|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5683 |
| Enzyme 1 Name |
Cytochrome P450 11B1, mitochondrial precursor |
| Enzyme 1 Synonyms |
- CYPXIB1
- P450C11
- P-450c11
- Steroid 11-beta-hydroxylase
|
| Enzyme 1 Gene Name |
CYP11B1 |
| Enzyme 1 Protein Sequence |
>Cytochrome P450 11B1, mitochondrial precursor
MALRAKAEVCMAVPWLSLQRAQALGTRAARVPRTVLPFEAMPQRPGNRWLRLLQIWREQG
YEDLHLEVHQTFQELGPIFRYDLGGAGMVCVMLPEDVEKLQQVDSLHPHRMSLEPWVAYR
QHRGHKCGVFLLNGPEWRFNRLRLNPEVLSPNAVQRFLPMVDAVARDFSQALKKKVLQNA
RGSLTLDVQPSIFHYTIEASNLALFGERLGLVGHSPSSASLNFLHALEVMFKSTVQLMFM
PRSLSRWTSPKVWKEHFEAWDCIFQYGDNCIQKIYQELAFSRPQQYTSIVAELLLNAELS
PDAIKANSMELTAGSVDTTVFPLLMTLFELARNPNVQQALRQESLAAAASISEHPQKATT
ELPLLRAALKETLRLYPVGLFLERVVSSDLVLQNYHIPAGTLVRVFLYSLGRNPALFPRP
ERYNPQRWLDIRGSGRNFYHVPFGFGMRQCLGRRLAEAEMLLLLHHVLKHLQVETLTQED
IKMVYSFILRPSMCPLLTFRAIN
|
| Enzyme 1 Number of Residues |
503 |
| Enzyme 1 Molecular Weight |
57530 |
| Enzyme 1 Theoretical pI |
9.42 |
| Enzyme 1 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- oxidoreductase activity
- tetrapyrrole binding
- transition metal ion binding
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 1 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 1 Specific Function |
Has steroid 11-beta-hydroxylase activity. In addition to this activity, the 18 or 19-hydroxylation of steroids and the aromatization of androstendione to estrone have also been ascribed to cytochrome P450 XIB |
| Enzyme 1 Pathways |
- Androgen and Estrogen Metabolism (map00150
)
- C21 Steroid Hormone Metabolism (map00140
)
|
| Enzyme 1 Reactions |
- a steroid + reduced adrenal ferredoxin + O2 = an 11beta-hydroxysteroid + oxidized adrenal ferredoxin + H2O
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
Not Available |
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
181333  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P15538  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
C11B1_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1512 bp
ATGGCACTCAGGGCAAAGGCAGAGGTGTGCATGGCAGTGCCCTGGCTGTCCCTGCAAAGG
GCACAGGCACTGGGCACGAGAGCCGCCCGGGTCCCCAGGACAGTGCTGCCCTTTGAAGCC
ATGCCCCGGCGTCCAGGCAACAGGTGGCTGAGGCTGCTGCAGATCTGGAGGGAGCAGGGT
TATGAGGACCTGCACCTGGAAGTACACCAGACCTTCCAGGAACTGGGGCCCATTTTCAGG
TACGATTTGGGAGGAGCAGGCATGGTGTGTGTGATGCTGCCGGAGGACGTGGAGAAGCTG
CAACAGGTGGACAGCCTGCATCCCCACAGGATGAGCCTGGAGCCCTGGGTGGCCTACAGA
CAACATCGTGGGCACAAATGTGGCGTGTTCTTGCTGAATGGGCCTGAATGGCGCTTCAAC
CGATTGCGGCTGAATCCAGAAGTGCTGTCGCCCAACGCTGTGCAGAGGTTCCTCCCGATG
GTGGATGCAGTGGCCAGGGACTTCTCCCAGGCCCTGAAGAAGAAGGTGCTGCAGAACGCC
CGGGGGAGCCTGACCCTGGACGTCCAGCCCAGCATCTTCCACTACACCATAGAAGCCAGC
AACTTGGCTCTTTTTGGAGAGCGGCTGGGCCTGGTTGGCCACAGCCCCAGTTCTGCCAGC
CTGAACTTCCTCCATGCCCTGGAGGTCATGTTCAAATCCACCGTCCAGCTCATGTTCATG
CCCAGGAGCCTGTCTCGCTGGACCAGCCCCAAGGTGTGGAAGGAGCACTTTGAGGCCTGG
GACTGCATCTTCCAGTACGGCGACAACTGTATCCAGAAAATCTATCAGGAACTGGCCTTC
AGCCGCCCTCAACAGTACACCAGCATCGTGGCGGAGCTCCTGTTGAATGCGGAACTGTCG
CCAGATGCCATCAAGGCCAACTCTATGGAACTCACTGCAGGGAGCGTGGACACGACGGTG
TTTCCCTTGCTGATGACGCTCTTTGAGCTGGCTCGGAACCCCAACGTGCAGCAGGCCCTG
CGCCAGGAGAGCCTGGCCGCCGCAGCCAGCATCAGTGAACATCCCCAGAAGGCAACCACC
GAGCTGCCCTTGCTGCGTGCGGCCCTCAAGGAGACCTTGCGGCTCTACCCTGTGGGTCTG
TTTCTGGAGCGAGTGGCGAGCTCAGACTTGGTGCTTCAGAACTACCACATCCCAGCTGGG
ACATTGGTGCGCGTGTTCCTCTACTCTCTGGGTCGCAACCCCGCCTTGTTCCCGAGGCCT
GAGCGCTATAACCCCCAGCGCTGGCTAGACATCAGGGGCTCCGGCAGGAACTTCTACCAC
GTGCCCTTTGGCTTTGGCATGCGCCAGTGCCTTGGGCGGCGCCTGGCAGAGGCAGAGATG
CTGCTGCTGCTGCACCATGTGCTGAAACACCTCCAGGTGGAGACACTAACCCAAGAGGAC
ATAAAGATGGTCTACAGCTTCATATTGAGGCCCAGCATGTGCCCCCTCCTCACCTTCAGA
GCCATCAACTAA
|
| Enzyme 1 GenBank Gene ID |
M32879  |
| Enzyme 1 GeneCard ID |
CYP11B1  |
| Enzyme 1 GenAtlas ID |
CYP11B1  |
| Enzyme 1 HGNC ID |
HGNC:2591  |
| Enzyme 1 Chromosome Location |
8 |
| Enzyme 1 Locus |
8q21 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Mornet E, Dupont J, Vitek A, White PC: Characterization of two genes encoding human steroid 11 beta-hydroxylase (P-450(11) beta). J Biol Chem. 1989 Dec 15;264(35):20961-7. [PubMed
]
- Kawamoto T, Mitsuuchi Y, Toda K, Miyahara K, Yokoyama Y, Nakao K, Hosoda K, Yamamoto Y, Imura H, Shizuta Y: Cloning of cDNA and genomic DNA for human cytochrome P-45011 beta. FEBS Lett. 1990 Sep 3;269(2):345-9. [PubMed
]
- Naiki Y, Kawamoto T, Mitsuuchi Y, Miyahara K, Toda K, Orii T, Imura H, Shizuta Y: A nonsense mutation (TGG [Trp116]-->TAG [Stop]) in CYP11B1 causes steroid 11 beta-hydroxylase deficiency. J Clin Endocrinol Metab. 1993 Dec;77(6):1677-82. [PubMed
]
- Chua SC, Szabo P, Vitek A, Grzeschik KH, John M, White PC: Cloning of cDNA encoding steroid 11 beta-hydroxylase (P450c11). Proc Natl Acad Sci U S A. 1987 Oct;84(20):7193-7. [PubMed
]
- Kawamoto T, Mitsuuchi Y, Toda K, Yokoyama Y, Miyahara K, Miura S, Ohnishi T, Ichikawa Y, Nakao K, Imura H, et al.: Role of steroid 11 beta-hydroxylase and steroid 18-hydroxylase in the biosynthesis of glucocorticoids and mineralocorticoids in humans. Proc Natl Acad Sci U S A. 1992 Feb 15;89(4):1458-62. [PubMed
]
- White PC, Dupont J, New MI, Leiberman E, Hochberg Z, Rosler A: A mutation in CYP11B1 (Arg-448----His) associated with steroid 11 beta-hydroxylase deficiency in Jews of Moroccan origin. J Clin Invest. 1991 May;87(5):1664-7. [PubMed
]
- Joehrer K, Geley S, Strasser-Wozak EM, Azziz R, Wollmann HA, Schmitt K, Kofler R, White PC: CYP11B1 mutations causing non-classic adrenal hyperplasia due to 11 beta-hydroxylase deficiency. Hum Mol Genet. 1997 Oct;6(11):1829-34. [PubMed
]
- Loidi L, Quinteiro C, Barros F, Dominguez F, Barreiro J, Pombo M: The C494F variant in the CYP11B1 gene is a sequence polymorphism in the Spanish population. J Clin Endocrinol Metab. 1999 Dec;84(12):4749. [PubMed
]
- Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed
]
- Halushka MK, Fan JB, Bentley K, Hsie L, Shen N, Weder A, Cooper R, Lipshutz R, Chakravarti A: Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis. Nat Genet. 1999 Jul;22(3):239-47. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5808 |
| Enzyme 2 Name |
Cytochrome P450 11B2, mitochondrial precursor |
| Enzyme 2 Synonyms |
- CYPXIB2
- P-450Aldo
- Aldosterone synthase
- ALDOS
- Aldosterone-synthesizing enzyme
- Steroid 18-hydroxylase
- P-450C18
|
| Enzyme 2 Gene Name |
CYP11B2 |
| Enzyme 2 Protein Sequence |
>Cytochrome P450 11B2, mitochondrial precursor
MALRAKAEVCVAAPWLSLQRARALGTRAARAPRTVLPFEAMPQHPGNRWLRLLQIWREQG
YEHLHLEMHQTFQELGPIFRYNLGGPRMVCVMLPEDVEKLQQVDSLHPCRMILEPWVAYR
QHRGHKCGVFLLNGPEWRFNRLRLNPDVLSPKAVQRFLPMVDAVARDFSQALKKKVLQNA
RGSLTLDVQPSIFHYTIEASNLALFGERLGLVGHSPSSASLNFLHALEVMFKSTVQLMFM
PRSLSRWISPKVWKEHFEAWDCIFQYGDNCIQKIYQELAFNRPQHYTGIVAELLLKAELS
LEAIKANSMELTAGSVDTTAFPLLMTLFELARNPDVQQILRQESLAAAASISEHPQKATT
ELPLLRAALKETLRLYPVGLFLERVVSSDLVLQNYHIPAGTLVQVFLYSLGRNAALFPRP
ERYNPQRWLDIRGSGRNFHHVPFGFGMRQCLGRRLAEAEMLLLLHHVLKHFLVETLTQED
IKMVYSFILRPGTSPLLTFRAIN
|
| Enzyme 2 Number of Residues |
503 |
| Enzyme 2 Molecular Weight |
57561 |
| Enzyme 2 Theoretical pI |
9.78 |
| Enzyme 2 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- oxidoreductase activity
- tetrapyrrole binding
- transition metal ion binding
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 2 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 2 Specific Function |
Preferentially catalyzes the conversion of 11- deoxycorticosterone to aldosterone via corticosterone and 18- hydroxycorticosterone |
| Enzyme 2 Pathways |
- C21 Steroid Hormone Metabolism (map00140
)
|
| Enzyme 2 Reactions |
- corticosterone + reduced adrenal ferredoxin + O2 = 18-hydroxycorticosterone + oxidized adrenal ferredoxin + H2O
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
181340  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P19099  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
C11B2_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1512 bp
ATGGCACTCAGGGCAAAGGCAGAGGTGTGCGTGGCAGCGCCCTGGCTGTGCCTGCAAAGG
GCACGGGCACTGGGCACTAGAGCCGCTCGGGCCCCTAGGACGGTGCTGCCGTTTGAAGCC
ATGCCCCAGCATCCAGGCAACAGGTGGCTGAGGCTGCTGCAGATGTGGAGGGAGCAGGGT
TATGAGCACCTGCACCTGGAGATGCACCAGACCTTCCAGGAGCTGGGGCCCATTTTCAGG
TACAACTTGGGAGGACCACGCATGGTGTGTGTGATGCTGCCGGAGGATGTGGAGAAGCTG
CAACAGGTGGACAGCCTGCATCCCTGCAGGATGATCCTGGAGCCCTGGGTGGCCATCAGA
CAACATCGTGGGCACAAATGTGGCGTGTTCTTGTTGAATGGGCCTGAATGGCGCTTCAAC
CGATTGCGGCTGAACCCAGATGTGCTGTCGCCCAAGGCCGTGCAGAGGTTCCTCCCGATG
GTGGATGCAGTGGCCAGGGACTTTTCCCAGGCCCTGAGGAAGAAGGTGCTGCAGAACGCC
CGGGGGAGCCTGACCCTGGACGTCCAGCCCAGCATCTTCCACTACACCATAGAAGCCAGC
AACTTAGCTCTTTTTGGAGAGCGGCTGGGCCTGGTTGGCCACAGCCCCAGTTCTGCCAGC
CTGAACTTCCTCCATGCCCTGGAGGTCATGTTCAAATCCACCGTCCAGCTCATGTTCATG
CCCAGGAGCCTGTCTCGCTGGATCAGCCCCAAGGTGTGGAAGGAGCACTTTGAGGCCTGG
GACTGCATCTTCCAGTACGGTGACAACTGTATCCAGAAAATCTACCAGGAACTGGCCTTC
AACCGCCCTCAACACTACACAGGCATCGTGGCAGAGCTCCTGTTGAAGGCGGAACTGTCA
CTAGAAGCCATCAAGGCCAACTCTATGGAACTCACTGCAGGGAGCGTGGACACGACAGCG
TTTCCGTTGCTGATGACGCTCTTTGAGCTGGCTCGGAACCCCGACGTGCAGCAGATCCTG
CGCAAGGAGAGCCTGGCCGCCGCAGCCAGCATCAGTGAACATCCCCAGAAGGCAACCACC
GAGCTGCCCTTGCTGCGGGCGGCCCTCAAGGAGACCTTGAGGCTCTACCCTGTGGGTCTG
TTTTTGGAGCGAGTGGTGAGCTCAGACTTGGTGCTTCAGAACTACCACATCCCAGCTGGG
ACATTGGTACAGGTTTTCCTCTACTCGCTGGGTCGCAATGCCGCCTTGTTCCCGAGGCCT
GAGCGGTATAATCCCCAGCGCTGGCTAGACATCAGGGGCTCCGGCAGGAACTTGCACCAC
GTGCCCTTTGGCTTTGGCATGCGCCAGTGCCTCGGGCGGCGCCTGGCAGAGGCAGAGATG
CTGCTGCTGCTGCACCACGTGCTGAAGCGCTTCCTGGTGGAGACACTAACTCAAGAGGAC
ATAAAGATGGTCTACAGCTTCATATTGAGGCCTGGCACGTCCCCCCTCCTCACTTTCAGA
GCGATTAACTAG
|
| Enzyme 2 GenBank Gene ID |
M32881  |
| Enzyme 2 GeneCard ID |
CYP11B2  |
| Enzyme 2 GenAtlas ID |
CYP11B2  |
| Enzyme 2 HGNC ID |
HGNC:2592  |
| Enzyme 2 Chromosome Location |
8 |
| Enzyme 2 Locus |
8q21-q22 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Mornet E, Dupont J, Vitek A, White PC: Characterization of two genes encoding human steroid 11 beta-hydroxylase (P-450(11) beta). J Biol Chem. 1989 Dec 15;264(35):20961-7. [PubMed
]
- Kawainoto T, Mitsuuchi Y, Ohnishi T, Ichikawa Y, Yokoyama Y, Sumimoto H, Toda K, Miyahara K, Kuribayashi I, Nakao K, et al.: Cloning and expression of a cDNA for human cytochrome P-450aldo as related to primary aldosteronism. Biochem Biophys Res Commun. 1990 Nov 30;173(1):309-16. [PubMed
]
- Pascoe L, Curnow KM, Slutsker L, Rosler A, White PC: Mutations in the human CYP11B2 (aldosterone synthase) gene causing corticosterone methyloxidase II deficiency. Proc Natl Acad Sci U S A. 1992 Jun 1;89(11):4996-5000. [PubMed
]
- Mitsuuchi Y, Kawamoto T, Naiki Y, Miyahara K, Toda K, Kuribayashi I, Orii T, Yasuda K, Miura K, Nakao K, et al.: Congenitally defective aldosterone biosynthesis in humans: the involvement of point mutations of the P-450C18 gene (CYP11B2) in CMO II deficient patients. Biochem Biophys Res Commun. 1992 Jan 31;182(2):974-9. [PubMed
]
- Mitsuuchi Y, Kawamoto T, Miyahara K, Ulick S, Morton DH, Naiki Y, Kuribayashi I, Toda K, Hara T, Orii T, et al.: Congenitally defective aldosterone biosynthesis in humans: inactivation of the P-450C18 gene (CYP11B2) due to nucleotide deletion in CMO I deficient patients. Biochem Biophys Res Commun. 1993 Feb 15;190(3):864-9. [PubMed
]
- Nomoto S, Massa G, Mitani F, Ishimura Y, Miyahara K, Toda K, Nagano I, Yamashiro T, Ogoshi S, Fukata J, Onishi S, Hashimoto K, Doi Y, Imura H, Shizuta Y: CMO I deficiency caused by a point mutation in exon 8 of the human CYP11B2 gene encoding steroid 18-hydroxylase (P450C18). Biochem Biophys Res Commun. 1997 May 19;234(2):382-5. [PubMed
]
- Peter M, Bunger K, Solyom J, Sippell WG: Mutation THR-185 ILE is associated with corticosterone methyl oxidase deficiency type II. Eur J Pediatr. 1998 May;157(5):378-81. [PubMed
]
- Portrat-Doyen S, Tourniaire J, Richard O, Mulatero P, Aupetit-Faisant B, Curnow KM, Pascoe L, Morel Y: Isolated aldosterone synthase deficiency caused by simultaneous E198D and V386A mutations in the CYP11B2 gene. J Clin Endocrinol Metab. 1998 Nov;83(11):4156-61. [PubMed
]
- Tamaki S, Iwai N, Tsujita Y, Kinoshita M: Genetic polymorphism of CYP11B2 gene and hypertension in Japanese. Hypertension. 1999 Jan;33(1 Pt 2):266-70. [PubMed
]
- Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed
]
- Halushka MK, Fan JB, Bentley K, Hsie L, Shen N, Weder A, Cooper R, Lipshutz R, Chakravarti A: Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis. Nat Genet. 1999 Jul;22(3):239-47. [PubMed
]
- Kayes-Wandover KM, Schindler RE, Taylor HC, White PC: Type 1 aldosterone synthase deficiency presenting in a middle-aged man. J Clin Endocrinol Metab. 2001 Mar;86(3):1008-12. [PubMed
]
- Dunlop FM, Crock PA, Montalto J, Funder JW, Curnow KM: A compound heterozygote case of type II aldosterone synthase deficiency. J Clin Endocrinol Metab. 2003 Jun;88(6):2518-26. [PubMed
]
|
| Enzyme 2 Metabolite References |
- Freel EM, Ingram M, Wallace AM, White A, Fraser R, Davies E, Connell JM: Effect of variation in CYP11B1 and CYP11B2 on corticosteroid phenotype and hypothalamic-pituitary-adrenal axis activity in hypertensive and normotensive subjects. Clin Endocrinol (Oxf). 2008 May;68(5):700-6. Epub 2007 Nov 2. [PubMed
]
|
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5822 |
| Enzyme 3 Name |
3-oxo-5-beta-steroid 4-dehydrogenase |
| Enzyme 3 Synonyms |
- Delta(4-3- ketosteroid 5-beta-reductase
- Aldo-keto reductase family 1 member D1
|
| Enzyme 3 Gene Name |
AKR1D1 |
| Enzyme 3 Protein Sequence |
>3-oxo-5-beta-steroid 4-dehydrogenase
MDLSAASHRIPLSDGNSIPIIGLGTYSEPKSTPKGACATSVKVAIDTGYRHIDGAYIYQN
EHEVGEAIREKIAEGKVRREDIFYCGKLWATNHVPEMVRPTLERTLRVLQLDYVDLYIIE
VPMAFKPGDEIYPRDENGKWLYHKSNLCATWEAMEACKDAGLVKSLGVSNFNRRQLELIL
NKPGLKHKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTSRNPIWVNVSSPPLLK
DALLNSLGKRYNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIE
ALNKNVRFVELLMWRDHPEYPFHDEY
|
| Enzyme 3 Number of Residues |
326 |
| Enzyme 3 Molecular Weight |
37377 |
| Enzyme 3 Theoretical pI |
7.58 |
| Enzyme 3 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 3 General Function |
Not Available |
| Enzyme 3 Specific Function |
Efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites. The bile acid intermediates 7- alpha,12-alpha-dihydroxy-4-cholesten-3-one and 7-alpha-hydroxy-4- cholesten-3-one can also act as substrates |
| Enzyme 3 Pathways |
- C21 Steroid Hormone Metabolism (map00140
)
|
| Enzyme 3 Reactions |
- 4,5beta-dihydrocortisone + NADP+ = cortisone + NADPH + H+
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
431857  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P51857  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
AK1D1_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>981 bp
ATGGATCTCAGTGCTGCAAGTCACCGCATACCTCTAAGTGATGGAAACAGCATTCCCATC
ATCGGACTTGGTACCTACTCAGAACCTAAATCGACCCCTAAGGGAGCCTGTGCAACATCG
GTGAAGGTTGCTATTGACACAGGGTACCGACATATTGATGGGGCCTACATCTACCAAAAT
GAACACGAAGTTGGGGAGGCCATCAGGGAGAAGATAGCAGAAGGAAAGGTGCGGAGGGAA
GATATCTTCTACTGTGGAAAGCTATGGGCTACAAATCATGTCCCAGAGATGGTCCGCCCA
ACCCTGGAGAGGACACTCAGGGTCCTCCAGCTAGATTATGTGGATCTTTACATCATTGAA
GTACCCATGGCCTTTAAGCCAGGAGATGAAATATACCCTAGAGATGAGAATGGCAAATGG
TTATATCACAAGTCAAATCTGTGTGCCACTTGGGAGGCGATGGAAGCTTGCAAAGACGCT
GGCTTGGTGAAATCCCTGGGAGTGTCCAATTTTAACCGCAGGCAGCTGGAGCTCATCCTG
AACAAGCCAGGACTCAAACACAAGCCAGTCAGCAACCAGGTTGAGTGCCATCCGTATTTC
ACCCAGCCAAAACTCTTGAAATTTTGCCAACAACATGACATTGTCATTACTGCATATAGC
CCTTTGGGGACCAGTAGGAATCCAATCTGGGTGAATGTTTCTTCTCCACCTTTGTTAAAG
GATGCACTTCTAAACTCATTGGGGAAAAGGTACAATAAGACAGCAGCTCAAATTGTTTTG
CGTTTCAACATCCAGCGAGGGGTGGTTGTCATTCCTAAAAGCTTTAATCTTGAAAGGATC
AAAGAAAATTTTCAGATCTTTGACTTTTCTCTCACTGAAGAAGAAATGAAGGACATTGAA
GCCTTGAATAAAAATGTCCGCTTTGTAGAATTGCTCATGTGGCGCGATCATCCTGAATAC
CCATTTCATGATGAATACTGA
|
| Enzyme 3 GenBank Gene ID |
Z28339  |
| Enzyme 3 GeneCard ID |
AKR1D1  |
| Enzyme 3 GenAtlas ID |
AKR1D1  |
| Enzyme 3 HGNC ID |
HGNC:388  |
| Enzyme 3 Chromosome Location |
7 |
| Enzyme 3 Locus |
7q32-q33 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Kondo KH, Kai MH, Setoguchi Y, Eggertsen G, Sjoblom P, Setoguchi T, Okuda KI, Bjorkhem I: Cloning and expression of cDNA of human delta 4-3-oxosteroid 5 beta-reductase and substrate specificity of the expressed enzyme. Eur J Biochem. 1994 Jan 15;219(1-2):357-63. [PubMed
]
- Charbonneau A, The VL: Genomic organization of a human 5beta-reductase and its pseudogene and substrate selectivity of the expressed enzyme. Biochim Biophys Acta. 2001 Jan 26;1517(2):228-35. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
6554 |
| Enzyme 4 Name |
Serine/threonine-protein kinase Sgk1 |
| Enzyme 4 Synonyms |
- Serum/glucocorticoid-regulated kinase 1
|
| Enzyme 4 Gene Name |
SGK |
| Enzyme 4 Protein Sequence |
>Serine/threonine-protein kinase Sgk1
MTVKTEAAKGTLTYSRMRGMVAILIAFMKQRRMGLNDFIQKIANNSYACKHPEVQSILKI
SQPQEPELMNANPSPPPSPSQQINLGPSSNPHAKPSDFHFLKVIGKGSFGKVLLARHKAE
EVFYAVKVLQKKAILKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTADKLYFVLDYIN
GGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTD
FGLCKENIEHNSTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSR
NTAEMYDNILNKPLQLKPNITNSARHLLEGLLQKDRTKRLGAKDDFMEIKSHVFFSLINW
DDLINKKITPPFNPNVSGPNDLRHFDPEFTEEPVPNSIGKSPDSVLVTASVKEAAEAFLG
FSYAPPTDSFL
|
| Enzyme 4 Number of Residues |
431 |
| Enzyme 4 Molecular Weight |
48943 |
| Enzyme 4 Theoretical pI |
8.81 |
| Enzyme 4 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleotide binding
- protein kinase activity
- protein serine/threonine kinase activity
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biopolymer metabolism
- biopolymer modification
- macromolecule metabolism
- metabolism
- physiological process
- protein amino acid phosphorylation
- protein modification
|
| Component |
| — |
|
| Enzyme 4 General Function |
Not Available |
| Enzyme 4 Specific Function |
Protein kinase that plays an important role in cellular stress response. Activates certain potassium, sodium, and chloride channels, suggesting an involvement in the regulation of processes such as cell survival, neuronal excitability, and renal sodium excretion. Sustained high levels and activity may contribute to conditions such as hypertension and diabetic nephropathy. Mediates cell survival signals, phosphorylates and negatively regulates pro-apoptotic FOXO3A. Phosphorylates NEDD4L, which leads to its inactivation and to the subsequent activation of various channels and transporters such as ENaC, Kv1.3, or EAAT1 |
| Enzyme 4 Pathways |
Not Available |
| Enzyme 4 Reactions |
Not Available |
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
1834511  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
O00141  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
SGK1_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>1296 bp
ATGACGGTGAAAACTGAGGCTGCTAAGGGCACCCTCACTTACTCCAGGATGAGGGGCATG
GTGGCAATTCTCATCGCTTTCATGAAGCAGAGGAGGATGGGTCTGAACGACTTTATTCAG
AAGATTGCCAATAACTCCTATGCATGCAAACACCCTGAAGTTCAGTCCATCTTGAAGATC
TCCCAACCTCAGGAGCCTGAGCTTATGAATGCCAACCCTTCTCCTCCACCAAGTCCTTCT
CAGCAAATCAACCTTGGCCCGTCGTCCAATCCTCATGCTAAACCATCTGACTTTCACTTC
TTGAAAGTGATCGGAAAGGGCAGTTTTGGAAAGGTTCTTCTAGCAAGACACAAGGCAGAA
GAAGTGTTCTATGCAGTCAAAGTTTTACAGAAGAAAGCAATCCTGAAAAAGAAAGAGGAG
AAGCATATTATGTCGGAGCGGAATGTTCTGTTGAAGAATGTGAAGCACCCTTTCCTGGTG
GGCCTTCACTTCTCTTTCCAGACTGCTGACAAATTGTACTTTGTCCTAGACTACATTAAT
GGTGGAGAGTTGTTCTACCATCTCCAGAGGGAACGCTGCTTCCTGGAACCACGGGCTCGT
TTCTATGCTGCTGAAATAGCCAGTGCCTTGGGCTACCTGCATTCACTGAACATCGTTTAT
AGAGACTTAAAACCAGAGAATATTTTGCTAGATTCACAGGGACACATTGTCCTTACTGAT
TTCGGACTCTGCAAGGAGAACATTGAACACAACAGCACAACATCCACCTTCTGTGGCACG
CCGGAGTATCTCGCACCTGAGGTGCTTCATAAGCAGCCTTATGACAGGACTGTGGACTGG
TGGTGCCTGGGAGCTGTCTTGTATGAGATGCTGTATGGCCTGCCGCCTTTTTATAGCCGA
AACACAGCTGAAATGTACGACAACATTCTGAACAAGCCTCTCCAGCTGAAACCAAATATT
ACAAATTCCGCAAGACACCTCCTGGAGGGCCTCCTGCAGAAGGACAGGACAAAGCGGCTC
GGGGCCAAGGATGACTTCATGGAGATTAAGAGTCATGTCTTCTTCTCCTTAATTAACTGG
GATGATCTCATTAATAAGAAGATTACTCCCCCTTTTAACCCAAATGTGAGTGGGCCCAAC
GAGCTACGGCACTTTGACCCCGAGTTTACCGAAGAGCCTGTCCCCAACTCCATTGGCAAG
TCCCCTGACAGCGTCCTCGTCACAGCCAGCGTCAAGGAAGCTGCCGAGGCTTTCCTAGGC
TTTTCCTATGCGCCTCCCACGGACTCTTTCCTCTGA
|
| Enzyme 4 GenBank Gene ID |
Y10032  |
| Enzyme 4 GeneCard ID |
SGK  |
| Enzyme 4 GenAtlas ID |
SGK  |
| Enzyme 4 HGNC ID |
HGNC:10810  |
| Enzyme 4 Chromosome Location |
6 |
| Enzyme 4 Locus |
6q23 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Waldegger S, Barth P, Raber G, Lang F: Cloning and characterization of a putative human serine/threonine protein kinase transcriptionally modified during anisotonic and isotonic alterations of cell volume. Proc Natl Acad Sci U S A. 1997 Apr 29;94(9):4440-5. [PubMed
]
- Waldegger S, Erdel M, Nagl UO, Barth P, Raber G, Steuer S, Utermann G, Paulmichl M, Lang F: Genomic organization and chromosomal localization of the human SGK protein kinase gene. Genomics. 1998 Jul 15;51(2):299-302. [PubMed
]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed
]
- Kobayashi T, Deak M, Morrice N, Cohen P: Characterization of the structure and regulation of two novel isoforms of serum- and glucocorticoid-induced protein kinase. Biochem J. 1999 Nov 15;344 Pt 1:189-97. [PubMed
]
- Kobayashi T, Cohen P: Activation of serum- and glucocorticoid-regulated protein kinase by agonists that activate phosphatidylinositide 3-kinase is mediated by 3-phosphoinositide-dependent protein kinase-1 (PDK1) and PDK2. Biochem J. 1999 Apr 15;339 ( Pt 2):319-28. [PubMed
]
- Lang F, Klingel K, Wagner CA, Stegen C, Warntges S, Friedrich B, Lanzendorfer M, Melzig J, Moschen I, Steuer S, Waldegger S, Sauter M, Paulmichl M, Gerke V, Risler T, Gamba G, Capasso G, Kandolf R, Hebert SC, Massry SG, Broer S: Deranged transcriptional regulation of cell-volume-sensitive kinase hSGK in diabetic nephropathy. Proc Natl Acad Sci U S A. 2000 Jul 5;97(14):8157-62. [PubMed
]
- Brunet A, Park J, Tran H, Hu LS, Hemmings BA, Greenberg ME: Protein kinase SGK mediates survival signals by phosphorylating the forkhead transcription factor FKHRL1 (FOXO3a). Mol Cell Biol. 2001 Feb;21(3):952-65. [PubMed
]
- Gamper N, Fillon S, Feng Y, Friedrich B, Lang PA, Henke G, Huber SM, Kobayashi T, Cohen P, Lang F: K+ channel activation by all three isoforms of serum- and glucocorticoid-dependent protein kinase SGK. Pflugers Arch. 2002 Oct;445(1):60-6. Epub 2002 Aug 28. [PubMed
]
- Maiyar AC, Leong ML, Firestone GL: Importin-alpha mediates the regulated nuclear targeting of serum- and glucocorticoid-inducible protein kinase (Sgk) by recognition of a nuclear localization signal in the kinase central domain. Mol Biol Cell. 2003 Mar;14(3):1221-39. [PubMed
]
|
| Enzyme 4 Metabolite References |
- Cordas E, Naray-Fejes-Toth A, Fejes-Toth G: Subcellular location of serum- and glucocorticoid-induced kinase-1 in renal and mammary epithelial cells. Am J Physiol Cell Physiol. 2007 May;292(5):C1971-81. Epub 2007 Jan 3. [PubMed
]
|
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
6752 |
| Enzyme 5 Name |
Epidermal growth factor receptor precursor |
| Enzyme 5 Synonyms |
- Receptor tyrosine-protein kinase ErbB-1
|
| Enzyme 5 Gene Name |
EGFR |
| Enzyme 5 Protein Sequence |
>Epidermal growth factor receptor precursor
MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEV
VLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALA
VLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDF
QNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGC
TGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYV
VTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFK
NCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAF
ENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKL
FGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCN
LLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVM
GENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPSIATGMVGALLLLLVV
ALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGS
GAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGI
CLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAA
RNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSY
GVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPK
FRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQ
QGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTED
SIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPSRDPHYQDPHSTAVGNPEYLN
TVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRV
APQSSEFIGA
|
| Enzyme 5 Number of Residues |
1210 |
| Enzyme 5 Molecular Weight |
134279 |
| Enzyme 5 Theoretical pI |
6.67 |
| Enzyme 5 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- epidermal growth factor receptor activity
- kinase activity
- nucleotide binding
- protein kinase activity
- protein-tyrosine kinase activity
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
- transmembrane receptor protein tyrosine kinase activity
|
| Process |
- biopolymer metabolism
- biopolymer modification
- cell communication
- cell surface receptor linked signal transduction
- cellular process
- enzyme linked receptor protein signaling pathway
- macromolecule metabolism
- metabolism
- physiological process
- protein amino acid phosphorylation
- protein modification
- signal transduction
- transmembrane receptor protein tyrosine kinase signaling pathway
|
| Component |
|
|
| Enzyme 5 General Function |
Not Available |
| Enzyme 5 Specific Function |
Isoform 2/truncated isoform may act as an antagonist |
| Enzyme 5 Pathways |
Not Available |
| Enzyme 5 Reactions |
Not Available |
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
757924  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P00533  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
EGFR_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>3633 bp
ATGCGACCCTCCGGGACGGCCGGGGCAGCGCTCCTGGCGCTGCTGGCTGCGCTCTGCCCG
GCGAGTCGGGCTCTGGAGGAAAAGAAAGTTTGCCAAGGCACGAGTAACAAGCTCACGCAG
TTGGGCACTTTTGAAGATCATTTTCTCAGCCTCCAGAGGATGTTCAATAACTGTGAGGTG
GTCCTTGGGAATTTGGAAATTACCTATGTGCAGAGGAATTATGATCTTTCCTTCTTAAAG
ACCATCCAGGAGGTGGCTGGTTATGTCCTCATTGCCCTCAACACAGTGGAGCGAATTCCT
TTGGAAAACCTGCAGATCATCAGAGGAAATATGTACTACGAAAATTCCTATGCCTTAGCA
GTCTTATCTAACTATGATGCAAATAAAACCGGACTGAAGGAGCTGCCCATGAGAAATTTA
CAGGAAATCCTGCATGGCGCCGTGCGGTTCAGCAACAACCCTGCCCTGTGCAACGTGGAG
AGCATCCAGTGGCGGGACATAGTCAGCAGTGACTTTCTCAGCAACATGTCGATGGACTTC
CAGAACCACCTGGGCAGCTGCCAAAAGTGTGATCCAAGCTGTCCCAATGGGAGCTGCTGG
GGTGCAGGAGAGGAGAACTGCCAGAAACTGACCAAAATCATCTGTGCCCAGCAGTGCTCC
GGGCGCTGCCGTGGCAAGTCCCCCAGTGACTGCTGCCACAACCAGTGTGCTGCAGGCTGC
ACAGGCCCCCGGGAGAGCGACTGCCTGGTCTGCCGCAAATTCCGAGACGAAGCCACGTGC
AAGGACACCTGCCCCCCACTCATGCTCTACAACCCCACCACGTACCAGATGGATGTGAAC
CCCGAGGGCAAATACAGCTTTGGTGCCACCTGCGTGAAGAAGTGTCCCCGTAATTATGTG
GTGACAGATCACGGCTCGTGCGTCCGAGCCTGTGGGGCCGACAGCTATGAGATGGAGGAA
GACGGCGTCCGCAAGTGTAAGAAGTGCGAAGGGCCTTGCCGCAAAGTGTGTAACGGAATA
GGTATTGGTGAATTTAAAGACTCACTCTCCATAAATGCTACGAATATTAAACACTTCAAA
AACTGCACCTCCATCAGTGGCGATCTCCACATCCTGCCGGTGGCATTTAGGGGTGACTCC
TTCACACATACTCCTCCTCTGGATCCACAGGAACTGGATATTCTGAAAACCGTAAAGGAA
ATCACAGGGTTTTTGCTGATTCAGGCTTGGCCTGAAAACAGGACGGACCTCCATGCCTTT
GAGAACCTAGAAATCATACGCGGCAGGACCAAGCAACATGGTCAGTTTTCTCTTGCAGTC
GTCAGCCTGAACATAACATCCTTGGGATTACGCTCCCTCAAGGAGATAAGTGATGGAGAT
GTGATAATTTCAGGAAACAAAAATTTGTGCTATGCAAATACAATAAACTGGAAAAAACTG
TTTGGGACCTCCGGTCAGAAAACCAAAATTATAAGCAACAGAGGTGAAAACAGCTGCAAG
GCCACAGGCCAGGTCTGCCATGCCTTGTGCTCCCCCGAGGGCTGCTGGGGCCCGGAGCCC
AGGGACTGCGTCTCTTGCCGGAATGTCAGCCGAGGCAGGGAATGCGTGGACAAGTGCAAG
CTTCTGGAGGGTGAGCCAAGGGAGTTTGTGGAGAACTCTGAGTGCATACAGTGCCACCCA
GAGTGCCTGCCTCAGGCCATGAACATCACCTGCACAGGACGGGGACCAGACAACTGTATC
CAGTGTGCCCACTACATTGACGGCCCCCACTGCGTCAAGACCTGCCCGGCAGGAGTCATG
GGAGAAAACAACACCCTGGTCTGGAAGTACGCAGACGCCGGCCATGTGTGCCACCTGTGC
CATCCAAACTGCACCTACGGATGCACTGGGCCAGGTCTTGAAGGCTGTCCAACGAATGGG
CCTAAGATCCCGTCCATCGCCACTGGGATGGTGGGGGCCCTCCTCTTGCTGCTGGTGGTG
GCCCTGGGGATCGGCCTCTTCATGCGAAGGCGCCACATCGTTCGGAAGCGCACGCTGCGG
AGGCTGCTGCAGGAGAGGGAGCTTGTGGAGCCTCTTACACCCAGTGGAGAAGCTCCCAAC
CAAGCTCTCTTGAGGATCTTGAAGGAAACTGAATTCAAAAAGATCAAAGTGCTGGGCTCC
GGTGCGTTCGGCACGGTGTATAAGGGACTCTGGATCCCAGAAGGTGAGAAAGTTAAAATT
CCCGTCGCTATCAAGGAATTAAGAGAAGCAACATCTCCGAAAGCCAACAAGGAAATCCTC
GATGAAGCCTACGTGATGGCCAGCGTGGACAACCCCCACGTGTGCCGCCTGCTGGGCATC
TGCCTCACCTCCACCGTGCAACTCATCACGCAGCTCATGCCCTTCGGCTGCCTCCTGGAC
TATGTCCGGGAACACAAAGACAATATTGGCTCCCAGTACCTGCTCAACTGGTGTGTGCAG
ATCGCAAAGGGCATGAACTACTTGGAGGACCGTCGCTTGGTGCACCGCGACCTGGCAGCC
AGGAACGTACTGGTGAAAACACCGCAGCATGTCAAGATCACAGATTTTGGGCTGGCCAAA
CTGCTGGGTGCGGAAGAGAAAGAATACCATGCAGAAGGAGGCAAAGTGCCTATCAAGTGG
ATGGCATTGGAATCAATTTTACACAGAATCTATACCCACCAGAGTGATGTCTGGAGCTAC
GGGGTGACCGTTTGGGAGTTGATGACCTTTGGATCCAAGCCATATGACGGAATCCCTGCC
AGCGAGATCTCCTCCATCCTGGAGAAAGGAGAACGCCTCCCTCAGCCACCCATATGTACC
ATCGATGTCTACATGATCATGGTCAAGTGCTGGATGATAGACGCAGATAGTCGCCCAAAG
TTCCGTGAGTTGATCATCGAATTCTCCAAAATGGCCCGAGACCCCCAGCGCTACCTTGTC
ATTCAGGGGGATGAAAGAATGCATTTGCCAAGTCCTACAGACTCCAACTTCTACCGTGCC
CTGATGGATGAAGAAGACATGGACGACGTGGTGGATGCCGACGAGTACCTCATCCCACAG
CAGGGCTTCTTCAGCAGCCCCTCCACGTCACGGACTCCCCTCCTGAGCTCTCTGAGTGCA
ACCAGCAACAATTCCACCGTGGCTTGCATTGATAGAAATGGGCTGCAAAGCTGTCCCATC
AAGGAAGACAGCTTCTTGCAGCGATACAGCTCAGACCCCACAGGCGCCTTGACTGAGGAC
AGCATAGACGACACCTTCCTCCCAGTGCCTGAATACATAAACCAGTCCGTTCCCAAAAGG
CCCGCTGGCTCTGTGCAGAATCCTGTCTATCACAATCAGCCTCTGAACCCCGCGCCCAGC
AGAGACCCACACTACCAGGACCCCCACAGCACTGCAGTGGGCAACCCCGAGTATCTCAAC
ACTGTCCAGCCCACCTGTGTCAACAGCACATTCGACAGCCCTGCCCACTGGGCCCAGAAA
GGCAGCCACCAAATTAGCCTGGACAACCCTGACTACCAGCAGGACTTCTTTCCCAAGGAA
GCCAAGCCAAATGGCATCTTTAAGGGCTCCACAGCTGAAAATGCAGAATACCTAAGGGTC
GCGCCACAAAGCAGTGAATTTATTGGAGCATGA
|
| Enzyme 5 GenBank Gene ID |
X00588  |
| Enzyme 5 GeneCard ID |
EGFR  |
| Enzyme 5 GenAtlas ID |
EGFR  |
| Enzyme 5 HGNC ID |
HGNC:3236  |
| Enzyme 5 Chromosome Location |
7 |
| Enzyme 5 Locus |
7p12 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Ullrich A, Coussens L, Hayflick JS, Dull TJ, Gray A, Tam AW, Lee J, Yarden Y, Libermann TA, Schlessinger J, et al.: Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells. Nature. 1984 May 31-Jun 6;309(5967):418-25. [PubMed
]
- Ilekis JV, Stark BC, Scoccia B: Possible role of variant RNA transcripts in the regulation of epidermal growth factor receptor expression in human placenta. Mol Reprod Dev. 1995 Jun;41(2):149-56. [PubMed
]
- Reiter JL, Maihle NJ: A 1.8 kb alternative transcript from the human epidermal growth factor receptor gene encodes a truncated form of the receptor. Nucleic Acids Res. 1996 Oct 15;24(20):4050-6. [PubMed
]
- Ilekis JV, Gariti J, Niederberger C, Scoccia B: Expression of a truncated epidermal growth factor receptor-like protein (TEGFR) in ovarian cancer. Gynecol Oncol. 1997 Apr;65(1):36-41. [PubMed
]
- Reiter JL, Threadgill DW, Eley GD, Strunk KE, Danielsen AJ, Sinclair CS, Pearsall RS, Green PJ, Yee D, Lampland AL, Balasubramaniam S, Crossley TD, Magnuson TR, James CD, Maihle NJ: Comparative genomic sequence analysis and isolation of human and mouse alternative EGFR transcripts encoding truncated receptor isoforms. Genomics. 2001 Jan 1;71(1):1-20. [PubMed
]
- Lin CR, Chen WS, Kruiger W, Stolarsky LS, Weber W, Evans RM, Verma IM, Gill GN, Rosenfeld MG: Expression cloning of human EGF receptor complementary DNA: gene amplification and three related messenger RNA products in A431 cells. Science. 1984 May 25;224(4651):843-8. [PubMed
]
- Xu YH, Ishii S, Clark AJ, Sullivan M, Wilson RK, Ma DP, Roe BA, Merlino GT, Pastan I: Human epidermal growth factor receptor cDNA is homologous to a variety of RNAs overproduced in A431 carcinoma cells. Nature. 1984 Jun 28-Jul 4;309(5971):806-10. [PubMed
]
- Simmen FA, Gope ML, Schulz TZ, Wright DA, Carpenter G, O'Malley BW: Isolation of an evolutionarily conserved epidermal growth factor receptor cDNA from human A431 carcinoma cells. Biochem Biophys Res Commun. 1984 Oct 15;124(1):125-32. [PubMed
]
- Haley J, Whittle N, Bennet P, Kinchington D, Ullrich A, Waterfield M: The human EGF receptor gene: structure of the 110 kb locus and identification of sequences regulating its transcription. Oncogene Res. 1987 Sep-Oct;1(4):375-96. [PubMed
]
- Haley JD, Waterfield MD: Contributory effects of de novo transcription and premature transcript termination in the regulation of human epidermal growth factor receptor proto-oncogene RNA synthesis. J Biol Chem. 1991 Jan 25;266(3):1746-53. [PubMed
]
- Ishii S, Xu YH, Stratton RH, Roe BA, Merlino GT, Pastan I: Characterization and sequence of the promoter region of the human epidermal growth factor receptor gene. Proc Natl Acad Sci U S A. 1985 Aug;82(15):4920-4. [PubMed
]
- Weber W, Gill GN, Spiess J: Production of an epidermal growth factor receptor-related protein. Science. 1984 Apr 20;224(4646):294-7. [PubMed
]
- Heisermann GJ, Gill GN: Epidermal growth factor receptor threonine and serine residues phosphorylated in vivo. J Biol Chem. 1988 Sep 15;263(26):13152-8. [PubMed
]
- Russo MW, Lukas TJ, Cohen S, Staros JV: Identification of residues in the nucleotide binding site of the epidermal growth factor receptor/kinase. J Biol Chem. 1985 May 10;260(9):5205-8. [PubMed
]
- Abe Y, Odaka M, Inagaki F, Lax I, Schlessinger J, Kohda D: Disulfide bond structure of human epidermal growth factor receptor. J Biol Chem. 1998 May 1;273(18):11150-7. [PubMed
]
- Mroczkowski B, Mosig G, Cohen S: ATP-stimulated interaction between epidermal growth factor receptor and supercoiled DNA. Nature. 1984 May 17-23;309(5965):270-3. [PubMed
]
- Carpenter G: Receptors for epidermal growth factor and other polypeptide mitogens. Annu Rev Biochem. 1987;56:881-914. [PubMed
]
- Chen WS, Lazar CS, Lund KA, Welsh JB, Chang CP, Walton GM, Der CJ, Wiley HS, Gill GN, Rosenfeld MG: Functional independence of the epidermal growth factor receptor from a domain required for ligand-induced internalization and calcium regulation. Cell. 1989 Oct 6;59(1):33-43. [PubMed
]
- Margolis BL, Lax I, Kris R, Dombalagian M, Honegger AM, Howk R, Givol D, Ullrich A, Schlessinger J: All autophosphorylation sites of epidermal growth factor (EGF) receptor and HER2/neu are located in their carboxyl-terminal tails. Identification of a novel site in EGF receptor. J Biol Chem. 1989 Jun 25;264(18):10667-71. [PubMed
]
- Smith KD, Davies MJ, Bailey D, Renouf DV, Hounsell EF: Analysis of the glycosylation patterns of the extracellular domain of the epidermal growth factor receptor expressed in Chinese hamster ovary fibroblasts. Growth Factors. 1996;13(1-2):121-32. [PubMed
]
- Sato C, Kim JH, Abe Y, Saito K, Yokoyama S, Kohda D: Characterization of the N-oligosaccharides attached to the atypical Asn-X-Cys sequence of recombinant human epidermal growth factor receptor. J Biochem (Tokyo). 2000 Jan;127(1):65-72. [PubMed
]
- Habib AA, Chatterjee S, Park SK, Ratan RR, Lefebvre S, Vartanian T: The epidermal growth factor receptor engages receptor interacting protein and nuclear factor-kappa B (NF-kappa B)-inducing kinase to activate NF-kappa B. Identification of a novel receptor-tyrosine kinase signalosome. J Biol Chem. 2001 Mar 23;276(12):8865-74. Epub 2000 Dec 14. [PubMed
]
|
| Enzyme 5 Metabolite References |
- McEneaney V, Harvey BJ, Thomas W: Aldosterone rapidly activates protein kinase D via a mineralocorticoid receptor/EGFR trans-activation pathway in the M1 kidney CCD cell line. J Steroid Biochem Mol Biol. 2007 Nov-Dec;107(3-5):180-90. Epub 2007 Jun 22. [PubMed
]
|
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
6767 |
| Enzyme 6 Name |
Serine/threonine-protein kinase D1 |
| Enzyme 6 Synonyms |
- nPKC-D1
- Protein kinase D
- Protein kinase C mu type
- nPKC-mu
|
| Enzyme 6 Gene Name |
PRKD1 |
| Enzyme 6 Protein Sequence |
>Serine/threonine-protein kinase D1
MSAPPVLRPPSPLLPVAAAAAAAAAALVPGSGPGPAPFLAPVAAPVGGISFHLQIGLSRE
PVLLLQDSSGDYSLAHVREMACSIVDQKFPECGFYGMYDKILLFRHDPTSENILQLVKAA
SDIQEGDLIEVVLSRSATFEDFQIRPHALFVHSYRAPAFCDHCGEMLWGLVRQGLKCEGC
GLNYHKRCAFKIPNNCSGVRRRRLSNVSLTGVSTIRTSSAELSTSAPDEPLLQKSPSESF
IGREKRSNSQSYIGRPIHLDKILMSKVKVPHTFVIHSYTRPTVCQYCKKLLKGLFRQGLQ
CKDCRFNCHKRCAPKVPNNCLGEVTINGDLLSPGAESDVVMEEGSDDNDSERNSGLMDDM
EEAMVQDAEMAMAECQNDSGEMQDPDPDHEDANRTISPSTSNNIPLMRVVQSVKHTKRKS
STVMKEGWMVHYTSKDTLRKRHYWRLDSKCITLFQNDTGSRYYKEIPLSEILSLEPVKTS
ALIPNGANPHCFEITTANVVYYVGENVVNPSSPSPNNSVLTSGVGADVARMWEIAIQHAL
MPVIPKGSSVGTGTNLHRDISVSISVSNCQIQENVDISTVYQIFPDEVLGSGQFGIVYGG
KHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVME
KLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPF
PQVKLCDFGFARIIGEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGT
FPFNEDEDIHDQIQNAAFMYPPNPWKEISHEAIDLINNLLQVKMRKRYSVDKTLSHPWLQ
DYQTWLDLRELECKIGERYITHESDDLRWEKYAGEQRLQYPTHLINPSASHSDTPETEET
EMKALGERVSIL
|
| Enzyme 6 Number of Residues |
912 |
| Enzyme 6 Molecular Weight |
101890 |
| Enzyme 6 Theoretical pI |
6.71 |
| Enzyme 6 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleotide binding
- protein kinase activity
- protein serine/threonine kinase activity
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biopolymer metabolism
- biopolymer modification
- cell communication
- cellular process
- intracellular signaling cascade
- macromolecule metabolism
- metabolism
- physiological process
- protein amino acid phosphorylation
- protein modification
- signal transduction
|
| Component |
| — |
|
| Enzyme 6 General Function |
Not Available |
| Enzyme 6 Specific Function |
This is calcium-independent, phospholipid-dependent, serine- and threonine-specific enzyme |
| Enzyme 6 Pathways |
Not Available |
| Enzyme 6 Reactions |
Not Available |
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
Not Available |
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
438373  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
Q15139  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
KPCD1_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>2739 bp
ATGAGCGCCCCTCCGGTCCTGCGGCCGCCCAGTCCGCTGCTGCCCGTGGCGGCGGCAGCT
GCCGCAGCGGCCGCCGCACTGGTCCCAGGGTCCGGGCCCGGGCCCGCGCCGTTCTTGGCT
CCTGTCGCGGCCCCGGTCGGGGGCATCTCGTTCCATCTGCAGATCGGCCTGAGCCGTGAG
CCGGTGCTGCTGCTGCAGGACTCGTCCGGGGACTACAGCCTGGCGCACGTCCGCGAGATG
GCTTGCTCCATTGTCGACCAGAAGTTCCCTGAATGTGGTTTCTACGGAATGTATGATAAG
ATCCTGCTTTTTCGCCATGACCCTACCTCTGAAAACATCCTTCAGCTGGTGAAAGCGGCC
AGTGATATCCAGGAAGGCGATCTTATTGAAGTGGTCTTGTCACGTTCCGCCACCTTTGAA
GACTTTCAGATTCGTCCCCACGCTCTCTTTGTTCATTCATACAGAGCTCCAGCTTTCTGT
GATCACTGTGGAGAAATGCTGTGGGGGCTGGTACGTCAAGGTCTTAAATGTGAAGGGTGT
GGTCTGAATTACCATAAGAGATGTGCATTTAAAATACCCAACAATTGCAGCGGTGTGAGG
CGGAGAAGGCTCTCAAACGTTTCCCTCACTGGGGTCAGCACCATCCGCACATCATCTGCT
GAACTCTCTACAAGTGCCCCTGATGAGCCCCTTCTGCAAAAATCACCATCAGAGTCGTTT
ATTGGTCGAGAGAAGAGGTCAAATTCTCAATCATACATTGGACGACCAATTCACCTTGAC
AAGATTTTGATGTCTAAAGTTAAAGTGCCGCACACATTTGTCATCCACTCCTACACCCGG
CCCACAGTGTGCCAGTACTGCAAGAAGCTTCTGAAGGGGCTTTTCAGGCAGGGCTTGCAG
TGCAAAGATTGCAGATTCAACTGCCATAAACGTTGTGCACCGAAAGTACCAAACAACTGC
CTTGGCGAAGTGACCATTAATGGAGATTTGCTTAGCCCTGGGGCAGAGTCTGATGTGGTC
ATGGAAGAAGGGAGTGATGACAATGATAGTGAAAGGAACAGTGGGCTCATGGATGATATG
GAAGAAGCAATGGTCCAAGATGCAGAGATGGCAATGGCAGAGTGCCAGAACGACAGTGGC
GAGATGCAAGATCCAGACCCAGACCACGAGGACGCCAACAGAACCATCAGTCCATCAACA
AGCAACAATATCCCACTCATGAGGGTAGTGCAGTCTGTCAAACACACGAAGAGGAAAAGC
AGCACAGTCATGAAAGAAGGATGGATGGTCCACTACACCAGCAAGGACACGCTGCGGAAA
CGGCACTATTGGAGATTGGATAGCAAATGTATTACCCTCTTTCAGAATGACACAGGAAGC
AGGTACTACAAGGAAATTCCTTTATCTGAAATTTTGTCTCTGGAACCAGTAAAAACTTCA
GCTTTAATTCCTAATGGGGCCAATCCTCATTGTTTCGAAATCACTACGGCAAATGTAGTG
TATTATGTGGGAGAAAATGTGGTCAATCCTTCCAGCCCATCACCAAATAACAGTGTTCTC
ACCAGTGGCGTTGGTGCAGATGTGGCCAGGATGTGGGAGATAGCCATCCAGCATGCCCTT
ATGCCCGTCATTCCCAAGGGCTCCTCCGTGGGTACAGGAACCAACTTGCACAGAGATATC
TCTGTGAGTATTTCAGTATCAAATTGCCAGATTCAAGAAAATGTGGACATCAGCACAGTA
TATCAGATTTTTCCTGATGAAGTACTGGGTTCTGGACAGTTTGGAATTGTTTATGGAGGA
AAACATCGTAAAACAGGAAGAGATGTAGCTATTAAAATCATTGACAAATTACGATTTCCA
ACAAAACAAGAAAGCCAGCTTCGTAATGAGGTTGCAATTCTACAGAACCTTCATCACCCT
GGTGTTGTAAATTTGGAGTGTATGTTTGAGACGCCTGAAAGAGTGTTTGTTGTTATGGAA
AAACTCCATGGAGACATGCTGGAAATGATCTTGTCAAGTGAAAAGGGCAGGTTGCCAGAG
CACATAACGAAGTTTTTAATTACTCAGATACTCGTGGCTTTGCGGCACCTTCATTTTAAA
AATATCGTTCACTGTGACCTCAAACCAGAAAATGTGTTGCTAGCCTCAGCTGATCCTTTT
CCTCAGGTGAAACTTTGTGATTTTGGTTTTGCCCGGATCATTGGAGAGAAGTCTTTCCGG
AGGTCAGTGGTGGGTACCCCCGCTTACCTGGCTCCTGAGGTCCTAAGGAACAAGGGCTAC
AATCGCTCTCTAGACATGTGGTCTGTTGGGGTCATCATCTATGTAAGCCTAAGCGGCACA
TTCCCATTTAATGAAGATGAAGACATACACGACCAAATTCAGAATGCAGCTTTCATGTAT
CCACCAAATCCCTGGAAGGAAATATCTCATGAAGCCATTGATCTTATCAACAATTTGCTG
CAAGTAAAAATGAGAAAGCGCTACAGTGTGGATAAGACCTTGAGCCACCCTTGGCTACAG
GACTATCAGACCTGGTTAGATTTGCGAGAGCTGGAATGCAAAATCGGGGAGCGCTACATC
ACCCATGAAAGTGATGACCTGAGGTGGGAGAAGTATGCAGGCGAGCAGCGGCTGCAGTAC
CCCACACACCTGATCAATCCAAGTGCTAGCCACAGTGACACTCCTGAGACTGAAGAAACA
GAAATGAAAGCCCTCGGTGAGCGTGTCAGCATCCTCTGA
|
| Enzyme 6 GenBank Gene ID |
X75756  |
| Enzyme 6 GeneCard ID |
PRKD1  |
| Enzyme 6 GenAtlas ID |
PRKD1  |
| Enzyme 6 HGNC ID |
HGNC:9407  |
| Enzyme 6 Chromosome Location |
14 |
| Enzyme 6 Locus |
14q11 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Johannes FJ, Prestle J, Eis S, Oberhagemann P, Pfizenmaier K: PKCu is a novel, atypical member of the protein kinase C family. J Biol Chem. 1994 Feb 25;269(8):6140-8. [PubMed
]
- Zemlickova E, Dubois T, Kerai P, Clokie S, Cronshaw AD, Wakefield RI, Johannes FJ, Aitken A: Centaurin-alpha(1) associates with and is phosphorylated by isoforms of protein kinase C. Biochem Biophys Res Commun. 2003 Aug 1;307(3):459-65. [PubMed
]
|
| Enzyme 6 Metabolite References |
- McEneaney V, Harvey BJ, Thomas W: Aldosterone regulates rapid trafficking of epithelial sodium channel subunits in renal cortical collecting duct cells via protein kinase D activation. Mol Endocrinol. 2008 Apr;22(4):881-92. Epub 2008 Jan 17. [PubMed
]
|
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
7297 |
| Enzyme 7 Name |
Glucocorticoid receptor |
| Enzyme 7 Synonyms |
- GR
|
| Enzyme 7 Gene Name |
NR3C1 |
| Enzyme 7 Protein Sequence |
>Glucocorticoid receptor
MDSKESLTPGREENPSSVLAQERGDVMDFYKTLRGGATVKVSASSPSLAVASQSDSKQRR
LLVDFPKGSVSNAQQPDLSKAVSLSMGLYMGETETKVMGNDLGFPQQGQISLSSGETDLK
LLEESIANLNRSTSVPENPKSSASTAVSAAPTEKEFPKTHSDVSSEQQHLKGQTGTNGGN
VKLYTTDQSTFDILQDLEFSSGSPGKETNESPWRSDLLIDENCLLSPLAGEDDSFLLEGN
SNEDCKPLILPDTKPKIKDNGDLVLSSPSNVTLPQVKTEKEDFIELCTPGVIKQEKLGTV
YCQASFPGANIIGNKMSAISVHGVSTSGGQMYHYDMNTASLSQQQDQKPIFNVIPPIPVG
SENWNRCQGSGDDNLTSLGTLNFPGRTVFSNGYSSPSMRPDVSSPPSSSSTATTGPPPKL
CLVCSDEASGCHYGVLTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRYRK
CLQAGMNLEARKTKKKIKGIQQATTGVSQETSENPGNKTIVPATLPQLTPTLVSLLEVIE
PEVLYAGYDSSVPDSTWRIMTTLNMLGGRQVIAAVKWAKAIPGFRNLHLDDQMTLLQYSW
MFLMAFALGWRSYRQSSANLLCFAPDLIINEQRMTLPCMYDQCKHMLYVSSELHRLQVSY
EEYLCMKTLLLLSSVPKDGLKSQELFDEIRMTYIKELGKAIVKREGNSSQNWQRFYQLTK
LLDSMHEVVENLLNYCFQTFLDKTMSIEFPEMLAEIITNQIPKYSNGNIKKLLFHQK
|
| Enzyme 7 Number of Residues |
777 |
| Enzyme 7 Molecular Weight |
85660 |
| Enzyme 7 Theoretical pI |
6.31 |
| Enzyme 7 GO Classification |
| Function |
- DNA binding
- binding
- glucocorticoid receptor activity
- ligand-dependent nuclear receptor activity
- nucleic acid binding
- receptor activity
- signal transducer activity
- steroid binding
- steroid hormone receptor activity
- transcription factor 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
- regulation of transcription, DNA-dependent
|
| Component |
- intracellular membrane-bound organelle
- membrane-bound organelle
- nucleus
- organelle
|
|
| Enzyme 7 General Function |
Not Available |
| Enzyme 7 Specific Function |
Receptor for glucocorticoids (GC). Has a dual mode of action:as a transcription factor that binds to glucocorticoid response elements (GRE) and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth |
| Enzyme 7 Pathways |
Not Available |
| Enzyme 7 Reactions |
Not Available |
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
31680  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
P04150  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
GCR_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>2334 bp
ATGGACTCCAAAGAATCATTAACTCCTGGTAGAGAAGAAAACCCCAGCAGTGTGCTTGCT
CAGGAGAGGGGAGATGTGATGGACTTCTATAAAACCCTAAGAGGAGGAGCTACTGTGAAG
GTTTCTGCGTCTTCACCCTCACTGGCTGTCGCTTCTCAATCAGACTCCAAGCAGCGAAGA
CTTTTGGTTGATTTTCCAAAAGGCTCAGTAAGCAATGCGCAGCAGCCAGATCTGTCCAAA
GCAGTTTCACTCTCAATGGGACTGTATATGGGAGAGACAGAAACAAAAGTGATGGGAAAT
GACCTGGGATTCCCACAGCAGGGCCAAATCAGCCTTTCCTCGGGGGAAACAGACTTAAAG
CTTTTGGAAGAAAGCATTGCAAACCTCAATAGGTCGACCAGTGTTCCAGAGAACCCCAAG
AGTTCAGCATCCACTGCTGTGTCTGCTGCCCCCACAGAGAAGGAGTTTCCAAAAACTCAC
TCTGATGTATCTTCAGAACAGCAACATTTGAAGGGCCAGACTGGCACCAACGGTGGCAAT
GTGAAATTGTATACCACAGACCAAAGCACCTTTGACATTTTGCAGGATTTGGAGTTTTCT
TCTGGGTCCCCAGGTAAAGAGACGAATGAGAGTCCTTGGAGATCAGACCTGTTGATAGAT
GAAAACTGTTTGCTTTCTCCTCTGGCGGGAGAAGACGATTCATTCCTTTTGGAAGGAAAC
TCGAATGAGGACTGCAAGCCTCTCATTTTACCGGACACTAAACCCAAAATTAAGGATAAT
GGAGATCTGGTTTTGTCAAGCCCCAGTAATGTAACACTGCCCCAAGTGAAAACAGAAAAA
GAAGATTTCATCGAACTCTGCACCCCTGGGGTAATTAAGCAAGAGAAACTGGGCACAGTT
TACTGTCAGGCAAGCTTTCCTGGAGCAAATATAATTGGTAATAAAATGTCTGCCATTTCT
GTTCATGGTGTGAGTACCTCTGGAGGACAGATGTACCACTATGACATGAATACAGCATCC
CTTTCTCAACAGCAGGATCAGAAGCCTATTTTTAATGTCATTCCACCAATTCCCGTTGGT
TCCGAAAATTGGAATAGGTGCCAAGGATCTGGAGATGACAACTTGACTTCTCTGGGGACT
CTGAACTTCCCTGGTCGAACAGTTTTTTCTAATGGCTATTCAAGCCCCAGCATGAGACCA
GATGTAAGCTCTCCTCCATCCAGCTCCTCAACAGCAACAACAGGACCACCTCCCAAACTC
TGCCTGGTGTGCTCTGATGAAGCTTCAGGATGTCATTATGGAGTCTTAACTTGTGGAAGC
TGTAAAGTTTTCTTCAAAAGAGCAGTGGAAGGACAGCACAATTACCTATGTGCTGGAAGG
AATGATTGCATCATCGATAAAATTCGAAGAAAAAACTGCCCAGCATGCCGCTATCGAAAA
TGTCTTCAGGCTGGAATGAACCTGGAAGCTCGAAAAACAAAGAAAAAAATAAAAGGAATT
CAGCAGGCCACTACAGGAGTCTCACAAGAAACCTCTGAAAATCCTGGTAACAAAACAATA
GTTCCTGCAACGTTACCACAACTCACCCCTACCCTGGTGTCACTGTTGGAGGTTATTGAA
CCTGAAGTGTTATATGCAGGATATGATAGCTCTGTTCCAGACTCAACTTGGAGGATCATG
ACTACGCTCAACATGTTAGGAGGGCGGCAAGTGATTGCAGCAGTGAAATGGGCAAAGGCA
ATACCAGGTTTCAGGAACTTACACCTGGATGACCAAATGACCCTACTGCAGTACTCCTGG
ATGTTTCTTATGGCATTTGCTCTGGGGTGGAGATCATATAGACAATCAAGTGCAAACCTG
CTGTGTTTTGCTCCTGATCTGATTATTAATGAGCAGAGAATGACTCTACCCTGCATGTAC
GACCAATGTAAACACATGCTGTATGTTTCCTCTGAGTTACACAGGCTTCAGGTATCTTAT
GAAGAGTATCTCTGTATGAAAACCTTACTGCTTCTCTCTTCAGTTCCTAAGGACGGTCTG
AAGAGCCAAGAGCTATTTGATGAAATTAGAATGACCTACATCAAAGAGCTAGGAAAAGCC
ATTGTCAAGAGGGAAGGAAACTCCAGCCAGAACTGGCAGCGGTTTTATCAACTGACAAAA
CTCTTGGATTCTATGCATGAAGTGGTTGAAAATCTCCTTAACTATTGCTTCCAAACATTT
TTGGATAAGACCATGAGTATTGAATTCCCCGAGATGTTAGCTGAAATCATCACCAATCAG
ATACCAAAATATTCAAATGGAAATATCAAAAAACTTCTGTTTCATCAAAAGTGA
|
| Enzyme 7 GenBank Gene ID |
X03225  |
| Enzyme 7 GeneCard ID |
NR3C1  |
| Enzyme 7 GenAtlas ID |
NR3C1  |
| Enzyme 7 HGNC ID |
HGNC:7978  |
| Enzyme 7 Chromosome Location |
5 |
| Enzyme 7 Locus |
5q31.3 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Hollenberg SM, Weinberger C, Ong ES, Cerelli G, Oro A, Lebo R, Thompson EB, Rosenfeld MG, Evans RM: Primary structure and expression of a functional human glucocorticoid receptor cDNA. Nature. 1985 Dec 19-1986 Jan 1;318(6047):635-41. [PubMed
]
- Encio IJ, Detera-Wadleigh SD: The genomic structure of the human glucocorticoid receptor. J Biol Chem. 1991 Apr 15;266(11):7182-8. [PubMed
]
- Leclerc S, Xie BX, Roy R, Govindan MV: Purification of a human glucocorticoid receptor gene promoter-binding protein. Production of polyclonal antibodies against the purified factor. J Biol Chem. 1991 May 15;266(14):8711-9. [PubMed
]
- Govindan MV, Pothier F, Leclerc S, Palaniswami R, Xie B: Human glucocorticoid receptor gene promotor-homologous down regulation. J Steroid Biochem Mol Biol. 1991;40(1-3):317-23. [PubMed
]
- Yudt MR, Cidlowski JA: Molecular identification and characterization of a and b forms of the glucocorticoid receptor. Mol Endocrinol. 2001 Jul;15(7):1093-103. [PubMed
]
- Weinberger C, Hollenberg SM, Rosenfeld MG, Evans RM: Domain structure of human glucocorticoid receptor and its relationship to the v-erb-A oncogene product. Nature. 1985 Dec 19-1986 Jan 1;318(6047):670-2. [PubMed
]
- Henriksson A, Almlof T, Ford J, McEwan IJ, Gustafsson JA, Wright AP: Role of the Ada adaptor complex in gene activation by the glucocorticoid receptor. Mol Cell Biol. 1997 Jun;17(6):3065-73. [PubMed
]
- Fryer CJ, Archer TK: Chromatin remodelling by the glucocorticoid receptor requires the BRG1 complex. Nature. 1998 May 7;393(6680):88-91. [PubMed
]
- Schneikert J, Hubner S, Martin E, Cato AC: A nuclear action of the eukaryotic cochaperone RAP46 in downregulation of glucocorticoid receptor activity. J Cell Biol. 1999 Sep 6;146(5):929-40. [PubMed
]
- Rivers C, Levy A, Hancock J, Lightman S, Norman M: Insertion of an amino acid in the DNA-binding domain of the glucocorticoid receptor as a result of alternative splicing. J Clin Endocrinol Metab. 1999 Nov;84(11):4283-6. [PubMed
]
- Moalli PA, Pillay S, Krett NL, Rosen ST: Alternatively spliced glucocorticoid receptor messenger RNAs in glucocorticoid-resistant human multiple myeloma cells. Cancer Res. 1993 Sep 1;53(17):3877-9. [PubMed
]
- Kayes-Wandover KM, White PC: Steroidogenic enzyme gene expression in the human heart. J Clin Endocrinol Metab. 2000 Jul;85(7):2519-25. [PubMed
]
- Mahajan MA, Samuels HH: A new family of nuclear receptor coregulators that integrate nuclear receptor signaling through CREB-binding protein. Mol Cell Biol. 2000 Jul;20(14):5048-63. [PubMed
]
- Diamond MI, Robinson MR, Yamamoto KR: Regulation of expanded polyglutamine protein aggregation and nuclear localization by the glucocorticoid receptor. Proc Natl Acad Sci U S A. 2000 Jan 18;97(2):657-61. [PubMed
]
- Wallace AD, Cidlowski JA: Proteasome-mediated glucocorticoid receptor degradation restricts transcriptional signaling by glucocorticoids. J Biol Chem. 2001 Nov 16;276(46):42714-21. Epub 2001 Sep 12. [PubMed
]
- Strickland I, Kisich K, Hauk PJ, Vottero A, Chrousos GP, Klemm DJ, Leung DY: High constitutive glucocorticoid receptor beta in human neutrophils enables them to reduce their spontaneous rate of cell death in response to corticosteroids. J Exp Med. 2001 Mar 5;193(5):585-93. [PubMed
]
- Tian S, Poukka H, Palvimo JJ, Janne OA: Small ubiquitin-related modifier-1 (SUMO-1) modification of the glucocorticoid receptor. Biochem J. 2002 Nov 1;367(Pt 3):907-11. [PubMed
]
- Wang Z, Frederick J, Garabedian MJ: Deciphering the phosphorylation "code" of the glucocorticoid receptor in vivo. J Biol Chem. 2002 Jul 19;277(29):26573-80. Epub 2002 May 8. [PubMed
]
- Wong CW, McNally C, Nickbarg E, Komm BS, Cheskis BJ: Estrogen receptor-interacting protein that modulates its nongenomic activity-crosstalk with Src/Erk phosphorylation cascade. Proc Natl Acad Sci U S A. 2002 Nov 12;99(23):14783-8. Epub 2002 Nov 1. [PubMed
]
- Bledsoe RK, Montana VG, Stanley TB, Delves CJ, Apolito CJ, McKee DD, Consler TG, Parks DJ, Stewart EL, Willson TM, Lambert MH, Moore JT, Pearce KH, Xu HE: Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition. Cell. 2002 Jul 12;110(1):93-105. [PubMed
]
- Kauppi B, Jakob C, Farnegardh M, Yang J, Ahola H, Alarcon M, Calles K, Engstrom O, Harlan J, Muchmore S, Ramqvist AK, Thorell S, Ohman L, Greer J, Gustafsson JA, Carlstedt-Duke J, Carlquist M: The three-dimensional structures of antagonistic and agonistic forms of the glucocorticoid receptor ligand-binding domain: RU-486 induces a transconformation that leads to active antagonism. J Biol Chem. 2003 Jun 20;278(25):22748-54. Epub 2003 Apr 9. [PubMed
]
- Hurley DM, Accili D, Stratakis CA, Karl M, Vamvakopoulos N, Rorer E, Constantine K, Taylor SI, Chrousos GP: Point mutation causing a single amino acid substitution in the hormone binding domain of the glucocorticoid receptor in familial glucocorticoid resistance. J Clin Invest. 1991 Feb;87(2):680-6. [PubMed
]
- Powers JH, Hillmann AG, Tang DC, Harmon JM: Cloning and expression of mutant glucocorticoid receptors from glucocorticoid-sensitive and -resistant human leukemic cells. Cancer Res. 1993 Sep 1;53(17):4059-65. [PubMed
]
- Karl M, Lamberts SW, Detera-Wadleigh SD, Encio IJ, Stratakis CA, Hurley DM, Accili D, Chrousos GP: Familial glucocorticoid resistance caused by a splice site deletion in the human glucocorticoid receptor gene. J Clin Endocrinol Metab. 1993 Mar;76(3):683-9. [PubMed
]
- Malchoff DM, Brufsky A, Reardon G, McDermott P, Javier EC, Bergh CH, Rowe D, Malchoff CD: A mutation of the glucocorticoid receptor in primary cortisol resistance. J Clin Invest. 1993 May;91(5):1918-25. [PubMed
]
- Ashraf J, Thompson EB: Identification of the activation-labile gene: a single point mutation in the human glucocorticoid receptor presents as two distinct receptor phenotypes. Mol Endocrinol. 1993 May;7(5):631-42. [PubMed
]
- Koper JW, Stolk RP, de Lange P, Huizenga NA, Molijn GJ, Pols HA, Grobbee DE, Karl M, de Jong FH, Brinkmann AO, Lamberts SW: Lack of association between five polymorphisms in the human glucocorticoid receptor gene and glucocorticoid resistance. Hum Genet. 1997 May;99(5):663-8. [PubMed
]
- Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed
]
- Feng J, Zheng J, Bennett WP, Heston LL, Jones IR, Craddock N, Sommer SS: Five missense variants in the amino-terminal domain of the glucocorticoid receptor: no association with puerperal psychosis or schizophrenia. Am J Med Genet. 2000 Jun 12;96(3):412-7. [PubMed
]
- Ruiz M, Lind U, Gafvels M, Eggertsen G, Carlstedt-Duke J, Nilsson L, Holtmann M, Stierna P, Wikstrom AC, Werner S: Characterization of two novel mutations in the glucocorticoid receptor gene in patients with primary cortisol resistance. Clin Endocrinol (Oxf). 2001 Sep;55(3):363-71. [PubMed
]
- Dobson MG, Redfern CP, Unwin N, Weaver JU: The N363S polymorphism of the glucocorticoid receptor: potential contribution to central obesity in men and lack of association with other risk factors for coronary heart disease and diabetes mellitus. J Clin Endocrinol Metab. 2001 May;86(5):2270-4. [PubMed
]
- Kino T, Stauber RH, Resau JH, Pavlakis GN, Chrousos GP: Pathologic human GR mutant has a transdominant negative effect on the wild-type GR by inhibiting its translocation into the nucleus: importance of the ligand-binding domain for intracellular GR trafficking. J Clin Endocrinol Metab. 2001 Nov;86(11):5600-8. [PubMed
]
- Mendonca BB, Leite MV, de Castro M, Kino T, Elias LL, Bachega TA, Arnhold IJ, Chrousos GP, Latronico AC: Female pseudohermaphroditism caused by a novel homozygous missense mutation of the GR gene. J Clin Endocrinol Metab. 2002 Apr;87(4):1805-9. [PubMed
]
- Vottero A, Kino T, Combe H, Lecomte P, Chrousos GP: A novel, C-terminal dominant negative mutation of the GR causes familial glucocorticoid resistance through abnormal interactions with p160 steroid receptor coactivators. J Clin Endocrinol Metab. 2002 Jun;87(6):2658-67. [PubMed
]
|
| Enzyme 7 Metabolite References |
- Gauer S, Segitz V, Goppelt-Struebe M: Aldosterone induces CTGF in mesangial cells by activation of the glucocorticoid receptor. Nephrol Dial Transplant. 2007 Nov;22(11):3154-9. Epub 2007 Jun 30. [PubMed
]
|
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
7555 |
| Enzyme 8 Name |
Fibronectin precursor |
| Enzyme 8 Synonyms |
- FN
- Cold-insoluble globulin
- CIG
|
| Enzyme 8 Gene Name |
FN1 |
| Enzyme 8 Protein Sequence |
>Fibronectin precursor
MLRGPGPGLLLLAVQCLGTAVPSTGASKSKRQAQQMVQPQSPVAVSQSKPGCYDNGKHYQ
INQQWERTYLGNALVCTCYGGSRGFNCESKPEAEETCFDKYTGNTYRVGDTYERPKDSMI
WDCTCIGAGRGRISCTIANRCHEGGQSYKIGDTWRRPHETGGYMLECVCLGNGKGEWTCK
PIAEKCFDHAAGTSYVVGETWEKPYQGWMMVDCTCLGEGSGRITCTSRNRCNDQDTRTSY
RIGDTWSKKDNRGNLLQCICTGNGRGEWKCERHTSVQTTSSGSGPFTDVRAAVYQPQPHP
QPPPYGHCVTDSGVVYSVGMQWLKTQGNKQMLCTCLGNGVSCQETAVTQTYGGNSNGEPC
VLPFTYNGRTFYSCTTEGRQDGHLWCSTTSNYEQDQKYSFCTDHTVLVQTQGGNSNGALC
HFPFLYNNHNYTDCTSEGRRDNMKWCGTTQNYDADQKFGFCPMAAHEEICTTNEGVMYRI
GDQWDKQHDMGHMMRCTCVGNGRGEWTCIAYSQLRDQCIVDDITYNVNDTFHKRHEEGHM
LNCTCFGQGRGRWKCDPVDQCQDSETGTFYQIGDSWEKYVHGVRYQCYCYGRGIGEWHCQ
PLQTYPSSSGPVEVFITETPSQPNSHPIQWNAPQPSHISKYILRWRPKNSVGRWKEATIP
GHLNSYTIKGLKPGVVYEGQLISIQQYGHQEVTRFDFTTTSTSTPVTSNTVTGETTPFSP
LVATSESVTEITASSFVVSWVSASDTVSGFRVEYELSEEGDEPQYLDLPSTATSVNIPDL
LPGRKYIVNVYQISEDGEQSLILSTSQTTAPDAPPDPTVDQVDDTSIVVRWSRPQAPITG
YRIVYSPSVEGSSTELNLPETANSVTLSDLQPGVQYNITIYAVEENQESTPVVIQQETTG
TPRSDTVPSPRDLQFVEVTDVKVTIMWTPPESAVTGYRVDVIPVNLPGEHGQRLPISRNT
FAEVTGLSPGVTYYFKVFAVSHGRESKPLTAQQTTKLDAPTNLQFVNETDSTVLVRWTPP
RAQITGYRLTVGLTRRGQPRQYNVGPSVSKYPLRNLQPASEYTVSLVAIKGNQESPKATG
VFTTLQPGSSIPPYNTEVTETTIVITWTPAPRIGFKLGVRPSQGGEAPREVTSDSGSIVV
SGLTPGVEYVYTIQVLRDGQERDAPIVNKVVTPLSPPTNLHLEANPDTGVLTVSWERSTT
PDITGYRITTTPTNGQQGNSLEEVVHADQSSCTFDNLSPGLEYNVSVYTVKDDKESVPIS
DTIIPAVPPPTDLRFTNIGPDTMRVTWAPPPSIDLTNFLVRYSPVKNEEDVAELSISPSD
NAVVLTNLLPGTEYVVSVSSVYEQHESTPLRGRQKTGLDSPTGIDFSDITANSFTVHWIA
PRATITGYRIRHHPEHFSGRPREDRVPHSRNSITLTNLTPGTEYVVSIVALNGREESPLL
IGQQSTVSDVPRDLEVVAATPTSLLISWDAPAVTVRYYRITYGETGGNSPVQEFTVPGSK
STATISGLKPGVDYTITVYAVTGRGDSPASSKPISINYRTEIDKPSQMQVTDVQDNSISV
KWLPSSSPVTGYRVTTTPKNGPGPTKTKTAGPDQTEMTIEGLQPTVEYVVSVYAQNPSGE
SQPLVQTAVTNIDRPKGLAFTDVDVDSIKIAWESPQGQVSRYRVTYSSPEDGIHELFPAP
DGEEDTAELQGLRPGSEYTVSVVALHDDMESQPLIGTQSTAIPAPTDLKFTQVTPTSLSA
QWTPPNVQLTGYRVRVTPKEKTGPMKEINLAPDSSSVVVSGLMVATKYEVSVYALKDTLT
SRPAQGVVTTLENVSPPRRARVTDATETTITISWRTKTETITGFQVDAVPANGQTPIQRT
IKPDVRSYTITGLQPGTDYKIYLYTLNDNARSSPVVIDASTAIDAPSNLRFLATTPNSLL
VSWQPPRARITGYIIKYEKPGSPPREVVPRPRPGVTEATITGLEPGTEYTIYVIALKNNQ
KSEPLIGRKKTDELPQLVTLPHPNLHGPEILDVPSTVQKTPFVTHPGYDTGNGIQLPGTS
GQQPSVGQQMIFEEHGFRRTTPPTTATPIRHRPRPYPPNVGEEIQIGHIPREDVDYHLYP
HGPGLNPNASTGQEALSQTTISWAPFQDTSEYIISCHPVGTDEEPLQFRVPGTSTSATLT
GLTRGATYNIIVEALKDQQRHKVREEVVTVGNSVNEGLNQPTDDSCFDPYTVSHYAVGDE
WERMSESGFKLLCQCLGFGSGHFRCDSSRWCHDNGVNYKIGEKWDRQGENGQMMSCTCLG
NGKGEFKCDPHEATCYDDGKTYHVGEQWQKEYLGAICSCTCFGGQRGWRCDNCRRPGGEP
SPEGTTGQSYNQYSQRYHQRTNTNVNCPIECFMPLDVQADREDSRE
|
| Enzyme 8 Number of Residues |
2386 |
| Enzyme 8 Molecular Weight |
262609 |
| Enzyme 8 Theoretical pI |
5.42 |
| Enzyme 8 GO Classification |
| Function |
| — |
| Process |
| — |
| Component |
|
|
| Enzyme 8 General Function |
Not Available |
| Enzyme 8 Specific Function |
Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape. Interaction with TNR mediates inhibition of cell adhesion and neurite outgrowth |
| Enzyme 8 Pathways |
Not Available |
| Enzyme 8 Reactions |
Not Available |
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
Not Available |
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
12053817  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
P02751  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
FINC_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>1929 bp
ATGCTTAGGGGTCCGGGGCCCGGGCTGCTGCTGCTGGCCGTCCAGTGCCTGGGGACAGCG
GTGCCCTCCACGGGAGCCTCGAAGAGCAAGAGGCAGGCTCAGCAAATGGTTCAGCCCCAG
TCCCCGGTGGCTGTCAGTCAAAGCAAGCCCGGTTGTTATGACAATGGAAAACACTATCAG
ATAAATCAACAGTGGGAGCGGACCTACCTAGGCAATGCGTTGGTTTGTACTTGTTATGGA
GGAAGCCGAGGTTTTAACTGCGAGAGTAAACCTGAAGCTGAAGAGACTTGCTTTGACAAG
TACACTGGGAACACTTACCGAGTGGGTGACACTTATGAGCGTCCTAAAGACTCCATGATC
TGGGACTGTACCTGCATCGGGGCTGGGCGAGGGAGAATAAGCTGTACCATCGCAAACCGC
TGCCATGAAGGGGGTCAGTCCTACAAGATTGGTGACACCTGGAGGAGACCACATGAGACT
GGTGGTTACATGTTAGAGTGTGTGTGTCTTGGTAATGGAAAAGGAGAATGGACCTGCAAG
CCCATAGCTGAGAAGTGTTTTGATCATGCTGCTGGGACTTCCTATGTGGTCGGAGAAACG
TGGGAGAAGCCCTACCAAGGCTGGATGATGGTAGATTGTACTTGCCTGGGAGAAGGCAGC
GGACGCATCACTTGCACTTCTAGAAATAGATGCAACGATCAGGACACAAGGACATCCTAT
AGAATTGGAGACACCTGGAGCAAGAAGGATAATCGAGGAAACCTGCTCCAGTGCATCTGC
ACAGGCAACGGCCGAGGAGAGTGGAAGTGTGAGAGGCACACCTCTGTGCAGACCACATCG
AGCGGATCTGGCCCCTTCACCGATGTTCGTGCAGCTGTTTACCAACCGCAGCCTCACCCC
CAGCCTCCTCCCTATGGCCACTGTGTCACAGACAGTGGTGTGGTCTACTCTGTGGGGATG
CAGTGGCTGAAGACACAAGGAAATAAGCAAATGCTTTGCACGTGCCTGGGCAACGGAGTC
AGCTGCCAAGAGACAGCTGTAACCCAGACTTACGGTGGCAACTCAAATGGAGAGCCATGT
GTCTTACCATTCACCTACAACGACAGGACGGACAGCACAACTTCGAATTATGAGCAGGAC
CAGAAATACTCTTTCTGCACAGACCACACTGTTTTGGTTCAGACTCGAGGAGGAAATTCC
AATGGTGCCTTGTGCCACTTCCCCTTCCTATACAACAACCACAATTACACTGATTGCACT
TCTGAGGGCAGAAGAGACAACATGAAGTGGTGTGGGACCACACAGAACTATGATGCCGAC
CAGAAGTTTGGGTTCTGCCCCATGGCTGCCCACGAGGAAATCTGCACAACCAATGAAGGG
GTCATGTACCGCATTGGAGATCAGTGGGATAAGCAGCATGACATGGGTCACATGATGAGG
TGCACGTGTGTTGGGAATGGTCGTGGGGAATGGACATGCATTGCCTACTCGCAGCTTCGA
GATCAGTGCATTGTTGATGACATCACTTACAATGTGAACGACACATTCCACAAGCGTCAT
GAAGAGGGGCACATGCTGAACTGTACATGCTTCGGTCAGGGTCGGGGCAGGTGGAAGTGT
GATCCCGTCGACCAATGCCAGGATTCAGAGACTGGGACGTTTTATCAAATTGGAGATTCA
TGGGAGAAGTATGTGCATGGTGTCAGATACCAGTGCTACTGCTATGGCCGTGGCATTGGG
GAGTGGCATTGCCAACCTTTACAGACCTATCCAAGCTCAAGTGGTCCTGTCGAAGTATTT
ATCACTGAGACTCCGAGTCAGCCCAACTCCCACCCCATCCAGTGGAATGCACCACAGCCA
TCTCACATTTCCAAGTACATTCTCAGGTGGAGACCTGTGAGTATCCCACCCAGAAACCTT
GGATACTGA
|
| Enzyme 8 GenBank Gene ID |
AJ276395  |
| Enzyme 8 GeneCard ID |
FN1  |
| Enzyme 8 GenAtlas ID |
FN1  |
| Enzyme 8 HGNC ID |
HGNC:3778  |
| Enzyme 8 Chromosome Location |
2 |
| Enzyme 8 Locus |
2q34 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Schor SL, Schor AM: Phenotypic and genetic alterations in mammary stroma: implications for tumour progression. Breast Cancer Res. 2001;3(6):373-9. Epub 2001 Sep 6. [PubMed
]
- Gutman A, Yamada KM, Kornblihtt A: Human fibronectin is synthesized as a pre-propolypeptide. FEBS Lett. 1986 Oct 20;207(1):145-8. [PubMed
]
- Dean DC, Bowlus CL, Bourgeois S: Cloning and analysis of the promotor region of the human fibronectin gene. Proc Natl Acad Sci U S A. 1987 Apr;84(7):1876-80. [PubMed
]
- Kornblihtt AR, Umezawa K, Vibe-Pedersen K, Baralle FE: Primary structure of human fibronectin: differential splicing may generate at least 10 polypeptides from a single gene. EMBO J. 1985 Jul;4(7):1755-9. [PubMed
]
- Calaycay J, Pande H, Lee T, Borsi L, Siri A, Shively JE, Zardi L: Primary structure of a DNA- and heparin-binding domain (Domain III) in human plasma fibronectin. J Biol Chem. 1985 Oct 5;260(22):12136-41. [PubMed
]
- Kornblihtt AR, Vibe-Pedersen K, Baralle FE: Human fibronectin: cell specific alternative mRNA splicing generates polypeptide chains differing in the number of internal repeats. Nucleic Acids Res. 1984 Jul 25;12(14):5853-68. [PubMed
]
- Paolella G, Henchcliffe C, Sebastio G, Baralle FE: Sequence analysis and in vivo expression show that alternative splicing of ED-B and ED-A regions of the human fibronectin gene are independent events. Nucleic Acids Res. 1988 Apr 25;16(8):3545-57. [PubMed
]
- Zardi L, Carnemolla B, Siri A, Petersen TE, Paolella G, Sebastio G, Baralle FE: Transformed human cells produce a new fibronectin isoform by preferential alternative splicing of a previously unobserved exon. EMBO J. 1987 Aug;6(8):2337-42. [PubMed
]
- Gutman A, Kornblihtt AR: Identification of a third region of cell-specific alternative splicing in human fibronectin mRNA. Proc Natl Acad Sci U S A. 1987 Oct;84(20):7179-82. [PubMed
]
- Pierschbacher MD, Ruoslahti E, Sundelin J, Lind P, Peterson PA: The cell attachment domain of fibronectin. Determination of the primary structure. J Biol Chem. 1982 Aug 25;257(16):9593-7. [PubMed
]
- Oldberg A, Linney E, Ruoslahti E: Molecular cloning and nucleotide sequence of a cDNA clone coding for the cell attachment domain in human fibronectin. J Biol Chem. 1983 Sep 10;258(17):10193-6. [PubMed
]
- Oldberg A, Ruoslahti E: Evolution of the fibronectin gene. Exon structure of cell attachment domain. J Biol Chem. 1986 Feb 15;261(5):2113-6. [PubMed
]
- Garcia-Pardo A, Rostagno A, Frangione B: Primary structure of human plasma fibronectin. Characterization of a 38 kDa domain containing the C-terminal heparin-binding site (Hep III site) and a region of molecular heterogeneity. Biochem J. 1987 Feb 1;241(3):923-8. [PubMed
]
- Bernard MP, Kolbe M, Weil D, Chu ML: Human cellular fibronectin: comparison of the carboxyl-terminal portion with rat identifies primary structural domains separated by hypervariable regions. Biochemistry. 1985 May 21;24(11):2698-704. [PubMed
]
- Kornblihtt AR, Vibe-Pedersen K, Baralle FE: Human fibronectin: molecular cloning evidence for two mRNA species differing by an internal segment coding for a structural domain. EMBO J. 1984 Jan;3(1):221-6. [PubMed
]
- Sekiguchi K, Klos AM, Kurachi K, Yoshitake S, Hakomori S: Human liver fibronectin complementary DNAs: identification of two different messenger RNAs possibly encoding the alpha and beta subunits of plasma fibronectin. Biochemistry. 1986 Aug 26;25(17):4936-41. [PubMed
]
- Parker AE, Boutell J, Carr A, Maciewicz RA: Novel cartilage-specific splice variants of fibronectin. Osteoarthritis Cartilage. 2002 Jul;10(7):528-34. [PubMed
]
- Umezawa K, Kornblihtt AR, Baralle FE: Isolation and characterization of cDNA clones for human liver fibronectin. FEBS Lett. 1985 Jul 1;186(1):31-4. [PubMed
]
- Vibe-Pedersen K, Magnusson S, Baralle FE: Donor and acceptor splice signals within an exon of the human fibronectin gene: a new type of differential splicing. FEBS Lett. 1986 Oct 27;207(2):287-91. [PubMed
]
- Garcia-Pardo A, Pearlstein E, Frangione B: Primary structure of human plasma fibronectin. Characterization of a 31,000-dalton fragment from the COOH-terminal region containing a free sulfhydryl group and a fibrin-binding site. J Biol Chem. 1985 Aug 25;260(18):10320-5. [PubMed
]
- Kornblihtt AR, Vibe-Pedersen K, Baralle FE: Isolation and characterization of cDNA clones for human and bovine fibronectins. Proc Natl Acad Sci U S A. 1983 Jun;80(11):3218-22. [PubMed
]
- Garcia-Pardo A, Pearlstein E, Frangione B: Primary structure of human plasma fibronectin. The 29,000-dalton NH2-terminal domain. J Biol Chem. 1983 Oct 25;258(20):12670-4. [PubMed
]
- Owens RJ, Baralle FE: Mapping the collagen-binding site of human fibronectin by expression in Escherichia coli. EMBO J. 1986 Nov;5(11):2825-30. [PubMed
]
- Liu MC, Yu S, Sy J, Redman CM, Lipmann F: Tyrosine sulfation of proteins from the human hepatoma cell line HepG2. Proc Natl Acad Sci U S A. 1985 Nov;82(21):7160-4. [PubMed
]
- Tressel T, McCarthy JB, Calaycay J, Lee TD, Legesse K, Shively JE, Pande H: Human plasma fibronectin. Demonstration of structural differences between the A- and B-chains in the III CS region. Biochem J. 1991 Mar 15;274 ( Pt 3):731-8. [PubMed
]
- Balbona K, Tran H, Godyna S, Ingham KC, Strickland DK, Argraves WS: Fibulin binds to itself and to the carboxyl-terminal heparin-binding region of fibronectin. J Biol Chem. 1992 Oct 5;267(28):20120-5. [PubMed
]
- Rostagno A, Williams MJ, Baron M, Campbell ID, Gold LI: Further characterization of the NH2-terminal fibrin-binding site on fibronectin. J Biol Chem. 1994 Dec 16;269(50):31938-45. [PubMed
]
- Sasaki T, Brakebusch C, Engel J, Timpl R: Mac-2 binding protein is a cell-adhesive protein of the extracellular matrix which self-assembles into ring-like structures and binds beta1 integrins, collagens and fibronectin. EMBO J. 1998 Mar 16;17(6):1606-13. [PubMed
]
- Baron M, Main AL, Driscoll PC, Mardon HJ, Boyd J, Campbell ID: 1H NMR assignment and secondary structure of the cell adhesion type III module of fibronectin. Biochemistry. 1992 Feb 25;31(7):2068-73. [PubMed
]
- Main AL, Harvey TS, Baron M, Boyd J, Campbell ID: The three-dimensional structure of the tenth type III module of fibronectin: an insight into RGD-mediated interactions. Cell. 1992 Nov 13;71(4):671-8. [PubMed
]
- Williams MJ, Phan I, Harvey TS, Rostagno A, Gold LI, Campbell ID: Solution structure of a pair of fibronectin type 1 modules with fibrin binding activity. J Mol Biol. 1994 Jan 28;235(4):1302-11. [PubMed
]
- Potts JR, Phan I, Williams MJ, Campbell ID: High-resolution structural studies of the factor XIIIa crosslinking site and the first type 1 module of fibronectin. Nat Struct Biol. 1995 Nov;2(11):946-50. [PubMed
]
- Sticht H, Pickford AR, Potts JR, Campbell ID: Solution structure of the glycosylated second type 2 module of fibronectin. J Mol Biol. 1998 Feb 13;276(1):177-87. [PubMed
]
- Fattorusso R, Pellecchia M, Viti F, Neri P, Neri D, Wuthrich K: NMR structure of the human oncofoetal fibronectin ED-B domain, a specific marker for angiogenesis. Structure. 1999 Apr 15;7(4):381-90. [PubMed
]
- Bocquier AA, Potts JR, Pickford AR, Campbell ID: Solution structure of a pair of modules from the gelatin-binding domain of fibronectin. Structure. 1999 Dec 15;7(12):1451-60. [PubMed
]
- Pickford AR, Smith SP, Staunton D, Boyd J, Campbell ID: The hairpin structure of the (6)F1(1)F2(2)F2 fragment from human fibronectin enhances gelatin binding. EMBO J. 2001 Apr 2;20(7):1519-29. [PubMed
]
- Niimi T, Osawa M, Yamaji N, Yasunaga K, Sakashita H, Mase T, Tanaka A, Fujita S: NMR structure of human fibronectin EDA. J Biomol NMR. 2001 Nov;21(3):281-4. [PubMed
]
- Schwarz-Linek U, Werner JM, Pickford AR, Gurusiddappa S, Kim JH, Pilka ES, Briggs JA, Gough TS, Hook M, Campbell ID, Potts JR: Pathogenic bacteria attach to human fibronectin through a tandem beta-zipper. Nature. 2003 May 8;423(6936):177-81. [PubMed
]
- Dickinson CD, Veerapandian B, Dai XP, Hamlin RC, Xuong NH, Ruoslahti E, Ely KR: Crystal structure of the tenth type III cell adhesion module of human fibronectin. J Mol Biol. 1994 Mar 4;236(4):1079-92. [PubMed
]
- Leahy DJ, Aukhil I, Erickson HP: 2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region. Cell. 1996 Jan 12;84(1):155-64. [PubMed
]
- Sharma A, Askari JA, Humphries MJ, Jones EY, Stuart DI: Crystal structure of a heparin- and integrin-binding segment of human fibronectin. EMBO J. 1999 Mar 15;18(6):1468-79. [PubMed
]
|
| Enzyme 8 Metabolite References |
- Lai L, Chen J, Hao CM, Lin S, Gu Y: Aldosterone promotes fibronectin production through a Smad2-dependent TGF-beta1 pathway in mesangial cells. Biochem Biophys Res Commun. 2006 Sep 15;348(1):70-5. Epub 2006 Jul 21. [PubMed
]
|
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
7620 |
| Enzyme 9 Name |
Natriuretic peptides B precursor [Contains: Gamma-brain natriuretic peptide; Brain natriuretic peptide 32 |
| Enzyme 9 Synonyms |
- BNP-32]
|
| Enzyme 9 Gene Name |
NPPB |
| Enzyme 9 Protein Sequence |
>Natriuretic peptides B precursor [Contains: Gamma-brain natriuretic peptide; Brain natriuretic peptide 32
MDPQTAPSRALLLLLFLHLAFLGGRSHPLGSPGSASDLETSGLQEQRNHLQGKLSELQVE
QTSLEPLQESPRPTGVWKSREVATEGIRGHRKMVLYTLRAPRSPKMVQGSGCFGRKMDRI
SSSSGLGCKVLRRH
|
| Enzyme 9 Number of Residues |
134 |
| Enzyme 9 Molecular Weight |
14726 |
| Enzyme 9 Theoretical pI |
11.01 |
| Enzyme 9 GO Classification |
| Function |
- hormone activity
- receptor binding
- signal transducer activity
|
| Process |
| — |
| Component |
|
|
| Enzyme 9 General Function |
Not Available |
| Enzyme 9 Specific Function |
Acts as a cardiac hormone with a variety of biological actions including natriuresis, diuresis, vasorelaxation, and inhibition of renin and aldosterone secretion. It is thought to play a key role in cardiovascular homeostasis. Helps restore the body's salt and water balance. Improves heart function |
| Enzyme 9 Pathways |
Not Available |
| Enzyme 9 Reactions |
Not Available |
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
Not Available |
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
179515  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
P16860  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
ANFB_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>405 bp
ATGGATCCCCAGACAGCACCTTCCCGGGCGCTCCTGCTCCTGCTCTTCTTGCATCTGGCT
TTCCTGGGAGGTCGTTCCCACCCGCTGGGCAGCCCCGGTTCAGCCTCGGACTTGGAAACG
TCCGGGTTACAGGAGCAGCGCAACCATTTGCAGGGCAAACTGTCGGAGCTGCAGGTGGAG
CAGACATCCCTGGAGCCCCTCCAGGAGAGCCCCCGTCCCACAGGTGTCTGGAAGTCCCGG
GAGGTAGCCACCGAGGGCATCCGTGGGCACCGCAAAATGGTCCTCTACACCCTGCGGGCA
CCACGAAGCCCCAAGATGGTGCAAGGGTCTGGCTGCTTTGGGAGGAAGATGGACCGGATC
AGCTCCTCCAGTGGCCTGGGCTGCAAAGTGCTGAGGCGGCATTAA
|
| Enzyme 9 GenBank Gene ID |
M31776  |
| Enzyme 9 GeneCard ID |
NPPB  |
| Enzyme 9 GenAtlas ID |
NPPB  |
| Enzyme 9 HGNC ID |
HGNC:7940  |
| Enzyme 9 Chromosome Location |
1 |
| Enzyme 9 Locus |
1p36.2 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Seilhamer JJ, Arfsten A, Miller JA, Lundquist P, Scarborough RM, Lewicki JA, Porter JG: Human and canine gene homologs of porcine brain natriuretic peptide. Biochem Biophys Res Commun. 1989 Dec 15;165(2):650-8. [PubMed
]
- Sudoh T, Maekawa K, Kojima M, Minamino N, Kangawa K, Matsuo H: Cloning and sequence analysis of cDNA encoding a precursor for human brain natriuretic peptide. Biochem Biophys Res Commun. 1989 Mar 31;159(3):1427-34. [PubMed
]
- Hino J, Tateyama H, Minamino N, Kangawa K, Matsuo H: Isolation and identification of human brain natriuretic peptides in cardiac atrium. Biochem Biophys Res Commun. 1990 Mar 16;167(2):693-700. [PubMed
]
- Kambayashi Y, Nakao K, Mukoyama M, Saito Y, Ogawa Y, Shiono S, Inouye K, Yoshida N, Imura H: Isolation and sequence determination of human brain natriuretic peptide in human atrium. FEBS Lett. 1990 Jan 1;259(2):341-5. [PubMed
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
7645 |
| Enzyme 10 Name |
Connective tissue growth factor precursor |
| Enzyme 10 Synonyms |
- Hypertrophic chondrocyte- specific protein 24
|
| Enzyme 10 Gene Name |
CTGF |
| Enzyme 10 Protein Sequence |
>Connective tissue growth factor precursor
MTAASMGPVRVAFVVLLALCSRPAVGQNCSGPCRCPDEPAPRCPAGVSLVLDGCGCCRVC
AKQLGELCTERDPCDPHKGLFCHFGSPANRKIGVCTAKDGAPCIFGGTVYRSGESFQSSC
KYQCTCLDGAVGCMPLCSMDVRLPSPDCPFPRRVKLPGKCCEEWVCDEPKDQTVVGPALA
AYRLEDTFGPDPTMIRANCLVQTTEWSACSKTCGMGISTRVTNDNASCRLEKQSRLCMVR
PCEADLEENIKKGKKCIRTPKISKPIKFELSGCTSMKTYRAKFCGVCTDGRCCTPHRTTT
LPVEFKCPDGEVMKKNMMFIKTCACHYNCPGDNDIFESLYYRKMYGDMA
|
| Enzyme 10 Number of Residues |
349 |
| Enzyme 10 Molecular Weight |
38092 |
| Enzyme 10 Theoretical pI |
8.03 |
| Enzyme 10 GO Classification |
| Function |
- binding
- growth factor binding
- insulin-like growth factor binding
- protein binding
|
| Process |
- regulation of biological process
- regulation of cell growth
- regulation of growth
|
| Component |
|
|
| Enzyme 10 General Function |
Not Available |
| Enzyme 10 Specific Function |
Major connective tissue mitoattractant secreted by vascular endothelial cells. Promotes proliferation and differentiation of chondrocytes. Mediates heparin- and divalent cation-dependent cell adhesion in many cell types including fibroblasts, myofibroblasts, endothelial and epithelial cells. Enhances fibroblast growth factor-induced DNA synthesis |
| Enzyme 10 Pathways |
Not Available |
| Enzyme 10 Reactions |
Not Available |
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
Not Available |
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
180924  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
P29279  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
CTGF_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>1050 bp
ATGACCGCCGCCAGTATGGGCCCCGTCCGCGTCGCCTTCGTGGTCCTCCTCGCCCTCTGC
AGCCGGCCGGCCGTCGGCCAGAACTGCAGCGGGCCGTGCCGGTGCCCGGACGAGCCGGCG
CCGCGCTGCCCGGCGGGCGTGAGCCTCGTGCTGGACGGCTGCGGCTGCTGCCGCGTCTGC
GCCAAGCAGCTGGGCGAGCTGTGCACCGAGCGCGACCCCTGCGACCCGCACAAGGGCCTC
TTCTGTGACTTCGGCTCCCCGGCCAACCGCAAGATCGGCGTGTGCACCGCCAAAGATGGT
GCTCCCTGCATCTTCGGTGGTACGGTGTACCGCAGCGGAGAGTCCTTCCAGAGCAGCTGC
AAGTACCAGTGCACGTGCCTGGACGGGGCGGTGGGCTGCATGCCCCTGTGCAGCATGGAC
GTTCGTCTGCCCAGCCCTGACTGCCCCTTCCCGAGGAGGGTCAAGCTGCCCGGGAAATGC
TGCGAGGAGTGGGTGTGTGACGAGCCCAAGGACCAAACCGTGGTTGGGCCTGCCCTCGCG
GCTTACCGACTGGAAGACACGTTTGGCCCAGACCCAACTATGATTAGAGCCAACTGCCTG
GTCCAGACCACAGAGTGGAGCGCCTGTTCCAAGACCTGTGGGATGGGCATCTCCACCCGG
GTTACCAATGACAACGCCTCCTGCAGGCTAGAGAAGCAGAGCCGCCTGTGCATGGTCAGG
CCTTGCGAAGCTGACCTGGAAGAGAACATTAAGAAGGGCAAAAAGTGCATCCGTACTCCC
AAAATCTCCAAGCCTATCAAGTTTGAGCTTTCTGGCTGCACCAGCATGAAGACATACCGA
GCTAAATTCTGTGGAGTATGTACCGACGGCCGATGCTGCACCCCCCACAGAACCACCACC
CTGCCGGTGGAGTTCAAGTGCCCTGACGGCGAGGTCATGAAGAAGAACATGATGTTCATC
AAGACCTGTGCCTGCCATTACAACTGTCCCGGAGACAATGACATCTTTGAATCGCTGTAC
TACAGGAAGATGTACGGAGACATGGCATGA
|
| Enzyme 10 GenBank Gene ID |
M92934  |
| Enzyme 10 GeneCard ID |
CTGF  |
| Enzyme 10 GenAtlas ID |
CTGF  |
| Enzyme 10 HGNC ID |
HGNC:2500  |
| Enzyme 10 Chromosome Location |
6 |
| Enzyme 10 Locus |
6q23.1 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Bradham DM, Igarashi A, Potter RL, Grotendorst GR: Connective tissue growth factor: a cysteine-rich mitogen secreted by human vascular endothelial cells is related to the SRC-induced immediate early gene product CEF-10. J Cell Biol. 1991 Sep;114(6):1285-94. [PubMed
]
- Igarashi A, Bradham DM, Okochi H, Grotendorst GR: Connective tissue growth factor. J Dermatol. 1992 Nov;19(11):642-3. [PubMed
]
- Oemar BS, Werner A, Garnier JM, Do DD, Godoy N, Nauck M, Marz W, Rupp J, Pech M, Luscher TF: Human connective tissue growth factor is expressed in advanced atherosclerotic lesions. Circulation. 1997 Feb 18;95(4):831-9. [PubMed
]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed
]
- Nakanishi T, Nishida T, Shimo T, Kobayashi K, Kubo T, Tamatani T, Tezuka K, Takigawa M: Effects of CTGF/Hcs24, a product of a hypertrophic chondrocyte-specific gene, on the proliferation and differentiation of chondrocytes in culture. Endocrinology. 2000 Jan;141(1):264-73. [PubMed
]
- Ball DK, Rachfal AW, Kemper SA, Brigstock DR: The heparin-binding 10 kDa fragment of connective tissue growth factor (CTGF) containing module 4 alone stimulates cell adhesion. J Endocrinol. 2003 Feb;176(2):R1-7. [PubMed
]
|
| Enzyme 10 Metabolite References |
- Gauer S, Segitz V, Goppelt-Struebe M: Aldosterone induces CTGF in mesangial cells by activation of the glucocorticoid receptor. Nephrol Dial Transplant. 2007 Nov;22(11):3154-9. Epub 2007 Jun 30. [PubMed
]
|
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
7648 |
| Enzyme 11 Name |
Type-1 angiotensin II receptor |
| Enzyme 11 Synonyms |
- AT1
- AT1AR
- AT1BR
|
| Enzyme 11 Gene Name |
AGTR1 |
| Enzyme 11 Protein Sequence |
>Type-1 angiotensin II receptor
MILNSSTEDGIKRIQDDCPKAGRHNYIFVMIPTLYSIIFVVGIFGNSLVVIVIYFYMKLK
TVASVFLLNLALADLCFLLTLPLWAVYTAMEYRWPFGNYLCKIASASVSFNLYASVFLLT
CLSIDRYLAIVHPMKSRLRRTMLVAKVTCIIIWLLAGLASLPAIIHRNVFFIENTNITVC
AFHYESQNSTLPIGLGLTKNILGFLFPFLIILTSYTLIWKALKKAYEIQKNKPRNDDIFK
IIMAIVLFFFFSWIPHQIFTFLDVLIQLGIIRDCRIADIVDTAMPITICIAYFNNCLNPL
FYGFLGKKFKRYFLQLLKYIPPKAKSHSNLSTKMSTLSYRPSDNVSSSTKKPAPCFEVE
|
| Enzyme 11 Number of Residues |
359 |
| Enzyme 11 Molecular Weight |
41062 |
| Enzyme 11 Theoretical pI |
9.71 |
| Enzyme 11 GO Classification |
| Function |
- C-X-C chemokine receptor activity
- G-protein chemoattractant receptor activity
- G-protein coupled receptor activity
- angiotensin receptor activity
- angiotensin type II receptor activity
- bradykinin receptor activity
- chemokine receptor activity
- peptide receptor activity, G-protein coupled
- receptor activity
- rhodopsin-like receptor activity
- signal transducer activity
- transmembrane receptor activity
|
| Process |
- G-protein coupled receptor protein signaling pathway
- cell communication
- cell surface receptor linked signal transduction
- cellular process
- signal transduction
|
| Component |
- cell
- integral to membrane
- intrinsic to membrane
- membrane
|
|
| Enzyme 11 General Function |
Not Available |
| Enzyme 11 Specific Function |
Receptor for angiotensin II. Mediates its action by association with G proteins that activate a phosphatidylinositol- calcium second messenger system |
| Enzyme 11 Pathways |
Not Available |
| Enzyme 11 Reactions |
Not Available |
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
- 28-52
65-87
103-124
143-162
193-214
241-262
276-296
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
179122  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
P30556  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
AGTR1_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>1080 bp
ATGATTCTCAACTCTTCTACTGAAGATGGTATTAAAAGAATCCAAGATGATTGTCCCAAA
GCTGGAAGGCATAATTACATATTTGTCATGATTCCTACTTTATACAGTATCATCTTTGTG
GTGGGAATATTTGGAAACAGCTTGGTGGTGATAGTCATTTACTTTTATATGAAGCTGAAG
ACTGTGGCCAGTGTTTTTCTTTTGAATTTAGCACTGGCTGACTTATGCTTTTTACTGACT
TTGCCACTATGGGCTGTCTACACAGCTATGGAATACCGCTGGCCCTTTGGCAATTACCTA
TGTAAGATTGCTTCAGCCAGCGTCAGTTTCAACCTGTACGCTAGTGTGTTTCTACTCACG
TGTCTCAGCATTGATCGATACCTGGCTATTGTTCACCCAATGAAGTCCCGCCTTCGACGC
ACAATGCTTGTAGCCAAAGTCACCTGCATCATCATTTGGCTGCTGGCAGGCTTGGCCAGT
TTGCCAGCTATAATCCATCGAAATGTATTTTTCATTGAGAACACCAATATTACAGTTTGT
GCTTTCCATTATGAGTCCCAAAATTCAACCCTCCCGATAGGGCTGGGCCTGACCAAAAAT
ATACTGGGTTTCCTGTTTCCTTTTCTGATCATTCTTACAAGTTATACTCTTATTTGGAAG
GCCCTAAAGAAGGCTTATGAAATTCAGAAGAACAAACCAAGAAATGATGATATTTTTAAG
ATAATTATGGCAATTGTGCTTTTCTTTTTCTTTTCCTGGATTCCCCACCAAATATTCACT
TTTCTGGATGTATTGATTCAACTAGGCATCATACGTGACTGTAGAATTGCAGATATTGTG
GACACGGCCATGCCTATCACCATTTGTATAGCTTATTTTAACAATTGCCTGAATCCTCTT
TTTTATGGCTTTCTGGGGAAAAAATTTAAAAGATATTTTCTCCAGCTTCTAAAATATATT
CCCCCAAAAGCCAAATCCCACTCAAACCTTTCAACAAAAATGAGCACGCTTTCCTACCGC
CCCTCAGATAATGTAAGCTCATCCACCAAGAAGCCTGCACCATGTTTTGAGGTTGAGTGA
|
| Enzyme 11 GenBank Gene ID |
M91464  |
| Enzyme 11 GeneCard ID |
AGTR1  |
| Enzyme 11 GenAtlas ID |
AGTR1  |
| Enzyme 11 HGNC ID |
HGNC:336  |
| Enzyme 11 Chromosome Location |
3 |
| Enzyme 11 Locus |
3q21-q25 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Mauzy CA, Hwang O, Egloff AM, Wu LH, Chung FZ: Cloning, expression, and characterization of a gene encoding the human angiotensin II type 1A receptor. Biochem Biophys Res Commun. 1992 Jul 15;186(1):277-84. [PubMed
]
- Furuta H, Guo DF, Inagami T: Molecular cloning and sequencing of the gene encoding human angiotensin II type 1 receptor. Biochem Biophys Res Commun. 1992 Feb 28;183(1):8-13. [PubMed
]
- Bergsma DJ, Ellis C, Kumar C, Nuthulaganti P, Kersten H, Elshourbagy N, Griffin E, Stadel JM, Aiyar N: Cloning and characterization of a human angiotensin II type 1 receptor. Biochem Biophys Res Commun. 1992 Mar 31;183(3):989-95. [PubMed
]
- Takayanagi R, Ohnaka K, Sakai Y, Nakao R, Yanase T, Haji M, Inagami T, Furuta H, Gou DF, Nakamuta M, et al.: Molecular cloning, sequence analysis and expression of a cDNA encoding human type-1 angiotensin II receptor. Biochem Biophys Res Commun. 1992 Mar 16;183(2):910-6. [PubMed
]
- Curnow KM, Pascoe L, White PC: Genetic analysis of the human type-1 angiotensin II receptor. Mol Endocrinol. 1992 Jul;6(7):1113-8. [PubMed
]
- Konishi H, Kuroda S, Inada Y, Fujisawa Y: Novel subtype of human angiotensin II type 1 receptor: cDNA cloning and expression. Biochem Biophys Res Commun. 1994 Mar 15;199(2):467-74. [PubMed
]
- Nawata H, Takayanagi R, Ohnaka K, Sakai Y, Imasaki K, Yanase T, Ikuyama S, Tanaka S, Ohe K: Type 1 angiotensin II receptors of adrenal tumors. Steroids. 1995 Jan;60(1):28-34. [PubMed
]
|
| Enzyme 11 Metabolite References |
- Yamada M, Kushibiki M, Osanai T, Tomita H, Okumura K: Vasoconstrictor effect of aldosterone via angiotensin II type 1 (AT1) receptor: possible role of AT1 receptor dimerization. Cardiovasc Res. 2008 Jul 1;79(1):169-78. Epub 2008 Mar 7. [PubMed
]
|
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
8137 |
| Enzyme 12 Name |
Mineralocorticoid receptor |
| Enzyme 12 Synonyms |
- MR
|
| Enzyme 12 Gene Name |
NR3C2 |
| Enzyme 12 Protein Sequence |
>Mineralocorticoid receptor
METKGYHSLPEGLDMERRWGQVSQAVERSSLGPTERTDENNYMEIVNVSCVSGAIPNNST
QGSSKEKQELLPCLQQDNNRPGILTSDIKTELESKELSATVAESMGLYMDSVRDADYSYE
QQNQQGSMSPAKIYQNVEQLVKFYKGNGHRPSTLSCVNTPLRSFMSDSGSSVNGGVMRAI
VKSPIMCHEKSPSVCSPLNMTSSVCSPAGINSVSSTTASFGSFPVHSPITQGTPLTCSPN
AENRGSRSHSPAHASNVGSPLSSPLSSMKSSISSPPSHCSVKSPVSSPNNVTLRSSVSSP
ANINNSRCSVSSPSNTNNRSTLSSPAASTVGSICSPVNNAFSYTASGTSAGSSTLRDVVP
SPDTQEKGAQEVPFPKTEEVESAISNGVTGQLNIVQYIKPEPDGAFSSSCLGGNSKINSD
SSFSVPIKQESTKHSCSGTSFKGNPTVNPFPFMDGSYFSFMDDKDYYSLSGILGPPVPGF
DGNCEGSGFPVGIKQEPDDGSYYPEASIPSSAIVGVNSGGQSFHYRIGAQGTISLSRSAR
DQSFQHLSSFPPVNTLVESWKSHGDLSSRRSDGYPVLEYIPENVSSSTLRSVSTGSSRPS
KICLVCGDEASGCHYGVVTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRL
QKCLQAGMNLGARKSKKLGKLKGIHEEQPQQQQPPPPPPPPQSPEEGTTYIAPAKEPSVN
TALVPQLSTISRALTPSPVMVLENIEPEIVYAGYDSSKPDTAENLLSTLNRLAGKQMIQV
VKWAKVLPGFKNLPLEDQITLIQYSWMCLSSFALSWRSYKHTNSQFLYFAPDLVFNEEKM
HQSAMYELCQGMHQISLQFVRLQLTFEEYTIMKVLLLLSTIPKDGLKSQAAFEEMRTNYI
KELRKMVTKCPNNSGQSWQRFYQLTKLLDSMHDLVSDLLEFCFYTFRESHALKVEFPAML
VEIISDQLPKVESGNAKPLYFHRK
|
| Enzyme 12 Number of Residues |
984 |
| Enzyme 12 Molecular Weight |
107068 |
| Enzyme 12 Theoretical pI |
7.42 |
| Enzyme 12 GO Classification |
| Function |
- DNA binding
- binding
- ligand-dependent nuclear receptor activity
- nucleic acid binding
- receptor activity
- signal transducer activity
- steroid hormone receptor activity
- transcription factor 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
- regulation of transcription, DNA-dependent
|
| Component |
- intracellular membrane-bound organelle
- membrane-bound organelle
- nucleus
- organelle
|
|
| Enzyme 12 General Function |
Carbohydrate transport and metabolism |
| Enzyme 12 Specific Function |
Receptor for both mineralocorticoids (MC) such as aldosterone and glucocorticoids (GC) such as corticosterone or cortisol. Binds to mineralocorticoid response elements (MRE) and transactivates target genes. The effect of MC is to increase ion and water transport and thus raise extracellular fluid volume and blood pressure and lower potassium levels |
| Enzyme 12 Pathways |
Not Available |
| Enzyme 12 Reactions |
Not Available |
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
307166  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
P08235  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
MCR_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>2955 bp
ATGGAGACCAAAGGCTACCACAGTCTCCCTGAAGGTCTAGATATGGAAAGACGGTGGGGT
CAAGTTTCTCAGGCTGTGGAGCGTTCTTCCCTGGGACCTACAGAGAGGACCGATGAGAAT
AACTACATGGAGATTGTCAACGTAAGCTGTGTTTCCGGTGCTATTCCAAACAACAGTACT
CAAGGAAGCAGCAAAGAAAAACAAGAACTACTCCCTTGCCTTCAGCAAGACAATAATCGG
CCTGGGATTTTAACATCTGATATTAAAACTGAGCTGGAATCTAAGGAACTTTCAGCAACT
GTAGCTGAGTCCATGGGTTTATATATGGATTCTGTAAGAGATGCTGACTATTCCTATGAG
CAGCAGAACCAACAAGGAAGCATGAGTCCAGCTAAGATTTATCAGAATGTTGAACAGCTG
GTGAAATTTTACAAAGGAAATGGCCATCGTCCTTCCACTCTAAGTTGTGTGAACACGCCC
TTGAGATCATTTATGTCTGACTCTGGGAGCTCCGTGAATGGTGGCGTCATGCGCGCCATT
GTTAAAAGCCCTATCATGTGTCATGAGAAAAGCCCGTCTGTTTGCAGCCCTCTGAACATG
ACATCTTCGGTTTGCAGCCCTGCTGGAATCAACTCTGTGTCCTCCACCACAGCCAGCTTT
GGCAGTTTTCCAGTGCACAGCCCAATCACCCAGGGAACTCCTCTGACATGCTCCCCTAAT
GCTGAAAATCGAGGCTCCAGGTCGCACAGCCCTGCACATGCTAGCAATGTGGGCTCTCCT
CTCTCAAGTCCGTTAAGTAGCATGAAATCCTCAATTTCCAGCCCTCCAAGTCACTGCAGT
GTAAAATCTCCAGTCTCCAGTCCCAATAATGTCACTCTGAGATCCTCTGTGTCTAGCCCT
GCAAATATTAACAACTCAAGGTGCTCTGTTTCCAGCCCTTCGAACACTAATAACAGATCC
ACGCTTTCCAGTCCGGCAGCCAGTACTGTGGGATCTATCTGTAGCCCTGTAAACAATGCC
TTCAGCTACACTGCTTCTGGCACCTCTGCTGGATCCAGTACATTGCGGGATGTGGTTCCC
AGTCCAGACACGCAGGAGAAAGGTGCTCAAGAGGTCCCTTTTCCTAAGACTGAGGAAGTA
GAGAGTGCCATCTCAAATGGTGTGACTGGCCAGCTTAATATTGTCCAGTACATAAAACCA
GAACCAGATGGAGCTTTTAGCAGCTCATGTCTAGGAGGAAATAGCAAAATAAATTCGGAT
TCTTCATTCTCAGTACCAATAAAGCAAGAATCAACCAAGCATTCATGTTCAGGCACCTCT
TTTAAAGGGAATCCAACAGTAAACCCGTTTCCATTTATGGATGGCTCGTATTTTTCCTTT
ATGGATGATAAAGACTATTATTCCCTATCAGGAATTTTAGGACCACCTGTGCCCGGCTTT
GATGGTAACTGTGAAGGCAGCGGATTCCCAGTGGGTATTAAACAAGAACCAGATGACGGG
AGCTATTACCCAGAGGCCAGCATCCCTTCCTCTGCTATTGTTGGGGTGAATTCAGGTGGA
CAGTCCTTCCACTACAGGATTGGTGCTCAAGGTACAATATCTTTATCACGATCGGCTAGA
GACCAATCTTTCCAACACCTGAGTTCCTTTCCTCCTGTCAATACTTTAGTGGAGTCATGG
AAATCACACGGCGACCTGTCGTCTAGAAGAAGTGATGGGTATCCGGTCTTAGAATACATT
CCAGAAAATGTATCAAGCTCTACTTTACGAAGTGTTTCTACTGGATCTTCAAGACCTTCA
AAAATATGTTTGGTGTGTGGGGATGAGGCTTCAGGATGCCATTATGGGGTAGTCACCTGT
GGCAGCTGCAAAGTTTTCTTCAAAAGAGCAGTGGAAGGGCAACACAACTATTTATGTGCT
GGAAGAAATGATTGCATCATTGATAAGATTCGACGAAAGAATTGTCCTGCTTGCAGACTT
CAGAAATGTCTTCAAGCTGGAATGAATTTAGGAGCACGAAAGTCAAAGAAGTTGGGAAAG
TTAAAAGGGATTCACGAGGAGCAGCCACAGCAGCAGCAGCCCCCACCCCCACCCCCACCC
CCGCAAAGCCCAGAGGAAGGGACAACGTACATCGCTCCTGCAAAAGAACCCTCGGTCAAC
ACAGCACTGGTTCCTCAGCTCTCCACAATCTCACGAGCGCTCACACCTTCCCCCGTTATG
GTCCTTGAAAACATTGAACCTGAAATTGTATATGCAGGCTATGACAGCTCAAAACCAGAT
ACAGCCGAAAATCTGCTCTCCACGCTCAACCGCTTAGCAGGCAAACAGATGATCCAAGTC
GTGAAGTGGGCAAAGGTACTTCCAGGATTTAAAAACTTGCCTCTTGAGGACCAAATTACC
CTAATCCAGTATTCTTGGATGTGTCTATCATCATTTGCCTTGAGCTGGAGATCGTACAAA
CATACGAACAGCCAATTTCTCTATTTTGCACCAGACCTAGTCTTTAATGAAGAGAAGATG
CATCAGTCTGCCATGTATGAACTATGCCAGGGGATGCACCAAATCAGCCTTCAGTTCGTT
CGACTGCAGCTCACCTTTGAAGAATACACCATCATGAAAGTTTTGCTGCTACTAAGCACA
ATTCCAAAGGATGGCCTCAAAAGCCAGGCTGCATTTGAAGAAATGAGGACAAATTACATC
AAAGAACTGAGGAAGATGGTAACTAAGTGTCCCAACAATTCTGGGCAGAGCTGGCAGAGG
TTCTACCAACTGACCAAGCTGCTGGACTCCATGCATGACCTGGTGAGCGACCTGCTGGAA
TTCTGCTTCTACACCTTCCGAGAGTCCCATGCGCTGAAGGTAGAGTTCCCCGCAATGCTG
GTGGAGATCATCAGCGACCAGCTGCCCAAGGTGGAGTCGGGGAACGCCAAGCCGCTCTAC
TTCCACCGGAAGTGA
|
| Enzyme 12 GenBank Gene ID |
M16801  |
| Enzyme 12 GeneCard ID |
NR3C2  |
| Enzyme 12 GenAtlas ID |
NR3C2  |
| Enzyme 12 HGNC ID |
HGNC:7979  |
| Enzyme 12 Chromosome Location |
4 |
| Enzyme 12 Locus |
4q31.1 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- Arriza JL, Weinberger C, Cerelli G, Glaser TM, Handelin BL, Housman DE, Evans RM: Cloning of human mineralocorticoid receptor complementary DNA: structural and functional kinship with the glucocorticoid receptor. Science. 1987 Jul 17;237(4812):268-75. [PubMed
]
- Zennaro MC, Souque A, Viengchareun S, Poisson E, Lombes M: A new human MR splice variant is a ligand-independent transactivator modulating corticosteroid action. Mol Endocrinol. 2001 Sep;15(9):1586-98. [PubMed
]
- Geller DS, Rodriguez-Soriano J, Vallo Boado A, Schifter S, Bayer M, Chang SS, Lifton RP: Mutations in the mineralocorticoid receptor gene cause autosomal dominant pseudohypoaldosteronism type I. Nat Genet. 1998 Jul;19(3):279-81. [PubMed
]
- Alnemri ES, Maksymowych AB, Robertson NM, Litwack G: Overexpression and characterization of the human mineralocorticoid receptor. J Biol Chem. 1991 Sep 25;266(27):18072-81. [PubMed
]
- Bloem LJ, Guo C, Pratt JH: Identification of a splice variant of the rat and human mineralocorticoid receptor genes. J Steroid Biochem Mol Biol. 1995 Nov;55(2):159-62. [PubMed
]
- Zennaro MC, Farman N, Bonvalet JP, Lombes M: Tissue-specific expression of alpha and beta messenger ribonucleic acid isoforms of the human mineralocorticoid receptor in normal and pathological states. J Clin Endocrinol Metab. 1997 May;82(5):1345-52. [PubMed
]
- Bruner KL, Derfoul A, Robertson NM, Guerriero G, Fernandes-Alnemri T, Alnemri ES, Litwack G: The unliganded mineralocorticoid receptor is associated with heat shock proteins 70 and 90 and the immunophilin FKBP-52. Recept Signal Transduct. 1997;7(2):85-98. [PubMed
]
- Lupo B, Mesnier D, Auzou G: Cysteines 849 and 942 of human mineralocorticoid receptor are crucial for steroid binding. Biochemistry. 1998 Sep 1;37(35):12153-9. [PubMed
]
- Hellal-Levy C, Fagart J, Souque A, Rafestin-Oblin ME: Mechanistic aspects of mineralocorticoid receptor activation. Kidney Int. 2000 Apr;57(4):1250-5. [PubMed
]
- Hellal-Levy C, Fagart J, Souque A, Wurtz JM, Moras D, Rafestin-Oblin ME: Crucial role of the H11-H12 loop in stabilizing the active conformation of the human mineralocorticoid receptor. Mol Endocrinol. 2000 Aug;14(8):1210-21. [PubMed
]
- Odermatt A, Arnold P, Frey FJ: The intracellular localization of the mineralocorticoid receptor is regulated by 11beta-hydroxysteroid dehydrogenase type 2. J Biol Chem. 2001 Jul 27;276(30):28484-92. Epub 2001 May 11. [PubMed
]
- Halushka MK, Fan JB, Bentley K, Hsie L, Shen N, Weder A, Cooper R, Lipshutz R, Chakravarti A: Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis. Nat Genet. 1999 Jul;22(3):239-47. [PubMed
]
- Tajima T, Kitagawa H, Yokoya S, Tachibana K, Adachi M, Nakae J, Suwa S, Katoh S, Fujieda K: A novel missense mutation of mineralocorticoid receptor gene in one Japanese family with a renal form of pseudohypoaldosteronism type 1. J Clin Endocrinol Metab. 2000 Dec;85(12):4690-4. [PubMed
]
- Geller DS, Farhi A, Pinkerton N, Fradley M, Moritz M, Spitzer A, Meinke G, Tsai FT, Sigler PB, Lifton RP: Activating mineralocorticoid receptor mutation in hypertension exacerbated by pregnancy. Science. 2000 Jul 7;289(5476):119-23. [PubMed
]
- Arai K, Nakagomi Y, Iketani M, Shimura Y, Amemiya S, Ohyama K, Shibasaki T: Functional polymorphisms in the mineralocorticoid receptor and amirolide-sensitive sodium channel genes in a patient with sporadic pseudohypoaldosteronism. Hum Genet. 2003 Jan;112(1):91-7. Epub 2002 Oct 25. [PubMed
]
|
| Enzyme 12 Metabolite References |
- White WB: Drospirenone with 17beta-estradiol in the postmenopausal woman with hypertension. Climacteric. 2007 Feb;10 Suppl 1:25-31. [PubMed
]
|
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
8258 |
| Enzyme 13 Name |
ADM precursor [Contains: Adrenomedullin |
| Enzyme 13 Synonyms |
- AM
- Proadrenomedullin N-20 terminal peptide
- ProAM-N20
- ProAM N-terminal 20 peptide
- PAMP]
|
| Enzyme 13 Gene Name |
ADM |
| Enzyme 13 Protein Sequence |
>ADM precursor [Contains: Adrenomedullin
MKLVSVALMYLGSLAFLGADTARLDVASEFRKKWNKWALSRGKRELRMSSSYPTGLADVK
AGPAQTLIRPQDMKGASRSPEDSSPDAARIRVKRYRQSMNNFQGLRSFGCRFGTCTVQKL
AHQIYQFTDKDKDNVAPRSKISPQGYGRRRRRSLPEAGPGRTLVSSKPQAHGAPAPPSGS
APHFL
|
| Enzyme 13 Number of Residues |
185 |
| Enzyme 13 Molecular Weight |
20421 |
| Enzyme 13 Theoretical pI |
11.45 |
| Enzyme 13 GO Classification |
| Function |
- hormone activity
- receptor binding
- signal transducer activity
|
| Process |
| — |
| Component |
|
|
| Enzyme 13 General Function |
Not Available |
| Enzyme 13 Specific Function |
AM and PAMP are potent hypotensive and vasodilatator agents. Numerous actions have been reported most related to the physiologic control of fluid and electrolyte homeostasis. In the kidney, am is diuretic and natriuretic, and both am and pamp inhibit aldosterone secretion by direct adrenal actions. In pituitary gland, both peptides at physiologically relevant doses inhibit basal ACTH secretion. Both peptides appear to act in brain and pituitary gland to facilitate the loss of plasma volume, actions which complement their hypotensive effects in blood vessels |
| Enzyme 13 Pathways |
Not Available |
| Enzyme 13 Reactions |
Not Available |
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
Not Available |
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
500612  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
P35318  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
ADML_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>558 bp
ATGAAGCTGGTTTCCGTCGCCCTGATGTACCTGGGTTCGCTCGCCTTCCTAGGCGCTGAC
ACCGCTCGGTTGGATGTCGCGTCGGAGTTTCGAAAGAAGTGGAATAAGTGGGCTCTGAGT
CGTGGGAAGAGGGAACTGCGGATGTCCAGCAGCTACCCCACCGGGCTCGCTGACGTGAAG
GCCGGGCCTGCCCAGACCCTTATTCGGCCCCAGGACATGAAGGGTGCCTCTCGAAGCCCC
GAAGACAGCAGTCCGGATGCCGCCCGCATCCGAGTCAAGCGCTACCGCCAGAGCATGAAC
AACTTCCAGGGCCTCCGGAGCTTTGGCTGCCGCTTCGGGACGTGCACGGTGCAGAAGCTG
GCACACCAGATCTACCAGTTCACAGATAAGGACAAGGACAACGTCGCCCCCAGGAGCAAG
ATCAGCCCCCAGGGCTACGGCCGCCGGCGCCGGCGCTCCCTGCCCGAGGCCGGCCCGGGT
CGGACTCTGGTGTCTTCTAAGCCACAAGCACACGGGGCTCCAGCCCCCCCGAGTGGAAGT
GCTCCCCACTTTCTTTAG
|
| Enzyme 13 GenBank Gene ID |
D14874  |
| Enzyme 13 GeneCard ID |
ADM  |
| Enzyme 13 GenAtlas ID |
ADM  |
| Enzyme 13 HGNC ID |
HGNC:259  |
| Enzyme 13 Chromosome Location |
11 |
| Enzyme 13 Locus |
11p15.4 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- Kitamura K, Sakata J, Kangawa K, Kojima M, Matsuo H, Eto T: Cloning and characterization of cDNA encoding a precursor for human adrenomedullin. Biochem Biophys Res Commun. 1993 Jul 30;194(2):720-5. [PubMed
]
- Ishimitsu T, Kojima M, Kangawa K, Hino J, Matsuoka H, Kitamura K, Eto T, Matsuo H: Genomic structure of human adrenomedullin gene. Biochem Biophys Res Commun. 1994 Aug 30;203(1):631-9. [PubMed
]
- Kitamura K, Kangawa K, Kawamoto M, Ichiki Y, Nakamura S, Matsuo H, Eto T: Adrenomedullin: a novel hypotensive peptide isolated from human pheochromocytoma. Biochem Biophys Res Commun. 1993 Apr 30;192(2):553-60. [PubMed
]
- Samson WK: Proadrenomedullin-derived peptides. Front Neuroendocrinol. 1998 Apr;19(2):100-27. [PubMed
]
- Champion HC, Nussdorfer GG, Kadowitz PJ: Structure-activity relationships of adrenomedullin in the circulation and adrenal gland. Regul Pept. 1999 Nov 30;85(1):1-8. [PubMed
]
|
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
8295 |
| Enzyme 14 Name |
Prostaglandin E2 receptor, EP4 subtype |
| Enzyme 14 Synonyms |
- Prostanoid EP4 receptor
- PGE receptor, EP4 subtype
|
| Enzyme 14 Gene Name |
PTGER4 |
| Enzyme 14 Protein Sequence |
>Prostaglandin E2 receptor, EP4 subtype
MSTPGVNSSASLSPDRLNSPVTIPAVMFIFGVVGNLVAIVVLCKSRKEQKETTFYTLVCG
LAVTDLLGTLLVSPVTIATYMKGQWPGGQPLCEYSTFILLFFSLSGLSIICAMSVERYLA
INHAYFYSHYVDKRLAGLTLFAVYASNVLFCALPNMGLGSSRLQYPDTWCFIDWTTNVTA
HAAYSYMYAGFSSFLILATVLCNVLVCGALLRMHRQFMRRTSLGTEQHHAAAAASVASRG
HPAASPALPRLSDFRRRRSFRRIAGAEIQMVILLIATSLVVLICSIPLVVRVFVNQLYQP
SLEREVSKNPDLQAIRIASVNPILDPWIYILLRKTVLSKAIEKIKCLFCRIGGSRRERSG
QHCSDSQRTSSAMSGHSRSFISRELKEISSTSQTLLPDLSLPDLSENGLGGRNLLPGVPG
MGLAQEDTTSLRTLRISETSDSSQGQDSESVLLVDEAGGSGRAGPAPKGSSLQVTFPSET
LNLSEKCI
|
| Enzyme 14 Number of Residues |
488 |
| Enzyme 14 Molecular Weight |
53120 |
| Enzyme 14 Theoretical pI |
8.91 |
| Enzyme 14 GO Classification |
| Function |
- G-protein coupled receptor activity
- icosanoid receptor activity
- prostaglandin E receptor activity
- prostaglandin receptor activity
- prostanoid receptor activity
- receptor activity
- rhodopsin-like receptor activity
- signal transducer activity
- transmembrane receptor activity
|
| Process |
- G-protein coupled receptor protein signaling pathway
- cell communication
- cell surface receptor linked signal transduction
- cellular process
- signal transduction
|
| Component |
- cell
- integral to membrane
- intrinsic to membrane
- membrane
|
|
| Enzyme 14 General Function |
Not Available |
| Enzyme 14 Specific Function |
Receptor for prostaglandin E2 (PGE2). The activity of this receptor is mediated by G(s) proteins that stimulate adenylate cyclase. Has a relaxing effect on smooth muscle. May play an important role in regulating renal hemodynamics, intestinal epithelial transport, adrenal aldosterone secretion, and uterine function |
| Enzyme 14 Pathways |
Not Available |
| Enzyme 14 Reactions |
Not Available |
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
Not Available |
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
452496  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
P35408  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
PE2R4_HUMAN  |
| Enzyme 14 PDB ID |
Not Available |
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>1467 bp
ATGTCCACTCCCGGGGTCAATTCGTCCGCCTCCTTGAGCCCCGACCGGCTGAACAGCCCA
GTGACCATCCCGGCGGTGATGTTCATCTTCGGGGTGGTGGGCAACCTGGTGGCCATCGTG
GTGCTGTGCAAGTCGCGCAAGGAGCAGAAGGAGACGACCTTCTACACGCTGGTATGTGGG
CTGGCTGTCACCGACCTGTTGGGCACTTTGTTGGTGAGCCCGGTGACCATCGCCACGTAC
ATGAAGGGCCAATGGCCCGGGGGCCAGCCGCTGTGCGAGTACAGCACCTTCATTCTGCTC
TTCTTCAGCCTGTCCGGCCTCAGCATCATCTGCGCCATGAGTGTCGAGCGCTACCTGGCC
ATCAACCATGCCTATTTCTACAGCCACTACGTGGACAAGCGATTGGCGGGCCTCACGCTC
TTTGCAGTCTATGCGTCCAACGTGCTCTTTTGCGCGCTGCCCAACATGGGTCTCGGTAGC
TCGCGGCTGCAGTACCCAGACACCTGGTGCTTCATCGACTGGACCACCAACGTGACGGCG
CACGCCGCCTACTCCTACATGTACGCGGGCTTCAGCTCCTTCCTCATTCTCGCCACCGTC
CTCTGCAACGTGCTTGTGTGCGGCGCGCTGCTCCGCATGCACCGCCAGTTCATGCGCCGC
ACCTCGCTGGGCACCGAGCAGCACCACGCGGCCGCGGCCGCCTCGGTTGCCTCCCGGGGC
CACCCCGCTGCCTCCCCAGCCTTGCCGCGCCTCAGCGACTTTCGGCGCCGCCGGAGCTTC
CGCCGCATCGCGGGCGCCGAGATCCAGATGGTCATCTTACTCATTGCCACCTCCCTGGTG
GTGCTCATCTGCTCCATCCCGCTCGTGGTGCGAGTATTCGTCAACCAGTTATATCAGCCA
AGTTTGGAGCGAGAAGTCAGTAAAAATCCAGATTTGCAGGCCATCCGAATTGCTTCTGTG
AACCCCATCCTAGACCCCTGGATATATATCCTCCTGAGAAAGACAGTGCTCAGTAAAGCA
ATAGAGAAGATCAAATGCCTCTTCTGCCGCATTGGCGGGTCCCGCAGGGAGCGCTCCGGA
CAGCACTGCTCAGACAGTCAAAGGACATCTTCTGCCATGTCAGGCCACTCTCGCTCCTTC
ATCTCCCGGGAGCTGAAGGAGATCAGCAGTACATCTCAGACCCTCCTGCCAGACCTCTCA
CTGCCAGACCTCAGTGAAAATGGCCTTGGAGGCAGGAATTTGCTTCCAGGTGTGCCTGGC
ATGGGCCTGGCCCAGGAAGACACCACCTCACTGAGGACTTTGCGAATATCAGAGACCTCA
GACTCTTCACAGGGTCAGGACTCAGAGAGTGTCTTACTGGTGGATGAGGCTGGTGGGAGC
GGCAGGGCTGGGCCTGCCCCTAAGGGGAGCTCCCTGCAAGTCACATTTCCCAGTGAAACA
CTGAACTTATCAGAAAAATGTATATAA
|
| Enzyme 14 GenBank Gene ID |
L28175  |
| Enzyme 14 GeneCard ID |
PTGER4  |
| Enzyme 14 GenAtlas ID |
PTGER4  |
| Enzyme 14 HGNC ID |
HGNC:9596  |
| Enzyme 14 Chromosome Location |
5 |
| Enzyme 14 Locus |
5p13.1 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- Bastien L, Sawyer N, Grygorczyk R, Metters KM, Adam M: Cloning, functional expression, and characterization of the human prostaglandin E2 receptor EP2 subtype. J Biol Chem. 1994 Apr 22;269(16):11873-7. [PubMed
]
- An S, Yang J, Xia M, Goetzl EJ: Cloning and expression of the EP2 subtype of human receptors for prostaglandin E2. Biochem Biophys Res Commun. 1993 Nov 30;197(1):263-70. [PubMed
]
- Foord SM, Marks B, Stolz M, Bufflier E, Fraser NJ, Lee MG: The structure of the prostaglandin EP4 receptor gene and related pseudogenes. Genomics. 1996 Jul 1;35(1):182-8. [PubMed
]
- Mori K, Tanaka I, Kotani M, Miyaoka F, Sando T, Muro S, Sasaki Y, Nakagawa O, Ogawa Y, Usui T, Ozaki S, Ichikawa A, Narumiya S, Nakao K: Gene expression of the human prostaglandin E receptor EP4 subtype: differential regulation in monocytoid and lymphoid lineage cells by phorbol ester. J Mol Med. 1996 Jun;74(6):333-6. [PubMed
]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
14192 |
| Enzyme 15 Name |
Melanophilin |
| Enzyme 15 Synonyms |
- Exophilin-3
- Synaptotagmin-like protein 2a
- Slp homolog lacking C2 domains a
- SlaC2-a
|
| Enzyme 15 Gene Name |
MLPH |
| Enzyme 15 Protein Sequence |
>Melanophilin
MGKKLDLSKLTDEEAQHVLEVVQRDFDLRRKEEERLEALKGKIKKESSKRELLSDTAHLN
ETHCARCLQPYQLLVNSKRQCLECGLFTCKSCGRVHPEEQGWICDPCHLARVVKIGSLEW
YYEHVKARFKRFGSAKVIRSLHGRLQGGAGPELISEERSGDSDQTDEDGEPGSEAQAQAQ
PFGSKKKRLLSVHDFDFEGDSDDSTQPQGHSLHLSSVPEARDSPQSLTDESCSEKAAPHK
AEGLEEADTGASGCHSHPEEQPTSISPSRHGALAELCPPGGSHRMALGTAAALGSNVIRN
EQLPLQYLADVDTSDEESIRAHVMASHHSKRRGRASSESQIFELNKHISAVECLLTYLEN
TVVPPLAKGLGAGVRTEADVEEEALRRKLEELTSNVSDQETSSEEEEAKDEKAEPNRDKS
VGPLPQADPEVGTAAHQTNRQEKSPQDPGDPVQYNRTTDEELSELEDRVAVTASEVQQAE
SEVSDIESRIAALRAAGLTVKPSGKPRRKSNLPIFLPRVAGKLGKRPEDPNADPSSEAKA
MAVPYLLRRKFSNSLKSQGKDDDSFDRKSVYRGSLTQRNPNARKGMASHTFAKPVVAHQS
|
| Enzyme 15 Number of Residues |
600 |
| Enzyme 15 Molecular Weight |
65950 |
| Enzyme 15 Theoretical pI |
5.98 |
| Enzyme 15 GO Classification |
| Function |
- GTPase binding
- Rab GTPase binding
- binding
- enzyme binding
- protein binding
- small GTPase binding
|
| Process |
- cellular physiological process
- intracellular protein transport
- physiological process
- protein transport
- transport
|
| Component |
| — |
|
| Enzyme 15 General Function |
Not Available |
| Enzyme 15 Specific Function |
Rab effector protein involved in melanosome transport. Serves as link between melanosome-bound RAB27A and the motor protein MYO5A |
| Enzyme 15 Pathways |
Not Available |
| Enzyme 15 Reactions |
Not Available |
| Enzyme 15 Pfam Domain Function |
Not Available |
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
10433552  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
Q9BV36  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
MELPH_HUMAN  |
| Enzyme 15 PDB ID |
Not Available |
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>1719 bp
ATGGGGAAGAAACTGGATCTTTCCAAGCTCACTGATGAAGAGGCCCAGCATGTCTTGGAA
GTTGTTCAACGAGATTTTGACCTCCGAAGGAAAGAAGAGGAACGGCTAGAGGCGTTGAAG
GGCAAGATTAAGAAGGAAAGCTCCAAGAGGGAGCTGCTTTCCGACACTGCCCATCTGAAC
GAGACCCACTGCGCCCGCTGCCTGCAGCCCTACCAGCTGCTTGTGAATAGCAAAAGGCAG
TGCCTGGAATGTGGCCTCTTCACCTGCAAAAGCTGTGGCCGCGTCCACCCGGAGGAGCAG
GGCTGGATCTGTGACCCCTGCCATCCGGCCAGAGTCGTGAAGATCGGCTCACTGGAGTGG
TACTATGAGCATGTGAAAGCCCGCTTCAAGAGGTTCGGAAGTGCCAAGGTCATCCGGTCC
CTCCACGGGCGGCTGCAGGGTGGAGCTGGGCCTGAACTGATATCTGAAGAGAGAAGTGGA
GACAGCGACCAGACAGATGAGGATGGAGAACCTGGCTCAGAGGCCCAGGCCCAGGCCCAG
CCCTTTGGCAGCAAAAAAAAGCGCCTCCTCTCCGTCCACGACTTCGACTTCGAGGGAGAC
TCAGATGACTCCACTCAGCCTCAAGGTCACTCCCTGCACCTGTCCTCAGTCCCTGAGGCC
AGGGACAGCCCACAGTCCCTTACAGATGAGTCCTGCTCAGAGAAGGCAGCCCCTCACAAG
GCTGAGGGCCTGGAGGAGGCTGATACTGGGGCCTCTGGGTGCCACTCCCATCCGGAAGAG
CAGCCGACCAGCATCTCACCTTCCAGACACGGCGCCCTGGCTGAGCTCTGCCCGCCTGGA
GGCTCCCACAGGATGGCCCTGGGGACTGCTGCTGCACTCGGGTCGAATGTCATCAGGAAT
GAGCAGCTGCCCCTGCAGTACTTGGCCGATGTGGACACCTCTGATGAGGAAAGCATCCGG
GCTCACGTGATGGCCTCCCACCATTCCAAGCGGAGAGGCCGGGCGTCTTCTGAGAGTCAG
GGTCTAGGTGCTGGAGCGCGCACGGAGGCCGACGTAGAGGAGGAGGCCCTGAGGAGGAAG
CTGGAGGAGCTGACCAGCAACGTCAGTGACCAGGAGACCTCGTCCGAGGAGGAGGAGGCC
AAGGACGAAAAGGCAGAGCCCAACAGGGACAAATCAGTTGGGCCTCTCCCCCAGGCGGAC
CCGGAGGTGGGCACGGCTGCCCATCAAACCAACAGACAGGAAAAAAGCCCCCAGGACCCT
GGGGACCCCGTCCAGTACAACAGGACCACAGATGAGGAGCTGTCAGAGCTGGAGGACAGA
GTGGCAGTGACGGCCTCAGAAGTCCAGCAGGCAGAGAGCGAGGTTTCAGACATTGAATCC
AGGATTGCAGCCCTGAGGGCCGCAGGGCTCACGGTGAAGCCCTCGGGAAAGCCCCGGAGG
AAGTCAAACCTCCCGATATTTCTCCCTCGAGTGGCTGGGAAACTTGGCAAGAGACCAGAG
GACCCAAATGCAGACCCTTCAAGTGAGGCCAAGGCAATGGCTGTGCCCTATCTTCTGAGA
AGAAAGTTCAGTAATTCCCTGAAAAGTCAAGGTAAAGATGATGATTCTTTTGATCGGAAA
TCAGTGTACCGAGGCTCGCTGACACGGAGAAACCCCAACGCGAGGAAAGGAATGGCCAGC
CACACCTTCGCGAAACCTGTGGTGGCCCACCAGTCCTAA
|
| Enzyme 15 GenBank Gene ID |
AK022207  |
| Enzyme 15 GeneCard ID |
Q9BV36  |
| Enzyme 15 GenAtlas ID |
MLPH  |
| Enzyme 15 HGNC ID |
HGNC:29643  |
| Enzyme 15 Chromosome Location |
Not Available |
| Enzyme 15 Locus |
Not Available |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- Nagashima K, Torii S, Yi Z, Igarashi M, Okamoto K, Takeuchi T, Izumi T: Melanophilin directly links Rab27a and myosin Va through its distinct coiled-coil regions. FEBS Lett. 2002 Apr 24;517(1-3):233-8. [PubMed
]
|
| Enzyme 15 Metabolite References |
- Martel JA, Michael D, Fejes-Toth G, Naray-Fejes-Toth A: Melanophilin, a novel aldosterone-induced gene in mouse cortical collecting duct cells. Am J Physiol Renal Physiol. 2007 Sep;293(3):F904-13. Epub 2007 Jul 3. [PubMed
]
|
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
16423 |
| Enzyme 16 Name |
Mitochondrial cytochrome P450, family 11, subfamily B, polypeptide 2 (Cytochrome P450, family 11, subfamily B, polypeptide 2) |
| Enzyme 16 Synonyms |
Not Available |
| Enzyme 16 Gene Name |
CYP11B2 |
| Enzyme 16 Protein Sequence |
>Mitochondrial cytochrome P450, family 11, subfamily B, polypeptide 2 (Cytochrome P450, family 11, subfamily B, polypeptide 2)
MALRAKAEVCVAAPWLSLQRARALGTRAARAPRTVLPFEAMPQHPGNRWLRLLQIWREQG
YEHLHLEMHQTFQELGPIFRYNLGGPRMVCVMLPEDVEKLQQVDSLHPCRMILEPWVAYR
QHRGHKCGVFLLNGPEWRFNRLRLNPDVLSPKAVQRFLPMVDAVARDFSQALKKKVLQNA
RGSLTLDVQPSIFHYTIEASNLALFGERLGLVGHSPSSASLNFLHALEVMFKSTVQLMFM
PRSLSRWISPKVWKEHFEAWDCIFQYGDNCIQKIYQELAFNRPQHYTGIVAELLLKAELS
LEAIKANSMELTAGSVDTTAFPLLMTLFELARNPDVQQILRQESLAAAASISEHPQKATT
ELPLLRAALKETLRLYPVGLFLERVVSSDLVLQNYHIPAGTLVQVFLYSLGRNAALFPRP
ERYNPQRWLDIRGSGRNFHHVPFGFGMRQCLGRRLAEAEMLLLLHHVLKHFLVETLTQED
IKMVYSFILRPGTSPLLTFRAIN
|
| Enzyme 16 Number of Residues |
503 |
| Enzyme 16 Molecular Weight |
57561 |
| Enzyme 16 Theoretical pI |
9.78 |
| Enzyme 16 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- oxidoreductase activity
- tetrapyrrole binding
- transition metal ion binding
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 16 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 16 Specific Function |
Not Available |
| Enzyme 16 Pathways |
Not Available |
| Enzyme 16 Reactions |
Not Available |
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
Not Available |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
B0ZBE4  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
B0ZBE4_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
Not Available |
| Enzyme 16 GenBank Gene ID |
EU326306  |
| Enzyme 16 GeneCard ID |
B0ZBE4  |
| Enzyme 16 GenAtlas ID |
Not Available |
| Enzyme 16 HGNC ID |
Not Available |
| Enzyme 16 Chromosome Location |
Not Available |
| Enzyme 16 Locus |
Not Available |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
Not Available |
| Enzyme 16 Metabolite References |
Not Available |