|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5568 |
| Enzyme 1 Name |
Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase |
| Enzyme 1 Synonyms |
- UDP-GlcNAc-2-epimerase/ManAc kinase[Includes: UDP-N- acetylglucosamine 2-epimerase
- Uridine diphosphate-N- acetylglucosamine-2-epimerase
- UDP-GlcNAc-2-epimerase
- N- acetylmannosamine kinase
- ManAc kinase]
|
| Enzyme 1 Gene Name |
GNE |
| Enzyme 1 Protein Sequence |
>Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
MEKNGNNRKLRVCVATCNRADYSKLAPIMFGIKTEPEFFELDVVVLGSHLIDDYGNTYRM
IEQDDFDINTRLHTIVRGEDEAAMVESVGLALVKLPDVLNRLKPDIMIVHGDRFDALALA
TSAALMNIRILHIEGGEVSGTIDDSIRHAITKLAHYHVCCTRSAEQHLISMCEDHDRILL
AGCPSYDKLLSAKNKDYMSIIRMWLGDDVKSKDYIVALQHPVTTDIKHSIKMFELTLDAL
ISFNKRTLVLFPNIDAGSKEMVRVMRKKGIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGN
SSCGVREVGAFGTPVINLGTRQIGRETGENVLHVRDADTQDKILQALHLQFGKQYPCSKI
YGDGNAVPRILKFLKSIDLQEPLQKKFCFPPVKENISQDIDHILETLSALAVDLGGTNLR
VAIVSMKGEIVKKYTQFNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNP
REGIVLHSTKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTL
ITGTGIGGGIIHQHELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREA
KKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNAKAQSILRTAGTALGLGVVNILHTM
NPSLVILSGVLASHYIHIVKDVIRQQALSSVQDVDVVVSDLVDPALLGAASMVLDYTTRR
IY
|
| Enzyme 1 Number of Residues |
722 |
| Enzyme 1 Molecular Weight |
79276 |
| Enzyme 1 Theoretical pI |
6.79 |
| Enzyme 1 GO Classification |
| Function |
- UDP-N-acetylglucosamine 2-epimerase activity
- catalytic activity
- isomerase activity
- racemase and epimerase activity
- racemase and epimerase activity, acting on carbohydrates and derivatives
|
| Process |
- N-acetylglucosamine metabolism
- UDP-N-acetylglucosamine metabolism
- amine metabolism
- amino sugar metabolism
- carbohydrate biosynthesis
- glucosamine metabolism
- lipopolysaccharide biosynthesis
- macromolecule biosynthesis
- macromolecule metabolism
- metabolism
- nitrogen compound metabolism
- physiological process
- polysaccharide biosynthesis
|
| Component |
| — |
|
| Enzyme 1 General Function |
Cell wall/membrane/envelope biogenesis |
| Enzyme 1 Specific Function |
Regulates and initiates biosynthesis of N- acetylneuraminic acid (NeuAc), a precursor of sialic acids. Plays an essential role in early development. Required for normal sialylation in hematopoietic cells. Sialylation is implicated in cell adhesion, signal transduction, tumorigenicity and metastatic behavior of malignant cells |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- UDP-N-acetyl-D-glucosamine = UDP-N-acetyl-D-mannosamine
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
4775362  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q9Y223  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
GLCNE_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>2169 bp
ATGGAGAAGAATGGAAATAACCGAAAGCTGCGGGTTTGTGTTGCTACTTGTAACCGTGCA
GATTATTCTAAACTTGCCCCGATCATGTTTGGCATTAAAACCGAACCTGAGTTCTTTGAA
CTTGATGTTGTGGTACTTGGCTCTCACCTGATAGATGACTATGGAAATACATATCGAATG
ATTGAACAAGATGACTTTGACATTAACACCAGGCTACACACAATTGTGAGGGGAGAAGAT
GAGGCAGCCATGGTGGAGTCAGTAGGCCTGGCCCTAGTGAAGCTGCCAGATGTCCTTAAT
CGCCTGAAGCCTGATATCATGATTGTTCATGGAGACAGGTTTGATGCCCTGGCTCTGGCC
ACATCTGCTGCCTTGATGAACATCCGAATCCTTCACATTGAAGGTGGGGAAGTCAGTGGG
ACCATTGATGACTCTATCAGACATGCCATAACAAAACTGGCTCATTATCATGTGTGCTGC
ACCCGCAGTGCAGAGCAGCACCTGATATCCATGTGTGAGGACCATGATCGCATCCTTTTG
GCAGGCTGCCCTTCCTATGACAAACTTCTCTCAGCCAAGAACAAAGACTACATGAGCATC
ATTCGCATGTGGCTAGGTGATGATGTAAAATCTAAAGATTACATTGTTGCACTACAGCAC
CCTGTGACCACTGACATTAAGCATTCCATAAAAATGTTTGAATTAACATTGGATGCACTT
ATCTCATTTAACAAGCGGACCCTAGTCCTGTTTCCAAATATTGACGCAGGGAGCAAAGAG
ATGGTTCGAGTGATGCGGAAGAAGGGCATTGAGCATCATCCCAACTTTCGTGCAGTTAAA
CACGTCCCATTTGACCAGTTTATACAGTTGGTTGCCCATGCTGGCTGTATGATTGGGAAC
AGCAGCTGTGGGGTTCGAGAAGTTGGAGCTTTTGGAACACCTGTGATCAACCTGGGAACA
CGTCAGATTGGAAGAGAAACAGGGGAGAATGTTCTTCATGTCCGGGATGCTGACACCCAA
GACAAAATATTGCAAGCACTGCACCTTCAGTTTGGTAAACAGTACCCTTGTTCAAAGATA
TATGGGGATGGAAATGCTGTTCCAAGGATTTTGAAGTTTCTCAAATCTATCGATCTTCAA
GAGCCACTGCAAAAGAAATTCTGCTTTCCTCCTGTGAAGGAGAATATCTCTCAAGATATT
GACCATATTCTTGAAACTCTAAGTGCCTTGGCCGTTGATCTTGGCGGGACGAACCTCCGA
GTTGCAATAGTCAGCATGAAGGGTGAAATAGTTAAGAAGTATACTCAGTTCAATCCTAAA
ACCTATGAAGAGAGGATTAATTTAATCCTACAGATGTGTGTGGAAGCTGCAGCAGAAGCT
GTAAAACTGAACTGCAGAATTTTGGGAGTAGGCATTTCCACAGGTGGCCGTGTAAATCCT
CGGGAAGGAATTGTGCTGCATTCAACCAAACTGATCCAAGAGTGGAACTCTGTGGACCTT
AGGACCCCCCTTTCTGACACTTTGCATCTCCCTGTGTGGGTAGACAATGATGGCAACTGT
GCTGCCCTGGCGGAAAGGAAATTTGGCCAAGGAAAGGGACTGGAAAACTTTGTTACACTT
ATCACAGGCACAGGAATCGGTGGTGGAATTATCCATCAGCATGAATTGATCCACGGAAGC
TCCTTCTGTGCTGCAGAACTGGGCCACCTTGTTGTGTCTCTGGATGGGCCTGATTGTTCC
TGTGGAAGCCATGGGTGCATTGAAGCATACGCCTCTGGAATGGCCTTGCAGAGGGAGGCA
AAAAAGCTCCATGATGAGGACCTGCTCTTGGTGGAAGGGATGTCAGTGCCAAAAGATGAG
GCTGTGGGTGCGCTCCATCTCATCCAAGCTGCGAAACTTGGCAATGCGAAGGCCCAGAGC
ATCCTAAGAACAGCTGGAACAGCTTTGGGTCTTGGGGTTGTGAACATCCTCCATACCATG
AATCCCTCCCTTGTGATCCTCTCCGGAGTCCTGGCCAGTCACTATATCCACATTGTCAAA
GACGTCATTCGCCAGCAGGCCTTGTCCTCCGTGCAGGACGTGGATGTGGTGGTTTCGGAT
TTGGTTGACCCCGCCCTGCTGGGTGCTGCCAGCATGGTTCTGGACTACACAACACGCAGG
ATCTACTAG
|
| Enzyme 1 GenBank Gene ID |
AJ238764  |
| Enzyme 1 GeneCard ID |
GNE  |
| Enzyme 1 GenAtlas ID |
GNE  |
| Enzyme 1 HGNC ID |
HGNC:23657  |
| Enzyme 1 Chromosome Location |
9 |
| Enzyme 1 Locus |
9p13.3 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Seppala R, Lehto VP, Gahl WA: Mutations in the human UDP-N-acetylglucosamine 2-epimerase gene define the disease sialuria and the allosteric site of the enzyme. Am J Hum Genet. 1999 Jun;64(6):1563-9. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
6229 |
| Enzyme 2 Name |
Phosphatidylinositol N-acetylglucosaminyltransferase subunit A |
| Enzyme 2 Synonyms |
- GlcNAc-PI synthesis protein
- Phosphatidylinositol- glycan biosynthesis class A protein
- PIG-A
|
| Enzyme 2 Gene Name |
PIGA |
| Enzyme 2 Protein Sequence |
>Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
MACRGGAGNGHRASATLSRVSPGSLYTCRTRTHNICMVSDFFYPNMGGVESHIYQLSQCL
IERGHKVIIVTHAYGNRKGIRYLTSGLKVYYLPLKVMYNQSTATTLFHSLPLLRYIFVRE
RVTIIHSHSSFSAMAHDALFHAKTMGLQTVFTDHSLFGFADVSSVLTNKLLTVSLCDTNH
IICVSYTSKENTVLRAALNPEIVSVIPNAVDPTDFTPDPFRRHDSITIVVVSRLVYRKGI
DLLSGIIPELCQKYPDLNFIIGGEGPKRIILEEVRERYQLHDRVRLLGALEHKDVRNVLV
QGHIFLNTSLTEAFCMAIVEAASCGLQVVSTRVGGIPEVLPENLIILCEPSVKSLCEGLE
KAIFQLKSGTLPAPENIHNIVKTFYTWRNVAERTEKVYDRVSVEAVLPMDKRLDRLISHC
GPVTGYIFALLAVFNFLFLIFLRWMTPDSIIDVAIDATGPRGAWTNNYSHSKRGGENNEI
SETR
|
| Enzyme 2 Number of Residues |
484 |
| Enzyme 2 Molecular Weight |
54127 |
| Enzyme 2 Theoretical pI |
8.41 |
| Enzyme 2 GO Classification |
| Function |
| — |
| Process |
- biosynthesis
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 2 General Function |
Cell wall/membrane/envelope biogenesis |
| Enzyme 2 Specific Function |
Necessary for the synthesis of N-acetylglucosaminyl- phosphatidylinositol, the very early intermediate in GPI-anchor biosynthesis |
| Enzyme 2 Pathways |
Not Available |
| Enzyme 2 Reactions |
- UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
219994  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P37287  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
PIGA_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1455 bp
ATGGCCTGTAGAGGAGGAGCTGGGAATGGCCACCGTGCCTCAGCTACACTCTCTCGGGTT
AGCCCTGGAAGTCTTTACACATGTAGAACCCGTACCCATAATATATGCATGGTATCTGAC
TTTTTCTACCCAAATATGGGAGGCGTGGAAAGCCACATTTACCAGCTCTCTCAGTGCCTG
ATTGAAAGAGGGCATAAGGTTATAATTGTCACCCATGCTTATGGAAATCGAAAAGGCATC
CGTTACCTCACCAGTGGCCTCAAAGTCTATTACTTGCCTCTGAAAGTCATGTACAACCAG
TCTACAGCCACGACCCTCTTTCACAGTCTGCCATTGCTCAGGTACATATTTGTTCGGGAG
AGAGTCACGATAATCCATTCACATAGTTCTTTTTCTGCTATGGCCCATGATGCTCTCTTC
CACGCCAAGACAATGGGGCTTCAGACAGTCTTCACGGACCATTCCCTTTTTGGATTTGCT
GATGTCAGCTCGGTGCTTACAAACAAGCTTCTAACCGTGTCTCTTTGTGATACAAACCAC
ATCATTTGTGTGTCTTATACTAGTAAGGAAAATACTGTACTAAGAGCAGCACTGAATCCT
GAAATAGTGTCCGTCATTCCTAATGCTGTAGATCCTACTGACTTCACTCCAGACCCATTT
AGAAGGCATGATAGTATAACTATTGTTGTTGTCAGCAGACTTGTTTACAGAAAAGGGATC
GATTTGCTTAGTGGTATAATACCTGAACTCTGTCAGAAATATCCAGATTTAAATTTCATA
ATTGGAGGAGAGGGACCAAAGAGAATCATTTTGGAAGAAGTTCGGGAAAGATACCAGCTG
CATGACAGGGTGCGTCTTTTGGGAGCTTTAGAACACAAGGATGTTAGAAATGTCTTAGTT
CAAGGACATATTTTTCTGAATACCTCCCTTACTGAAGCATTCTGCATGGCGATCGTGGAA
GCAGCCAGTTGTGGTTTACAGGTTGTAAGTACCAGAGTTGGTGGAATTCCTGAGGTGCTT
CCAGAAAACCTTATTATTTTATGTGAGCCTTCAGTAAAATCTTTGTGTGAAGGATTGGAA
AAGGCTATTTTCCAACTGAAGTCAGGGACATTGCCAGCTCCAGAAAACATCCATAACATA
GTAAAGACTTTCTACACCTGGAGGAATGTTGCAGAAAGAACTGAAAAGGTATATGACCGG
GTATCAGTGGAAGCTGTGTTGCCAATGGACAAACGACTGGACAGACTTATTTCTCACTGC
GGCCCAGTAACAGGCTACATCTTTGCTTTGTTGGCAGTTTTCAACTTCCTCTTCCTCATT
TTCTTGAGATGGATGACTCCAGATTCTATCATTGATGTTGCAATAGATGCCACTGGGCCA
CGGGGTGCCTGGACTAATAACTATTCTCACAGTAAAAGAGGGGGTGAGAATAATGAGATA
TCTGAAACCAGGTAG
|
| Enzyme 2 GenBank Gene ID |
D11466  |
| Enzyme 2 GeneCard ID |
PIGA  |
| Enzyme 2 GenAtlas ID |
PIGA  |
| Enzyme 2 HGNC ID |
HGNC:8957  |
| Enzyme 2 Chromosome Location |
X |
| Enzyme 2 Locus |
Xp22.1 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Miyata T, Takeda J, Iida Y, Yamada N, Inoue N, Takahashi M, Maeda K, Kitani T, Kinoshita T: The cloning of PIG-A, a component in the early step of GPI-anchor biosynthesis. Science. 1993 Feb 26;259(5099):1318-20. [PubMed
]
- Bessler M, Hillmen P, Longo L, Luzzatto L, Mason PJ: Genomic organization of the X-linked gene (PIG-A) that is mutated in paroxysmal nocturnal haemoglobinuria and of a related autosomal pseudogene mapped to 12q21. Hum Mol Genet. 1994 May;3(5):751-7. [PubMed
]
- Iida Y, Takeda J, Miyata T, Inoue N, Nishimura J, Kitani T, Maeda K, Kinoshita T: Characterization of genomic PIG-A gene: a gene for glycosylphosphatidylinositol-anchor biosynthesis and paroxysmal nocturnal hemoglobinuria. Blood. 1994 Jun 1;83(11):3126-31. [PubMed
]
- Yu J, Nagarajan S, Ueda E, Knez JJ, Petersen RB, Medof ME: Characterization of alternatively spliced PIG-A transcripts in normal and paroxysmal nocturnal hemoglobinuria cells. Braz J Med Biol Res. 1994 Feb;27(2):195-201. [PubMed
]
- Takeda J, Miyata T, Kawagoe K, Iida Y, Endo Y, Fujita T, Takahashi M, Kitani T, Kinoshita T: Deficiency of the GPI anchor caused by a somatic mutation of the PIG-A gene in paroxysmal nocturnal hemoglobinuria. Cell. 1993 May 21;73(4):703-11. [PubMed
]
- Bessler M, Mason PJ, Hillmen P, Miyata T, Yamada N, Takeda J, Luzzatto L, Kinoshita T: Paroxysmal nocturnal haemoglobinuria (PNH) is caused by somatic mutations in the PIG-A gene. EMBO J. 1994 Jan 1;13(1):110-7. [PubMed
]
- Ware RE, Rosse WF, Howard TA: Mutations within the Piga gene in patients with paroxysmal nocturnal hemoglobinuria. Blood. 1994 May 1;83(9):2418-22. [PubMed
]
- Nafa K, Bessler M, Castro-Malaspina H, Jhanwar S, Luzzatto L: The spectrum of somatic mutations in the PIG-A gene in paroxysmal nocturnal hemoglobinuria includes large deletions and small duplications. Blood Cells Mol Dis. 1998 Sep;24(3):370-84. [PubMed
]
- Yoon JH, Cho HI, Park SS, Chang YH, Kim BK: Mutation analysis of the PIG-A gene in Korean patients with paroxysmal nocturnal haemoglobinuria. J Clin Pathol. 2002 Jun;55(6):410-3. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
6368 |
| Enzyme 3 Name |
UDP-N-acetylhexosamine pyrophosphorylase |
| Enzyme 3 Synonyms |
- Antigen X
- AGX
- Sperm- associated antigen 2[Includes: UDP-N-acetylgalactosamine pyrophosphorylase
- AGX-1
- UDP-N-acetylglucosamine pyrophosphorylase
- AGX-2]
|
| Enzyme 3 Gene Name |
UAP1 |
| Enzyme 3 Protein Sequence |
>UDP-N-acetylhexosamine pyrophosphorylase
MNINDLKLTLSKAGQEHLLRFWNELEEAQQVELYAELQAMNFEELNFFFQKAIEGFNQSS
HQKNVDARMEPVPREVLGSATRDQDQLQAWESEGLFQISQNKVAVLLLAGGQGTRLGVAY
PKGMYDVGLPSRKTLFQIQAERILKLQQVAEKYYGNKCIIPWYIMTSGRTMESTKEFFTK
HKYFGLKKENVIFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDME
QRGIWSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQ
VVEYSEISLATAQKRSSDGRLLFNAGNIANHFFTVPFLRDVVNVYEPQLQHHVAQKKIPY
VDTQGQLIKPDKPNGIKMEKFVFDIFQFAKKFVVYEVLREDEFSPLKNADSQNGKDNPTT
ARHALMSLHHCWVLNAGGHFIDENGSRLPAIPRSATNGKSETITADVNHNLKDANDVPIQ
CEISPLISYAGEGLESYVADKEFHAPLIIDENGVHELVKNGI
|
| Enzyme 3 Number of Residues |
522 |
| Enzyme 3 Molecular Weight |
58770 |
| Enzyme 3 Theoretical pI |
6.29 |
| Enzyme 3 GO Classification |
| Function |
- catalytic activity
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 3 General Function |
Not Available |
| Enzyme 3 Specific Function |
Converts UDP and GlcNAc-1-P into UDP-GlcNAc, and UDP and GalNAc-1-P into UDP-GalNAc. Isoform AGX1 has 2 to 3 times higher activity towards GalNAc-1-P, while isoform AGX2 has 8 times more activity towards GlcNAc-1-P |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-D-glucosamine
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
7717462  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q16222  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
UAP1_HUMAN  |
| Enzyme 3 PDB ID |
1JVG  |
| Enzyme 3 PDB File |
Show |
| Enzyme 3 3D Structure |
|
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>1518 bp
ATGAACATTAATGACCTCAAACTCACGTTGTCCAAAGCTGGGCAAGAGCACCTACTACGT
TTCTGGAATGAGCTTGAAGAAGCCCAACAGGTAGAACTTTATGCAGAGCTCCAGGCCATG
AACTTTGAGGAGCTGAACTTCTTTTTCCAAAAGGCCATTGAAGGTTTTAACCAGTCTTCT
CACCAAAAGAATGTGGATGCACGAATGGAACCTGTGCCTCGAGAGGTATTAGGCAGTGCT
ACAAGGGATCAAGATCAGCTCCAGGCCTGGGAAAGTGAAGGACTTTTCCAGATTTCTCAG
AATAAAGTAGCAGTTCTTCTTCTAGCTGGTGGGCAGGGGACAAGACTCGGCGTTGCATAT
CCTAAGGGGATGTATGATGTTGGTTTGCCATCCCGTAAGACACTTTTTCAGATTCAAGCA
GAGCGTATCCTGAAGCTACAGCAGGTTGCTGAAAAATATTATGGCAACAAATGCATTATT
CCATGGTATATAATGACCAGTGGCAGAACAATGGAATCTACAAAGGAGTTCTTCACCAAG
CACAAGTACTTTGGTTTAAAAAAAGAGAATGTAATCTTTTTTCAGCAAGGAATGCTCCCC
GCCATGAGTTTTGATGGGAAAATTATTTTGGAAGAGAAGAACAAAGTTTCTATGGCTCCA
GATGGGAATGGTGGTCTTTATCGGGCACTTGCAGCCCAGAATATTGTGGAGGATATGGAG
CAAAGAGGCATTTGGAGCATTCATGTCTATTGTGTTGACAACATATTAGTAAAAGTGGCA
GACCCACGGTTCATTGGATTTTGCATTCAGAAAGGAGCAGACTGTGGAGCAAAGGTGGTA
GAGAAAACGAACCCTACAGAACCAGTTGGAGTGGTTTGCCGAGTGGATGGAGTTTACCAG
GTGGTAGAATATAGTGAGATTTCCCTGGCAACAGCTCAAAAACGAAGCTCAGACGGACGA
CTGCTGTTCAATGCGGGGAACATTGCCAACCATTTCTTCACTGTACCATTTCTGAGAGAT
GTTGTCAATGTTTATGAACCTCAGTTGCAGCACCATGTGGCTCAAAAGAAGATTCCTTAT
GTGGATACCCAAGGACAGTTAATTAAGCCAGACAAACCCAATGGAATAAAGATGGAAAAA
TTTGTCTTTGACATCTTCCAGTTTGCAAAGAAGTTTGTGGTATATGAAGTATTGCGAGAA
GATGAGTTTTCCCCACTAAAGAATGCTGATAGTCAGAATGGGAAAGACAACCCTACTACT
GCAAGGCATGCTTTGATGTCCCTTCATCATTGCTGGGTCCTCAATGCAGGGGGCCATTTC
ATAGATGAAAATAGCTCTCGCCTTCCAGCAATTCCCCGCTTGAAGGATGCCAATGATGTA
CCAATCCAATGTGAAATCTCTCCTCTTATCTCCTATGCTGGAGAAGGATTAGAAAGTTAT
GTGGCAGATAAAGAATTCCATGCACCTCTAATCATCGATGAGAATGGAGTTCATGAGCTG
GTGAAAAATGGTATTTGA
|
| Enzyme 3 GenBank Gene ID |
S73498  |
| Enzyme 3 GeneCard ID |
UAP1  |
| Enzyme 3 GenAtlas ID |
UAP1  |
| Enzyme 3 HGNC ID |
HGNC:12457  |
| Enzyme 3 Chromosome Location |
1 |
| Enzyme 3 Locus |
1q23.3 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Diekman AB, Goldberg E: Characterization of a human antigen with sera from infertile patients. Biol Reprod. 1994 May;50(5):1087-93. [PubMed
]
- Mio T, Yabe T, Arisawa M, Yamada-Okabe H: The eukaryotic UDP-N-acetylglucosamine pyrophosphorylases. Gene cloning, protein expression, and catalytic mechanism. J Biol Chem. 1998 Jun 5;273(23):14392-7. [PubMed
]
- Wang-Gillam A, Pastuszak I, Elbein AD: A 17-amino acid insert changes UDP-N-acetylhexosamine pyrophosphorylase specificity from UDP-GalNAc to UDP-GlcNAc. J Biol Chem. 1998 Oct 16;273(42):27055-7. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
6385 |
| Enzyme 4 Name |
UDP-N-acetylglucosamine--dolichyl-phosphate N- acetylglucosaminephosphotransferase |
| Enzyme 4 Synonyms |
- GPT
- G1PT
- N- acetylglucosamine-1-phosphate transferase
- GlcNAc-1-P transferase
|
| Enzyme 4 Gene Name |
DPAGT1 |
| Enzyme 4 Protein Sequence |
>UDP-N-acetylglucosamine--dolichyl-phosphate N- acetylglucosaminephosphotransferase
MWAFSELPMPLLINLIVSLLGFVATVTLIPAFRGHFIAARLCGQDLNKTSRQQIPESQGV
ISGAVFLIILFCFIPFPFLNCFVKEQCKAFPHHEFVALIGALLAICCMIFLGFADDVLNL
RWRHKLLLPTAASLPLLMVYFTNFGNTTIVVPKPFRPILGLHLDLGILYYVYMGLLAVFC
TNAINILAGINGLEAGQSLVISASIIVFNLVELEGDCRDDHVFSLYFMIPFFFTTLGLLY
HNWYPSRVFVGDTFCYFAGMTFAVVGILGHFSKTMLLFFMPQVFNFLYSLPQLLHIIPCP
RHRIPRLNIKTGKLEMSYSKFKTKSLSFLGTFILKVAESLQLVTVHQSETEDGEFTECNN
MTLINLLLKVLGPIHERNLTLLLLLLQILGSAITFSIRYQLVRLFYDV
|
| Enzyme 4 Number of Residues |
408 |
| Enzyme 4 Molecular Weight |
46091 |
| Enzyme 4 Theoretical pI |
8.07 |
| Enzyme 4 GO Classification |
| Function |
|
| Process |
- lipid metabolism
- metabolism
- physiological process
- primary metabolism
|
| Component |
|
|
| Enzyme 4 General Function |
Cell wall/membrane/envelope biogenesis |
| Enzyme 4 Specific Function |
Catalyzes the initial step in the synthesis of dolichol- P-P-oligosaccharides |
| Enzyme 4 Pathways |
|
| Enzyme 4 Reactions |
- UDP-N-acetyl-D-glucosamine + dolichyl phosphate = UMP + N-acetyl-D-glucosaminyl-diphosphodolichol
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
Not Available |
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
2239119  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
Q9H3H5  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
GPT_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>1203 bp
ATGCCGCTGCTGATCAATTTGATCGTCTCGCTGCTGGGATTTGTGGCCACAGTCACCCTC
ATCCCGGCCTTCCTGGGCCACTTCATTGCTGCGCGCCTCTGTGGTCAGGACCTCAACAAA
ACCAGCCGACAGCAGATCCCAGAATCCCAGGGAGTGATCAGCGGTGCTGTTTTCCTTATC
ATCCTCTTCTGCTTCATCCCTTTCCCCTTCCTGAACTGCTTTGTGAAGGAGCAGTGTAAG
GCATTCCCCCACCATGAATTTGTGGCCCTGATAGGTGCCCTCCTTGCCATCTGCTGCATG
ATCTTCCTGGGCTTTGCGGATGATGTACTGAATCTGCGCTGGCGCCATAAGCTGCTGCTA
CCTACAGCTGCCTCACTACCTCTCCTCATGGTCTATTTCACCAACTTTGGCAACACGACC
ATTGTGGTGCCCAAGCCCTTCCGCCCGATACTTGGCCTGCATCTGGACTTGGGAATCCTG
TACTATGTCTACATGGGGCTGCTGGCAGTGTTCTGTACCAATGCCATCAATATCCTAGCA
GGAATTAACGGCCTAGAGGCTGGCCAGTCACTAGTCATTTCTGCTTCCATCATTGTCTTC
AACCTGGTAGAGTTGGAAGGTGATTGTCGGGATGATCATGTCTTTTCCCTCTACTTCATG
ATACCCTTTTTTTTCACCACTTTGGGATTGCTCTACCACAACTGGTACCCATCACGGGTG
TTTGTGGGAGATACCTTCTGTTACTTTGCTGGCATGACCTTTGCCGTGGTGGGCATCTTG
GGACACTTCAGCAAGACCATGCTACTATTCTTCATGCCCCAGGTGTTCAACTTCCTCTAC
TCACTGCCTCAGCTCCTGCATATCATCCCCTGCCCTCGCCACCGCATACCCAGACTCAAT
ATCAAGACAGGCAAACTGGAGATGAGCTATTCCAAGTTCAAGACCAAGAGCCTCTCTTTC
TTGGGCACCTTTATTTTAAAGGTGGCAGAGAGCCTCCAGCTGGTGACAGTACACCAGAGT
GAGACTGAAGATGGTGAATTCACTGAATGTAACAACATGACCCTCATCAACTTGCTACTT
AAAGTCCTTGGGCCCATACATGAGAGAAACCTCACATTGCTCCTGCTGCTGCTGCAGATC
CTGGGCAGTGCCATCACCTTCTCCATTCGATATCAGCTCGTTCGACTCTTCTATGATGTC
TGA
|
| Enzyme 4 GenBank Gene ID |
Z82022  |
| Enzyme 4 GeneCard ID |
DPAGT1  |
| Enzyme 4 GenAtlas ID |
DPAGT1  |
| Enzyme 4 HGNC ID |
HGNC:2995  |
| Enzyme 4 Chromosome Location |
11 |
| Enzyme 4 Locus |
11q23.3 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Eckert V, Blank M, Mazhari-Tabrizi R, Mumberg D, Funk M, Schwarz RT: Cloning and functional expression of the human GlcNAc-1-P transferase, the enzyme for the committed step of the dolichol cycle, by heterologous complementation in Saccharomyces cerevisiae. Glycobiology. 1998 Jan;8(1):77-85. [PubMed
]
- Wu X, Rush JS, Karaoglu D, Krasnewich D, Lubinsky MS, Waechter CJ, Gilmore R, Freeze HH: Deficiency of UDP-GlcNAc:Dolichol Phosphate N-Acetylglucosamine-1 Phosphate Transferase (DPAGT1) causes a novel congenital disorder of Glycosylation Type Ij. Hum Mutat. 2003 Aug;22(2):144-50. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
7038 |
| Enzyme 5 Name |
Hyaluronan synthase 1 |
| Enzyme 5 Synonyms |
- Hyaluronate synthase 1
- Hyaluronic acid synthase 1
- HA synthase 1
- HuHAS1
|
| Enzyme 5 Gene Name |
HAS1 |
| Enzyme 5 Protein Sequence |
>Hyaluronan synthase 1
MRQQDAPKPTPAARRCSGLARRVLTIAFALLILGLMTWAYAAGVPLASDRYGLLAFGLYG
AFLSAHLVAQSLFAYLEHRRVAAAARGPLDAATARSVALTISAYQEDPAYLRQCLASARA
LLYPRARLRVLMVVDGNRAEDLYMVDMFREVFADEDPATYVWDGNYHQPWEPAAAGAVGA
GAYREVEAEDPGRLAVEALVRTRRCVCVAQRWGGKREVMYTAFKALGDSVDYVQVCDSDT
RLDPMALLELVRVLDEDPRVGAVGGDVRILNPLDSWVSFLSSLRYWVAFNVERACQSYFH
CVSCISGPLGLYRNNLLQQFLEAWYNQKFLGTHCTFGDDRHLTNRMLSMGYATKYTSRSR
CYSETPSSFLRWLSQQTRWSKSYFREWLYNALWWHRHHAWMTYEAVVSGLFPFFVAATVL
RLFYAGRPWALLWVLLCVQGVALAKAAFAAWLRGCLRMVLLSLYAPLYMCGLLPAKFLAL
VTMNQSGWGTSGRRKLAANYVPLLPLALWALLLLGGLVRSVAHEARADWSGPSRAAEAYH
LAAGAGAYVGYWVAMLTLYWVGVRRLCRRRTGGYRVQV
|
| Enzyme 5 Number of Residues |
578 |
| Enzyme 5 Molecular Weight |
64886 |
| Enzyme 5 Theoretical pI |
9.47 |
| Enzyme 5 GO Classification |
Not Available |
| Enzyme 5 General Function |
Cell wall/membrane/envelope biogenesis |
| Enzyme 5 Specific Function |
Plays a role in hyaluronan/hyaluronic acid (HA) synthesis. Also able to catalyze the synthesis of chito- oligosaccharide depending on the substrate |
| Enzyme 5 Pathways |
Not Available |
| Enzyme 5 Reactions |
- n UDP-N-acetyl-D-glucosamine + n UDP-D-glucuronate = [beta-N-acetyl-D-glucosaminyl(1-> 4)beta-D-glucuronosyl(1-> 3)]n+ 2n UDP
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
- 26-46
53-73
400-420
431-451
458-478
498-518
541-561
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
1556465  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
Q92839  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
HAS1_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>1737 bp
ATGAGACAGCAGGACGCGCCCAAGCCCACTCCTGCAGCCCGCCGCTGCTCCGGCCTGGCC
CGGAGGGTGCTGACCATCGCCTTCGCCCTGCTCATCCTGGGCCTCATGACCTGGGCCTAC
GCCGCCGGGGTGCCGCTGGCCTCCGATCGCTACGGCCTCCTGGCCTTCGGCCTCTACGGG
GCCTTCCTTTCAGCGCACCTGGTGGCGCAGAGCCTCTTCGCGTACCTGGAGCACCGGCGG
GTGGCGGCGGCGGCGCGGGGGCCGCTGGATGCAGCCACCGCGCGCAGTGTGGCGCTGACC
ATCTCCGCCTACCAGGAGGACCCCGCGTACCTGCGCCAGTGCCTGGCGTCCGCCCGCGCC
CTGCTGTACCCGCGCGCGCGGCTGCGCGTCCTCATGGTGGTGGATGGCAACCGCGCCGAG
GACCTCTACATGGTCGACATGTTCCGCGAGGTCTTCGCTGACGAGGACCCCGCCACGTAC
GTGTGGGACGGCAACTACCACCAGCCCTGGGAACCCGCGGCGGCGGGCGCGGTGGGCGCC
GGAGCCTATCGGGAGGTGGAGGCGGAGGATCCTGGGCGGCTGGCAGTGGAGGCGCTGGTG
AGGACTCGCAGGTGCGTGTGCGTGGCGCAGCGCTGGGGCGGCAAGCGCGAGGTCATGTAC
ACAGCCTTCAAGGCGCTCGGAGATTCGGTGGACTACGTGCAGGTCTGTGACTCGGACACA
AGGTTGGACCCCATGGCACTGCTGGAGCTCGTGCGGGTACTGGACGAGGACCCCCGGGTA
GGGGCTGTTGGTGGGGACGTGCGGATCCTTAACCCTCTGGACTCCTGGGTCAGCTTCCTA
AGCAGCCTGCGATACTGGGTAGCCTTCAATGTGGAGCGGGCTTGTCAGAGCTACTTCCAC
TGTGTATCCTGCATCAGCGGTCCTCTAGGCCTATATAGGAATAACCTCTTGCAGCAGTTT
CTTGAGGCCTGGTACAACCAGAAGTTCCTGGGTACCCACTGTACTTTTGGGGATGACCGG
CACCTCACCAACCGCATGCTCAGCATGGGTTATGCTACCAAGTACACCTCCAGGTCCCGC
TGCTACTCAGAGACGCCCTCGTCCTTCCTGCGGTGGCTGAGCCAGCAGACACGCTGGTCC
AAGTCGTACTTCCGTGAGTGGCTGTACAACGCGCTCTGGTGGCACCGGCACCATGCGTGG
ATGACCTACGAGGCGGTGGTCTCCGGCCTGTTCCCCTTCTTCGTGGCGGCCACTGTGCTG
CGTCTGTTCTACGCGGGCCGCCCTTGGGCGCTGCTGTGGGTGCTGCTGTGCGTGCAGGGC
GTGGCACTGGCCAAGGCGGCCTTCGCGGCCTGGCTGCGGGGCTGCCTGCGCATGGTGCTT
CTCTCGCTCTACGCGCCCCTCTACATGTGTGGCCTCCTGCCTGCCAAGTTCCTGGCGCTA
GTCACCATGAACCAGAGTGGCTGGGGCACCTCGGGCCGGCGGAAGCTGGCCGCTAACTAC
GTCCCTCTGCTGCCCCTGGCGCTCTGGGCGCTGCTGCTGCTTGGGGGCCTGGTCCGCAGC
GTAGCACACGAGGCCAGGGCCGACTGGAGCGGCCCTTCCCGCGCAGCCGAGGCCTACCAC
TTGGCCGCGGGGGCCGGCGCCTACGTGGGCTACTGGGTGGCCATGTTGACGCTGTACTGG
GTGGGCGTGCGGAGGCTTTGCCGGCGGCGGACCGGGGGCTACCGCGTCCAGGTGTGA
|
| Enzyme 5 GenBank Gene ID |
U59269  |
| Enzyme 5 GeneCard ID |
HAS1  |
| Enzyme 5 GenAtlas ID |
HAS1  |
| Enzyme 5 HGNC ID |
HGNC:4818  |
| Enzyme 5 Chromosome Location |
19 |
| Enzyme 5 Locus |
19q13.4 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Shyjan AM, Heldin P, Butcher EC, Yoshino T, Briskin MJ: Functional cloning of the cDNA for a human hyaluronan synthase. J Biol Chem. 1996 Sep 20;271(38):23395-9. [PubMed
]
- Itano N, Kimata K: Molecular cloning of human hyaluronan synthase. Biochem Biophys Res Commun. 1996 May 24;222(3):816-20. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
7039 |
| Enzyme 6 Name |
Exostosin-like 3 |
| Enzyme 6 Synonyms |
- Glucuronyl-galactosyl-proteoglycan 4- alpha-N-acetylglucosaminyltransferase
- Putative tumor suppressor protein EXTL3
- Multiple exostosis-like protein 3
- Hereditary multiple exostoses gene isolog
- EXT-related protein 1
|
| Enzyme 6 Gene Name |
EXTL3 |
| Enzyme 6 Protein Sequence |
>Exostosin-like 3
MTGYTMLRNGGAGNGGQTCMLRWSNRIRLTWLSFTLFVILVFFPLIAHYYLTTLDEADEA
GKRIFGPRVGNELCEVKHVLDLCRIRESVSEELLQLEAKRQELNSEIAKLNLKIEACKKS
IENAKQDLLQLKNVISQTEHSYKELMAQNQPKLSLPIRLLPEKDDAGLPPPKATRGCRLH
NCFDYSRCPLTSGFPVYVYDSDQFVFGSYLDPLVKQAFQATARANVYVTENADIACLYVI
LVGEMQEPVVLRPAELEKQLYSLPHWRTDGHNHVIINLSRKSDTQNLLYNVSTGRAMVAQ
STFYTVQYRPGFDLVVSPLVHAMSEPNFMEIPPQVPVKRKYLFTFQGEKIESLRSSLQEA
RSFEEEMEGDPPADYDDRIIATLKAVQDSKLDQVLVEFTCKNQPKPSLPTEWALCGERED
RLELLKLSTFALIITPGDPRLVISSGCATRLFEALEVGAVPVVLGEQVQLPYQDMLQWNE
AALVVPKPRVTEVHFLLRSLSDSDLLAMRRQGRFLWETYFSTADSIFNTVLAMIRTRIQI
PAAPIREEAAAEIPHRSGKAAGTDPNMADNGDLDLGPVETEPPYASPRYLRNFTLTVTDF
YRSWNCAPGPFHLFPHTPFDPVLPSEAKFLGSGTGFRPIGGGAGGSGKEFQAALGGNVPR
EQFTVVMLTYEREEVLMNSLERLNGLPYLNKVVVVWNSPKLPSEDLLWPDIGVPIMVVRT
EKNSLNNRFLPWNEIETEAILSIDDDAHLRHDEIMFGFRVWREARDRIVGFPGRYHAWDI
PHQSWLYNSNYSCELSMVLTGAAFFHKYYAYLYSYVMPQAIRDMVDEYINCEDIAMNFLV
SHITRKPPIKVTSRWTFRCPGCPQALSHDDSHFHERHKCINFFVKVYGYMPLLYTQFRVD
SVLFKTRLPHDKTKCFKFI
|
| Enzyme 6 Number of Residues |
919 |
| Enzyme 6 Molecular Weight |
104750 |
| Enzyme 6 Theoretical pI |
6.48 |
| Enzyme 6 GO Classification |
| Function |
| — |
| Process |
| — |
| Component |
|
|
| Enzyme 6 General Function |
Not Available |
| Enzyme 6 Specific Function |
Probable glycosyltransferase |
| Enzyme 6 Pathways |
- Chondroitin / Heparan sulfate biosynthesis (map00532
)
|
| Enzyme 6 Reactions |
- UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->3)-beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl-proteoglycan = UDP + alpha-N-acetyl-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl-proteoglycan
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
2897905  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
O43909  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
EXTL3_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>2760 bp
ATGACAGGCTATACCATGCTGCGGAATGGGGGCGCGGGGAACGGAGGTCAGACCTGCATG
CTGCGCTGGTCCAACCGCATCCGCCTCACGTGGCTCAGCTTCACGCTCTTTGTCATCCTG
GTCTTCTTCCCGCTCATCGCCCACTATTACCTCACCACTCTGGATGAGGCTGATGAGGCA
GGCAAGCGGATTTTTGGTCCCCGGGTGGGGAACGAGCTGTGCGAGGTGAAGCACGTGCTG
GATCTGTGCCGCATCCGGGAGTCGGTGAGTGAAGAGCTCCTGCAGCTGGAGGCCAAGCGC
CAAGAGCTGAACAGCGAGATCGCCAAGCTGAATCTGAAGATCGAAGCCTGTAAGAAGAGC
ATTGAGAACGCCAAGCAGGACCTGCTCCAGCTCAAGAATGTCATCAGCCAGACCGAGCAT
TCCTACAAGGAGCTCATGGCCCAGAACCAGCCCAAGCTGTCCCTGCCCATCCGACTGCTC
CCAGAGAAGGACGATGCCGGCCTCCCTCCCCCGAAGGCCACTCGGGGCTGCCGGCTACAC
AACTGCTTTGATTATTCTCGTTGCCCTCTCACCTCTGGCTTCCCGGTCTACGTCTATGAC
AGTGACCAGTTTGTCTTTGGCAGCTACCTGGATCCCTTGGTCAAGCAGGCTTTTCAGGCG
ACAGCACGAGCTAACGTTTATGTTACAGAAAATGCAGACATCGCCTGCCTTTACGTGATA
CTAGTGGGAGAGATGCAGGAGCCGGTGGTGCTGCGGCCTGCTGAGCTGGAGAAGCAGTTG
TATTCCCTGCCACACTGGCGGACGGATGGACACAACCATGTCATCATCAATCTGTCACGT
AAGTCAGATACACAGAACCTTCTCTATAACGTCAGTACTGGCCGTGCCATGGTGGCCCAG
TCCACCTTCTACACTGTCCAGTACAGACCTGGCTTTGACTTGGTCGTATCACCGCTGGTC
CATGCCATGTCTGAGCCCAACTTCATGGAAATCCCACCACAGGTGCCGGTGAAGCGGAAA
TATCTCTTCACCTTCCAGGGCGAGAAGATTGAGTCTCTGAGGTCTAGCCTTCAGGAGGCC
CGCTCCTTCGAAGAGGAAATGGAGGGCGACCCTCCCGCCGACTACGATGACCGGATCATT
GCCACCCTGAAGGCGGTGCAGGACAGCAAGCTGGATCAGGTCCTGGTGGAATTCACCTGC
AAAAACCAGCCCAAACCCAGCCTGCCGACTGAGTGGGCACTGTGTGGAGAGCGGGAGGAC
CGCTTGGAATTGCTGAAGCTCTCCACCTTCGCCCTCATCATTACCCCCGGGGACCCTCGC
TTGGTTATTTCCTCTGGGTGTGCAACACGGCTCTTCGAAGCCCTGGAAGTCGGTGCCGTC
CCGGTGGTGCTGGGGGAGCAGGTCCAGCTTCCCTACCAGGACATGCTGCAGTGGAACGAG
GCGGCCCTGGTGGTGCCAAAGCCTCGTGTTACCGAGGTTCATTTCCTGCTCAGAAGCCTC
TCCGATAGTGACCTCCTGGCTATGAGGCGGCAAGGCCGCTTTCTCTGGGAGACTTACTTC
TCCACTGCTGACAGTATTTTTAATACCGTGCTGGCTATGATTAGGACTCGCATCCAGATC
CCAGCCGCTCCCATCCGGGAAGAGGCGGCAGCTGAGATCCCCCACCGTTCAGGCAAGGCG
GCTGGAACTGACCCCAACATGGCTGACAACGGGGACCTGGACCTGGGGCCAGTGGAGACG
GAGCCGCCCTACGCCTCACCCAGATACCTCCGCAATTTCACTCTGACTGTCACTGACTTT
TACCGCAGCTGGAACTGTGCTCCAGGGCCTTTCCATCTTTTCCCCCACACTCCCTTTGAC
CCTGTGTTGCCCTCAGAGGCCAAATTCTTGGGCTCAGGGACTGGCTTTCGGCCTATTGGT
GGTGGAGCTGGGGGTTCTGGCAAGGAATTTCAGGCAGCGCTTGGAGGCAATGTTCCCCGA
GAGCAGTTCACGGTGGTGATGTTGACTTATGAGCGGGAGGAAGTGCTTATGAACTCTTTA
GAGAGGCTGAATGGCCTCCCTTACCTGAACAAGGTCGTGGTGGTGTGGAATTCTCCCAAG
CTGCCATCAGAGGACCTTCTGTGGCCTGACATTGGCGTCCCCATCATGGTGGTCCGTACT
GAGAAGAACAGTTTGAACAACCGATTCTTACCCTGGAATGAAATTGAGACAGAGGCCATC
CTGTCCATTGATGACGATGCTCACCTCCGCCATGACGAAATCATGTTTGGGTTCCGGGTG
TGGAGAGAAGCTCGGGACCGCATCGTGGGCTTCCCTGGCCGTTACCACGCATGGGACATC
CCCCATCAGTCCTGGCTCTACAACTCCAACTACTCCTGTGAGCTGTCCATGGTGCTGACA
GGTGCTGCCTTCTTTCACAAGTATTATGCCTACCTGTATTCTTATGTGATGCCCCAGGCC
ATCCGGGACATGGTGGATGAATACATCAACTGTGAGGACATTGCCATGAACTTCCTTGTC
TCCCACATCACTCGGAAGCCCCCCATCAAGGTGACCTCACGGTGGACATTCCGATGCCCA
GGATGCCCTCAGGCCCTGTCTCATGATGACTCCCACTTCCACGAGCGGCACAAGTGCATC
AACTTCTTCGTGAAGGTGTACGGCTACATGCCCCTCCTGTACACGCAGTTCAGGGTGGAT
TCTGTGCTCTTCAAGACACGCCTGCCCCATGACAAGACCAAGTGCTTCAAGTTCATCTAG
|
| Enzyme 6 GenBank Gene ID |
AF001690  |
| Enzyme 6 GeneCard ID |
EXTL3  |
| Enzyme 6 GenAtlas ID |
EXTL3  |
| Enzyme 6 HGNC ID |
HGNC:3518  |
| Enzyme 6 Chromosome Location |
8 |
| Enzyme 6 Locus |
8p21 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Van Hul W, Wuyts W, Hendrickx J, Speleman F, Wauters J, De Boulle K, Van Roy N, Bossuyt P, Willems PJ: Identification of a third EXT-like gene (EXTL3) belonging to the EXT gene family. Genomics. 1998 Jan 15;47(2):230-7. [PubMed
]
- Saito T, Seki N, Yamauchi M, Tsuji S, Hayashi A, Kozuma S, Hori T: Structure, chromosomal location, and expression profile of EXTR1 and EXTR2, new members of the multiple exostoses gene family. Biochem Biophys Res Commun. 1998 Feb 4;243(1):61-6. [PubMed
]
- Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [PubMed
]
- McCormick C, Duncan G, Goutsos KT, Tufaro F: The putative tumor suppressors EXT1 and EXT2 form a stable complex that accumulates in the Golgi apparatus and catalyzes the synthesis of heparan sulfate. Proc Natl Acad Sci U S A. 2000 Jan 18;97(2):668-73. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
7040 |
| Enzyme 7 Name |
Exostosin-2 |
| Enzyme 7 Synonyms |
- Glucuronosyl-N- acetylglucosaminyl-proteoglycan/N-acetylglucosaminyl-proteoglycan 4- alpha-N-acetylglucosaminyltransferase
- Putative tumor suppressor protein EXT2
- Multiple exostoses protein 2
|
| Enzyme 7 Gene Name |
EXT2 |
| Enzyme 7 Protein Sequence |
>Exostosin-2
MCASVKYNIRGPALIPRMKTKHRIYYITLFSIVLLGLIATGMFQFWPHSIESSNDWNVEK
RSIRDVPVVRLPADSPIPERGDLSCRMHTCFDVYRCGFNPKNKIKVYIYALKKYVDDFGV
SVSNTISREYNELLMAISDSDYYTDDINRACLFVPSIDVLNQNTLRIKETAQAMAQLSRW
DRGTNHLLFNMLPGGPPDYNTALDVPRDRALLAGGGFSTWTYRQGYDVSIPVYSPLSAEV
DLPEKGPGPRQYFLLSSQVGLHPEYREDLEALQVKHGESVLVLDKCTNLSEGVLSVRKRC
HKHQVFDYPQVLQEATFCVVLRGARLGQAVLSDVLQAGCVPVVIADSYILPFSEVLDWKR
ASVVVPEEKMSDVYSILQSIPQRQIEEMQRQARWFWEAYFQSIKAIALATLQIINDRIYP
YAAISYEEWNDPPAVKWGSVSNPLFLPLIPPQSQGFTAIVLTYDRVESLFRVITEVSKVP
SLSKLLVVWNNQNKNPPEDSLWPKIRVPLKVVRTAENKLSNRFFPYDEIETEAVLAIDDD
IIMLTSDELQFGYEVWREFPDRLVGYPGRLHLWDHEMNKWKYESEWTNEVSMVLTGAAFY
HKYFNYLYTYKMPGDIKNWVDAHMNCEDIAMNFLVANVTGKAVIKVTPRKKFKCPECTAI
DGLSLDQTHMVERSECINKFASVFGTMPLKVVEHRADPVLYKDDFPEKLKSFPNIGSL
|
| Enzyme 7 Number of Residues |
718 |
| Enzyme 7 Molecular Weight |
82255 |
| Enzyme 7 Theoretical pI |
6.51 |
| Enzyme 7 GO Classification |
| Function |
| — |
| Process |
| — |
| Component |
|
|
| Enzyme 7 General Function |
Not Available |
| Enzyme 7 Specific Function |
Glycosyltransferase required for the biosynthesis of heparan-sulfate. The EXT1/EXT2 complex possesses substantially higher glycosyltransferase activity than EXT1 or EXT2 alone. Appears to be a tumor suppressor |
| Enzyme 7 Pathways |
- Chondroitin / Heparan sulfate biosynthesis (map00532
)
|
| Enzyme 7 Reactions |
- UDP-alpha-D-glucuronate + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan = UDP + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
Not Available |
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
1518042  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
Q93063  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
EXT2_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>2157 bp
ATGTGTGCGTCGGTCAAGTATAATATCCGGGGTCCTGCCCTCATCCCAAGAATGAAGACC
AAGCACCGAATCTACTATATCACCCTCTTCTCCATTGTCCTCCTGGGCCTCATTGCCACT
GGCATGTTTCAGTTTTGGCCCCATTCTATCGAGTCCTCAAATGACTGGAATGTAGAGAAG
CGCAGCATCCGTGATGTGCCGGTTGTTAGGCTGCCAGCCGACAGTCCCATCCCAGAGCGG
GGGGATCTCAGTTGCAGAATGCACACGTGTTTTGATGTCTATCGCTGTGGCTTCAACCCA
AAGAACAAAATCAAGGTGTATATCTATGCTCTGAAAAAGTACGTGGATGACTTTGGCGTC
TCTGTCAGCAACACCATCTCCCGGGAGTATAATGAACTGCTCATGGCCATCTCAGACAGT
GACTACTACACTGATGACATCAACCGGGCCTGTCTGTTTGTTCCCTCCATCGATGTGCTT
AACCAGAACACACTGCGCATCAAGGAGACAGCACAAGCGATGGCCCAGCTCTCTAGGTGG
GATCGAGGTACGAATCACCTGTTGTTCAACATGTTGCCTGGAGGTCCCCCAGATTATAAC
ACAGCCCTGGATGTCCCCAGAGACAGGGCCCTGTTGGCTGGTGGCGGCTTTTCTACGTGG
ACTTACCGGCAAGGCTACGATGTCAGCATTCCTGTCTATAGTCCACTGTCAGCTGAGGTG
GATCTTCCAGAGAAAGGACCAGGTCCACGGCAATACTTCCTCCTGTCATCTCAGGTGGGT
CTCCATCCTGAGTACAGAGAGGACCTAGAAGCCCTCCAGGTCAAACATGGAGAGTCAGTG
TTAGTACTCGATAAATGCACCAACCTCTCAGAGGGTGTCCTTTCTGTCCGTAAGCGCTGC
CACAAGCACCAGGTCTTCGATTACCCACAGGTGCTACAGGAGGCTACTTTCTGTGTGGTT
CTTCGTGGAGCTCGGCTGGGCCAGGCAGTATTGAGCGATGTGTTACAAGCTGGCTGTGTC
CCGGTTGTCATTGCAGACTCCTATATTTTGCCTTTCTCTGAAGTTCTTGACTGGAAGAGA
GCATCTGTGGTTGTACCAGAAGAAAAGATGTCAGATGTGTACAGTATTTTGCAGAGCATC
CCCCAAAGACAGATTGAAGAAATGCAGAGACAGGCCCGGTGGTTCTGGGAAGCGTACTTC
CAGTCAATTAAAGCCATTGCCCTGGCCACCCTGCAGATTATCAATGACCGGATCTATCCA
TATGCTGCCATCTCCTATGAAGAATGGAATGACCCTCCTGCTGTGAAGTGGGGCAGCGTG
AGCAATCCACTCTTCCTCCCGCTGATCCCACCACAGTCTCAAGGGTTCACCGCCATAGTC
CTCACCTACGACCGAGTAGAGAGCCTCTTCCGGGTCATCACTGAAGTGTCCAAGGTGCCC
AGTCTATCCAAACTACTTGTCGTCTGGAATAATCAGAATAAAAACCCTCCAGAAGATTCT
CTCTGGCCCAAAATCCGGGTTCCATTAAAAGTTGTGAGGACTGCTGAAAACAAGTTAAGT
AACCGTTTCTTCCCTTATGATGAAATCGAGACAGAAGCTGTTCTGGCCATTGATGATGAT
ATCATTATGCTGACCTCTGACGAGCTGCAATTTGGTTATGAGGTCTGGCGGGAATTTCCT
GACCGGTTGGTGGGTTACCCGGGTCGTCTGCATCTCTGGGACCATGAGATGAATAAGTGG
AAGTATGAGTCTGAGTGGACGAATGAAGTGTCCATGGTGCTCACTGGGGCAGCTTTTTAT
CACAAGTATTTTAATTACCTGTATACCTACAAAATGCCTGGGGATATCAAGAACTGGGTA
GATGCTCATATGAACTGTGAAGATATTGCCATGAACTTCCTGGTGGCCAACGTCACGGGA
AAAGCAGTTATCAAGGTAACCCCACGAAAGAAATTCAAGTGTCCTGAGTGCACAGCCATA
GATGGGCTTTCACTAGACCAAACACACATGGTGGAGAGGTCAGAGTGCATCAACAAGTTT
GCTTCAGTCTTCGGGACCATGCCTCTCAAGGTGGTGGAACACCGAGCTGACCCTGTCCTG
TACAAAGATGACTTTCCTGAGAAGCTGAAGAGCTTCCCCAACATTGGCAGCTTATGA
|
| Enzyme 7 GenBank Gene ID |
U62740  |
| Enzyme 7 GeneCard ID |
EXT2  |
| Enzyme 7 GenAtlas ID |
EXT2  |
| Enzyme 7 HGNC ID |
HGNC:3513  |
| Enzyme 7 Chromosome Location |
11 |
| Enzyme 7 Locus |
11p12-p11 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Stickens D, Clines G, Burbee D, Ramos P, Thomas S, Hogue D, Hecht JT, Lovett M, Evans GA: The EXT2 multiple exostoses gene defines a family of putative tumour suppressor genes. Nat Genet. 1996 Sep;14(1):25-32. [PubMed
]
- Wuyts W, Van Hul W, Wauters J, Nemtsova M, Reyniers E, Van Hul EV, De Boulle K, de Vries BB, Hendrickx J, Herrygers I, Bossuyt P, Balemans W, Fransen E, Vits L, Coucke P, Nowak NJ, Shows TB, Mallet L, van den Ouweland AM, McGaughran J, Halley DJ, Willems PJ: Positional cloning of a gene involved in hereditary multiple exostoses. Hum Mol Genet. 1996 Oct;5(10):1547-57. [PubMed
]
- Clines GA, Ashley JA, Shah S, Lovett M: The structure of the human multiple exostoses 2 gene and characterization of homologs in mouse and Caenorhabditis elegans. Genome Res. 1997 Apr;7(4):359-67. [PubMed
]
- Kobayashi S, Morimoto K, Shimizu T, Takahashi M, Kurosawa H, Shirasawa T: Association of EXT1 and EXT2, hereditary multiple exostoses gene products, in Golgi apparatus. Biochem Biophys Res Commun. 2000 Feb 24;268(3):860-7. [PubMed
]
- Simmons AD, Musy MM, Lopes CS, Hwang LY, Yang YP, Lovett M: A direct interaction between EXT proteins and glycosyltransferases is defective in hereditary multiple exostoses. Hum Mol Genet. 1999 Nov;8(12):2155-64. [PubMed
]
- Wuyts W, Van Hul W: Molecular basis of multiple exostoses: mutations in the EXT1 and EXT2 genes. Hum Mutat. 2000;15(3):220-7. [PubMed
]
- Philippe C, Porter DE, Emerton ME, Wells DE, Simpson AH, Monaco AP: Mutation screening of the EXT1 and EXT2 genes in patients with hereditary multiple exostoses. Am J Hum Genet. 1997 Sep;61(3):520-8. [PubMed
]
- Xu L, Xia J, Jiang H, Zhou J, Li H, Wang D, Pan Q, Long Z, Fan C, Deng HX: Mutation analysis of hereditary multiple exostoses in the Chinese. Hum Genet. 1999 Jul-Aug;105(1-2):45-50. [PubMed
]
- Park KJ, Shin KH, Ku JL, Cho TJ, Lee SH, Choi IH, Phillipe C, Monaco AP, Porter DE, Park JG: Germline mutations in the EXT1 and EXT2 genes in Korean patients with hereditary multiple exostoses. J Hum Genet. 1999;44(4):230-4. [PubMed
]
- Shi YR, Wu JY, Tsai FJ, Lee CC, Tsai CH: An R223P mutation in EXT2 gene causes hereditary multiple exostoses. Hum Mutat. 2000 Apr;15(4):390-1. [PubMed
]
- Seki H, Kubota T, Ikegawa S, Haga N, Fujioka F, Ohzeki S, Wakui K, Yoshikawa H, Takaoka K, Fukushima Y: Mutation frequencies of EXT1 and EXT2 in 43 Japanese families with hereditary multiple exostoses. Am J Med Genet. 2001 Feb 15;99(1):59-62. [PubMed
]
- Bernard MA, Hall CE, Hogue DA, Cole WG, Scott A, Snuggs MB, Clines GA, Ludecke HJ, Lovett M, Van Winkle WB, Hecht JT: Diminished levels of the putative tumor suppressor proteins EXT1 and EXT2 in exostosis chondrocytes. Cell Motil Cytoskeleton. 2001 Feb;48(2):149-62. [PubMed
]
- Gigante M, Matera MG, Seripa D, Izzo AM, Venanzi R, Giannotti A, Digilio MC, Gravina C, Lazzari M, Monteleone G, Monteleone M, Dallapiccola B, Fazio VM: Ext-mutation analysis in Italian sporadic and hereditary osteochondromas. Int J Cancer. 2001 Nov 20;95(6):378-83. [PubMed
]
- Francannet C, Cohen-Tanugi A, Le Merrer M, Munnich A, Bonaventure J, Legeai-Mallet L: Genotype-phenotype correlation in hereditary multiple exostoses. J Med Genet. 2001 Jul;38(7):430-4. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
7041 |
| Enzyme 8 Name |
Exostosin-like 1 |
| Enzyme 8 Synonyms |
- Glucuronosyl-N-acetylglucosaminyl- proteoglycan 4-alpha-N-acetylglucosaminyltransferase
- Exostosin-L
- Multiple exostosis-like protein
|
| Enzyme 8 Gene Name |
EXTL1 |
| Enzyme 8 Protein Sequence |
>Exostosin-like 1
MQSWRRRKSLWLALSASWLLLVLLGGFSLLRLALPPRPRPGASQGWPRWLDAELLQSFSQ
PGELPEDAVSPPQAPHGGSCNWESCFDTSKCRGDGLKVFVYPAVGTISETHRRILASIEG
SRFYTFSPAGACLLLLLSLDAQTGECSSMPLQWNRGRNHLVLRLHPAPCPRTFQLGQAMV
AEASPTVDSFRPGFDVALPFLPEAHPLRGGAPGQLRQHSPQPGVALLALEEERGGWRTAD
TGSSACPWDGRCEQDPGPGQTQRQETLPNATFCLISGHRPEAASRFLQALQAGCIPVLLS
PRWELPFSEVIDWTKAAIVADERLPLQVLAALQEMSPARVLALRQQTQFLWDAYFSSVEK
VIHTTLEVIQDRIFGTSAHPSLLWNSPPGALLALSTFSTSPQDFPFYYLQQGSRPEGRFS
ALIWVGPPGQPPLKLIQAVAGSQHCAQILVLWSNERPLPSRWPETAVPLTVIDGHRKVSD
RFYPYSTIRTDAILSLDARSSLSTSEVDFAFLVWQSFPERMVGFLTSSHFWDEAHGGWGY
TAERTNEFSMVLTTAAFYHRYYHTLFTHSLPKALRTLADEAPTCVDVLMNFIVAAVTKLP
PIKVPYGKQRQEAAPLAPGGPGPRPKPPAPAPDCINQIAAAFGHMPLLSSRLRLDPVLFK
DPVSVQRKKYRSLEKP
|
| Enzyme 8 Number of Residues |
676 |
| Enzyme 8 Molecular Weight |
74697 |
| Enzyme 8 Theoretical pI |
8.26 |
| Enzyme 8 GO Classification |
| Function |
| — |
| Process |
| — |
| Component |
|
|
| Enzyme 8 General Function |
Not Available |
| Enzyme 8 Specific Function |
Probable glycosyltransferase |
| Enzyme 8 Pathways |
- Chondroitin / Heparan sulfate biosynthesis (map00532
)
|
| Enzyme 8 Reactions |
- UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan = UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
Not Available |
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
1524413  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
Q92935  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
EXTL1_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>2031 bp
ATGCAGTCGTGGAGGAGAAGAAAGTCCCTGTGGCTGGCACTGTCAGCCTCCTGGCTCCTG
CTTGTCCTGCTGGGAGGCTTCTCCCTTCTCCGCCTGGCGTTGCCTCCCAGACCTCGGCCC
GGGGCTTCCCAAGGCTGGCCCCGCTGGCTGGATGCAGAGCTCCTGCAGAGCTTCTCCCAG
CCTGGAGAGCTCCCAGAAGATGCCGTTTCACCTCCTCAAGCCCCTCATGGTGGCAGCTGC
AACTGGGAATCTTGCTTTGATACCTCAAAGTGCAGGGGCGATGGCCTTAAGGTATTCGTG
TACCCAGCGGTTGGAACCATCTCTGAGACTCATCGCAGGATCCTGGCTTCCATTGAGGGC
TCTCGCTTCTACACATTCAGCCCTGCTGGGGCCTGCCTCCTCCTCCTCCTCAGCCTGGAC
GCCCAGACTGGAGAGTGCAGCTCAATGCCTCTGCAATGGAACAGGGGCAGGAACCATCTG
GTCCTCCGTCTCCACCCGGCTCCCTGCCCCAGGACCTTCCAGCTGGGACAGGCTATGGTG
GCTGAGGCCAGCCCCACGGTGGACTCCTTCCGGCCCGGCTTTGATGTGGCCCTCCCTTTT
CTCCCTGAAGCCCACCCGTTGCGAGGTGGGGCTCCTGGCCAGCTGCGGCAACACAGCCCC
CAGCCCGGGGTAGCCCTGCTAGCCCTGGAAGAGGAGAGGGGTGGGTGGCGCACAGCAGAC
ACTGGCTCCTCTGCCTGCCCCTGGGATGGGCGCTGTGAGCAAGACCCTGGACCTGGGCAG
ACCCAGCGCCAGGAGACGCTGCCCAATGCCACCTTCTGCCTCATCTCTGGCCACCGTCCC
GAGGCTGCCTCGCGCTTCCTCCAAGCCCTGCAGGCCGGCTGCATCCCAGTGCTTCTCAGC
CCCCGCTGGGAGCTGCCCTTCTCCGAGGTCATCGACTGGACCAAGGCAGCCATCGTAGCT
GATGAGAGGCTCCCACTTCAGGTCCTGGCTGCCCTCCAGGAGATGTCCCCTGCACGGGTC
CTCGCCCTGCGTCAGCAGACCCAGTTTCTATGGGATGCCTACTTCTCCTCAGTGGAGAAG
GTCATCCATACCACTCTGGAGGTTATTCAGGACCGGATTTTTGGAACATCAGCTAACCCC
TCACTGCTGTGGAACAGCCCCCCAGGGGCACTCCTGGCCCTGTCTACTTTTTCCACAAGC
CCCCAGGACTTCCCCTTCTACTACCTGCAACAGGGCTCCCGCCCTGAGGGCAGATTCAGC
GCCCTGATCTGGGTGGGGCCCCCAGGCCAGCCCCCTCTGAAGCTCATCCAGGCGGTGGCA
GGCTCCCAGCACTGTGCCCAGATCTTGGTTCTCTGGAGCAATGAGAGGCCACTCCCATCC
AGGTGGCCGGAGACAGCTGTGCCCTTGACAGTCATTGATGGGCACAGGAAGGTTAGTGAT
CGCTTCTACCCATATAGCACCATCAGAACAGATGCCATCCTCAGCCTCGATGCCCGCAGC
AGTCTTTCCACAAGTGAGGTGGACTTTGCCTTTCTGGTGTGGCAGAGCTTCCCAGAGCGG
ATGGTGGGCTTCCTGACGTCGAGCCATTTCTGGGACGAGGCCCATGGTGGCTGGGGCTAC
ACTGCTGAGAGGACCAACGAATTCTCCATGGTTCTCACCACAGCCGCCTTCTACCATAGG
TATTACCACACTCTCTTCACCCACTCCCTGCCCAAGGCTCTGAGGACCCTGGCAGATGAG
GCACCCACCTGTGTGGACGTCCTGATGAATTTCATAGTAGCAGCAGTCACCAAGCTGCCC
CCTATCAAGGTGCCCTATGGCAAGCAGCGCCAGGAGGCTGCTCCACTGGCGCCTGGGGGC
CCGGGGCCCAGGCCAAAGCCGCCTGCCCCAGCCCCCGACTGCATCAACCAGATAGCGGCA
GCGTTCGGCCACATGCCCTTGCTGTCCTCTCGTCTGCGTCTGGACCCGGTGCTGTTTAAG
GACCCGGTGTCCGTGCAGCGCAAGAAGTACCGCAGCCTGGAGAAGCCCTAG
|
| Enzyme 8 GenBank Gene ID |
U67191  |
| Enzyme 8 GeneCard ID |
EXTL1  |
| Enzyme 8 GenAtlas ID |
EXTL1  |
| Enzyme 8 HGNC ID |
HGNC:3515  |
| Enzyme 8 Chromosome Location |
1 |
| Enzyme 8 Locus |
1p36.1 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Wise CA, Clines GA, Massa H, Trask BJ, Lovett M: Identification and localization of the gene for EXTL, a third member of the multiple exostoses gene family. Genome Res. 1997 Jan;7(1):10-6. [PubMed
]
- Xu L, Xia J, Jiang H, Zhou J, Li H, Wang D, Pan Q, Long Z, Fan C, Deng HX: Mutation analysis of hereditary multiple exostoses in the Chinese. Hum Genet. 1999 Jul-Aug;105(1-2):45-50. [PubMed
]
- Wuyts W, Spieker N, Van Roy N, De Boulle K, De Paepe A, Willems PJ, Van Hul W, Versteeg R, Speleman F: Refined physical mapping and genomic structure of the EXTL1 gene. Cytogenet Cell Genet. 1999;86(3-4):267-70. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
7042 |
| Enzyme 9 Name |
N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase |
| Enzyme 9 Synonyms |
- Poly-N-acetyllactosamine extension enzyme
- I-beta- 1,3-N-acetylglucosaminyltransferase
- iGnT
- UDP-GlcNAc:betaGal beta- 1,3-N-acetylglucosaminyltransferase 1
|
| Enzyme 9 Gene Name |
B3GNT1 |
| Enzyme 9 Protein Sequence |
>N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase
MQMSYAIRCAFYQLLLAALMLVAMLQLLYLSLLSGLHGQEEQDQYFEFFPPSPRSVDQVK
AQLRTALASGGVLDASGDYRVYRGLLKTTMDPNDVILATHASVDNLLHLSGLLERWEGPL
SVSVFAATKEEAQLATVLAYALSSHCPDMRARVAMHLVCPSRYEAAVPDPREPGEFALLR
SCQEVFDKLARVAQPGINYALGTNVSYPNNLLRNLAREGANYALVIDVDMVPSEGLWRGL
REMLDQSNQWGGTALVVPAFEIRRARRMPMNKNELVQLYQVGEVRPFYYGLCTPCQAPTN
YSRWVNLPEESLLRPAYVVPWQDPWEPFYVAGGKVPTFDERFRQYGFNRISQACELHVAG
FDFEVLNEGFLVHKGFKEALKFHPQKEAENQHNKILYRQFKQELKAKYPNSPRRC
|
| Enzyme 9 Number of Residues |
415 |
| Enzyme 9 Molecular Weight |
47120 |
| Enzyme 9 Theoretical pI |
7.22 |
| Enzyme 9 GO Classification |
Not Available |
| Enzyme 9 General Function |
Not Available |
| Enzyme 9 Specific Function |
Can initiate the synthesis or the elongation of the linear poly-N-acetyllactosaminoglycans |
| Enzyme 9 Pathways |
- Blood group glycolipid biosynthesis-neolactoseries (map00602
)
- Keratan sulfate biosynthesis (map00533
)
|
| Enzyme 9 Reactions |
- UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
|
| Enzyme 9 Pfam Domain Function |
Not Available |
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
Not Available |
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
2745741  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
O43505  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
B3GN1_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>1248 bp
ATGCAGATGTCCTACGCCATCCGGTGCGCCTTCTACCAGCTGCTGCTGGCCGCGCTCATG
CTGGTGGCGATGCTGCAGCTGCTCTACCTGTCGCTGCTGTCCGGACTGCACGGGCAGGAG
GAGCAAGACCAATATTTTGAGTTCTTTCCCCCGTCCCCACGGTCCGTGGACCAGGTCAAG
GCGCAGCTCCGCACCGCGCTGGCCTCTGGAGGCGTCCTGGACGCTAGCGGCGATTACCGC
GTCTACAGGGGCCTGCTGAAGACCACCATGGACCCCAACGATGTGATCCTGGCCACGCAC
GCCAGCGTGGACAACCTGCTGCACCTGTCGGGTCTGCTGGAGCGCTGGGAGGGCCCGCTG
TCCGTGTCGGTGTTCGCGGCCACCAAGGAGGAGGCGCAGCTGGCCACGGTGCTGGCCTAC
GCGCTGAGCAGCCACTGCCCCGACATGCGCGCCAGGGTCGCCATGCACCTCGTGTGCCCC
TCGCGTTACGAGGCAGCCGTGCCCGACCCCCGGGAGCCGGGGGAGTTTGCCCTGCTGCGG
TCCTGCCAGGAGGTCTTTGACAAGCTAGCCAGGGTGGCCCAGCCCGGGATTAATTATGCG
CTGGGCACCAATGTCTCCTACCCCAATAACCTGCTGAGGAATCTGGCTCGTGAGGGGGCC
AACTATGCCCTGGTGATCGATGTGGACATGGTGCCCAGCGAGGGGCTGTGGAGAGGCCTG
CGGGAAATGCTGGATCAGAGCAACCAGTGGGGAGGCACCGCGCTGGTGGTGCCTGCCTTC
GAAATCCGAAGAGCCCGCCGCATGCCCATGAACAAAAACGAGCTGGTGCAGCTCTACCAG
GTTGGCGAGGTGCGGCCCTTCTATTATGGGTTGTGCACCCCCTGCCAGGCACCCACCAAC
TATTCCCGCTGGGTCAACCTGCCGGAAGAGAGCTTGCTGCGGCCCGCCTACGTGGTACCT
TGGCAGGACCCCTGGGAGCCATTCTACGTGGCAGGAGGCAAGGTGCCCACCTTCGACGAG
CGCTTTCGGCAGTACGGCTTCAACCGAATCAGCCAGGCCTGCGAGCTGCATGTGGCGGGG
TTTGATTTTGAGGTCCTGAACGAAGGTTTCTTGGTTCATAAGGGCTTCAAAGAAGCGTTG
AAGTTCCATCCCCAAAAGGAGGCTGAAAATCAGCACAATAAGATCCTATATCGCCAGTTC
AAACAGGAGTTGAAGGCCAAGTACCCCAACTCTCCCCGACGCTGCTGA
|
| Enzyme 9 GenBank Gene ID |
AF029893  |
| Enzyme 9 GeneCard ID |
B3GNT1  |
| Enzyme 9 GenAtlas ID |
B3GNT1  |
| Enzyme 9 HGNC ID |
HGNC:15685  |
| Enzyme 9 Chromosome Location |
11 |
| Enzyme 9 Locus |
11q13.1 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Sasaki K, Kurata-Miura K, Ujita M, Angata K, Nakagawa S, Sekine S, Nishi T, Fukuda M: Expression cloning of cDNA encoding a human beta-1,3-N-acetylglucosaminyltransferase that is essential for poly-N-acetyllactosamine synthesis. Proc Natl Acad Sci U S A. 1997 Dec 23;94(26):14294-9. [PubMed
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
7043 |
| Enzyme 10 Name |
Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase V |
| Enzyme 10 Synonyms |
- Mannoside acetylglucosaminyltransferase 5
- Alpha- mannoside beta-1,6-N-acetylglucosaminyltransferase
- N- acetylglucosaminyl-transferase V
- GNT-V
- GlcNAc-T V
|
| Enzyme 10 Gene Name |
MGAT5 |
| Enzyme 10 Protein Sequence |
>Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase V
MALFTPWKLSSQKLGFFLVTFGFIWGMMLLHFTIQQRTQPESSSMLREQILDLSKRYIKA
LAEENRNVVDGPYAGVMTAYDLKKTLAVLLDNILQRIGKLESKVDNLVVNGTGTNSTNST
TAVPSLVALEKINVADIINGAQEKCVLPPMDGYPHCEGKIKWMKDMWRSDPCYADYGVDG
STCSFFIYLSEVENWCPHLPWRAKNPYEEADHNSLAEIRTDFNILYSMMKKHEEFRWMRL
RIRRMADAWIQAIKSLAEKQNLEKRKRKKVLVHLGLLTKESGFKIAETAFSGGPLGELVQ
WSDLITSLYLLGHDIRISASLAELKEIMKKVVGNRSGCPTVGDRIVELIYIDIVGLAQFK
KTLGPSWVHYQCMLRVLDSFGTEPEFNHANYAQSKGHKTPWGKWNLNPQQFYTMFPHTPD
NSFLGFVVEQHLNSSDIHHINEIKRQNQSLVYGKVDSFWKNKKIYLDIIHTYMEVHATVY
GSSTKNIPSYVKNHGILSGRDLQFLLRETKLFVGLGFPYEGPAPLEAIANGCAFLNPKFN
PPKSSKNTDFFIGKPTLRELTSQHPYAEVFIGRPHVWTVDLNNQEEVEDAVKAILNQKIE
PYMPYEFTCEGMLQRINAFIEKQDFCHGQVMWPPLSALQVKLAEPGQSCKQVCQESQLIC
EPSFFQHLNKDKDMLKYKVTCQSSELAKDILVPSFDPKNKHCVFQGDLLLFSCAGAHPRH
QRVCPCRDFIKGQVALCKDCL
|
| Enzyme 10 Number of Residues |
741 |
| Enzyme 10 Molecular Weight |
84544 |
| Enzyme 10 Theoretical pI |
8.21 |
| Enzyme 10 GO Classification |
Not Available |
| Enzyme 10 General Function |
Not Available |
| Enzyme 10 Specific Function |
Catalyzes the addition of N-acetylglucosamine in beta 1- 6 linkage to the alpha-linked mannose of biantennary N-linked oligosaccharides. It is one of the most important enzymes involved in the regulation of the biosynthesis of glycoprotein oligosaccharides |
| Enzyme 10 Pathways |
|
| Enzyme 10 Reactions |
- UDP-N-acetyl-D-glucosamine + 6-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R = UDP + 6-(2,6-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
|
| Enzyme 10 Pfam Domain Function |
Not Available |
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
Not Available |
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
870752  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
Q09328  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
MGAT5_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>2226 bp
ATGGCTCTCTTCACTCCGTGGAAGTTGTCCTCTCAGAAGCTGGGCTTTTTCCTGGTGACT
TTTGGCTTCATTTGGGGTATGATGCTTCTGCACTTTACCATCCAGCAGCGAACTCAGCCT
GAAAGCAGCTCCATGCTGCGCGAGCAGATCCTGGACCTCAGCAAAAGGTACATCAAGGCA
CTGGCAGAAGAAAACAGGAATGTGGTGGATGGGCCATACGCTGGAGTCATGACAGCTTAT
GATCTGAAGAAAACCCTTGCTGTGTTATTAGATAACATTTTGCAGCGCATTGGCAAGTTG
GAGTCGAAGGTGGACAATCTTGTTGTCAATGGCACCGGAACAAACTCAACCAACTCCACT
ACAGCTGTTCCCAGCTTGGTTGCACTTGAGAAAATTAATGTGGCAGATATCATTAACGGA
GCTCAAGAAAAATGTGTATTGCCTCCTATGGACGGCTACCCTCACTGTGAGGGAAAGATC
AAGTGGATGAAAGACATGTGGCGTTCAGATCCCTGCTACGCAGACTATGGAGTGGATGGA
TCCACCTGCTCTTTTTTTATTTACCTCAGTGAGGTTGAAAATTGGTGTCCTCATTTACCT
TGGAGAGCAAAAAATCCCTACGAAGAAGCTGATCATAATTCATTGGCGGAAATTCGTACA
GATTTTAATATTCTCTACAGTATGATGAAAAAGCATGAAGAATTCCGGTGGATGAGACTA
CGGATCCGGCGAATGGCTGACGCATGGATCCAAGCAATCAAGTCCCTGGCAGAAAAGCAG
AACCTTGAAAAGAGAAAGCGGAAGAAAGTCCTCGTTCACCTGGGACTCCTGACCAAGGAA
TCTGGATTTAAGATTGCAGAGACAGCTTTCAGTGGTGGCCCTCTTGGTGAATTAGTTCAA
TGGAGTGATTTAATTACATCTCTGTACTTACTGGGCCATGACATTAGGATTTCAGCTTCA
CTGGCTGAGCTCAAGGAAATCATGAAGAAGGTTGTAGGAAACCGATCTGGCTGCCCAACT
GTAGGAGACAGAATTGTTGAGCTCATTTACATTGATATTGTAGGACTTGCTCAATTCAAG
AAAACTCTTGGACCATCCTGGGTTCATTACCAGTGCATGCTCCGAGTCCTTGATTCATTT
GGTACTGAACCCGAATTTAATCATGCAAATTATGCCCAATCGAAAGGCCACAAGACCCCT
TGGGGAAAATGGAATCTGAACCCTCAGCAGTTTTATACCATGTTCCCTCATACCCCAGAC
AACAGCTTTCTGGGGTTTGTGGTTGAGCAGCACCTGAACTCCAGTGATATCCACCACATT
AATGAAATCAAAAGGCAGAACCAGTCCCTTGTGTATGGCAAAGTGGATAGCTTCTGGAAG
AATAAGAAGATCTACTTGGACATTATTCACACATACATGGAAGTGCATGCAACTGTTTAT
GGCTCCAGCACAAAGAATATTCCCAGTTACGTGAAAAACCATGGTATCCTCAGTGGACGG
GACCTGCAGTTCCTTCTTCGAGAAACCAAGTTGTTTGTTGGACTTGGGTTCCCTTACGAG
GGCCCAGCTCCCCTGGAAGCTATCGCAAATGGATGTGCTTTTCTGAATCCCAAGTTCAAC
CCACCCAAAAGCAGCAAAAACACAGACTTTTTCATTGGCAAGCCAACTCTGAGAGAGCTG
ACATCCCAGCATCCTTACGCTGAAGTTTTCATCGGGCGGCCACATGTGTGGACTGTTGAC
CTCAACAATCAGGAGGAAGTAGAGGATGCAGTGAAAGCAATTTTAAATCAGAAGATTGAG
CCATACATGCCATATGAATTTACGTGCGAGGGGATGCTACAGAGAATCAATGCTTTCATT
GAAAAACAGGACTTCTGCCATGGGCAAGTGATGTGGCCACCCCTCAGCGCCCTACAGGTC
AAGCTTGCTGAGCCCGGGCAGTCCTGCAAGCAGGTGTGCCAGGAGAGCCAGCTCATCTGC
GAGCCTTCTTTCTTCCAGCACCTCAACAAGGACAAGGACATGCTGAAGTACAAGGTGACC
TGCCAAAGCTCAGAGCTGGCCAAGGACATCCTGGTGCCCTCCTTTGACCCTAAGAATAAG
CACTGTGTGTTTCAAGGTGACCTCCTGCTCTTCAGCTGTGCAGGCGCCCACCCCAGGCAC
CAGAGGGTCTGCCCCTGCCGGGACTTCATCAAGGGCCAGGTGGCTCTCTGCAAAGACTGC
CTATAG
|
| Enzyme 10 GenBank Gene ID |
D17716  |
| Enzyme 10 GeneCard ID |
MGAT5  |
| Enzyme 10 GenAtlas ID |
MGAT5  |
| Enzyme 10 HGNC ID |
HGNC:7049  |
| Enzyme 10 Chromosome Location |
2 |
| Enzyme 10 Locus |
2q21 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Saito H, Nishikawa A, Gu J, Ihara Y, Soejima H, Wada Y, Sekiya C, Niikawa N, Taniguchi N: cDNA cloning and chromosomal mapping of human N-acetylglucosaminyltransferase V+. Biochem Biophys Res Commun. 1994 Jan 14;198(1):318-27. [PubMed
]
- Park C, Jin UH, Lee YC, Cho TJ, Kim CH: Characterization of UDP-N-acetylglucosamine:alpha-6-d-mannoside beta-1,6-N-acetylglucosaminyltransferase V from a human hepatoma cell line Hep3B. Arch Biochem Biophys. 1999 Jul 15;367(2):281-8. [PubMed
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
7046 |
| Enzyme 11 Name |
Hyaluronan synthase 3 |
| Enzyme 11 Synonyms |
- Hyaluronate synthase 3
- Hyaluronic acid synthase 3
- HA synthase 3
|
| Enzyme 11 Gene Name |
HAS3 |
| Enzyme 11 Protein Sequence |
>Hyaluronan synthase 3
MPVQLTTALRVVGTSLFALAVLGGILAAYVTGYQFIHTEKHYLSFGLYGAILGLHLLIQS
LFAFLEHRRMRRAGQALKLPSPRRGSVALCIAAYQEDPDYLRKCLRSAQRISFPDLKVVM
VVDGNRQEDAYMLDIFHEVLGGTEQAGFFVWRSNFHEAGEGETEASLQEGMDRVRDVVRA
STFSCIMQKWGGKREVMYTAFKALGDSVDYIQVCDSDTVLDPACTIEMLRVLEEDPQVGG
VGGDVQILNKYDSWISFLSSVRYWMAFNVERACQSYFGCVQCISGPLGMYRNSLLQQFLE
DWYHQKFLGSKCSFGDDRHLTNRVLSLGYRTKYTARSKCLTETPTKYLRWLNQQTRWSKS
YFREWLYNSLWFHKHHLWMTYESVVTGFFPFFLIATVIQLFYRGRIWNILLFLLTVQLVG
IIKATYACFLRGNAEMIFMSLYSLLYMSSLLPAKIFAIATINKSGWGTSGRKTIVVNFIG
LIPVSIWVAVLLEGLAYTAYCQDLFSETELAFLVSGAILYGCYWVALLMLYLAIIARRCG
KKPEQYSLAFAEV
|
| Enzyme 11 Number of Residues |
553 |
| Enzyme 11 Molecular Weight |
63071 |
| Enzyme 11 Theoretical pI |
8.48 |
| Enzyme 11 GO Classification |
Not Available |
| Enzyme 11 General Function |
Cell wall/membrane/envelope biogenesis |
| Enzyme 11 Specific Function |
Plays a role in hyaluronan/hyaluronic acid (HA) synthesis |
| Enzyme 11 Pathways |
Not Available |
| Enzyme 11 Reactions |
- n UDP-N-acetyl-D-glucosamine + n UDP-D-glucuronate = [beta-N-acetyl-D-glucosaminyl(1-> 4)beta-D-glucuronosyl(1-> 3)]n+ 2n UDP
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
Not Available |
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
7110558  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
O00219  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
HAS3_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>1662 bp
ATGCCGGTGCAGCTGACGACAGCCCTGCGTGTGGTGGGCACCAGCCTGTTTGCCCTGGCA
GTGCTGGGTGGCATCCTGGCAGCCTATGTGACGGGCTACCAGTTCATCCACACGGAAAAG
CACTACCTGTCCTTCGGCCTGTACGGCGCCATCCTGGGCCTGCACCTGCTCATTCAGAGC
CTTTTTGCCTTCCTGGAGCACCGGCGCATGCGACGTGCCGGCCAGGCCCTGAAGCTGCCC
TCCCCGCGGCGGGGCTCGGTGGCACTGTGCATTGCCGCATACCAGGAGGACCCTGACTAC
TTGCGCAAGTGCCTGCGCTCGGCCCAGCGCATCTCCTTCCCTGACCTCAAGGTGGTCATG
GTGGTGGATGGCAACCGCCAGGAGGACGCCTACATGCTGGACATCTTCCACGAGGTGCTG
GGCGGCACCGAGCAGGCCGGCTTCTTTGTGTGGCGCAGCAACTTCCATGAGGCAGGCGAG
GGTGAGACGGAGGCCAGCCTGCAGGAGGGCATGGACCGTGTGCGGGATGTGGTGCGGGCC
AGCACCTTCTCGTGCATCATGCAGAAGTGGGGAGGCAAGCGCGAGGTCATGTACACGGCC
TTCAAGGCCCTCGGCGATTCGGTGGACTACATCCAGGTGTGCGACTCTGACACTGTGCTG
GATCCAGCCTGCACCATCGAGATGCTTCGAGTCCTGGAGGAGGATCCCCAAGTAGGGGGA
GTCGGGGGAGATGTCCAGATCCTCAACAAGTACGACTCATGGATTTCCTTCCTGAGCAGC
GTGCGGTACTGGATGGCCTTCAACGTGGAGCGGGCCTGCCAGTCCTACTTTGGCTGTGTG
CAGTGTATTAGTGGGCCCTTGGGCATGTACCGCAACAGCCTCCTCCAGCAGTTCCTGGAG
GACTGGTACCATCAGAAGTTCCTAGGCAGCAAGTGCAGCTTCGGGGATGACCGGCACCTC
ACCAACCGAGTCCTGAGCCTTGGCTACCGAACTAAGTATACCGCGCGCTCCAAGTGCCTC
ACAGAGACCCCCACTAAGTACCTCCGGTGGCTCAACCAGCAAACCCGCTGGAGCAAGTCT
TACTTCCGGGAGTGGCTCTACAACTCTCTGTGGTTCCATAAGCACCACCTCTGGATGACC
TACGAGTCAGTGGTCACGGGTTTCTTCCCCTTCTTCCTCATTGCCACGGTTATACAGCTT
TTCTACCGGGGCCGCATCTGGAACATTCTCCTCTTCCTGCTGACGGTGCAGCTGGTGGGC
ATTATCAAGGCCACCTACGCCTGCTTCCTTCGGGGCAATGCAGAGATGATCTTCATGTCC
CTCTACTCCCTCCTCTATATGTCCAGCCTTCTGCCGGCCAAGATCTTTGCCATTGCTACC
ATCAACAAATCTGGCTGGGGCACCTCTGGCCGAAAAACCATTGTGGTGAACTTCATTGGC
CTCATTCCTGTGTCCATCTGGGTGGCAGTTCTCCTGGAGGGGCTGGCCTACACAGCTTAT
TGCCAGGACCTGTTCAGTGAGACAGAGCTAGCCTTCCTTGTCTCTGGGGCTATACTGTAT
GGCTGCTACTGGGTGGCCCTCCTCATGCTATATCTGGCCATCATCGCCCGGCGATGTGGG
AAGAAGCCGGAGCAGTACAGCTTGGCTTTTGCTGAGGTGTGA
|
| Enzyme 11 GenBank Gene ID |
AF232772  |
| Enzyme 11 GeneCard ID |
HAS3  |
| Enzyme 11 GenAtlas ID |
HAS3  |
| Enzyme 11 HGNC ID |
HGNC:4820  |
| Enzyme 11 Chromosome Location |
16 |
| Enzyme 11 Locus |
16q22.1 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Spicer AP, Olson JS, McDonald JA: Molecular cloning and characterization of a cDNA encoding the third putative mammalian hyaluronan synthase. J Biol Chem. 1997 Apr 4;272(14):8957-61. [PubMed
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
7047 |
| Enzyme 12 Name |
Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase |
| Enzyme 12 Synonyms |
- N-glycosyl-oligosaccharide-glycoprotein N- acetylglucosaminyltransferase III
- N-acetylglucosaminyltransferase III
- GNT-III
- GlcNAc-T III
|
| Enzyme 12 Gene Name |
MGAT3 |
| Enzyme 12 Protein Sequence |
>Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase
MKMRRYKLFLMFCMAGLCLISFLHFFKTLSYVTFPRELASLSPNLVSSFFWNNAPVTPQA
SPEPGGPDLLRTPLYSHSPLLQPLPPSKAAEELHRVDLVLPEDTTEYFVRTKAGGVCFKP
GTKMLERPPPGRPEEKPEGANGSSARRPPRYLLSARERTGGRGARRKWVECVCLPGWHGP
SCGVPTVVQYSNLPTKERLVPREVPRRVINAINVNHEFDLLDVRFHELGDVVDAFVVCES
NFTAYGEPRPLKFREMLTNGTFEYIRHKVLYVFLDHFPPGGRQDGWIADDYLRTFLTQDG
VSRLRNLRPDDVFIIDDADEIPARDGVLFLKLYDGWTEPFAFHMRKSLYGFFWKQPGTLE
VVSGCTVDMLQAVYGLDGIRLRRRQYYTMPNFRQYENRTGHILVQWSLGSPLHFAGWHCS
WCFTPEGIYFKLVSAQNGDFPRWGDYEDKRDLNYIRGLIRTGGWFDGTQQEYPPADPSEH
MYAPKYLLKNYDRFHYLLDNPYQEPRSTAAGGWRHRGPEGRPPARGKLDEAEV
|
| Enzyme 12 Number of Residues |
533 |
| Enzyme 12 Molecular Weight |
61314 |
| Enzyme 12 Theoretical pI |
8.37 |
| Enzyme 12 GO Classification |
| Function |
- UDP-glycosyltransferase activity
- acetylglucosaminyltransferase activity
- beta-1,4-mannosylglycoprotein 4-beta-N-acetylglucosaminyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring glycosyl groups
|
| 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 |
It is involved in the regulation of the biosynthesis and biological function of glycoprotein oligosaccharides. Catalyzes the addition of N-acetylglucosamine in beta 1-4 linkage to the beta-linked mannose of the trimannosyl core of N-linked sugar chains. It is one of the most important enzymes involved in the regulation of the biosynthesis of glycoprotein oligosaccharides |
| Enzyme 12 Pathways |
|
| Enzyme 12 Reactions |
- UDP-N-acetyl-D-glucosamine + beta-D-mannosyl-R = UDP + 4-(N-acetyl-beta-D-glucosaminyl)-beta-D-mannosyl-R
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
Not Available |
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
398138  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
Q09327  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
MGAT3_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>1596 bp
ATGAGACGCTACAAGCTCTTTCTCATGTTCTGTATGGCCGGCCTGTGCCTCATCTCCTTC
CTGCACTTCTTCAAGACCCTGTCCTATGTCACCTTCCCCCGAGAACTGGCCTCCCTCAGC
CCTAACCTGGTGTCCAGCTTTTTCTGGAACAATGCCCCGGTCACGCCCCAGGCCAGCCCC
GAGCCAGGAGGCCCTGACCTGCTGCGTACCCCACTCTACTCCCACTCGCCCCTGCTGCAG
CCGCTGCCGCCCAGCAAGGCGGCCGAGGAGCTCCACCGGGTGGACTTGGTGCTGCCCGAG
GACACCACCGAGTATTTCGTGCGCACCAAGGCCGGCGGCGTCTGCTTCAAACCCGGCACC
AAGATGCTGGAGAGGCCGCCCCCGGGACGGCCGGAGGAGAAGCCTGAGGGGGCCAACGGC
TCCTCGGCCCGGCGGCCACCCCGGTACCTCCTGAGCGCCCGGGAGCGCACGGGGGGCCGA
GGCGCCCGGCGCAAGTGGGTGGAGTGCGTGTGCCTGCCCGGCTGGCACGGACCCAGCTGC
GGCGTGCCCACTGTGGTGCAGTACTCCAACCTGCCCACCAAGGAGCGGCTGGTGCCCAGG
GAGGTGCCGCGCCGCGTCATCAACGCCATCAACGTCAACCACGAGTTCGACCTGCTGGAC
GTGCGCTTCCACGAGCTGGGCGACGTGGTGGACGCCTTTGTGGTGTGCGAGTCCAACTTC
ACGGCTTATGGGGAGCCGCGGCCGCTCAAGTTCCGGGAGATGCTGACCAATGGCACCTTC
GAGTACATCCGCCACAAGGTGCTCTATGTCTTCCTGGACCACTTCCCGCCCGGCGGCCGG
CAGGACGGCTGGATCGCCGACGACTACCTGCGCACCTTCCTCACCCAGGACGGCGTCTCG
CGGCTGCGCAACCTGCGGCCCGACGACGTCTTCATCATTGACGATGCGGACGAGATCCCG
GCCCGTGACGGCGTCCTTTTCCTCAAGCTCTACGATGGCTGGACCGAGCCCTTCGCCTTC
CACATGCGCACGTCGCTCTACGGCTTCTTCTGGAAGCAGCCGGGCACCCTGGAGGTGGTG
TCAGGCTGCACGGTGGACATGCTGCAGGCAGTGTATGGGCTGGACGGCATCCGCCTGCGC
CGCCGCCAGTACTACACCATGCCCAACTTCAGACAGTATGAGAACCGCACCGGCCACATC
CTGGTGCAGTGGTCGCTGGGCAGCCCCCTGCACTTCGCCGGCTGGCACTGCTCCTGGTGC
TTCACGCCCGAGGGCATCTACTTCAAGCTCGTGTCCGCCCAGAATGGCGACTTCCCACGC
TGGGGTGACTACGAGGACAAGCGGGACCTGAACTACATCCGCGGCCTGATCCGCACCGGG
GGCTGGTTCGACGGCACGCAGCAGGAGTACCCGCCTGCAGACCCCAGCGAGCACATGTAT
GCGCCCAAGTACCTGCTGAAGAACTACGACCGGTTCCACTACCTGCTGGACAACCCCTAC
CAGGAGCCCAGGAGCACGGCGGCGGGCGGGTGGCGCCACAGGGGTCCCGAGGGAAGGCCG
CCCGCCCGGGGCAAACTGGACGAGGCGGAAGTCTAG
|
| Enzyme 12 GenBank Gene ID |
D13789  |
| Enzyme 12 GeneCard ID |
MGAT3  |
| Enzyme 12 GenAtlas ID |
MGAT3  |
| Enzyme 12 HGNC ID |
HGNC:7046  |
| Enzyme 12 Chromosome Location |
22 |
| Enzyme 12 Locus |
22q13.1 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- Ihara Y, Nishikawa A, Tohma T, Soejima H, Niikawa N, Taniguchi N: cDNA cloning, expression, and chromosomal localization of human N-acetylglucosaminyltransferase III (GnT-III). J Biochem (Tokyo). 1993 Jun;113(6):692-8. [PubMed
]
- Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
7269 |
| Enzyme 13 Name |
Hyaluronan synthase 2 |
| Enzyme 13 Synonyms |
- Hyaluronate synthase 2
- Hyaluronic acid synthase 2
- HA synthase 2
|
| Enzyme 13 Gene Name |
HAS2 |
| Enzyme 13 Protein Sequence |
>Hyaluronan synthase 2
MHCERFLCILRIIGTTLFGVSLLLGITAAYIVGYQFIQTDNYYFSFGLYGAFLASHLIIQ
SLFAFLEHRKMKKSLETPIKLNKTVALCIAAYQEDPDYLRKCLQSVKRLTYPGIKVVMVI
DGNSEDDLYMMDIFSEVMGRDKSATYIWKNNFHEKGPGETDESHKESSQHVTQLVLSNKS
ICIMQKWGGKREVMYTAFRALGRSVDYVQVCDSDTMLDPASSVEMVKVLEEDPMVGGVGG
DVQILNKYDSWISFLSSVRYWMAFNIERACQSYFGCVQCISGPLGMYRNSLLHEFVEDWY
NQEFMGNQCSFGDDRHLTNRVLSLGYATKYTARSKCLTETPIEYLRWLNQQTRWSKSYFR
EWLYNAMWFHKHHLWMTYEAIITGFFPFFLIATVIQLFYRGKIWNILLFLLTVQLVGLIK
SSFASCLRGNIVMVFMSLYSVLYMSSLLPAKMFAIATINKAGWGTSGRKTIVVNFIGLIP
VSVWFTILLGGVIFTIYKESKRPFSESKQTVLIVGTLLYACYWVMLLTLYVVLINKCGRR
KKGQQYDMVLDV
|
| Enzyme 13 Number of Residues |
552 |
| Enzyme 13 Molecular Weight |
63567 |
| Enzyme 13 Theoretical pI |
8.74 |
| Enzyme 13 GO Classification |
Not Available |
| Enzyme 13 General Function |
Cell wall/membrane/envelope biogenesis |
| Enzyme 13 Specific Function |
Plays a role in hyaluronan/hyaluronic acid (HA) synthesis |
| Enzyme 13 Pathways |
Not Available |
| Enzyme 13 Reactions |
- n UDP-N-acetyl-D-glucosamine + n UDP-D-glucuronate = [beta-N-acetyl-D-glucosaminyl(1-> 4)beta-D-glucuronosyl(1-> 3)]n+ 2n UDP
|
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
Not Available |
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
1543068  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
Q92819  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
HAS2_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>1659 bp
ATGCATTGTGAGAGGTTTCTATGTATCCTGAGAATAATTGGAACCACACTCTTTGGAGTC
TCTCTCCTCCTTGGAATCACAGCTGCTTATATTGTTGGCTACCAGTTTATCCAAACGGAT
AATTACTATTTCTCTTTTGGACTGTATGGTGCCTTTTTGGCATCACACCTCATCATCCAA
AGCCTGTTTGCCTTTTTGGAGCACCGAAAAATGAAAAAATCCCTAGAAACCCCCATAAAG
TTGAACAAAACAGTTGCCCTTTGCATCGCTGCCTATCAAGAAGATCCAGACTACTTAAGG
AAATGTTTGCAATCTGTGAAAAGGCTAACCTACCCTGGGATTAAAGTTGTCATGGTCATA
GATGGGAACTCAGAAGATGACCTTTACATGATGGACATCTTCAGTGAAGTCATGGGCAGA
GACAAATCAGCCACTTATATCTGGAAGAACAACTTCCACGAAAAGGGTCCCGGTGAGACA
GATGAGTCACATAAAGAAAGCTCGCAACACGTAACGCAATTGGTCTTGTCCAACAAAAGT
ATCTGCATCATGCAAAAATGGGGTGGAAAAAGAGAAGTCATGTACACAGCCTTCAGAGCA
CTGGGACGAAGTGTGGATTATGTACAGGTTTGTGATTCAGACACTATGCTTGACCCAGCC
TCATCTGTGGAGATGGTAAAAGTTTTAGAAGAAGATCCCATGGTTGGAGGTGTTGGGGGA
GATGTCCAGATTTTAAACAAGTACGATTCCTGGATCTCATTCCTCAGCAGTGTAAGATAT
TGGATGGCTTTTAATATAGAAAGGGCCTGTCAGTCTTATTTTGGGTGTGTTCAGTGCATT
AGTGGACCTCTGGGAATGTACAGAAACTCCTTGTTGCATGAGTTTGTGGAAGATTGGTAC
AATCAAGAATTTATGGGCAACCAATGTAGCTTTGGTGATGACAGGCATCTCACGAACCGG
GTGCTGAGCCTGGGCTATGCAACAAAATACACAGCTCGATCTAAGTGCCTTACTGAAACA
CCTATAGAGTATCTCAGATGGCTAAACCAGCAGACCCGTTGGAGCAAGTCCTACTTCCGA
GAATGGCTGTACAATGCAATGTGGTTTCACAAACATCACTTGTGGATGACCTACGAAGCG
ATTATCACTGGATTCTTTCCTTTCTTTCTCATTGCCACAGTAATCCAGCTCTTCTACCGG
GGTAAAATTTGGAACATTCTCCTCTTCTTGTTAACTGTCCAGCTAGTAGGTCTCATAAAA
TCATCTTTTGCCAGCTGCCTTAGAGGAAATATCGTCATGGTCTTCATGTCTCTCTACTCA
GTGTTATACATGTCGAGTTTACTTCCCGCCAAGATGTTTGCAATTGCAACAATAAACAAA
GCTGGGTGGGGCACATCAGGAAGGAAAACCATTGTTGTTAATTTCATAGGACTCATTCCA
GTATCAGTTTGGTTTACAATCCTCCTGGGTGGTGTGATTTTCACCATTTATAAGGAGTCT
AAAAGGCCATTTTCAGAATCCAAACAGACAGTTCTAATTGTTGGAACGTTGCTCTATGCA
TGCTATTGGGTCATGCTTTTGACGCTGTATGTAGTTCTCATCAATAAGTGTGGCAGGCGG
AAGAAGGGACAACAATATGACATGGTGCTTGATGTATGA
|
| Enzyme 13 GenBank Gene ID |
U54804  |
| Enzyme 13 GeneCard ID |
HAS2  |
| Enzyme 13 GenAtlas ID |
HAS2  |
| Enzyme 13 HGNC ID |
HGNC:4819  |
| Enzyme 13 Chromosome Location |
8 |
| Enzyme 13 Locus |
8q24.12 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- Watanabe K, Yamaguchi Y: Molecular identification of a putative human hyaluronan synthase. J Biol Chem. 1996 Sep 20;271(38):22945-8. [PubMed
]
|
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
8392 |
| Enzyme 14 Name |
N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase |
| Enzyme 14 Synonyms |
- N-acetylglucosaminyltransferase
- I-branching enzyme
- IGNT
|
| Enzyme 14 Gene Name |
GCNT2 |
| Enzyme 14 Protein Sequence |
>N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase
MPLSMRYLFIISVSSVIIFIVFSVFNFGGDPSFQRLNISDPLRLTQVCTSFINGKTRFLW
KNKLMIHEKSSCKEYLTQSHYITAPLSKEEADFPLAYIMVIHHHFDTFARLFRAIYMPQN
IYCVHVDEKATTEFKDAVEQLLSCFPNAFLASKMEPVVYGGISRLQADLNCIRDLSAFEV
SWKYVINTCGQDFPLKTNKEIVQYLKGFKGKNITPGVLPPAHAIGRTKYVHQEHLGKELS
YVIRTTALKPPPPHNLTIYFGSAYVALSREFANFVLHDPRAVDLLQWSKDTFSPDEHFWV
TLNRIPGVPGSMPNASWTGNLRAIKWSDMEDRHGGCHGHYVHGICIYGNGDLKWLVNSPS
LFANKFELNTYPLTVECLELRHRERTLNQSETAIQPSWYF
|
| Enzyme 14 Number of Residues |
400 |
| Enzyme 14 Molecular Weight |
45855 |
| Enzyme 14 Theoretical pI |
8.32 |
| Enzyme 14 GO Classification |
| Function |
- UDP-glycosyltransferase activity
- acetylglucosaminyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring glycosyl groups
|
| Process |
| — |
| Component |
|
|
| Enzyme 14 General Function |
Not Available |
| Enzyme 14 Specific Function |
Branching enzyme that converts linear into branched poly-N-acetyllactosaminoglycans. Introduces the blood group I antigen during embryonic development. It is closely associated with the development and maturation of erythroid cells |
| Enzyme 14 Pathways |
- Blood group glycolipid biosynthesis-neolactoseries (map00602
)
|
| Enzyme 14 Reactions |
- UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,6-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
|
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
Not Available |
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
307298  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
Q06430  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
GCNT2_HUMAN  |
| Enzyme 14 PDB ID |
Not Available |
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>1203 bp
ATGCCTTTATCAATGCGTTACCTCTTCATAATTTCTGTCTCTAGTGTAATTATTTTTATC
GTCTTCTCTGTGTTCAATTTTGGGGGAGATCCAAGCTTCCAAAGGCTAAATATCTCAGAC
CCTTTGAGGCTGACTCAAGTTTGCACATCTTTTATCAATGGAAAAACACGTTTCCTGTGG
AAAAACAAACTAATGATCCATGAGAAGTCTTCTTGCAAGGAATACTTGACCCAGAGCCAC
TACATCACAGCCCCTTTATCTAAGGAAGAAGCTGACTTTCCCTTGGCATATATAATGGTC
ATCCATCATCACTTTGACACCTTTGCAAGGCTCTTCAGGGCTATTTACATGCCCCAAAAT
ATCTACTGTGTTCATGTGGATGAAAAAGCAACAACTGAATTTAAAGATGCGGTAGAGCAA
CTATTAAGCTGCTTCCCAAACGCTTTTCTGGCTTCCAAGATGGAACCCGTTGTCTATGGA
GGGATCTCCAGGCTCCAGGCTGACCTGAACTGCATCAGAGATCTTTCTGCCTTCGAGGTC
TCATGGAAGTACGTTATCAACACCTGTGGGCAAGACTTCCCCCTGAAAACCAACAAGGAA
ATAGTTCAGTATCTGAAAGGATTTAAAGGTAAAAATATCACCCCAGGGGTGCTGCCCCCA
GCTCATGCAATTGGACGGACTAAATATGTCCACCAAGAGCACCTGGGCAAAGAGCTTTCC
TATGTGATAAGAACAACAGCGTTGAAACCGCCTCCCCCCCATAATCTCACAATTTACTTT
GGCTCTGCCTATGTGGCTCTATCAAGAGAGTTTGCCAACTTTGTTCTGCATGACCCACGG
GCTGTTGATTTGCTCCAGTGGTCCAAGGACACTTTCAGTCCTGATGAGCATTTCTGGGTG
ACACTCAATAGGATTCCAGGTGTTCCTGGCTCTATGCCAAATGCATCCTGGACTGGAAAC
CTCAGAGCTATAAAGTGGAGTGACATGGAAGACAGACACGGAGGCTGCCACGGCCACTAT
GTACATGGTATTTGTATCTATGGAAACGGAGACTTAAAGTGGCTGGTTAATTCACCAAGC
CTGTTTGCTAACAAGTTTGAGCTTAATACCTACCCCCTTACTGTGGAATGCCTAGAACTG
AGGCATCGCGAAAGAACCCTCAATCAGAGTGAAACTGCGATACAACCCAGCTGGTATTTT
TGA
|
| Enzyme 14 GenBank Gene ID |
L19659  |
| Enzyme 14 GeneCard ID |
GCNT2  |
| Enzyme 14 GenAtlas ID |
GCNT2  |
| Enzyme 14 HGNC ID |
HGNC:4204  |
| Enzyme 14 Chromosome Location |
6 |
| Enzyme 14 Locus |
6p24 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- Bierhuizen MF, Mattei MG, Fukuda M: Expression of the developmental I antigen by a cloned human cDNA encoding a member of a beta-1,6-N-acetylglucosaminyltransferase gene family. Genes Dev. 1993 Mar;7(3):468-78. [PubMed
]
- Bierhuizen MF, Maemura K, Kudo S, Fukuda M: Genomic organization of core 2 and I branching beta-1,6-N-acetylglucosaminyltransferases. Implication for evolution of the beta-1,6-N-acetylglucosaminyltransferase gene family. Glycobiology. 1995 Jun;5(4):417-25. [PubMed
]
- Sasaki K, Kurata-Miura K, Ujita M, Angata K, Nakagawa S, Sekine S, Nishi T, Fukuda M: Expression cloning of cDNA encoding a human beta-1,3-N-acetylglucosaminyltransferase that is essential for poly-N-acetyllactosamine synthesis. Proc Natl Acad Sci U S A. 1997 Dec 23;94(26):14294-9. [PubMed
]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
8492 |
| Enzyme 15 Name |
UDP-N-acetylglucosamine transporter |
| Enzyme 15 Synonyms |
- Golgi UDP-GlcNAc transporter
- Solute carrier family 35 member A3
|
| Enzyme 15 Gene Name |
SLC35A3 |
| Enzyme 15 Protein Sequence |
>UDP-N-acetylglucosamine transporter
MFANLKYVSLGILVFQTTSLVLTMRYSRTLKEEGPRYLSSTAVVVAELLKIMACILLVYK
DSKCSLRALNRVLHDEILNKPMETLKLAIPSGIYTLQNNLLYVALSNLDAATYQVTYQLK
ILTTALFSVSMLSKKLGVYQWLSLVILMTGVAFVQWPSDSQLDSKELSAGSQFVGLMAVL
TACFSSGFAGVYFEKILKETKQSVWIRNIQLGFFGSIFGLMGVYIYDGELVSKNGFFQGY
NRLTWIVVVLQALGGLVIAAVIKYADNILKGFATSLSIILSTLISYFWLQDFVPTSVFFL
GAILVITATFLYGYDPKPAGNPTKA
|
| Enzyme 15 Number of Residues |
325 |
| Enzyme 15 Molecular Weight |
35985 |
| Enzyme 15 Theoretical pI |
9.51 |
| Enzyme 15 GO Classification |
| Function |
- carbohydrate transporter activity
- carrier activity
- electrochemical potential-driven transporter activity
- nucleotide-sugar transporter activity
- porter activity
- sugar porter activity
- transporter activity
|
| Process |
- carbohydrate transport
- cellular physiological process
- nucleotide-sugar transport
- physiological process
- transport
|
| Component |
- Golgi membrane
- cell
- integral to membrane
- intrinsic to membrane
- membrane
- organelle membrane
|
|
| Enzyme 15 General Function |
Carbohydrate transport and metabolism |
| Enzyme 15 Specific Function |
Uridine diphosphate-N-acetylglucosamine transporter in the Golgi apparatus |
| Enzyme 15 Pathways |
Not Available |
| Enzyme 15 Reactions |
Not Available |
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
- 8-24
42-58
138-154
173-189
209-225
246-262
268-284
295-311
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
4903004  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
Q9Y2D2  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
S35A3_HUMAN  |
| Enzyme 15 PDB ID |
Not Available |
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>978 bp
ATGTTCGCCAACCTAAAATACGTTTCCCTGGGAATTTTGGTCTTTCAGACTACCAGTTTG
GTTCTAACAATGCGTTATTCCAGAACTTTAAAAGAAGAAGGACCTCGTTATCTATCTTCT
ACAGCAGTGGTTGTTGCTGAACTTTTGAAGATAATGGCCTGCATTTTATTGGTCTACAAA
GACAGCAAATGTAGTCTAAGAGCACTGAATCGAGTACTACATGATGAAATTCTTAATAAA
CCTATGGAAACACTTAAACTTGCTATTCCATCAGGGATCTATACTCTTCAGAATAATTTA
CTGTATGTGGCACTATCAAATCTAGATGCAGCTACTTATCAGGTCACGTATCAGTTAAAA
ATTCTTACAACAGCATTATTTTCTGTGTCTATGCTTAGTAAAAAATTGGGTGTATACCAG
TGGCTGTCCCTAGTAATTTTGATGACAGGAGTTGCTTTTGTACAGTGGCCCTCAGATTCT
CAGCTTGATTCTAAGGAACTTTCAGCTGGTTCTCAATTTGTAGGACTCATGGCAGTTCTC
ACAGCATGTTTTTCAAGTGGCTTTGCTGGGGTTTACTTTGAGAAAATCTTAAAAGAAACA
AAACAATCAGTGTGGATAAGAAATATTCAGCTTGGTTTCTTTGGAAGTATATTTGGATTA
ATGGGTGTATACATTTATGATGGAGAACTGGTATCAAAGAATGGATTTTTTCAGGGATAT
AACCGACTGACCTGGATAGTAGTTGTTCTTCAGGCACTTGGAGGCCTTGTAATAGCTGCT
GTTATTAAGTATGCAGATAATATTTTAAAAGGATTTGCAACCTCTTTATCGATAATATTA
TCAACATTGATCTCCTATTTTTGGCTTCAAGATTTTGTGCCAACCAGTGTCTTTTTCCTT
GGAGCCATCCTTGTAATAACAGCTACTTTTTTGTATGGTTATGATCCCAAACCTGCAGGA
AATCCCACTAAAGCATAG
|
| Enzyme 15 GenBank Gene ID |
AB021981  |
| Enzyme 15 GeneCard ID |
SLC35A3  |
| Enzyme 15 GenAtlas ID |
SLC35A3  |
| Enzyme 15 HGNC ID |
HGNC:11023  |
| Enzyme 15 Chromosome Location |
1 |
| Enzyme 15 Locus |
1p21 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- Ishida N, Yoshioka S, Chiba Y, Takeuchi M, Kawakita M: Molecular cloning and functional expression of the human Golgi UDP-N-acetylglucosamine transporter. J Biochem. 1999 Jul;126(1):68-77. [PubMed
]
|
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
8792 |
| Enzyme 16 Name |
Beta-1,3-N-acetylglucosaminyltransferase bGnT-2 |
| Enzyme 16 Synonyms |
- Hypothetical protein B3GNT1
|
| Enzyme 16 Gene Name |
bGnT-2 |
| Enzyme 16 Protein Sequence |
>Beta-1,3-N-acetylglucosaminyltransferase bGnT-2
MSVGRRRIKLLGILMMANVFIYFIMEVSKSSSQEKNGKGEVIIPKEKFWKISTPPEAYWN
REQEKLNRQYNPILSMLTNQTGEAGRLSNISHLNYCEPDLRVTSVVTGFNNLPDRFKDFL
LYLRCRNYSLLIDQPDKCAKKPFLLLAIKSLTPHFARRQAIRESWGQESNAGNQTVVRVF
LLGQTPPEDNHPDLSDMLKFESEKHQDILMWNYRDTFFNLSLKEVLFLRWVSTSCPDTEF
VFKGDDDVFVNTHHILNYLNSLSKTKAKDLFIGDVIHNAGPHRDKKLKYYIPEVVYSGLY
PPYAGGGGFLYSGHLALRLYHITDQVHLYPIDDVYTGMCLQKLGLVPEKHKGFRTFDIEE
KNKNNICSYVDLMLVHSRKPQEMIDIWSQLQSAHLKC
|
| Enzyme 16 Number of Residues |
397 |
| Enzyme 16 Molecular Weight |
46023 |
| Enzyme 16 Theoretical pI |
8.75 |
| Enzyme 16 GO Classification |
| Function |
- catalytic activity
- galactosyltransferase activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- biopolymer metabolism
- biopolymer modification
- macromolecule metabolism
- metabolism
- physiological process
- protein amino acid glycosylation
- protein modification
|
| Component |
|
|
| Enzyme 16 General Function |
Not Available |
| 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 |
12619294  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
Q54AC1  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
Q54AC1_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>1194 bp
ATGAGTGTTGGACGTCGAAGAATAAAGTTGTTGGGTATCCTGATGATGGCAAATGTCTTC
ATTTATTTTATTATGGAAGTCTCCAAAAGCAGTAGCCAAGAAAAAAATGGAAAAGGGGAA
GTAATAATACCCAAAGAGAAGTTCTGGAAGATATCTACCCCTCCCGAGGCATACTGGAAC
CGAGAGCAAGAGAAGCTGAACCGGCAGTACAACCCCATCCTGAGCATGCTGACCAACCAG
ACGGGGGAGGCGGGCAGGCTCTCCAATATAAGCCATCTGAACTACTGCGAACCTGACCTG
AGGGTCACGTCGGTGGTTACGGGTTTTAACAACTTGCCGGACAGATTTAAAGACTTTCTG
CTGTATTTGAGATGCCGCAATTATTCACTGCTTATAGATCAGCCGGATAAGTGTGCAAAG
AAACCTTTCTTGTTGCTGGCGATTAAGTCCCTCACTCCACATTTTGCCAGAAGGCAAGCA
ATCCGGGAATCCTGGGGCCAAGAAAGCAACGCAGGGAACCAAACGGTGGTGCGAGTCTTC
CTGCTGGGCCAGACACCCCCAGAGGACAACCACCCCGACCTTTCAGATATGCTGAAATTT
GAGAGTGAGAAGCACCAAGACATTCTTATGTGGAACTACAGAGACACTTTCTTCAACTTG
TCTCTGAAGGAAGTGCTGTTTCTCAGGTGGGTAAGTACTTCCTGCCCAGACACTGAGTTT
GTTTTCAAGGGCGATGACGATGTTTTTGTGAACACCCATCACATCCTGAATTACTTGAAT
AGTTTATCCAAGACCAAAGCCAAAGATCTCTTCATAGGTGATGTGATCCACAATGCTGGA
CCTCATCGGGATAAGAAGCTGAAGTACTACATCCCAGAAGTTGTTTACTCTGGCCTCTAC
CCACCCTATGCAGGGGGAGGGGGGTTCCTCTACTCCGGCCACCTGGCCCTGAGGCTGTAC
CATATCACTGACCAGGTCCATCTCTACCCCATTGATGACGTTTATACTGGAATGTGCCTT
CAGAAACTCGGCCTCGTTCCAGAGAAACACAAAGGCTTCAGGACATTTGATATCGAGGAG
AAAAACAAAAATAACATCTGCTCCTATGTAGATCTGATGTTAGTACATAGTAGAAAACCT
CAAGAGATGATTGATATTTGGTCTCAGTTGCAGAGTGCTCATTTAAAATGCTAA
|
| Enzyme 16 GenBank Gene ID |
AB049584  |
| Enzyme 16 GeneCard ID |
bGnT-2  |
| Enzyme 16 GenAtlas ID |
bGnT-2  |
| Enzyme 16 HGNC ID |
HGNC:15629  |
| Enzyme 16 Chromosome Location |
Not Available |
| Enzyme 16 Locus |
Not Available |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- Shiraishi N, Natsume A, Togayachi A, Endo T, Akashima T, Yamada Y, Imai N, Nakagawa S, Koizumi S, Sekine S, Narimatsu H, Sasaki K: Identification and characterization of three novel beta 1,3-N-acetylglucosaminyltransferases structurally related to the beta 1,3-galactosyltransferase family. J Biol Chem. 2001 Feb 2;276(5):3498-507. Epub 2000 Oct 19. [PubMed
]
|
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
11945 |
| Enzyme 17 Name |
Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A |
| Enzyme 17 Synonyms |
- UDP-N-acetylglucosamine: alpha-1,3-D-mannoside beta- 1,4-N-acetylglucosaminyltransferase IVa
- N-glycosyl-oligosaccharide- glycoprotein N-acetylglucosaminyltransferase IVa
- N- acetylglucosaminyltransferase IVa
- GnT-IVa
- GlcNAc-T IVa[Contains: Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A soluble form]
|
| Enzyme 17 Gene Name |
MGAT4A |
| Enzyme 17 Protein Sequence |
>Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A
MRLRNGTVATALAFITSFLTLSWYTTWQNGKEKLIAYQREFLALKERLRIAEHRISQRSS
ELNTIVQQFKRVGAETNGSKDALNKFSDNTLKLLKELTSKKSLQVPSIYYHLPHLLKNEG
SLQPAVQIGNGRTGVSIVMGIPTVKREVKSYLIETLHSLIDNLYPEEKLDCVIVVFIGET
DIDYVHGVVANLEKEFSKEISSGLVEVISPPESYYPDLTNLKETFGDSKERVRWRTKQNL
DYCFLMMYAQEKGIYYIQLEDDIIVKQNYFNTIKNFALQLSSEEWMILEFSQLGFIGKMF
QAPDLTLIVEFIFMFYKEKPIDWLLDHILWVKVCNPEKDAKHCDRQKANLRIRFRPSLFQ
HVGLHSSLSGKIQKLTDKDYMKPLLLKIHVNPPAEVSTSLKVYQGHTLEKTYMGEDFFWA
ITPIAGDYILFKFDKPVNVESYLFHSGNQEHPGDILLNTTVEVLPFKSEGLEISKETKDK
RLEDGYFRIGKFENGVAEGMVDPSLNPISAFRLSVIQNSAVWAILNEIHIKKATN
|
| Enzyme 17 Number of Residues |
535 |
| Enzyme 17 Molecular Weight |
61545 |
| Enzyme 17 Theoretical pI |
Not Available |
| Enzyme 17 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- carbohydrate metabolism
- macromolecule metabolism
- metabolism
- physiological process
|
| Component |
|
|
| Enzyme 17 General Function |
Not Available |
| Enzyme 17 Specific Function |
Glycosyltransferase that participates in the transfer of N-acetylglucosamine (GlcNAc) to the core mannose residues of N- linked glycans. Catalyzes the formation of the GlcNAcbeta1-4 branch on the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans. Essential for the production of tri- and tetra-antennary N-linked sugar chains. Involved in glucose transport by mediating SLC2A2/GLUT2 glycosylation, thereby controlling cell-surface expression of SLC2A2 in pancreatic beta cells |
| Enzyme 17 Pathways |
- Glycan structures - biosynthesis 1 (map01030
)
- N-Glycan biosynthesis (map00510
)
|
| Enzyme 17 Reactions |
- ((N-acetyl-D-glucosaminyl)2-(alpha-D-mannosyl)2-beta-D-mannosyl-diacetylchitobiosyl)-L-asparagine (protein) + UDP-N-acetyl-D-glucosamine --> H+ + ((N-acetyl-D-glucosaminyl)3-(alpha-D-mannosyl)2-beta-D-mannosyl-diacetylchitobiosyl)-L-asparagine (protein) + UDP
|
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
6329074  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
Q9UM21  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
MGT4A_HUMAN  |
| Enzyme 17 PDB ID |
Not Available |
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
Not Available |
| Enzyme 17 GenBank Gene ID |
AB000616  |
| Enzyme 17 GeneCard ID |
Not Available |
| Enzyme 17 GenAtlas ID |
MGAT4A  |
| Enzyme 17 HGNC ID |
HGNC:7047  |
| Enzyme 17 Chromosome Location |
Not Available |
| Enzyme 17 Locus |
Not Available |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
- Yoshida A, Minowa MT, Takamatsu S, Hara T, Oguri S, Ikenaga H, Takeuchi M: Tissue specific expression and chromosomal mapping of a human UDP-N-acetylglucosamine: alpha1,3-d-mannoside beta1, 4-N-acetylglucosaminyltransferase. Glycobiology. 1999 Mar;9(3):303-10. [PubMed
]
|
| Enzyme 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
11946 |
| Enzyme 18 Name |
Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B |
| Enzyme 18 Synonyms |
- UDP-N-acetylglucosamine: alpha-1,3-D-mannoside beta- 1,4-N-acetylglucosaminyltransferase IVb
- N-glycosyl-oligosaccharide- glycoprotein N-acetylglucosaminyltransferase IVb
- N- acetylglucosaminyltransferase IVb
- GnT-IVb
- GlcNAc-T IVb
|
| Enzyme 18 Gene Name |
MGAT4B |
| Enzyme 18 Protein Sequence |
>Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B
MRLRNGTFLTLLLFCLCAFLSLSWYAALSGQKGDVVDVYQREFLALRDRLHAAEQESLKR
SKELNLVLDEIKRAVSERQALRDGDGNRTWGRLTEDPRLKPWNGSHRHVLHLPTVFHHLP
HLLAKESSLQPAVRVGQGRTGVSVVMGIPSVRREVHSYLTDTLHSLISELSPQEKEDSVI
VVLIAETDSQYTSAVTENIKALFPTEIHSGLLEVISPSPHFYPDFSRLRESFGDPKERVR
WRTKQNLDYCFLMMYAQSKGIYYVQLEDDIVAKPNYLSTMKNFALQQPSEDWMILEFSQL
GFIGKMFKSLDLSLIVEFILMFYRDKPIDWLLDHILWVKVCNPEKDAKHCDRQKANLRIR
FKPSLFQHVGTHSSLAGKIQKLKDKDFGKQALRKEHVNPPAEVSTSLKTYQHFTLEKAYL
REDFFWAFTPAAGDFIRFRFFQPLRLERFFFRSGNIEHPEDKLFNTSVEVLPFDNPQSDK
EALQEGRTATLRYPRSPDGYLQIGSFYKGVAEGEVDPAFGPLEALRLSIQTDSPVWVILS
EIFLKKAD
|
| Enzyme 18 Number of Residues |
548 |
| Enzyme 18 Molecular Weight |
63199 |
| Enzyme 18 Theoretical pI |
Not Available |
| Enzyme 18 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- carbohydrate metabolism
- macromolecule metabolism
- metabolism
- physiological process
|
| Component |
|
|
| Enzyme 18 General Function |
Not Available |
| Enzyme 18 Specific Function |
Glycosyltransferase that participates in the transfer of N-acetylglucosamine (GlcNAc) to the core mannose residues of N- linked glycans. Catalyzes the formation of the GlcNAcbeta1-4 branch on the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans. Essential for the production of tri- and tetra-antennary N-linked sugar chains. Has lower affinities for donors or acceptors than MGAT4A, suggesting that, under physiological conditions, it is not the main contributor in N- glycan biosynthesis |
| Enzyme 18 Pathways |
- Glycan structures - biosynthesis 1 (map01030
)
- N-Glycan biosynthesis (map00510
)
|
| Enzyme 18 Reactions |
- ((N-acetyl-D-glucosaminyl)2-(alpha-D-mannosyl)2-beta-D-mannosyl-diacetylchitobiosyl)-L-asparagine (protein) + UDP-N-acetyl-D-glucosamine --> H+ + ((N-acetyl-D-glucosaminyl)3-(alpha-D-mannosyl)2-beta-D-mannosyl-diacetylchitobiosyl)-L-asparagine (protein) + UDP
|
| Enzyme 18 Pfam Domain Function |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
5748487  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
Q9UQ53  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
MGT4B_HUMAN  |
| Enzyme 18 PDB ID |
Not Available |
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
Not Available |
| Enzyme 18 GenBank Gene ID |
AB000624  |
| Enzyme 18 GeneCard ID |
Not Available |
| Enzyme 18 GenAtlas ID |
MGAT4B  |
| Enzyme 18 HGNC ID |
HGNC:7048  |
| Enzyme 18 Chromosome Location |
Not Available |
| Enzyme 18 Locus |
Not Available |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
- Yoshida A, Minowa MT, Takamatsu S, Hara T, Ikenaga H, Takeuchi M: A novel second isoenzyme of the human UDP-N-acetylglucosamine:alpha1,3-D-mannoside beta1,4-N-acetylglucosaminyltransferase family: cDNA cloning, expression, and chromosomal assignment. Glycoconj J. 1998 Dec;15(12):1115-23. [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 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
11996 |
| Enzyme 19 Name |
UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 5 |
| Enzyme 19 Synonyms |
- Beta3Gn-T5
- BGnT-5
- Beta-1,3-N- acetylglucosaminyltransferase-5
- Lactotriaosylceramide synthase
- Lc(3Cer synthase
- Lc3 synthase
|
| Enzyme 19 Gene Name |
B3GNT5 |
| Enzyme 19 Protein Sequence |
>UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 5
MRMLVSGRRVKKWQLIIQLFATCFLASLMFFWEPIDNHIVSHMKSYSYRYLINSYDFVND
TLSLKHTSAGPRYQYLINHKEKCQAQDVLLLLFVKTAPENYDRRSGIRRTWGNENYVRSQ
LNANIKTLFALGTPNPLEGEELQRKLAWEDQRYNDIIQQDFVDSFYNLTLKLLMQFSWAN
TYCPHAKFLMTADDDIFIHMPNLIEYLQSLEQIGVQDFWIGRVHRGAPPIRDKSSKYYVS
YEMYQWPAYPDYTAGAAYVISGDVAAKVYEASQTLNSSLYIDDVFMGLCANKIGIVPQDH
VFFSGEGKTPYHPCIYEKMMTSHGHLEDLQDLWKNATDPKVKTISKGFFGQIYCRLMKII
LLCKISYVDTYPCRAAFI
|
| Enzyme 19 Number of Residues |
378 |
| Enzyme 19 Molecular Weight |
44053 |
| Enzyme 19 Theoretical pI |
Not Available |
| Enzyme 19 GO Classification |
| Function |
- catalytic activity
- galactosyltransferase activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- biopolymer metabolism
- biopolymer modification
- macromolecule metabolism
- metabolism
- physiological process
- protein amino acid glycosylation
- protein modification
|
| Component |
|
|
| Enzyme 19 General Function |
Not Available |
| Enzyme 19 Specific Function |
Beta-1,3-N-acetylglucosaminyltransferase that plays a key role in the synthesis of lacto- or neolacto-series carbohydrate chains on glycolipids, notably by participating in biosynthesis of HNK-1 and Lewis X carbohydrate structures. Has strong activity toward lactosylceramide (LacCer) and neolactotetraosylceramide (nLc(4)Cer; paragloboside), resulting in the synthesis of Lc(3)Cer and neolactopentaosylceramide (nLc(5)Cer), respectively. Probably plays a central role in regulating neolacto-series glycolipid synthesis during embryonic development |
| Enzyme 19 Pathways |
Not Available |
| Enzyme 19 Reactions |
- galactosyl glucosyl ceramide + UDP-N-acetyl-D-glucosamine --> (Gal)1 (Glc)1 (GlcNAc)1 (Cer)1 + H+ + UDP
|
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
13568434  |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
Q9BYG0  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
B3GN5_HUMAN  |
| Enzyme 19 PDB ID |
Not Available |
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
Not Available |
| Enzyme 19 GenBank Gene ID |
AB045278  |
| Enzyme 19 GeneCard ID |
Not Available |
| Enzyme 19 GenAtlas ID |
B3GNT5  |
| Enzyme 19 HGNC ID |
HGNC:15684  |
| Enzyme 19 Chromosome Location |
Not Available |
| Enzyme 19 Locus |
Not Available |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
- Togayachi A, Akashima T, Ookubo R, Kudo T, Nishihara S, Iwasaki H, Natsume A, Mio H, Inokuchi J, Irimura T, Sasaki K, Narimatsu H: Molecular cloning and characterization of UDP-GlcNAc:lactosylceramide beta 1,3-N-acetylglucosaminyltransferase (beta 3Gn-T5), an essential enzyme for the expression of HNK-1 and Lewis X epitopes on glycolipids. J Biol Chem. 2001 Jun 22;276(25):22032-40. Epub 2001 Mar 30. [PubMed
]
- Henion TR, Zhou D, Wolfer DP, Jungalwala FB, Hennet T: Cloning of a mouse beta 1,3 N-acetylglucosaminyltransferase GlcNAc(beta 1,3)Gal(beta 1,4)Glc-ceramide synthase gene encoding the key regulator of lacto-series glycolipid biosynthesis. J Biol Chem. 2001 Aug 10;276(32):30261-9. Epub 2001 May 30. [PubMed
]
|
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
15260 |
| Enzyme 20 Name |
N-acetylglucosamine-1-phosphotransferase subunits alpha/beta |
| Enzyme 20 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 20 Gene Name |
GNPTAB |
| Enzyme 20 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 20 Number of Residues |
1256 |
| Enzyme 20 Molecular Weight |
143623 |
| Enzyme 20 Theoretical pI |
7.17 |
| Enzyme 20 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 20 General Function |
Not Available |
| Enzyme 20 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 20 Pathways |
Not Available |
| Enzyme 20 Reactions |
Not Available |
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
74474848  |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
Q3T906  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
GNPTA_HUMAN  |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 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 20 GenBank Gene ID |
AM085438  |
| Enzyme 20 GeneCard ID |
Q3T906  |
| Enzyme 20 GenAtlas ID |
GNPTAB  |
| Enzyme 20 HGNC ID |
HGNC:29670  |
| Enzyme 20 Chromosome Location |
12 |
| Enzyme 20 Locus |
12q23.2 |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 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 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
15261 |
| Enzyme 21 Name |
cDNA FLJ75238, highly similar to Homo sapiens asparagine-linked glycosylation 14 homolog (yeast) (ALG14), mRNA (Asparagine-linked glycosylation 14 homolog (Yeast), isoform CRA_b) |
| Enzyme 21 Synonyms |
Not Available |
| Enzyme 21 Gene Name |
ALG14 |
| Enzyme 21 Protein Sequence |
>cDNA FLJ75238, highly similar to Homo sapiens asparagine-linked glycosylation 14 homolog (yeast) (ALG14), mRNA (Asparagine-linked glycosylation 14 homolog (Yeast), isoform CRA_b)
MVCVLVLAAAAGAVAVFLILRIWVVLRSMDVTPRESLSILVVAGSGGHTTEILRLLGSLS
NAYSPRHYVIADTDEMSANKINSFELDRADRDPSNMYTKYYIHRIPRSREVQQSWPSTVF
TTLHSMWLSFPLIHRVKPDLVLCNGPGTCVPICVSALLLGILGIKKVIIVYVESICRVET
LSMSGKILFHLSDYFIVQWPALKEKYPKSVYLGRIV
|
| Enzyme 21 Number of Residues |
216 |
| Enzyme 21 Molecular Weight |
24151 |
| Enzyme 21 Theoretical pI |
9.16 |
| Enzyme 21 GO Classification |
Not Available |
| Enzyme 21 General Function |
Not Available |
| Enzyme 21 Specific Function |
Not Available |
| Enzyme 21 Pathways |
Not Available |
| Enzyme 21 Reactions |
Not Available |
| Enzyme 21 Pfam Domain Function |
Not Available |
| Enzyme 21 Signals |
|
| Enzyme 21 Transmembrane Regions |
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
158259813  |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
A8K030  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
A8K030_HUMAN  |
| Enzyme 21 PDB ID |
Not Available |
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
>651 bp
ATGGTGTGCGTTCTCGTTCTAGCTGCGGCCGCAGGAGCTGTGGCGGTTTTCCTAATCCTG
CGAATATGGGTAGTGCTTCGTTCCATGGACGTTACGCCCCGGGAGTCTCTCAGTATCTTG
GTAGTGGCTGGGTCCGGTGGGCATACCACTGAGATCCTGAGGCTGCTTGGGAGCTTGTCC
AATGCCTACTCACCTAGACATTATGTCATTGCTGACACTGATGAAATGAGTGCCAATAAA
ATAAATTCTTTTGAACTAGATCGAGCTGATAGAGACCCTAGTAACATGTATACCAAATAC
TACATTCACCGAATTCCAAGAAGCCGGGAGGTTCAGCAGTCCTGGCCCTCCACCGTTTTC
ACCACCTTGCACTCCATGTGGCTCTCCTTTCCCCTAATTCACAGGGTGAAGCCAGATTTG
GTGTTGTGTAACGGACCAGGAACATGTGTTCCTATCTGTGTATCTGCCCTTCTCCTTGGG
ATACTAGGAATAAAGAAAGTGATCATTGTCTACGTTGAAAGCATCTGCCGTGTAGAAACG
TTATCCATGTCCGGAAAGATTCTGTTTCATCTCTCAGATTACTTCATTGTTCAGTGGCCG
GCTCTGAAAGAAAAGTATCCCAAATCGGTGTACCTTGGGCGAATTGTTTGA
|
| Enzyme 21 GenBank Gene ID |
AK289395  |
| Enzyme 21 GeneCard ID |
A8K030  |
| Enzyme 21 GenAtlas ID |
Not Available |
| Enzyme 21 HGNC ID |
Not Available |
| Enzyme 21 Chromosome Location |
Not Available |
| Enzyme 21 Locus |
Not Available |
| Enzyme 21 SNPs |
SNPJam Report  |
| Enzyme 21 General References |
Not Available |
| Enzyme 21 Metabolite References |
Not Available |
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
15262 |
| Enzyme 22 Name |
cDNA FLJ78031, highly similar to Homo sapiens beta3GnT6 beta-1,3-N- acetylglucosaminyltransferase 6 (HCG2018639) |
| Enzyme 22 Synonyms |
Not Available |
| Enzyme 22 Gene Name |
Not Available |
| Enzyme 22 Protein Sequence |
>cDNA FLJ78031, highly similar to Homo sapiens beta3GnT6 beta-1,3-N- acetylglucosaminyltransferase 6 (HCG2018639)
MAFPCRRSLTAKTLACLLVGVSFLALQQWFLQAPRSPREERSPQEETPEGPTDAPAADEP
PSELVPGPPCVANASANATADFEQLPARIQDFLRYRHCRHFPLLWDAPAKCAGGRGVFLL
LAVKSAPEHYERRELIRRTWGQERSYGGRPVRRLFLLGTPGPEDEARAERLAELVALEAR
EHGDVLQWAFADTFLNLTLKHLHLLDWLAARCPHARFLLSGDDDVFVHTANVVRFLQAQP
PGRHLFSGQLMEGSVPIRDSWSKYFVPPQLFPGSAYPVYCSGGGFLLSGPTARALRAAAR
HTPLFPIDDAYMGMCLERAGLAPSGHEGIRPFGVQLPGAQQSSFDPCMYRELLLVHRFAP
YEMLLMWKALHSPALSCDRGHRVS
|
| Enzyme 22 Number of Residues |
384 |
| Enzyme 22 Molecular Weight |
42748 |
| Enzyme 22 Theoretical pI |
7.76 |
| Enzyme 22 GO Classification |
Not Available |
| Enzyme 22 General Function |
Not Available |
| Enzyme 22 Specific Function |
Not Available |
| Enzyme 22 Pathways |
Not Available |
| Enzyme 22 Reactions |
Not Available |
| Enzyme 22 Pfam Domain Function |
Not Available |
| Enzyme 22 Signals |
|
| Enzyme 22 Transmembrane Regions |
|
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
158259007  |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
A8K9Q8  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
A8K9Q8_HUMAN  |
| Enzyme 22 PDB ID |
Not Available |
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 Gene Sequence |
>1155 bp
ATGGCTTTTCCCTGCCGCAGGTCCCTGACTGCCAAGACTCTGGCCTGCCTCCTGGTGGGC
GTGAGTTTCTTAGCACTGCAGCAGTGGTTCCTCCAGGCGCCAAGGTCCCCGCGGGAGGAG
AGGTCCCCGCAGGAGGAGACGCCAGAGGGTCCCACCGACGCTCCCGCGGCTGACGAGCCG
CCCTCGGAGCTCGTCCCCGGGCCCCCGTGCGTGGCGAACGCCTCGGCGAACGCCACGGCC
GACTTCGAGCAGCTGCCCGCGCGCATCCAGGACTTCCTGCGGTACCGCCACTGCCGCCAC
TTCCCGCTGCTTTGGGACGCACCGGCCAAGTGCGCCGGCGGCCGAGGCGTGTTCCTGCTC
CTGGCGGTGAAGTCGGCGCCTGAGCACTACGAGCGACGCGAGCTCATCCGGCGCACGTGG
GGGCAAGAGCGCAGCTACGGCGGGCGGCCAGTGCGCCGCCTCTTTCTATTGGGCACCCCG
GGCCCCGAGGACGAGGCGCGCGCGGAGCGGCTGGCGGAGCTGGTGGCGCTGGAGGCGCGC
GAGCACGGCGACGTGCTGCAGTGGGCCTTCGCGGACACCTTCCTCAACCTCACGCTCAAG
CACCTGCACTTGCTCGACTGGCTGGCTGCACGCTGCCCGCACGCGCGCTTTCTGCTCAGC
GGCGACGACGACGTGTTCGTGCACACCGCCAACGTAGTCCGCTTCCTGCAGGCGCAGCCA
CCCGGCCGCCACCTGTTCTCCGGCCAGCTCATGGAGGGCTCCGTGCCCATCCGCGACAGC
TGGAGCAAGTACTTCGTGCCGCCGCAGCTCTTCCCCGGGTCCGCTTACCCGGTGTACTGC
AGCGGCGGCGGCTTCCTCCTGTCCGGCCCCACGGCCCGGGCCCTGCGCGCGGCCGCCCGC
CACACCCCGCTCTTCCCCATCGACGACGCCTACATGGGCATGTGTCTGGAGCGCGCCGGC
CTGGCGCCCAGCGGCCACGAGGGCATCCGGCCCTTCGGCGTGCAGCTGCCTGGCGCACAG
CAGTCCTCCTTCGACCCCTGCATGTACCGCGAGTTGCTGCTAGTGCACCGCTTCGCGCCC
TACGAGATGCTGCTCATGTGGAAGGCGCTGCACAGCCCCGCGCTCAGCTGTGACCGGGGA
CACCGGGTCTCCTGA
|
| Enzyme 22 GenBank Gene ID |
AK292773  |
| Enzyme 22 GeneCard ID |
A8K9Q8  |
| Enzyme 22 GenAtlas ID |
Not Available |
| Enzyme 22 HGNC ID |
Not Available |
| Enzyme 22 Chromosome Location |
Not Available |
| Enzyme 22 Locus |
Not Available |
| Enzyme 22 SNPs |
Not Available |
| Enzyme 22 General References |
Not Available |
| Enzyme 22 Metabolite References |
Not Available |
|
Enzyme 23
[top]
|
| Enzyme 23 ID |
15263 |
| Enzyme 23 Name |
UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (EC 5.1.3.14) (Glucosamine (UDP-N-acetyl)-2-epimerase/N- acetylmannosamine kinase, isoform CRA_a) |
| Enzyme 23 Synonyms |
Not Available |
| Enzyme 23 Gene Name |
GNE |
| Enzyme 23 Protein Sequence |
>UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (EC 5.1.3.14) (Glucosamine (UDP-N-acetyl)-2-epimerase/N- acetylmannosamine kinase, isoform CRA_a)
METYGYLQRESCFQGPHELYFKNLSKRNKQIMEKNGNNRKLRVCVATCNRADYSKLAPIM
FGIKTEPEFFELDVVVLGSHLIDDYGNTYRMIEQDDFDINTRLHTIVRGEDEAAMVESVG
LALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVSGTIDDSIRHA
ITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWLGDDV
KSKDYIVALQHPVTTDIKHSIKMFELTLDALISFNKRTLVLFPNIDAGSKEMVRVMRKKG
IEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVREVGAFGTPVINLGTRQIGRETGE
NVLHVRDADTQDKILQALHLQFGKQYPCSKIYGDGNAVPRILKFLKSIDLQEPLQKKFCF
PPVKENISQDIDHILETLSALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERINLI
LQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVLHSTKLIQEWNSVDLRTPLSDTLH
LPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGH
LVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQ
AAKLGNAKAQSILRTAGTALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIRQQALS
SVQDVDVVVSDLVDPALLGAASMVLDYTTRRIY
|
| Enzyme 23 Number of Residues |
753 |
| Enzyme 23 Molecular Weight |
83067 |
| Enzyme 23 Theoretical pI |
6.93 |
| Enzyme 23 GO Classification |
| Function |
- ATP binding
- UDP-N-acetylglucosamine 2-epimerase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- hexokinase activity
- isomerase activity
- nucleotide binding
- phosphotransferase activity, alcohol group as acceptor
- purine nucleotide binding
- racemase and epimerase activity
- racemase and epimerase activity, acting on carbohydrates and derivatives
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- N-acetylglucosamine metabolism
- UDP-N-acetylglucosamine metabolism
- alcohol metabolism
- amine metabolism
- amino sugar metabolism
- carbohydrate biosynthesis
- cellular metabolism
- glucosamine metabolism
- glucose catabolism
- glucose metabolism
- glycolysis
- hexose metabolism
- lipopolysaccharide biosynthesis
- macromolecule biosynthesis
- macromolecule metabolism
- metabolism
- monosaccharide metabolism
- nitrogen compound metabolism
- physiological process
- polysaccharide biosynthesis
|
| Component |
| — |
|
| Enzyme 23 General Function |
Cell wall/membrane/envelope biogenesis |
| Enzyme 23 Specific Function |
Not Available |
| Enzyme 23 Pathways |
Not Available |
| Enzyme 23 Reactions |
- UDP-N-acetyl-D-glucosamine = UDP-N-acetyl-D-mannosamine [RN:R00420] ALL_REAC R00420
- (other) R00414
|
| Enzyme 23 Pfam Domain Function |
|
| Enzyme 23 Signals |
|
| Enzyme 23 Transmembrane Regions |
|
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
150368575  |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
A6PZH2  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
A6PZH2_HUMAN  |
| Enzyme 23 PDB ID |
Not Available |
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 Gene Sequence |
>2262 bp
ATGGAAACCTATGGTTATCTGCAGAGGGAGTCATGCTTTCAAGGACCTCATGAACTCTAT
TTTAAGAACCTCTCAAAACGAAACAAGCAAATCATGGAGAAGAATGGAAATAACCGAAAG
CTGCGGGTTTGTGTTGCTACTTGTAACCGTGCAGATTATTCTAAACTTGCCCCGATCATG
TTTGGCATTAAAACCGAACCTGAGTTCTTTGAACTTGATGTTGTGGTACTTGGCTCTCAC
CTGATAGATGACTATGGAAATACATATCGAATGATTGAACAAGATGACTTTGACATTAAC
ACCAGGCTACACACAATTGTGAGGGGAGAAGATGAGGCAGCCATGGTGGAGTCAGTAGGC
CTGGCCCTAGTGAAGCTGCCAGATGTCCTTAATCGCCTGAAGCCTGATATCATGATTGTT
CATGGAGACAGGTTTGATGCCCTGGCTCTGGCCACATCTGCTGCCTTGATGAACATCCGA
ATCCTTCACATTGAAGGTGGGGAAGTCAGTGGGACCATTGATGACTCTATCAGACATGCC
ATAACAAAACTGGCTCATTATCATGTGTGCTGCACCCGCAGTGCAGAGCAGCACCTGATA
TCCATGTGTGAGGACCATGATCGCATCCTTTTGGCAGGCTGCCCTTCCTATGACAAACTT
CTCTCAGCCAAGAACAAAGACTACATGAGCATCATTCGCATGTGGCTAGGTGATGATGTA
AAATCTAAAGATTACATTGTTGCACTACAGCACCCTGTGACCACTGACATTAAGCATTCC
ATAAAAATGTTTGAATTAACATTGGATGCACTTATCTCATTTAACAAGCGGACCCTAGTC
CTGTTTCCAAATATTGACGCAGGGAGCAAAGAGATGGTTCGAGTGATGCGGAAGAAGGGC
ATTGAGCATCATCCCAACTTTCGTGCAGTTAAACACGTCCCATTTGACCAGTTTATACAG
TTGGTTGCCCATGCTGGCTGTATGATTGGGAACAGCAGCTGTGGGGTTCGAGAAGTTGGA
GCTTTTGGAACACCTGTGATCAACCTGGGAACACGTCAGATTGGAAGAGAAACAGGGGAG
AATGTTCTTCATGTCCGGGATGCTGACACCCAAGACAAAATATTGCAAGCACTGCACCTT
CAGTTTGGTAAACAGTACCCTTGTTCAAAGATATATGGGGATGGAAATGCTGTTCCAAGG
ATTTTGAAGTTTCTCAAATCTATCGATCTTCAAGAGCCACTGCAAAAGAAATTCTGCTTT
CCTCCTGTGAAGGAGAATATCTCTCAAGATATTGACCATATTCTTGAAACTCTAAGTGCC
TTGGCCGTTGATCTTGGCGGGACGAACCTCCGAGTTGCAATAGTCAGCATGAAGGGTGAA
ATAGTTAAGAAGTATACTCAGTTCAATCCTAAAACCTATGAAGAGAGGATTAATTTAATC
CTACAGATGTGTGTGGAAGCTGCAGCAGAAGCTGTAAAACTGAACTGCAGAATTTTGGGA
GTAGGCATTTCCACAGGTGGCCGTGTAAATCCTCGGGAAGGAATTGTGCTGCATTCAACC
AAACTGATCCAAGAGTGGAACTCTGTGGACCTTAGGACCCCCCTTTCTGACACTTTGCAT
CTCCCTGTGTGGGTAGACAATGATGGCAACTGTGCTGCCCTGGCGGAAAGGAAATTTGGC
CAAGGAAAGGGACTGGAAAACTTTGTTACACTTATCACAGGCACAGGAATCGGTGGTGGA
ATTATCCATCAGCATGAATTGATCCACGGAAGCTCCTTCTGTGCTGCAGAACTGGGCCAC
CTTGTTGTGTCTCTGGATGGGCCTGATTGTTCCTGTGGAAGCCATGGGTGCATTGAAGCA
TACGCCTCTGGAATGGCCTTGCAGAGGGAGGCAAAAAAGCTCCATGATGAGGACCTGCTC
TTGGTGGAAGGGATGTCAGTGCCAAAAGATGAGGCTGTGGGTGCGCTCCATCTCATCCAA
GCTGCGAAACTTGGCAATGCGAAGGCCCAGAGCATCCTAAGAACAGCTGGAACAGCTTTG
GGTCTTGGGGTTGTGAACATCCTCCATACCATGAATCCCTCCCTTGTGATCCTCTCCGGA
GTCCTGGCCAGTCACTATATCCACATTGTCAAAGACGTCATTCGCCAGCAGGCCTTGTCC
TCCGTGCAGGACGTGGATGTGGTGGTTTCGGATTTGGTTGACCCCGCCCTGCTGGGTGCT
GCCAGCATGGTTCTGGACTACACAACACGCAGGATCTACTAG
|
| Enzyme 23 GenBank Gene ID |
AM697708  |
| Enzyme 23 GeneCard ID |
A6PZH2  |
| Enzyme 23 GenAtlas ID |
Not Available |
| Enzyme 23 HGNC ID |
Not Available |
| Enzyme 23 Chromosome Location |
Not Available |
| Enzyme 23 Locus |
Not Available |
| Enzyme 23 SNPs |
SNPJam Report  |
| Enzyme 23 General References |
Not Available |
| Enzyme 23 Metabolite References |
Not Available |
|
Enzyme 24
[top]
|
| Enzyme 24 ID |
16538 |
| Enzyme 24 Name |
cDNA, FLJ93080, highly similar to Homo sapiens UDP-N-acteylglucosamine pyrophosphorylase 1 (UAP1), mRNA (UDP-N-acteylglucosamine pyrophosphorylase 1, isoform CRA_a) |
| Enzyme 24 Synonyms |
Not Available |
| Enzyme 24 Gene Name |
UAP1 |
| Enzyme 24 Protein Sequence |
>cDNA, FLJ93080, highly similar to Homo sapiens UDP-N-acteylglucosamine pyrophosphorylase 1 (UAP1), mRNA (UDP-N-acteylglucosamine pyrophosphorylase 1, isoform CRA_a)
MNINDLKLTLSKAGQEHLLRFWNELEEAQQVELYAELQAMNFEELNFFFQKAIEGFNQSS
HQKNVDARMEPVPREVLGSATRDQDQLQAWESEGLFQISQNKVAVLLLAGGQGTRLGVAY
PKGMYDVGLPSRKTLFQIQAERILKLQQVAEKYYGNKCIIPWYIMTSGRTMESTKEFFTK
HKYFGLKKENVIFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDME
QRGIWSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQ
VVEYSEISLATAQKRSSDGRLLFNAGNIANHFFTVPFLRDVVNVYEPQLQHHVAQKKIPY
VDTQGQLIKPDKPNGIKMEKFVFDIFQFAKKFVVYEVLREDEFSPLKNADSQNGKDNPTT
ARHALMSLHHCWVLNAGGHFIDENGSRLPAIPRLKDANDVPIQCEISPLISYAGEGLESY
VADKEFHAPLIIDENGVHELVKNGI
|
| Enzyme 24 Number of Residues |
505 |
| Enzyme 24 Molecular Weight |
57029 |
| Enzyme 24 Theoretical pI |
6.33 |
| Enzyme 24 GO Classification |
| Function |
- catalytic activity
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 24 General Function |
Not Available |
| Enzyme 24 Specific Function |
Not Available |
| Enzyme 24 Pathways |
Not Available |
| Enzyme 24 Reactions |
Not Available |
| Enzyme 24 Pfam Domain Function |
|
| Enzyme 24 Signals |
|
| Enzyme 24 Transmembrane Regions |
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
Not Available |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
B2R6R8  |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
B2R6R8_HUMAN  |
| Enzyme 24 PDB ID |
1JV3  |
| Enzyme 24 PDB File |
Show |
| Enzyme 24 3D Structure |
|
| Enzyme 24 Cellular Location |
Not Available |
| Enzyme 24 Gene Sequence |
Not Available |
| Enzyme 24 GenBank Gene ID |
AK312685  |
| Enzyme 24 GeneCard ID |
B2R6R8  |
| Enzyme 24 GenAtlas ID |
Not Available |
| Enzyme 24 HGNC ID |
Not Available |
| Enzyme 24 Chromosome Location |
Not Available |
| Enzyme 24 Locus |
Not Available |
| Enzyme 24 SNPs |
SNPJam Report  |
| Enzyme 24 General References |
Not Available |
| Enzyme 24 Metabolite References |
Not Available |
|
Enzyme 25
[top]
|
| Enzyme 25 ID |
16544 |
| Enzyme 25 Name |
Glycosyltransferase 28 domain containing 1, isoform CRA_b |
| Enzyme 25 Synonyms |
- SubName: cDNA, FLJ92520, Homo sapiens uncharacterized hematopoietic stem/progenitor cellsprotein MDS031 (MDS031), mRNA
|
| Enzyme 25 Gene Name |
GLT28D1 |
| Enzyme 25 Protein Sequence |
>Glycosyltransferase 28 domain containing 1, isoform CRA_b
MKCVFVTVGTTSFDDLIACVSAPDSLQKIESLGYNRLILQIGRGTVVPEPFSTESFTLDV
YRYKDSLKEDIQKADLVISHAGAGSCLETLEKGKPLVVVINEKLMNNHQLELAKQLHKEG
HLFYCTCSTLPGLLQSMDLSTLKCYPPGQPEKFSAFLDKVVGLQK
|
| Enzyme 25 Number of Residues |
165 |
| Enzyme 25 Molecular Weight |
18225 |
| Enzyme 25 Theoretical pI |
6.50 |
| Enzyme 25 GO Classification |
| Function |
- binding
- carbohydrate binding
- catalytic activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- biopolymer metabolism
- biopolymer modification
- carbohydrate metabolism
- lipid glycosylation
- lipid modification
- macromolecule metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 25 General Function |
Not Available |
| Enzyme 25 Specific Function |
Not Available |
| Enzyme 25 Pathways |
Not Available |
| Enzyme 25 Reactions |
Not Available |
| Enzyme 25 Pfam Domain Function |
|
| Enzyme 25 Signals |
|
| Enzyme 25 Transmembrane Regions |
|
| Enzyme 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
Not Available |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
B2R5L5  |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
B2R5L5_HUMAN  |
| Enzyme 25 PDB ID |
Not Available |
| Enzyme 25 Cellular Location |
Not Available |
| Enzyme 25 Gene Sequence |
Not Available |
| Enzyme 25 GenBank Gene ID |
AK312229  |
| Enzyme 25 GeneCard ID |
B2R5L5  |
| Enzyme 25 GenAtlas ID |
Not Available |
| Enzyme 25 HGNC ID |
Not Available |
| Enzyme 25 Chromosome Location |
Not Available |
| Enzyme 25 Locus |
Not Available |
| Enzyme 25 SNPs |
SNPJam Report  |
| Enzyme 25 General References |
Not Available |
| Enzyme 25 Metabolite References |
Not Available |
|
Enzyme 26
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|
| Enzyme 26 ID |
16545 |
| Enzyme 26 Name |
cDNA FLJ31605 fis, clone NT2RI2002729, highly similar to Alpha-1,6-mannosyl-glycoprotein2-beta-N- acetylglucosaminyltransferase (Mannosyl (Alpha-1,6-)-glycoprotein beta-1,2-N-acetylglucosaminyltransferase) |
| Enzyme 26 Synonyms |
Not Available |
| Enzyme 26 Gene Name |
MGAT2 |
| Enzyme 26 Protein Sequence |
>cDNA FLJ31605 fis, clone NT2RI2002729, highly similar to Alpha-1,6-mannosyl-glycoprotein2-beta-N- acetylglucosaminyltransferase (Mannosyl (Alpha-1,6-)-glycoprotein beta-1,2-N-acetylglucosaminyltransferase)
MRFRIYKRKVLILTLVVAACGFVLWSSNGRQRKNEALAPPLLDAEPARGAGGRGGDHPSV
AVGIRRVSNVSAASLVPAVPQPEADNLTLRYRSLVYQLNFDQTLRNVDKAGTWAPRELVL
VVQVHNRPEYLRLLLDSLRKAQGIDNVLVIFSHDFWSTEINQLIAGVNFCPVLQVFFPFS
IQLYPNEFPGSDPRDCPRDLPKNAALKLGCINAEYPDSFGHYREAKFSQTKHHWWWKLHF
VWERVKILRDYAGLILFLEEDHYLAPDFYHVFKKMWKLKQQECPECDVLSLGTYSASRSF
YGMADKVDVKTWKSTEHNMGLALTRNAYQKLIECTDTFCTYDDYNWDWTLQYLTVSCLPK
FWKVLVPQIPRIFHAGDCGMHHKKTCRPSTQSAQIESLLNNNKQYMFPETLTISEKFTVV
AISPPRKNGGWGDIRDHELCKSYRRLQ
|
| Enzyme 26 Number of Residues |
447 |
| Enzyme 26 Molecular Weight |
51551 |
| Enzyme 26 Theoretical pI |
8.94 |
| Enzyme 26 GO Classification |
| Function |
- UDP-glycosyltransferase activity
- acetylglucosaminyltransferase activity
- alpha-1,6-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring glycosyl groups
|
| Process |
- carbohydrate metabolism
- macromolecule metabolism
- metabolism
- oligosaccharide biosynthesis
- oligosaccharide metabolism
- physiological process
|
| Component |
- Golgi apparatus
- Golgi stack
- cell
- integral to membrane
- intracellular membrane-bound organelle
- intrinsic to membrane
- membrane
- membrane-bound organelle
- organelle
|
|
| Enzyme 26 General Function |
Not Available |
| Enzyme 26 Specific Function |
Not Available |
| Enzyme 26 Pathways |
Not Available |
| Enzyme 26 Reactions |
Not Available |
| Enzyme 26 Pfam Domain Function |
|
| Enzyme 26 Signals |
|
| Enzyme 26 Transmembrane Regions |
|
| Enzyme 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
Not Available |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
B3KPC5  |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
B3KPC5_HUMAN  |
| Enzyme 26 PDB ID |
Not Available |
| Enzyme 26 Cellular Location |
Not Available |
| Enzyme 26 Gene Sequence |
Not Available |
| Enzyme 26 GenBank Gene ID |
AK056167  |
| Enzyme 26 GeneCard ID |
B3KPC5  |
| Enzyme 26 GenAtlas ID |
Not Available |
| Enzyme 26 HGNC ID |
Not Available |
| Enzyme 26 Chromosome Location |
14 |
| Enzyme 26 Locus |
14q21 |
| Enzyme 26 SNPs |
SNPJam Report  |
| Enzyme 26 General References |
Not Available |
| Enzyme 26 Metabolite References |
Not Available |
|
Enzyme 27
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|
| Enzyme 27 ID |
16546 |
| Enzyme 27 Name |
cDNA, FLJ93340, Homo sapiens exostoses (multiple)-like 2 (EXTL2), mRNA (Exostoses (Multiple)-like 2, isoform CRA_a) |
| Enzyme 27 Synonyms |
Not Available |
| Enzyme 27 Gene Name |
EXTL2 |
| Enzyme 27 Protein Sequence |
>cDNA, FLJ93340, Homo sapiens exostoses (multiple)-like 2 (EXTL2), mRNA (Exostoses (Multiple)-like 2, isoform CRA_a)
MRCCHICKLPGRVMGIRVLRLSLVVILVLLLVAGALTALLPSVKEDKMLMLRREIKSQGK
STMDSFTLIMQTYNRTDLLLKLLNHYQAVPNLHKVIVVWNNIGEKAPDELWNSLGPHPIP
VIFKQQTANRMRNRLQVFPELETNAVLMVDDDTLISTPDLVFAFSVWQQFPDQIVGFVPR
KHVSTSSGIYSYGSFEMQAPGSGNGDQYSMVLIGASFFNSKYLELFQRQPAAVHALIDDT
QNCDDIAMNFIIAKHIGKTSGIFVKPVNMDNLEKETNSGYSGMWHRAEHALQRSYCINKL
VNIYDSMPLRYSNIMISQFGFPYANYKRKI
|
| Enzyme 27 Number of Residues |
330 |
| Enzyme 27 Molecular Weight |
37466 |
| Enzyme 27 Theoretical pI |
9.24 |
| Enzyme 27 GO Classification |
Not Available |
| Enzyme 27 General Function |
Not Available |
| Enzyme 27 Specific Function |
Not Available |
| Enzyme 27 Pathways |
Not Available |
| Enzyme 27 Reactions |
Not Available |
| Enzyme 27 Pfam Domain Function |
|
| Enzyme 27 Signals |
|
| Enzyme 27 Transmembrane Regions |
|
| Enzyme 27 Essentiality |
Not Available |
| Enzyme 27 GenBank ID Protein |
Not Available |
| Enzyme 27 UniProtKB/Swiss-Prot ID |
B2R795  |
| Enzyme 27 UniProtKB/Swiss-Prot Entry Name |
B2R795_HUMAN  |
| Enzyme 27 PDB ID |
Not Available |
| Enzyme 27 Cellular Location |
Not Available |
| Enzyme 27 Gene Sequence |
Not Available |
| Enzyme 27 GenBank Gene ID |
AK312895  |
| Enzyme 27 GeneCard ID |
B2R795  |
| Enzyme 27 GenAtlas ID |
Not Available |
| Enzyme 27 HGNC ID |
Not Available |
| Enzyme 27 Chromosome Location |
Not Available |
| Enzyme 27 Locus |
Not Available |
| Enzyme 27 SNPs |
SNPJam Report  |
| Enzyme 27 General References |
Not Available |
| Enzyme 27 Metabolite References |
Not Available |
|
Enzyme 28
[top]
|
| Enzyme 28 ID |
16547 |
| Enzyme 28 Name |
cDNA, FLJ93616, highly similar to Homo sapiens exostoses (multiple) 1 (EXT1), mRNA (Exostoses (Multiple) 1) |
| Enzyme 28 Synonyms |
Not Available |
| Enzyme 28 Gene Name |
EXT1 |
| Enzyme 28 Protein Sequence |
>cDNA, FLJ93616, highly similar to Homo sapiens exostoses (multiple) 1 (EXT1), mRNA (Exostoses (Multiple) 1)
MQAKKRYFILLSAGSCLALLFYFGGLQFRASRSHSRREEHSGRNGLHHPSPDHFWPRFPD
ALRPFVPWDQLENEDSSVHISPRQKRDANSSIYKGKKCRMESCFDFTLCKKNGFKVYVYP
QQKGEKIAESYQNILAAIEGSRFYTSDPSQACLFVLSLDTLDRDQLSPQYVHNLRSKVQS
LHLWNNGRNHLIFNLYSGTWPDYTEDVGFDIGQAMLAKASISTENFRPNFDVSIPLFSKD
HPRTGGERGFLKFNTIPPLRKYMLVFKGKRYLTGIGSDTRNALYHVHNGEDVVLLTTCKH
GKDWQKHKDSRCDRDNTEYEKYDYREMLHNATFCLVPRGRRLGSFRFLEALQAACVPVML
SNGWELPFSEVINWNQAAVIGDERLLLQIPSTIRSIHQDKILALRQQTQFLWEAYFSSVE
KIVLTTLEIIQDRIFKHISRNSLIWNKHPGGLFVLPQYSSYLGDFPYYYANLGLKPPSKF
TAVIHAVTPLVSQSQPVLKLLVAAAKSQYCAQIIVLWNCDKPLPAKHRWPATAVPVVVIE
GESKVMSSRFLPYDNIITDAVLSLDEDTVLSTTEVDFAFTVWQSFPERIVGYPARSHFWD
NSKERWGYTSKWTNDYSMVLTGAAIYHKYYHYLYSHYLPASLKNMVDQLANCEDILMNFL
VSAVTKLPPIKVTQKKQYKETMMGQTSRASRWADPDHFAQRQSCMNTFASWFGYMPLIHS
QMRLDPVLFKDQVSILRKKYRDIERL
|
| Enzyme 28 Number of Residues |
746 |
| Enzyme 28 Molecular Weight |
86256 |
| Enzyme 28 Theoretical pI |
9.34 |
| Enzyme 28 GO Classification |
| Function |
| — |
| Process |
| — |
| Component |
|
|
| Enzyme 28 General Function |
Not Available |
| Enzyme 28 Specific Function |
Not Available |
| Enzyme 28 Pathways |
Not Available |
| Enzyme 28 Reactions |
Not Available |
| Enzyme 28 Pfam Domain Function |
|
| Enzyme 28 Signals |
|
| Enzyme 28 Transmembrane Regions |
|
| Enzyme 28 Essentiality |
Not Available |
| Enzyme 28 GenBank ID Protein |
Not Available |
| Enzyme 28 UniProtKB/Swiss-Prot ID |
B2R7V2  |
| Enzyme 28 UniProtKB/Swiss-Prot Entry Name |
B2R7V2_HUMAN  |
| Enzyme 28 PDB ID |
Not Available |
| Enzyme 28 Cellular Location |
Not Available |
| Enzyme 28 Gene Sequence |
Not Available |
| Enzyme 28 GenBank Gene ID |
AK313129  |
| Enzyme 28 GeneCard ID |
B2R7V2  |
| Enzyme 28 GenAtlas ID |
Not Available |
| Enzyme 28 HGNC ID |
Not Available |
| Enzyme 28 Chromosome Location |
Not Available |
| Enzyme 28 Locus |
Not Available |
| Enzyme 28 SNPs |
SNPJam Report  |
| Enzyme 28 General References |
Not Available |
| Enzyme 28 Metabolite References |
Not Available |