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Human Metabolome Database Version 2.5

 

Showing metabocard for Creatine (HMDB00064)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-28 10:46:23
Accession Number HMDB00064
Secondary Accession Numbers Not Available
Common Name Creatine
Description Creatine is an amino acid that occurs in vertebrate tissues and in urine. In muscle tissue, creatine generally occurs as phosphocreatine. Creatine is excreted as creatinine in the urine. Creatine functions as part of the cell's energy shuttle. The high energy phosphate group of ATP is transferred to creatine to form phosphocreatine in the following reaction: Cr + ATP <-> PCr + ADP. This reaction is reversibly catalyzed by creatine kinase. In the human body creatine is synthesized mainly in the liver by the use of parts from three different amino acids - arginine, glycine, and methionine. 95% of it is later stored in the skeletal muscles, with the rest in the brain, heart, testes.
Synonyms
  1. ((amino(imino)methyl)(methyl)amino)acetate
  2. ((amino(imino)methyl)(methyl)amino)acetic acid
  3. (alpha-Methylguanido)acetate
  4. (alpha-Methylguanido)acetic acid
  5. Cosmocair C 100
  6. Creatin
  7. Creatine
  8. Creatine hydrate
  9. Kreatin
  10. Krebiozon
  11. Methylguanidoacetate
  12. Methylguanidoacetic acid
  13. N-(Aminoiminomethyl)-N-Methyl-Glycine
  14. N-Methyl-N-guanylglycine
  15. Phosphagen
  16. [[Amino(imino)methyl](methyl)amino]acetate
  17. [[Amino(imino)methyl](methyl)amino]acetic acid
Chemical IUPAC Name 2-(carbamimidoyl-methyl-amino)acetic acid
Chemical Formula C4H9N3O2
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
  • carboxylic acid
  • guanidine
Biofunction
  • Component of Arginine and proline metabolism
  • Component of Glycine, serine and threonine metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 131.133
Monoisotopic Molecular Weight 131.069473
Isomeric SMILES CN(CC(O)=O)C(N)=N
Canonical SMILES CN(CC(O)=O)C(N)=N
KEGG Compound ID C00300 Link Image
BioCyc ID CREATINE Link Image
BiGG ID 34543 Link Image
Wikipedia Link Creatine Link Image
NuGOwiki Link HMDB00064 Link Image
Metagene Link HMDB00064 Link Image
METLIN ID 7 Link Image
PubChem Compound 586 Link Image
PubChem Substance 10327145 Link Image
ChEBI ID 16919 Link Image
CAS Registry Number 57-00-1
InChI Identifier InChI=1/C4H9N3O2/c1-7(4(5)6)2-3(8)9/h2H2,1H3,(H3,5,6)(H,8,9)
Synthesis Reference Thalhammer, Franz; Gastner, Thomas. Preparation of creatine, creatine monohydrate and guanidinoacetic acid. Ger. Offen. (2007), 5pp.
Melting Point (Experimental) 303 oC
Experimental Water Solubility 13.3 mg/mL at 18 oC [YALKOWSKY,SH & DANNENFELSER,RM (1992)] Source: PhysProp
Predicted Water Solubility 4.11 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.2 [Predicted by PubChem via XLOGP]; -1.59 [Predicted by ALOGPS]; -3.72 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm
  • Extracellular
  • mitochondria
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
Adipose Tissue —
Bladder —
Brain —
Epidermis —
Fibroblasts —
Heart —
Intestine —
Kidney —
Muscle —
Myelin —
Nerve Cells —
Neuron —
Placenta —
Platelet —
Prostate —
Skeletal Muscle —
Spleen —
Testes —
Concentrations (Normal)
Biofluid Blood
Value 84.0 +/- 23.2 uM
Age Newborn:0-30 days old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 90. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 53.0 (17.0 - 82.0) uM
Age Children:1-13 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 90. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 30.1 +/- 12.3 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Marescau B, De Deyn PP, Holvoet J, Possemiers I, Nagels G, Saxena V, Mahler C: Guanidino compounds in serum and urine of cirrhotic patients. Metabolism. 1995 May;44(5):584-8. [PubMed Link Image]
Biofluid Blood
Value 54.8 +/- 21.0 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Marescau B, De Deyn PP, Holvoet J, Possemiers I, Nagels G, Saxena V, Mahler C: Guanidino compounds in serum and urine of cirrhotic patients. Metabolism. 1995 May;44(5):584-8. [PubMed Link Image]
Biofluid CSF
Value 44 +/- 13 uM
Age N/A
Sex Both
Patient information Normal
Comments Not Available
References
  • Wishart DS, Lewis MJ, Morrissey JA, Flegel MD, Jeroncic K, Xiong Y, Cheng D, Eisner R, Gautam B, Tzur D, Sawhney S, Bamforth F, Greiner R, Li L: The human cerebrospinal fluid metabolome. J Chromatogr B Analyt Technol Biomed Life Sci. 2008 Aug 15;871(2):164-173. Epub 2008 May 8. [PubMed Link Image]
Biofluid Urine
Value 113.0 (0.00-654.0) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Bales JR, Higham DP, Howe I, Nicholson JK, Sadler PJ: Use of high-resolution proton nuclear magnetic resonance spectroscopy for rapid multi-component analysis of urine. Clin Chem. 1984 Mar;30(3):426-32. [PubMed Link Image]
Biofluid Urine
Value 26.0 (5.0-95.0) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Male
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 46.0 (9.0-135.0) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
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 167 +/- 43 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Shaykhutdinov RA, MacInnis GD, Dowlatabadi R, Weljie AM, Vogel HJ. Quantitative analysis of metabolite concentrations in human urine samples using 13C{1H} NMR spectroscopy. Metabolomics. 2009
Concentrations (Abnormal)
Biofluid Blood
Value 25.7 (16.5 - 30.8) uM
Age Adult:>18 yrs old
Sex Male
Condition Cirrhosis
Comments Not Available
References
  • Marescau B, De Deyn PP, Holvoet J, Possemiers I, Nagels G, Saxena V, Mahler C: Guanidino compounds in serum and urine of cirrhotic patients. Metabolism. 1995 May;44(5):584-8. [PubMed Link Image]
Biofluid Blood
Value 40.3 (28.3-56.6) uM
Age Adult:>18 yrs old
Sex Female
Condition Cirrhosis
Comments Not Available
References
  • Marescau B, De Deyn PP, Holvoet J, Possemiers I, Nagels G, Saxena V, Mahler C: Guanidino compounds in serum and urine of cirrhotic patients. Metabolism. 1995 May;44(5):584-8. [PubMed Link Image]
Biofluid Urine
Value 37.0 (0.0-197.0) umol/mmol creatinine
Age N/A
Sex Both
Condition Lung Cancer
Comments Not Available
References
Biofluid Urine
Value 1540 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Condition Rhabdomyolysis
Comments Not Available
References
  • Bairaktari E, Seferiadis K, Liamis G, Psihogios N, Tsolas O, Elisaf M: Rhabdomyolysis-related renal tubular damage studied by proton nuclear magnetic resonance spectroscopy of urine. Clin Chem. 2002 Jul;48(7):1106-9. [PubMed Link Image]
Associated Disorders
Condition References
Cirrhosis
  • Marescau B, De Deyn PP, Holvoet J, Possemiers I, Nagels G, Saxena V, Mahler C: Guanidino compounds in serum and urine of cirrhotic patients. Metabolism. 1995 May;44(5):584-8. [PubMed Link Image]
Lung Cancer —
Rhabdomyolysis
  • Bairaktari E, Seferiadis K, Liamis G, Psihogios N, Tsolas O, Elisaf M: Rhabdomyolysis-related renal tubular damage studied by proton nuclear magnetic resonance spectroscopy of urine. Clin Chem. 2002 Jul;48(7):1106-9. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Arginine and Proline Metabolism SMP00020 Link Image map00330 Link Image
Glycine and Serine Metabolism SMP00004 Link Image map00260 Link Image
General References
  1. Schonberger B: [Overactive bladder--which diagnosis investigations are necessary before initiating primary treatment?] Urologe A. 2003 Jun;42(6):787-92. Epub 2003 Apr 25. [PubMed Link Image]
  2. Mercimek-Mahmutoglu S, Stoeckler-Ipsiroglu S, Adami A, Appleton R, Araujo HC, Duran M, Ensenauer R, Fernandez-Alvarez E, Garcia P, Grolik C, Item CB, Leuzzi V, Marquardt I, Muhl A, Saelke-Kellermann RA, Salomons GS, Schulze A, Surtees R, van der Knaap MS, Vasconcelos R, Verhoeven NM, Vilarinho L, Wilichowski E, Jakobs C: GAMT deficiency: features, treatment, and outcome in an inborn error of creatine synthesis. Neurology. 2006 Aug 8;67(3):480-4. Epub 2006 Jul 19. [PubMed Link Image]
  3. McConell GK, Shinewell J, Stephens TJ, Stathis CG, Canny BJ, Snow RJ: Creatine supplementation reduces muscle inosine monophosphate during endurance exercise in humans. Med Sci Sports Exerc. 2005 Dec;37(12):2054-61. [PubMed Link Image]
  4. McMorris T, Harris RC, Swain J, Corbett J, Collard K, Dyson RJ, Dye L, Hodgson C, Draper N: Effect of creatine supplementation and sleep deprivation, with mild exercise, on cognitive and psychomotor performance, mood state, and plasma concentrations of catecholamines and cortisol. Psychopharmacology (Berl). 2006 Mar;185(1):93-103. Epub 2006 Jan 17. [PubMed Link Image]
  5. Wang PF, McLeish MJ, Kneen MM, Lee G, Kenyon GL: An unusually low pK(a) for Cys282 in the active site of human muscle creatine kinase. Biochemistry. 2001 Oct 2;40(39):11698-705. [PubMed Link Image]
  6. Olsen S, Aagaard P, Kadi F, Tufekovic G, Verney J, Olesen JL, Suetta C, Kjaer M: Creatine supplementation augments the increase in satellite cell and myonuclei number in human skeletal muscle induced by strength training. J Physiol. 2006 Jun 1;573(Pt 2):525-34. Epub 2006 Mar 31. [PubMed Link Image]
  7. Ellington WR: A dimeric creatine kinase from a sponge: implications in terms of phosphagen kinase evolution. Comp Biochem Physiol B Biochem Mol Biol. 2000 May;126(1):1-7. [PubMed Link Image]
  8. Fredericks S, Murray JF, Bewick M, Chang R, Collinson PO, Carter ND, Holt DW: Cardiac troponin T and creatine kinase MB are not increased in exterior oblique muscle of patients with renal failure. Clin Chem. 2001 Jun;47(6):1023-30. [PubMed Link Image]
  9. Jiao YF, Okumiya T, Saibara T, Kudo Y, Sugiura T: Erythrocyte creatine as a marker of excessive erythrocyte destruction due to hypersplenism in patients with liver cirrhosis. Clin Biochem. 2001 Jul;34(5):395-8. [PubMed Link Image]
  10. Subramanian A, Gupta A, Saxena S, Gupta A, Kumar R, Nigam A, Kumar R, Mandal SK, Roy R: Proton MR CSF analysis and a new software as predictors for the differentiation of meningitis in children. NMR Biomed. 2005 Jun;18(4):213-25. [PubMed Link Image]
  11. Nicholson JK, Buckingham MJ, Sadler PJ: High resolution 1H n.m.r. studies of vertebrate blood and plasma. Biochem J. 1983 Jun 1;211(3):605-15. [PubMed Link Image]
  12. Sheth NP, Sennett B, Berns JS: Rhabdomyolysis and acute renal failure following arthroscopic knee surgery in a college football player taking creatine supplements. Clin Nephrol. 2006 Feb;65(2):134-7. [PubMed Link Image]
  13. Jenkins CB, Ghidini A, Spong CY, Eglinton GS, Pezzullo JC, Michejda M: Evaluation of early second trimester maternal serum creatine kinase isoenzyme BB as a marker of poor pregnancy outcome. Fetal Diagn Ther. 1997 Nov-Dec;12(6):356-9. [PubMed Link Image]
  14. Lukaszuk JM, Robertson RJ, Arch JE, Moyna NM: Effect of a defined lacto-ovo-vegetarian diet and oral creatine monohydrate supplementation on plasma creatine concentration. J Strength Cond Res. 2005 Nov;19(4):735-40. [PubMed Link Image]
  15. Preen DB, Dawson BT, Goodman C, Beilby J, Ching S: Comparison of erythrocyte and skeletal muscle creatine accumulation following creatine loading. Int J Sport Nutr Exerc Metab. 2005 Feb;15(1):84-93. [PubMed Link Image]
  16. Poortmans JR, Kumps A, Duez P, Fofonka A, Carpentier A, Francaux M: Effect of oral creatine supplementation on urinary methylamine, formaldehyde, and formate. Med Sci Sports Exerc. 2005 Oct;37(10):1717-20. [PubMed Link Image]
  17. Yoshizumi WM, Tsourounis C: Effects of creatine supplementation on renal function. J Herb Pharmacother. 2004;4(1):1-7. [PubMed Link Image]
  18. Harris RC, Almada AL, Harris DB, Dunnett M, Hespel P: The creatine content of Creatine Serum and the change in the plasma concentration with ingestion of a single dose. J Sports Sci. 2004 Sep;22(9):851-7. [PubMed Link Image]
  19. Mendes RR, Pires I, Oliveira A, Tirapegui J: Effects of creatine supplementation on the performance and body composition of competitive swimmers. J Nutr Biochem. 2004 Aug;15(8):473-8. [PubMed Link Image]
  20. Bales JR, Higham DP, Howe I, Nicholson JK, Sadler PJ: Use of high-resolution proton nuclear magnetic resonance spectroscopy for rapid multi-component analysis of urine. Clin Chem. 1984 Mar;30(3):426-32. [PubMed Link Image]
  21. Wikipedia Link Image
Metabolic Enzymes
  1. Guanidinoacetate N-methyltransferase
  2. Glycine amidinotransferase, mitochondrial precursor
  3. Creatine kinase, sarcomeric mitochondrial precursor
  4. Creatine kinase B-type
  5. Creatine kinase, ubiquitous mitochondrial precursor
  6. Creatine kinase M-type
  7. Sodium- and chloride-dependent creatine transporter 1
  8. cDNA FLJ78469, highly similar to Homo sapiens creatine kinase, brain
  9. Paired mesoderm homeobox protein 1
  10. DNA-binding protein inhibitor ID-3
  11. Creatine transporter SLC6A8 splice variant C
Enzyme 1 [top]
Enzyme 1 ID 5663
Enzyme 1 Name Guanidinoacetate N-methyltransferase
Enzyme 1 Synonyms Not Available
Enzyme 1 Gene Name GAMT
Enzyme 1 Protein Sequence >Guanidinoacetate N-methyltransferase 
MSAPSATPIFAPGENCSPAWGAAPAAYDAADTHLRILGKPVMERWETPYMHALAAAASSK
GGRVLEVGFGMAIAASKVQEAPIDEHWIIECNDGVFQRLRDWAPRQTHKVIPLKGLWEDV
APTLPDGHFDGILYDTYPLSEETWHTHQFNFIKNHAFRLLKPGGVLTYCNLTSWGELMKS
KYSDITIMFEETQVPALLEAGFRRENIRTEVMALVPPADCRYYAFPQMITPLVTKG
Enzyme 1 Number of Residues 236
Enzyme 1 Molecular Weight 26318
Enzyme 1 Theoretical pI 6.09
Enzyme 1 GO Classification Not Available
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function S-adenosyl-L-methionine + guanidinoacetate = S-adenosyl-L-homocysteine + creatine
Enzyme 1 Pathways
  • Arginine and Proline Metabolism (map00330 Link Image)
  • Glycine, Serine and Threonine Metabolism (map00260 Link Image)
Enzyme 1 Reactions
  • S-adenosyl-L-methionine + guanidinoacetate = S-adenosyl-L-homocysteine + creatine
Enzyme 1 Pfam Domain Function Not Available
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 1212946 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q14353 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name GAMT_HUMAN Link Image
Enzyme 1 PDB ID 1XCL Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >711 bp 
ATGAGCGCCCCCAGCGCGACCCCCATCTTCGCGCCCGGCGAGAACTGCAGCCCCGCGTGG
GGGGCGGCGCCCGCGGCCTACGACGCAGCGGACACGCACCTGCGCATCCTGGGCAAGCCG
GTGATGGAGCGCTGGGAGACCCCCTATATGCACGCGCTGGCCGCCGCCGCCTCCTCCAAA
GGGGGCCGGGTCCTGGAGGTGGGCTTTGGCATGGCCATCGCAGCGTCAAAGGTGCAGGAG
GCGCCCATTGATGAGCATTGGATCATCGAGTGCAATGACGGCGTCTTCCAGCGGCTCCGG
GACTGGGCCCCACGGCAGACACACAAGGTCATCCCCTTGAAAGGCCTGTGGGAGGATGTG
GCACCCACCCTGCCTGACGGTCACTTTGATGGGATCCTGTACGACACGTACCCACTCTCG
GAGGAGACCTGGCACACACACCAGTTCAACTTCATCAAGAACCACGCCTTTCGCCTGCTG
AAGCCGGGGGGCGTCCTCACCTACTGCAACCTCACCTCCTGGGGGGAGCTGATGAAGTCC
AAGTACTCAGACATCACCATCATGTTTGAGGAGACGCAGGTGCCCGCGCTGCTGGAGGCC
GGCTTCCGGAGGGAGAACATCCGTACGGAGGTGATGGCGCTGGTCCCACCGGCCGACTGC
CGCTACTACGCCTTCCCACAGATGATCACGCCCCTGGTGACCAAAGGCTGA
Enzyme 1 GenBank Gene ID Z49878 Link Image
Enzyme 1 GeneCard ID GAMT Link Image
Enzyme 1 GenAtlas ID GAMT Link Image
Enzyme 1 HGNC ID HGNC:4136 Link Image
Enzyme 1 Chromosome Location 19
Enzyme 1 Locus 19p13.3
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Isbrandt D, von Figura K: Cloning and sequence analysis of human guanidinoacetate N-methyltransferase cDNA. Biochim Biophys Acta. 1995 Dec 27;1264(3):265-7. [PubMed Link Image]
  2. Jenne DE, Olsen AS, Zimmer M: The human guanidinoacetate methyltransferase (GAMT) gene maps to a syntenic region on 19p13.3, homologous to band C of mouse chromosome 10, but GAMT is not mutated in jittery mice. Biochem Biophys Res Commun. 1997 Sep 29;238(3):723-7. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5702
Enzyme 2 Name Glycine amidinotransferase, mitochondrial precursor
Enzyme 2 Synonyms
  1. L- arginine:glycine amidinotransferase
  2. Transamidinase
  3. AT
Enzyme 2 Gene Name GATM
Enzyme 2 Protein Sequence >Glycine amidinotransferase, mitochondrial precursor 
MLRVRCLRGGSRGAEAVHYIGSRLGRTLTGWVQRTFQSTQAATASSRNSCAADDKATEPL
PKDCPVSSYNEWDPLEEVIVGRAENACVPPFTIEVKANTYEKYWPFYQKQGGHYFPKDHL
KKAVAEIEEMCNILKTEGVTVRRPDPIDWSLKYKTPDFESTGLYSAMPRDILIVVGNEII
EAPMAWRSRFFEYRAYRSIIKDYFHRGAKWTTAPKPTMADELYNQDYPIHSVEDRHKLAA
QGKFVTTEFEPCFDAADFIRAGRDIFAQRSQVTNYLGIEWMRRHLAPDYRVHIISFKDPN
PMHIDATFNIIGPGIVLSNPDRPCHQIDLFKKAGWTIITPPTPIIPDDHPLWMSSKWLSM
NVLMLDEKRVMVDANEVPIQKMFEKLGITTIKVNIRNANSLGGGFHCWTCDVRRRGTLQS
YLD
Enzyme 2 Number of Residues 423
Enzyme 2 Molecular Weight 48456
Enzyme 2 Theoretical pI 8.15
Enzyme 2 GO Classification Not Available
Enzyme 2 General Function Amino acid transport and metabolism
Enzyme 2 Specific Function L-arginine + glycine = L-ornithine + guanidinoacetate
Enzyme 2 Pathways
  • Arginine and Proline Metabolism (map00330 Link Image)
  • Glycine, Serine and Threonine Metabolism (map00260 Link Image)
Enzyme 2 Reactions
  • L-arginine + glycine = L-ornithine + guanidinoacetate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 545385 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P50440 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name GATM_HUMAN Link Image
Enzyme 2 PDB ID 3JDW Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1272 bp 
ATGCTGCGGGTGCGGTGTCTGCGCGGCGGGAGCCGCGGCGCCGAGGCGGTGCACTACATC
GGATCTCGGCTTGGACGAACCTTGACAGGATGGGTGCAGCGAACTTTCCAGAGCACCCAG
GCAGCTACGGCTTCCTCCCGGAACTCCTGTGCAGCTGACGACAAAGCCACTGAGCCTCTG
CCCAAGGACTGCCCTGTCTCTTCTTACAACGAATGGGACCCCTTAGAGGAAGTGATAGTG
GGCAGAGCAGAAAACGCCTGTGTTCCACCGTTCACCATCGAGGTGAAGGCCAACACATAT
GAAAAGTACTGGCCATTTTACCAGAAGCAAGGAGGGCATTATTTTCCCAAAGATCATTTG
AAAAAGGCTGTTGCTGAAATTGAAGAAATGTGCAATATTTTAAAAACGGAAGGAGTGACA
GTAAGGAGGCCTGACCCCATTGACTGGTCATTGAAGTATAAAACTCCTGATTTTGAGTCT
ACGGGTTTATACAGTGCAATGCCTCGAGACATCCTGATAGTTGTGGGCAATGAGATTATC
GAGGCTCCCATGGCATGGCGTTCACGCTTCTTTGAGTACCGAGCGTACAGGTCAATTATC
AAAGACTACTTCCACCGTGGCGCCAAGTGGACAACAGCTCCTAAGCCCACAATGGCTGAT
GAGCTTTATAACCAGGATTATCCCATCCACTCTGTAGAAGACAGACACAAATTGGCTGCT
CAGGGAAAATTTGTGACAACTGAGTTTGAGCCATGCTTTGATGCTGCTGACTTCATTCGA
GCTGGAAGAGATATTTTTGCACAGAGAAGCCAGGTTACAAACTACCTAGGCATTGAATGG
ATGCGTAGGCATCTTGCTCCAGACTACAGAGTGCATATCATCTCCTTTAAAGATCCCAAT
CCCATGCATATTGATGCTACCTTCAACATCATTGGACCTGGTATTGTGCTTTCCAACCCT
GACCGACCATGTCACCAGATTGATCTTTTCAAGAAAGCAGGATGGACTATCATTACTCCT
CCAACACCAATCATCCCAGACGATCATCCACTCTGGATGTCATCCAAATGGCTTTCCATG
AATGTCTTAATGCTAGATGAAAAACGTGTTATGGTGGATGCCAATGAAGTTCCAATTCAA
AAGATGTTTGAAAAGCTGGGTATCACTACCATTAAAGTTAACATTCGTAATGCCAATTCC
CTGGGAGGAGGCTTCCATTGCTGGACCTGCGATGTCCGGCGCCGAGGCACCCTACAGTCC
TACTTGGACTGA
Enzyme 2 GenBank Gene ID S68805 Link Image
Enzyme 2 GeneCard ID GATM Link Image
Enzyme 2 GenAtlas ID GATM Link Image
Enzyme 2 HGNC ID HGNC:4175 Link Image
Enzyme 2 Chromosome Location 15
Enzyme 2 Locus 15q21.1
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Humm A, Huber R, Mann K: The amino acid sequences of human and pig L-arginine:glycine amidinotransferase. FEBS Lett. 1994 Feb 14;339(1-2):101-7. [PubMed Link Image]
  2. Humm A, Fritsche E, Mann K, Gohl M, Huber R: Recombinant expression and isolation of human L-arginine:glycine amidinotransferase and identification of its active-site cysteine residue. Biochem J. 1997 Mar 15;322 ( Pt 3):771-6. [PubMed Link Image]
  3. Humm A, Fritsche E, Steinbacher S: Structure and reaction mechanism of L-arginine:glycine amidinotransferase. Biol Chem. 1997 Mar-Apr;378(3-4):193-7. [PubMed Link Image]
  4. Humm A, Fritsche E, Steinbacher S, Huber R: Crystal structure and mechanism of human L-arginine:glycine amidinotransferase: a mitochondrial enzyme involved in creatine biosynthesis. EMBO J. 1997 Jun 16;16(12):3373-85. [PubMed Link Image]
  5. Fritsche E, Humm A, Huber R: The ligand-induced structural changes of human L-Arginine:Glycine amidinotransferase. A mutational and crystallographic study. J Biol Chem. 1999 Jan 29;274(5):3026-32. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5993
Enzyme 3 Name Creatine kinase, sarcomeric mitochondrial precursor
Enzyme 3 Synonyms
  1. S- MtCK
  2. Mib-CK
  3. Basic-type mitochondrial creatine kinase
Enzyme 3 Gene Name CKMT2
Enzyme 3 Protein Sequence >Creatine kinase, sarcomeric mitochondrial precursor 
MASIFSKLLTGRNASLLFATMGTSVLTTGYLLNRQKVCAEVREQPRLFPPSADYPDLRKH
NNCMAECLTPAIYAKLRNKVTPNGYTLDQCIQTGVDNPGHPFIKTVGMVAGDEESYEVFA
DLFDPVIKLRHNGYDPRVMKHTTDLDASKITQGQFDEHYVLSSRVRTGRSIRGLSLPPAC
TRAERREVENVAITALEGLKGDLAGRYYKLSEMTEQDQQRLIDDHFLFDKPVSPLLTCAG
MARDWPDARGIWHNYDKTFLIWINEEDHTRVISMEKGGNMKRVFERFCRGLKEVERLIQE
RGWEFMWNERLGYILTCPSNLGTGLRAGVHVRIPKLSKDPRFSKILENLRLQKRGTGGVD
TAAVADVYDISNIDRIGRSEVELVQIVIDGVNYLVDCEKKLERGQDIKVPPPLPQFGKK
Enzyme 3 Number of Residues 419
Enzyme 3 Molecular Weight 47505
Enzyme 3 Theoretical pI 8.31
Enzyme 3 GO Classification
Function
  • catalytic activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
—
Component
—
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa
Enzyme 3 Pathways
Enzyme 3 Reactions
  • ATP + creatine = ADP + phosphocreatine
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-27
Enzyme 3 Transmembrane Regions Not Available
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 338237 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P17540 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name KCRS_HUMAN Link Image
Enzyme 3 PDB ID 1CRK Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1260 bp 
ATGGCCAGTATCTTTTCTAAGTTGCTAACTGGCCGCAATGCTTCTCTGCTGTTTGCTACC
ATGGGCACCAGTGTCCTGACCACCGGGTACCTGCTGAACCGGCAGAAAGTGTGTGCCGAG
GTCCGGGAGCAGCCTAGGCTATTTCCTCCAAGCGCAGACTACCCAGACCTGCGCAAGCAC
AACAACTGCATGGCCGAGTGCCTCACCCCCGCCATTTATTCCAAGCTTCGCAACAAGGTG
ACACCCAACGGCTACACGCTGGACCAGTGCATCCAGACTGGAGTGGACAACCCTGGCCAC
CCCTTCATAAAGACTGTGGGCATGGTGGCTGGTGACGAGGAGTCCTATGAGGTGTTTGCT
GACCTTTTTGACCCCGTCATCAAACTAAGACACAACGGCTATGACCCCAGGGTGATGAAG
CACACAACGGATCTGGATGCATCAAAGATCACCCAAGGGCAGTTCGACGAGCATTACGTG
CTGTCTTCTCGGGTGCGCACTGGCCGCAGCATCCGTGGGCTGAGCCTGCCTCCAGCCTGC
ACCCGGGCCGAGCGAAGGGAGGTAGAGAACGTGGCCATCACTGCCCTGGAGGGCCTCAAG
GGGGACCTGGCTGGCCGCTACTACAAGCTGTCCGAGATGACGGAGCAGGACCAGCAGCGG
CTCATCGATGACCACTTTCTGTTTGATAAGCCAGTGTCCCCTTTATTAACATGTGCTGGG
ATGGCCCGTGACTGGCCAGATGCCAGGGGAATCTGGCATAATTATGATAAGACATTTCTC
ATCTGGATAAATGAGGAGGATCACACCAGGGTAATCTCAATGGAAAAAGGAGGCAATATG
AAACGAGTATTTGAGCGATTCTGTCGTGGACTAAAAGAAGTAGAACGGTTAATCCAAGAA
CGAGGCTGGGAGTTCATGTGGAATGAGCGCCTAGGATACATTTTGACCTGTCCTTCGAAC
CTTGGAACAGGACTACGAGCTGGTGTCCACGTTAGGATCCCAAAGCTCAGCAAGGACCCA
CGCTTTTCTAAGATCCTGGAAAACCTAAGACTCCAGAAGCGTGGCACAGGTGGTGTGGAC
ACTGCCGCGGTCGCAGATGTGTACGACATTTCCAACATAGATAGAATTGGTCGATCAGAG
GTTGAGCTTGTTCAGATAGTCATCGATGGAGTCAATTACCTGGTGGATTGTGAAAAGAAG
TTGGAGAGAGGCCAAGATATTAAGGTGCCACCCCCTCTGCCTCAGTTTGGCAAAAAGTAA
Enzyme 3 GenBank Gene ID J05401 Link Image
Enzyme 3 GeneCard ID CKMT2 Link Image
Enzyme 3 GenAtlas ID CKMT2 Link Image
Enzyme 3 HGNC ID HGNC:1996 Link Image
Enzyme 3 Chromosome Location 5
Enzyme 3 Locus 5q13.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Haas RC, Strauss AW: Separate nuclear genes encode sarcomere-specific and ubiquitous human mitochondrial creatine kinase isoenzymes. J Biol Chem. 1990 Apr 25;265(12):6921-7. [PubMed Link Image]
  2. Haas RC, Korenfeld C, Zhang ZF, Perryman B, Roman D, Strauss AW: Isolation and characterization of the gene and cDNA encoding human mitochondrial creatine kinase. J Biol Chem. 1989 Feb 15;264(5):2890-7. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5994
Enzyme 4 Name Creatine kinase B-type
Enzyme 4 Synonyms
  1. Creatine kinase B chain
  2. B-CK
Enzyme 4 Gene Name CKB
Enzyme 4 Protein Sequence >Creatine kinase B-type 
MPFSNSHNALKLRFPAEDEFPDLSAHNNHMAKVLTPELYAELRAKSTPSGFTLDDVIQTG
VDNPGHPYIMTVGCVAGDEESYEVFKDLFDPIIEDRHGGYKPSDEHKTDLNPDNLQGGDD
LDPNYVLSSRVRTGRSIRGFCLPPHCSRGERRAIEKLAVEALSSLDGDLAGRYYALKSMT
EAEQQQLIDDHFLFDKPVSPLLLASGMARDWPDARGIWHNDNKTFLVWVNEEDHLRVISM
QKGGNMKEVFTRFCTGLTQIETLFKSKDYEFMWNPHLGYILTCPSNLGTGLRAGVHIKLP
NLGKHEKFSEVLKRLRLQKRGTGGVDTAAVGGVFDVSNADRLGFSEVELVQMVVDGVKLL
IEMEQRLEQGQAIDDLMPAQK
Enzyme 4 Number of Residues 381
Enzyme 4 Molecular Weight 42645
Enzyme 4 Theoretical pI 5.30
Enzyme 4 GO Classification
Function
  • catalytic activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
—
Component
—
Enzyme 4 General Function Not Available
Enzyme 4 Specific Function Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa
Enzyme 4 Pathways
Enzyme 4 Reactions
  • ATP + creatine = ADP + phosphocreatine
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 180572 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P12277 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name KCRB_HUMAN Link Image
Enzyme 4 PDB ID 1G0W Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1146 bp 
ATGCCCTTCTCCAACAGCCACAACGCACTGAAGCTGCGCTTCCCGGCCGAGGACGAGTTC
CCCGACCTGAGCGCCCACAACAACCACATGGCCAAGGTGCTGACCCCCGAGCTGTACGCG
GACGTGCGCGCCAAGAGCACGCCGAGCGGCTTCACGCTGGACGACGTCATCCAGACAGGC
GTGGACAACCCGGGCCACCCGTACATCATGACCGTGGGCTGCGTGGCGGGCGACGAGGAG
TCCTACGAAGTGTTCAAGGATCTCTTCGACCCCATCATCGAGGACCGGCACCGGCGCTAC
AAGCCCAGCGATGACGACAAGACCGACCTCAACCCCGACAACCTGCAGGGCGGCGACGAC
CTGGACCCCAACTACGTGCTGAGCTCGCGGGTGGCCACGGGCCGCAGCATCCGTGGCTTC
TGCCTCCCCCCGCACTGCAGCCGCGGGGAGCGCCGAGCCATCGAGAAGCTCGCGGTGGAA
GCCCTGTCCAGCCTGGACGGCGACCTGGCGGGCCGATACTACGCGCTCAAGAGCATGACG
GAGGCGGAGCAGCAGCAGCTCATCGACGACCACTTCCTCTTCGACAAGCCCGTGTCGCCC
CTGCTGCTGGCCTCGGGCATGGCCCGCGACTGGCCCGACGCCGCGCGTATCTGGCACAAT
GACAATAAGACCTTCCTGGTGTGGGTCAACGAGGAGGACCACCTGCGGGTCATCTCCATG
CAGAAGGGGGGCAACATGAAGGAGGTGTTCACCCGCTTCTGCACCGGCCTCACCCAGATT
GAAACTCTCTTCAAGTCTAAGGACTATGAGTTCATGTGGAACCCTCACCTGGGCTACATC
CTCACCTGCCCATCCAACCTGGGCACCGGGCTGCGGGCAGGTGTCGATATCAAGCTGCCC
AACCTGGGCAAGCATGAGAAGTTCTCGGAGGTGCTTAAGCGGCTGCGACTTCAGAAGCGA
GGCACAGGCGGTGTGGACACGGCTGCGGTGGGCGGGGTCTTCGACGTCTCCAACGCTGAC
CGCCTGGGCTTCTCAGAGGTGGAGCTGGTGCAGATGGTGGTGGACGGAGTGAAGCTGCTC
ATCGAGATGGAACAGCGGCTGGAGCAGGGCCAGGCCATCGACGACCTCATGCCTGCCCAG
AAATGA
Enzyme 4 GenBank Gene ID M16451 Link Image
Enzyme 4 GeneCard ID CKB Link Image
Enzyme 4 GenAtlas ID CKB Link Image
Enzyme 4 HGNC ID HGNC:1991 Link Image
Enzyme 4 Chromosome Location 14
Enzyme 4 Locus 14q32
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Villarreal-Levy G, Ma TS, Kerner SA, Roberts R, Perryman MB: Human creatine kinase: isolation and sequence analysis of cDNA clones for the B subunit, development of subunit specific probes and determination of gene copy number. Biochem Biophys Res Commun. 1987 May 14;144(3):1116-27. [PubMed Link Image]
  2. Mariman EC, Broers CA, Claesen CA, Tesser GI, Wieringa B: Structure and expression of the human creatine kinase B gene. Genomics. 1987 Oct;1(2):126-37. [PubMed Link Image]
  3. Kaye FJ, McBride OW, Battey JF, Gazdar AF, Sausville EA: Human creatine kinase-B complementary DNA. Nucleotide sequence, gene expression in lung cancer, and chromosomal assignment to two distinct loci. J Clin Invest. 1987 May;79(5):1412-20. [PubMed Link Image]
  4. Mariman EC, Schepens JT, Wieringa B: Complete nucleotide sequence of the human creatine kinase B gene. Nucleic Acids Res. 1989 Aug 11;17(15):6385. [PubMed Link Image]
  5. Daouk GH, Kaddurah-Daouk R, Putney S, Kingston R, Schimmel P: Isolation of a functional human gene for brain creatine kinase. J Biol Chem. 1988 Feb 15;263(5):2442-6. [PubMed Link Image]
  6. Lin L, Perryman MB, Friedman D, Roberts R, Ma TS: Determination of the catalytic site of creatine kinase by site-directed mutagenesis. Biochim Biophys Acta. 1994 May 18;1206(1):97-104. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5995
Enzyme 5 Name Creatine kinase, ubiquitous mitochondrial precursor
Enzyme 5 Synonyms
  1. U- MtCK
  2. Mia-CK
  3. Acidic-type mitochondrial creatine kinase
Enzyme 5 Gene Name CKMT1A
Enzyme 5 Protein Sequence >Creatine kinase, ubiquitous mitochondrial precursor 
MAGPFSRLLSARPGLRLLALAGAGSLAAGFLLRPEPVRAASERRRLYPPSAEYPDLRKHN
NCMASHLTPAVYARLCDKTTPTGWTLDQCIQTGVDNPGHPFIKTVGMVAGDEETYEVFAD
LFDPVIQERHNGYDPRTMKHTTDLDASKIRSGYFDERYVLSSRVRTGRSIRGLSLPPACT
RAERREVERVVVDALSGLKGDLAGRYYRLSEMTEAEQQQLIDDHFLFDKPVSPLLTAAGM
ARDWPDARGIWHNNEKSFLIWVNEEDHTRVISMEKGGNMKRVFERFCRGLKEVERLIQER
GWEFMWNERLGYILTCPSNLGTGLRAGVHIKLPLLSKDSRFPKILENLRLQKRGTGGVDT
AATGGVFDISNLDRLGKSEVELVQLVIDGVNYLIDCERRLERGQDIRIPTPVIHTKH
Enzyme 5 Number of Residues 417
Enzyme 5 Molecular Weight 47037
Enzyme 5 Theoretical pI 8.47
Enzyme 5 GO Classification
Function
  • catalytic activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
—
Component
—
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa
Enzyme 5 Pathways
Enzyme 5 Reactions
  • ATP + creatine = ADP + phosphocreatine
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-29
Enzyme 5 Transmembrane Regions Not Available
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 180590 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P12532 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name KCRU_HUMAN Link Image
Enzyme 5 PDB ID 1QK1 Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1254 bp 
ATGGCTGGTCCCTTCTCCCGTCTGCTGTCCGCCCGCCCGGGACTCAGGCTCCTGGCTTTG
GCCGGAGCGGGGTCTCTAGCCGCTGGGTTTCTGCTCCGACCGGAACCTGTACGAGCTGCC
AGTGAACGACGGAGGCTGTATCCCCCGAGCGCTGAGTACCCAGACCTCCGAAAGCACAAC
AACTGCATGGCCAGTCACCTGACCCCAGCAGTCTATGCACGGCTCTGCGACAAGACCACA
CCCACTGGTTGGACGCTAGATCAGTGTATCCAGACTGGCGTGGACAACCCTGGCCACCCC
TTCATCAAGACTGTGGGCATGGTGGCTGGAGATGAGGAGACCTATGAGGTATTTGCTGAC
CTGTTTGACCCTGTGATCCAAGAGCGACACAATGGATATGACCCCCGGACAATGAAGCAC
ACCACGGATCTAGATGCCAGTAAAATCCGTTCTGGCTACTTTGATGAGAGGTATGTATTG
TCCTCTAGAGTCAGAACTGGCCGAAGCATCCGAGGACTCAGTCTGCCTCCAGCTTGCACT
CGAGCAGAGCGACGAGAGGTGGAACGTGTTGTGGTGGATGCACTGAGTGGCCTGAAGGGT
GACCTGGCTGGACGTTACTATAGGCTCAGTGAGATGACAGAGGCTGAACAGCAGCAGCTT
ATTGATGACCACTTTCTGTTTGATAAGCCTGTGTCCCCGTTGCTGACTGCAGCAGGAATG
GCTCGAGACTGGCCAGATGCTCGTGGAATTTGGCACAACAATGAGAAGAGCTTCCTGATC
TGGGTGAATGAGGAGGATCATACACGGGTGATCTCCATGGAGAAGGGTGGTAACATGAAG
AGAGTGTTTGAAAGATTCTGCCGAGGCCTCAAAGAGGTGGAGAGACTTATCCAAGAACGT
GGCTGGGAGTTCATGTGGAATGAGCGTTTGGGATACATCTTGACCTGTCCATCTAACCTG
GGCACTGGACTTCGGGCAGGAGTGCACATCAAACTGCCCCTGCTAAGCAAAGATAGCCGC
TTCCCAAAGATCCTGGAGAACCTAAGACTCCAAAAACGTGGTACTGGAGGAGTGGACACT
GCTGCTACAGGCGGTGTCTTTGATATTTCTAATTTGGACCGACTAGGCAAATCAGAGGTG
GAGCTGGTGCAACTGGTCATCGATGGAGTAAACTATTTGATTGATTGTGAACGGCGTCTG
GAGAGAGGCCAGGATATCCGCATCCCCACACCTGTCATCCACACCAAGCATTAA
Enzyme 5 GenBank Gene ID J04469 Link Image
Enzyme 5 GeneCard ID CKMT1A Link Image
Enzyme 5 GenAtlas ID CKMT1A Link Image
Enzyme 5 HGNC ID HGNC:31736 Link Image
Enzyme 5 Chromosome Location 15
Enzyme 5 Locus 15q15
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Haas RC, Korenfeld C, Zhang ZF, Perryman B, Roman D, Strauss AW: Isolation and characterization of the gene and cDNA encoding human mitochondrial creatine kinase. J Biol Chem. 1989 Feb 15;264(5):2890-7. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5996
Enzyme 6 Name Creatine kinase M-type
Enzyme 6 Synonyms
  1. Creatine kinase M chain
  2. M-CK
Enzyme 6 Gene Name CKM
Enzyme 6 Protein Sequence >Creatine kinase M-type 
MPFGNTHNKFKLNYKPEEEYPDLSKHNNHMAKVLTLELYKKLRDKETPSGFTVDDVIQTG
VDNPGHPFIMTVGCVAGDEESYEVFKELFDPIISDRHGGYKPTDKHKTDLNHENLKGGDD
LDPNYVLSSRVRTGRSIKGYTLPPHCSRGERRAVEKLSVEALNSLTGEFKGKYYPLKSMT
EKEQQQLIDDHFLFDKPVSPLLLASGMARDWPDARGIWHNDNKSFLVWVNEEDHLRVISM
EKGGNMKEVFRRFCVGLQKIEEIFKKAGHPFMWNQHLGYVLTCPSNLGTGLRGGVHVKLA
HLSKHPKFEEILTRLRLQKRGTGGVDTAAVGSVFDVSNADRLGSSEVEQVQLVVDGVKLM
VEMEKKLEKGQSIDDMIPAQK
Enzyme 6 Number of Residues 381
Enzyme 6 Molecular Weight 43102
Enzyme 6 Theoretical pI 7.28
Enzyme 6 GO Classification
Function
  • catalytic activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
—
Component
—
Enzyme 6 General Function Not Available
Enzyme 6 Specific Function Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa
Enzyme 6 Pathways
Enzyme 6 Reactions
  • ATP + creatine = ADP + phosphocreatine
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 180576 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P06732 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name KCRM_HUMAN Link Image
Enzyme 6 PDB ID 1I0E Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1146 bp 
ATGCCATTCGGTAACACCCACAACAAGTTCAAGCTGAATTACAAGCCTGAGGAGGAGTAC
CCCGACCTCAGCAAACATAACAACCACATGGCCAAGGTACTGACCCTTGAACTCTACAAG
AAGCTGCGGGACAAGGAGATCCCATCTGGCTTCACTGTAGACGATGTCATCCAGACAGGA
GTGGACAACCCAGGTCACCCCTTCATCATGACCGTGGGCTGCGTGGCTGGTGATGAGGAG
TCCTACGAAGTTTTCAAGGAACTCTTTGACCCCATCATCTCGGATCGCCACGGGGGCTAC
AAACCCACTGACAAGCACAAGACTGACCTCAACCATGAAAACCTCAAGGGTGGAGACGAC
CTGGACCCCAACTACGTGCTCAGCAGCCCGGTCCGCACTGGCCGCAGCATCAAGGGCTAC
ACGTTGCCCCCACACTGCTCCCGTGGCGAGCGCCGGGCGGTGGAGAAGCTCTCTGTGGAA
GCTCTCAACAGCCTGACGGGCGAGTTCAAAGGGAAGTACTACCCTCTGAAGAGCATGACG
GAGAAGGAGCAGCAGCAGCTCATCGATGACCACTTCCAGTTCGACAAGCCCGTGTCCCCG
CTGCTGCTGGCCTCAGGCATGGCCCGCCACTGGCCCGACGCCCCTGGCATCTGGCACAAT
GACAACAAGAGCTTCCTGGTGTGGGTGAACGAGGAGGATCACCTCCGGGTCATCTCCATG
GAGAAGGGGGGCAACATGAAGGAGGTTTTCCGCCGCTTCTGCGTAGGGCTGCAGAAGATT
GAGGAGATCTTTAAGAAAGCTGGCCACCCCTTCATGTGGAACCAGCACCTGGGCTACGTG
CTCACCTGCCCATCCAACCTGGGCACTGGGCTGCGTGGAGGCGTGCATGTGAAGCTGGCG
CACCTGAGCAAGCACCCCAAGTTCGAGGAGATCCTCACCCGCCTGCGTCTGCAGAAGAGG
GGTACAGGTGCGGTGGACACAGCTGCCGTGGGCTCAGTATTTGACGTGTCCAACGCTGAT
CGGCTGGGCTCGTCCGAAGTAGAACAGGTGCAGCTGGTGGTGGATGGTGTGAAGCTCATG
GTGGAAATGGAGAAGAAGTTGGAGAAAGGCCAGTCCATCGACGACATGATCCCCGCCCAG
AAGTAG
Enzyme 6 GenBank Gene ID M14780 Link Image
Enzyme 6 GeneCard ID CKM Link Image
Enzyme 6 GenAtlas ID CKM Link Image
Enzyme 6 HGNC ID HGNC:1994 Link Image
Enzyme 6 Chromosome Location 19
Enzyme 6 Locus 19q13.2-q13.3
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Perryman MB, Kerner SA, Bohlmeyer TJ, Roberts R: Isolation and sequence analysis of a full-length cDNA for human M creatine kinase. Biochem Biophys Res Commun. 1986 Nov 14;140(3):981-9. [PubMed Link Image]
  2. Trask RV, Strauss AW, Billadello JJ: Developmental regulation and tissue-specific expression of the human muscle creatine kinase gene. J Biol Chem. 1988 Nov 15;263(32):17142-9. [PubMed Link Image]
  3. Nigro JM, Schweinfest CW, Rajkovic A, Pavlovic J, Jamal S, Dottin RP, Hart JT, Kamarck ME, Rae PM, Carty MD, et al.: cDNA cloning and mapping of the human creatine kinase M gene to 19q13. Am J Hum Genet. 1987 Feb;40(2):115-25. [PubMed Link Image]
  4. Hamburg RJ, Friedman DL, Olson EN, Ma TS, Cortez MD, Goodman C, Puleo PR, Perryman MB: Muscle creatine kinase isoenzyme expression in adult human brain. J Biol Chem. 1990 Apr 15;265(11):6403-9. [PubMed Link Image]
  5. Tang L, Zhou HM, Lin ZJ: Crystallization and preliminary X-ray analysis of human muscle creatine kinase. Acta Crystallogr D Biol Crystallogr. 1999 Mar;55(Pt 3):669-70. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 8380
Enzyme 7 Name Sodium- and chloride-dependent creatine transporter 1
Enzyme 7 Synonyms
  1. CT1
  2. Creatine transporter 1
  3. Solute carrier family 6 member 8
Enzyme 7 Gene Name SLC6A8
Enzyme 7 Protein Sequence >Sodium- and chloride-dependent creatine transporter 1 
MAKKSAENGIYSVSGDEKKGPLIAPGPDGAPAKGDGPVGLGTPGGRLAVPPRETWTRQMD
FIMSCVGFAVGLGNVWRFPYLCYKNGGGVFLIPYVLIALVGGIPIFFLEISLGQFMKAGS
INVWNICPLFKGLGYASMVIVFYCNTYYIMVLAWGFYYLVKSFTTTLPWATCGHTWNTPD
CVEIFRHEDCANASLANLTCDQLADRRSPVIEFWENKVLRLSGGLEVPGALNWEVTLCLL
ACWVLVYFCVWKGVKSTGKIVYFTATFPYVVLVVLLVRGVLLPGALDGIIYYLKPDWSKL
GSPQVWIDAGTQIFFSYAIGLGALTALGSYNRFNNNCYKDAIILALINSGTSFFAGFVVF
SILGFMAAEQGVHISKVAESGPGLAFIAYPRAVTLMPVAPLWAALFFFMLLLLGLDSQFV
GVEGFITGLLDLLPASYYFRFQREISVALCCALCFVIDLSMVTDGGMYVFQLFDYYSASG
TTLLWQAFWECVVVAWVYGADRFMDDIACMIGYRPCPWMKWCWSFFTPLVCMGIFIFNVV
YYEPLVYNNTYVYPWWGEAMGWAFALSSMLCVPLHLLGCLLRAKGTMAERWQHLTQPIWG
LHHLEYRAQDADVRGLTTLTPVSESSKVVVVESVM
Enzyme 7 Number of Residues 635
Enzyme 7 Molecular Weight 70523
Enzyme 7 Theoretical pI 6.38
Enzyme 7 GO Classification
Function
  • cofactor transporter activity
  • creatine transporter activity
  • creatine:sodium symporter activity
  • neurotransmitter transporter activity
  • neurotransmitter:sodium symporter activity
  • transporter activity
Process
  • cellular physiological process
  • neurotransmitter transport
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • integral to plasma membrane
  • intrinsic to membrane
  • membrane
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function Required for the uptake of creatine in muscles and brain
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • 61-81 88-108 139-159 231-251 270-290 305-325 342-362 395-415 445-465 480-500 521-541 561-581
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 493132 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P48029 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name SC6A8_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1908 bp 
ATGGCGAAGAAGAGCGCCGAGAACGGCATCTATAGCGTGTCCGGCGACGAGAAGAAGGGC
CCCCTCATCGCGCCCGGGCCCGACGGGGCCCCGGCCAAGGGCGACGGCCCCGTGGGCCTG
GGGACACCCGGCGGCCGCCTGGCCGTGCCGCCGCGCGAGACCTGGACGCGCCAGATGGAC
TTCATCATGTCGTGCGTGGGCTTCGCCGTGGGCTTGGGCAACGTGTGGCGCTTCCCCTAC
CTGTGCTACAAGAACGGCGGAGGTGTGTTCCTTATTCCCTACGTCCTGATCGCCCTGGTT
GGAGGAATCCCCATTTTCTTCTTAGAGATCTCGCTGGGCCAGTTCATGAAGGCCGGCAGC
ATCAATGTCTGGAACATCTGTCCCCTGTTCAAAGGCCTGGGCTACGCCTCCATGGTGATC
GTCTTCTACTGCAACACCTACTACATCATGGTGCTGGCCTGGGGCTTCTATTACCTGGTC
AAGTCCTTTACCACCACGCTGCCCTGGGCCACATGTGGCCACACCTGGAACACTCCCGAC
TGCGTGGAGATCTTCCGCCATGAAGACTGTGCCAATGCCAGCCTGGCCAACCTCACCTGT
GACCAGCTTGCTGACCGCCGGTCCCCTGTCATCGAGTTCTGGGAGAACAAAGTCTTGAGG
CTGTCTGGGGGACTGGAGGTGCCAGGGGCCCTCAACTGGGAGGTGACCCTTTGTCTGCTG
GCCTGCTGGGTGCTGGTCTACTTCTGTGTCTGGAAGGGGGTCAAATCCACGGGAAAGATC
GTGTACTTCACTGCTACATTCCCCTACGTGGTCCTGGTCGTGCTGCTGGTGCGTGGAGTG
CTGCTGCCTGGCCCCCTGGATGGCATCATTTACTATCTCAAGCCTGACTGGTCAAAGCTG
GGGTCCCCTCAGGTGTGGATAGATGCGGGGACCCAGATTTTCTTTTCTTACGCCATTGGC
CTGGGGGCCCTCACAGCCCTGGGCAGCTACAACCGCTTCAACAACAACTGCTACAAGGAC
GCCATCATCCTGGCTCTCATCAACAGTGGGACCAGCTTCTTTGCTGGCTTCGTGGTCTTC
TCCATCCTGGGCTTCATGGCTGCAGAGCAGGGCGTGCACATCTCCAAGGTGGCAGAGTCA
GGGCCGGGCCTGGCCTTCATCGCCTACCCGCGGGCTGTCACGCTGATGCCAGTGGCCCCA
CTCTGGGCTGCCCTGTTCTTCTTCATGCTGTTGCTGCTTGGTCTCGACAGCCAGTTTGTA
GGTGTGGAGGGCTTCATCACCGGCCTCCTCGACCTCCTCCCGGCCTCCTACTACTTCCGT
TTCCAAAGGGAGATCTCTGTGGCCCTCTGTTGTGCCCTCTGCTTTGTCATCGATCTCTCC
ATGGTGACTGATGGCGGGATGTACGTCTTCCAGCTGTTTGACTACTACTCGGCCAGCGGC
ACCACCCTGCTCTGGCAGGCCTTTTGGGAGTGCGTGGTGGTGGCCTGGGTGTACGGAGCT
GACCGCTTCATGGACGACATTGCCTGTATGATCGGGTACCGACCTTGCCCCTGGATGAAA
TGGTGCTGGTCCTTCTTCACCCCGCTGGTCTGCATGGGCATCTTCATCTTCAACGTTGTG
TACTACGAGCCGCTGGTCTACAACAACACCTACGTGTACCCGTGGTGGGGTGAGGCCATG
GGCTGGGCCTTCGCCCTGTCCTCCATGCTGTGCGTGCCGCTGCACCTCCTGGGCTGCCTC
CTCAGGGCCAAGGGCACCATGGCTGAGCGCTGGCAGCACCTGACCCAGCCCATCTGGGGC
CTCCACCACTTGGAGTACCGAGCTCAGGACGCAGATGTCAGGGGCCTGACCACCCTGACC
CCAGTGTCCGAGAGCAGCAAGGTCGTCGTGGTGGAGAGTGTCATGTGA
Enzyme 7 GenBank Gene ID L31409 Link Image
Enzyme 7 GeneCard ID SLC6A8 Link Image
Enzyme 7 GenAtlas ID SLC6A8 Link Image
Enzyme 7 HGNC ID HGNC:11055 Link Image
Enzyme 7 Chromosome Location X
Enzyme 7 Locus Xq28
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Nash SR, Giros B, Kingsmore SF, Rochelle JM, Suter ST, Gregor P, Seldin MF, Caron MG: Cloning, pharmacological characterization, and genomic localization of the human creatine transporter. Receptors Channels. 1994;2(2):165-74. [PubMed Link Image]
  2. Sora I, Richman J, Santoro G, Wei H, Wang Y, Vanderah T, Horvath R, Nguyen M, Waite S, Roeske WR, et al.: The cloning and expression of a human creatine transporter. Biochem Biophys Res Commun. 1994 Oct 14;204(1):419-27. [PubMed Link Image]
  3. Sandoval N, Bauer D, Brenner V, Coy JF, Drescher B, Kioschis P, Korn B, Nyakatura G, Poustka A, Reichwald K, Rosenthal A, Platzer M: The genomic organization of a human creatine transporter (CRTR) gene located in Xq28. Genomics. 1996 Jul 15;35(2):383-5. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 12998
Enzyme 8 Name cDNA FLJ78469, highly similar to Homo sapiens creatine kinase, brain
Enzyme 8 Synonyms
  1. CKB, mRNA
  2. Creatine kinase, brain, isoform CRA_c
Enzyme 8 Gene Name CKB
Enzyme 8 Protein Sequence >cDNA FLJ78469, highly similar to Homo sapiens creatine kinase, brain 
MPFSNSHNALKLRFPAEDEFPDLSAHNNHMAKVLTPELYAELRAKSTPSGFTLDDVIQTG
VDNPGHPYIMTVGCVAGDEESYEVFKDLFDPIIEDRHGGYKPSDEHKTDLNPDNLQGGDD
LDPNYVLSSRVRTGRSIRGFCLPPHCSRGERRAIEKLAVEALSSLDGDLAGRYYALKSMT
EAEQQQLIDDHFLFDKPVSPLLLASGMARDWPDARGIWHNDNKTFLVWVNEEDHLRVISM
QKGGNMKEVFTRFCTGLTQIETLFKSKDYEFMWNPHLGYILTCPSNLGTGLRAGVHIKLP
NLGKHEKFSEVLKRLRLQKRGTGGVDTAAVGGVFDVSNADRLGFSEVELVQMVVDGVKLL
IEMEQRLEQGQAIDDLMPAQK
Enzyme 8 Number of Residues 381
Enzyme 8 Molecular Weight 42645
Enzyme 8 Theoretical pI 5.30
Enzyme 8 GO Classification Not Available
Enzyme 8 General Function Not Available
Enzyme 8 Specific Function Not Available
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function Not Available
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 158261225 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID A8K236 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name A8K236_HUMAN Link Image
Enzyme 8 PDB ID 1G0W Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence Not Available
Enzyme 8 GenBank Gene ID AK290101 Link Image
Enzyme 8 GeneCard ID A8K236 Link Image
Enzyme 8 GenAtlas ID Not Available
Enzyme 8 HGNC ID Not Available
Enzyme 8 Chromosome Location Not Available
Enzyme 8 Locus Not Available
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References Not Available
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 17001
Enzyme 9 Name Paired mesoderm homeobox protein 1
Enzyme 9 Synonyms
  1. Paired-related homeobox protein 1
  2. PRX-1
  3. Homeobox protein PHOX1
Enzyme 9 Gene Name PRRX1
Enzyme 9 Protein Sequence >Paired mesoderm homeobox protein 1 
MTSSYGHVLERQPALGGRLDSPGNLDTLQAKKNFSVSHLLDLEEAGDMVAAQADENVGEA
GRSLLESPGLTSGSDTPQQDNDQLNSEEKKKRKQRRNRTTFNSSQLQALERVFERTHYPD
AFVREDLARRVNLTEARVQVWFQNRRAKFRRNERAMLANKNASLLKSYSGDVTAVEQPIV
PRPAPRPTDYLSWGTASPYSAMATYSATCANNSPAQGINMANSIANLRLKAKEYSLQRNQ
VPTVN
Enzyme 9 Number of Residues 245
Enzyme 9 Molecular Weight 27297
Enzyme 9 Theoretical pI 9.91
Enzyme 9 GO Classification
Function
  • DNA binding
  • binding
  • nucleic acid binding
  • transcription factor activity
Process
  • development
  • regulation of biological process
  • regulation of cellular metabolism
  • regulation of metabolism
  • regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • regulation of physiological process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 9 General Function Not Available
Enzyme 9 Specific Function Acts as a transcriptional regulator of muscle creatine kinase (MCK) and so has a role in the establishment of diverse mesodermal muscle types. The protein binds to an A/T-rich element in the muscle creatine enhancer
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein Not Available
Enzyme 9 UniProtKB/Swiss-Prot ID P54821 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name PRRX1_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence Not Available
Enzyme 9 GenBank Gene ID Z97200 Link Image
Enzyme 9 GeneCard ID P54821 Link Image
Enzyme 9 GenAtlas ID PRRX1 Link Image
Enzyme 9 HGNC ID HGNC:9142 Link Image
Enzyme 9 Chromosome Location Not Available
Enzyme 9 Locus Not Available
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Grueneberg DA, Natesan S, Alexandre C, Gilman MZ: Human and Drosophila homeodomain proteins that enhance the DNA-binding activity of serum response factor. Science. 1992 Aug 21;257(5073):1089-95. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 17002
Enzyme 10 Name DNA-binding protein inhibitor ID-3
Enzyme 10 Synonyms
  1. Inhibitor of DNA binding 3
  2. ID-like protein inhibitor HLH 1R21
  3. Helix-loop-helix protein HEIR-1
Enzyme 10 Gene Name ID3
Enzyme 10 Protein Sequence >DNA-binding protein inhibitor ID-3 
MKALSPVRGCYEAVCCLSERSLAIARGRGKGPAAEEPLSLLDDMNHCYSRLRELVPGVPR
GTQLSQVEILQRVIDYILDLQVVLAEPAPGPPDGPHLPIQTAELAPELVISNDKRSFCH
Enzyme 10 Number of Residues 119
Enzyme 10 Molecular Weight 12969
Enzyme 10 Theoretical pI 5.64
Enzyme 10 GO Classification
Function
  • transcription regulator activity
Process
  • regulation of biological process
  • regulation of cellular metabolism
  • regulation of metabolism
  • regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • regulation of physiological process
  • regulation of transcription
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 10 General Function Not Available
Enzyme 10 Specific Function ID (inhibitor of DNA binding) HLH proteins lack a basic DNA-binding domain but are able to form heterodimers with other HLH proteins, thereby inhibiting DNA binding. ID-3 inhibits the binding of E2A-containing protein complexes to muscle creatine kinase E-box enhancer. May inhibit other transcription factors
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions Not Available
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein Not Available
Enzyme 10 UniProtKB/Swiss-Prot ID Q02535 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name ID3_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 X69111 Link Image
Enzyme 10 GeneCard ID Q02535 Link Image
Enzyme 10 GenAtlas ID ID3 Link Image
Enzyme 10 HGNC ID HGNC:5362 Link Image
Enzyme 10 Chromosome Location Not Available
Enzyme 10 Locus Not Available
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Deed RW, Bianchi SM, Atherton GT, Johnston D, Santibanez-Koref M, Murphy JJ, Norton JD: An immediate early human gene encodes an Id-like helix-loop-helix protein and is regulated by protein kinase C activation in diverse cell types. Oncogene. 1993 Mar;8(3):599-607. [PubMed Link Image]
  2. Deed RW, Hirose T, Mitchell EL, Santibanez-Koref MF, Norton JD: Structural organisation and chromosomal mapping of the human Id-3 gene. Gene. 1994 Dec 30;151(1-2):309-14. [PubMed Link Image]
  3. Ellmeier W, Aguzzi A, Kleiner E, Kurzbauer R, Weith A: Mutually exclusive expression of a helix-loop-helix gene and N-myc in human neuroblastomas and in normal development. EMBO J. 1992 Jul;11(7):2563-71. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 17003
Enzyme 11 Name Creatine transporter SLC6A8 splice variant C
Enzyme 11 Synonyms Not Available
Enzyme 11 Gene Name SLC6A8
Enzyme 11 Protein Sequence >Creatine transporter SLC6A8 splice variant C 
MAAEQGVHISKVAESGPGLAFIAYPRAVTLMPVAPLWAALFFFMLLLLGLDSQFVGVEGF
ITGLLDLLPASYYFRFQREISVALCCALCFVIDLSMVTDGGMYVFQLFDYYSASGTTLLW
QAFWECVVVAWVYGADRFMDDIACMIGYRPCPWMKWCWSFFTPLVCMGIFIFNVVYYEPL
VYNNTYVYPWWGEAMGWAFALSSMLCVPLHLLGCLLRAKGTMAERWQHLTQPIWGLHHLE
YRAQDADVRGLTTLTPVSESSKVVVVESVM
Enzyme 11 Number of Residues 270
Enzyme 11 Molecular Weight 30580
Enzyme 11 Theoretical pI 4.78
Enzyme 11 GO Classification
Function
  • neurotransmitter transporter activity
  • neurotransmitter:sodium symporter activity
  • transporter activity
Process
  • cellular physiological process
  • neurotransmitter transport
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • integral to plasma membrane
  • intrinsic to membrane
  • membrane
Enzyme 11 General Function Not Available
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 B2KY47 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name B2KY47_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 EU280316 Link Image
Enzyme 11 GeneCard ID B2KY47 Link Image
Enzyme 11 GenAtlas ID Not Available
Enzyme 11 HGNC ID Not Available
Enzyme 11 Chromosome Location Not Available
Enzyme 11 Locus Not Available
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References Not Available
Enzyme 11 Metabolite References Not Available