|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5442 |
| Enzyme 1 Name |
Glucokinase |
| Enzyme 1 Synonyms |
- Hexokinase-4
- Hexokinase type IV
- HK IV
- HK4
- Hexokinase-D
|
| Enzyme 1 Gene Name |
GCK |
| Enzyme 1 Protein Sequence |
>Glucokinase
MLDDRARMEAAKKEKVEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPT
YVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEEGQWSVKTKHQMYSIPEDAMTGTAE
MLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNN
VVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQN
VELVEGDEGRMCVNTEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGE
LVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESDTGDRKQIYNILSTLGLRPS
TTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFK
ERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACKKACMLGQ
|
| Enzyme 1 Number of Residues |
465 |
| Enzyme 1 Molecular Weight |
52192 |
| Enzyme 1 Theoretical pI |
4.85 |
| Enzyme 1 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- hexokinase activity
- nucleotide binding
- phosphotransferase activity, alcohol group as acceptor
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolism
- cellular metabolism
- glucose catabolism
- glucose metabolism
- glycolysis
- hexose metabolism
- metabolism
- monosaccharide metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 1 General Function |
Not Available |
| Enzyme 1 Specific Function |
Catalyzes the initial step in utilization of glucose by the beta-cell and liver at physiological glucose concentration. Glucokinase has a high Km for glucose, and so it is effective only when glucose is abundant. The role of GCK is to provide G6P for the synthesis of glycogen. Pancreatic glucokinase plays an important role in modulating insulin secretion. Hepatic glucokinase helps to facilitate the uptake and conversion of glucose by acting as an insulin-sensitive determinant of hepatic glucose usage |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- ATP + D-glucose = ADP + D-glucose 6-phosphate
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
179427  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P35557  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
HXK4_HUMAN  |
| Enzyme 1 PDB ID |
1V4T  |
| Enzyme 1 PDB File |
Show |
| Enzyme 1 3D Structure |
|
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1398 bp
ATGCTGGACGACAGAGCCAGGATGGAGGCCGCCAAGAAGGAGAAGGTAGAGCAGATCCTG
GCAGAGTTCCAGCTGCAGGAGGAGGACCTGAAGAAGGTGATGAGACGGATGCAGAAGGAG
ATGGACCGCGGCCTGAGGCTGGAGACCCATGAAGAGGCCAGTGTGAAGATGCTGCCCACC
TACGTGCGCTCCACCCCAGAAGGCTCAGAAGTCGGGGACTTCCTCTCCCTGGACCTGGGT
GGCACTAACTTCAGGGTGATGCTGGTGAAGGTGGGAGAAGGTGAGGAGGGGCAGTGGAGC
GTGAAGACCAAACACCAGATGTACTCCATCCCCGAGGACGCCATGACCGGCACTGCTGAG
ATGCTCTTCGACTACATCTCTGAGTGCATCTCCGACTTCCTGGACAAGCATCAGATGAAA
CACAAGAAGCTGCCCCTGGGCTTCACCTTCTCCTTTCCTGTGAGGCACGAAGACATCGAT
AAGGGCATCCTTCTCAACTGGACCAAGGGCTTCAAGGCCTCAGGAGCAGAAGGGAACAAT
GTCGTGGGGCTTCTGCGAGACGCTATCAAACGGAGAGGGGACTTTGAAATGGATGTGGTG
GCAATGGTGAATGACACGGTGGCCACGATGATCTCCTGCTACTACGAAGACCATCAGTGC
GAGGTCGGCATGATCGTGGGCACGGGCTGCAATGCCTGCTACATGGAGGAGATGCAGAAT
GTGGAGCTGGTGGAGGGGGACGAGGGCCGCATGTGCGTCAATACCGAGTGGGGCGCCTTC
GGGGACTCCGGCGAGCTGGACGAGTTCCTGCTGGAGTATGACCGCCTGGTGGACGAGAGC
TCTGCAAACCCCGGTCAGCAGCTGTATGAGAAGCTCATAGGTGGCAAGTACATGGGCGAG
CTGGTGCGGCTTGTGCTGCTCAGGCTCGTGGACGAAAACCTGCTCTTCCACGGGGAGGCC
TCCGAGCAGCTGCGCACACGCGGAGCCTTCGAGACGCGCTTCGTGTCGCAGGTGGAGAGC
GACACGGGCGACCGCAAGCAGATCTACAACATCCTGAGCACGCTGGGGCTGCGACCCTCG
ACCACCGACTGCGACATCGTGCGCCGCGCCTGCGAGAGCGTGTCTACGCGCGCTGCGCAC
ATGTGCTCGGCGGGGCTGGCGGGCGTCATCAACCGCATGCGCGAGAGCCGCAGCGAGGAC
GTAATGCGCATCACTGTGGGCGTGGATGGCTCCGTGTACAAGCTGCACCCCAGCTTCAAG
GAGCGGTTCCATGCCAGCGTGCGCAGGCTGACGCCCAGCTGCGAGATCACCTTCATCGAG
TCGGAGGAGGGCAGTGGCCGGGGCGCGGCCCTGGTCTCGGCGGTGGCCTGTAAGAAGGCC
TGTATGCTGGGCCAGTGA
|
| Enzyme 1 GenBank Gene ID |
M88011  |
| Enzyme 1 GeneCard ID |
GCK  |
| Enzyme 1 GenAtlas ID |
GCK  |
| Enzyme 1 HGNC ID |
HGNC:4195  |
| Enzyme 1 Chromosome Location |
7 |
| Enzyme 1 Locus |
7p15.3-p15.1 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Tanizawa Y, Matsutani A, Chiu KC, Permutt MA: Human glucokinase gene: isolation, structural characterization, and identification of a microsatellite repeat polymorphism. Mol Endocrinol. 1992 Jul;6(7):1070-81. [PubMed
]
- Tanizawa Y, Koranyi LI, Welling CM, Permutt MA: Human liver glucokinase gene: cloning and sequence determination of two alternatively spliced cDNAs. Proc Natl Acad Sci U S A. 1991 Aug 15;88(16):7294-7. [PubMed
]
- Nishi S, Stoffel M, Xiang K, Shows TB, Bell GI, Takeda J: Human pancreatic beta-cell glucokinase: cDNA sequence and localization of the polymorphic gene to chromosome 7, band p 13. Diabetologia. 1992 Aug;35(8):743-7. [PubMed
]
- Koranyi LI, Tanizawa Y, Welling CM, Rabin DU, Permutt MA: Human islet glucokinase gene. Isolation and sequence analysis of full-length cDNA. Diabetes. 1992 Jul;41(7):807-11. [PubMed
]
- Stoffel M, Froguel P, Takeda J, Zouali H, Vionnet N, Nishi S, Weber IT, Harrison RW, Pilkis SJ, Lesage S, et al.: Human glucokinase gene: isolation, characterization, and identification of two missense mutations linked to early-onset non-insulin-dependent (type 2) diabetes mellitus. Proc Natl Acad Sci U S A. 1992 Aug 15;89(16):7698-702. [PubMed
]
- Sakura H, Eto K, Kadowaki H, Simokawa K, Ueno H, Koda N, Fukushima Y, Akanuma Y, Yazaki Y, Kadowaki T: Structure of the human glucokinase gene and identification of a missense mutation in a Japanese patient with early-onset non-insulin-dependent diabetes mellitus. J Clin Endocrinol Metab. 1992 Dec;75(6):1571-3. [PubMed
]
- St Charles R, Harrison RW, Bell GI, Pilkis SJ, Weber IT: Molecular model of human beta-cell glucokinase built by analogy to the crystal structure of yeast hexokinase B. Diabetes. 1994 Jun;43(6):784-91. [PubMed
]
- Stoffel M, Patel P, Lo YM, Hattersley AT, Lucassen AM, Page R, Bell JI, Bell GI, Turner RC, Wainscoat JS: Missense glucokinase mutation in maturity-onset diabetes of the young and mutation screening in late-onset diabetes. Nat Genet. 1992 Oct;2(2):153-6. [PubMed
]
- Chiu KC, Tanizawa Y, Permutt MA: Glucokinase gene variants in the common form of NIDDM. Diabetes. 1993 Apr;42(4):579-82. [PubMed
]
- Stoffel M, Bell KL, Blackburn CL, Powell KL, Seo TS, Takeda J, Vionnet N, Xiang KS, Gidh-Jain M, Pilkis SJ, et al.: Identification of glucokinase mutations in subjects with gestational diabetes mellitus. Diabetes. 1993 Jun;42(6):937-40. [PubMed
]
- Takeda J, Gidh-Jain M, Xu LZ, Froguel P, Velho G, Vaxillaire M, Cohen D, Shimada F, Makino H, Nishi S, et al.: Structure/function studies of human beta-cell glucokinase. Enzymatic properties of a sequence polymorphism, mutations associated with diabetes, and other site-directed mutants. J Biol Chem. 1993 Jul 15;268(20):15200-4. [PubMed
]
- Gidh-Jain M, Takeda J, Xu LZ, Lange AJ, Vionnet N, Stoffel M, Froguel P, Velho G, Sun F, Cohen D, et al.: Glucokinase mutations associated with non-insulin-dependent (type 2) diabetes mellitus have decreased enzymatic activity: implications for structure/function relationships. Proc Natl Acad Sci U S A. 1993 Mar 1;90(5):1932-6. [PubMed
]
- Hager J, Blanche H, Sun F, Vaxillaire NV, Poller W, Cohen D, Czernichow P, Velho G, Robert JJ, Cohen N, et al.: Six mutations in the glucokinase gene identified in MODY by using a nonradioactive sensitive screening technique. Diabetes. 1994 May;43(5):730-3. [PubMed
]
- Velho G, Blanche H, Vaxillaire M, Bellanne-Chantelot C, Pardini VC, Timsit J, Passa P, Deschamps I, Robert JJ, Weber IT, Marotta D, Pilkis SJ, Lipkind GM, Bell GI, Froguel P: Identification of 14 new glucokinase mutations and description of the clinical profile of 42 MODY-2 families. Diabetologia. 1997 Feb;40(2):217-24. [PubMed
]
- Hattersley AT, Beards F, Ballantyne E, Appleton M, Harvey R, Ellard S: Mutations in the glucokinase gene of the fetus result in reduced birth weight. Nat Genet. 1998 Jul;19(3):268-70. [PubMed
]
- Glaser B, Kesavan P, Heyman M, Davis E, Cuesta A, Buchs A, Stanley CA, Thornton PS, Permutt MA, Matschinsky FM, Herold KC: Familial hyperinsulinism caused by an activating glucokinase mutation. N Engl J Med. 1998 Jan 22;338(4):226-30. [PubMed
]
- Ng MC, Cockburn BN, Lindner TH, Yeung VT, Chow CC, So WY, Li JK, Lo YM, Lee ZS, Cockram CS, Critchley JA, Bell GI, Chan JC: Molecular genetics of diabetes mellitus in Chinese subjects: identification of mutations in glucokinase and hepatocyte nuclear factor-1alpha genes in patients with early-onset type 2 diabetes mellitus/MODY. Diabet Med. 1999 Nov;16(11):956-63. [PubMed
]
- Nam JH, Lee HC, Kim YH, Cha BS, Song YD, Lim SK, Kim KR, Huh KB: Identification of glucokinase mutation in subjects with post-renal transplantation diabetes mellitus. Diabetes Res Clin Pract. 2000 Dec;50(3):169-76. [PubMed
]
- Njolstad PR, Sovik O, Cuesta-Munoz A, Bjorkhaug L, Massa O, Barbetti F, Undlien DE, Shiota C, Magnuson MA, Molven A, Matschinsky FM, Bell GI: Neonatal diabetes mellitus due to complete glucokinase deficiency. N Engl J Med. 2001 May 24;344(21):1588-92. [PubMed
]
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| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5444 |
| Enzyme 2 Name |
Hexokinase-3 |
| Enzyme 2 Synonyms |
- Hexokinase type III
- HK III
|
| Enzyme 2 Gene Name |
HK3 |
| Enzyme 2 Protein Sequence |
>Hexokinase-3
MDSIGSSGLRQGEETLSCSEEGLPGPSDSSELVQECLQQFKVTRAQLQQIQASLLGSMEQ
ALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGATGASLRVLWVTLTGIEGHRVEP
RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRST
LISWTKGFRCSGVEGQDVVQLLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVG
LVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSLSDDGALGPVLTTFDHTLDHESLN
PGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEMEDPST
GAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQ
VAVATGGRVCERHPRFCSVLQGTVMLLAPECDVSLIPSVDGGGRGVAMVTAVAARLAAHR
RLLEETLAPFRLNHDQLAAVQAQMRKAMAKGLRGEASSLRMLPTFVRATPDGSERGDFLA
LDLGGTNFRVLLVRVTTGVQITSEIYSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQ
SLPLGFTFSFPCRQLGLDQGILLNWTKGFKASDCEGQDVVSLLREAITRRQAVELNVVAI
VNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGD
DGSLAMLSTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGQQIQ
RLQTRDIFKTKFLSEIESDSLALRQVRAILEDLGLPLTSDDALMVLEVCQAVSQRAAQLC
GAGVAAVVEKIRGNRGLEELAVSVGVDGTLYKLHPRFSSLVAATVRELAPRCVVTFLQSE
DGSGKGAALVTAVACRLAQLTRV
|
| Enzyme 2 Number of Residues |
923 |
| Enzyme 2 Molecular Weight |
98921 |
| Enzyme 2 Theoretical pI |
5.11 |
| Enzyme 2 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- hexokinase activity
- nucleotide binding
- phosphotransferase activity, alcohol group as acceptor
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolism
- cellular metabolism
- glucose catabolism
- glucose metabolism
- glycolysis
- hexose metabolism
- metabolism
- monosaccharide metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 2 General Function |
Not Available |
| Enzyme 2 Specific Function |
ATP + D-hexose = ADP + D-hexose 6-phosphate |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- ATP + D-hexose = ADP + D-hexose 6-phosphate
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
1255788  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P52790  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
HXK3_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>2772 bp
ATGGACTCCATTGGGTCTTCAGGGTTGCGGCAGGGGGAAGAAACCCTGAGTTGCTCTGAG
GAGGGCTTGCCCGGGCCCTCAGACAGCTCAGAGCTGGTGCAGGAGTGCCTGCAGCAGTTC
AAGGTGACAAGGGCACAGCTACAGCAGATCCAAGCCAGCCTCTTGGGTTCCATGGAGCAG
GCGCTGAGGGGACAGGCCAGCCCTGCCCCTGCGGTCCGGATGCTGCCTACATACGTGGGG
TCCACCCCACATGGCACTGAGCAAGGAGACTTCGTGGTGCTGGAGCTGGGGGCCACAGGG
GCCTCACTGCGTGTTTTGTGGGTGACTCTAACTGGCATTGAGGGGCATAGGGTGGAGCCC
AGAAGCCAGGAGTTTGTGATCCCCCAAGAGGTGATGCTGGGTGCTGGCCAGCAGCTCTTT
GACTTTGCTGCCCACTGCCTGTCTGAGTTCCTGGATGCGCAGCCTGTGAACAAACAGGGT
CTGCAGCTTGGCTTCAGCTTCTCTTTCCCTTGTCACCAGACGGGCTTGGACAGGAGCACC
CTCATTTCCTGGACCAAAGGTTTTAGGTGCAGTGGTGTGGAAGGCCAGGATGTGGTCCAG
CTGCTGAGAGATGCCATTCGGAGGCAGGGGGCCTACAACATCGACGTGGTTGCTGTGGTG
AACGACACAGTGGGCACCATGATGGGCTGTGAGCCGGGGGTCAGGCCGTGTGAGGTTGGG
CTAGTTGTAGACACGGGCACCAACGCGTGTTACATGGAGGAGGCACGGCATGTGGCAGTG
CTGGACGAAGACCGGGGCCGCGTCTGCGTCAGCGTCGAGTGGGGCTCCTTAAGCGATGAT
GGGGCGCTGGGACCAGTGCTGACCACCTTCGACCATACCCTGGACCATGAGTCCCTGAAT
CCTGGTGCTCAGAGGTTTGAGAAGATGATCGGAGGCCTGTACCTGGGTGAGCTGGTGCGG
CTGGTGCTGGCTCACTTGGCCCGGTGTGGGGTCCTCTTTGGTGGCTGCACCTCCCCTGCC
CTGCTGAGCCAAGGCAGCATCCTCCTGGAACACGTGGCTGAGATGGAGGACCCCTCTACT
GGGGCAGCCCGTGTCCATGCTATCCTGCAGGACTTGGGCCTGAGCCCTGGGGCTTCGGAT
GTTGAGCTTGTGCAGCACGTCTGTGCGGCCGTGTGCACGCGGGCTGCCCAGCTCTGTGCT
GCCGCCCTGGCCGCTGTTCTCTCCTGCCTCCAGCACAGCCGGGAGCAACAAACACTCCAG
GTTGCTGTGGCCACCGGAGGCCGAGTGTGTGAGCGGCACCCCAGGTTCTGCAGCGTCCTG
CAGGGGACAGTGATGCTCCTGGCCCCGGAATGCGATGTCTCCTTAATCCCCTCTGTGGAT
GGTGGTGGCCGGGGAGTGGCGATGGTGACTGCTGTGGCTGCCCGTCTGGCTGCCCACCGG
CGCCTGCTGGAGGAGACCCTGGCCCCATTCCGGTTGAACCATGATCAACTGGCTGCGGTT
CAGGCACAGATGCGGAAGGCCATGGCCAAGGGGCTCCGAGGGGAGGCCTCCTCCCTTCGC
ATGCTGCCCACTTTCGTCCGGGCCACCCCTGACGGCAGCGAGCGAGGGGATTTCCTGGCC
CTGGACCTCGGGGGCACGAACTTCCGTGTCCTCCTGGTACGTGTGACCACAGGCGTGCAG
ATCACCAGCGAGATCTACTCCATTCCCGAGACTGTGGCCCAGGGTTCTGGGCAGCAGCTC
TTTGACCACATCGTGGACTGCATCGTGGACTTCCAGCAGAAGCAGGGCCTGAGCGGGCAG
AGCCTCCCACTGGGTTTTACCTTCTCCTTCCCATGTAGGCAGCTTGGCCTAGACCAGGGC
ATCCTCCTGAACTGGACCAAGGGTTTCAAGGCATCAGACTGCGAGGGCCAAGATGTCGTG
AGTCTGTTGCGGGAAGCCATCACTCGCAGACAGGCAGTGGAGCTGAATGTGGTTGCCATT
GTCAATGACACGGTGGGGACCATGATGTCCTGTGGCTATGAGGACCCCCGTTGCGAGATA
GGCCTCATTGTCGGAACCGGCACCAATGCCTGCTACATGGAGGAGCTCCGGAATGTGGCG
GGCGTGCCTGGGGACTCAGGCCGCATGTGCATCAACATGGAGTGGGGCGCCTTTGGGGAC
GATGGCTCTCTGGCCATGCTCAGCACCCGCTTTGATGCAAGTGTGGACCAGGCGTCCATC
AACCCCGGCAAGCAGAGGTTTGAAAAGATGATCAGCGGCATGTACCTGGGGGAGATCGTC
CGCCACATCCTTTTACATTTAACCAGCCTTGGCGTTCTCTTCCGGGGCCAGCAGATCCAG
CGCCTTCAGACCAGGGACATCTTCAAGACCAAGTTCCTCTCTGAGATCGAAAGTGACAGC
CTGGCCCTGCGGCAGGTCCGAGCCATCCTAGAGGATCTGGGGCTACCCCTGACCTCAGAT
GACGCCCTGATGGTGCTAGAGGTGTGCCAGGCTGTGTCCCAGAGGGCTGCCCAGCTCTGT
GGGGCGGGTGTAGCTGCCGTGGTGGAGAAGATCCGGGGGAACCGGGGCCTGGAAGAGCTG
GCAGTGTCTGTGGGGGTGGATGGAACGCTCTACAAGCTGCACCCGCGCTTCTCCAGCCTG
GTGGCGGCCACAGTGCGGGAGCTGGCCCCTCGCTGTGTGGTCACGTTCCTGCAGTCAGAG
GATGGGTCCGGCAAAGGTGCGGCCCTGGTCACCGCTGTTGCCTGCCGCCTTGCGCAGTTG
ACTCGTGTCTGA
|
| Enzyme 2 GenBank Gene ID |
U51333  |
| Enzyme 2 GeneCard ID |
HK3  |
| Enzyme 2 GenAtlas ID |
HK3  |
| Enzyme 2 HGNC ID |
HGNC:4925  |
| Enzyme 2 Chromosome Location |
5 |
| Enzyme 2 Locus |
5q35.2 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Furuta H, Nishi S, Le Beau MM, Fernald AA, Yano H, Bell GI: Sequence of human hexokinase III cDNA and assignment of the human hexokinase III gene (HK3) to chromosome band 5q35.2 by fluorescence in situ hybridization. Genomics. 1996 Aug 15;36(1):206-9. [PubMed
]
- Palma F, Agostini D, Mason P, Dacha M, Piccoli G, Biagiarelli B, Fiorani M, Stocchi V: Purification and characterization of the carboxyl-domain of human hexokinase type III expressed as fusion protein. Mol Cell Biochem. 1996 Feb 9;155(1):23-9. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5445 |
| Enzyme 3 Name |
Hexokinase-2 |
| Enzyme 3 Synonyms |
- Hexokinase type II
- HK II
- Muscle form hexokinase
|
| Enzyme 3 Gene Name |
HK2 |
| Enzyme 3 Protein Sequence |
>Hexokinase-2
MIASHLLAYFFTELNHDQVQKVDQYLYHMRLSDETLLEISKRFRKEMEKGLGATTHPTAA
VKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNGLQKVEMENQIYAIPEDIMR
GSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGV
EGRDVVALIRKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYME
EMRHIDMVEGDEGRMCINMEWGAFGDDGSLNDIRTEFDQEIDMGSLNPGKQLFEKMISGM
YMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDISDIEGEKDGIRKAREVLMRLG
LDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKH
PHFAKRLHKTVRRLVPGCDVRFLRSEDGSGKGAAMVTAVAYRLADQHRARQKTLEHLQLS
HDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRV
LLVRVRNGKWGGVEMHNKIYAIPQEVMHGTGDELFDHIVQCIADFLEYMGMKGVSLPLGF
TFSFPCQQNSLDESILLKWTKGFKASGCEGEDVVTLLKEAIHRREEFDLDVVAVVNDTVG
TMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGCLDD
FRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRG
IFETKFLSQIESDCLALLQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAA
VVDRIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHETVKDLAPKCDVSFLQSEDGSGKG
AALITAVACRIREAGQR
|
| Enzyme 3 Number of Residues |
917 |
| Enzyme 3 Molecular Weight |
102381 |
| Enzyme 3 Theoretical pI |
5.93 |
| Enzyme 3 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- hexokinase activity
- nucleotide binding
- phosphotransferase activity, alcohol group as acceptor
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolism
- cellular metabolism
- glucose catabolism
- glucose metabolism
- glycolysis
- hexose metabolism
- metabolism
- monosaccharide metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 3 General Function |
Not Available |
| Enzyme 3 Specific Function |
ATP + D-hexose = ADP + D-hexose 6-phosphate |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- ATP + D-hexose = ADP + D-hexose 6-phosphate
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
587202  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P52789  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
HXK2_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>2754 bp
ATGATTGCCTCGCATCTGCTTGCCTACTTCTTCACGGAGCTCAACCATGACCAAGTGCAG
AAGGTTGACCAGTATCTCTACCACATGCGCCTCTCTGATGAGACCCTCTTGGAGATCTCT
AAGCGGTTCCGCAAGGAGATGGAGAAAGGGCTTGGAGCCACCACTCACCCTACTGCAGCA
GTGAAGATGCTGCCCACCTTTGTGAGGTCCACTCCAGATGGGACAGAACACGGAGAGTTC
CTGGCTCTGGATCTTGGAGGGACCAACTTCCGTGTGCTTTGGGTGAAAGTAACGGACAAT
GGGCTCCAGAAGGTGGAGATGGAGAATCAGATCTATGCCATCCCTGAGGACATCATGCGA
GGCAGTGGCACCCAGCTGTTTGACCACATTGCCGAATGCCTGGCTAACTTCATGGATAAG
CTACAAATCAAAGACAAGAAGCTCCCACTGGGTTTTACCTTCTCGTTCCCCTGCCACCAG
ACTAAACTAGACGAGAGTTTCCTGGTCTCATGGACCAAGGGATTCAAGTCCAGTGGAGTG
GAAGGCAGAGACGTTGTGGCTCTGATCCGGAAGGCCATCCAGAGGAGAGGGGACTTTGAT
ATCGACATTGTGGCTGTGGTGAATGACACAGTTGGGACCATGATGACCTGTGGTTATGAT
GACCACAACTGTGAGATTGGTCTCATTGTGGGCACGGGCAGCAACGCCTGCTACATGGAA
GAGATGCGCCACATCGACATGGTGGAAGGCGATGAGGGGCGGATGTGTATCAATATGGAG
TGGGGGGCCTTCGGGGACGATGGCTCGCTCAACGACATTCGCACTGAGTTTGACCAGGAG
ATTGACATGGGCTCACTGAACCCGGGAAAGCAACTGTTTGAGAAGATGATCAGTGGGATG
TACATGGGGGAGCTGGTGAGGCTTATCCTGGTGAAGATGGCCAAGGAGGAGCTGCTCTTT
GGGGGGAAGCTCAGCCCAGAGCTTCTCAACACCGGTCGCTTTGAGACCAAAGACATCTCA
GACATTGAAGGGGAGAAGGATGGCATCCGGAAGGCCCGTGAGGTCCTGATGCGGTTGGGC
CTGGACCCGACTCAGGAGGACTGCGTGGCCACTCACCGGATCTGCCAGATCGTGTCCACA
CGCTCCGCCAGCCTGTGCGCAGCCACCCTGGCCGCCGTGCTGCAGCGCATCAAGGAGAAC
AAAGGCGAGGAGCGGCTGCGCTCTACTATTGGGGTCGACGGTTCCGTCTACAAGAAACAC
CCCCATTTTGCCAAGCGTCTACATAAGACCGTGCGGCGGCTGGTGCCCGGCTGCGATGTC
CGCTTCCTCCGCTCCGAGGATGGCAGTGGCAAAGGTGCAGCCATGGTGACAGCAGTGGCT
TACCGGCTGGCCGATCAACACCGTGCCCGCCAGAAGACATTAGAGCATCTGCAGCTGAGC
CATGACCAGCTGCTGGAGGTCAAGAGGAGGATGAAGGTAGAAATGGAGCGAGGTCTGAGC
AAGGAGACTCATGCCAGTGCCCCCGTCAAGATGCTGCCCACCTACGTGTGTGCTACCCCG
GACGGCACAGAGAAAGGGGACTTCTTGGCCTTGGACCTTGGAGGAACAAATTTCCGGGTC
CTGCTGGTCCGTGTTCGGAATGGGAAGTGGGGTGGAGTGGAGATGCACAACAAGATCTAC
GCCATCCCGCAGGAGGTCATGCACGGCACCGGGGACGAGCTCTTTGACCACATTGTCCAG
TGCATCGCGGACTTCCTCGAGTACATGGGCATGAAGGGCGTGTCCCTGCCTCTGGGTTTT
ACCTTCTCCTTCCCCTGCCAGCAGAACAGCCTGGACGAGAGCATCCTCCTCAAGTGGACA
AAAGGCTTCAAGGCATCTGGCTGCGAGGGCGAGGACGTGGTGACCCTGCTGAAGGAAGCG
ATCCACCGGCGAGAGGAGTTTGACCTGGATGTGGTTGCTGTGGTGAACGACACAGTCGGA
ACTATGATGACCTGTGGCTTTGAAGACCCTCACTGTGAAGTTGGCCTCATTGTTGGCACG
GGCAGCAATGCCTGCTACATGGAGGAGATGCGCAACGTGGAACTGGTGGAAGGAGAAGAG
GGGCGGATGTGTGTGAACATGGAATGGGGGGCCTTCGGGGACAATGGATGCCTAGATGAC
TTCCGCACAGAATTTGATGTGGCTGTGGATGAGCTTTCACTCAACCCCGGCAAGCAGAGG
TTCGAGAAAATGATCAGTGGAATGTACCTGGGTGAGATTGTCCGTAACATTCTCATCGAT
TTCACCAAGCGTGGACTACTCTTCCGAGGCCGCATCTCAGAGCGGCTCAAGACAAGGGGC
ATCTTTGAAACCAAGTTCTTGTCTCAGATTGAGAGTGACTGCCTGGCCCTGCTGCAAGTC
CGAGCCACCCTGCAACACTTAGGGCTTGAGAGCACCTGTGACGACAGCATCATTGTTAAG
GAGGTGTGCACTGTGGTGGCCCGGCGGGCAGCCCAGCTCTGTGGCGCAGGCATGGCCGCT
GTGGTGGACAGGATACGAGAAAACCGTGGGCTGGACGCTCTCAAAGTGACAGTGGGTGTG
GATGGGACCCTCTACAAGCTACATCCTCACTTTGCCAAAGTCATGCATGAGACAGTGAAG
GACCTGGCTCCGAAATGTGATGTGTCTTTCCTGCAGTCAGAGGATGGCAGCGGGAAGGGG
GCGGCGCTCATCACTGCTGTGGCCTGCCGCATCCGTGAGGCTGGACAGCGATAG
|
| Enzyme 3 GenBank Gene ID |
Z46376  |
| Enzyme 3 GeneCard ID |
HK2  |
| Enzyme 3 GenAtlas ID |
HK2  |
| Enzyme 3 HGNC ID |
HGNC:4923  |
| Enzyme 3 Chromosome Location |
2 |
| Enzyme 3 Locus |
2p13 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Lehto M, Huang X, Davis EM, Le Beau MM, Laurila E, Eriksson KF, Bell GI, Groop L: Human hexokinase II gene: exon-intron organization, mutation screening in NIDDM, and its relationship to muscle hexokinase activity. Diabetologia. 1995 Dec;38(12):1466-74. [PubMed
]
- Deeb SS, Malkki M, Laakso M: Human hexokinase II: sequence and homology to other hexokinases. Biochem Biophys Res Commun. 1993 Nov 30;197(1):68-74. [PubMed
]
- Shinohara Y, Yamamoto K, Kogure K, Ichihara J, Terada H: Steady state transcript levels of the type II hexokinase and type 1 glucose transporter in human tumor cell lines. Cancer Lett. 1994 Jul 15;82(1):27-32. [PubMed
]
- Laakso M, Malkki M, Deeb SS: Amino acid substitutions in hexokinase II among patients with NIDDM. Diabetes. 1995 Mar;44(3):330-4. [PubMed
]
- Vidal-Puig A, Printz RL, Stratton IM, Granner DK, Moller DE: Analysis of the hexokinase II gene in subjects with insulin resistance and NIDDM and detection of a Gln142-->His substitution. Diabetes. 1995 Mar;44(3):340-6. [PubMed
]
- Echwald SM, Bjorbaek C, Hansen T, Clausen JO, Vestergaard H, Zierath JR, Printz RL, Granner DK, Pedersen O: Identification of four amino acid substitutions in hexokinase II and studies of relationships to NIDDM, glucose effectiveness, and insulin sensitivity. Diabetes. 1995 Mar;44(3):347-53. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5447 |
| Enzyme 4 Name |
Hexokinase-1 |
| Enzyme 4 Synonyms |
- Hexokinase type I
- HK I
- Brain form hexokinase
|
| Enzyme 4 Gene Name |
HK1 |
| Enzyme 4 Protein Sequence |
>Hexokinase-1
MIAAQLLAYYFTELKDDQVKKIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTAT
VKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESEVYDTPENIVH
GSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGV
EGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYME
ELRHIDLVEGDEGRMCINTEWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGM
YLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGLHNAKEILTRLG
VEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTH
PQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETLAHFHLT
KDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRV
LLVKIRSGKKRTVEMHNKIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGF
TFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLLRDAIKRREEFDLDVVAVVNDTVG
TMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGCLDD
IRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRG
IFETKFLSQIESDRLALLQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAA
VVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMHQTVKELSPKCNVSFLLSEDGSGKG
AALITAVGVRLRTEASS
|
| Enzyme 4 Number of Residues |
917 |
| Enzyme 4 Molecular Weight |
102487 |
| Enzyme 4 Theoretical pI |
6.78 |
| Enzyme 4 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- hexokinase activity
- nucleotide binding
- phosphotransferase activity, alcohol group as acceptor
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolism
- cellular metabolism
- glucose catabolism
- glucose metabolism
- glycolysis
- hexose metabolism
- metabolism
- monosaccharide metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 4 General Function |
Not Available |
| Enzyme 4 Specific Function |
ATP + D-hexose = ADP + D-hexose 6-phosphate |
| Enzyme 4 Pathways |
|
| Enzyme 4 Reactions |
- ATP + D-hexose = ADP + D-hexose 6-phosphate
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
184021  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
P19367  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
HXK1_HUMAN  |
| Enzyme 4 PDB ID |
1HKB  |
| Enzyme 4 PDB File |
Show |
| Enzyme 4 3D Structure |
|
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>2754 bp
ATGATCGCCGCGCAGCTCCTGGCCTATTACTTCACGGAGCTGAAGGATGACCAGGTCAAA
AAGATTGACAAGTATCTGTATGCCATGCGGCTCTCCGATGAAACTCTCATAGATATCATG
ACTCGCTTCAGGAAGGAGATGAAGAATGGCCTCTCCCGGGATTTTAATCCAACAGCCACA
GTCAAGATGTTGCCAACATTCGTAAGGTCCATTCCTGATGGCTCTGAAAAGGGAGATTTC
ATTGCCCTGGATCTTGGTGGGTCTTCCTTTCGAATTCTGCGGGTGCAAGTGAATCATGAG
AAAAACCAGAATGTTCACATGGAGTCCGAGGTTTATGACACCCCAGAGAACATCGTGCAC
GGCAGTGGAAGCCAGCTTTTTGATCATGTTGCTGAGTGCCTGGGAGATTTCATGGAGAAA
AGGAAGATCAAGGACAAGAAGTTACCTGTGGGATTCACGTTTTCTTTTCCTTGCCAACAA
TCCAAAATAGATGAGGCCATCCTGATCACCTGGACAAAGCGATTTAAAGCGAGCGGAGTG
GAAGGAGCAGATGTGGTCAAACTGCTTAACAAAGCCATCAAAAAGCGAGGGGACTATGAT
GCCAACATCGTAGCTGTGGTGAATGACACAGTGGGCACCATGATGACCTGTGGCTATGAC
GACCAGCACTGTGAAGTCGGCCTGATCATCGGCACTGGCACCAATGCTTGCTACATGGAG
GAACTGAGGCACATTGATCTGGTGGAAGGAGACGAGGGGAGGATGTGTATCAATACAGAA
TGGGGAGCCTTTGGAGACGATGGATCATTAGAAGACATCCGGACAGAGTTTGACAGGGAG
ATAGACCGGGGATCCCTCAACCCTGGAAAACAGCTGTTTGAGAAGATGGTCAGTGGCATG
TACTTGGGAGAGCTGGTTCGACTGATCCTAGTCAAGATGGCCAAGGAGGGCCTCTTATTT
GAAGGGCGGATCACCCCGGAGCTGCTCACCCGAGGGAAGTTTAACACCAGTGATGTGTCA
GCCATCGAAAAGAATAAGGAAGGCCTCCACAATGCCAAAGAAATCCTGACCCGCCTGGGA
GTGGAGCCGTCCGATGATGACTGTGTCTCAGTCCAGCACGTTTGCACCATTGTCTCATTT
CGCTCAGCCAACTTGGTGGCTGCCACACTGGGCGCCATCTTGAACCGCCTGCGTGATAAC
AAGGGCACACCCAGGCTGCGGACCACGGTTGGTGTCGACGGATCTCTTTACAAGACGCAC
CCACAGTATTCCCGGCGTTTCCACAAGACTCTAAGGCGCTTGGTGCCAGACTCCGATGTG
CGCTTCCTCCTCTCGGAGAGTGGCAGCGGCAAGGGGGCTGCCATGGTGACGGCGGTGGCC
TACCGCTTGGCCGAGCAGCACCGGCAGATAGAGGAGACCCTGGCTCATTTCCACCTCACC
AAAGACATGCTGCTGGAGGTGAAGAAGAGGATGCGGGCCGAGATGGAGCTGGGGCTGAGG
AAGCAGACGCACAACAATGCCGTGGTTAAGATGCTGCCCTCCTTCGTCCGGAGAACTCCC
GACGGGACCGAGAATGGTGACTTCTTGGCCCTGGATCTTGGAGGAACCAATTTCCGTGTG
CTGCTGGTGAAAATCCGTAGTGGGAAAAAGAGAACGGTGGAAATGCACAACAAGATCTAC
GCCATTCCTATTGAAATCATGCAGGGCACTGGGGAAGAGCTGTTTGATCACATTGTCTCC
TGCATCTCTGACTTCTTGGACTACATGGGGATCAAAGGCCCCAGGATGCCTCTGGGCTTC
ACGTTCTCATTTCCCTGCCAGCAGACGAGTCTGGACGCGGGAATCTTGATCACGTGGACA
AAGGGTTTTAAGGCAACAGACTGCGTGGGCCACGATGTAGTCACCTTACTAAGGGATGCG
ATAAAAAGGAGAGAGGAATTTGACCTGGACGTGGTGGCTGTGGTCAACGACACAGTGGGC
ACCATGATGACCTGTGCTTATGAGGAGCCCACCTGTGAGGTTGGACTCATTGTTGGGACC
GGCAGCAATGCCTGCTACATGGAGGAGATGAAGAACGTGGAGATGGTGGAGGGGGACCAG
GGGCAGATGTGCATCAACATGGAGTGGGGGGCCTTTGGGGACAACGGGTGTCTGGATGAT
ATCAGGACACACTACGACAGACTGGTGAACGAATATTCCCTAAATGCTGGGAAACAAAGG
TATGAGAAGATGATCAGTGGTATGTACCTGGGTGAAATCGTCCGCAACATCTTAATCGAC
TTCACCAAGAAGGGATTCCTCTTCCGAGGGCAGATCTCTGAGACGATGAAGACCCGGGGC
ATCTTTGAGACCAAGTTTCTCTCTCAGATCGAGAGTGACCGATTAGCACTGCTCCAGGTC
CGGGCTATCCTCCAGCAGCTAGGTCTGAATAGCACCTGCGATGACAGTATCCTCGTCAAG
ACAGTGTGCGGGGTGGTGTCCAGGAGGGCCGCACAGCTGTGTGGCGCAGGCATGGCTGCG
GTTGTGGATAAGATCCGCGAGAACAGAGGACTGGACCGTCTGAATGTGACTGTGGGAGTG
GACGGGACACTCTACAAGCTTCATCCACACTTCTCCAGAATCATGCACCAGACGGTGAAG
GAACTGTCACCAAAATGTAACGTGTCCTTCCTCCTGTCTGAGGATGGCAGCGGCAAGGGG
GCCGCCCTCATCACGGCCGTGGGCGTGCGGTTACGCACAGAGGCAAGCAGCTAA
|
| Enzyme 4 GenBank Gene ID |
M75126  |
| Enzyme 4 GeneCard ID |
HK1  |
| Enzyme 4 GenAtlas ID |
HK1  |
| Enzyme 4 HGNC ID |
HGNC:4922  |
| Enzyme 4 Chromosome Location |
10 |
| Enzyme 4 Locus |
10q22 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Nishi S, Seino S, Bell GI: Human hexokinase: sequences of amino- and carboxyl-terminal halves are homologous. Biochem Biophys Res Commun. 1988 Dec 30;157(3):937-43. [PubMed
]
- Ruzzo A, Andreoni F, Magnani M: Structure of the human hexokinase type I gene and nucleotide sequence of the 5' flanking region. Biochem J. 1998 Apr 15;331 ( Pt 2):607-13. [PubMed
]
- Magnani M, Bianchi M, Casabianca A, Stocchi V, Daniele A, Altruda F, Ferrone M, Silengo L: A recombinant human 'mini'-hexokinase is catalytically active and regulated by hexose 6-phosphates. Biochem J. 1992 Jul 1;285 ( Pt 1):193-9. [PubMed
]
- Magnani M, Serafini G, Bianchi M, Casabianca A, Stocchi V: Human hexokinase type I microheterogeneity is due to different amino-terminal sequences. J Biol Chem. 1991 Jan 5;266(1):502-5. [PubMed
]
- Murakami K, Piomelli S: Identification of the cDNA for human red blood cell-specific hexokinase isozyme. Blood. 1997 Feb 1;89(3):762-6. [PubMed
]
- Andreoni F, Ruzzo A, Magnani M: Structure of the 5' region of the human hexokinase type I (HKI) gene and identification of an additional testis-specific HKI mRNA. Biochim Biophys Acta. 2000 Sep 7;1493(1-2):19-26. [PubMed
]
- Aleshin AE, Zeng C, Fromm HJ, Honzatko RB: Crystallization and preliminary X-ray analysis of human brain hexokinase. FEBS Lett. 1996 Aug 5;391(1-2):9-10. [PubMed
]
- Aleshin AE, Zeng C, Bourenkov GP, Bartunik HD, Fromm HJ, Honzatko RB: The mechanism of regulation of hexokinase: new insights from the crystal structure of recombinant human brain hexokinase complexed with glucose and glucose-6-phosphate. Structure. 1998 Jan 15;6(1):39-50. [PubMed
]
- Aleshin AE, Zeng C, Bartunik HD, Fromm HJ, Honzatko RB: Regulation of hexokinase I: crystal structure of recombinant human brain hexokinase complexed with glucose and phosphate. J Mol Biol. 1998 Sep 18;282(2):345-57. [PubMed
]
- Rosano C, Sabini E, Rizzi M, Deriu D, Murshudov G, Bianchi M, Serafini G, Magnani M, Bolognesi M: Binding of non-catalytic ATP to human hexokinase I highlights the structural components for enzyme-membrane association control. Structure. 1999 Nov 15;7(11):1427-37. [PubMed
]
- Aleshin AE, Kirby C, Liu X, Bourenkov GP, Bartunik HD, Fromm HJ, Honzatko RB: Crystal structures of mutant monomeric hexokinase I reveal multiple ADP binding sites and conformational changes relevant to allosteric regulation. J Mol Biol. 2000 Mar 3;296(4):1001-15. [PubMed
]
- Bianchi M, Magnani M: Hexokinase mutations that produce nonspherocytic hemolytic anemia. Blood Cells Mol Dis. 1995;21(1):2-8. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5997 |
| Enzyme 5 Name |
Alpha-galactosidase A precursor |
| Enzyme 5 Synonyms |
- Melibiase
- Alpha-D- galactoside galactohydrolase
- Alpha-D-galactosidase A
- Agalsidase alfa
|
| Enzyme 5 Gene Name |
GLA |
| Enzyme 5 Protein Sequence |
>Alpha-galactosidase A precursor
MQLRNPELHLGCALALRFLALVSWDIPGARALDNGLARTPTMGWLHWERFMCNLDCQEEP
DSCISEKLFMEMAELMVSEGWKDAGYEYLCIDDCWMAPQRDSEGRLQADPQRFPHGIRQL
ANYVHSKGLKLGIYADVGNKTCAGFPGSFGYYDIDAQTFADWGVDLLKFDGCYCDSLENL
ADGYKHMSLALNRTGRSIVYSCEWPLYMWPFQKPNYTEIRQYCNHWRNFADIDDSWKSIK
SILDWTSFNQERIVDVAGPGGWNDPDMLVIGNFGLSWNQQVTQMALWAIMAAPLFMSNDL
RHISPQAKALLQDKDVIAINQDPLGKQGYQLRQGDNFEVWERPLSGLAWAVAMINRQEIG
GPRSYTIAVASLGKGVACNPACFITQLLPVKRKLGFYEWTSRLRSHINPTGTVLLQLENT
MQMSLKDLL
|
| Enzyme 5 Number of Residues |
429 |
| Enzyme 5 Molecular Weight |
48767 |
| Enzyme 5 Theoretical pI |
5.27 |
| Enzyme 5 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on glycosyl bonds
- hydrolase activity, hydrolyzing O-glycosyl compounds
|
| Process |
- carbohydrate metabolism
- macromolecule metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 5 General Function |
Not Available |
| Enzyme 5 Specific Function |
Hydrolysis of terminal, non-reducing alpha-D- galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactohydrolase |
| Enzyme 5 Pathways |
|
| Enzyme 5 Reactions |
- Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactohydrolase
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
Not Available |
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
757912  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P06280  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
AGAL_HUMAN  |
| Enzyme 5 PDB ID |
1R47  |
| Enzyme 5 PDB File |
Show |
| Enzyme 5 3D Structure |
|
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>1290 bp
ATGCAGCTGAGGAACCCAGAACTACATCTGGGCTGCGCGCTTGCGCTTCGCTTCCTGGCC
CTCGTTTCCTGGGACATCCCTGGGGCTAGAGCACTGGACAATGGATTGGCAAGGACGCCT
ACCATGGGCTGGCTGCACTGGGAGCGCTTCATGTGCAACCTTGACTGCCAGGAAGAGCCA
GATTCCTGCATCAGTGAGAAGCTCTTCATGGAGATGGCAGAGCTCATGGTCTCAGAAGGC
TGGAAGGATGCAGGTTATGAGTACCTCTGCATTGATGACTGTTGGATGGCTCCCCAAAGA
GATTCAGAAGGCAGACTTCAGGCAGACCCTCAGCGCTTTCCTCATGGGATTCGCCAGCTA
GCTAATTATGTTCACAGCAAAGGACTGAAGCTAGGGATTTATGCAGATGTTGGAAATAAA
ACCTGCGCAGGCTTCCCTGGGAGTTTTGGATACTACGACATTGATGCCCAGACCTTTGCT
GACTGGGGAGTAGATCTGCTAAAATTTGATGGTTGTTACTGTGACAGTTTGGAAAATTTG
GCAGATGGTTATAAGCACATGTCCTTGGCCCTGAATAGGACTGGCAGAAGCATTGTGTAC
TCCTGTGAGTGGCCTCTTTATATGTGGCCCTTTCAAAAGCCCAATTATACAGAAATCCGA
CAGTACTGCAATCACTGGCGAAATTTTGCTGACATTGATGATTCCTGGAAAAGTATAAAG
AGTATCTTGGACTGGACATCTTTTAACCAGGAGAGAATTGTTGATGTTGCTGGACCAGGG
GGTTGGAATGACCCAGATATGTTAGTGATTGGCAACTTTGGCCTCAGCTGGAATCAGCAA
GTAACTCAGATGGCCCTCTGGGCTATCATGGCTGCTCCTTTATTCATGTCTAATGACCTC
CGACACATCAGCCCTCAAGCCAAAGCTCTCCTTCAGGATAAGGACGTAATTGCCATCAAT
CAGGACCCCTTGGGCAAGCAAGGGTACCAGCTTAGACAGGGAGACAACTTTGAAGTGTGG
GAACGACCTCTCTCAGGCTTAGCCTGGGCTGTAGCTATGATAAACCGGCAGGAGATTGGT
GGACCTCGCTCTTATACCATCGCAGTTGCTTCCCTGGGTAAAGGAGTGGCCTGTAATCCT
GCCTGCTTCATCACACAGCTCCTCCCTGTGAAAAGGAAGCTAGGGTTCTATGAATGGACT
TCAAGGTTAAGAAGTCACATAAATCCCACAGGCACTGTTTTGCTTCAGCTAGAAAATACA
ATGCAGATGTCATTAAAAGACTTACTTTAA
|
| Enzyme 5 GenBank Gene ID |
X05790  |
| Enzyme 5 GeneCard ID |
GLA  |
| Enzyme 5 GenAtlas ID |
GLA  |
| Enzyme 5 HGNC ID |
HGNC:4296  |
| Enzyme 5 Chromosome Location |
X |
| Enzyme 5 Locus |
Xq22 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Tsuji S, Martin BM, Kaslow DC, Migeon BR, Choudary PV, Stubbleflied BK, Mayor JA, Murray GJ, Barranger JA, Ginns EI: Signal sequence and DNA-mediated expression of human lysosomal alpha-galactosidase A. Eur J Biochem. 1987 Jun 1;165(2):275-80. [PubMed
]
- Kornreich R, Desnick RJ, Bishop DF: Nucleotide sequence of the human alpha-galactosidase A gene. Nucleic Acids Res. 1989 Apr 25;17(8):3301-2. [PubMed
]
- Oeltjen JC, Liu X, Lu J, Allen RC, Muzny D, Belmont JW, Gibbs RA: Sixty-nine kilobases of contiguous human genomic sequence containing the alpha-galactosidase A and Bruton's tyrosine kinase loci. Mamm Genome. 1995 May;6(5):334-8. [PubMed
]
- Bishop DF, Calhoun DH, Bernstein HS, Hantzopoulos P, Quinn M, Desnick RJ: Human alpha-galactosidase A: nucleotide sequence of a cDNA clone encoding the mature enzyme. Proc Natl Acad Sci U S A. 1986 Jul;83(13):4859-63. [PubMed
]
- Quinn M, Hantzopoulos P, Fidanza V, Calhoun DH: A genomic clone containing the promoter for the gene encoding the human lysosomal enzyme, alpha-galactosidase A. Gene. 1987;58(2-3):177-88. [PubMed
]
- Bishop DF, Kornreich R, Desnick RJ: Structural organization of the human alpha-galactosidase A gene: further evidence for the absence of a 3' untranslated region. Proc Natl Acad Sci U S A. 1988 Jun;85(11):3903-7. [PubMed
]
- Novo FJ, Kruszewski A, MacDermot KD, Goldspink G, Gorecki DC: Editing of human alpha-galactosidase RNA resulting in a pyrimidine to purine conversion. Nucleic Acids Res. 1995 Jul 25;23(14):2636-40. [PubMed
]
- Eng CM, Desnick RJ: Molecular basis of Fabry disease: mutations and polymorphisms in the human alpha-galactosidase A gene. Hum Mutat. 1994;3(2):103-11. [PubMed
]
- Koide T, Ishiura M, Iwai K, Inoue M, Kaneda Y, Okada Y, Uchida T: A case of Fabry's disease in a patient with no alpha-galactosidase A activity caused by a single amino acid substitution of Pro-40 by Ser. FEBS Lett. 1990 Jan 1;259(2):353-6. [PubMed
]
- von Scheidt W, Eng CM, Fitzmaurice TF, Erdmann E, Hubner G, Olsen EG, Christomanou H, Kandolf R, Bishop DF, Desnick RJ: An atypical variant of Fabry's disease with manifestations confined to the myocardium. N Engl J Med. 1991 Feb 7;324(6):395-9. [PubMed
]
- Sakuraba H, Oshima A, Fukuhara Y, Shimmoto M, Nagao Y, Bishop DF, Desnick RJ, Suzuki Y: Identification of point mutations in the alpha-galactosidase A gene in classical and atypical hemizygotes with Fabry disease. Am J Hum Genet. 1990 Nov;47(5):784-9. [PubMed
]
- Bernstein HS, Bishop DF, Astrin KH, Kornreich R, Eng CM, Sakuraba H, Desnick RJ: Fabry disease: six gene rearrangements and an exonic point mutation in the alpha-galactosidase gene. J Clin Invest. 1989 Apr;83(4):1390-9. [PubMed
]
- Ishii S, Sakuraba H, Suzuki Y: Point mutations in the upstream region of the alpha-galactosidase A gene exon 6 in an atypical variant of Fabry disease. Hum Genet. 1992 Apr;89(1):29-32. [PubMed
]
- Eng CM, Resnick-Silverman LA, Niehaus DJ, Astrin KH, Desnick RJ: Nature and frequency of mutations in the alpha-galactosidase A gene that cause Fabry disease. Am J Hum Genet. 1993 Dec;53(6):1186-97. [PubMed
]
- Davies JP, Winchester BG, Malcolm S: Mutation analysis in patients with the typical form of Anderson-Fabry disease. Hum Mol Genet. 1993 Jul;2(7):1051-3. [PubMed
]
- Davies J, Christomanou H, Winchester B, Malcolm S: Detection of 8 new mutations in the alpha-galactosidase A gene in Fabry disease. Hum Mol Genet. 1994 Apr;3(4):667-9. [PubMed
]
- Eng CM, Niehaus DJ, Enriquez AL, Burgert TS, Ludman MD, Desnick RJ: Fabry disease: twenty-three mutations including sense and antisense CpG alterations and identification of a deletional hot-spot in the alpha-galactosidase A gene. Hum Mol Genet. 1994 Oct;3(10):1795-9. [PubMed
]
- Okumiya T, Ishii S, Takenaka T, Kase R, Kamei S, Sakuraba H, Suzuki Y: Galactose stabilizes various missense mutants of alpha-galactosidase in Fabry disease. Biochem Biophys Res Commun. 1995 Sep 25;214(3):1219-24. [PubMed
]
- Okumiya T, Ishii S, Kase R, Kamei S, Sakuraba H, Suzuki Y: Alpha-galactosidase gene mutations in Fabry disease: heterogeneous expressions of mutant enzyme proteins. Hum Genet. 1995 May;95(5):557-61. [PubMed
]
- Madsen KM, Hasholt L, Sorensen SA, Fermer ML, Dahl N: Two novel mutations (L32P) and (G85N) among five different missense mutations in six Danish families with Fabry's disease. Hum Mutat. 1995;5(3):277-8. [PubMed
]
- Nakao S, Takenaka T, Maeda M, Kodama C, Tanaka A, Tahara M, Yoshida A, Kuriyama M, Hayashibe H, Sakuraba H, et al.: An atypical variant of Fabry's disease in men with left ventricular hypertrophy. N Engl J Med. 1995 Aug 3;333(5):288-93. [PubMed
]
- Davies JP, Eng CM, Hill JA, Malcolm S, MacDermot K, Winchester B, Desnick RJ: Fabry disease: fourteen alpha-galactosidase A mutations in unrelated families from the United Kingdom and other European countries. Eur J Hum Genet. 1996;4(4):219-24. [PubMed
]
- Cariolou MA, Christodoulides M, Manoli P, Kokkofitou A, Tsambaos D: Novel trinucleotide deletion in Fabry's disease. Hum Genet. 1996 Apr;97(4):468-70. [PubMed
]
- Germain D, Biasotto M, Tosi M, Meo T, Kahn A, Poenaru L: Fluorescence-assisted mismatch analysis (FAMA) for exhaustive screening of the alpha-galactosidase A gene and detection of carriers in Fabry disease. Hum Genet. 1996 Dec;98(6):719-26. [PubMed
]
- Blanch LC, Meaney C, Morris CP: A sensitive mutation screening strategy for Fabry disease: detection of nine mutations in the alpha-galactosidase A gene. Hum Mutat. 1996;8(1):38-43. [PubMed
]
- Redonnet-Vernhet I, Ploos van Amstel JK, Jansen RP, Wevers RA, Salvayre R, Levade T: Uneven X inactivation in a female monozygotic twin pair with Fabry disease and discordant expression of a novel mutation in the alpha-galactosidase A gene. J Med Genet. 1996 Aug;33(8):682-8. [PubMed
]
- Takata T, Okumiya T, Hayashibe H, Shimmoto M, Kase R, Itoh K, Utsumi K, Kamei S, Sakuraba H: Screening and detection of gene mutations in Japanese patients with Fabry disease by non-radioactive single-stranded conformation polymorphism analysis. Brain Dev. 1997 Mar;19(2):111-6. [PubMed
]
- Eng CM, Ashley GA, Burgert TS, Enriquez AL, D'Souza M, Desnick RJ: Fabry disease: thirty-five mutations in the alpha-galactosidase A gene in patients with classic and variant phenotypes. Mol Med. 1997 Mar;3(3):174-82. [PubMed
]
- Miyazaki T, Kajita M, Ohmori S, Mizutani N, Niwa T, Murata Y, Seo H: A novel mutation (E358K) in the alpha-galactosidase A gene detected in a Japanese family with Fabry disease. Hum Mutat. 1998;Suppl 1:S139-40. [PubMed
]
- Okumiya T, Kawamura O, Itoh K, Kase R, Ishii S, Kamei S, Sakuraba H: Novel missense mutation (M72V) of alpha-galactosidase gene and its expression product in an atypical Fabry hemizygote. Hum Mutat. 1998;Suppl 1:S213-6. [PubMed
]
- Guffon N, Froissart R, Chevalier-Porst F, Maire I: Mutation analysis in 11 French patients with Fabry disease. Hum Mutat. 1998;Suppl 1:S288-90. [PubMed
]
- Germain DP, Poenaru L: Fabry disease: identification of novel alpha-galactosidase A mutations and molecular carrier detection by use of fluorescent chemical cleavage of mismatches. Biochem Biophys Res Commun. 1999 Apr 21;257(3):708-13. [PubMed
]
- Beyer EM, Karpova EA, Udalova OV, Ploos van Amstel JK, van Diggelen OP, Tsvetkova IV: The multiple cases of Fabry disease in a Russian family caused by an E341K amino acid substitution in the alpha-galactosidase A. Clin Chim Acta. 1999 Feb;280(1-2):81-9. [PubMed
]
- Topaloglu AK, Ashley GA, Tong B, Shabbeer J, Astrin KH, Eng CM, Desnick RJ: Twenty novel mutations in the alpha-galactosidase A gene causing Fabry disease. Mol Med. 1999 Dec;5(12):806-11. [PubMed
]
- Lee JK, Kim GH, Kim JS, Kim KK, Lee MC, Yoo HW: Identification of four novel mutations in five unrelated Korean families with Fabry disease. Clin Genet. 2000 Sep;58(3):228-33. [PubMed
]
- Ashton-Prolla P, Tong B, Shabbeer J, Astrin KH, Eng CM, Desnick RJ: Fabry disease: twenty-two novel mutations in the alpha-galactosidase A gene and genotype/phenotype correlations in severely and mildly affected hemizygotes and heterozygotes. J Investig Med. 2000 Jul;48(4):227-35. [PubMed
]
- Germain DP, Salard D, Fellmann F, Azibi K, Caillaud C, Bernard MC, Poenaru L: Identification of a novel de novo mutation (G373D) in the alpha-galactosidase A gene (GLA) in a patient affected with Fabry disease. Hum Mutat. 2001 Apr;17(4):353. [PubMed
]
- Blaydon D, Hill J, Winchester B: Fabry disease: 20 novel GLA mutations in 35 families. Hum Mutat. 2001 Nov;18(5):459. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
6149 |
| Enzyme 6 Name |
Alpha-mannosidase 2 |
| Enzyme 6 Synonyms |
- Alpha-mannosidase II
- Mannosyl- oligosaccharide 1,3-1,6-alpha-mannosidase
- MAN II
- Golgi alpha- mannosidase II
- Mannosidase alpha class 2A member 1
|
| Enzyme 6 Gene Name |
MAN2A1 |
| Enzyme 6 Protein Sequence |
>Alpha-mannosidase 2
MKLSRQFTVFGSAIFCVVIFSLYLMLDRGHLDYPRNPRREGSFPQGQLSMLQEKIDHLER
LLAENNEIISNIRDSVINLSESVEDGPKSSQSNFSQGAGSHLLPSQLSLSVDTADCLFAS
QSGSHNSDVQMLDVYSLISFDNPDGGVWKQGFDITYESNEWDTEPLQVFVVPHSHNDPGW
LKTFNDYFRDKTQYIFNNMVLKLKEDSRRKFIWSEISYLSKWWDIIDIQKKDAVKSLIEN
GQLEIVTGGWVMPDEATPHYFALIDQLIEGHQWLENNIGVKPRSGWAIDPFGHSPTMAYL
LNRAGLSHMLIQRVHYAVKKHFALHKTLEFFWRQNWDLGSVTDILCHMMPFYSYDIPHTC
GPDPKICCQFDFKRLPGGRFGCPWGVPPETIHPGNVQSRARMLLDQYRKKSKLFRTKVLL
APLGDDFRYCEYTEWDLQFKNYQQLFDYMNSQSKFKVKIQFGTLSDFFDALDKADETQRD
KGQSMFPVLSGDFFTYADRDDHYWSGYFTSRPFYKRMDRIMESHLRAAEILYYFALRQAH
KYKINKFLSSSLYTALTEARRNLGLFQHHDAITGTAKDWVVVDYGTRLFHSLMVLEKIIG
NSAFLLILKDKLTYDSYSPDTFLEMDLKQKSQDSLPQKNIIRLSAEPRYLVVYNPLEQDR
ISLVSVYVSSPTVQVFSASGKPVEVQVSAVWDTANTISETAYEISFRAHIPPLGLKVYKI
LESASSNSHLADYVLYKNKVEDSGIFTIKNMINTEEGITLENSFVLLRFDQTGLMKQMMT
KEDGKHHEVNVQFSWYGTTIKRDKSGAYLFLPDGNAKPYVYTTPPFVRVTHGRIYSEVTC
FFDHVTHRVRLYHIQGIEGQSVEVSNIVDIRKVYNREIAMKISSDIKSQNRFYTDLNGYQ
IQPRMTLSKLPLQANVYPMTTMAYIQDAKHRLTLLSAQSLGVSSLNSGQIEVIMDRRLMQ
DDNRGLEQGIQDNKITANLFRILLEKRSAVNTEEEKKSVSYPSLLSHITSSLMNHPVIPM
ANKFSSPTLELQGEFSPLQSSLPCDIHLVNLRTIQSKVGNGHSNEAALILHRKGFDCRFS
SKGTGLFCSTTQGKILVQKLLNKFIVESLTPSSLSLMHSPPGTQNISEINLSPMEISTFR
IQLR
|
| Enzyme 6 Number of Residues |
1144 |
| Enzyme 6 Molecular Weight |
131142 |
| Enzyme 6 Theoretical pI |
7.61 |
| Enzyme 6 GO Classification |
| Function |
- alpha-mannosidase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on glycosyl bonds
- hydrolase activity, hydrolyzing O-glycosyl compounds
- mannosidase activity
|
| Process |
- alcohol metabolism
- carbohydrate metabolism
- cellular metabolism
- hexose metabolism
- macromolecule metabolism
- mannose metabolism
- metabolism
- monosaccharide metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 6 General Function |
Carbohydrate transport and metabolism |
| Enzyme 6 Specific Function |
Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway |
| Enzyme 6 Pathways |
|
| Enzyme 6 Reactions |
- Hydrolysis of the terminal 1,3- and 1,6-linked alpha-D-mannose residues in the mannosyl-oligosaccharide Man5(GlcNAc)3
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
Not Available |
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
1117827  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
Q16706  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
MA2A1_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>3435 bp
ATGAAGTTAAGCCGCCAGTTCACCGTGTTCGGCAGTGCGATCTTCTGTGTGGTGATTTTC
TCGCTCTACCTGATGCTGGACCGGGGTCACTTAGACTACCCCAGGAACCCGCGCCGCGAG
GGCTCCTTCCCTCAGGGCCAGCTCTCAATGTTGCAAGAAAAAATAGACCATTTGGAGCGT
TTGCTAGCTGAGAATAATGAGATCATCTCAAATATTAGAGACTCAGTCATCAATTTGAGT
GAGTCTGTGGAGGATGGTCCGAAAAGTTCACAAAGCAATTTCAGCCAAGGTGCTGGCTCA
CATCTTCTGCCCTCACAATTATCCCTCTCAGTTGACACTGCAGACTGTCTGTTTGCTTCA
CAAAGTGGAAGTCACAATTCAGATGTGCAGATGTTGGATGTTTACAGTCTAATTTCTTTT
GACAATCCAGATGGTGGAGTTTGGAAGCAAGGATTTGACATTACTTATGAATCTAATGAA
TGGGACACTGAACCCCTTCAAGTCTTTGTGGTGCCTCATTCCCATAACGACCCAGGTTGG
TTGAAGACTTTCAATGACTACTTTAGAGACAAGACTCAGTATATTTTTAATAACATGGTC
CTAAAGCTGAAAGAAGACTCACGGAGGAAGTTTATTTGGTCTGAGATCTCTTACCTTTCA
AAGTGGTGGGATATTATAGATATTCAGAAGAAGGATGCTGTTAAAAGTTTAATAGAAAAT
GGTCAGCTTGAAATTGTGACAGGTGGCTGGGTTATGCCTGATGAAGCTACTCCACATTAT
TTTGCCTTAATTGATCAACTAATTGAAGGACATCAGTGGCTGGAAAATAATATAGGAGTG
AAACCTCGGTCCGGCTGGGCTATTGATCCCTTTGGACACTCACCAACAATGGCTTATCTT
CTAAACCGTGCTGGACTTTCTCACATGCTTATCCAGAGAGTTCATTATGCAGTTAAAAAA
CACTTTGCACTGCATAAAACATTGGAGTTTTTTTGGAGACAGAATTGGGATCTGGGATCT
GTCACAGATATTTTATGCCACATGATGCCCTTCTACAGCTATGACATCCCTCACACTTGT
GGACCTGATCCTAAAATATGCTGCCAGTTTGATTTTAAACGTCTTCCTGGAGGCAGATTT
GGTTGTCCCTGGGGAGTCCCCCCAGAAACAATACATCCTGGAAATGTCCAAAGCAGGGCT
CGGATGCTACTAGATCAGTACCGAAAGAAGTCAAAGCTTTTTCGAACCAAAGTTCTCCTG
GCTCCACTAGGAGATGATTTCCGCTACTGTGAATACACGGAATGGGATTTACAGTTTAAG
AATTATCAGCAGCTTTTTGATTATATGAATTCTCAGTCCAAGTTTAAAGTTAAGATACAG
TTTGGAACTTTATCAGATTTTTTTGATGCGCTGGATAAAGCAGATGAAACTCAGAGAGAC
AAGGGCCAATCGATGTTCCCTGTTTTAAGTGGAGATTTTTTCACTTATGCCGATCGAGAT
GATCATTACTGGAGTGGCTATTTTACATCCAGACCCTTTTACAAACGAATGGACAGAATC
ATGGAATCTCATTTAAGGGCTGCTGAAATTCTTTACTATTTCGCCCTGAGACAAGCTCAC
AAATACAAGATAAATAAATTTCTCTCATCATCACTTTACACGGCACTGACAGAAGCCAGA
AGGAATTTGGGACTGTTTCAACATCATGATGCTATCACAGGAACTGCAAAAGACTGGGTG
GTTGTGGATTATGGTACCAGACTTTTTCATTCGTTAATGGTTTTGGAGAAGATAATTGGA
AATTCTGCATTTCTTCTTATTGGGAAGGACAAACTCACATACGACTCTTACTCTCCTGAT
ACCTTCCTGGAGATGGATTTGAAACAAAAATCACAAGATTCTCTGCCACAAAAAAATATA
ATAAGGCTGAGTGCGGAGCCAAGGTACCTTGTGGTCTATAATCCTTTAGAACAAGACCGA
ATCTCGTTGGTCTCAGTCTATGTGAGTTCCCCGACAGTGCAAGTGTTCTCTGCTTCAGGA
AAACCTGTGGAAGTTCAAGTCAGCGCAGTTTGGGATACAGCAAATACTATTTCAGAAACA
GCCTATGAGATCTCTTTTCGAGCACATATACCGCCATTGGGACTGAAAGTGTATAAGATT
TTGGAATCAGCAAGTTCAAATTCACATTTAGCTGATTATGTCTTGTATAAGAATAAAGTA
GAAGATAGCGGAATTTTCACCATAAAGAATATGATAAATACTGAAGAAGGTATAACACTA
GAGAACTCCTTTGTTTTACTTCGGTTTGATCAAACTGGACTTATGAAGCAAATGATGACT
AAAGAAGATGGTAAACACCATGAAGTAAATGTGCAATTTTCATGGTATGGAACCACAATT
AAAAGAGACAAAAGTGGTGCCTACCTCTTCTTACCTGATGGTAATGCCAAGCCTTATGTT
TACACAACACCGCCCTTTGTCAGAGTGACACATGGAAGGATTTATTCGGAAGTGACTTGC
TTTTTTGACCATGTTACTCATAGAGTCCGACTATACCACATACAGGGAATAGAAGGACAG
TCTGTGGAAGTTTCCAATATTGTGGACATCCGAAAAGTATATAACCGTGAGATTGCAATG
AAAATTTCTTCTGATATAAAAAGCCAAAATAGATTTTATACTGACCTAAATGGGTACCAG
ATTCAACCTAGAATGACACTGAGCAAATTGCCTCTTCAAGCAAATGTCTATCCCATGACC
ACAATGGCCTATATCCAGGATGCCAAACATCGTTTGACACTGCTCTCTGCTCAGTCATTA
GGGGTTTCGAGTTTGAATAGTGGTCAGATTGAAGTTATCATGGATCGAAGACTCATGCAA
GATGATAATCGTGGCCTTGAGCAAGGTATCCAGGATAACAAGATTACAGCTAATCTATTT
CGAATACTACTAGAAAAAAGAAGTGCTGTTAATACGGAAGAAGAAAAGAAGTCGGTCAGT
TATCCTTCTCTCCTTAGCCACATAACTTCTTCTCTCATGAATCATCCAGTCATTCCAATG
GCAAATAAGTTCTCCTCACCTACCCTTGAGCTGCAAGGTGAATTCTCTCCATTACAGTCA
TCTTTGCCTTGTGACATTCATCTGGTTAATTTGAGAACAATACAGTCAAAGGTGGGCAAT
GGGCACTCCAATGAGGCAGCCTTGATCCTCCACAGAAAAGGGTTTGATTGTCGGTTCTCT
AGCAAAGGCACAGGGCTGTTTTGTTCTACTACTCAGGGAAAGATATTGGTACAGAAACTT
TTAAACAAGTTTATTGTCGAAAGTCTCACACCTTCATCACTATCCTTGATGCATTCACCT
CCCGGCACTCAGAATATAAGTGAGATCAACTTGAGTCCAATGGAAATCAGCACATTCCGA
ATCCAGTTGAGGTGA
|
| Enzyme 6 GenBank Gene ID |
U31520  |
| Enzyme 6 GeneCard ID |
MAN2A1  |
| Enzyme 6 GenAtlas ID |
MAN2A1  |
| Enzyme 6 HGNC ID |
HGNC:6824  |
| Enzyme 6 Chromosome Location |
5 |
| Enzyme 6 Locus |
5q21-q22 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Misago M, Liao YF, Kudo S, Eto S, Mattei MG, Moremen KW, Fukuda MN: Molecular cloning and expression of cDNAs encoding human alpha-mannosidase II and a previously unrecognized alpha-mannosidase IIx isozyme. Proc Natl Acad Sci U S A. 1995 Dec 5;92(25):11766-70. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
6150 |
| Enzyme 7 Name |
Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB |
| Enzyme 7 Synonyms |
- Processing alpha-1,2-mannosidase IB
- Alpha-1,2-mannosidase IB
- Mannosidase alpha class 1A member 2
|
| Enzyme 7 Gene Name |
MAN1A2 |
| Enzyme 7 Protein Sequence |
>Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB
MTTPALLPLSGRRIPPLNLGPPSFPHHRATLRLSEKFILLLILSAFITLCFGAFFFLPDS
SKHKRFDLGLEDVLIPHVDAGKGAKNPGVFLIHGPDEHRHREEEERLRNKIRADHEKALE
EAKEKLRKSREEIRAEIQTEKNKVVQEMKIKENKPLPPVPIPNLVGIRGGDPEDNDIREK
REKIKEMMKHAWDNYRTYGWGHNELRPIARKGHSPNIFGSSQMGATIVDALDTLYIMGLH
DEFLDGQRWIEDNLDFSVNSEVSVFEVNIRFIGGLLAAYYLSGEEIFKIKAVQLAEKLLP
AFNTPTGIPWAMVNLKSGVGRNWGWASAGSSILAEFGTLHMEFIHLSYLTGDLTYYKKVM
HIRKLLQKMDRPNGLYPNYLNPRTGRWGQYHTSVGGLGDSFYEYLLKAWLMSDKTDHEAR
KMYDDAIEAIEKHLIKKSRGGLTFIGEWKNGHLEKKMGHLACFAGGMFALGADGSRADKA
GHYLELGAEIARTCHESYDRTALKLGPESFKFDGAVEAVAVRQAEKYYILRPEVIETYWY
LWRFTHDPRYRQWGWEAALAIEKYCRVNGGFSGVKDVYSSTPTHDDVQQSFFLAETLKYL
YLLFSGDDLLPLDHWVFNTEAHPLPVLHLANTTLSGNPAVR
|
| Enzyme 7 Number of Residues |
641 |
| Enzyme 7 Molecular Weight |
73004 |
| Enzyme 7 Theoretical pI |
7.67 |
| Enzyme 7 GO Classification |
| Function |
- binding
- calcium ion binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on glycosyl bonds
- hydrolase activity, hydrolyzing O-glycosyl compounds
- ion binding
- mannosidase activity
- mannosyl-oligosaccharide 1,2-alpha-mannosidase activity
- mannosyl-oligosaccharide mannosidase activity
|
| Process |
- biopolymer metabolism
- biopolymer modification
- macromolecule metabolism
- metabolism
- physiological process
- protein amino acid N-linked glycosylation
- protein amino acid glycosylation
- protein modification
|
| Component |
|
|
| Enzyme 7 General Function |
Not Available |
| Enzyme 7 Specific Function |
Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2) |
| Enzyme 7 Pathways |
- High-mannose type N-glycan biosynthesis (map00513
)
- N-Glycan biosynthesis (map00510
)
|
| Enzyme 7 Reactions |
- Hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
3025750  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
O60476  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
MA1A2_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>758 bp
ATCATACATCTGTCGGTGGCCTGGGAGACAGTTTTTATGAATACTTACTGAAAGCATGGT
TGATGTCAGATAAAACAGACCATGAGGCAAGAAAGATGTATGATGATGCTATTGAGGCTA
TAGAAAAACATCTTATTAAGAAGTCTCGTGGAGGTCTTACCTTTATTGGAGAATGGAAGA
ATGGGCACTTGGAAAAAAAGATGGGGCATTTGGCCTGCTTTGCTGGGGGAATGTTTGCAC
TAGGAGCAGATGGTTCCAGAGCAGATAAAGCTGGTCATTATTTAGAGCTAGGGGCAGAAA
TTGCACGTACTTGTCATGAGTCATATGACAGAACTGCATTAAAGCTAGGTCCTGAATCAT
TCAAGTTTGATGGTGCAGTGGAGGCTGTGGCTGTCCGGCAGGCTGAAAAGTATTATATCC
TCCGTCCAGAAGTAATTGAAACCTATTGGTACCTATGGCGATTCACTCACGATCCAAGAT
ACAGGCAGTGGGGCTGGGAAGCAGCACTGGCCATTGAAAAGTATTGCCGAGTTAATGGTG
GGTTTTCTGGAGTCAAAGATGTATATTCCTCTACTCCTACACATGATGATGTACAGCAGA
GCTTTTTTCTTGCTGAAACATTAAAATATTTGTATCTGCTGTTCTCCGGTGATGACCTTT
TACCTTTAGACCACTGGGTGTTTAATACAGAGGCTCACCCTCTGCCTGTGTTACATTTAG
CCAACACCACACTTTCAGGTAATCCTGCTGTTCGATGA
|
| Enzyme 7 GenBank Gene ID |
AF053626  |
| Enzyme 7 GeneCard ID |
MAN1A2  |
| Enzyme 7 GenAtlas ID |
MAN1A2  |
| Enzyme 7 HGNC ID |
HGNC:6822  |
| Enzyme 7 Chromosome Location |
1 |
| Enzyme 7 Locus |
1p13 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Tremblay LO, Campbell Dyke N, Herscovics A: Molecular cloning, chromosomal mapping and tissue-specific expression of a novel human alpha1,2-mannosidase gene involved in N-glycan maturation. Glycobiology. 1998 Jun;8(6):585-95. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
6151 |
| Enzyme 8 Name |
Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase |
| Enzyme 8 Synonyms |
- ER alpha-1,2-mannosidase
- Mannosidase alpha class 1B member 1
- Man9GlcNAc2-specific-processing alpha-mannosidase
|
| Enzyme 8 Gene Name |
MAN1B1 |
| Enzyme 8 Protein Sequence |
>Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase
MAACEGRRSGALGSSQSDFLTPPVGGAPWAVATTVVMYPPPPPPPHRDFISVTLSFGENY
DNSKSWRRRSCWRKWKQLSRLQRNMILFLLAFLLFCGLLFYINLADHWKALAFRLEEEQK
MRPEIAGLKPANPPVLPAPQKADTDPENLPEISSQKTQRHIQRGPPHLQIRPPSQDLKDG
TQEEATKRQEAPVDPRPEGDPQRTVISWRGAVIEPEQGTELPSRRAEVPTKPPLPPARTQ
GTPVHLNYRQKGVIDVFLHAWKGYRKFAWGHDELKPVSRSFSEWFGLGLTLIDALDTMWI
LGLRKEFEEARKWVSKKLHFEKDVDVNLFESTIRILGGLLSAYHLSGDSLFLRKAEDFGN
RLMPAFRTPSKIPYSDVNIGTGVAHPPRWTSDSTVAEVTSIQLEFRELSRLTGDKKFQEA
VEKVTQHIHGLSGKKDGLVPMFINTHSGLFTHLGVFTLGARADSYYEYLLKQWIQGGKQE
TQLLEDYVEAIEGVRTHLLRHSEPSKLTFVGELAHGRFSAKMDHLVCFLPGTLALGVYHG
LPASHMELAQELMETCYQMNRQMETGLSPEIVHFNLYPQPGRRDVEVKPADRHNLLRPET
VESLFYLYRVTGDRKYQDWGWEILQSFSRFTRVPSGGYSSINNVQDPQKPEPRDKMESFF
LGETLKYLFLLFSDDPNLLSLDAYVFNTEAHPLPIWTPA
|
| Enzyme 8 Number of Residues |
699 |
| Enzyme 8 Molecular Weight |
79581 |
| Enzyme 8 Theoretical pI |
7.80 |
| Enzyme 8 GO Classification |
| Function |
- binding
- calcium ion binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on glycosyl bonds
- hydrolase activity, hydrolyzing O-glycosyl compounds
- ion binding
- mannosidase activity
- mannosyl-oligosaccharide 1,2-alpha-mannosidase activity
- mannosyl-oligosaccharide mannosidase activity
|
| Process |
- biopolymer metabolism
- biopolymer modification
- macromolecule metabolism
- metabolism
- physiological process
- protein amino acid N-linked glycosylation
- protein amino acid glycosylation
- protein modification
|
| Component |
|
|
| Enzyme 8 General Function |
Not Available |
| Enzyme 8 Specific Function |
Involved in the maturation of Asn-linked oligosaccharides. Trim a single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2). The only product is the Man(8)GlcNAc(2) isomer B, the form lacking the middle-arm terminal alpha 1,2-mannose. It may be involved in glycoprotein quality control since it is important to target misfolded glycoproteins for degradation |
| Enzyme 8 Pathways |
- High-mannose type N-glycan biosynthesis (map00513
)
- N-Glycan biosynthesis (map00510
)
|
| Enzyme 8 Reactions |
- Hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
6066222  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
Q9UKM7  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
MA1B1_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>2100 bp
ATGGCTGCCTGCGAGGGCAGGAGAAGCGGAGCTCTCGGTTCCTCTCAGTCGGACTTCCTG
ACGCCGCCAGTGGGCGGGGCCCCTTGGGCCGTCGCCACCACTGTAGTCATGTACCCACCG
CCGCCGCCGCCGCCTCATCGGGACTTCATCTCGGTGACGCTGAGCTTTGGCGAGAGCTAT
GACAACAGCAAGAGTTGGCGGCGGCGCTCGTGCTGGAGGAAATGGAAGCAACTGTCGAGA
TTGCAGCGGAATATGATTCTCTTCCTCCTTGCCTTTCTGCTTTTCTGTGGACTCCTCTTC
TACATCAACTTGGCTGACCATTGGAAAGCTCTGGCTTTCAGGCTAGAGGAAGAGCAGAAG
ATGAGGCCAGAAATTGCTGGGTTAAAACCAGCAAATCCACCCGTCTTACCAGCTCCTCAG
AAGGCGGACACCGACCCTGAGAACTTACCTGAGATTTCGTCACAGAAGACACAAAGACAC
ATCCAGCGGGGACCACCTCACCTGCAGATTAGACCCCCAAGCCAAGACCTGAAGGATGGG
ACCCAGGAGGAGGCCACAAAAAGGCAAGAAGCCCCTGTGGATCCCCGCCCGGAAGGAGAT
CCGCAGAGGACAGTCATCAGCTGGAGGGGAGCGGTGATCGAGCCTGAGCAGGGCACCGAG
CTCCCTTCAAGAAGAGCAGAAGTGCCCACCAAGCCTCCCCTGCCACCGGCCAGGACACAG
GGCACACCAGTGCATCTGAACTATCGCCAGAAGGGCGTGATTGACGTCTTCCTGCATGCA
TGGAAAGGATACCGCAAGTTTGCATGGGGCCATGACGAGCTGAAGCCTGTGTCCAGGTCC
TTCAGTGAGTGGTTTGGCCTCGGTCTCACACTGATCGACGCGCTGGACACCATGTGGATC
TTGGGTCTGAGGAAAGAATTTGAGGAAGCCAGGAAGTGGGTGTCGAAGAAGTTACACTTT
GAAAAGGACGTGGACGTCAACCTGTTTGAGAGCACGATCCGCATCCTGGGGGGGCTCCTG
AGTGCCTACCACCTGTCTGGGGACAGCCTCTTCCTGAGGAAAGCTGAGGATTTTGGAAAT
CGGCTAATGCCTGCCTTCAGAACACCATCCAAGATTCCTTACTCGGATGTGAACATCGGT
ACTGGAGTTGCCCACCCGCCACGGTGGACCTCCGACAGCACTGTGGCCGAGGTGACCAGC
ATTCAGCTGGAGTTCCGGGAGCTCTCCCGTCTCACAGGGGATAAGAAGTTTCAGGAGGCA
GTGGAGAAGGTGACACAGCACATCCACGGCCTGTCTGGGAAGAAGGATGGGCTGGTGCCC
ATGTTCATCAATACCCACAGTGGCCTCTTCACCCACCTGGGCGTATTCACGCTGGGCGCC
AGGGCCGACAGCTACTATGAGTACCTGCTGAAGCAGTGGATCCAGGGCGGGAAGCAGGAG
ACACAGCTGCTGGAAGACTACGTGGAAGCCATCGAGGGTGTCAGAACGCACCTGCTGCGG
CACTCCGAGCCCAGTAAGCTCACCTTTGTGGGGGAGCTTGCCCACGGCCGCTTCAGTGCC
AAGATGGACCACCTGGTGTGCTTCCTGCCAGGGACGCTGGCTCTGGGCGTCTACCACGGC
CTGCCCGCCAGCCACATGGAGCTGGCCCAGGAGCTCATGGAGACTTGTTACCAGATGAAC
CGGCAGATGGAGACGGGGCTGAGTCCCGAGATCGTGCACTTCAACCTTTACCCCCAGCCG
GGCCGTCGGGACGTGGAGGTCAAGCCAGCAGACAGGCACAACCTGCTGCGGCCAGAGACC
GTGGAGAGCCTGTTCTACCTGTACCGCGTCACAGGGGACCGCAAATACCAGGACTGGGGC
TGGGAGATTCTGCAGAGCTTCAGCCGATTCACACGGGTCCCCTCGGGTGGCTATTCTTCC
ATCAACAATGTCCAGGATCCTCAGAAGCCCGAGCCTAGGGACAAGATGGAGAGCTTCTTC
CTGGGGGAGACGCTCAAGTATCTGTTCTTGCTCTTCTCCGATGACCCAAACCTGCTCAGC
CTGGACGCCTACGTGTTCAACACCGAAGCCCACCCTCTGCCTATCTGGACCCCTGCCTAG
|
| Enzyme 8 GenBank Gene ID |
AF148509  |
| Enzyme 8 GeneCard ID |
MAN1B1  |
| Enzyme 8 GenAtlas ID |
MAN1B1  |
| Enzyme 8 HGNC ID |
HGNC:6823  |
| Enzyme 8 Chromosome Location |
9 |
| Enzyme 8 Locus |
9q34 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Tremblay LO, Herscovics A: Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis. Glycobiology. 1999 Oct;9(10):1073-8. [PubMed
]
- Gonzalez DS, Karaveg K, Vandersall-Nairn AS, Lal A, Moremen KW: Identification, expression, and characterization of a cDNA encoding human endoplasmic reticulum mannosidase I, the enzyme that catalyzes the first mannose trimming step in mammalian Asn-linked oligosaccharide biosynthesis. J Biol Chem. 1999 Jul 23;274(30):21375-86. [PubMed
]
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
6152 |
| Enzyme 9 Name |
Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA |
| Enzyme 9 Synonyms |
- Processing alpha-1,2-mannosidase IA
- Alpha-1,2-mannosidase IA
- Mannosidase alpha class 1A member 1
- Man(9-alpha-mannosidase
- Man9-mannosidase
|
| Enzyme 9 Gene Name |
MAN1A1 |
| Enzyme 9 Protein Sequence |
>Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA
MPVGGLLPLFSSPAGGVLGGGLGGGGGRKGSGPAALRLTEKFVLLLVFSAFITLCFGAIF
FLPDSSKLLSGVLFHSSPALQPAADHKPGPGARAEDAAEGRARRREEGAPGDPEAALEDN
LARIRENHERALREAKETLQKLPEEIQRDILLEKKKVAQDQLRDKAPFRGLPPVDFVPPI
GVESREPADAAIREKRAKIKEMMKHAWNNYKGYAWGLNELKPISKGGHSSSLFGNIKGAT
IVDALDTLFIMEMKHEFEEAKSWVEENLDFNVNAEISVFEVNIRFVGGLLSAYYLSGEEI
FRKKAVELGVKLLPAFHTPSGIPWALLNMKSGIGRNWPWASGGSSILAEFGTLHLEFMHL
SHLSGNPIFAEKVMNIRTVLNKLEKPQGLYPNYLNPSSGQWGQHHVSVGGLGDSFYEYLL
KAWLMSDKTDLEAKKMYFDAVQAIETHLIRKSSSGLTYIAEWKGGLLEHKMGHLTCFAGG
MFALGADAAPEGMAQHYLELGAEIARTCHESYNRTFMKLGPEAFRFDGGVEAIATRQNEK
YYILRPEVMETYMYMWRLTHDPKYRKWAWEAVEALENHCRVNGGYSGLRDVYLLHESYDD
VQQSFFLAETLKYLYLIFSDDDLLPLEHWIFNSEAHLLPILPKDKKEVEIREE
|
| Enzyme 9 Number of Residues |
653 |
| Enzyme 9 Molecular Weight |
72969 |
| Enzyme 9 Theoretical pI |
6.44 |
| Enzyme 9 GO Classification |
| Function |
- binding
- calcium ion binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on glycosyl bonds
- hydrolase activity, hydrolyzing O-glycosyl compounds
- ion binding
- mannosidase activity
- mannosyl-oligosaccharide 1,2-alpha-mannosidase activity
- mannosyl-oligosaccharide mannosidase activity
|
| Process |
- biopolymer metabolism
- biopolymer modification
- macromolecule metabolism
- metabolism
- physiological process
- protein amino acid N-linked glycosylation
- protein amino acid glycosylation
- protein modification
|
| Component |
|
|
| Enzyme 9 General Function |
Not Available |
| Enzyme 9 Specific Function |
Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2) |
| Enzyme 9 Pathways |
- High-mannose type N-glycan biosynthesis (map00513
)
- N-Glycan biosynthesis (map00510
)
|
| Enzyme 9 Reactions |
- Hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
56202626  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
P33908  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
MA1A1_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>1146 bp
AATGCTGAAATTTCTGTCTTTGAAGTAAATATACGCTTTGTTGGTGGACTACTCTCAGCC
TACTATCTGTCTGGAGAAGAGATTTTTCGAAAGAAAGCAGTGGAACTTGGGGTAAAATTG
CTACCTGCATTTCATACTCCCTCTGGAATACCTTGGGCATTGCTGAATATGAAAAGTGGT
ATTGGAAGGAACTGGCCCTGGGCCTCTGGAGGCAGCAGTATTCTGGCAGAATTTGGAACC
CTGCATTTGGAGTTTATGCACTTGAGCCACTTATCAGGAAACCCCATCTTTGCTGAAAAG
GTAATGAATATTCGAACAGTACTGAACAAACTGGAAAAACCACAAGGCCTTTATCCTAAC
TATCTGAATCCCAGTAGTGGACAGTGGGGTCAACATCATGTATCAGTTGGAGGACTTGGA
GACAGCTTCTATGAGTATTTGCTGAAGGCCTGGTTAATGTCTGACAAGACAGATCTGGAA
GCTAAGAAGATGTATTTTGATGCTGTTCAGGCTATCGAGACTCATTTGATCCGCAAGTCT
AGCAGCGGACTAACTTATATCGCAGAGTGGAAAGGGGGCCTCCTGGAGCACAAGATGGGC
CACCTGACCTGCTTCGCGGGGGGCATGTTCGCACTCGGGGCTGATGCAGCTCCCGAAGGC
ATGGCCCAACACTACCTTGAACTCGGGGCTGAAATTGCCCGTACTTGTCATGAATCATAT
AATCGAACATTTATGAAACTGGGACCAGAAGCTTTCAGATTTGATGGTGGTGTTGAAGCC
ATCGCTACAAGACAAAATGAAAAATACTACATCTTACGGCCAGAAGTTATGGAGACTTAC
ATGTATATGTGGAGACTGACTCATGATCCAAAGTACAGGAAATGGGCCTGGGAAGCCGTA
GAGGCCTTGGAAAACCATTGCAGAGTGAATGGAGGCTATTCAGGCCTAAGGGATGTTTAC
CTTCTTCATGAGAGTTATGATGATGTGCAGCAGAGTTTCTTCCTGGCAGAGACATTGAAA
TATTTGTACCTAATATTTTCTGACGACGATCTTCTTCCACTGGAGCATTGGATCTTCAAT
AGCGAGGCACATCTTCTCCCTATCCTCCCTAAAGATAAAAAGGAAGTTGAAATCAGAGAG
GAATAA
|
| Enzyme 9 GenBank Gene ID |
AL022722  |
| Enzyme 9 GeneCard ID |
MAN1A1  |
| Enzyme 9 GenAtlas ID |
MAN1A1  |
| Enzyme 9 HGNC ID |
HGNC:6821  |
| Enzyme 9 Chromosome Location |
6 |
| Enzyme 9 Locus |
6q22 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- 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
]
- Bause E, Bieberich E, Rolfs A, Volker C, Schmidt B: Molecular cloning and primary structure of Man9-mannosidase from human kidney. Eur J Biochem. 1993 Oct 15;217(2):535-40. [PubMed
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
6927 |
| Enzyme 10 Name |
Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase |
| Enzyme 10 Synonyms |
- Dol-P-Man-dependent alpha(1-3-mannosyltransferase
- Not56-like protein
|
| Enzyme 10 Gene Name |
ALG3 |
| Enzyme 10 Protein Sequence |
>Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase
MAAGLRKRGRSGSAAQAEGLCKQWLQRAWQERRLLLREPRYTLLVAACLCLAEVGITFWV
IHRVAYTEIDWKAYMAEVEGVINGTYDYTQLQGDTGPLVYPAGFVYIFMGLYYATSRGTD
IRMAQNIFAVLYLATLLLVFLIYHQTCKVPPFVFFFMCCASYRVHSIFVLRLFNDPVAMV
LLFLSINLLLAQRWGWGCCFFSLAVSVKMNVLLFAPGLLFLLLTQFGFRGALPKLGICAG
LQVVLGLPFLLENPSGYLSRSFDLGRQFLFHWTVNWRFLPEALFLHRAFHLALLTAHLTL
LLLFALCRWHRTGESILSLLRDPSKRKVPPQPLTPNQIVSTLFTSNFIGICFSRSLHYQF
YVWYFHTLPYLLWAMPARWLTHLLRLLVLGLIELSWNTYPSTSCSSAALHICHAVILLQL
WLGPQPFPKSTQHSKKAH
|
| Enzyme 10 Number of Residues |
438 |
| Enzyme 10 Molecular Weight |
50127 |
| Enzyme 10 Theoretical pI |
9.69 |
| Enzyme 10 GO Classification |
| Function |
- catalytic activity
- mannosyltransferase activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
| — |
| Component |
- cell
- endoplasmic reticulum
- integral to membrane
- intracellular membrane-bound organelle
- intrinsic to membrane
- membrane
- membrane-bound organelle
- organelle
|
|
| Enzyme 10 General Function |
Not Available |
| Enzyme 10 Specific Function |
Adds the first Dol-P-Man derived mannose in an alpha 1,3 linkage to Man5GlcNAc2-PP-Dol |
| Enzyme 10 Pathways |
Not Available |
| Enzyme 10 Reactions |
Not Available |
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
- 41-61
95-115
123-143
149-169
172-192
203-223
231-251
289-309
332-352
356-376
407-427
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
1654000  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
Q92685  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
ALG3_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>1317 bp
ATGGCGGCTGGGCTGCGGAAACGCGGCCGGTCCGGTTCCGCGGCCCAGGCAGAGGGACTC
TGCAAGCAATGGCTGCAGCGCGCCTGGCAAGAGCGGCGCCTGCTGCTGCGGGAGCCGCGC
TACACGCTGCTGGTGGCCGCCTGCCTCTGCCTGGCGGAGGTGGGCATCACCTTCTGGGTC
ATTCACAGGGTGGCATACACAGAGATTGACTGGAAGGCCTACATGGCCGAGGTAGAAGGC
GTCATCAATGGTACCTATGACTATACCCAACTGCAGGGTGACACCGGACCACTTGTGTAC
CCAGCTGGTTTCGTGTACATCTTTATGGGGTTGTACTATGCCACCAGCCGAGGCACTGAC
ATCCGCATGGCCCAGAACATCTTTGCTGTGCTCTACCTGGCTACCTTGCTGCTTGTCTTC
TTGATCTATCACCAGACCTGCAAGGTACCTCCCTTCGTCTTTTTCTTCATGTGCTGCGCC
TCTTACCGTGTCCACTCCATCTTTGTGCTGCGGCTCTTCAATGACCCAGTGGCCATGGTG
CTGCTCTTCCTCAGTATCAACCTCCTGCTGGCCCAGCGCTGGGGCTGGGGCTGCTGCTTT
TTCAGCCTGGCAGTCTCTGTGAAGATGAATGTGCTGCTCTTCGCCCCTGGGTTACTGTTT
CTTCTCCTCACACAGTTTGGCTTCCGTGGGGCCCTCCCCAAGCTGGGAATCTGTGCTGGC
CTTCAGGTGGTGCTGGGGCTGCCCTTCCTGCTGGAGAACCCCAGCGGCTACCTGTCCCGC
TCCTTTGACCTTGGCCGCCAGTTTCTGTTCCACTGGACAGTGAACTGGCGCTTCCTCCCA
GAGGCGCTCTTCCTGCATCGAGCCTTCCACCTGGCCCTGTTGACTGCCCACCTCACCCTG
CTCCTGCTGTTTGCCCTCTGCAGGTGGCACAGGACAGGGGAAAGTATCTTGTCGCTGCTG
AGGGATCCCTCCAAAAGGAAGGTTCCACCCCAGCCCCTTACACCCAACCAGATCGTTTCT
ACCCTCTTCACCTCCAACTTCATTGGCATCTGCTTCAGCCGCTCCCTCCACTACCAGTTC
TACGTCTGGTATTTCCACACACTGCCCTACCTCCTGTGGGCCATGCCTGCACGGTGGCTC
ACACACCTGCTCAGGTTGTTGGTGCTGGGGCTCATCGAGCTCTCCTGGAACACATACCCT
TCCACATCCTGCAGCTCTGCTGCCCTGCACATATGCCATGCCGTCATCCTGCTGCAGCTC
TGGCTGGGCCCGCAGCCTTTCCCCAAGAGCACCCAACACAGCAAGAAAGCCCACTGA
|
| Enzyme 10 GenBank Gene ID |
Y09022  |
| Enzyme 10 GeneCard ID |
ALG3  |
| Enzyme 10 GenAtlas ID |
ALG3  |
| Enzyme 10 HGNC ID |
HGNC:23056  |
| Enzyme 10 Chromosome Location |
3 |
| Enzyme 10 Locus |
3q27.1 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Korner C, Knauer R, Stephani U, Marquardt T, Lehle L, von Figura K: Carbohydrate deficient glycoprotein syndrome type IV: deficiency of dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase. EMBO J. 1999 Dec 1;18(23):6816-22. [PubMed
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
7418 |
| Enzyme 11 Name |
Glycophorin B precursor |
| Enzyme 11 Synonyms |
- PAS-3
- Sialoglycoprotein delta
- SS-active sialoglycoprotein
- CD235b antigen
|
| Enzyme 11 Gene Name |
GYPB |
| Enzyme 11 Protein Sequence |
>Glycophorin B precursor
MYGKIIFVLLLSEIVSISALSTTEVAMHTSTSSSVTKSYISSQTNGETGQLVHRFTVPAP
VVIILIILCVMAGIIGTILLISYTIRRLIKA
|
| Enzyme 11 Number of Residues |
91 |
| Enzyme 11 Molecular Weight |
9796 |
| Enzyme 11 Theoretical pI |
9.73 |
| Enzyme 11 GO Classification |
| Function |
| — |
| Process |
| — |
| Component |
|
|
| Enzyme 11 General Function |
Not Available |
| Enzyme 11 Specific Function |
This protein is a minor sialoglycoprotein in erythrocyte membranes |
| Enzyme 11 Pathways |
Not Available |
| Enzyme 11 Reactions |
Not Available |
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
183313  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
P06028  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
GLPB_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>276 bp
ATGTATGGAAAAATAATCTTTGTATTACTATTGTCAGAAATTGTGAGCATATCAGCATTA
AGTACCACTGAGGTGGCAATGCACACTTCAACCTCTTCTTCAGTCACAAAGAGTTACATC
TCATCACAGACAAATGGAGAAACGGGACAACTTGTCCATCGTTTCACTGTACCAGCTCCT
GTAGTGATAATACTCATTATTTTGTGTGTGATGGCTGGTATTATTGGAACGATCCTCTTA
ATTTCTTACACTATTCGCCGACTGATAAAGGCATGA
|
| Enzyme 11 GenBank Gene ID |
J02982  |
| Enzyme 11 GeneCard ID |
GYPB  |
| Enzyme 11 GenAtlas ID |
GYPB  |
| Enzyme 11 HGNC ID |
HGNC:4703  |
| Enzyme 11 Chromosome Location |
4 |
| Enzyme 11 Locus |
4q28-q31 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Siebert PD, Fukuda M: Molecular cloning of a human glycophorin B cDNA: nucleotide sequence and genomic relationship to glycophorin A. Proc Natl Acad Sci U S A. 1987 Oct;84(19):6735-9. [PubMed
]
- Tate CG, Tanner MJ: Isolation of cDNA clones for human erythrocyte membrane sialoglycoproteins alpha and delta. Biochem J. 1988 Sep 15;254(3):743-50. [PubMed
]
- Kudo S, Fukuda M: Structural organization of glycophorin A and B genes: glycophorin B gene evolved by homologous recombination at Alu repeat sequences. Proc Natl Acad Sci U S A. 1989 Jun;86(12):4619-23. [PubMed
]
- Huang CH, Blumenfeld OO: Molecular genetics of human erythrocyte MiIII and MiVI glycophorins. Use of a pseudoexon in construction of two delta-alpha-delta hybrid genes resulting in antigenic diversification. J Biol Chem. 1991 Apr 15;266(11):7248-55. [PubMed
]
- Blanchard D, Dahr W, Hummel M, Latron F, Beyreuther K, Cartron JP: Glycophorins B and C from human erythrocyte membranes. Purification and sequence analysis. J Biol Chem. 1987 Apr 25;262(12):5808-11. [PubMed
]
- Dahr W, Beyreuther K, Moulds J, Unger P: Hybrid glycophorins from human erythrocyte membranes. I. Isolation and complete structural analysis of the hybrid sialoglycoprotein from Dantu-positive red cells of the N.E. variety. Eur J Biochem. 1987 Jul 1;166(1):31-6. [PubMed
]
- Huang CH, Spruell P, Moulds JJ, Blumenfeld OO: Molecular basis for the human erythrocyte glycophorin specifying the Miltenberger class I (MiI) phenotype. Blood. 1992 Jul 1;80(1):257-63. [PubMed
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
11077 |
| Enzyme 12 Name |
Mannosyl-oligosaccharide 1,2-alpha-mannosidase IC |
| Enzyme 12 Synonyms |
- Processing alpha-1,2-mannosidase IC
- Alpha-1,2-mannosidase IC
- Mannosidase alpha class 1C member 1
- HMIC
|
| Enzyme 12 Gene Name |
MAN1C1 |
| Enzyme 12 Protein Sequence |
>Mannosyl-oligosaccharide 1,2-alpha-mannosidase IC
MLMRKVPGFVPASPWGLRLPQKFLFLLFLSGLVTLCFGALFLLPHSSRLKRLFLAPRTQQ
PGLEVVAEIAGHAPAREQEPPPNPAPAAPAPGEDDPSSWASPRRRKGGLRRTRPTGPREE
ATAARGNSIPASRPGDEGVPFRFDFNAFRSRLRHPVLGTRADESQEPQSQVRAQREKIKE
MMQFAWQSYKRYAMGKNELRPLTKDGYEGNMFGGLSGATVIDSLDTLYLMELKEEFQEAK
AWVGESFHLNVSGEASLFEVNIRYIGGLLSAFYLTGEEVFRIKAIRLGEKLLPAFNTPTG
IPKGVVSFKSGNWGWATAGSSSILAEFGSLHLEFLHLTELSGNQVFAEKVRNIRKVLRKI
EKPFGLYPNFLSPVSGNWVQHHVSVGGLGDSFYEYLIKSWLMSGKTDMEAKNMYYEALEA
IETYLLNVSPGGLTYIAEWRGGILDHKMGHLACFSGGMIALGAEDAKEEKRAHYRELAAQ
ITKTCHESYARSDTKLGPEAFWFNSGREAVATQLSESYYILRPEVVESYMYLWRQTHNPI
YREWGWEVVLALEKYCRTEAGFSGIQDVYSSTPNHDNKQQSFFLAETLKYLYLLFSEDDL
LSLEDWVFNTEAHPLPVNHSDSSGRAWGRH
|
| Enzyme 12 Number of Residues |
630 |
| Enzyme 12 Molecular Weight |
70911 |
| Enzyme 12 Theoretical pI |
Not Available |
| Enzyme 12 GO Classification |
| Function |
- binding
- calcium ion binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on glycosyl bonds
- hydrolase activity, hydrolyzing O-glycosyl compounds
- ion binding
- mannosidase activity
- mannosyl-oligosaccharide 1,2-alpha-mannosidase activity
- mannosyl-oligosaccharide mannosidase activity
|
| Process |
- biopolymer metabolism
- biopolymer modification
- macromolecule metabolism
- metabolism
- physiological process
- protein amino acid N-linked glycosylation
- protein amino acid glycosylation
- protein modification
|
| Component |
|
|
| Enzyme 12 General Function |
Not Available |
| Enzyme 12 Specific Function |
Involved in the maturation of Asn-linked oligosaccharides. Trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce first Man(8)GlcNAc(2) then Man(6)GlcNAc and a small amount of Man(5)GlcNAc |
| Enzyme 12 Pathways |
- Glycan structures - biosynthesis 1 (map01030
)
- High-mannose type N-glycan biosynthesis (map00513
)
- N-Glycan biosynthesis (map00510
)
|
| Enzyme 12 Reactions |
- H2O + (alpha-D-mannosyl)7-beta-D-mannosyl-diacetylchitobiosyl-L-asparagine, isoform A (protein) --> (alpha-D-mannosyl)6-beta-D-mannosyl-diacetylchitobiosyl-L-asparagine (protein) + D-Mannose
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
9664312  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
Q9NR34  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
MA1C1_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
Not Available |
| Enzyme 12 GenBank Gene ID |
AF261655  |
| Enzyme 12 GeneCard ID |
Not Available |
| Enzyme 12 GenAtlas ID |
MAN1C1  |
| Enzyme 12 HGNC ID |
HGNC:19080  |
| Enzyme 12 Chromosome Location |
Not Available |
| Enzyme 12 Locus |
Not Available |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- Tremblay LO, Herscovics A: Characterization of a cDNA encoding a novel human Golgi alpha 1, 2-mannosidase (IC) involved in N-glycan biosynthesis. J Biol Chem. 2000 Oct 13;275(41):31655-60. [PubMed
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
15209 |
| Enzyme 13 Name |
cDNA FLJ78173, highly similar to Homo sapiens hexokinase 1 (HK1) mRNA |
| Enzyme 13 Synonyms |
Not Available |
| Enzyme 13 Gene Name |
Not Available |
| Enzyme 13 Protein Sequence |
>cDNA FLJ78173, highly similar to Homo sapiens hexokinase 1 (HK1) mRNA
MIAAQLLAYYFTELKDDQVKKIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTAT
VKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESEVYDTPENIVH
GSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGV
EGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYME
ELRHIDLVEGDEGRMCINTEWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGM
YLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGLHNAKEILTRLG
VEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTH
PQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETLAHFHLT
KDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRV
LLVKIRSGKKRTVEMHNKIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGF
TFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLLRDAIKRREEFDLDVVAVVNDTVG
TMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGCLDD
IRTHYDRLVDEYSLNAGKQGYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRG
IFETKFLSQIESDRLALLQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAA
VVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMHQTVKELSPKCNVSFLLSEDGSGKG
AALITAVGVRLRTEASS
|
| Enzyme 13 Number of Residues |
917 |
| Enzyme 13 Molecular Weight |
102388 |
| Enzyme 13 Theoretical pI |
6.70 |
| Enzyme 13 GO Classification |
Not Available |
| Enzyme 13 General Function |
Not Available |
| Enzyme 13 Specific Function |
Not Available |
| Enzyme 13 Pathways |
Not Available |
| Enzyme 13 Reactions |
Not Available |
| Enzyme 13 Pfam Domain Function |
Not Available |
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
158257456  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
A8K7J7  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
A8K7J7_HUMAN  |
| Enzyme 13 PDB ID |
1HKB  |
| Enzyme 13 PDB File |
Show |
| Enzyme 13 3D Structure |
|
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>2754 bp
ATGATCGCCGCGCAGCTCCTGGCCTATTACTTCACGGAGCTGAAGGATGACCAGGTCAAA
AAGATTGACAAGTATCTGTATGCCATGCGGCTCTCCGATGAAACTCTCATAGATATCATG
ACTCGCTTCAGGAAGGAGATGAAGAATGGCCTCTCCCGGGATTTTAATCCAACAGCCACA
GTCAAGATGTTGCCAACATTCGTAAGGTCCATTCCTGATGGCTCTGAAAAGGGAGATTTC
ATTGCCCTGGATCTTGGTGGGTCTTCCTTTCGAATTCTGCGGGTGCAAGTGAATCATGAG
AAAAACCAGAATGTTCACATGGAGTCCGAGGTTTATGACACCCCAGAGAACATCGTGCAC
GGCAGTGGAAGCCAGCTTTTTGATCATGTTGCTGAGTGCCTGGGAGATTTCATGGAGAAA
AGGAAGATCAAGGACAAGAAGTTACCTGTGGGATTCACGTTTTCTTTTCCTTGCCAACAA
TCCAAAATAGATGAGGCCATCCTGATCACCTGGACAAAGCGATTTAAAGCGAGCGGAGTG
GAAGGAGCAGATGTGGTCAAACTGCTTAACAAAGCCATCAAAAAGCGAGGGGACTATGAT
GCCAACATCGTAGCTGTGGTGAATGACACAGTGGGCACCATGATGACCTGTGGCTATGAC
GACCAGCACTGTGAAGTCGGCCTGATCATCGGCACTGGCACCAATGCTTGCTACATGGAG
GAACTGAGGCACATTGATCTGGTGGAAGGAGACGAGGGGAGGATGTGTATCAATACAGAA
TGGGGAGCCTTTGGAGACGATGGATCATTAGAAGACATCCGGACAGAGTTTGACAGGGAG
ATAGACCGGGGATCCCTCAACCCTGGAAAACAGCTGTTTGAGAAGATGGTCAGTGGCATG
TACTTGGGAGAGCTGGTTCGACTGATCCTAGTCAAGATGGCCAAGGAGGGCCTCTTATTT
GAAGGGCGGATCACCCCGGAGCTGCTCACCCGAGGGAAGTTTAACACCAGTGATGTGTCA
GCCATCGAAAAGAATAAGGAAGGCCTCCACAATGCCAAAGAAATCCTGACCCGCCTGGGA
GTGGAGCCGTCCGATGATGACTGTGTCTCAGTCCAGCACGTTTGCACCATTGTCTCATTT
CGCTCAGCCAACTTGGTGGCTGCCACACTGGGCGCCATCTTGAACCGCCTGCGTGATAAC
AAGGGCACACCCAGGCTGCGGACCACGGTTGGTGTCGACGGATCTCTTTACAAGACGCAC
CCACAGTATTCCCGGCGTTTCCACAAGACTCTAAGGCGCTTGGTGCCAGACTCCGATGTG
CGCTTCCTCCTCTCGGAGAGTGGCAGCGGCAAGGGGGCTGCCATGGTGACGGCGGTGGCC
TACCGCTTGGCCGAGCAGCACCGGCAGATAGAGGAGACCCTGGCTCATTTCCACCTCACC
AAAGACATGCTGCTGGAGGTGAAGAAGAGGATGCGGGCCGAGATGGAGCTGGGGCTGAGG
AAGCAGACGCACAACAATGCCGTGGTTAAGATGCTGCCCTCCTTCGTCCGGAGAACTCCC
GACGGGACCGAGAATGGTGACTTCTTGGCCCTGGATCTTGGAGGAACCAATTTCCGTGTG
CTGCTGGTGAAAATCCGTAGTGGGAAAAAGAGAACGGTGGAAATGCACAACAAGATCTAC
GCCATTCCTATTGAAATCATGCAGGGCACTGGGGAAGAGCTGTTTGATCACATTGTCTCC
TGCATCTCTGACTTCTTGGACTACATGGGGATCAAAGGCCCCAGGATGCCTCTGGGCTTC
ACGTTCTCATTTCCCTGCCAGCAGACGAGTCTGGACGCGGGAATCTTGATCACGTGGACA
AAGGGTTTTAAGGCAACAGACTGCGTGGGCCACGATGTAGTCACCTTACTAAGGGATGCG
ATAAAAAGGAGAGAGGAATTTGACCTGGACGTGGTGGCTGTGGTCAACGACACAGTGGGC
ACCATGATGACCTGTGCTTATGAGGAGCCCACCTGTGAGGTTGGACTCATTGTTGGGACC
GGCAGCAATGCCTGCTACATGGAGGAGATGAAGAACGTGGAGATGGTGGAGGGGGACCAG
GGGCAGATGTGCATCAACATGGAGTGGGGGGCCTTTGGGGACAACGGGTGTCTGGATGAT
ATCAGGACACACTACGACAGACTGGTGGACGAATATTCCCTAAATGCTGGGAAACAAGGG
TATGAGAAGATGATCAGTGGTATGTACCTGGGTGAAATCGTCCGCAACATCTTAATCGAC
TTCACCAAGAAGGGATTCCTCTTCCGAGGGCAGATCTCTGAGACGCTGAAGACCCGGGGC
ATCTTTGAGACCAAGTTTCTCTCTCAGATCGAGAGTGACCGATTAGCACTGCTCCAGGTC
CGGGCTATCCTCCAGCAGCTAGGTCTGAATAGCACCTGCGATGACAGTATCCTCGTCAAG
ACAGTGTGCGGGGTGGTGTCCAGGAGGGCCGCACAGCTGTGTGGCGCAGGCATGGCTGCG
GTTGTGGATAAGATCCGCGAGAACAGAGGACTGGACCGTCTGAATGTGACTGTGGGAGTG
GACGGGACACTCTACAAGCTTCATCCACACTTCTCCAGAATCATGCACCAGACGGTGAAG
GAACTGTCACCAAAATGTAACGTGTCCTTCCTCCTGTCTGAGGATGGCAGCGGCAAGGGG
GCCGCCCTCATCACGGCCGTGGGCGTGCGGTTACGCACAGAGGCAAGCAGCTAA
|
| Enzyme 13 GenBank Gene ID |
AK292012  |
| Enzyme 13 GeneCard ID |
A8K7J7  |
| Enzyme 13 GenAtlas ID |
Not Available |
| Enzyme 13 HGNC ID |
Not Available |
| Enzyme 13 Chromosome Location |
Not Available |
| Enzyme 13 Locus |
Not Available |
| Enzyme 13 SNPs |
Not Available |
| Enzyme 13 General References |
Not Available |
| Enzyme 13 Metabolite References |
Not Available |
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Enzyme 14
[top]
|
| Enzyme 14 ID |
15260 |
| Enzyme 14 Name |
N-acetylglucosamine-1-phosphotransferase subunits alpha/beta |
| Enzyme 14 Synonyms |
- GlcNAc-1-phosphotransferase subunits alpha/beta
- Stealth protein GNPTAB
- UDP-N-acetylglucosamine-1-phosphotransferase subunits alpha/beta
- Contains: RecName: N-acetylglucosamine-1-phosphotransferase subunit alpha
- Contains: RecName: N-acetylglucosamine-1-phosphotransferase subunit beta
|
| Enzyme 14 Gene Name |
GNPTAB |
| Enzyme 14 Protein Sequence |
>N-acetylglucosamine-1-phosphotransferase subunits alpha/beta
MLFKLLQRQTYTCLSHRYGLYVCFLGVVVTIVSAFQFGEVVLEWSRDQYHVLFDSYRDNI
AGKSFQNRLCLPMPIDVVYTWVNGTDLELLKELQQVREQMEEEQKAMREILGKNTTEPTK
KSEKQLECLLTHCIKVPMLVLDPALPANITLKDLPSLYPSFHSASDIFNVAKPKNPSTNV
SVVVFDSTKDVEDAHSGLLKGNSRQTVWRGYLTTDKEVPGLVLMQDLAFLSGFPPTFKET
NQLKTKLPENLSSKVKLLQLYSEASVALLKLNNPKDFQELNKQTKKNMTIDGKELTISPA
YLLWDLSAISQSKQDEDISASRFEDNEELRYSLRSIERHAPWVRNIFIVTNGQIPSWLNL
DNPRVTIVTHQDVFRNLSHLPTFSSPAIESHIHRIEGLSQKFIYLNDDVMFGKDVWPDDF
YSHSKGQKVYLTWPVPNCAEGCPGSWIKDGYCDKACNNSACDWDGGDCSGNSGGSRYIAG
GGGTGSIGVGQPWQFGGGINSVSYCNQGCANSWLADKFCDQACNVLSCGFDAGDCGQDHF
HELYKVILLPNQTHYIIPKGECLPYFSFAEVAKRGVEGAYSDNPIIRHASIANKWKTIHL
IMHSGMNATTIHFNLTFQNTNDEEFKMQITVEVDTREGPKLNSTAQKGYENLVSPITLLP
EAEILFEDIPKEKRFPKFKRHDVNSTRRAQEEVKIPLVNISLLPKDAQLSLNTLDLQLEH
GDITLKGYNLSKSALLRSFLMNSQHAKIKNQAIITDETNDSLVAPQEKQVHKSILPNSLG
VSERLQRLTFPAVSVKVNGHDQGQNPPLDLETTARFRVETHTQKTIGGNVTKEKPPSLIV
PLESQMTKEKKITGKEKENSRMEENAENHIGVTEVLLGRKLQHYTDSYLGFLPWEKKKYF
QDLLDEEESLKTQLAYFTDSKNTGRQLKDTFADSLRYVNKILNSKFGFTSRKVPAHMPHM
IDRIVMQELQDMFPEEFDKTSFHKVRHSEDMQFAFSYFYYLMSAVQPLNISQVFDEVDTD
QSGVLSDREIRTLATRIHELPLSLQDLTGLEHMLINCSKMLPADITQLNNIPPTQESYYD
PNLPPVTKSLVTNCKPVTDKIHKAYKDKNKYRFEIMGEEEIAFKMIRTNVSHVVGQLDDI
RKNPRKFVCLNDNIDHNHKDAQTVKAVLRDFYESMFPIPSQFELPREYRNRFLHMHELQE
WRAYRDKLKFWTHCVLATLIMFTIFSFFAEQLIALKRKIFPRRRIHKEASPNRIRV
|
| Enzyme 14 Number of Residues |
1256 |
| Enzyme 14 Molecular Weight |
143623 |
| Enzyme 14 Theoretical pI |
7.17 |
| Enzyme 14 GO Classification |
| Function |
- binding
- calcium ion binding
- cation binding
- ion binding
- protein binding
- transcription factor binding
|
| Process |
- cell differentiation
- cellular process
|
| Component |
- cell
- intracellular membrane-bound organelle
- membrane
- membrane-bound organelle
- nucleus
- organelle
|
|
| Enzyme 14 General Function |
Not Available |
| Enzyme 14 Specific Function |
Catalyzes the formation of mannose 6-phosphate (M6P) markers on high mannose type oligosaccharides in the Golgi apparatus. M6P residues are required to bind to the M6P receptors (MPR), which mediate the vesicular transport of lysosomal enzymes to the endosomal/prelysosomal compartment |
| Enzyme 14 Pathways |
Not Available |
| Enzyme 14 Reactions |
Not Available |
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
74474848  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
Q3T906  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
GNPTA_HUMAN  |
| Enzyme 14 PDB ID |
Not Available |
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>3771 bp
ATGCTGTTCAAGCTCCTGCAGAGACAGACCTATACCTGCCTGTCCCACAGGTATGGGCTC
TACGTGTGCTTCTTGGGCGTCGTTGTCACCATCGTCTCCGCCTTCCAGTTCGGAGAGGTG
GTTCTGGAATGGAGCCGAGATCAATACCATGTTTTGTTTGATTCCTATAGAGACAATATT
GCTGGAAAGTCCTTTCAGAATCGGCTTTGTCTGCCCATGCCGATTGACGTTGTTTACACC
TGGGTGAATGGCACAGATCTTGAACTACTGAAGGAACTACAGCAGGTCAGAGAACAGATG
GAGGAGGAGCAGAAAGCAATGAGAGAAATCCTTGGGAAAAACACAACGGAACCTACTAAG
AAGAGTGAGAAGCAGTTAGAGTGTTTGCTAACACACTGCATTAAGGTGCCAATGCTTGTC
CTGGACCCAGCCCTGCCAGCCAACATCACCCTGAAGGACCTGCCATCTCTTTATCCTTCT
TTTCATTCTGCCAGTGACATTTTCAATGTTGCAAAACCAAAAAACCCTTCTACCAATGTC
TCAGTTGTTGTTTTTGACAGTACTAAGGATGTTGAAGATGCCCACTCTGGACTGCTTAAA
GGAAATAGCAGACAGACAGTATGGAGGGGCTACTTGACAACAGATAAAGAAGTCCCTGGA
TTAGTGCTAATGCAAGATTTGGCTTTCCTGAGTGGATTTCCACCAACATTCAAGGAAACA
AATCAACTAAAAACAAAATTGCCAGAAAATCTTTCCTCTAAAGTCAAACTGTTGCAGTTG
TATTCAGAGGCCAGTGTAGCGCTTCTAAAACTGAATAACCCCAAGGATTTTCAAGAATTG
AATAAGCAAACTAAGAAGAACATGACCATTGATGGAAAAGAACTGACCATAAGTCCTGCA
TATTTATTATGGGATCTGAGCGCCATCAGCCAGTCTAAGCAGGATGAAGACATCTCTGCC
AGTCGTTTTGAAGATAACGAAGAACTGAGGTACTCATTGCGATCTATCGAGAGGCATGCA
CCATGGGTTCGGAATATTTTCATTGTCACCAACGGGCAGATTCCATCCTGGCTGAACCTT
GACAATCCTCGAGTGACAATAGTAACACACCAGGATGTTTTTCGAAATTTGAGCCACTTG
CCTACCTTTAGTTCACCTGCTATTGAAAGTCACATTCATCGCATCGAAGGGCTGTCCCAG
AAGTTTATTTACCTAAATGATGATGTCATGTTTGGGAAGGATGTCTGGCCAGATGATTTT
TACAGTCACTCCAAAGGCCAGAAGGTTTATTTGACATGGCCTGTGCCAAACTGTGCCGAG
GGCTGCCCAGGTTCCTGGATTAAGGATGGCTATTGTGACAAGGCTTGTAATAATTCAGCC
TGCGATTGGGATGGTGGGGATTGCTCTGGAAACAGTGGAGGGAGTCGCTATATTGCAGGA
GGTGGAGGTACTGGGAGTATTGGAGTTGGACAGCCCTGGCAGTTTGGTGGAGGAATAAAC
AGTGTCTCTTACTGTAATCAGGGATGTGCGAATTCCTGGCTCGCTGATAAGTTCTGTGAC
CAAGCATGCAATGTCTTGTCCTGTGGGTTTGATGCTGGCGACTGTGGGCAAGATCATTTT
CATGAATTGTATAAAGTGATCCTTCTCCCAAACCAGACTCACTATATTATTCCAAAAGGT
GAATGCCTGCCTTATTTCAGCTTTGCAGAAGTAGCCAAAAGAGGAGTTGAAGGTGCCTAT
AGTGACAATCCAATAATTCGACATGCTTCTATTGCCAACAAGTGGAAAACCATCCACCTC
ATAATGCACAGTGGAATGAATGCCACCACAATACATTTTAATCTCACGTTTCAAAATACA
AACGATGAAGAGTTCAAAATGCAGATAACAGTGGAGGTGGACACAAGGGAGGGACCAAAA
CTGAATTCTACAGCCCAGAAGGGTTACGAAAATTTAGTTAGTCCCATAACACTTCTTCCA
GAGGCGGAAATCCTTTTTGAGGATATTCCCAAAGAAAAACGCTTCCCGAAGTTTAAGAGA
CATGATGTTAACTCAACAAGGAGAGCCCAGGAAGAGGTGAAAATTCCCCTGGTAAATATT
TCACTCCTTCCAAAAGACGCCCAGTTGAGTCTCAATACCTTGGATTTGCAACTGGAACAT
GGAGACATCACTTTGAAAGGATACAATTTGTCCAAGTCAGCCTTGCTGAGATCATTTCTG
ATGAACTCACAGCATGCTAAAATAAAAAATCAAGCTATAATAACAGATGAAACAAATGAC
AGTTTGGTGGCTCCACAGGAAAAACAGGTTCATAAAAGCATCTTGCCAAACAGCTTAGGA
GTGTCTGAAAGATTGCAGAGGTTGACTTTTCCTGCAGTGAGTGTAAAAGTGAATGGTCAT
GACCAGGGTCAGAATCCACCCCTGGACTTGGAGACCACAGCAAGATTTAGAGTGGAAACT
CACACCCAAAAAACCATAGGCGGAAATGTGACAAAAGAAAAGCCCCCATCTCTGATTGTT
CCACTGGAAAGCCAGATGACAAAAGAAAAGAAAATCACAGGGAAAGAAAAAGAGAACAGT
AGAATGGAGGAAAATGCTGAAAATCACATAGGCGTTACTGAAGTGTTACTTGGAAGAAAG
CTGCAGCATTACACAGATAGTTACTTGGGCTTTTTGCCATGGGAGAAAAAAAAGTATTTC
CAAGATCTTCTCGACGAAGAAGAGTCATTGAAGACACAATTGGCATACTTCACTGATAGC
AAAAATACTGGGAGGCAACTAAAAGATACATTTGCAGATTCCCTCAGATATGTAAATAAA
ATTCTAAATAGCAAGTTTGGATTCACATCGCGGAAAGTCCCTGCTCACATGCCTCACATG
ATTGACCGGATTGTTATGCAAGAACTGCAAGATATGTTCCCTGAAGAATTTGACAAGACG
TCATTTCACAAAGTGCGCCATTCTGAGGATATGCAGTTTGCCTTCTCTTATTTTTATTAT
CTCATGAGTGCAGTGCAGCCACTGAATATATCTCAAGTCTTTGATGAAGTTGATACAGAT
CAATCTGGTGTCTTGTCTGACAGAGAAATCCGAACACTGGCTACCAGAATTCACGAACTG
CCGTTAAGTTTGCAGGATTTGACAGGTCTGGAACACATGCTAATAAATTGCTCAAAAATG
CTTCCTGCTGATATCACGCAGCTAAATAATATTCCACCAACTCAGGAATCCTACTATGAT
CCCAACCTGCCACCGGTCACTAAAAGTCTAGTAACAAACTGTAAACCAGTAACTGACAAA
ATCCACAAAGCATATAAGGACAAAAACAAATATAGGTTTGAAATCATGGGAGAAGAAGAA
ATCGCTTTTAAAATGATTCGTACCAACGTTTCTCATGTGGTTGGCCAGTTGGATGACATA
AGAAAAAACCCTAGGAAGTTTGTTTGCCTGAATGACAACATTGACCACAATCATAAAGAT
GCTCAGACAGTGAAGGCTGTTCTCAGGGACTTCTATGAATCCATGTTCCCCATACCTTCC
CAATTTGAACTGCCAAGAGAGTATCGAAACCGTTTCCTTCATATGCATGAGCTGCAGGAA
TGGAGGGCTTATCGAGACAAATTGAAGTTTTGGACCCATTGTGTACTAGCAACATTGATT
ATGTTTACTATATTCTCATTTTTTGCTGAGCAGTTAATTGCACTTAAGCGGAAGATATTT
CCCAGAAGGAGGATACACAAAGAAGCTAGTCCCAATCGAATCAGAGTATAG
|
| Enzyme 14 GenBank Gene ID |
AM085438  |
| Enzyme 14 GeneCard ID |
Q3T906  |
| Enzyme 14 GenAtlas ID |
GNPTAB  |
| Enzyme 14 HGNC ID |
HGNC:29670  |
| Enzyme 14 Chromosome Location |
12 |
| Enzyme 14 Locus |
12q23.2 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- Nagase T, Ishikawa K, Kikuno R, Hirosawa M, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Oct 29;6(5):337-45. [PubMed
]
- Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed
]
|
| Enzyme 14 Metabolite References |
Not Available |