDSLVLYNRVAVQGDVVRELKAKKAPKEDVDAA
VKQLLSLKAEYKEKTGQEYKPGNPPAEIGQNISSNSSASILESKSLYDEVAAQGEVVRKL
KAEKSPKAKINEAVECLLSLKAQYKEKTGKEYIPGQPPLSQSSDSSPTRNSEPAGLETPE
AKVLFDKVASQGEVVRKLKTEKAPKDQVDIAVQELLQLKAQYKSLIGVEYKPVSATGAED
KDKKKKEKENKSEKQNKPQKQNDGQRKDPSKNQGGGLSSSGAGEGQGPKKQTRLGLEAKK
EENLADWYSQVITKSEMIEYHDISGCYILRPWAYAIWEAIKDFFDAEIKKLGVENCYFPM
FVSQSALEKEKTHVADFAPEVAWVTRSGKTELAEPIAIRPTSETVMYPAYAKWVQSHRDL
PIKLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFATMEEAAEEVLQILDLYAQVYEEL
LAIPVVKGRKTEKEKFAGGDYTTTIEAFISASGRAIQGGTSHHLGQNFSKMFEIVFEDPK
IPGEKQFAYQNSWGLTTRTIGVMTMVHGDNMGLVLPPRVACVQVVIIPCGITNALSEEDK
EALIAKCNDYRRRLLSVNIRVRADLRDNYSPGWKFNHWELKGVPIRLEVGPRDMKSCQFV
AVRRDTGEKLTVAENEAETKLQAILEDIQVTLFTRASEDLKTHMVVANTMEDFQKILDSG
KIVQIPFCGEIDCEDWIKKTTARDQDLEPGAPSMGAKSLCIPFKPLCELQPGAKCVCGKN
PAKYYTLFGRSY
Enzyme 5 Number of Residues 1512
Enzyme 5 Molecular Weight 170589.7
Enzyme 5 Theoretical pI 7.34
Enzyme 5 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • aminoacyl-tRNA ligase activity
  • binding
  • catalytic activity
  • glutamate-tRNA ligase activity
  • ligase activity
  • ligase activity, forming aminoacyl-tRNA and related compounds
  • ligase activity, forming carbon-oxygen bonds
  • nucleoside binding
  • nucleotide binding
  • proline-tRNA ligase activity
  • purine nucleoside binding
Process
  • RNA metabolic process
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • cellular macromolecule metabolic process
  • glutamyl-tRNA aminoacylation
  • macromolecule biosynthetic process
  • macromolecule metabolic process
  • metabolic process
  • ncRNA metabolic process
  • prolyl-tRNA aminoacylation
  • tRNA aminoacylation
  • tRNA aminoacylation for protein translation
  • tRNA metabolic process
  • translation
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 5 General Function Involved in nucleotide binding
Enzyme 5 Specific Function Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction:the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA
Enzyme 5 Pathways
Enzyme 5 Reactions
  • ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu [RN:R05578]
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 P07814 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name SYEP_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >4539 bp
ATGGCGACGCTCTCTCTGACCGTGAATTCAGGAGACCCTCCGCTAGGAGCTTTGCTGGCA
GTAGAACACGTGAAAGACGATGTCAGCATTTCCGTTGAAGAAGGGAAAGAGAATATTCTT
CATGTTTCTGAAAATGTGATATTCACAGATGTGAATTCTATACTTCGCTACTTGGCTAGA
GTTGCAACTACAGCTGGGTTATATGGCTCTAATCTGATGGAACATACTGAGATTGATCAC
TGGTTGGAGTTCAGTGCTACAAAATTATCTTCATGTGATTCCTTTACTTCTACAATTAAT
GAACTCAATCATTGCCTGTCTCTGAGAACATACTTAGTTGGAAACTCCTTGAGTTTAGCA
GATTTATGTGTTTGGGCCACCCTAAAAGGAAATGCTGCCTGGCAAGAACAGTTGAAACAG
AAGAAAGCTCCAGTTCATGTAAAACGTTGGTTTGGCTTTCTTGAAGCCCAGCAGGCCTTC
CAGTCAGTAGGTACCAAGTGGGATGTTTCAACAACCAAAGCTCGAGTGGCACCTGAGAAA
AAGCAAGATGTTGGGAAATTTGTTGAGCTTCCAGGTGCGGAGATGGGAAAGGTTACCGTC
AGATTTCCTCCAGAGGCCAGTGGTTACTTACACATTGGGCATGCAAAAGCTGCTCTTCTG
AACCAGCACTACCAGGTTAACTTTAAAGGGAAACTGATCATGAGATTTGATGACACAAAT
CCTGAAAAAGAAAAGGAAGATTTTGAGAAGGTTATCTTGGAAGATGTTGCAATGTTGCAT
ATCAAACCAGATCAATTTACTTATACTTCGGATCATTTTGAAACTATAATGAAGTATGCA
GAGAAGCTAATTCAAGAAGGGAAGGCTTATGTGGATGATACTCCTGCTGAACAGATGAAA
GCAGAACGTGAGCAGAGGATAGAATCTAAACATAGAAAAAACCCTATTGAGAAGAATCTA
CAAATGTGGGAAGAAATGAAAAAAGGGAGCCAGTTTGGTCAGTCCTGTTGTTTGCGAGCA
AAAATTGACATGAGTAGTAACAATGGATGCATGAGAGATCCAACCCTTTATCGCTGCAAA
ATTCAACCACATCCAAGAACTGGAAATAAATACAATGTTTATCCAACATATGATTTTGCC
TGCCCCATAGTTGACAGCATCGAAGGTGTTACACATGCCCTGAGAACAACAGAATACCAT
GACAGAGATGAGCAGTTTTACTGGATTATTGAAGCTTTAGGCATAAGAAAACCATATATT
TGGGAATATAGTCGGCTAAATCTCAACAACACAGTGCTATCCAAAAGAAAACTCACATGG
TTTGTCAATGAAGGACTAGTAGATGGATGGGATGACCCAAGATTTCCTACGGTTCGTGGT
GTACTGAGAAGAGGGATGACAGTTGAAGGACTGAAACAGTTTATTGCTGCTCAGGGCTCC
TCACGTTCAGTCGTGAACATGGAGTGGGACAAAATCTGGGCGTTTAACAAAAAGGTTATT
GACCCAGTGGCTCCACGATATGTTGCATTACTGAAGAAAGAAGTGATCCCAGTGAATGTA
CCTGAAGCTCAGGAGGAGATGAAAGAAGTAGCCAGACACCCAAAGAATCCTGAGGTTGGC
TTGAAGCCTGTGTGGTATAGTCCCAAAGTTTTCATTGAAGGTGCTGATGCAGAGACTTTT
TCGGAGGGTGAGATGGTTACATTTATAAATTGGGGCAACCTCAACATTACAAAAATACAC
AAAAATGCAGATGGAAAAATCATATCTCTTGATGCAAAGTTGAATTTGGAAAACAAAGAC
TACAAGAAAACCACTAAGGTCACTTGGCTTGCAGAGACTACACATGCTCTTCCTATTCCA
GTAATCTGTGTCACTTATGAGCACTTGATCACAAAGCCAGTGCTAGGAAAAGACGAGGAC
TTTAAGCAGTATGTCAACAAGAACAGTAAGCATGAAGAGCTAATGCTAGGGGATCCCTGC
CTTAAGGATTTGAAAAAAGGAGATATTATACAACTCCAGAGAAGAGGATTCTTCATATGT
GATCAACCTTATGAACCTGTTAGCCCATATAGTTGCAAGGAAGCCCCGTGTGTTTTGATA
TACATTCCTGATGGGCACACAAAGGAAATGCCAACATCAGGGTCAAAGGAAAAGACCAAA
GTAGAAGCCACAAAAAATGAGACCTCTGCTCCTTTTAAGGAAAGACCAACACCTTCTCTG
AATAATAATTGTACTACATCTGAGGATTCCTTGGTCCTTTACAATAGAGTGGCTGTTCAA
GGAGATGTGGTTCGTGAATTAAAAGCCAAGAAAGCACCAAAGGAAGATGTAGATGCAGCT
GTAAAACAGCTTTTGTCTTTGAAAGCTGAATATAAGGAGAAAACTGGCCAGGAATATAAA
CCTGGAAACCCTCCTGCTGAAATAGGACAGAATATTTCTTCTAATTCCTCAGCAAGTATT
CTGGAAAGTAAATCTCTGTATGATGAAGTTGCTGCACAAGGGGAGGTGGTTCGTAAGCTA
AAAGCTGAAAAATCCCCTAAGGCTAAAATAAATGAAGCTGTAGAATGCTTACTGTCCCTG
AAGGCTCAGTATAAAGAAAAAACTGGGAAGGAGTACATACCTGGTCAGCCCCCATTATCT
CAAAGTTCGGATTCAAGCCCAACCAGAAATTCTGAACCTGCTGGTTTAGAAACACCAGAA
GCGAAAGTACTTTTTGACAAAGTAGCTTCTCAAGGGGAAGTAGTTCGGAAACTTAAAACT
GAAAAAGCCCCTAAGGATCAAGTAGATATAGCTGTTCAAGAACTCCTTCAGCTAAAGGCA
CAGTACGAGTCTTTGATAGGAGTAGAGTATAAGCCTGTGTCGGCCACTGGAGCTGAGGAC
AAAGATAAGAAGAAGAAAGAAAAAGAAAATAAATCTGAAAAGCAGAATAAGCCTCAGAAA
CAAAATGATGGCCAAAGGAAAGACCCTTCTAAAAACCAAGGAGGTGGGCTCTCATCAAGT
GGAGCAGGAGAAGGGCAGGGGCCTAAGAAACAGACCAGGTTGGGTCTTGAGGCAAAAAAA
GAAGAAAATCTTGCTGATTGGTATTCTCAGGTCATCACAAAATCAGAAATGATTGAATAC
CATGACGTAAGTGGCTGTTATATTCTTCGTCCCTGGGCCTATGCCATTTGGGAAGCCATC
AAGGACTTTTTTGATGCTGAGATCAAGAAACTTGGTGTTGAAAACTGCTACTTCCCCATG
TTTGTGTCTCAAAGTGCATTAGAGAAAGAGAAGACTCATGTTGCTGACTTTGCCCCAGAG
GTTGCTTGGGTTACAAGATCTGGCAAAACCGAGCTGGCAGAACCAATTGCCATTCGTCCT
ACTAGTGAAACAGTAATGTATCCTGCATATGCAAAATGGGTACAATCACACAGAGACCTG
CCCATCAAGCTCAATCAGTGGTGCAATGTGGTGCGTTGGGAATTCAAGCATCCTCAGCCT
TTCCTACGTACTCGTGAATTTCTTTGGCAGGAAGGGCACAGTGCTTTTGTTACCGTGGAA
GAGGCAGCGGAAGAGGTCTTGCAGATACTTGACTTATATGCTCAGGTATATGAAGAACTC
CTGGCAATTCCTGTTGTTAAAGGAAGAAAGACGGAAAAGGAAAAATTTGCAGGAGGAGAC
TATACAACTACAATAGAAGCATTTATATCTGCTAGTGGAAGAGCTATCCAGGGAGGAACA
TCACATCATTTAGGGCAGAATTTTTCCAAAATGTTTGAAATCGTTTTTGAAGATCCAAAG
ATACCAGGAGAGAAGCAATTTGCCTATCAAAACTCCTGGGGCCTGACAACTCGAACTATT
GGTGTTATGACCATGGTTCATGGGGACAACATGGGTTTAGTATTACCACCCCGTGTAGCA
TGTGTTCAGGTGGTGATTATTCCTTGTGGCATTACCAATGCACTTTCTGAAGAAGACAAA
GAAGCGCTGATTGCAAAATGCAATGATTATCGAAGGCGATTACTCAGTGTTAACATCCGC
GTTAGAGCTGATTTACGAGATAATTATTCTCCAGGTTGGAAATTCAATCACTGGGAGCTC
AAGGGAGTTCCCATTAGACTTGAAGTTGGGCCACGTGATATGAAGAGCTGTCAGTTTGTA
GCCGTCAGACGAGATACTGGAGAAAAGCTGACAGTTGCTGAAAATGAGGCAGAGACTAAA
CTTCAAGCTATTTTGGAAGACATCCAGGTCACCCTTTTCACAAGGGCTTCTGAAGACCTT
AAGACTCATATGGTTGTGGCTAATACAATGGAAGACTTTCAGAAGATACTAGATTCTGGA
AGGATTGTTCAGATTCCATTCTGTGGGGAAATTGACTGTGAGGACTGGATCAAAAAGACC
ACTGCCAGGGATCAAGATCTTGAACCTGGTGCTCCATCCATGGGAGCTAAAAGCCTTTGC
ATCCCCTTCAAACCACTCTGTGAACTGCAGCCTGGAGCCAAATGTGTCTGTGGCAAGAAC
CCTGCCAAGTACTACACCTTATTTGGTCGCAGCTACTGA
Enzyme 5 GenBank Gene ID CR933648 Link Image
Enzyme 5 GeneCard ID EPRS Link Image
Enzyme 5 GenAtlas ID EPRS Link Image
Enzyme 5 HGNC ID HGNC:3418 Link Image
Enzyme 5 Chromosome Location 1
Enzyme 5 Locus 1q41-q42
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. 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]
  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. Fett R, Knippers R: The primary structure of human glutaminyl-tRNA synthetase. A highly conserved core, amino acid repeat regions, and homologies with translation elongation factors. J Biol Chem. 1991 Jan 25;266(3):1448-55. [PubMed Link Image]
  5. Thommes P, Fett R, Schray B, Kunze N, Knippers R: The core region of human glutaminyl-tRNA synthetase homologies with the Escherichia coli and yeast enzymes. Nucleic Acids Res. 1988 Jun 24;16(12):5391-406. [PubMed Link Image]
  6. Cerini C, Kerjan P, Astier M, Gratecos D, Mirande M, Semeriva M: A component of the multisynthetase complex is a multifunctional aminoacyl-tRNA synthetase. EMBO J. 1991 Dec;10(13):4267-77. [PubMed Link Image]
  7. Kaiser E, Eberhard D, Knippers R: Exons encoding the highly conserved part of human glutaminyl-tRNA synthetase. J Mol Evol. 1992 Jan;34(1):45-53. [PubMed Link Image]
  8. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  9. Kato T, Daigo Y, Hayama S, Ishikawa N, Yamabuki T, Ito T, Miyamoto M, Kondo S, Nakamura Y: A novel human tRNA-dihydrouridine synthase involved in pulmonary carcinogenesis. Cancer Res. 2005 Jul 1;65(13):5638-46. [PubMed Link Image]
  10. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  11. 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]
  12. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
  13. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  14. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  15. 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]
  16. 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]
  17. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  18. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  19. 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]
  20. Jeong EJ, Hwang GS, Kim KH, Kim MJ, Kim S, Kim KS: Structural analysis of multifunctional peptide motifs in human bifunctional tRNA synthetase: identification of RNA-binding residues and functional implications for tandem repeats. Biochemistry. 2000 Dec 26;39(51):15775-82. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 6147
Enzyme 6 Name Cytosol aminopeptidase
Enzyme 6 Synonyms
  1. Leucine aminopeptidase 3
  2. LAP-3
  3. Leucyl aminopeptidase
  4. Peptidase S
  5. Proline aminopeptidase
  6. Prolyl aminopeptidase
Enzyme 6 Gene Name LAP3
Enzyme 6 Protein Sequence >Cytosol aminopeptidase
MFLLPLPAAGRVVVRRLAVRRFGSRSLSTADMTKGLVLGIYSKEKEDDVPQFTSAGENFD
KLLAGKLRETLNISGPPLKAGKTRTFYGLHQDFPSVVLVGLGKKAAGIDEQENWHEGKEN
IRAAVAAGCRQIQDLELSSVEVDPCGDAQAAAEGAVLGLYEYDDLKQKKKMAVSAKLYGS
GDQEAWQKGVLFASGQNLARQLMETPANEMTPTRFAEIIEKNLKSASSKTEVHIRPKSWI
EEQAMGSFLSVAKGSDEPPVFLEIHYKGSPNANEPPLVFVGKGITFDSGGISIKASANMD
LMRADMGGAATICSAIVSAAKLNLPINIIGLAPLCENMPSGKANKPGDVVRAKNGKTIQV
DNTDAEGRLILADALCYAHTFNPKVILNAATLTGAMDVALGSGATGVFTNSSWLWNKLFE
ASIETGDRVWRMPLFEHYTRQVVDCQLADVNNIGKYRSAGACTAAAFLKEFVTHPKWAHL
DIAGVMTNKDEVPYLRKGMTGRPTRTLIEFLLRFSQDNA
Enzyme 6 Number of Residues 519
Enzyme 6 Molecular Weight 56165.8
Enzyme 6 Theoretical pI 8.05
Enzyme 6 GO Classification
Function
  • aminopeptidase activity
  • binding
  • catalytic activity
  • cation binding
  • exopeptidase activity
  • hydrolase activity
  • ion binding
  • manganese ion binding
  • metal ion binding
  • metalloexopeptidase activity
  • metallopeptidase activity
  • peptidase activity
  • peptidase activity, acting on L-amino acid peptides
  • transition metal ion binding
Process
  • macromolecule metabolic process
  • metabolic process
  • protein metabolic process
  • proteolysis
Component
  • cell part
  • cytoplasm
  • intracellular
  • intracellular part
Enzyme 6 General Function Involved in aminopeptidase activity
Enzyme 6 Specific Function Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides
Enzyme 6 Pathways
Enzyme 6 Reactions
  • Release of N-terminal proline from a peptide ALL_REAC (other) R00135 COFACTOR Manganese [CPD:C00034]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 4335941 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P28838 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name AMPL_HUMAN Link Image
Enzyme 6 PDB ID 1LAP Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1560 bp
ATGTTCTTGCTGCCTCTTCCGGCTGCGGGGCGAGTAGTCGTCCGACGTCTGGCCGTAGTA
CGTTCTGGGAGCCGGAGTCTCTCCACCGCAGACATGACGAAGGGCCTTGTTTTAGGAATC
TATTCCAAAGAAAAAGAAGATGATGTGCCACAGTTCACAAGTGCAGGAGAGAATTTTGAT
AAATTGTTAGCTGGAAAGCTGAGAGAGACTTTGAACATATCTGGACCACCTCTGAAGGCA
GGGAAGACTCGAACCTTTTATGGTCTGCATCAGGACTTCCCCAGCGTGGTGCTAGTTGGC
CTCGGCAAAAAGGCAGCTGGAATCGACGAACAGGAAAACTGGCATGAAGGCAAAGAAAAC
ATCAGAGCTGCTGTTGCAGCGGGGTGCAGGCAGATTCAAGACCTGGAGCTCTCGTCTGTG
GAGGTGGATCCCTGTGGAGACGCTCAGGCTGCTGCGGAGGGAGCGGTGCTTGGTCTCTAT
GAATACGATGACCTAAAGCAAAAAAAGAAGATGGCTGTGTCGGCAAAGCTCTATGGAAGT
GGGGATCAGGAGGCCTGGCAGAAAGGAGTCCTGTTTGCTTCTGGGCAGAACTTGGCACGC
CAATTGATGGAGACGCCAGCCAATGAGATGACGCCAACCAGATTTGCCGAAATTATTGAG
AAGAATCTCAAAAGTGCTAGTAGTAAAACCGAGGTCCATATCAGACCCAAGTCTTGGATT
GAGGAACAGGCAATGGGATCATTCCTCAGTGTGGCCAAAGGATCTGACGAGCCCCCAGTC
TTCTTGGAAATTCACTACAAAGGCAGCCCCAATGCAAACGAACCACCCCTGGTGTTTGTT
GGGAAAGGAATTACCTTTGACAGTGGTGGTATCTCCATCAAGGCTTCTGCAAATATGGAC
CTCATGAGGGCTGACATGGGAGGAGCTGCAACTATATGCTCAGCCATCGTGTCTGCTGCA
AAGTTAAATTTGCCCATTAATATTATAGGTCTGGCCCCTCTTTGTGAAAATATGCCCAGC
GGCAAGGCCAACAAGCCGGGGGATGTTGTTAGAGCCAAAAACGGGAAGACCATCCAGGTT
GATAACACTGATGCTGAGGGGAGGCTCATACTGGCTGATGCGCTCTGTTACGCACACACG
TTTAACCCGAAGGTCATCCTCAATGCCGCCACCTTAACAGGTGCCATGGATGTAGCTTTG
GGATCAGGTGCCACTGGGGTCTTTACCAATTCATCCTGGCTCTGGAACAAACTCTTCGAG
GCCAGCATTGAAACAGGGGACCGTGTCTGGAGGATGCCTCTCTTCGAACATTATACAAGA
CAGGTTGTAGATTGCCAGCTTGCTGATGTTAACAACATTGGAAAATACAGATCTGCAGGA
GCATGTACAGCTGCAGCATTCCTGAAAGAATTCGTAACTCATCCTAAGTGGGCACATTTA
GACATAGCAGGCGTGATGACCAACAAAGATGAAGTTCCCTATCTACGGAAAGGCATGACT
GGGAGGCCCACAAGGACTCTCATTGAGTTCTTACTTCGTTTCAGTCAAGACAATGCTTAG
Enzyme 6 GenBank Gene ID AF061738 Link Image
Enzyme 6 GeneCard ID LAP3 Link Image
Enzyme 6 GenAtlas ID LAP3 Link Image
Enzyme 6 HGNC ID HGNC:18449 Link Image
Enzyme 6 Chromosome Location 4
Enzyme 6 Locus 4p15.32
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 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. 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]
  3. Matsushima M, Takahashi T, Ichinose M, Miki K, Kurokawa K, Takahashi K: Structural and immunological evidence for the identity of prolyl aminopeptidase with leucyl aminopeptidase. Biochem Biophys Res Commun. 1991 Aug 15;178(3):1459-64. [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 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 7521
Enzyme 7 Name Proline dehydrogenase, mitochondrial
Enzyme 7 Synonyms
  1. Proline oxidase
  2. Proline oxidase 2
  3. p53-induced gene 6 protein
Enzyme 7 Gene Name PRODH
Enzyme 7 Protein Sequence >Proline dehydrogenase, mitochondrial
MLEFVMREWKKSRKLLGQRLFNKLMKMTFYGHFVAGEDQESIQPLLRHYRAFGVSAILDY
GVEEDLSPEEAEHKEMESCTSAAERDGSGTNKRDKQYQAHRAFGDRRNGVISARTYFYAN
EAKCDSHMETFLRCIEASGRVSDDGFIAIKLTALGRPQFLLQFSEVLAKWRCFFHQMAVE
QGQAGLAAMDTKLEVAVLQESVAKLGIASRAEIEDWFTAETLGVSGTMDLLDWSSLIDSR
TKLSKHLVVPNAQTGQLEPLLSRFTEEEELQMTRMLQRMDVLAKKATEMGVRLMVDAEQT
YFQPAISRLTLEMQRKFNVEKPLIFNTYQCYLKDAYDNVTLDVELARREGWCFGAKLVRG
AYLAQERARAAEIGYEDPINPTYEATNAMYHRCLDYVLEELKHNAKAKVMVASHNEDTVR
FALRRMEELGLHPADHQVYFGQLLGMCDQISFPLGQAGYPVYKYVPYGPVMEVLPYLSRR
ALENSSLMKGTHRERQLLWLELLRRLRTGNLFHRPA
Enzyme 7 Number of Residues 516
Enzyme 7 Molecular Weight 59230.4
Enzyme 7 Theoretical pI 6.88
Enzyme 7 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 7 General Function Involved in proline dehydrogenase activity
Enzyme 7 Specific Function Converts proline to delta-1-pyrroline-5-carboxylate
Enzyme 7 Pathways
Enzyme 7 Reactions
  • L-proline + acceptor = (S)-1-pyrroline-5-carboxylate + reduced acceptor [RN:R01253]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 2677802 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID O43272 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name PROD_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 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 7 GenBank Gene ID U82381 Link Image
Enzyme 7 GeneCard ID PRODH Link Image
Enzyme 7 GenAtlas ID PRODH Link Image
Enzyme 7 HGNC ID HGNC:9453 Link Image
Enzyme 7 Chromosome Location 2
Enzyme 7 Locus 22q11.21
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 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 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 8489
Enzyme 8 Name Pyrroline-5-carboxylate reductase 3
Enzyme 8 Synonyms
  1. P5C reductase 3
  2. P5CR 3
  3. Pyrroline-5-carboxylate reductase-like protein
Enzyme 8 Gene Name PYCRL
Enzyme 8 Protein Sequence >Pyrroline-5-carboxylate reductase 3
MAAAEPSPRRVGFVGAGRMAGAIAQGLIRAGKVEAQHILASAPTDRNLCHFQALGCRTTH
SNQEVLQSCLLVIFATKPHVLPAVLAEVAPVVTTEHILVSVAAGVSLSTLEELLPPNTRV
LRVLPNLPCVVQEGAIVMARGRHVGSSETNLLQHLLEACGRCEEVPEAYVDIHTGLSGSG
VAFVCAFSEALAEGAVKMGMPSSLAHRIAAQTLLGTAKMLLHEGQHPAQLRSDVCTPGGT
TIYGLHALEQGGLRAATMSAVEAATCRAKELSRK
Enzyme 8 Number of Residues 274
Enzyme 8 Molecular Weight 28649.0
Enzyme 8 Theoretical pI 7.55
Enzyme 8 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 8 General Function Involved in oxidoreductase activity
Enzyme 8 Specific Function L-proline + NAD(P)(+) = 1-pyrroline-5- carboxylate + NAD(P)H
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions
  • L-proline + NAD(P)+ = 1-pyrroline-5-carboxylate + NAD(P)H + H+ [RN:R01248 R01251]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein Not Available
Enzyme 8 UniProtKB/Swiss-Prot ID Q53H96 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name P5CR3_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >825 bp
ATGGCAGCTGCGGAGCCGTCTCCGCGGCGCGTGGGCTTCGTGGGCGCGGGCCGCATGGCG
GGGGCCATCGCGCAGGGCCTCATCAGAGCAGGAAAAGTGGAAGCTCAGCACATACTGGCC
AGTGCACCAACAGACAGGAACCTATGTCACTTTCAAGCTCTGGGTTGCCGGACCACGCAC
TCCAACCAGGAGGTGCTGCAGAGCTGCCTGCTCGTCATCTTTGCCACCAAGCCTCATGTG
CTGCCAGCTGTCCTGGCAGAGGTGGCTCCTGTGGTCACCACTGAACACATCTTGGTGTCC
GTGGCTGCTGGGGTGTCTCTGAGCACCCTGGAGGAGCTGCTGCCCCCGAACACACGGGTG
CTGCGGGTCTTGCCCAACCTGCCCTGTGTGGTCCAGGAAGGGGCCATAGTGATGGCGCGG
GGCCGCCACGTGGGGAGCAGCGAGACCAACCTCCTGCAGCATCTGCTGGAGGCCTGTGGG
CGGTGTGAGGAGGTGCCTGAAGCCTACGTCGACATCCACACTGGCCTCAGTGGCAGTGGC
GTGGCCTTCGTGTGTGCATTCTCCGAGGCCCTGGCTGAAGGAGCCGTCAAGATGGGCATG
CCCAGCAGCCTGGCCCACCGCATCGCTGCCCAGACCCTGCTGGGGACGGCCAAGATGCTG
CTGCACGAGGGCCAACACCCAGCCCAGCTGCGCTCAGACGTGTGCACCCCGGGTGGCACC
ACCATCTATGGACTCCACGCCCTGGAGCAGGGCGGGCTGCGAGCAGCCACCATGAGCGCC
GTGGAGGCTGCCACCTGCCGGGCCAAGGAGCTCAGCAGAAAGTAG
Enzyme 8 GenBank Gene ID AK001500 Link Image
Enzyme 8 GeneCard ID PYCRL Link Image
Enzyme 8 GenAtlas ID PYCRL Link Image
Enzyme 8 HGNC ID HGNC:25846 Link Image
Enzyme 8 Chromosome Location 8
Enzyme 8 Locus 8q24.3
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 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. 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]
  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]
  4. 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 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 8833
Enzyme 9 Name Sodium-dependent proline transporter
Enzyme 9 Synonyms
  1. Solute carrier family 6 member 7
Enzyme 9 Gene Name SLC6A7
Enzyme 9 Protein Sequence >Sodium-dependent proline transporter
MKKLQGAHLRKPVTPDLLMTPSDQGDVDLDVDFAAHRGNWTGKLDFLLSCIGYCVGLGNV
WRFPYRAYTNGGGAFLVPYFLMLAICGIPLFFLELSLGQFSSLGPLAVWKISPLFKGAGA
AMLLIVGLVAIYYNMIIAYVLFYLFASLTSDLPWEHCGNWWNTELCLEHRVSKDGNGALP
LNLTCTVSPSEEYWSRYVLHIQGSQGIGSPGEIRWNLCLCLLLAWVIVFLCILKGVKSSG
KVVYFTATFPYLILLMLLVRGVTLPGAWKGIQFYLTPQFHHLLSSKVWIEAALQIFYSLG
VGFGGLLTFASYNTFHQNIYRDTFIVTLGNAITSILAGFAIFSVLGYMSQELGVPVDQVA
KAGPGLAFVVYPQAMTMLPLSPFWSFLFFFMLLTLGLDSQFAFLETIVTAVTDEFPYYLR
PKKAVFSGLICVAMYLMGLILTTDGGMYWLVLLDDYSASFGLMVVVITTCLAVTRVYGIQ
RFCRDIHMMLGFKPGLYFRACWLFLSPATLLALMVYSIVKYQPSEYGSYRFPPWAELLGI
LMGLLSCLMIPAGMLVAVLREEGSLWERLQQASRPAMDWGPSLEENRTGMYVATLAGSQS
PKPLMVHMRKYGGITSFENTAIEVDREIAEEEESMM
Enzyme 9 Number of Residues 636
Enzyme 9 Molecular Weight 70909.9
Enzyme 9 Theoretical pI 6.66
Enzyme 9 GO Classification
Function
  • neurotransmitter transporter activity
  • neurotransmitter:sodium symporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • establishment of localization
  • neurotransmitter transport
  • transport
Component
  • cell part
  • integral to membrane
  • integral to plasma membrane
  • intrinsic to membrane
  • membrane
  • membrane part
Enzyme 9 General Function Involved in neurotransmitter:sodium symporter activity
Enzyme 9 Specific Function Terminates the action of proline by its high affinity sodium-dependent reuptake into presynaptic terminals
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • 46-66 74-93 117-137 215-233 242-259 295-312 324-345 378-397 425-443 459-479 500-519 538-556
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 134304856 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q99884 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name SC6A7_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >1911 bp
ATGAAGAAGCTCCAGGGAGCTCACCTCCGCAAGCCTGTCACCCCAGACCTGCTGATGACC
CCCAGTGACCAGGGCGATGTCGACCTGGATGTGGACTTTGCTGCACACCGGGGGAACTGG
ACAGGCAAGCTGGACTTCCTGCTGTCCTGCATTGGCTACTGTGTAGGCCTGGGGAATGTC
TGGCGCTTCCCCTATCGAGCGTACACCAATGGAGGAGGCGCCTTCCTCGTGCCCTACTTC
CTCATGCTGGCCATCTGTGGCATCCCCCTCTTCTTCCTGGAGCTCTCCCTGGGCCAGTTC
TCCAGCCTAGGGCCCCTGGCTGTCTGGAAAATCAGCCCTCTCTTCAAAGGCGCCGGCGCA
GCCATGCTGCTCATCGTGGGCTTGGTGGCCATCTACTACAACATGATCATCGCCTACGTG
CTCTTCTACCTCTTCGCCTCCCTCACCAGCGACCTACCCTGGGAGCACTGTGGCAACTGG
TGGAACACAGAACTCTGCCTGGAGCACAGAGTCTCCAAGGACGGCAACGGGGCCCTGCCC
CTCAACCTCACCTGCACCGTCAGCCCCAGCGAGGAGTACTGGAGCCGCTACGTCCTCCAC
ATCCAAGGCAGCCAGGGCATCGGCAGCCCTGGGGAGATCCGCTGGAACCTCTGCCTCTGC
CTGCTGCTGGCCTGGGTCATCGTGTTCCTCTGTATCCTCAAGGGTGTGAAGTCTTCGGGC
AAGGTGGTGTATTTCACGGCCACGTTCCCCTACCTCATCCTGCTCATGCTGCTGGTCCGC
GGAGTCACCCTCCCAGGGGCCTGGAAGGGCATCCAGTTCTATCTCACCCCCCAGTTCCAC
CACTTGTTGTCTTCCAAGGTGTGGATTGAAGCTGCTCTTCAGATCTTCTATTCCCTGGGT
GTGGGCTTCGGGGGGCTCCTCACCTTTGCCTCCTACAACACGTTTCACCAGAACATCTAT
AGAGACACTTTCATCGTCACTCTGGGCAACGCCATCACCAGCATCCTGGCTGGCTTTGCC
ATCTTCTCCGTGCTGGGCTACATGTCTCAGGAGCTGGGCGTGCCTGTGGACCAAGTAGCC
AAAGCAGGCCCTGGCCTGGCCTTTGTCGTCTACCCACAGGCCATGACCATGCTGCCTCTG
TCACCCTTCTGGTCCTTTCTCTTCTTCTTCATGCTTCTGACTCTCGGCCTAGATAGCCAG
TTTGCTTTTCTGGAGACCATTGTGACAGCTGTGACAGATGAGTTCCCATACTACCTGCGG
CCCAAGAAGGCGGTGTTCTCAGGGCTCATCTGCGTGGCCATGTACCTGATGGGGCTGATC
CTCACCACTGATGGGGGCATGTACTGGCTGGTCCTTCTGGATGACTACAGCGCCAGCTTC
GGGCTGATGGTGGTGGTTATCACCACGTGCCTTGCCGTGACACGGGTGTATGGCATTCAG
AGGTTCTGCCGAGACATCCACATGATGCTGGGCTTCAAGCCGGGCCTCTACTTCAGGGCC
TGCTGGCTGTTCCTGTCCCCAGCCACGCTCTTGGCCCTCATGGTGTATAGCATCGTCAAG
TACCAGCCCTCGGAGTATGGCAGTTACCGCTTCCCGCCCTGGGCTGAGCTGCTGGGCATC
CTGATGGGCCTGCTGTCCTGCCTCATGATCCCAGCTGGCATGCTGGTGGCTGTGCTTCGA
GAAGAGGGCTCACTCTGGGAGCGGCTCCAACAGGCCAGCCGGCCGGCCATGGACTGGGGA
CCATCGCTGGAGGAGAACCGGACGGGCATGTATGTGGCCACGCTGGCTGGGAGCCAGTCA
CCAAAGCCACTGATGGTGCACATGCGCAAGTACGGGGGCATCACCAGCTTCGAGAACACG
GCCATCGAGGTGGACCGTGAGATTGCAGAGGAGGAGGAGTCGATGATGTGA
Enzyme 9 GenBank Gene ID NM_014228.3 Link Image
Enzyme 9 GeneCard ID SLC6A7 Link Image
Enzyme 9 GenAtlas ID SLC6A7 Link Image
Enzyme 9 HGNC ID HGNC:11054 Link Image
Enzyme 9 Chromosome Location 5
Enzyme 9 Locus 5q31-q32
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Shafqat S, Velaz-Faircloth M, Henzi VA, Whitney KD, Yang-Feng TL, Seldin MF, Fremeau RT Jr: Human brain-specific L-proline transporter: molecular cloning, functional expression, and chromosomal localization of the gene in human and mouse genomes. Mol Pharmacol. 1995 Aug;48(2):219-29. [PubMed Link Image]
  2. Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W, Hellsten U, Tran-Gyamfi M, She X, Prabhakar S, Aerts A, Altherr M, Bajorek E, Black S, Branscomb E, Caoile C, Challacombe JF, Chan YM, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Lopez F, Lou Y, Martinez D, Medina C, Morgan J, Nandkeshwar R, Noonan JP, Pitluck S, Pollard M, Predki P, Priest J, Ramirez L, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wheeler J, Wu K, Yang J, Dickson M, Cheng JF, Eichler EE, Olsen A, Pennacchio LA, Rokhsar DS, Richardson P, Lucas SM, Myers RM, Rubin EM: The DNA sequence and comparative analysis of human chromosome 5. Nature. 2004 Sep 16;431(7006):268-74. [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]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 12995
Enzyme 10 Name cDNA FLJ75752, highly similar to Homo sapiens pyrroline-5-carboxylate reductase family, member 2
Enzyme 10 Synonyms
  1. PYCR2, mRNA
  2. Pyrroline-5-carboxylate reductase family, member 2, isoform CRA_b
Enzyme 10 Gene Name PYCR2
Enzyme 10 Protein Sequence >cDNA FLJ75752, highly similar to Homo sapiens pyrroline-5-carboxylate reductase family, member 2
MSVGFIGAGQLAYALARGFTAAGILSAHKIIASSPEMNLPTVSALRKMGVNLTRSNKETV
KHSDVLFLAVKPHIIPFILDEIGADVQARHIVVSCAAGVTISSVEKKLMAFQPAPKVIRC
MTNTPVVVQEGATVYATGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAY
AFMALDALADGGVKMGLPRRLAIQLGAQALLGAAKMLLDSEQHPCQLKDNVCSPGGATIH
ALHFLESGGFRSLLINAVEASCIRTRELQSMADQEKISPAALKKTLLDRVKLESPTVSTL
TPSSPGKLLTRSLALGGKKD
Enzyme 10 Number of Residues 320
Enzyme 10 Molecular Weight 33638
Enzyme 10 Theoretical pI 7.87
Enzyme 10 GO Classification Not Available
Enzyme 10 General Function Amino acid transport and metabolism
Enzyme 10 Specific Function Not Available
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions Not Available
Enzyme 10 Pfam Domain Function Not Available
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 158257258 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID A8K798 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name A8K798_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence Not Available
Enzyme 10 GenBank Gene ID AK291913 Link Image
Enzyme 10 GeneCard ID A8K798 Link Image
Enzyme 10 GenAtlas ID Not Available
Enzyme 10 HGNC ID Not Available
Enzyme 10 Chromosome Location Not Available
Enzyme 10 Locus Not Available
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References Not Available
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 12996
Enzyme 11 Name Uncharacterized protein PRODH
Enzyme 11 Synonyms Not Available
Enzyme 11 Gene Name PRODH
Enzyme 11 Protein Sequence >Uncharacterized protein PRODH
RHGSEARPARAAPLHSPLRPAVHGAGLPRAARSGPSGRARRWVGHGSAAAGARRGLRQRA
GGVPQPANLGAGAEPAGAALVRLARAAGAPRAAAVCFQETSRTEAIQQAHEDDLLWAFCS
RGGESIQPLLRHYRAFGVSAILDYGVEEDLSPEEAEHKEMESCTSAAERDGSGTNKRDKQ
YQAHWAFGDRRNGVISARTYFYANEAKCDSHMETFLRCIEASGRVSDDGFIAIKLTALGR
PQFLLQFSEVLAKWRCFFHQMAVEQGQAGLAAMDTKLEVAVLQESVAKLGIASRAEIEDW
FTAETLGVSGTMDLLDWSSLIDSRTKLSKHLVVPNAQTGQLEPLLSRFTEEEELQMTRML
QRMDVLAKKATEMGVRLMVDAEQTYFQPAISRLTLEMQRKFNVEKPLIFNTYQPHPADAY
DNVTLDVELARREGWCFGAKLVRGAYLAQERARAAEIGYEDPINPTYEATNAMYHRCLDY
VLEELKHNAKAKVMVASHNEDTVRFALRRMEELGLHPADHRVYFGQLLGMCDQISFPLGQ
AGYPVYKYVPYGPVMEVLPYLSRRALENSSLMKGTHRERQLLWLELLRRLRTGNLFHRPA
Enzyme 11 Number of Residues 600
Enzyme 11 Molecular Weight 66921
Enzyme 11 Theoretical pI 8.01
Enzyme 11 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 11 General Function Amino acid transport and metabolism
Enzyme 11 Specific Function Not Available
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions Not Available
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein Not Available
Enzyme 11 UniProtKB/Swiss-Prot ID A6NF53 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name A6NF53_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence Not Available
Enzyme 11 GenBank Gene ID AC007326 Link Image
Enzyme 11 GeneCard ID A6NF53 Link Image
Enzyme 11 GenAtlas ID PRODH Link Image
Enzyme 11 HGNC ID HGNC:9453 Link Image
Enzyme 11 Chromosome Location Not Available
Enzyme 11 Locus Not Available
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 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 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 12997
Enzyme 12 Name Melastatin 1 splicing variant
Enzyme 12 Synonyms Not Available
Enzyme 12 Gene Name MLSN1
Enzyme 12 Protein Sequence >Melastatin 1 splicing variant
MYIRVSYDTKPDSLLHLMVKDWQLELPKLLISVHGGLQNFEMQPKLKQVFGKGLIKAAMT
TGAWIFTGGVSTGVISHVGDALKDHSSKSRGRVCAIGIAPWGIVENKEDLVGKDVTRVYQ
TMSNPLSKLSVLNNSHTHFILADNGTLGKYGAEVKLRRLLEKHISLQKINTRLGQGVPLV
GLVVEGGPNVVSIVLEYLQEEPPIPVVICDGSGRASDILSFAHKYCEEGG
Enzyme 12 Number of Residues 230
Enzyme 12 Molecular Weight 25053
Enzyme 12 Theoretical pI 8.79
Enzyme 12 GO Classification Not Available
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 Not Available
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 33235690 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q7Z4N3 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name Q7Z4N3_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 AB115500 Link Image
Enzyme 12 GeneCard ID Q7Z4N3 Link Image
Enzyme 12 GenAtlas ID TRPM1 Link Image
Enzyme 12 HGNC ID HGNC:7146 Link Image
Enzyme 12 Chromosome Location Not Available
Enzyme 12 Locus Not Available
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 13791
Enzyme 13 Name Transient receptor potential cation channel subfamily M member 1
Enzyme 13 Synonyms
  1. Long transient receptor potential channel 1
  2. LTrpC1
  3. Melastatin-1
Enzyme 13 Gene Name TRPM1
Enzyme 13 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 13 Number of Residues 1603
Enzyme 13 Molecular Weight 182177.0
Enzyme 13 Theoretical pI 6.82
Enzyme 13 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 13 General Function Involved in ion channel activity
Enzyme 13 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 13 Pathways Not Available
Enzyme 13 Reactions Not Available
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • 525-545 746-766 831-851 853-873 898-918 929-949 962-982 1055-1075 1106-1126
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 94538366 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q7Z4N2 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name TRPM1_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 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 13 GenBank Gene ID NM_002420.4 Link Image
Enzyme 13 GeneCard ID TRPM1 Link Image
Enzyme 13 GenAtlas ID TRPM1 Link Image
Enzyme 13 HGNC ID HGNC:7146 Link Image
Enzyme 13 Chromosome Location 1
Enzyme 13 Locus 15q13.3
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 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 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 14401
Enzyme 14 Name Prolyl 3-hydroxylase 1
Enzyme 14 Synonyms
  1. Growth suppressor 1
  2. Leucine- and proline-enriched proteoglycan 1
  3. Leprecan-1
Enzyme 14 Gene Name LEPRE1
Enzyme 14 Protein Sequence >Prolyl 3-hydroxylase 1
MAVRALKLLTTLLAVVAAASQAEVESEAGWGMVTPDLLFAEGTAAYARGDWPGVVLSMER
ALRSRAALRALRLRCRTQCAADFPWELDPDWSPSPAQASGAAALRDLSFFGGLLRRAACL
RRCLGPPAAHSLSEEMELEFRKRSPYNYLQVAYFKINKLEKAVAAAHTFFVGNPEHMEMQ
QNLDYYQTMSGVKEADFKDLETQPHMQEFRLGVRLYSEEQPQEAVPHLEAALQEYFVAYE
ECRALCEGPYDYDGYNYLEYNADLFQAITDHYIQVLNCKQNCVTELASHPSREKPFEDFL
PSHYNYLQFAYYNIGNYTQAVECAKTYLLFFPNDEVMNQNLAYYAAMLGEEHTRSIGPRE
SAKEYRQRSLLEKELLFFAYDVFGIPFVDPDSWTPEEVIPKRLQEKQKSERETAVRISQE
IGNLMKEIETLVEEKTKESLDVSRLTREGGPLLYEGISLTMNSKLLNGSQRVVMDGVISD
HECQELQRLTNVAATSGDGYRGQTSPHTPNEKFYGVTVFKALKLGQEGKVPLQSAHLYYN
VTEKVRRIMESYFRLDTPLYFSYSHLVCRTAIEEVQAERKDDSHPVHVDNCILNAETLVC
VKEPPAYTFRDYSAILYLNGDFDGGNFYFTELDAKTVTAEVQPQCGRAVGFSSGTENPHG
VKAVTRGQRCAIALWFTLDPRHSERDRVQADDLVKMLFSPEEMDLSQEQPLDAQQGPPEP
AQESLSGSESKPKDEL
Enzyme 14 Number of Residues 736
Enzyme 14 Molecular Weight 83393.2
Enzyme 14 Theoretical pI 4.79
Enzyme 14 GO Classification
Function
  • L-ascorbic acid binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
  • transition metal ion binding
  • vitamin binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 14 General Function Involved in oxidoreductase activity
Enzyme 14 Specific Function Basement membrane-associated chondroitin sulfate proteoglycan (CSPG). Has prolyl 3-hydroxylase activity catalyzing the post-translational formation of 3-hydroxyproline in -Xaa-Pro- Gly- sequences in collagens, especially types IV and V. May be involved in the secretory pathway of cells. Has growth suppressive activity in fibroblasts
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions
  • procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-3-hydroxy-L-proline + succinate + CO2 [RN:R03218]
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • 1-22
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 186928835 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID Q32P28 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name P3H1_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >2211 bp
ATGGCGGTACGCGCGTTGAAGCTGCTGACCACACTGCTGGCTGTCGTGGCCGCTGCCTCC
CAAGCCGAGGTCGAGTCCGAGGCAGGATGGGGCATGGTGACGCCTGATCTGCTCTTCGCC
GAGGGGACCGCAGCCTACGCGCGCGGGGACTGGCCCGGGGTGGTCCTGAGCATGGAACGG
GCGCTGCGCTCCCGGGCAGCCCTCCGCGCCCTTCGCCTGCGCTGCCGCACCCAGTGTGCC
GCCGACTTCCCGTGGGAGCTGGACCCCGACTGGTCCCCCAGCCCGGCCCAGGCCTCGGGC
GCCGCCGCCCTGCGCGACCTGAGCTTCTTCGGGGGCCTTCTGCGTCGCGCTGCCTGCCTG
CGCCGCTGCCTCGGGCCGCCGGCCGCCCACTCGCTCAGCGAAGAGATGGAGCTGGAGTTC
CGCAAGCGGAGCCCCTACAACTACCTGCAGGTCGCCTACTTCAAGATCAACAAGTTGGAG
AAAGCTGTTGCTGCAGCACACACCTTCTTCGTGGGCAATCCTGAGCACATGGAAATGCAG
CAGAACCTAGACTATTACCAAACCATGTCTGGAGTGAAGGAGGCCGACTTCAAGGATCTT
GAGACTCAACCCCATATGCAAGAATTTCGACTGGGAGTGCGACTCTACTCAGAGGAACAG
CCACAGGAAGCTGTGCCCCACCTAGAGGCGGCGCTGCAAGAATACTTTGTGGCCTATGAG
GAGTGCCGTGCCCTCTGCGAAGGGCCCTATGACTACGATGGCTACAACTACCTTGAGTAC
AACGCTGACCTCTTCCAGGCCATCACAGATCATTACATCCAGGTCCTCAACTGTAAGCAG
AACTGTGTCACGGAGCTTGCTTCCCACCCAAGTCGAGAGAAGCCCTTTGAAGACTTCCTC
CCATCGCATTATAATTATCTGCAGTTTGCCTACTATAACATTGGGAATTATACACAGGCT
GTTGAATGTGCCAAGACCTATCTTCTCTTCTTCCCCAATGACGAGGTGATGAACCAAAAT
TTGGCCTATTATGCAGCTATGCTTGGAGAAGAACACACCAGATCCATCGGCCCCCGTGAG
AGTGCCAAGGAGTACCGACAGCGAAGCCTACTGGAAAAAGAACTGCTTTTCTTCGCTTAT
GATGTTTTTGGAATTCCCTTTGTGGATCCGGATTCATGGACTCCAGAAGAAGTGATTCCC
AAGAGATTGCAAGAGAAACAGAAGTCAGAACGGGAAACAGCCGTACGCATCTCCCAGGAG
ATTGGGAACCTTATGAAGGAAATCGAGACCCTTGTGGAAGAGAAGACCAAGGAGTCACTG
GATGTGAGCAGACTGACCCGGGAAGGTGGCCCCCTGCTGTATGAAGGCATCAGTCTCACC
ATGAACTCCAAACTCCTGAATGGTTCCCAGCGGGTGGTGATGGACGGCGTAATCTCTGAC
CACGAGTGTCAGGAGCTGCAGAGACTGACCAATGTGGCAGCAACCTCAGGAGATGGCTAC
CGGGGTCAGACCTCCCCACATACTCCCAATGAAAAGTTCTATGGTGTCACTGTCTTCAAA
GCCCTCAAGCTGGGGCAAGAAGGCAAAGTTCCTCTGCAGAGTGCCCACCTGTACTACAAC
GTGACGGAGAAGGTGCGGCGCATCATGGAGTCCTACTTCCGCCTGGATACGCCCCTCTAC
TTTTCCTACTCTCATCTGGTGTGCCGCACTGCCATCGAAGAGGTCCAGGCAGAGAGGAAG
GATGATAGTCATCCAGTCCACGTGGACAACTGCATCCTGAATGCCGAGACCCTCGTGTGT
GTCAAAGAGCCCCCAGCCTACACCTTCCGCGACTACAGCGCCATCCTTTACCTAAATGGG
GACTTCGATGGCGGAAACTTTTATTTCACTGAACTGGATGCCAAGACCGTGACGGCAGAG
GTGCAGCCTCAGTGTGGAAGAGCCGTGGGATTCTCTTCAGGCACTGAAAACCCACATGGA
GTGAAGGCTGTCACCAGGGGGCAGCGCTGTGCCATCGCCCTGTGGTTCACCCTGGACCCT
CGACACAGCGAGCGGGACAGGGTGCAGGCAGATGACCTGGTGAAGATGCTCTTCAGCCCA
GAAGAGATGGACCTCTCCCAGGAGCAGCCCCTGGATGCCCAGCAGGGCCCCCCCGAACCT
GCACAAGAGTCTCTCTCAGGCAGTGAATCGAAGCCCAAGGATGAGCTATGA
Enzyme 14 GenBank Gene ID NM_022356.3 Link Image
Enzyme 14 GeneCard ID LEPRE1 Link Image
Enzyme 14 GenAtlas ID LEPRE1 Link Image
Enzyme 14 HGNC ID HGNC:19316 Link Image
Enzyme 14 Chromosome Location 1
Enzyme 14 Locus 1p34.1
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Kaul SC, Sugihara T, Yoshida A, Nomura H, Wadhwa R: Gros1, a potential growth suppressor on chromosome 1: its identity to basement membrane-associated proteoglycan, leprecan. Oncogene. 2000 Jul 27;19(32):3576-83. [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. Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T: Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. DNA Res. 2005;12(2):117-26. [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. Cabral WA, Chang W, Barnes AM, Weis M, Scott MA, Leikin S, Makareeva E, Kuznetsova NV, Rosenbaum KN, Tifft CJ, Bulas DI, Kozma C, Smith PA, Eyre DR, Marini JC: Prolyl 3-hydroxylase 1 deficiency causes a recessive metabolic bone disorder resembling lethal/severe osteogenesis imperfecta. Nat Genet. 2007 Mar;39(3):359-65. Epub 2007 Feb 4. [PubMed Link Image]
  6. 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 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 14402
Enzyme 15 Name Prolyl 3-hydroxylase 2
Enzyme 15 Synonyms
  1. Leprecan-like protein 1
  2. Myxoid liposarcoma-associated protein 4
Enzyme 15 Gene Name LEPREL1
Enzyme 15 Protein Sequence >Prolyl 3-hydroxylase 2
MRERIWAPPLLLLLPLLLPPPLWGGPPDSPRRELELEPGPLQPFDLLYASGAAAYYSGDY
ERAVRDLEAALRSHRRLREIRTRCARHCAARHPLPPPPPGEGPGAELPLFRSLLGRARCY
RSCETQRLGGPASRHRVSEDVRSDFQRRVPYNYLQRAYIKLNQLEKAVEAAHTFFVANPE
HMEMQQNIENYRATAGVEALQLVDREAKPHMESYNAGVKHYEADDFEMAIRHFEQALREY
FVEDTECRTLCEGPQRFEEYEYLGYKAGLYEAIADHYMQVLVCQHECVRELATRPGRLSP
IENFLPLHYDYLQFAYYRVGEYVKALECAKAYLLCHPDDEDVLDNVDYYESLLDDSIDPA
SIEAREDLTMFVKRHKLESELIKSAAEGLGFSYTEPNYWIRYGGRQDENRVPSGVNVEGA
EVHGFSMGKKLSPKIDRDLREGGPLLYENITFVYNSEQLNGTQRVLLDNVLSEEQCRELH
SVASGIMLVGDGYRGKTSPHTPNEKFEGATVLKALKSGYEGRVPLKSARLFYDISEKARR
IVESYFMLNSTLYFSYTHMVCRTALSGQQDRRNDLSHPIHADNCLLDPEANECWKEPPAY
TFRDYSALLYMNDDFEGGEFIFTEMDAKTVTASIKPKCGRMISFSSGGENPHGVKAVTKG
KRCAVALWFTLDPLYRELERIQADEVIAILDQEQQGKHELNINPKDEL
Enzyme 15 Number of Residues 708
Enzyme 15 Molecular Weight 80983.7
Enzyme 15 Theoretical pI 5.47
Enzyme 15 GO Classification
Function
  • L-ascorbic acid binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
  • transition metal ion binding
  • vitamin binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 15 General Function Involved in oxidoreductase activity
Enzyme 15 Specific Function Has prolyl 3-hydroxylase activity catalyzing the post- translational formation of 3-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens, especially types IV and V
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions
  • procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-3-hydroxy-L-proline + succinate + CO2 [RN:R03218]
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • 1-24
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 27526730 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID Q8IVL5 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name P3H2_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >2127 bp
ATGCGGGAGCGCATCTGGGCGCCGCCGCTGCTGCTGCTGCTGCCGCTGCTACTGCCGCCG
CCACTGTGGGGCGGCCCCCCGGACAGCCCACGCCGGGAGCTGGAGCTGGAGCCCGGGCCT
CTGCAGCCCTTCGACCTGCTCTACGCCAGCGGCGCGGCCGCCTACTACAGCGGAGACTAC
GAGCGAGCGGTGCGCGACTTGGAAGCGGCGCTGCGCAGCCACCGGCGCCTGCGGGAAATC
CGCACGCGCTGTGCCCGCCACTGCGCGGCGCGCCACCCGCTCCCGCCCCCGCCCCCCGGC
GAGGGCCCCGGCGCTGAGCTGCCCCTTTTCCGCTCCTTGTTGGGGCGGGCGCGCTGTTAT
CGCAGCTGTGAGACCCAGCGCCTCGGGGGCCCCGCATCCCGCCACCGCGTCAGCGAGGAT
GTGCGCAGCGACTTCCAGCGCAGAGTGCCCTACAACTACCTGCAGCGGGCCTACATCAAG
CTTAACCAGCTCGAAAAAGCAGTGGAAGCAGCTCACACATTTTTCGTGGCTAACCCTGAG
CACATGGAAATGCAGCAGAACATTGAGAATTACAGGGCGACAGCTGGTGTTGAAGCATTG
CAGTTGGTAGACAGAGAAGCCAAGCCACACATGGAGAGTTACAATGCAGGAGTTAAACAT
TATGAGGCTGATGACTTTGAGATGGCTATCAGGCATTTCGAACAAGCCTTAAGAGAATAT
TTCGTTGAAGATACAGAATGCCGGACCCTATGTGAGGGGCCTCAGAGATTTGAAGAATAT
GAGTATTTAGGGTATAAGGCTGGTCTGTATGAAGCTATTGCAGATCACTACATGCAGGTG
CTTGTTTGTCAGCATGAATGTGTGAGGGAACTTGCCACCCGCCCTGGCCGCCTCTCTCCC
ATCGAGAATTTTCTTCCTCTGCACTATGATTACCTACAGTTTGCCTACTATCGAGTTGGT
GAGTATGTGAAAGCCCTGGAGTGTGCCAAAGCCTATCTTCTATGCCATCCAGATGATGAG
GATGTCCTAGACAATGTGGATTACTATGAGAGTCTGCTGGATGATAGCATTGACCCGGCA
TCCATTGAGGCCAGAGAGGATTTAACAATGTTTGTGAAACGTCATAAGCTGGAGTCTGAG
CTGATAAAATCAGCTGCAGAAGGTCTGGGGTTTTCATACACTGAACCGAATTATTGGATC
AGATATGGAGGACGACAGGATGAGAATCGGGTCCCTTCAGGAGTGAACGTAGAGGGAGCA
GAAGTTCATGGATTCTCAATGGGAAAAAAGCTATCACCCAAGATAGATCGAGACCTAAGA
GAAGGTGGTCCTCTACTCTATGAGAACATCACATTCGTCTACAACTCGGAGCAGCTGAAC
GGGACTCAGCGGGTTCTCCTGGATAACGTCCTGTCGGAAGAACAGTGCCGGGAGCTCCAC
AGCGTGGCCAGTGGAATCATGCTTGTTGGTGATGGATACAGAGGAAAAACTTCACCCCAT
ACACCCAATGAAAAGTTTGAAGGTGCAACTGTCCTGAAAGCACTCAAATCTGGTTATGAA
GGTCGAGTCCCACTGAAGAGCGCTCGTCTGTTTTATGACATCAGCGAAAAGGCTCGAAGG
ATTGTAGAATCTTATTTTATGCTGAACTCAACTCTGTATTTTTCCTATACACACATGGTC
TGCCGAACAGCCCTGTCTGGTCAGCAGGATAGAAGAAATGACCTCAGTCATCCCATCCAT
GCTGACAACTGTTTGTTGGATCCAGAGGCCAACGAATGCTGGAAGGAGCCTCCTGCTTAC
ACATTTCGAGACTATAGTGCTCTCCTATATATGAATGATGACTTTGAAGGAGGAGAATTC
ATATTCACAGAGATGGATGCTAAGACTGTGACTGCCTCTATAAAACCAAAATGTGGGCGC
ATGATCAGCTTCTCATCTGGAGGAGAGAACCCTCATGGGGTGAAGGCAGTCACCAAGGGA
AAGAGGTGTGCTGTGGCTCTGTGGTTCACCTTGGACCCACTTTATAGAGAATTGGAGCGA
ATACAGGCTGATGAAGTGATTGCAATTCTGGATCAAGAACAGCAAGGGAAGCATGAACTG
AATATCAACCCTAAAGATGAGCTATAA
Enzyme 15 GenBank Gene ID AJ430351 Link Image
Enzyme 15 GeneCard ID LEPREL1 Link Image
Enzyme 15 GenAtlas ID LEPREL1 Link Image
Enzyme 15 HGNC ID HGNC:19317 Link Image
Enzyme 15 Chromosome Location 3
Enzyme 15 Locus 3q28
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Thelin-Jarnum S, Lassen C, Panagopoulos I, Mandahl N, Aman P: Identification of genes differentially expressed in TLS-CHOP carrying myxoid liposarcomas. Int J Cancer. 1999 Sep 24;83(1):30-3. [PubMed Link Image]
  2. Jarnum S, Kjellman C, Darabi A, Nilsson I, Edvardsen K, Aman P: LEPREL1, a novel ER and Golgi resident member of the Leprecan family. Biochem Biophys Res Commun. 2004 Apr 30;317(2):342-51. [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. 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]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 14403
Enzyme 16 Name Prolyl 3-hydroxylase 3
Enzyme 16 Synonyms
  1. Leprecan-like protein 2
  2. Protein B
Enzyme 16 Gene Name LEPREL2
Enzyme 16 Protein Sequence >Prolyl 3-hydroxylase 3
MLRLLRPLLLLLLLPPPGSPEPPGLTQLSPGAPPQAPDLLYADGLRAYAAGAWAPAVALL
REALRSQAALGRVRLDCGASCAADPGAALPAVLLGAPEPDSGPGPTQGSWERQLLRAALR
RADCLTQCAARRLGPGGAARLRVGSALRDAFRRREPYNYLQRAYYQLKKLDLAAAAAHTF
FVANPMHLQMREDMAKYRRMSGVRPQSFRDLETPPHWAAYDTGLELLGRQEAGLALPRLE
EALQGSLAQMESCRADCEGPEEQQGAEEEEDGAASQGGLYEAIAGHWIQVLQCRQRCVGE
TATRPGRSFPVPDFLPNQLRRLHEAHAQVGNLSQAIENVLSVLLFYPEDEAAKRALNQYQ
AQLGEPRPGLGPREDIQRFILRSLGEKRQLYYAMEHLGTSFKDPDPWTPAALIPEALREK
LREDQEKRPWDHEPVKPKPLTYWKDVLLLEGVTLTQDSRQLNGSERAVLDGLLTPAECGV
LLQLAKDAAGAGARSGYRGRRSPHTPHERFEGLTVLKAAQLARAGTVGSQGAKLLLEVSE
RVRTLTQAYFSPERPLHLSFTHLVCRSAIEGEQEQRMDLSHPVHADNCVLDPDTGECWRE
PPAYTYRDYSGLLYLNDDFQGGDLFFTEPNALTVTARVRPRCGRLVAFSSGVENPHGVWA
VTRGRRCALALWHTWAPEHREQEWIEAKELLQESQEEEEEEEEEMPSKDPSPEPPSRRHQ
RVQDKTGRAPRVREEL
Enzyme 16 Number of Residues 736
Enzyme 16 Molecular Weight 81835.7
Enzyme 16 Theoretical pI 6.26
Enzyme 16 GO Classification
Function
  • L-ascorbic acid binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
  • transition metal ion binding
  • vitamin binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 16 General Function Involved in iron ion binding
Enzyme 16 Specific Function Has prolyl 3-hydroxylase activity catalyzing the post- translational formation of 3-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens, especially types IV and V
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions
  • procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-3-hydroxy-L-proline + succinate + CO2 [RN:R03218]
Enzyme 16 Pfam Domain Function Not Available
Enzyme 16 Signals
  • 1-20
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 27526728 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID Q8IVL6 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name P3H3_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >2211 bp
ATGCTCCGGCTCCTCCGGCCGCTGCTGCTACTGCTGCTGCTGCCTCCCCCGGGGTCCCCT
GAGCCCCCCGGCCTGACCCAGCTGTCCCCGGGGGCGCCCCCGCAGGCCCCCGACTTGCTC
TACGCTGACGGGCTGCGCGCCTACGCGGCCGGGGCTTGGGCGCCGGCCGTGGCGCTGCTG
CGGGAGGCGCTGCGGAGCCAGGCGGCGCTGGGCCGGGTGCGGCTGGATTGCGGGGCGAGC
TGCGCGGCCGATCCGGGCGCCGCGCTCCCCGCCGTGCTTCTCGGGGCCCCGGAGCCCGAC
TCCGGGCCGGGACCCACGCAGGGGTCCTGGGAGCGACAGCTTCTCCGTGCAGCGCTCCGC
CGCGCAGACTGCCTGACCCAGTGCGCAGCACGGAGGCTGGGCCCCGGGGGCGCGGCGCGG
CTTCGCGTGGGGAGCGCGCTCCGGGACGCCTTCCGCCGTCGGGAGCCCTACAACTACCTG
CAGAGGGCCTATTACCAGTTGAAGAAGCTGGATCTGGCAGCTGCGGCAGCACACACCTTC
TTTGTAGCAAACCCCATGCACCTGCAGATGCGGGAGGACATGGCTAAGTACAGACGAATG
TCGGGAGTTCGGCCCCAGAGCTTCCGGGACCTGGAGACGCCCCCACACTGGGCAGCCTAT
GACACTGGCCTGGAGCTACTGGGGCGCCAGGAGGCAGGACTGGCACTGCCCAGGCTAGAG
GAGGCTCTTCAGGGGAGCCTGGCCCAGATGGAGAGCTGCCGTGCTGACTGTGAGGGGCCT
GAGGAGCAGCAGGGGGCTGAAGAAGAGGAGGATGGGGCTGCGAGCCAGGGGGGCCTCTAT
GAGGCCATTGCAGGACACTGGATTCAGGTCCTGCAGTGCCGGCAACGCTGTGTGGGGGAA
ACAGCCACACGCCCTGGTCGCAGCTTCCCTGTCCCAGACTTCCTTCCCAACCAGCTGAGG
CGGCTACATGAGGCCCATGCTCAGGTGGGCAATCTGTCCCAGGCTATAGAAAATGTCCTG
AGTGTCCTGCTCTTCTACCCGGAGGATGAGGCTGCCAAGAGGGCTCTGAACCAGTACCAG
GCCCAGCTGGGAGAGCCGAGACCTGGCCTCGGACCCAGAGAGGACATCCAGCGCTTCATC
CTCCGATCCCTGGGGGAGAAGAGGCAGCTCTACTATGCCATGGAGCACCTGGGGACCAGC
TTCAAGGATCCTGACCCCTGGACCCCTGCAGCTCTCATCCCTGAGGCACTTAGAGAAAAG
CTCAGAGAGGATCAAGAGAAGAGGCCTTGGGACCATGAGCCCGTGAAGCCAAAGCCCTTG
ACCTACTGGAAGGATGTCCTTCTCCTGGAGGGTGTGACCTTGACCCAGGATTCCAGGCAG
CTGAATGGGTCGGAGCGGGCGGTGTTGGATGGGCTGCTCACCCCAGCCGAGTGTGGGGTG
CTGCTGCAGCTGGCTAAGGATGCAGCTGGGGCTGGAGCCAGGTCTGGCTATCGTGGTCGC
CGCTCCCCTCACACCCCCCATGAACGCTTCGAGGGGCTCACGGTGCTTAAGGCTGCGCAG
CTGGCCCGGGCTGGGACAGTGGGCAGTCAGGGTGCTAAGCTGCTTCTGGAGGTGAGCGAG
CGGGTGCGGACCTTGACCCAGGCCTACTTCTCCCCGGAACGGCCCCTGCATCTGTCCTTC
ACCCACCTGGTGTGCCGCAGCGCCATAGAAGGAGAGCAAGAGCAGCGCATGGACCTGAGT
CACCCAGTGCACGCAGACAACTGCGTCCTGGACCCTGACACGGGAGAGTGCTGGCGGGAG
CCCCCAGCCTACACCTATCGGGACTACAGCGGACTCCTCTACCTCAACGATGACTTCCAG
GGTGGGGACCTGTTCTTCACGGAGCCCAACGCCCTCACTGTCACGGCTCGGGTGCGTCCT
CGCTGTGGGCGCCTTGTGGCCTTCAGCTCCGGTGTCGAGAATCCCCATGGGGTGTGGGCC
GTGACTCGGGGACGGCGCTGTGCCCTGGCACTGTGGCACACGTGGGCACCTGAGCACAGG
GAGCAGGAGTGGATAGAAGCCAAAGAACTGCTGCAGGAGTCACAGGAGGAGGAGGAAGAG
GAAGAGGAAGAAATGCCCAGCAAAGACCCTTCCCCAGAGCCCCCTAGCCGCAGGCACCAG
AGGGTCCAAGACAAGACTGGAAGGGCACCTCGGGTTCGGGAGGAGCTGTGA
Enzyme 16 GenBank Gene ID AJ430349 Link Image
Enzyme 16 GeneCard ID LEPREL2 Link Image
Enzyme 16 GenAtlas ID LEPREL2 Link Image
Enzyme 16 HGNC ID HGNC:19318 Link Image
Enzyme 16 Chromosome Location 1
Enzyme 16 Locus 12q13
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Ansari-Lari MA, Muzny DM, Lu J, Lu F, Lilley CE, Spanos S, Malley T, Gibbs RA: A gene-rich cluster between the CD4 and triosephosphate isomerase genes at human chromosome 12p13. Genome Res. 1996 Apr;6(4):314-26. [PubMed Link Image]
  2. Ansari-Lari MA, Shen Y, Muzny DM, Lee W, Gibbs RA: Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination. Genome Res. 1997 Mar;7(3):268-80. [PubMed Link Image]
  3. Jarnum S, Kjellman C, Darabi A, Nilsson I, Edvardsen K, Aman P: LEPREL1, a novel ER and Golgi resident member of the Leprecan family. Biochem Biophys Res Commun. 2004 Apr 30;317(2):342-51. [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]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 14855
Enzyme 17 Name Prolyl 4-hydroxylase subunit alpha-3
Enzyme 17 Synonyms
  1. 4-PH alpha-3
  2. Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-3
Enzyme 17 Gene Name P4HA3
Enzyme 17 Protein Sequence >Prolyl 4-hydroxylase subunit alpha-3
MGPGARLAALLAVLALGTGDPERAAARGDTFSALTSVARALAPERRLLGLLRRYLRGEEA
RLRDLTRFYDKVLSLHEDSTTPVANPLLAFTLIKRLQSDWRNVVHSLEASENIRALKDGY
EKVEQDLPAFEDLEGAARALMRLQDVYMLNVKGLARGVFQRVTGSAITDLYSPKRLFSLT
GDDCFQVGKVAYDMGDYYHAIPWLEEAVSLFRGSYGEWKTEDEASLEDALDHLAFAYFRA
GNVSCALSLSREFLLYSPDNKRMARNVLKYERLLAESPNHVVAEAVIQRPNIPHLQTRDT
YEGLCQTLGSQPTLYQIPSLYCSYETNSNAYLLLQPIRKEVIHLEPYIALYHDFVSDSEA
QKIRELAEPWLQRSVVASGEKQLQVEYRISKSAWLKDTVDPKLVTLNHRIAALTGLDVRP
PYAEYLQVVNYGIGGHYEPHFDHATSPSSPLYRMKSGNRVATFMIYLSSVEAGGATAFIY
ANLSVPVVRNAALFWWNLHRSGEGDSDTLHAGCPVLVGDKWVANKWIHEYGQEFRRPCSS
SPED
Enzyme 17 Number of Residues 544
Enzyme 17 Molecular Weight 61125.7
Enzyme 17 Theoretical pI 6.46
Enzyme 17 GO Classification
Function
  • L-ascorbic acid binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
  • oxidoreductase activity, acting on single donors with incorporation of molecular oxygen
  • oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
  • peptidyl-proline dioxygenase activity
  • procollagen-proline 4-dioxygenase activity
  • procollagen-proline dioxygenase activity
  • transition metal ion binding
  • vitamin binding
Process
  • metabolic process
  • oxidation reduction
Component
  • endoplasmic reticulum
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • organelle
Enzyme 17 General Function Involved in oxidoreductase activity
Enzyme 17 Specific Function Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins
Enzyme 17 Pathways
Enzyme 17 Reactions
  • procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2 [RN:R03219]
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • 1-19
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 36962719 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID Q7Z4N8 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name P4HA3_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >1635 bp
ATGGGTCCTGGGGCGCGGCTGGCGGCGCTGCTGGCGGTGCTGGCGCTCGGGACAGGAGAC
CCAGAAAGGGCTGCGGCTCGGGGCGACACGTTCTCGGCGCTGACCAGCGTGGCGCGCGCC
CTGGCGCCCGAGCGCCGGCTGCTGGGGCTGCTGAGGCGGTACCTGCGCGGGGAGGAGGCG
CGGCTGCGGGACCTGACTAGATTCTACGACAAGGTACTTTCTTTGCATGAGGATTCAACA
ACCCCTGTGGCTAACCCTCTGCTTGCATTTACTCTCATCAAACGCCTGCAGTCTGACTGG
AGGAATGTGGTACATAGTCTGGAGGCCAGTGAGAACATCCGAGCTCTGAAGGATGGCTAT
GAGAAGGTGGAGCAAGACCTTCCAGCCTTTGAGGACCTTGAGGGAGCAGCAAGGGCCCTG
ATGCGGCTGCAGGACGTGTACATGCTCAATGTGAAAGGCCTGGCCCGAGGTGTCTTTCAG
AGAGTCACTGGCTCTGCCATCACTGACCTGTACAGCCCCAAACGGCTCTTTTCTCTCACA
GGGGATGACTGCTTCCAAGTTGGCAAGGTGGCCTATGACATGGGGGATTATTACCATGCC
ATTCCATGGCTGGAGGAGGCTGTCAGTCTCTTCCGAGGATCTTACGGAGAGTGGAAGACA
GAGGATGAGGCAAGTCTAGAAGATGCCTTGGATCACTTGGCCTTTGCTTATTTCCGGGCA
GGAAATGTTTCGTGTGCCCTCAGCCTCTCTCGGGAGTTTCTTCTCTACAGCCCAGATAAT
AAGAGGATGGCCAGGAATGTCTTGAAATATGAAAGGCTCTTGGCAGAGAGCCCCAACCAC
GTGGTAGCTGAGGCTGTCATCCAGAGGCCCAATATACCCCACCTGCAGACCAGAGACACC
TACGAGGGGCTATGTCAGACCCTGGGTTCCCAGCCCACTCTCTACCAGATCCCTAGCCTC
TACTGTTCCTATGAGACCAATTCCAACGCCTACCTGCTGCTCCAGCCCATCCGGAAGGAG
GTCATCCACCTGGAGCCCTACATTGCTCTCTACCATGACTTCGTCAGTGACTCAGAGGCT
CAGAAAATTAGAGAACTTGCAGAACCATGGCTACAGAGGTCAGTGGTGGCATCAGGGGAG
AAGCAGTTACAAGTGGAGTACCGCATCAGCAAAAGTGCCTGGCTGAAGGACACTGTTGAC
CCAAAACTGGTGACCCTCAACCACCGCATTGCTGCCCTCACAGGCCTTGATGTCCGGCCT
CCCTATGCAGAGTATCTGCAGGTGGTGAACTATGGCATCGGAGGACACTATGAGCCTCAC
TTTGACCATGCTACGTCACCAAGCAGCCCCCTCTACAGAATGAAGTCAGGAAACCGAGTT
GCAACATTTATGATCTATCTGAGCTCGGTGGAAGCTGGAGGAGCCACAGCCTTCATCTAT
GCCAACCTCAGCGTGCCTGTGGTTAGGAATGCAGCACTGTTTTGGTGGAACCTGCACAGG
AGTGGTGAAGGGGACAGTGACACACTTCATGCTGGCTGTCCTGTCCTGGTGGGAGATAAG
TGGGTGGCCAACAAGTGGATACATGAGTATGGACAGGAATTCCGCAGACCCTGCAGCTCC
AGCCCTGAAGACTGA
Enzyme 17 GenBank Gene ID AY313448 Link Image
Enzyme 17 GeneCard ID P4HA3 Link Image
Enzyme 17 GenAtlas ID P4HA3 Link Image
Enzyme 17 HGNC ID HGNC:30135 Link Image
Enzyme 17 Chromosome Location 1
Enzyme 17 Locus 11q13.4
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Kukkola L, Hieta R, Kivirikko KI, Myllyharju J: Identification and characterization of a third human, rat, and mouse collagen prolyl 4-hydroxylase isoenzyme. J Biol Chem. 2003 Nov 28;278(48):47685-93. Epub 2003 Sep 18. [PubMed Link Image]
  2. Van Den Diepstraten C, Papay K, Bolender Z, Brown A, Pickering JG: Cloning of a novel prolyl 4-hydroxylase subunit expressed in the fibrous cap of human atherosclerotic plaque. Circulation. 2003 Aug 5;108(5):508-11. Epub 2003 Jul 21. [PubMed Link Image]
  3. 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]
  4. 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]
  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]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 14992
Enzyme 18 Name Egl nine homolog 1
Enzyme 18 Synonyms
  1. Hypoxia-inducible factor prolyl hydroxylase 2
  2. HIF-PH2
  3. HIF-prolyl hydroxylase 2
  4. HPH-2
  5. Prolyl hydroxylase domain-containing protein 2
  6. PHD2
  7. SM-20
Enzyme 18 Gene Name EGLN1
Enzyme 18 Protein Sequence >Egl nine homolog 1
MANDSGGPGGPSPSERDRQYCELCGKMENLLRCSRCRSSFYCCKEHQRQDWKKHKLVCQG
SEGALGHGVGPHQHSGPAPPAAVPPPRAGAREPRKAAARRDNASGDAAKGKVKAKPPADP
AAAASPCRAAAGGQGSAVAAEAEPGKEEPPARSSLFQEKANLYPPSNTPGDALSPGGGLR
PNGQTKPLPALKLALEYIVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTDGQL
VSQKSDSSKDIRGDKITWIEGKEPGCETIGLLMSSMDDLIRHCNGKLGSYKINGRTKAMV
ACYPGNGTGYVRHVDNPNGDGRCVTCIYYLNKDWDAKVSGGILRIFPEGKAQFADIEPKF
DRLLFFWSDRRNPHEVQPAYATRYAITVWYFDADERARAKVKYLTGEKGVRVELNKPSDS
VGKDVF
Enzyme 18 Number of Residues 426
Enzyme 18 Molecular Weight 46020.6
Enzyme 18 Theoretical pI 8.66
Enzyme 18 GO Classification
Function
  • L-ascorbic acid binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
  • transition metal ion binding
  • vitamin binding
  • zinc ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 18 General Function Involved in oxidoreductase activity
Enzyme 18 Specific Function Catalyzes the post-translational formation of 4- hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates HIF-1 alpha at 'Pro-402' and 'Pro-564', and HIF-2 alpha. Functions as a cellular oxygen sensor and, under normoxic conditions, targets HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitination complex
Enzyme 18 Pathways Not Available
Enzyme 18 Reactions Not Available
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein Not Available
Enzyme 18 UniProtKB/Swiss-Prot ID Q9GZT9 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name EGLN1_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >1281 bp
ATGGCCAATGACAGCGGCGGGCCCGGCGGGCCGAGCCCGAGCGAGCGAGACCGGCAGTAC
TGCGAGCTGTGCGGGAAGATGGAGAACCTGCTGCGCTGCAGCCGCTGCCGCAGCTCCTTC
TACTGCTGCAAGGAGCACCAGCGTCAGGACTGGAAGAAGCACAAGCTCGTGTGCCAGGGC
AGCGAGGGCGCCCTCGGCCACGGAGTGGGCCCACACCAGCATTCCGGCCCCGCGCCGCCG
GCTGCAGTGCCGCCGCCCAGGGCCGGGGCCCGGGAGCCCAGGAAGGCAGCGGCGCGCCGG
GACAACGCCTCCGGGGACGCGGCCAAGGGAAAAGTAAAGGCCAAGCCCCCGGCCGACCCA
GCGGCGGCCGCGTCGCCGTGTCGTGCGGCCGCCGGCGGCCAGGGCTCGGCGGTGGCTGCC
GAAGCCGAGCCCGGCAAGGAGGAGCCGCCGGCCCGCTCATCGCTGTTCCAGGAGAAGGCG
AACCTGTACCCCCCAAGCAACACGCCCGGGGATGCGCTGAGCCCCGGCGGCGGCCTGCGG
CCCAACGGGCAGACGAAGCCCCTGCCGGCGCTGAAGCTGGCGCTCGAGTACATCGTGCCG
TGCATGAACAAGCACGGCATCTGTGTGGTGGACGACTTCCTCGGCAAGGAGACCGGACAG
CAGATCGGCGACGAGGTGCGCGCCCTGCACGACACCGGGAAGTTCACGGACGGGCAGCTG
GTCAGCCAGAAGAGTGACTCGTCCAAGGACATCCGAGGCGATAAGATCACCTGGATCGAG
GGCAAGGAGCCCGGCTGCGAAACCATTGGGCTGCTCATGAGCAGCATGGACGACCTGATA
CGCCACTGTAACGGGAAGCTGGGCAGCTACAAAATCAATGGCCGGACGAAAGCCATGGTT
GCTTGTTATCCGGGCAATGGAACGGGTTATGTACGTCATGTTGATAATCCAAATGGAGAT
GGAAGATGTGTGACATGTATATATTATCTTAATAAAGACTGGGATGCCAAGGTAAGTGGA
GGTATACTTCGAATTTTTCCAGAAGGCAAAGCCCAGTTTGCTGACATTGAACCCAAATTT
GATAGACTGCTGTTTTTCTGGTCTGACCGTCGCAACCCTCATGAAGTACAACCAGCATAT
GCTACAAGGTACGCAATAACTGTTTGGTATTTTGATGCAGATGAGAGAGCACGAGCTAAA
GTAAAATATCTAACAGGTGAAAAAGGTGTGAGGGTTGAACTCAATAAACCTTCAGATTCG
GTCGGTAAAGACGTCTTCTAG
Enzyme 18 GenBank Gene ID AF229245 Link Image
Enzyme 18 GeneCard ID EGLN1 Link Image
Enzyme 18 GenAtlas ID EGLN1 Link Image
Enzyme 18 HGNC ID HGNC:1232 Link Image
Enzyme 18 Chromosome Location 1
Enzyme 18 Locus 1q42.1
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Dupuy D, Aubert I, Duperat VG, Petit J, Taine L, Stef M, Bloch B, Arveiler B: Mapping, characterization, and expression analysis of the SM-20 human homologue, c1orf12, and identification of a novel related gene, SCAND2. Genomics. 2000 Nov 1;69(3):348-54. [PubMed Link Image]
  2. Taylor MS: Characterization and comparative analysis of the EGLN gene family. Gene. 2001 Sep 5;275(1):125-32. [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]
  4. 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]
  5. Semenza GL: HIF-1, O(2), and the 3 PHDs: how animal cells signal hypoxia to the nucleus. Cell. 2001 Oct 5;107(1):1-3. [PubMed Link Image]
  6. Epstein AC, Gleadle JM, McNeill LA, Hewitson KS, O'Rourke J, Mole DR, Mukherji M, Metzen E, Wilson MI, Dhanda A, Tian YM, Masson N, Hamilton DL, Jaakkola P, Barstead R, Hodgkin J, Maxwell PH, Pugh CW, Schofield CJ, Ratcliffe PJ: C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell. 2001 Oct 5;107(1):43-54. [PubMed Link Image]
  7. Ivan M, Haberberger T, Gervasi DC, Michelson KS, Gunzler V, Kondo K, Yang H, Sorokina I, Conaway RC, Conaway JW, Kaelin WG Jr: Biochemical purification and pharmacological inhibition of a mammalian prolyl hydroxylase acting on hypoxia-inducible factor. Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13459-64. Epub 2002 Sep 26. [PubMed Link Image]
  8. Oehme F, Ellinghaus P, Kolkhof P, Smith TJ, Ramakrishnan S, Hutter J, Schramm M, Flamme I: Overexpression of PH-4, a novel putative proline 4-hydroxylase, modulates activity of hypoxia-inducible transcription factors. Biochem Biophys Res Commun. 2002 Aug 16;296(2):343-9. [PubMed Link Image]
  9. Cioffi CL, Liu XQ, Kosinski PA, Garay M, Bowen BR: Differential regulation of HIF-1 alpha prolyl-4-hydroxylase genes by hypoxia in human cardiovascular cells. Biochem Biophys Res Commun. 2003 Apr 11;303(3):947-53. [PubMed Link Image]
  10. Ozer A, Wu LC, Bruick RK: The candidate tumor suppressor ING4 represses activation of the hypoxia inducible factor (HIF). Proc Natl Acad Sci U S A. 2005 May 24;102(21):7481-6. Epub 2005 May 16. [PubMed Link Image]
  11. 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]
  12. McDonough MA, Li V, Flashman E, Chowdhury R, Mohr C, Lienard BM, Zondlo J, Oldham NJ, Clifton IJ, Lewis J, McNeill LA, Kurzeja RJ, Hewitson KS, Yang E, Jordan S, Syed RS, Schofield CJ: Cellular oxygen sensing: Crystal structure of hypoxia-inducible factor prolyl hydroxylase (PHD2). Proc Natl Acad Sci U S A. 2006 Jun 27;103(26):9814-9. Epub 2006 Jun 16. [PubMed Link Image]
  13. Percy MJ, Zhao Q, Flores A, Harrison C, Lappin TR, Maxwell PH, McMullin MF, Lee FS: A family with erythrocytosis establishes a role for prolyl hydroxylase domain protein 2 in oxygen homeostasis. Proc Natl Acad Sci U S A. 2006 Jan 17;103(3):654-9. Epub 2006 Jan 9. [PubMed Link Image]
  14. Percy MJ, Furlow PW, Beer PA, Lappin TR, McMullin MF, Lee FS: A novel erythrocytosis-associated PHD2 mutation suggests the location of a HIF binding groove. Blood. 2007 Sep 15;110(6):2193-6. Epub 2007 Jun 19. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 14993
Enzyme 19 Name Egl nine homolog 2
Enzyme 19 Synonyms
  1. Estrogen-induced tag 6
  2. HPH-3
  3. Hypoxia-inducible factor prolyl hydroxylase 1
  4. HIF-PH1
  5. HIF-prolyl hydroxylase 1
  6. HPH-1
  7. Prolyl hydroxylase domain-containing protein 1
  8. PHD1
Enzyme 19 Gene Name EGLN2
Enzyme 19 Protein Sequence >Egl nine homolog 2
MDSPCQPQPLSQALPQLPGSSSEPLEPEPGRARMGVESYLPCPLLPSYHCPGVPSEASAG
SGTPRATATSTTASPLRDGFGGQDGGELRPLQSEGAAALVTKGCQRLAAQGARPEAPKRK
WAEDGGDAPSPSKRPWARQENQEAEREGGMSCSCSSGSGEASAGLMEEALPSAPERLALD
YIVPCMRYYGICVKDSFLGAALGGRVLAEVEALKRGGRLRDGQLVSQRAIPPRSIRGDQI
AWVEGHEPGCRSIGALMAHVDAVIRHCAGRLGSYVINGRTKAMVACYPGNGLGYVRHVDN
PHGDGRCITCIYYLNQNWDVKVHGGLLQIFPEGRPVVANIEPLFDRLLIFWSDRRNPHEV
KPAYATRYAITVWYFDAKERAAAKDKYQLASGQKGVQVPVSQPPTPT
Enzyme 19 Number of Residues 407
Enzyme 19 Molecular Weight 43650.0
Enzyme 19 Theoretical pI 7.97
Enzyme 19 GO Classification
Function
  • L-ascorbic acid binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
  • transition metal ion binding
  • vitamin binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 19 General Function Involved in oxidoreductase activity
Enzyme 19 Specific Function Catalyzes the post-translational formation of 4- hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates HIF-1 alpha at 'Pro-402' and 'Pro-564', and HIF-2 alpha. Functions as a cellular oxygen sensor and, under normoxic conditions, targets HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. May play a role in cell growth regulation. Isoform p40 and isoform p43 exhibit the same level of activity
Enzyme 19 Pathways Not Available
Enzyme 19 Reactions Not Available
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 14547148 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q96KS0 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name EGLN2_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >1224 bp
ATGGACAGCCCGTGCCAGCCGCAGCCCCTAAGTCAGGCTCTCCCTCAGTTACCAGGGTCT
TCGTCAGAGCCCTTGGAGCCTGAGCCTGGCCGGGCCAGGATGGGAGTGGAGAGTTACCTG
CCCTGTCCCCTGCTCCCCTCCTACCACTGTCCAGGAGTGCCTAGTGAGGCCTCGGCAGGG
AGTGGGACCCCCAGAGCCACAGCCACCTCTACCACTGCCAGCCCTCTTCGGGACGGTTTT
GGCGGGCAGGATGGTGGTGAGCTGCGGCCGCTGCAGAGTGAAGGCGCTGCAGCGCTGGTC
ACCAAGGGGTGCCAGCGATTGGCAGCCCAGGGCGCACGGCCTGAGGCCCCCAAACGGAAA
TGGGCCGAGGATGGTGGGGATGCCCCTTCACCCAGCAAACGGCCCTGGGCCAGGCAAGAG
AACCAGGAGGCAGAGCGGGAGGGTGGCATGAGCTGCAGCTGCAGCAGTGGCAGTGGTGAG
GCCAGTGCTGGGCTGATGGAGGAGGCGCTGCCCTCTGCGCCCGAGCGCCTGGCCCTGGAC
TATATCGTGCCCTGCATGCGGTACTACGGCATCTGCGTCAAGGACAGCTTCCTGGGGGCA
GCACTGGGCGGTCGCGTGCTGGCCGAGGTGGAGGCCCTCAAACGGGGTGGGCGCCTGCGA
GACGGGCAGCTAGTGAGCCAGAGGGCGATCCCGCCGCGCAGCATCCGTGGGGACCAGATT
GCCTGGGTGGAAGGCCATGAACCAGGCTGTCGAAGCATTGGTGCCCTCATGGCCCATGTG
GACGCCGTCATCCGCCACTGCGCAGGGCGGCTGGGCAGCTATGTCATCAACGGGCGCACC
AAGGCCATGGTGGCGTGTTACCCAGGCAACGGGCTCGGGTACGTAAGGCACGTTGACAAT
CCCCACGGCGATGGGCGCTGCATCACCTGTATCTATTACCTGAATCAGAACTGGGACGTT
AAGGTGCATGGCGGCCTGCTGCAGATCTTCCCTGAGGGCCGGCCCGTGGTAGCCAACATC
GAGCCACTCTTTGACCGGTTGCTCATTTTCTGGTCTGACCGGCGGAACCCCCACGAGGTG
AAGCCAGCCTATGCCACCAGGTACGCCATCACTGTCTGGTATTTTGATGCCAAGGAGCGG
GCAGCAGCCAAAGACAAGTATCAGCTAGCATCAGGACAGAAAGGTGTCCAAGTACCTGTA
TCACAGCCGCCTACGCCCACCTAG
Enzyme 19 GenBank Gene ID AJ310544 Link Image
Enzyme 19 GeneCard ID EGLN2 Link Image
Enzyme 19 GenAtlas ID EGLN2 Link Image
Enzyme 19 HGNC ID HGNC:14660 Link Image
Enzyme 19 Chromosome Location 1
Enzyme 19 Locus 19q13.2
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Taylor MS: Characterization and comparative analysis of the EGLN gene family. Gene. 2001 Sep 5;275(1):125-32. [PubMed Link Image]
  2. Seth P, Krop I, Porter D, Polyak K: Novel estrogen and tamoxifen induced genes identified by SAGE (Serial Analysis of Gene Expression). Oncogene. 2002 Jan 24;21(5):836-43. [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. 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]
  5. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [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. Semenza GL: HIF-1, O(2), and the 3 PHDs: how animal cells signal hypoxia to the nucleus. Cell. 2001 Oct 5;107(1):1-3. [PubMed Link Image]
  8. Epstein AC, Gleadle JM, McNeill LA, Hewitson KS, O'Rourke J, Mole DR, Mukherji M, Metzen E, Wilson MI, Dhanda A, Tian YM, Masson N, Hamilton DL, Jaakkola P, Barstead R, Hodgkin J, Maxwell PH, Pugh CW, Schofield CJ, Ratcliffe PJ: C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell. 2001 Oct 5;107(1):43-54. [PubMed Link Image]
  9. Oehme F, Ellinghaus P, Kolkhof P, Smith TJ, Ramakrishnan S, Hutter J, Schramm M, Flamme I: Overexpression of PH-4, a novel putative proline 4-hydroxylase, modulates activity of hypoxia-inducible transcription factors. Biochem Biophys Res Commun. 2002 Aug 16;296(2):343-9. [PubMed Link Image]
  10. McNeill LA, Hewitson KS, Gleadle JM, Horsfall LE, Oldham NJ, Maxwell PH, Pugh CW, Ratcliffe PJ, Schofield CJ: The use of dioxygen by HIF prolyl hydroxylase (PHD1). Bioorg Med Chem Lett. 2002 Jun 17;12(12):1547-50. [PubMed Link Image]
  11. Tian YM, Mole DR, Ratcliffe PJ, Gleadle JM: Characterization of different isoforms of the HIF prolyl hydroxylase PHD1 generated by alternative initiation. Biochem J. 2006 Jul 1;397(1):179-86. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 14994
Enzyme 20 Name Egl nine homolog 3
Enzyme 20 Synonyms
  1. HPH-1
  2. Hypoxia-inducible factor prolyl hydroxylase 3
  3. HIF-PH3
  4. HIF-prolyl hydroxylase 3
  5. HPH-3
  6. Prolyl hydroxylase domain-containing protein 3
  7. PHD3
Enzyme 20 Gene Name EGLN3
Enzyme 20 Protein Sequence >Egl nine homolog 3
MPLGHIMRLDLEKIALEYIVPCLHEVGFCYLDNFLGEVVGDCVLERVKQLHCTGALRDGQ
LAGPRAGVSKRHLRGDQITWIGGNEEGCEAISFLLSLIDRLVLYCGSRLGKYYVKERSKA
MVACYPGNGTGYVRHVDNPNGDGRCITCIYYLNKNWDAKLHGGILRIFPEGKSFIADVEP
IFDRLLFFWSDRRNPHEVQPSYATRYAMTVWYFDAEERAEAKKKFRNLTRKTESALTED
Enzyme 20 Number of Residues 239
Enzyme 20 Molecular Weight 27261.1
Enzyme 20 Theoretical pI 7.70
Enzyme 20 GO Classification
Function
  • L-ascorbic acid binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
  • transition metal ion binding
  • vitamin binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 20 General Function Involved in oxidoreductase activity
Enzyme 20 Specific Function Catalyzes the post-translational formation of 4- hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates HIF-1 alpha at 'Pro-564', and HIF-2 alpha. Functions as a cellular oxygen sensor and, under normoxic conditions, targets HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. May play a role in cell growth regulation in muscle cells and in apoptosis in neuronal tissue. Promotes cell death through a caspase-dependent mechanism
Enzyme 20 Pathways Not Available
Enzyme 20 Reactions Not Available
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 14547150 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID Q9H6Z9 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name EGLN3_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >720 bp
ATGCCCCTGGGACACATCATGAGGCTGGACCTGGAGAAAATTGCCCTGGAGTACATCGTG
CCCTGTCTGCACGAGGTGGGCTTCTGCTACCTGGACAACTTCCTGGGCGAGGTGGTGGGC
GACTGCGTCCTGGAGCGCGTCAAGCAGCTGCACTGCACCGGGGCCCTGCGGGACGGCCAG
CTGGCGGGGCCGCGCGCCGGCGTCTCCAAGCGACACCTGCGGGGCGACCAGATCACGTGG
ATCGGGGGCAACGAGGAGGGCTGCGAGGCCATCAGCTTCCTCCTGTCCCTCATCGACAGG
CTGGTCCTCTACTGCGGGAGCCGGCTGGGCAAATACTACGTCAAGGAGAGGTCTAAGGCA
ATGGTGGCTTGCTATCCGGGAAATGGAACAGGTTATGTTCGCCACGTGGACAACCCCAAC
GGTGATGGTCGCTGCATCACCTGCATCTACTATCTGAACAAGAATTGGGATGCCAAGCTA
CATGGTGGGATCCTGCGGATATTTCCAGAGGGGAAATCATTCATAGCAGATGTGGAGCCC
ATTTTTGACAGACTCCTGTTCTTCTGGTCAGATCGTAGGAACCCACACGAAGTGCAGCCC
TCTTACGCAACCAGATATGCTATGACTGTCTGGTACTTTGATGCTGAAGAAAGGGCAGAA
GCCAAAAAGAAATTCAGGAATTTAACTAGGAAAACTGAATCTGCCCTCACTGAAGACTGA
Enzyme 20 GenBank Gene ID AJ310545 Link Image
Enzyme 20 GeneCard ID EGLN3 Link Image
Enzyme 20 GenAtlas ID EGLN3 Link Image
Enzyme 20 HGNC ID HGNC:14661 Link Image
Enzyme 20 Chromosome Location 1
Enzyme 20 Locus 14q13.1
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Taylor MS: Characterization and comparative analysis of the EGLN gene family. Gene. 2001 Sep 5;275(1):125-32. [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. Epstein AC, Gleadle JM, McNeill LA, Hewitson KS, O'Rourke J, Mole DR, Mukherji M, Metzen E, Wilson MI, Dhanda A, Tian YM, Masson N, Hamilton DL, Jaakkola P, Barstead R, Hodgkin J, Maxwell PH, Pugh CW, Schofield CJ, Ratcliffe PJ: C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell. 2001 Oct 5;107(1):43-54. [PubMed Link Image]
  5. Semenza GL: HIF-1, O(2), and the 3 PHDs: how animal cells signal hypoxia to the nucleus. Cell. 2001 Oct 5;107(1):1-3. [PubMed Link Image]
  6. Bruick RK, McKnight SL: A conserved family of prolyl-4-hydroxylases that modify HIF. Science. 2001 Nov 9;294(5545):1337-40. Epub 2001 Oct 11. [PubMed Link Image]
  7. Oehme F, Ellinghaus P, Kolkhof P, Smith TJ, Ramakrishnan S, Hutter J, Schramm M, Flamme I: Overexpression of PH-4, a novel putative proline 4-hydroxylase, modulates activity of hypoxia-inducible transcription factors. Biochem Biophys Res Commun. 2002 Aug 16;296(2):343-9. [PubMed Link Image]
  8. Cioffi CL, Liu XQ, Kosinski PA, Garay M, Bowen BR: Differential regulation of HIF-1 alpha prolyl-4-hydroxylase genes by hypoxia in human cardiovascular cells. Biochem Biophys Res Commun. 2003 Apr 11;303(3):947-53. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 14995
Enzyme 21 Name Transmembrane prolyl 4-hydroxylase
Enzyme 21 Synonyms
  1. P4H-TM
  2. Hypoxia-inducible factor prolyl hydroxylase 4
  3. HIF-PH4
  4. HIF-prolyl hydroxylase 4
  5. HPH-4
Enzyme 21 Gene Name P4HTM
Enzyme 21 Protein Sequence >Transmembrane prolyl 4-hydroxylase
MAAAAVTGQRPETAAAEEASRPQWAPPDHCQAQAAAGLGDGEDAPVRPLCKPRGICSRAY
FLVLMVFVHLYLGNVLALLLFVHYSNGDESSDPGPQHRAQGPGPEPTLGPLTRLEGIKVG
HERKVQLVTDRDHFIRTLSLKPLLFEIPGFLTDEECRLIIHLAQMKGLQRSQILPTEEYE
EAMSTMQVSQLDLFRLLDQNRDGHLQLREVLAQTRLGNGWWMTPESIQEMYAAIKADPDG
DGVLSLQEFSNMDLRDFHKYMRSHKAESSELVRNSHHTWLYQGEGAHHIMRAIRQRVLRL
TRLSPEIVELSEPLQVVRYGEGGHYHAHVDSGPVYPETICSHTKLVANESVPFETSCRYM
TVLFYLNNVTGGGETVFPVADNRTYDEMSLIQDDVDLRDTRRHCDKGNLRVKPQQGTAVF
WYNYLPDGQGWVGDVDDYSLHGGCLVTRGTKWIANNWINVDPSRARQALFQQEMARLARE
GGTDSQPEWALDRAYRDARVEL
Enzyme 21 Number of Residues 502
Enzyme 21 Molecular Weight 56660.5
Enzyme 21 Theoretical pI 5.99
Enzyme 21 GO Classification
Function
  • L-ascorbic acid binding
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
  • transition metal ion binding
  • vitamin binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 21 General Function Involved in calcium ion binding
Enzyme 21 Specific Function Catalyzes the post-translational formation of 4- hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates HIF1A at 'Pro-402' and 'Pro-564'. May function as a cellular oxygen sensor and, under normoxic conditions, may target HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitination complex
Enzyme 21 Pathways Not Available
Enzyme 21 Reactions Not Available
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • 61-81
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 29570771 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q9NXG6 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name P4HTM_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >1509 bp
ATGGCGGCAGCGGCGGTGACAGGCCAGCGGCCTGAGACCGCGGCGGCCGAGGAGGCCTCG
AGGCCGCAGTGGGCGCCGCCAGACCACTGCCAGGCTCAGGCGGCGGCCGGGCTGGGCGAC
GGCGAGGACGCACCGGTGCGTCCGCTGTGCAAGCCCCGCGGCATCTGCTCGCGCGCCTAC
TTCCTGGTGCTGATGGTGTTCGTGCACCTGTACCTGGGTAACGTGCTGGCGCTGCTGCTC
TTCGTGCACTACAGCAACGGCGACGAAAGCAGCGATCCCGGGCCCCAACACCGTGCCCAG
GGCCCCGGGCCCGAGCCCACCTTAGGTCCCCTCACCCGGCTGGAGGGCATCAAGGTGGGG
CACGAGCGTAAGGTCCAGCTGGTCACCGACAGGGATCACTTCATCCGAACCCTCAGCCTC
AAGCCGCTGCTCTTCGAAATCCCCGGCTTCCTGACTGATGAAGAGTGTCGGCTCATCATC
CATCTGGCGCAGATGAAGGGGTTACAGCGCAGCCAGATCCTGCCTACTGAAGAGTATGAA
GAGGCAATGAGCACTATGCAGGTCAGCCAGCTGGACCTCTTCCGGCTGCTGGACCAGAAC
CGTGATGGGCACCTTCAGCTCCGTGAGGTTCTGGCCCAGACTCGCCTGGGAAATGGATGG
TGGATGACTCCAGAGAGCATTCAGGAGATGTACGCCGCGATCAAGGCTGACCCTGATGGT
GACGGAGTGCTGAGTCTGCAGGAGTTCTCCAACATGGACCTTCGGGACTTCCACAAGTAC
ATGAGGAGCCACAAGGCAGAGTCCAGTGAGCTGGTGCGGAACAGCCACCATACCTGGCTC
TACCAGGGTGAGGGTGCCCACCACATCATGCGTGCCATCCGCCAGAGGGTGCTGCGCCTC
ACTCGCCTGTCGCCTGAGATCGTGGAGCTCAGCGAGCCGCTGCAGGTTGTTCGATATGGT
GAGGGGGGCCACTACCATGCCCACGTGGACAGTGGGCCTGTGTACCCAGAGACCATCTGC
TCCCATACCAAGCTGGTAGCCAACGAGTCTGTACCCTTCGAGACCTCCTGCCGCTACATG
ACAGTGCTGTTTTATTTGAACAACGTCACTGGTGGGGGCGAGACTGTTTTCCCTGTAGCA
GATAACAGAACCTACGATGAAATGAGTCTGATTCAGGATGACGTGGACCTCCGTGACACA
CGGAGGCACTGTGACAAGGGAAACCTGCGTGTCAAGCCCCAACAGGGCACAGCAGTCTTC
TGGTACAACTACCTGCCTGATGGGCAAGGTTGGGTGGGTGACGTAGACGACTACTCGCTG
CACGGGGGCTGCCTGGTCACGCGCGGCACCAAGTGGATTGCCAACAACTGGATTAATGTG
GACCCCAGCCGAGCGCGGCAAGCGCTGTTCCAACAGGAGATGGCCCGCCTTGCCCGAGAA
GGGGGCACCGACTCACAGCCCGAGTGGGCTCTGGACCGGGCCTACCGCGATGCGCGCGTG
GAACTCTGA
Enzyme 21 GenBank Gene ID NM_177939.2 Link Image
Enzyme 21 GeneCard ID P4HTM Link Image
Enzyme 21 GenAtlas ID P4HTM Link Image
Enzyme 21 HGNC ID HGNC:28858 Link Image
Enzyme 21 Chromosome Location 3
Enzyme 21 Locus 3p21.31
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Oehme F, Ellinghaus P, Kolkhof P, Smith TJ, Ramakrishnan S, Hutter J, Schramm M, Flamme I: Overexpression of PH-4, a novel putative proline 4-hydroxylase, modulates activity of hypoxia-inducible transcription factors. Biochem Biophys Res Commun. 2002 Aug 16;296(2):343-9. [PubMed Link Image]
  2. 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]
  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. 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]
  5. Koivunen P, Tiainen P, Hyvarinen J, Williams KE, Sormunen R, Klaus SJ, Kivirikko KI, Myllyharju J: An endoplasmic reticulum transmembrane prolyl 4-hydroxylase is induced by hypoxia and acts on hypoxia-inducible factor alpha. J Biol Chem. 2007 Oct 19;282(42):30544-52. Epub 2007 Aug 27. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 15080
Enzyme 22 Name cDNA FLJ75964, highly similar to Homo sapiens prolyl-tRNA synthetase (mitochondrial)(putative) (PARS2), mRNA (Prolyl-tRNA synthetase (Mitochondrial)(Putative))
Enzyme 22 Synonyms Not Available
Enzyme 22 Gene Name PARS2
Enzyme 22 Protein Sequence >cDNA FLJ75964, highly similar to Homo sapiens prolyl-tRNA synthetase (mitochondrial)(putative) (PARS2), mRNA (Prolyl-tRNA synthetase (Mitochondrial)(Putative))
MEGLLTRCRALPALATCSRQLSGYVPCRFHHCAPRRGRRLLLSRVFQPQNLREDRVLSLQ
DKSDDLTCKSQRLMLQVGLIYPASPGCYHLLPYTVRAMEKLVRVIDQEMQAIGGQKVNMP
SLSPAELWQATNRWDLMGKELLRLRDRHGKEYCLGPTHEEAITALIASQKKLSYKQLPFL
LYQVTRKFRDEPRPRFGLLRGREFYMKDMYTFDSSPEAAQQTYSLVCDAYCSLFNKLGLP
FVKVQADVGTIGGTVSHEFQLPVDIGEDRLAICPRCSFSANMETLDLSQMNCPACQGPLT
KTKGIEVGHTFYLGTKYSSIFNAQFTNVCGKPTLAEMGCYGLGVTRILAAAIEVLSTEDC
VRWPSLLAPYQACLIPPKKGSKEQAASELIGQLYDHITEAVPQLHGEVLLDDRTHLTIGN
RLKDANKFGYPFVIIAGKRALEDPAHFEVWCQNTGEVAFLTKDGVMDLLTPVQTV
Enzyme 22 Number of Residues 475
Enzyme 22 Molecular Weight 53263
Enzyme 22 Theoretical pI 8.17
Enzyme 22 GO Classification Not Available
Enzyme 22 General Function Translation, ribosomal structure and biogenesis
Enzyme 22 Specific Function Not Available
Enzyme 22 Pathways Not Available
Enzyme 22 Reactions Not Available
Enzyme 22 Pfam Domain Function Not Available
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 158260381 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID A8K0W4 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name A8K0W4_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >1428 bp
ATGGAAGGGCTGCTGACAAGATGCAGAGCATTGCCCGCCCTGGCCACCTGCAGCCGCCAG
CTCTCTGGGTATGTTCCTTGCAGGTTTCACCACTGTGCCCCAAGAAGAGGGCGGCGCCTG
CTGCTGTCTCGTGTGTTCCAGCCACAGAACCTTCGGGAAGACCGGGTGCTCTCCCTGCAG
GACAAATCTGATGACCTGACCTGTAAGAGCCAGCGGCTGATGCTGCAGGTGGGCCTGATC
TACCCAGCAAGCCCCGGCTGTTACCACCTCCTGCCATATACCGTCCGTGCCATGGAGAAG
CTCGTGCGAGTGATAGACCAGGAGATGCAGGCCATCGGGGGCCAGAAAGTCAACATGCCC
AGCCTCAGCCCGGCAGAGCTCTGGCAAGCCACCAACCGGTGGGACTTGATGGGCAAAGAG
CTGCTAAGACTTAGAGACAGGCATGGCAAGGAATACTGCTTAGGACCAACTCACGAGGAA
GCCATTACGGCCTTAATTGCCTCCCAGAAGAAACTGTCCTACAAGCAGCTTCCCTTCCTG
CTGTACCAAGTGACAAGGAAGTTTCGGGATGAGCCCAGGCCCCGCTTTGGTCTTCTCCGT
GGCCGAGAGTTTTACATGAAGGATATGTACACCTTTGACTCCTCCCCAGAGGCTGCCCAG
CAGACCTACAGCCTGGTGTGTGATGCCTACTGCAGCCTGTTCAACAAGCTAGGGCTGCCA
TTTGTCAAGGTCCAGGCCGATGTGGGCACCATCGGGGGCACAGTGTCTCATGAGTTCCAG
CTCCCAGTGGATATTGGAGAGGACCGGCTTGCCATCTGTCCCCGCTGCAGCTTCTCAGCC
AACATGGAGACACTAGACTTGTCACAAATGAACTGCCCTGCTTGCCAGGGCCCATTGACT
AAAACCAAAGGCATTGAGGTGGGGCACACATTTTACCTGGGTACCAAGTACTCATCCATT
TTCAATGCCCAGTTTACCAATGTCTGTGGCAAACCAACCCTGGCTGAAATGGGGTGCTAT
GGCTTGGGTGTGACACGGATCTTGGCTGCTGCCATTGAAGTCCTCTCTACAGAAGACTGT
GTCCGCTGGCCCAGCCTACTGGCCCCTTACCAAGCCTGCCTCATCCCCCCTAAGAAGGGC
AGTAAGGAGCAGGCGGCCTCCGAGCTCATAGGGCAGCTGTACGACCACATCACAGAGGCA
GTGCCTCAGCTTCACGGGGAGGTGCTCCTGGACGACAGGACCCATCTGACCATCGGAAAC
AGACTGAAAGATGCCAACAAGTTTGGCTACCCCTTTGTGATAATCGCTGGCAAGAGGGCC
CTGGAGGACCCTGCACATTTTGAGGTTTGGTGTCAGAACACTGGTGAGGTGGCCTTCCTC
ACCAAAGATGGAGTCATGGATTTACTGACCCCAGTGCAGACTGTCTAA
Enzyme 22 GenBank Gene ID AK289679 Link Image
Enzyme 22 GeneCard ID A8K0W4 Link Image
Enzyme 22 GenAtlas ID Not Available
Enzyme 22 HGNC ID Not Available
Enzyme 22 Chromosome Location Not Available
Enzyme 22 Locus Not Available
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References Not Available
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 16948
Enzyme 23 Name Probable proline racemase
Enzyme 23 Synonyms Not Available
Enzyme 23 Gene Name C14orf149
Enzyme 23 Protein Sequence >Probable proline racemase
MESALAVPRLPPHDPGTPVLSVVDMHTGGEPLRIVLAGCPEVSGPTLLAKRRYMRQHLDH
VRRRLMFEPRGHRDMYGAVLVPSELPDAHLGVLFLHNEGYSSMCGHAVLALGRFALDFGL
VPAPPAGTREARVNIHCPCGLVTAFVACEDGRSHGPVRFHSVPAFVLATDLMVDVPGHGK
VMVDIAYGGAFYAFVTAEKLGLDICSAKTRDLVDAASAVTEAVKAQFKINHPDSEDLAFL
YGTILTDGKDAYTKEPTTNICVFADEQVDRSPTGSGVTARIALQYHKGLLELNQMRAFKS
SATGSVFTGKAVREAKCGDFKAVIVEVSGQAHYTGTASFIIEDDDPLRDGFLLK
Enzyme 23 Number of Residues 354
Enzyme 23 Molecular Weight 38137.4
Enzyme 23 Theoretical pI 6.67
Enzyme 23 GO Classification
Function
  • amino-acid racemase activity
  • catalytic activity
  • isomerase activity
  • proline racemase activity
  • racemase and epimerase activity
  • racemase and epimerase activity, acting on amino acids and derivatives
Process
Component
Enzyme 23 General Function Involved in proline racemase activity
Enzyme 23 Specific Function Catalyzes the interconversion of L- and D-proline
Enzyme 23 Pathways Not Available
Enzyme 23 Reactions
  • L-proline = D-proline [RN:R01255]
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • None
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein Not Available
Enzyme 23 UniProtKB/Swiss-Prot ID Q96EM0 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name PRCM_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >1065 bp
ATGGAGAGCGCGCTGGCGGTGCCCCGGCTGCCCCCGCATGATCCAGGGACGCCGGTGCTG
TCGGTGGTGGACATGCACACGGGCGGCGAGCCCTTGCGTATCGTGCTGGCGGGGTGTCCG
GAGGTGTCTGGGCCCACCCTGCTGGCCAAGCGGCGCTACATGCGCCAGCACCTTGACCAC
GTGCGGCGACGGCTCATGTTCGAGCCCCGAGGGCACCGGGACATGTACGGGGCGGTCCTA
GTCCCGAGCGAGCTGCCGGACGCGCATCTGGGCGTCCTGTTCCTGCACAACGAGGGCTAC
AGCTCCATGTGCGGCCACGCAGTGCTGGCGCTGGGCCGCTTCGCTTTGGACTTCGGGCTT
GTGCCGGCGCCCCCTGCGGGCACCCGCGAGGCCCGCGTCAATATCCACTGCCCCTGCGGG
CTGGTGACCGCCTTCGTGGCATGCGAGGACGGCCGCAGCCACGGACCGGTGCGCTTCCAC
AGCGTCCCGGCCTTCGTGCTGGCCACAGATCTCATGGTGGATGTTCCTGGACATGGAAAG
GTGATGGTGGACATTGCATATGGCGGTGCATTTTATGCATTTGTTACTGCTGAAAAGTTA
GGACTAGACATTTGTTCTGCAAAGACCAGGGACCTTGTGGATGCAGCGAGTGCAGTGACA
GAGGCAGTGAAAGCTCAGTTTAAAATTAATCATCCTGATAGTGAAGACCTTGCCTTTTTA
TATGGAACTATATTAACAGATGGAAAAGATGCTTATACCAAGGAACCAACCACCAACATT
TGTGTTTTTGCAGATGAACAGGTTGACAGAAGTCCCACTGGCTCAGGAGTGACAGCCCGA
ATTGCCTTACAGTATCACAAAGGGCTTCTGGAACTGAACCAGATGAGAGCCTTCAAAAGC
AGTGCAACTGGCTCAGTATTCACAGGGAAAGCTGTGAGGGAAGCGAAATGTGGTGATTTT
AAAGCTGTTATAGTGGAAGTATCAGGACAAGCCCATTACACGGGTACAGCAAGCTTTATA
ATAGAAGATGACGACCCATTGAGGGATGGATTTCTTCTCAAGTGA
Enzyme 23 GenBank Gene ID AK058165 Link Image
Enzyme 23 GeneCard ID C14orf149 Link Image
Enzyme 23 GenAtlas ID C14orf149 Link Image
Enzyme 23 HGNC ID HGNC:20488 Link Image
Enzyme 23 Chromosome Location 1
Enzyme 23 Locus 14q23.1
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 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. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [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]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 16950
Enzyme 24 Name Peptidyl-prolyl cis-trans isomerase F, mitochondrial
Enzyme 24 Synonyms
  1. PPIase F
  2. Cyclophilin F
  3. Rotamase F
Enzyme 24 Gene Name PPIF
Enzyme 24 Protein Sequence >Peptidyl-prolyl cis-trans isomerase F, mitochondrial
MLALRCGSRWLGLLSVPRSVPLRLPAARACSKGSGDPSSSSSSGNPLVYLDVDANGKPLG
RVVLELKADVVPKTAENFRALCTGEKGFGYKGSTFHRVIPSFMCQAGDFTNHNGTGGKSI
YGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDV
VKKIESFGSKSGRTSKKIVITDCGQLS
Enzyme 24 Number of Residues 207
Enzyme 24 Molecular Weight 22040.1
Enzyme 24 Theoretical pI 9.95
Enzyme 24 GO Classification
Function
  • catalytic activity
  • cis-trans isomerase activity
  • isomerase activity
  • peptidyl-prolyl cis-trans isomerase activity
Process
  • cellular protein metabolic process
  • macromolecule metabolic process
  • metabolic process
  • protein folding
  • protein metabolic process
Component
Enzyme 24 General Function Involved in peptidyl-prolyl cis-trans isomerase activity
Enzyme 24 Specific Function PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides
Enzyme 24 Pathways Not Available
Enzyme 24 Reactions
  • peptidylproline (omega=180) = peptidylproline (omega=0) [RN:R04273]
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein Not Available
Enzyme 24 UniProtKB/Swiss-Prot ID P30405 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name PPIF_HUMAN Link Image
Enzyme 24 PDB ID 2BIU Link Image
Enzyme 24 PDB File Show
Enzyme 24 3D Structure
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >624 bp
ATGCTGGCGCTGCGCTGCGGCTCCCGCTGGCTCGGCCTGCTCTCCGTCCCGCGCTCCGTG
CCGCTGCGCCTCCCCGCGGCCCGCGCCTGCAGCAAGGGCTCCGGCGACCCGTCCTCTTCC
TCCTCCTCCGGGAACCCGCTCGTGTACCTGGACGTGGACGCCAACGGGAAGCCGCTCGGC
CGCGTGGTGCTGGAGCTGAAGGCAGATGTCGTCCCAAAGACAGCTGAGAACTTCAGAGCC
CTGTGCACTGGTGAGAAGGGCTTCGGCTACAAAGGCTCCACCTTCCACAGGGTGATCCCT
TCCTTCATGTGCCAGGCGGGCGACTTCACCAACCACAATGGCACAGGCGGGAAGTCCATC
TACGGAAGCCGCTTTCCTGACGAGAACTTTACACTGAAGCACGTGGGGCCAGGTGTCCTG
TCCATGGCTAATGCTGGTCCTAACACCAACGGCTCCCAGTTCTTCATCTGCACCATAAAG
ACAGACTGGTTGGATGGCAAGCATGTTGTGTTCGGTCACGTCAAAGAGGGCATGGACGTC
GTGAAGAAAATAGAATCTTTCGGCTCTAAGAGTGGGAGGACATCCAAGAAGATTGTCATC
ACAGACTGTGGCCAGTTGAGCTAA
Enzyme 24 GenBank Gene ID M80254 Link Image
Enzyme 24 GeneCard ID PPIF Link Image
Enzyme 24 GenAtlas ID PPIF Link Image
Enzyme 24 HGNC ID HGNC:9259 Link Image
Enzyme 24 Chromosome Location 1
Enzyme 24 Locus 10q22-q23
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References
  1. Bergsma DJ, Eder C, Gross M, Kersten H, Sylvester D, Appelbaum E, Cusimano D, Livi GP, McLaughlin MM, Kasyan K, et al.: The cyclophilin multigene family of peptidyl-prolyl isomerases. Characterization of three separate human isoforms. J Biol Chem. 1991 Dec 5;266(34):23204-14. [PubMed Link Image]
  2. 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]
  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. 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 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 16952
Enzyme 25 Name Peptidyl-prolyl cis-trans isomerase A
Enzyme 25 Synonyms
  1. PPIase A
  2. Cyclophilin A
  3. Cyclosporin A-binding protein
  4. Rotamase A
Enzyme 25 Gene Name PPIA
Enzyme 25 Protein Sequence >Peptidyl-prolyl cis-trans isomerase A
MVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGF
MCQGGDFTRHNGTGGKSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTE
WLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIADCGQLE
Enzyme 25 Number of Residues 165
Enzyme 25 Molecular Weight 18012.4
Enzyme 25 Theoretical pI 7.97
Enzyme 25 GO Classification
Function
  • catalytic activity
  • cis-trans isomerase activity
  • isomerase activity
  • peptidyl-prolyl cis-trans isomerase activity
Process
  • cellular protein metabolic process
  • macromolecule metabolic process
  • metabolic process
  • protein folding
  • protein metabolic process
Component
Enzyme 25 General Function Involved in peptidyl-prolyl cis-trans isomerase activity
Enzyme 25 Specific Function PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides
Enzyme 25 Pathways Not Available
Enzyme 25 Reactions
  • peptidylproline (omega=180) = peptidylproline (omega=0) [RN:R04273]
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 30309 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID P62937 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name PPIA_HUMAN Link Image
Enzyme 25 PDB ID 1CWM Link Image
Enzyme 25 PDB File Show
Enzyme 25 3D Structure
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >498 bp
ATGGTCAACCCCACCGTGTTCTTCGACATTGCCGTCGACGGCGAGCCCTTGGGCCGCGTC
TCCTTTGAGCTGTTTGCAGACAAGGTCCCAAAGACAGCAGAAAATTTTCGTGCTCTGAGC
ACTGGAGAGAAAGGATTTGGTTATAAGGGTTCCTGCTTTCACAGAATTATTCCAGGGTTT
ATGTGTCAGGGTGGTGACTTCACACGCCATAATGGCACTGGTGGCAAGTCCATCTATGGG
GAGAAATTTGAAGATGAGAACTTCATCCTAAAGCATACGGGTCCTGGCATCTTGTCCATG
GCAAATGCTGGACCCAACACAAATGGTTCCCAGTTTTTCATCTGCACTGCCAAGACTGAG
TGGTTGGATGGCAAGCATGTGGTGTTTGGCAAAGTGAAAGAAGGCATGAATATTGTGGAG
GCCATGGAGCGCTTTGGGTCCAGGAATGGCAAGACCAGCAAGAAGATCACCATTGCTGAC
TGTGGACAACTCGAATAA
Enzyme 25 GenBank Gene ID Y00052 Link Image
Enzyme 25 GeneCard ID PPIA Link Image
Enzyme 25 GenAtlas ID PPIA Link Image
Enzyme 25 HGNC ID HGNC:9253 Link Image
Enzyme 25 Chromosome Location 7
Enzyme 25 Locus 7p13
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. Haendler B, Hofer-Warbinek R, Hofer E: Complementary DNA for human T-cell cyclophilin. EMBO J. 1987 Apr;6(4):947-50. [PubMed Link Image]
  2. Haendler B, Hofer E: Characterization of the human cyclophilin gene and of related processed pseudogenes. Eur J Biochem. 1990 Jul 5;190(3):477-82. [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. Meier U, Beier-Hellwig K, Klug J, Linder D, Beier HM: Identification of cyclophilin A from human decidual and placental tissue in the first trimester of pregnancy. Hum Reprod. 1995 May;10(5):1305-10. [PubMed Link Image]
  5. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  6. Liu J, Chen CM, Walsh CT: Human and Escherichia coli cyclophilins: sensitivity to inhibition by the immunosuppressant cyclosporin A correlates with a specific tryptophan residue. Biochemistry. 1991 Mar 5;30(9):2306-10. [PubMed Link Image]
  7. Luban J, Bossolt KL, Franke EK, Kalpana GV, Goff SP: Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B. Cell. 1993 Jun 18;73(6):1067-78. [PubMed Link Image]
  8. Gevaert K, Staes A, Van Damme J, De Groot S, Hugelier K, Demol H, Martens L, Goethals M, Vandekerckhove J: Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC. Proteomics. 2005 Sep;5(14):3589-99. [PubMed Link Image]
  9. Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y: Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell. 2006 Aug;23(4):607-18. [PubMed Link Image]
  10. Meierhofer D, Wang X, Huang L, Kaiser P: Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry. J Proteome Res. 2008 Oct;7(10):4566-76. Epub 2008 Sep 10. [PubMed Link Image]
  11. 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]
  12. Kallen J, Spitzfaden C, Zurini MG, Wider G, Widmer H, Wuthrich K, Walkinshaw MD: Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy. Nature. 1991 Sep 19;353(6341):276-9. [PubMed Link Image]
  13. Ke HM, Zydowsky LD, Liu J, Walsh CT: Crystal structure of recombinant human T-cell cyclophilin A at 2.5 A resolution. Proc Natl Acad Sci U S A. 1991 Nov 1;88(21):9483-7. [PubMed Link Image]
  14. Pflugl G, Kallen J, Schirmer T, Jansonius JN, Zurini MG, Walkinshaw MD: X-ray structure of a decameric cyclophilin-cyclosporin crystal complex. Nature. 1993 Jan 7;361(6407):91-4. [PubMed Link Image]
  15. Mikol V, Kallen J, Pflugl G, Walkinshaw MD: X-ray structure of a monomeric cyclophilin A-cyclosporin A crystal complex at 2.1 A resolution. J Mol Biol. 1993 Dec 20;234(4):1119-30. [PubMed Link Image]
  16. Zhao Y, Ke H: Crystal structure implies that cyclophilin predominantly catalyzes the trans to cis isomerization. Biochemistry. 1996 Jun 11;35(23):7356-61. [PubMed Link Image]
  17. Vajdos FF, Yoo S, Houseweart M, Sundquist WI, Hill CP: Crystal structure of cyclophilin A complexed with a binding site peptide from the HIV-1 capsid protein. Protein Sci. 1997 Nov;6(11):2297-307. [PubMed Link Image]
  18. Kallen J, Mikol V, Taylor P, Walkinshaw MD: X-ray structures and analysis of 11 cyclosporin derivatives complexed with cyclophilin A. J Mol Biol. 1998 Oct 23;283(2):435-49. [PubMed Link Image]
  19. Huai Q, Kim HY, Liu Y, Zhao Y, Mondragon A, Liu JO, Ke H: Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes. Proc Natl Acad Sci U S A. 2002 Sep 17;99(19):12037-42. Epub 2002 Sep 6. [PubMed Link Image]
  20. Jin L, Harrison SC: Crystal structure of human calcineurin complexed with cyclosporin A and human cyclophilin. Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13522-6. Epub 2002 Sep 30. [PubMed Link Image]
  21. Theriault Y, Logan TM, Meadows R, Yu L, Olejniczak ET, Holzman TF, Simmer RL, Fesik SW: Solution structure of the cyclosporin A/cyclophilin complex by NMR. Nature. 1993 Jan 7;361(6407):88-91. [PubMed Link Image]
  22. Ottiger M, Zerbe O, Guntert P, Wuthrich K: The NMR solution conformation of unligated human cyclophilin A. J Mol Biol. 1997 Sep 12;272(1):64-81. [PubMed Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 16953
Enzyme 26 Name Peptidyl-prolyl cis-trans isomerase B
Enzyme 26 Synonyms
  1. PPIase B
  2. CYP-S1
  3. Cyclophilin B
  4. Rotamase B
  5. S-cyclophilin
  6. SCYLP
Enzyme 26 Gene Name PPIB
Enzyme 26 Protein Sequence >Peptidyl-prolyl cis-trans isomerase B
MLRLSERNMKVLLAAALIAGSVFFLLLPGPSAADEKKKGPKVTVKVYFDLRIGDEDVGRV
IFGLFGKTVPKTVDNFVALATGEKGFGYKNSKFHRVIKDFMIQGGDFTRGDGTGGKSIYG
ERFPDENFKLKHYGPGWVSMANAGKDTNGSQFFITTVKTAWLDGKHVVFGKVLEGMEVVR
KVESTKTDSRDKPLKDVIIADCGKIEVEKPFAIAKE
Enzyme 26 Number of Residues 216
Enzyme 26 Molecular Weight 23742.4
Enzyme 26 Theoretical pI 10.07
Enzyme 26 GO Classification
Function
  • catalytic activity
  • cis-trans isomerase activity
  • isomerase activity
  • peptidyl-prolyl cis-trans isomerase activity
Process
  • cellular protein metabolic process
  • macromolecule metabolic process
  • metabolic process
  • protein folding
  • protein metabolic process
Component
Enzyme 26 General Function Involved in peptidyl-prolyl cis-trans isomerase activity
Enzyme 26 Specific Function PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides
Enzyme 26 Pathways Not Available
Enzyme 26 Reactions
  • peptidylproline (omega=180) = peptidylproline (omega=0) [RN:R04273]
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • 1-33
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein Not Available
Enzyme 26 UniProtKB/Swiss-Prot ID P23284 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name PPIB_HUMAN Link Image
Enzyme 26 PDB ID 1CYN Link Image
Enzyme 26 PDB File Show
Enzyme 26 3D Structure
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >651 bp
ATGCTGCGCCTCTCCGAACGCAACATGAAGGTGCTCCTTGCCGCCGCCCTCATCGCGGGG
TCCGTCTTCTTCCTGCTGCTGCCGGGACCTTCTGCGGCCGATGAGAAGAAGAAGGGGCCC
AAAGTCACCGTCAAGGTGTATTTTGACCTACGAATTGGAGATGAAGATGTAGGCCGGGTG
ATCTTTGGTCTCTTCGGAAAGACTGTTCCAAAAACAGTGGATAATTTTGTGGCCTTAGCT
ACAGGAGAGAAAGGATTTGGCTACAAAAACAGCAAATTCCATCGTGTAATCAAGGACTTC
ATGATCCAGGGCGGAGACTTCACCAGGGGAGATGGCACAGGAGGAAAGAGCATCTACGGT
GAGCGCTTCCCCGATGAGAACTTCAAACTGAAGCACTACGGGCCTGGCTGGGTGAGCATG
GCCAACGCAGGCAAAGACACCAACGGCTCCCAGTTCTTCATCACGACAGTCAAGACAGCC
TGGCTAGATGGCAAGCATGTGGTGTTTGGCAAAGTTCTAGAGGGCATGGAGGTGGTGCGG
AAGGTGGAGAGCACCAAGACAGACAGCCGGGATAAACCCCTGAAGGATGTGATCATCGCA
GACTGCGGCAAGATCGAGGTGGAGAAGCCCTTTGCCATCGCCAAGGAGTAG
Enzyme 26 GenBank Gene ID M63573 Link Image
Enzyme 26 GeneCard ID PPIB Link Image
Enzyme 26 GenAtlas ID PPIB Link Image
Enzyme 26 HGNC ID HGNC:9255 Link Image
Enzyme 26 Chromosome Location 1
Enzyme 26 Locus 15q21-q22
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References
  1. Spik G, Haendler B, Delmas O, Mariller C, Chamoux M, Maes P, Tartar A, Montreuil J, Stedman K, Kocher HP, et al.: A novel secreted cyclophilin-like protein (SCYLP). J Biol Chem. 1991 Jun 15;266(17):10735-8. [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. 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]
  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. Price ER, Zydowsky LD, Jin MJ, Baker CH, McKeon FD, Walsh CT: Human cyclophilin B: a second cyclophilin gene encodes a peptidyl-prolyl isomerase with a signal sequence. Proc Natl Acad Sci U S A. 1991 Mar 1;88(5):1903-7. [PubMed Link Image]
  6. Hasel KW, Glass JR, Godbout M, Sutcliffe JG: An endoplasmic reticulum-specific cyclophilin. Mol Cell Biol. 1991 Jul;11(7):3484-91. [PubMed Link Image]
  7. Rasmussen HH, van Damme J, Puype M, Gesser B, Celis JE, Vandekerckhove J: Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. Electrophoresis. 1992 Dec;13(12):960-9. [PubMed Link Image]
  8. Arber S, Krause KH, Caroni P: s-cyclophilin is retained intracellularly via a unique COOH-terminal sequence and colocalizes with the calcium storage protein calreticulin. J Cell Biol. 1992 Jan;116(1):113-25. [PubMed Link Image]
  9. Chi A, Valencia JC, Hu ZZ, Watabe H, Yamaguchi H, Mangini NJ, Huang H, Canfield VA, Cheng KC, Yang F, Abe R, Yamagishi S, Shabanowitz J, Hearing VJ, Wu C, Appella E, Hunt DF: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. J Proteome Res. 2006 Nov;5(11):3135-44. [PubMed Link Image]
  10. van Dijk FS, Nesbitt IM, Zwikstra EH, Nikkels PG, Piersma SR, Fratantoni SA, Jimenez CR, Huizer M, Morsman AC, Cobben JM, van Roij MH, Elting MW, Verbeke JI, Wijnaendts LC, Shaw NJ, Hogler W, McKeown C, Sistermans EA, Dalton A, Meijers-Heijboer H, Pals G: PPIB mutations cause severe osteogenesis imperfecta. Am J Hum Genet. 2009 Oct;85(4):521-7. Epub 2009 Sep 24. [PubMed Link Image]
  11. Mikol V, Kallen J, Walkinshaw MD: X-ray structure of a cyclophilin B/cyclosporin complex: comparison with cyclophilin A and delineation of its calcineurin-binding domain. Proc Natl Acad Sci U S A. 1994 May 24;91(11):5183-6. [PubMed Link Image]
  12. Barnes AM, Carter EM, Cabral WA, Weis M, Chang W, Makareeva E, Leikin S, Rotimi CN, Eyre DR, Raggio CL, Marini JC: Lack of cyclophilin B in osteogenesis imperfecta with normal collagen folding. N Engl J Med. 2010 Feb 11;362(6):521-8. Epub 2010 Jan 20. [PubMed Link Image]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 16954
Enzyme 27 Name Peptidyl-prolyl cis-trans isomerase G
Enzyme 27 Synonyms
  1. PPIase G
  2. Peptidyl-prolyl isomerase G
  3. CASP10
  4. Clk-associating RS-cyclophilin
  5. CARS-Cyp
  6. CARS-cyclophilin
  7. SR-cyclophilin
  8. SR-cyp
  9. SRcyp
  10. Cyclophilin G
  11. Rotamase G
Enzyme 27 Gene Name PPIG
Enzyme 27 Protein Sequence >Peptidyl-prolyl cis-trans isomerase G
MGIKVQRPRCFFDIAINNQPAGRVVFELFSDVCPKTCENFRCLCTGEKGTGKSTQKPLHY
KSCLFHRVVKDFMVQGGDFSEGNGRGGESIYGGFFEDESFAVKHNKEFLLSMANRGKDTN
GSQFFITTKPTPHLDGHHVVFGQVISGQEVVREIENQKTDAASKPFAEVRILSCGELIPK
SKVKKEEKKRHKSSSSSSSSSSDSDSSSDSQSSSDSSDSESATEEKSKKRKKKHRKNSRK
HKKEKKKRKKSKKSASSESEAENLEAQPQSTVRPEEIPPIPENRFLMRKSPPKADEKERK
NRERERERECNPPNSQPASYQRRLLVTRSGRKIKGRGPRRYRTPSRSRSRDRFRRSETPP
HWRQEMQRAQRMRVSSGERWIKGDKSELNEIKENQRSPVRVKERKITDHRNVSESPNRKN
EKEKKVKDHKSNSKERDIRRNSEKDDKYKNKVKKRAKSKSRSKSKEKSKSKERDSKHNRN
EEKRMRSRSKGRDHENVKEKEKQSDSKGKDQERSRSKEKSKQLESKSNEHDHSKSKEKDR
RAQSRSRECDITKGKHSYNSRTRERSRSRDRSRRVRSRTHDRDRSRSKEYHRYREQEYRR
RGRSRSRERRTPPGRSRSKDRRRRRRDSRSSEREESQSRNKDKYRNQESKSSHRKENSES
EKRMYSKSRDHNSSNNSREKKADRDQSPFSKIKQSSQDNELKSSMLKNKEDEKIRSSVEK
ENQKSKGQENDHVHEKNKKFDHESSPGTDEDKSG
Enzyme 27 Number of Residues 754
Enzyme 27 Molecular Weight 88616.5
Enzyme 27 Theoretical pI 11.01
Enzyme 27 GO Classification
Function
  • catalytic activity
  • cis-trans isomerase activity
  • isomerase activity
  • peptidyl-prolyl cis-trans isomerase activity
Process
  • cellular protein metabolic process
  • macromolecule metabolic process
  • metabolic process
  • protein folding
  • protein metabolic process
Component
Enzyme 27 General Function Involved in peptidyl-prolyl cis-trans isomerase activity
Enzyme 27 Specific Function PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be implicated in the folding, transport, and assembly of proteins. May play an important role in the regulation of pre-mRNA splicing
Enzyme 27 Pathways Not Available
Enzyme 27 Reactions
  • peptidylproline (omega=180) = peptidylproline (omega=0) [RN:R04273]
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 42560244 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID Q13427 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name PPIG_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence >2265 bp
ATGGGAATAAAGGTTCAACGTCCTCGATGTTTTTTTGACATTGCCATTAACAATCAACCT
GCTGGAAGAGTTGTCTTTGAATTATTTTCTGATGTGTGCCCCAAAACATGCGAGAACTTT
CGTTGTCTTTGTACAGGTGAAAAGGGGACCGGGAAATCAACTCAGAAACCATTACATTAT
AAGAGTTGTCTCTTTCACAGAGTTGTCAAGGATTTTATGGTTCAAGGTGGTGACTTCAGT
GAAGGAAATGGACGAGGAGGGGAATCTATCTATGGAGGATTTTTTGAAGACGAGAGTTTC
GCTGTTAAACACAACAAAGAATTTCTCTTGTCAATGGCCAACAGAGGGAAGGATACAAAT
GGTTCACAGTTCTTCATAACAACGAAACCAACTCCTCATTTAGATGGGCATCATGTTGTT
TTTGGACAAGTAATCTCTGGTCAAGAAGTTGTAAGAGAGATTGAAAACCAGAAAACAGAT
GCAGCTAGCAAACCGTTTGCGGAGGTACGGATACTCAGTTGTGGAGAGCTGATTCCCAAA
TCTAAAGTTAAGAAAGAAGAAAAGAAAAGGCATAAATCATCATCATCTTCCTCCTCCTCA
TCTAGTGACTCAGATAGCTCAAGTGATTCTCAGTCCTCTTCTGATTCCTCTGATTCCGAA
AGTGCTACTGAAGAGAAATCAAAGAAAAGAAAAAAGAAACATCGGAAAAATTCCCGAAAA
CACAAGAAAGAAAAGAAAAAGCGAAAGAAAAGCAAGAAGAGTGCATCTAGTGAGAGTGAA
GCTGAAAATCTTGAAGCACAACCCCAGTCTACTGTCCGTCCAGAAGAGATCCCTCCTATA
CCTGAAAATAGATTCCTAATGAGAAAAAGTCCTCCTAAAGCTGATGAGAAGGAAAGGAAA
AACAGAGAGAGAGAAAGGGAAAGAGAGTGTAATCCACCTAACTCCCAGCCTGCTTCATAC
CAGAGACGACTTTTAGTTACTAGATCTGGCAGGAAAATTAAAGGAAGAGGACCAAGGCGT
TATCGAACTCCTTCCAGATCCAGATCAAGGGATCGTTTCAGACGTAGTGAGACTCCTCCA
CATTGGAGGCAAGAGATGCAGAGAGCTCAAAGAATGAGGGTATCAAGTGGTGAAAGATGG
ATCAAGGGGGATAAGAGTGAGTTGAATGAAATAAAAGAAAATCAGAGAAGTCCAGTTAGA
GTAAAAGAGAGAAAAATAACAGATCACAGGAATGTATCTGAGAGTCCAAACAGAAAAAAT
GAAAAGGAGAAGAAAGTTAAAGACCATAAATCTAACAGCAAAGAGAGAGACATCAGAAGA
AATTCAGAAAAAGATGACAAGTATAAAAACAAAGTGAAGAAAAGGGCCAAATCTAAAAGT
AGGAGTAAGAGCAAAGAGAAATCAAAGAGTAAAGAAAGAGATTCAAAACATAATAGAAAT
GAAGAAAAGAGGATGAGGTCAAGGAGTAAAGGAAGGGATCATGAAAATGTTAAAGAAAAA
GAAAAGCAGTCTGATTCTAAAGGAAAAGATCAGGAAAGGAGTAGAAGTAAAGAGAAGTCT
AAACAGTTAGAATCAAAGAGTAATGAGCATGATCACAGTAAAAGTAAGGAAAAGGATAGA
CGCGCACAATCCAGGAGTAGAGAATGTGATATAACTAAAGGTAAACACAGTTATAATAGC
AGAACAAGAGAACGAAGCAGAAGTAGGGACAGAAGCAGAAGAGTGCGATCAAGAACCCAT
GACAGAGATCGCAGCAGAAGCAAGGAGTACCATAGATACAGAGAACAGGAATACAGGAGA
AGAGGACGGTCACGAAGCCGAGAGAGAAGAACACCACCAGGAAGATCAAGAAGTAAAGAT
AGGAGGAGAAGGAGGAGAGACTCACGGAGCTCAGAGAGAGAAGAAAGTCAAAGCAGAAAC
AAAGACAAATACAGAAACCAAGAGAGTAAGAGCTCACACAGAAAAGAAAATTCTGAGAGT
GAGAAAAGAATGTACTCTAAAAGTCGTGATCATAATAGCTCAAATAACAGCAGGGAAAAA
AAGGCTGATAGAGATCAAAGTCCCTTCTCAAAAATAAAACAAAGCAGTCAGGACAATGAA
TTAAAGTCCTCCATGTTGAAAAATAAGGAGGATGAGAAGATCAGATCCTCAGTGGAAAAA
GAAAACCAAAAATCAAAAGGTCAAGAAAATGACCATGTACATGAAAAAAATAAAAAATTT
GATCATGAATCAAGCCCTGGAACAGATGAAGACAAAAGCGGATGA
Enzyme 27 GenBank Gene ID NM_004792.2 Link Image
Enzyme 27 GeneCard ID PPIG Link Image
Enzyme 27 GenAtlas ID PPIG Link Image
Enzyme 27 HGNC ID HGNC:14650 Link Image
Enzyme 27 Chromosome Location 2
Enzyme 27 Locus 2q31.1
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References
  1. Nestel FP, Colwill K, Harper S, Pawson T, Anderson SK: RS cyclophilins: identification of an NK-TR1-related cyclophilin. Gene. 1996 Nov 21;180(1-2):151-5. [PubMed Link Image]
  2. Bourquin JP, Stagljar I, Meier P, Moosmann P, Silke J, Baechi T, Georgiev O, Schaffner W: A serine/arginine-rich nuclear matrix cyclophilin interacts with the C-terminal domain of RNA polymerase II. Nucleic Acids Res. 1997 Jun 1;25(11):2055-61. [PubMed Link Image]
  3. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [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. Lin CL, Leu S, Lu MC, Ouyang P: Over-expression of SR-cyclophilin, an interaction partner of nuclear pinin, releases SR family splicing factors from nuclear speckles. Biochem Biophys Res Commun. 2004 Aug 27;321(3):638-47. [PubMed Link Image]
  6. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  7. 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]
  8. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
  9. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
  10. 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]
  11. 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 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 16955
Enzyme 28 Name Probable prolyl-tRNA synthetase, mitochondrial
Enzyme 28 Synonyms
  1. Proline--tRNA ligase
  2. ProRS
Enzyme 28 Gene Name PARS2
Enzyme 28 Protein Sequence >Probable prolyl-tRNA synthetase, mitochondrial
MEGLLTRCRALPALATCSRQLSGYVPCRFHHCAPRRGRRLLLSRVFQPQNLREDRVLSLQ
DKSDDLTCKSQRLMLQVGLIYPASPGCYHLLPYTVRAMEKLVRVIDQEMQAIGGQKVNMP
SLSPAELWQATNRWDLMGKELLRLRDRHGKEYCLGPTHEEAITALIASQKKLSYKQLPFL
LYQVTRKFRDEPRPRFGLLRGREFYMKDMYTFDSSPEAAQQTYSLVCDAYCSLFNKLGLP
FVKVQADVGTIGGTVSHEFQLPVDIGEDRLAICPRCSFSANMETLDLSQMNCPACQGPLT
KTKGIEVGHTFYLGTKYSSIFNAQFTNVCGKPTLAEMGCYGLGVTRILAAAIEVLSTEDC
VRWPSLLAPYQACLIPPKKGSKEQAASELIGQLYDHITEAVPQLHGEVLLDDRTHLTIGN
RLKDANKFGYPFVIIAGKRALEDPAHFEVWCQNTGEVAFLTKDGVMDLLTPVQTV
Enzyme 28 Number of Residues 475
Enzyme 28 Molecular Weight 53262.2
Enzyme 28 Theoretical pI 8.17
Enzyme 28 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • aminoacyl-tRNA ligase activity
  • binding
  • catalytic activity
  • ligase activity
  • ligase activity, forming aminoacyl-tRNA and related compounds
  • ligase activity, forming carbon-oxygen bonds
  • nucleoside binding
  • nucleotide binding
  • proline-tRNA ligase activity
  • purine nucleoside binding
Process
  • RNA metabolic process
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • cellular macromolecule metabolic process
  • macromolecule biosynthetic process
  • macromolecule metabolic process
  • metabolic process
  • ncRNA metabolic process
  • prolyl-tRNA aminoacylation
  • tRNA aminoacylation
  • tRNA aminoacylation for protein translation
  • tRNA metabolic process
  • translation
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 28 General Function Involved in nucleotide binding
Enzyme 28 Specific Function ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro)
Enzyme 28 Pathways Not Available
Enzyme 28 Reactions
  • ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro [RN:R03661]
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 34303926 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID Q7L3T8 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name SYPM_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence >1428 bp
ATGGAAGGGCTGCTGACAAGATGCAGAGCATTGCCCGCCCTGGCCACCTGCAGCCGCCAG
CTCTCTGGGTATGTTCCTTGCAGGTTTCACCACTGTGCCCCAAGAAGAGGGCGGCGCCTG
CTGCTGTCTCGTGTGTTCCAGCCACAGAACCTTCGGGAAGACCGGGTGCTCTCCCTGCAG
GACAAATCTGATGACCTGACCTGTAAGAGCCAGCGGCTGATGCTGCAGGTGGGCCTGATC
TACCCAGCAAGCCCCGGCTGTTACCACCTCCTGCCATATACCGTCCGTGCCATGGAGAAG
CTCGTGCGAGTGATAGACCAGGAGATGCAGGCCATCGGGGGCCAGAAAGTCAACATGCCC
AGCCTCAGCCCGGCAGAGCTCTGGCAAGCCACCAACCGGTGGGACTTGATGGGCAAAGAG
CTGCTAAGACTTAGAGACAGGCATGGCAAGGAATACTGCTTAGGACCAACTCACGAGGAA
GCCATTACGGCCTTAATTGCCTCCCAGAAGAAACTGTCCTACAAGCAGCTTCCCTTCCTG
CTGTACCAAGTGACAAGGAAGTTTCGGGATGAGCCCAGGCCCCGCTTTGGTCTTCTCCGT
GGCCGAGAGTTTTACATGAAGGATATGTACACCTTTGACTCCTCCCCAGAGGCTGCCCAG
CAGACCTACAGCCTGGTGTGTGATGCCTACTGCAGCCTGTTCAACAAGCTAGGGCTGCCA
TTTGTCAAGGTCCAGGCCGATGTGGGCACCATCGGGGGCACAGTGTCTCATGAGTTCCAG
CTCCCAGTGGATATTGGAGAGGACCGGCTTGCCATCTGTCCCCGCTGCAGCTTCTCAGCC
AACATGGAGACACTAGACTTGTCACAAATGAACTGCCCTGCTTGCCAGGGCCCATTGACT
AAAACCAAAGGCATTGAGGTGGGGCACACATTTTACCTGGGTACCAAGTACTCATCCATT
TTCAATGCCCAGTTTACCAATGTCTGTGGCAAACCAACCCTGGCTGAAATGGGGTGCTAT
GGCTTGGGTGTGACACGGATCTTGGCTGCTGCCATTGAAGTCCTCTCTACAGAAGACTGT
GTCCGCTGGCCCAGCCTACTGGCCCCTTACCAAGCCTGCCTCATCCCCCCTAAGAAGGGC
AGTAAGGAGCAGGCGGCCTCCGAGCTCATAGGGCAGCTGTACGACCACATCACAGAGGCA
GTGCCTCAGCTTCACGGGGAGGTGCTCCTGGACGACAGGACCCATCTGACCATCGGAAAC
AGACTGAAAGATGCCAACAAGTTTGGCTACCCCTTTGTGATAATCGCTGGCAAGAGGGCC
CTGGAGGACCCTGCACATTTTGAGGTTTGGTGTCAGAACACTGGTGAGGTGGCCTTCCTC
ACCAAAGATGGAGTCATGGATTTACTGACCCCAGTGCAGACTGTCTAA
Enzyme 28 GenBank Gene ID NM_152268.3 Link Image
Enzyme 28 GeneCard ID PARS2 Link Image
Enzyme 28 GenAtlas ID PARS2 Link Image
Enzyme 28 HGNC ID HGNC:30563 Link Image
Enzyme 28 Chromosome Location 1
Enzyme 28 Locus 1p32.2
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 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. 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]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 16956
Enzyme 29 Name Peptidyl-prolyl cis-trans isomerase H
Enzyme 29 Synonyms
  1. PPIase H
  2. Rotamase H
  3. Small nuclear ribonucleoprotein particle-specific cyclophilin H
  4. CypH
  5. U-snRNP-associated cyclophilin SnuCyp-20
  6. USA-CYP
Enzyme 29 Gene Name PPIH
Enzyme 29 Protein Sequence >Peptidyl-prolyl cis-trans isomerase H
MAVANSSPVNPVVFFDVSIGGQEVGRMKIELFADVVPKTAENFRQFCTGEFRKDGVPIGY
KGSTFHRVIKDFMIQGGDFVNGDGTGVASIYRGPFADENFKLRHSAPGLLSMANSGPSTN
GCQFFITCSKCDWLDGKHVVFGKIIDGLLVMRKIENVPTGPNNKPKLPVVISQCGEM
Enzyme 29 Number of Residues 177
Enzyme 29 Molecular Weight 19208.0
Enzyme 29 Theoretical pI 8.22
Enzyme 29 GO Classification
Function
  • catalytic activity
  • cis-trans isomerase activity
  • isomerase activity
  • peptidyl-prolyl cis-trans isomerase activity
Process
  • cellular protein metabolic process
  • macromolecule metabolic process
  • metabolic process
  • protein folding
  • protein metabolic process
Component
Enzyme 29 General Function Involved in peptidyl-prolyl cis-trans isomerase activity
Enzyme 29 Specific Function PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Participates in pre-mRNA splicing. May play a role in the assembly of the U4/U5/U6 tri-snRNP complex. May act as a chaperone
Enzyme 29 Pathways Not Available
Enzyme 29 Reactions
  • peptidylproline (omega=180) = peptidylproline (omega=0) [RN:R04273]
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • None
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein Not Available
Enzyme 29 UniProtKB/Swiss-Prot ID O43447 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name PPIH_HUMAN Link Image
Enzyme 29 PDB ID 1MZW Link Image
Enzyme 29 PDB File Show
Enzyme 29 3D Structure
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >534 bp
ATGGCGGTGGCAAATTCAAGTCCTGTTAACCCCGTGGTGTTCTTTGATGTCAGTATTGGC
GGTCAGGAAGTTGGCCGCATGAAGATCGAGCTCTTTGCAGACGTTGTGCCTAAGACGGCC
GAGAACTTTAGGCAGTTCTGCACCGGAGAATTCAGGAAAGATGGGGTTCCAATAGGATAC
AAAGGAAGCACCTTCCACAGGGTCATAAAGGATTTCATGATTCAGGGTGGAGATTTTGTT
AATGGAGATGGTACTGGAGTCGCCAGTATTTACCGGGGGCCATTTGCAGATGAAAATTTT
AAACTTAGACACTCAGCTCCAGGCCTGCTTTCCATGGCGAACAGTGGTCCAAGTACAAAT
GGCTGTCAGTTCTTTATCACCTGCTCTAAGTGCGATTGGCTGGATGGGAAGCATGTGGTG
TTTGGAAAAATCATCGATGGACTTCTAGTGATGAGAAAGATTGAGAATGTTCCCACAGGC
CCCAACAATAAGCCCAAGCTACCTGTGGTGATCTCGCAGTGTGGGGAGATGTAG
Enzyme 29 GenBank Gene ID AF016371 Link Image
Enzyme 29 GeneCard ID PPIH Link Image
Enzyme 29 GenAtlas ID PPIH Link Image
Enzyme 29 HGNC ID HGNC:14651 Link Image
Enzyme 29 Chromosome Location 1
Enzyme 29 Locus 1p34.1
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References
  1. Horowitz DS, Kobayashi R, Krainer AR: A new cyclophilin and the human homologues of yeast Prp3 and Prp4 form a complex associated with U4/U6 snRNPs. RNA. 1997 Dec;3(12):1374-87. [PubMed Link Image]
  2. Teigelkamp S, Achsel T, Mundt C, Gothel SF, Cronshagen U, Lane WS, Marahiel M, Luhrmann R: The 20kD protein of human [U4/U6.U5] tri-snRNPs is a novel cyclophilin that forms a complex with the U4/U6-specific 60kD and 90kD proteins. RNA. 1998 Feb;4(2):127-41. [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. Horowitz DS, Lee EJ, Mabon SA, Misteli T: A cyclophilin functions in pre-mRNA splicing. EMBO J. 2002 Feb 1;21(3):470-80. [PubMed Link Image]
  5. 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]
  6. Reidt U, Reuter K, Achsel T, Ingelfinger D, Luhrmann R, Ficner R: Crystal structure of the human U4/U6 small nuclear ribonucleoprotein particle-specific SnuCyp-20, a nuclear cyclophilin. J Biol Chem. 2000 Mar 17;275(11):7439-42. [PubMed Link Image]
  7. Reidt U, Wahl MC, Fasshauer D, Horowitz DS, Luhrmann R, Ficner R: Crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60K peptide. J Mol Biol. 2003 Aug 1;331(1):45-56. [PubMed Link Image]
Enzyme 29 Metabolite References Not Available