1. 2-(acetylamino)-2-deoxyhexose
2. 2-Acetamido-2-deoxy-D-glucose
3. 2-Acetamido-2-deoxyglucose
4. 2-Acetamido-D-glucose
5. 2-Acetylamino-2-deoxy-D-glucose
6. Acetylglucosamine
7. Glcnac
8. N-acetylchitosamine
9. N-acetylglucosamine

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• Cytoplasm (Predicted from LogP)
• Extracellular
• lysosome

• Breast Milk
• Urine

1. Nakagawa F, Schulte BA, Spicer SS: Lectin cytochemical evaluation of somatosensory neurons and their peripheral and central processes in rat and man. Cell Tissue Res. 1986;245(3):579-89. [PubMed ]
2. Hatcher VB, Schwarzmann GO, Jeanloz RW, McArthur JW: Changes in the sialic acid concentration in the major cervical glycoprotein from the bonnet monkey (Macaca radiata) during a hormonally induced cycle. Fertil Steril. 1977 Jun;28(6):682-8. [PubMed ]
3. Percheron F: [Beta-D-mannosidase] Bull Acad Natl Med. 1995 May;179(5):881-91; discussion 892. [PubMed ]
4. Collard CD, Montalto MC, Reenstra WR, Buras JA, Stahl GL: Endothelial oxidative stress activates the lectin complement pathway: role of cytokeratin 1. Am J Pathol. 2001 Sep;159(3):1045-54. [PubMed ]
5. Mollicone R, Candelier JJ, Mennesson B, Couillin P, Venot AP, Oriol R: Five specificity patterns of (1----3)-alpha-L-fucosyltransferase activity defined by use of synthetic oligosaccharide acceptors. Differential expression of the enzymes during human embryonic development and in adult tissues. Carbohydr Res. 1992 Apr 10;228(1):265-76. [PubMed ]
6. Kottgen E, Hell B, Muller C, Kainer F, Tauber R: Developmental changes in the glycosylation and binding properties of human fibronectins. Characterization of the glycan structures and ligand binding of human fibronectins from adult plasma, cord blood and amniotic fluid. Biol Chem Hoppe Seyler. 1989 Dec;370(12):1285-94. [PubMed ]
7. Madrid JF, Castells MT, Martinez-Menarguez JA, Aviles M, Hernandez F, Ballesta J: Subcellular characterization of glycoproteins in the principal cells of human gallbladder. A lectin cytochemical study. Histochemistry. 1994 Mar;101(3):195-204. [PubMed ]
8. Weiner B, Fischer T, Waxman S: Hemostasis in the era of the chronic anticoagulated patient. J Invasive Cardiol. 2003 Nov;15(11):669-73; quiz 674. [PubMed ]
9. Yates AD, Watkins WM: Enzymes involved in the biosynthesis of glycoconjugates. A UDP-2-acetamido-2-deoxy-D-glucose: beta-D-galactopyranosyl-(1 leads to 4)-saccharide (1 leads to 3)-2-acetamido-2-deoxy-beta-D- glucopyranosyltransferase in human serum. Carbohydr Res. 1983 Aug 16;120:251-68. [PubMed ]
10. Wikipedia

1. Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
2. N-acylglucosamine 2-epimerase
3. Beta-1,4-galactosyltransferase 2
4. Beta-1,4-galactosyltransferase 1
5. Beta-hexosaminidase beta chain precursor
6. Beta-hexosaminidase alpha chain precursor
7. N-acetylglucosamine kinase
8. Acidic mammalian chitinase precursor
9. N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase precursor
10. Chitotriosidase-1 precursor
11. Beta-1,4-galactosyltransferase 3
12. Beta-1,4-galactosyltransferase 4
13. Alpha-N-acetylglucosaminidase precursor
14. Lysozyme C precursor
15. Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1
16. Lysozyme-like protein 1
17. cDNA, FLJ93218, Homo sapiens UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase,polypeptide 1 (B4GALT1), mRNA (UDP-Gal:betaGlcNAc beta 1,4-galactosyltransferase, polypeptide 1, isoform CRA_a)
18. cDNA FLJ38554 fis, clone HCHON2002496, highly similar to Beta-1,4-galactosyltransferase 2 (EC 2.4.1.-)
19. cDNA, FLJ95212, Homo sapiens UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase,polypeptide 4 (B4GALT4), mRNA (UDP-Gal:betaGlcNAc beta 1,4-galactosyltransferase, polypeptide 4, isoform CRA_a)
20. cDNA FLJ46063 fis, clone TBAES2007428, highly similar to N-acetylglucosamine-1-phosphodiesteralpha-N- acetylglucosaminidase (EC 3.1.4.45)
21. Lysozyme-like protein 2
22. Sperm acrosome-associated protein 5
23. Lysozyme-like protein 6

1. UDP-GlcNAc-2-epimerase/ManAc kinase[Includes: UDP-N- acetylglucosamine 2-epimerase
2. Uridine diphosphate-N- acetylglucosamine-2-epimerase
3. UDP-GlcNAc-2-epimerase
4. N- acetylmannosamine kinase
5. ManAc kinase]

MEKNGNNRKLRVCVATCNRADYSKLAPIMFGIKTEPEFFELDVVVLGSHLIDDYGNTYRM
IEQDDFDINTRLHTIVRGEDEAAMVESVGLALVKLPDVLNRLKPDIMIVHGDRFDALALA
TSAALMNIRILHIEGGEVSGTIDDSIRHAITKLAHYHVCCTRSAEQHLISMCEDHDRILL
AGCPSYDKLLSAKNKDYMSIIRMWLGDDVKSKDYIVALQHPVTTDIKHSIKMFELTLDAL
ISFNKRTLVLFPNIDAGSKEMVRVMRKKGIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGN
SSCGVREVGAFGTPVINLGTRQIGRETGENVLHVRDADTQDKILQALHLQFGKQYPCSKI
YGDGNAVPRILKFLKSIDLQEPLQKKFCFPPVKENISQDIDHILETLSALAVDLGGTNLR
VAIVSMKGEIVKKYTQFNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNP
REGIVLHSTKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTL
ITGTGIGGGIIHQHELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREA
KKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNAKAQSILRTAGTALGLGVVNILHTM
NPSLVILSGVLASHYIHIVKDVIRQQALSSVQDVDVVVSDLVDPALLGAASMVLDYTTRR
IY

• Aminosugars metabolism (map00530 )

• UDP-N-acetyl-D-glucosamine = UDP-N-acetyl-D-mannosamine

• Epimerase_2 (PF02350 )
• ROK (PF00480 )

• None

• None

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

1. 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 ]

1. GlcNAc 2-epimerase
2. N- acetyl-D-glucosamine 2-epimerase
3. AGE
4. Renin-binding protein
5. RnBP

MEKERETLQAWKERVGQELDRVVAFWMEHSHDQEHGGFFTCLGREGRVYDDLKYVWLQGR
QVWMYCRLYRTFERFRHAQLLDAAKAGGEFLLRYARVAPPGKKCAFVLTRDGRPVKVQRT
IFSECFYTMAMNELWRATGEVRYQTEAVEMMDQIVHWVQEDASGLGRPQLQGAPAAEPMA
VPMMLLNLVEQLGEADEELAGKYAELGDWCARRILQHVQRDGQAVLENVSEGGKELPGCL
GRQQNPGHTLEAGWFLLRHCIRKGDPELRAHVIDKFLLLPFHSGWDPDHGGLFYFQDADN
FCPTQLEWAMKLWWPHSEAMIAFLMGYSDSGDPVLLRLFYQVAEYTFRQFRDPEYGEWFG
YLSREGKVALSIKGGPFKGCFHVPRCLAMCEEMLGALLSRPAPAPSPAPTPACRGAE

• Aminosugars metabolism (map00530 )

• N-acyl-D-glucosamine = N-acyl-D-mannosamine

• GlcNAc_2-epim (PF07221 )

• None

• None

ATGGAGAAAGAGCGAGAGACTCTGCAGGCCTGGAAGGAGCGCGTGGGGCAGGAGCTGGAC
CGCGTGGTGGCTTTCTGGATGGAGCACTCCCACGACCAGGAGCACGGGGGCTTCTTCACG
TGCCTTGGCCGCGAGGGGCGGGTGTATGATGACCTCAAGTATGTGTGGCTGCAGGGGAGG
CAGGTATGGATGTATTGTCGCCTGTACCGCACTTTCGAGCGCTTCCGCCATGCTCAGCTT
CTGGACGCAGCAAAAGCAGGTGGTGAGTTCTTGCTGCGGTATGCCCGGGTGGCACCTCCT
GGCAAGAAGTGTGCCTTTGTGCTGACTCGGGACGGCCGCCCGGTCAAGGTGCAGCGAACC
ATCTTCAGTGAGTGTTTCTACACCATGGCCATGAACGAGCTGTGGAGAGCCACAGGGGAA
GTGCGGTACCAGACGGAAGCGGTGGAGATGATGGATCAGATCGTCCACTGGGTGCAGGAG
GACGCGTCGGGACTGGGCCGGCCCCAGCTCCAGGGGGCCCCGGCTGCGGAGCCCATGGCG
GTGCCCATGATGCTACTGAACCTGGTGGAGCAGCTCGGGGAGGCAGATGAGGAGCTGGCG
GGCAAATACGCAGAGCTGGGGGACTGGTGCGCCCGGAGGATTCTGCAGCACGTGCAGAGG
GATGGACAAGCTGTGCTGGAGAATGTGTCAGAGGGTGGCAAGGAACTTCCTGGCTGCCTG
GGGAGACAGCAGAACCCAGGCCACACGCTGGAAGCCGGCTGGTTTCTGCTCCGTCATTGC
ATTCGGAAAGGCGACCCCGAACTTCGAGCCCACGTGATTGACAAGTTCCTATTGTTGCCC
TTCCACTCCGGATGGGACCCTGACCACGGAGGCCTCTTTTACTTCCAGGATGCTGATAAC
TTCTGCCCCACCCAGCTGGAGTGGGCCATGAAGCTCTGGTGGCCACACAGTGAAGCCATG
ATTGCCTTCCTCATGGGTTACAGTGACAGTGGGGACCCTGTGCTGCTGCGCCTCTTCTAC
CAAGTGGCTGAGTACACCTTCCGCCAGTTTCGCGATCCCGAGTACGGGGAATGGTTTGGC
TACCTGAGCCGAGAGGGCAAGGTGGCCCTCTCCATCAAGGGAGGTCCTTTCAAAGGCTGC
TTCCACGTGCCGCGGTGCCTAGCCATGTGCGAGGAGATGCTGGGCGCCCTGCTGAGCCGC
CCCGCCCCCGCCCCCTCCCCCGCCCCCACCCCCGCCTGCCGAGGCGCGGAATAA

1. Inoue H, Takahashi S, Fukui K, Miyake Y: Genetic and molecular properties of human and rat renin-binding proteins with reference to the function of the leucine zipper motif. J Biochem (Tokyo). 1991 Oct;110(4):493-500. [PubMed ]
2. Takahashi S, Takahashi K, Kaneko T, Ogasawara H, Shindo S, Kobayashi M: Human renin-binding protein is the enzyme N-acetyl-D-glucosamine 2-epimerase. J Biochem (Tokyo). 1999 Feb;125(2):348-53. [PubMed ]

1. Beta-1,4-GalTase 2
2. Beta4Gal-T2
3. b4Gal-T2
4. UDP-galactose:beta-N-acetylglucosamine beta- 1,4-galactosyltransferase 2
5. UDP-Gal:beta-GlcNAc beta-1,4- galactosyltransferase 2[Includes: Lactose synthase A protein
6. Nal synthetase
7. Beta-N-acetylglucosaminylglycopeptide beta-1,4- galactosyltransferase

MSRLLGGTLERVCKAVLLLCLLHFLVAVILYFDVYAQHLAFFSRFSARGPAHALHPAASS
SSSSSNCSRPNATASSSGLPEVPSALPGPTAPTLPPCPDSPPGLVGRLLIEFTSPMPLER
VQRENPGVLMGGRYTPPDCTPAQTVAVIIPFRHREHHLRYWLHYLHPILRRQRLRYGVYV
INQHGEDTFNRAKLLNVGFLEALKEDAAYDCFIFSDVDLVPMDDRNLYRCGDQPRHFAIA
MDKFGFRLPYAGYFGGVSGLSKAQFLRINGFPNEYWGWGGEDDDIFNRISLTGMKISRPD
IRIGRYRMIKHDRDKHNEPNPQRFTKIQNTKLTMKRDGIGSVRYQVLEVSRQPLFTNITV
DIGRPPSWPPRG

• Keratan sulfate biosynthesis (map00533 )
• N-Glycan biosynthesis (map00510 )

• UDP-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine

• Galactosyl_T_2 (PF02709 )

• 1-27

ATGAGCAGACTGCTGGGGGGGACGCTGGAGCGCGTCTGCAAGGCTGTGCTCCTTCTCTGC
CTGCTGCACTTCCTCGTGGCCGTCATCCTCTACTTTGACGTCTACGCCCAGCACCTGGCC
TTCTTCAGCCGCTTCAGTGCCCGAGGCCCTGCCCATGCCCTCCACCCAGCTGCTAGCAGC
AGCAGCAGCAGCAGCAACTGCTCCCGGCCCAACGCCACCGCCTCTAGCTCCGGGCTCCCT
GAGGTCCCCAGTGCCCTGCCCGGTCCCACGGCTCCCACGCTGCCACCCTGTCCTGACTCG
CCACCTGGTCTTGTGGGCAGACTGCTGATCGAGTTCACCTCACCCATGCCCCTGGAGCGG
GTGCAGAGGGAGAACCCAGGCGTGCTCATGGGCGGCCGATACACACCGCCCGACTGCACC
CCAGCCCAGACGGTGGCGGTCATCATCCCCTTTAGACACCGGGAACACCACCTGCGCTAC
TGGCTCCACTATCTACACCCCATCTTGAGGCGGCAGCGGCTGCGCTACGGCGTCTATGTC
ATCAACCAGCATGGTGAGGACACCTTCAACCGGGCCAAGCTGCTTAACGTGGGCTTCCTA
GAGGCGCTGAAGGAGGATGCCGCCTATGACTGCTTCATCTTCAGCGATGTGGACCTGGTC
CCCATGGATGACCGCAACCTATACCGCTGCGGCGACCAACCCCGCCACTTTGCCATTGCC
ATGGACAAGTTTGGCTTCCGGCTTCCCTATGCTGGCTACTTTGGAGGTGTGTCAGGCCTG
AGTAAGGCTCAGTTTCTGAGAATCAATGGCTTCCCCAATGAGTACTGGGGCTGGGGTGGC
GAGGATGATGACATCTTCAACCGGATCTCCCTGACTGGGATGAAGATCTCACGCCCAGAC
ATCCGAATCGGCCGCTACCGCATGATCAAGCACGACCGCGACAAGCATAACGAACCTAAC
CCTCAGAGGTTTACCAAGATTCAAAACACGAAGCTGACCATGAAGCGGGACGGCATTGGG
TCAGTGCGGTACCAGGTCTTGGAGGTGTCTCGGCAACCACTCTTCACCAATATCACAGTG
GACATTGGGCGGCCTCCGTCGTGGCCCCCTCGGGGCTGA

1. Almeida R, Amado M, David L, Levery SB, Holmes EH, Merkx G, van Kessel AG, Rygaard E, Hassan H, Bennett E, Clausen H: A family of human beta4-galactosyltransferases. Cloning and expression of two novel UDP-galactose:beta-n-acetylglucosamine beta1, 4-galactosyltransferases, beta4Gal-T2 and beta4Gal-T3. J Biol Chem. 1997 Dec 19;272(51):31979-91. [PubMed ]
2. Lo NW, Shaper JH, Pevsner J, Shaper NL: The expanding beta 4-galactosyltransferase gene family: messages from the databanks. Glycobiology. 1998 May;8(5):517-26. [PubMed ]
3. Guo S, Sato T, Shirane K, Furukawa K: Galactosylation of N-linked oligosaccharides by human beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed in Sf-9 cells. Glycobiology. 2001 Oct;11(10):813-20. [PubMed ]
4. Amado M, Almeida R, Schwientek T, Clausen H: Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions. Biochim Biophys Acta. 1999 Dec 6;1473(1):35-53. [PubMed ]

1. Beta-1,4-GalTase 1
2. Beta4Gal-T1
3. b4Gal-T1
4. UDP-galactose:beta-N-acetylglucosamine beta- 1,4-galactosyltransferase 1
5. UDP-Gal:beta-GlcNAc beta-1,4- galactosyltransferase 1[Includes: Lactose synthase A protein
6. Nal synthetase
7. Beta-N-acetylglucosaminylglycopeptide beta-1,4- galactosyltransferase

MRLREPLLSGSAAMPGASLQRACRLLVAVCALHLGVTLVYYLAGRDLSRLPQLVGVSTPL
QGGSNSAAAIGQSSGELRTGGARPPPPLGASSQPRPGGDSSPVVDSGPGPASNLTSVPVP
HTTALSLPACPEESPLLVGPMLIEFNMPVDLELVAKQNPNVKMGGRYAPRDCVSPHKVAI
IIPFRNRQEHLKYWLYYLHPVLQRQQLDYGIYVINQAGDTIFNRAKLLNVGFQEALKDYD
YTCFVFSDVDLIPMNDHNAYRCFSQPRHISVAMDKFGFSLPYVQYFGGVSALSKQQFLTI
NGFPNNYWGWGGEDDDIFNRLVFRGMSISRPNAVVGRCRMIRHSRDKKNEPNPQRFDRIA
HTKETMLSDGLNSLTYQVLDVQRYPLYTQITVDIGTPS

• Keratan sulfate biosynthesis (map00533 )
• N-Glycan biosynthesis (map00510 )

• UDP-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine

• Galactosyl_T_2 (PF02709 )

• 1-37

ATGAGGCTTCGGGAGCCGCTCCTGAGCGGCGCCGCGATGCCAGGCGCGTCCCTACAGCGG
GCCTGCCGCCTGCTCGTGGCCGTCTGCGCTCTGCACCTTGGCGTCACCCTCGTTTACTAC
CTGGCTGGCCGCGACCTGAGCCGCCTGCCCCAACTGGTCGGAGTCTCCACACCGCTGCAG
GGCGGCTCGAACAGTGCCGCCGCCATCGGGCAGTCCTCCGGGGAGCTCCGGACCGGAGGG
GCCCGGCCGCCGCCTCCTCTAGGCGCCTCCTCCCAGCCGCGCCCGGGTGGCGACTCCAGC
CCAGTCGTGGATTCTGGCCCTGGCCCCGCTAGCAACTTGACCTCGGTCCCAGTGCCCCAC
ACCACCGCACTGTCGCTGCCCGCCTGCCCTGAGGAGTCCCCGCTGCTTGTGGGCCCCATG
CTGATTGAGTTTAACATGCCTGTGGACCTGGAGCTCGTGGCAAAGCAGAACCCAAATGTG
AAGATGGGCGGCCGCTATGCCCCCAGGGACTGCGTCTCTCCTCACAAAGTGGCCATCATC
ATTCCATTCCGCAACCGGCAGGAGCACCTCAAGTACTGGCTATATTATTTGCACCCAGTC
CTGCAGCGCCAGCAGCTGGACTATGGCATCTATGGCATCTATGTTATCAACCAGGCGGGA
GACACTATATTCAATCGTGCTAAGCTCCTCAATGTTGGCTTTCAAGAAGCCTTGAAGGAC
TATGACTACACCTGCTTTGTGTTTAGTGACGTGGACCTCATCCCAATGAATGACCATAAT
GCGTACAGGTGTTTTTCACAGCCACGGCACATTTCCGTTGCAATGGATAAGTTTGGATTC
AGCCTACCTTATGTTCAGTATTTTGGAGGTGTCTCTGCTCTAAGTAAACAACAGTTTCTA
ACCATCAATGGATTTCCTAATAATTATTGGGGCTGGGGAGGAGAAGATGATGACATTTTT
AACAGATTAGTTTTTAGAGGCATGTCTATATCTCGCCCAAATGCTGTGGTCGGGAGGTGT
CGCATGATCCGCCACTCAAGAGACAAAAAAAATGAACCCAATCCTCAGAGGTTTGACCGA
ATTGCACACACAAAGGAGACAATGCTCTCTGATGGTTTGAACTCACTCACCTACCAGGTG
CTGGATGTACAGAGATACCCATTGTATACCCAAATCACAGTGGACATCGGGACACCGAGC
TAG

1. Masri KA, Appert HE, Fukuda MN: Identification of the full-length coding sequence for human galactosyltransferase (beta-N-acetylglucosaminide: beta 1,4-galactosyltransferase). Biochem Biophys Res Commun. 1988 Dec 15;157(2):657-63. [PubMed ]
2. Watzele G, Berger EG: Near identity of HeLa cell galactosyltransferase with the human placental enzyme. Nucleic Acids Res. 1990 Dec 11;18(23):7174. [PubMed ]
3. Mengle-Gaw L, McCoy-Haman MF, Tiemeier DC: Genomic structure and expression of human beta-1,4-galactosyltransferase. Biochem Biophys Res Commun. 1991 May 15;176(3):1269-76. [PubMed ]
4. Uejima T, Uemura M, Nozawa S, Narimatsu H: Complementary DNA cloning for galactosyltransferase associated with tumor and determination of antigenic epitopes recognized by specific monoclonal antibodies. Cancer Res. 1992 Nov 15;52(22):6158-63. [PubMed ]
5. Kudo T, Narimatsu H: The beta 1,4-galactosyltransferase gene is post-transcriptionally regulated during differentiation of mouse F9 teratocarcinoma cells. Glycobiology. 1995 Jun;5(4):397-403. [PubMed ]
6. Chatterjee SK, Mukerjee S, Tripathi PK: Analysis of the sequences of human beta-1,4-galactosyltransferase cDNA clones. Int J Biochem Cell Biol. 1995 Mar;27(3):329-36. [PubMed ]
7. Appert HE, Rutherford TJ, Tarr GE, Wiest JS, Thomford NR, McCorquodale DJ: Isolation of a cDNA coding for human galactosyltransferase. Biochem Biophys Res Commun. 1986 Aug 29;139(1):163-8. [PubMed ]
8. Appert HE, Rutherford TJ, Tarr GE, Thomford NR, McCorquodale DJ: Isolation of galactosyltransferase from human milk and the determination of its N-terminal amino acid sequence. Biochem Biophys Res Commun. 1986 Jul 16;138(1):224-9. [PubMed ]
9. Aoki D, Appert HE, Johnson D, Wong SS, Fukuda MN: Analysis of the substrate binding sites of human galactosyltransferase by protein engineering. EMBO J. 1990 Oct;9(10):3171-8. [PubMed ]
10. Lopez LC, Youakim A, Evans SC, Shur BD: Evidence for a molecular distinction between Golgi and cell surface forms of beta 1,4-galactosyltransferase. J Biol Chem. 1991 Aug 25;266(24):15984-91. [PubMed ]
11. Yamaguchi N, Fukuda MN: Golgi retention mechanism of beta-1,4-galactosyltransferase. Membrane-spanning domain-dependent homodimerization and association with alpha- and beta-tubulins. J Biol Chem. 1995 May 19;270(20):12170-6. [PubMed ]
12. Amado M, Almeida R, Schwientek T, Clausen H: Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions. Biochim Biophys Acta. 1999 Dec 6;1473(1):35-53. [PubMed ]

1. N-acetyl-beta- glucosaminidase
2. Beta-N-acetylhexosaminidase
3. Hexosaminidase B
4. Cervical cancer proto-oncogene 7
5. HCC-7[Contains: Beta- hexosaminidase beta-B chain
6. Beta-hexosaminidase beta-A chain]

MELCGLGLPRPPMLLALLLATLLAAMLALLTQVALVVQVAEAARAPSVSAKPGPALWPLP
LSVKMTPNLLHLAPENFYISHSPNSTAGPSCTLLEEAFRRYHGYIFGFYKWHHEPAEFQA
KTQVQQLLVSITLQSECDAFPNISSDESYTLLVKEPVAVLKANRVWGALRGLETFSQLVY
QDSYGTFTINESTIIDSPRFSHRGILIDTSRHYLPVKIILKTLDAMAFNKFNVLHWHIVD
DQSFPYQSITFPELSNKGSYSLSHVYTPNDVRMVIEYARLRGIRVLPEFDTPGHTLSWGK
GQKDLLTPCYSRQNKLDSFGPINPTLNTTYSFLTTFFKEISEVFPDQFIHLGGDEVEFKC
WESNPKIQDFMRQKGFGTDFKKLESFYIQKVLDIIATINKGSIVWQEVFDDKAKLAPGTI
VEVWKDSAYPEELSRVTASGFPVILSAPWYLDLISYGQDWRKYYKVEPLDFGGTQKQKQL
FIGGEACLWGEYVDATNLTPRLWPRASAVGERLWSSKDVRDMDDAYDRLTRHRCRMVERG
IAAQPLYAGYCNHENM

• Aminosugars metabolism (map00530 )
• Globoside metabolism (map00603 )
• Glycosaminoglycan degradation (map00531 )
• N-Glycan degradation (map00511 )

• Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides

• Glyco_hydro_20 (PF00728 )
• Glyco_hydro_20b (PF02838 )

• None

• 13-35

GTCCCGAGGCTCCGGCTCGGCAGACCGGGCGGAAAGCAGCCGAGCGGCCATGGAGCTGTG
CGGGCTGGGGCTGCCCCGGCCGCCCATGCTGCTGGCGCTGCTGTTGGCGACATGCTGGCG
GCGATGTTGGCGCTGCTGACTCAGGTGGCGCTGGTGGTGCAGGTGGCGGAGGCGGCTCGG
GCCCCGAGCGTCTCGGCCAAGCCGGGGCCGGCGCTGTGGCCCCTGCCGCTCTCGGTGAAG
ATGACCCCGAACCTGCTGCATCTCGCCCCGGAGAACTTCTACATCAGCCACAGCCCCAAT
TCCACGGCGGGCCCCTCCTGCACCCTGCTGGAGGAAGCGTTTCGACGATATCATGGCTAT
ATTTTTGGTTTCTACAAGTGGCATCATGAACCTGCTGAATTCCAGGCTAAAACCCAGGTT
CAGCAACTTCTTGTCTCAATCACCCTTCAGTCAGAGTGTGATGCTTTCCCCAACATATCT
TCAGATGAGTCTTATACTTTACTTGTGAAAGAACCAGTGGCTGTCCTTAAGGCCAACAGA
GTTTGGGGAGCATTACGAGGTTTAGAGACCTTTAGCCAGTTAGTTTATCAAGATTCTTAT
GGAACTTTCACCATCAATGAATCCACCATTATTGATTCTCCAAGGTTTTCTCACAGAGGA
ATTTTGATTGATACATCCAGACATTATCTGCCAGTTAAGATTATTCTTAAAACTCTGGAT
GCCATGGCTTTTAATAAGTTTAATGTTCTTCACTGGCACATAGTTGATGACCAGTCTTTC
CCATATCAGAGCATCACTTTTCCTGAGTTAAGCAATAAAGGAAGCTATTCTTTGTCTCAT
GTTTATACACCAAATGATGTCCGTATGGTGATTGAATATGCCAGATTACGAGGAATTCGA
GTCCTGCCAGAATTTGATACCCCTGGGCATACACTATCTTGGGGAAAAGGTCAGAAAGAC
CTCCTGACTCCATGTTACAGTAGACAAAACAAGTTGGACTCTTTTGGACCTATAAACCCT
ACTCTGAATACAACATACAGCTTCCTTACTACATTTTTCAAAGAAATTAGTGAGGTGTTT
CCAGATCAATTCATTCATTTGGGAGGAGATGAAGTGGAATTTAAATGTTGGGAATCAAAT
CCAAAAATTCAAGATTTCATGAGGCAAAAAGGCTTTGGCACAGATTTTAAGAAACTAGAA
TCTTTCTACATTCAAAAGGTTTTGGATATTATTGCAACCATAAACAAGGGATCCATTGTC
TGGCAGGAGGTTTTTGATGATAAAGCAAAGCTTGCGCCGGGCACAATAGTTGAAGTATGG
AAAGACAGCGCATATCCTGAGGAACTCAGTAGAGTCACAGCATCTGGCTTCCCTGTAATC
CTTTCTGCTCCTTGGTACTTAGATTTGATTAGCTATGGACAAGATTGGAGGAAATACTAT
AAAGTGGAACCTCTTGATTTTGGCGGTACTCAGAAACAGAAACAACTTTTCATTGGTGGA
GAAGCTTGTCTATGGGGAGAATATGTGGATGCAACTAACCTCACTCCAAGATTATGGCCT
CGGGCAAGTGCTGTTGGTGAGAGACTCTGGAGTTCCAAAGATGTCAGAGATATGGATGAC
GCCTATGACAGACTGACAAGGCACCGCTGCAGGATGGTCGAACGTGGAATAGCTGCACAA
CCTCTTTATGCTGGATATTGTAACCATGAGAACATGTAA

1. Korneluk RG, Mahuran DJ, Neote K, Klavins MH, O'Dowd BF, Tropak M, Willard HF, Anderson MJ, Lowden JA, Gravel RA: Isolation of cDNA clones coding for the alpha-subunit of human beta-hexosaminidase. Extensive homology between the alpha- and beta-subunits and studies on Tay-Sachs disease. J Biol Chem. 1986 Jun 25;261(18):8407-13. [PubMed ]
2. Neote K, Bapat B, Dumbrille-Ross A, Troxel C, Schuster SM, Mahuran DJ, Gravel RA: Characterization of the human HEXB gene encoding lysosomal beta-hexosaminidase. Genomics. 1988 Nov;3(4):279-86. [PubMed ]
3. Proia RL: Gene encoding the human beta-hexosaminidase beta chain: extensive homology of intron placement in the alpha- and beta-chain genes. Proc Natl Acad Sci U S A. 1988 Mar;85(6):1883-7. [PubMed ]
4. Sonderfeld-Fresko S, Proia RL: Synthesis and assembly of a catalytically active lysosomal enzyme, beta-hexosaminidase B, in a cell-free system. J Biol Chem. 1988 Sep 15;263(26):13463-9. [PubMed ]
5. Neote K, Brown CA, Mahuran DJ, Gravel RA: Translation initiation in the HEXB gene encoding the beta-subunit of human beta-hexosaminidase. J Biol Chem. 1990 Dec 5;265(34):20799-806. [PubMed ]
6. Stirling J, Leung A, Gravel RA, Mahuran D: Localization of the pro-sequence within the total deduced primary structure of human beta-hexosaminidase B. FEBS Lett. 1988 Apr 11;231(1):47-50. [PubMed ]
7. Mahuran DJ: Characterization of human placental beta-hexosaminidase I2. Proteolytic processing intermediates of hexosaminidase A. J Biol Chem. 1990 Apr 25;265(12):6794-9. [PubMed ]
8. Hubbes M, Callahan J, Gravel R, Mahuran D: The amino-terminal sequences in the pro-alpha and -beta polypeptides of human lysosomal beta-hexosaminidase A and B are retained in the mature isozymes. FEBS Lett. 1989 Jun 5;249(2):316-20. [PubMed ]
9. Mahuran DJ, Neote K, Klavins MH, Leung A, Gravel RA: Proteolytic processing of pro-alpha and pro-beta precursors from human beta-hexosaminidase. Generation of the mature alpha and beta a beta b subunits. J Biol Chem. 1988 Apr 5;263(10):4612-8. [PubMed ]
10. O'Dowd BF, Quan F, Willard HF, Lamhonwah AM, Korneluk RG, Lowden JA, Gravel RA, Mahuran DJ: Isolation of cDNA clones coding for the beta subunit of human beta-hexosaminidase. Proc Natl Acad Sci U S A. 1985 Feb;82(4):1184-8. [PubMed ]
11. O'Dowd BF, Cumming DA, Gravel RA, Mahuran D: Oligosaccharide structure and amino acid sequence of the major glycopeptides of mature human beta-hexosaminidase. Biochemistry. 1988 Jul 12;27(14):5216-26. [PubMed ]
12. Zhang H, Li XJ, Martin DB, Aebersold R: Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol. 2003 Jun;21(6):660-6. Epub 2003 May 18. [PubMed ]
13. Schuette CG, Weisgerber J, Sandhoff K: Complete analysis of the glycosylation and disulfide bond pattern of human beta-hexosaminidase B by MALDI-MS. Glycobiology. 2001 Jul;11(7):549-56. [PubMed ]
14. Tews I, Perrakis A, Oppenheim A, Dauter Z, Wilson KS, Vorgias CE: Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease. Nat Struct Biol. 1996 Jul;3(7):638-48. [PubMed ]
15. Mahuran DJ: The biochemistry of HEXA and HEXB gene mutations causing GM2 gangliosidosis. Biochim Biophys Acta. 1991 Feb 22;1096(2):87-94. [PubMed ]
16. Banerjee P, Siciliano L, Oliveri D, McCabe NR, Boyers MJ, Horwitz AL, Li SC, Dawson G: Molecular basis of an adult form of beta-hexosaminidase B deficiency with motor neuron disease. Biochem Biophys Res Commun. 1991 Nov 27;181(1):108-15. [PubMed ]
17. Wakamatsu N, Kobayashi H, Miyatake T, Tsuji S: A novel exon mutation in the human beta-hexosaminidase beta subunit gene affects 3' splice site selection. J Biol Chem. 1992 Feb 5;267(4):2406-13. [PubMed ]
18. Bolhuis PA, Ponne NJ, Bikker H, Baas F, Vianney de Jong JM: Molecular basis of an adult form of Sandhoff disease: substitution of glutamine for arginine at position 505 of the beta-chain of beta-hexosaminidase results in a labile enzyme. Biochim Biophys Acta. 1993 Sep 8;1182(2):142-6. [PubMed ]
19. Kuroki Y, Itoh K, Nadaoka Y, Tanaka T, Sakuraba H: A novel missense mutation (C522Y) is present in the beta-hexosaminidase beta-subunit gene of a Japanese patient with infantile Sandhoff disease. Biochem Biophys Res Commun. 1995 Jul 17;212(2):564-71. [PubMed ]
20. Gomez-Lira M, Sangalli A, Mottes M, Perusi C, Pignatti PF, Rizzuto N, Salviati A: A common beta hexosaminidase gene mutation in adult Sandhoff disease patients. Hum Genet. 1995 Oct;96(4):417-22. [PubMed ]
21. Zhang ZX, Wakamatsu N, Akerman BR, Mules EH, Thomas GH, Gravel RA: A second, large deletion in the HEXB gene in a patient with infantile Sandhoff disease. Hum Mol Genet. 1995 Apr;4(4):777-80. [PubMed ]
22. Redonnet-Vernhet I, Mahuran DJ, Salvayre R, Dubas F, Levade T: Significance of two point mutations present in each HEXB allele of patients with adult GM2 gangliosidosis (Sandhoff disease) homozygosity for the Ile207-->Val substitution is not associated with a clinical or biochemical phenotype. Biochim Biophys Acta. 1996 Nov 15;1317(2):127-33. [PubMed ]
23. Narkis G, Adam A, Jaber L, Pennybacker M, Proia RL, Navon R: Molecular basis of heat labile hexosaminidase B among Jews and Arabs. Hum Mutat. 1997;10(6):424-9. [PubMed ]
24. Fujimaru M, Tanaka A, Choeh K, Wakamatsu N, Sakuraba H, Isshiki G: Two mutations remote from an exon/intron junction in the beta-hexosaminidase beta-subunit gene affect 3'-splice site selection and cause Sandhoff disease. Hum Genet. 1998 Oct;103(4):462-9. [PubMed ]
25. Hou Y, McInnes B, Hinek A, Karpati G, Mahuran D: A Pro504 --> Ser substitution in the beta-subunit of beta-hexosaminidase A inhibits alpha-subunit hydrolysis of GM2 ganglioside, resulting in chronic Sandhoff disease. J Biol Chem. 1998 Aug 14;273(33):21386-92. [PubMed ]

1. N-acetyl- beta-glucosaminidase
2. Beta-N-acetylhexosaminidase
3. Hexosaminidase A

MTSSRLWFSLLLAAAFAGRATALWPWPQNFQTSDQRYVLYPNNFQFQYDVSSAAQPGCSV
LDEAFQRYRDLLFGSGSWPRPYLTGKRHTLEKNVLVVSVVTPGCNQLPTLESVENYTLTI
NDDQCLLLSETVWGALRGLETFSQLVWKSAEGTFFINKTEIEDFPRFPHRGLLLDTSRHY
LPLSSILDTLDVMAYNKLNVFHWHLVDDPSFPYESFTFPELMRKGSYNPVTHIYTAQDVK
EVIEYARLRGIRVLAEFDTPGHTLSWGPGIPGLLTPCYSGSEPSGTFGPVNPSLNNTYEF
MSTFFLEVSSVFPDFYLHLGGDEVDFTCWKSNPEIQDFMRKKGFGEDFKQLESFYIQTLL
DIVSSYGKGYVVWQEVFDNKVKIQPDTIIQVWREDIPVNYMKELELVTKAGFRALLSAPW
YLNRISYGPDWKDFYVVEPLAFEGTPEQKALVIGGEACMWGEYVDNTNLVPRLWPRAGAV
AERLWSNKLTSDLTFAYERLSHFRCELLRRGVQAQPLNVGFCEQEFEQT

• Aminosugars metabolism (map00530 )
• Globoside metabolism (map00603 )
• Glycosaminoglycan degradation (map00531 )
• N-Glycan degradation (map00511 )

• Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides

• Glyco_hydro_20 (PF00728 )
• Glyco_hydro_20b (PF02838 )

• 1-22

TTACCCGAACAACTTTCAATTCCAGTACGATGTCAGCTCGGCCGCGCAGCCCGGCTGCTC
AGTCCTCGACGAGGCCTTCCAGCGCTATCGTGACCTGCTTTTCGGTTCCGGGTCTTGGCC
CCGTCCTTACCTCACAGGGAAACGGCATACACTGGAGAAGAATGTGTTGGTTGTCTCTGT
AGTCACACCTGGATGTAACCAGCTTCCTACTTTGGAGTCAGTGGAGAATTATACCCTGAC
CATAAATGATGACCAGTGTTTACTCCTCTCTGAGACTGTCTGGGGAGCTCTCCGAGGTCT
GGAGACTTTTAGCCAGCTTGTTTGGAAATCTGCTGAGGGCACATTCTTTATCAACAAGAC
TGAGATTGAGGACTTTCCCCGCTTTCCTCACCGGGGCTTGCTGTTGGATACATCTCGCCA
TTACCTGCCACTCTCTAGCATCCTGGACACTCTGGATGTCATGGCGTACAATAAATTGAA
CGTGTTCCACTGGCATCTGGTAGATGATCCTTCCTTCCCATATGAGAGCTTCACTTTTCC
AGAGCTCATGAGAAAGGGGTCCTACAACCCTGTCACCCACATCTACACAGCACAGGATGT
GAAGGAGGTCATTGAATACGCACGGCTCCGGGGTATCCGTGTGCTTGCAGAGTTTGACAC
TCCTGGCCACACTTTGTCCTGGGGACCAGGTATCCCTGGATTACTGACTCCTTGCTACTC
TGGGTCTGAGCCCTCTGGCACCTTTGGACCAGTGAATCCCAGTCTCAATAATACCTATGA
GTTCATGAGCACATTCTTCTTAGAAGTCAGCTCTGTCTTCCCAGATTTTTATCTTCATCT
TGGAGGAGATGAGGTTGATTTCACCTGCTGGAAGTCCAACCCAGAGATCCAGGACTTTAT
GAGGAAGAAAGGCTTCGGTGAGGACTTCAAGCAGCTGGAGTCCTTCTACATCCAGACGCT
GCTGGACATCGTCTCTTCTTATGGCAAGGGCTATGTGGTCTGGCAGGAGGTGTTTGATAA
TAAAGTAAAGATTCAGCCAGACACAATCATACAGGTGTGGCGAGAGGATATTCCAGTGAA
CTATATGAAGGAGCTGGAACTGGTCACCAAGGCCGGCTTCCGGGCCCTTCTCTCTGCCCC
CTGGTACCTGAACCGTATATCCTATGGCCCTGACTGGAAGGATTTCTACGTAGTGGAACC
CCTGGCATTTGAAGGTACCCCTGAGCAGAAGGCTCTGGTGATTGGTGGAGAGGCTTGTAT
GTGGGGAGAATATGTGGACAACACAAACCTGGTCCCCAGGCTCTGGCCCAGAGCAGGGGC
TGTTGCCGAAAGGCTGTGGAGCAACAAGTTGACATCTGACCTGACATTTGCCTATGAACG
TTTGTCACACTTCCGCTGTGAGTTGCTGAGGCGAGGTGTCCAGGCCCAACCCCTCAATGT
AGGCTTCTGTGAGCAGGAGTTTGAACAGACCTGAG

1. Myerowitz R, Piekarz R, Neufeld EF, Shows TB, Suzuki K: Human beta-hexosaminidase alpha chain: coding sequence and homology with the beta chain. Proc Natl Acad Sci U S A. 1985 Dec;82(23):7830-4. [PubMed ]
2. Triggs-Raine BL, Akerman BR, Clarke JT, Gravel RA: Sequence of DNA flanking the exons of the HEXA gene, and identification of mutations in Tay-Sachs disease. Am J Hum Genet. 1991 Nov;49(5):1041-54. [PubMed ]
3. Korneluk RG, Mahuran DJ, Neote K, Klavins MH, O'Dowd BF, Tropak M, Willard HF, Anderson MJ, Lowden JA, Gravel RA: Isolation of cDNA clones coding for the alpha-subunit of human beta-hexosaminidase. Extensive homology between the alpha- and beta-subunits and studies on Tay-Sachs disease. J Biol Chem. 1986 Jun 25;261(18):8407-13. [PubMed ]
4. Proia RL, Soravia E: Organization of the gene encoding the human beta-hexosaminidase alpha-chain. J Biol Chem. 1987 Apr 25;262(12):5677-81. [PubMed ]
5. Mahuran DJ, Neote K, Klavins MH, Leung A, Gravel RA: Proteolytic processing of pro-alpha and pro-beta precursors from human beta-hexosaminidase. Generation of the mature alpha and beta a beta b subunits. J Biol Chem. 1988 Apr 5;263(10):4612-8. [PubMed ]
6. O'Dowd BF, Cumming DA, Gravel RA, Mahuran D: Oligosaccharide structure and amino acid sequence of the major glycopeptides of mature human beta-hexosaminidase. Biochemistry. 1988 Jul 12;27(14):5216-26. [PubMed ]
7. Weitz G, Proia RL: Analysis of the glycosylation and phosphorylation of the alpha-subunit of the lysosomal enzyme, beta-hexosaminidase A, by site-directed mutagenesis. J Biol Chem. 1992 May 15;267(14):10039-44. [PubMed ]
8. Tse R, Vavougios G, Hou Y, Mahuran DJ: Identification of an active acidic residue in the catalytic site of beta-hexosaminidase. Biochemistry. 1996 Jun 11;35(23):7599-607. [PubMed ]
9. Tews I, Perrakis A, Oppenheim A, Dauter Z, Wilson KS, Vorgias CE: Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease. Nat Struct Biol. 1996 Jul;3(7):638-48. [PubMed ]
10. Mahuran DJ: The biochemistry of HEXA and HEXB gene mutations causing GM2 gangliosidosis. Biochim Biophys Acta. 1991 Feb 22;1096(2):87-94. [PubMed ]
11. Myerowitz R: Tay-Sachs disease-causing mutations and neutral polymorphisms in the Hex A gene. Hum Mutat. 1997;9(3):195-208. [PubMed ]
12. Nakano T, Muscillo M, Ohno K, Hoffman AJ, Suzuki K: A point mutation in the coding sequence of the beta-hexosaminidase alpha gene results in defective processing of the enzyme protein in an unusual GM2-gangliosidosis variant. J Neurochem. 1988 Sep;51(3):984-7. [PubMed ]
13. Navon R, Proia RL: The mutations in Ashkenazi Jews with adult GM2 gangliosidosis, the adult form of Tay-Sachs disease. Science. 1989 Mar 17;243(4897):1471-4. [PubMed ]
14. Tanaka A, Punnett HH, Suzuki K: A new point mutation in the beta-hexosaminidase alpha subunit gene responsible for infantile Tay-Sachs disease in a non-Jewish Caucasian patient (a Kpn mutant). Am J Hum Genet. 1990 Sep;47(3):568-74. [PubMed ]
15. Akli S, Chelly J, Lacorte JM, Poenaru L, Kahn A: Seven novel Tay-Sachs mutations detected by chemical mismatch cleavage of PCR-amplified cDNA fragments. Genomics. 1991 Sep;11(1):124-34. [PubMed ]
16. Mules EH, Hayflick S, Miller CS, Reynolds LW, Thomas GH: Six novel deleterious and three neutral mutations in the gene encoding the alpha-subunit of hexosaminidase A in non-Jewish individuals. Am J Hum Genet. 1992 Apr;50(4):834-41. [PubMed ]
17. Triggs-Raine BL, Mules EH, Kaback MM, Lim-Steele JS, Dowling CE, Akerman BR, Natowicz MR, Grebner EE, Navon R, Welch JP, et al.: A pseudodeficiency allele common in non-Jewish Tay-Sachs carriers: implications for carrier screening. Am J Hum Genet. 1992 Oct;51(4):793-801. [PubMed ]
18. Fernandes M, Kaplan F, Natowicz M, Prence E, Kolodny E, Kaback M, Hechtman P: A new Tay-Sachs disease B1 allele in exon 7 in two compound heterozygotes each with a second novel mutation. Hum Mol Genet. 1992 Dec;1(9):759-61. [PubMed ]
19. Trop I, Kaplan F, Brown C, Mahuran D, Hechtman P: A glycine250--> aspartate substitution in the alpha-subunit of hexosaminidase A causes juvenile-onset Tay-Sachs disease in a Lebanese-Canadian family. Hum Mutat. 1992;1(1):35-9. [PubMed ]
20. Akalin N, Shi HP, Vavougios G, Hechtman P, Lo W, Scriver CR, Mahuran D, Kaplan F: Novel Tay-Sachs disease mutations from China. Hum Mutat. 1992;1(1):40-6. [PubMed ]
21. Cao Z, Natowicz MR, Kaback MM, Lim-Steele JS, Prence EM, Brown D, Chabot T, Triggs-Raine BL: A second mutation associated with apparent beta-hexosaminidase A pseudodeficiency: identification and frequency estimation. Am J Hum Genet. 1993 Dec;53(6):1198-205. [PubMed ]
22. Akli S, Chomel JC, Lacorte JM, Bachner L, Kahn A, Poenaru L: Ten novel mutations in the HEXA gene in non-Jewish Tay-Sachs patients. Hum Mol Genet. 1993 Jan;2(1):61-7. [PubMed ]
23. Harmon DL, Gardner-Medwin D, Stirling JL: Two new mutations in a late infantile Tay-Sachs patient are both in exon 1 of the beta-hexosaminidase alpha subunit gene. J Med Genet. 1993 Feb;30(2):123-8. [PubMed ]
24. Tomczak J, Grebner EE: Three novel beta-hexosaminidase A mutations in obligate carriers of Tay-Sachs disease. Hum Mutat. 1994;4(1):71-2. [PubMed ]
25. Tanaka A, Sakazaki H, Murakami H, Isshiki G, Suzuki K: Molecular genetics of Tay-Sachs disease in Japan. J Inherit Metab Dis. 1994;17(5):593-600. [PubMed ]
26. Triggs-Raine B, Richard M, Wasel N, Prence EM, Natowicz MR: Mutational analyses of Tay-Sachs disease: studies on Tay-Sachs carriers of French Canadian background living in New England. Am J Hum Genet. 1995 Apr;56(4):870-9. [PubMed ]
27. Peleg L, Meltzer F, Karpati M, Goldman B: GM2 gangliosidosis B1 variant: biochemical and molecular characterization of hexosaminidase A. Biochem Mol Med. 1995 Apr;54(2):126-32. [PubMed ]
28. Navon R, Khosravi R, Korczyn T, Masson M, Sonnino S, Fardeau M, Eymard B, Lefevre M, Turpin JC, Rondot P, et al.: A new mutation in the HEXA gene associated with a spinal muscular atrophy phenotype. Neurology. 1995 Mar;45(3 Pt 1):539-43. [PubMed ]
29. De Gasperi R, Gama Sosa MA, Battistini S, Yeretsian J, Raghavan S, Zelnik N, Leshinsky E, Kolodny EH: Late-onset GM2 gangliosidosis: Ashkenazi Jewish family with an exon 5 mutation (Tyr180-->His) in the Hex A alpha-chain gene. Neurology. 1996 Aug;47(2):547-52. [PubMed ]
30. Akerman BR, Natowicz MR, Kaback MM, Loyer M, Campeau E, Gravel RA: Novel mutations and DNA-based screening in non-Jewish carriers of Tay-Sachs disease. Am J Hum Genet. 1997 May;60(5):1099-106. [PubMed ]
31. Kaufman M, Grinshpun-Cohen J, Karpati M, Peleg L, Goldman B, Akstein E, Adam A, Navon R: Tay-Sachs disease and HEXA mutations among Moroccan Jews. Hum Mutat. 1997;10(4):295-300. [PubMed ]
32. Gil Ribeiro M, Pinto RA, Suzuki K, Sa Miranda MC: Two novel (1334delC and 1363G to A, G455R) mutations in exon 12 of the beta-hexosaminidase alpha-chain gene in two Portuguese patients. Hum Mutat. 1997;10(5):359-60. [PubMed ]
33. Drucker L, Hemli JA, Navon R: Two mutated HEXA alleles in a Druze patient with late-infantile Tay-Sachs disease. Hum Mutat. 1997;10(6):451-7. [PubMed ]
34. Petroulakis E, Cao Z, Clarke JT, Mahuran DJ, Lee G, Triggs-Raine B: W474C amino acid substitution affects early processing of the alpha-subunit of beta-hexosaminidase A and is associated with subacute G(M2) gangliosidosis. Hum Mutat. 1998;11(6):432-42. [PubMed ]
35. Tanaka A, Hoang LT, Nishi Y, Maniwa S, Oka M, Yamano T: Different attenuated phenotypes of GM2 gangliosidosis variant B in Japanese patients with HEXA mutations at codon 499, and five novel mutations responsible for infantile acute form. J Hum Genet. 2003;48(11):571-4. Epub 2003 Oct 18. [PubMed ]

1. GlcNAc kinase

MAAIYGGVEGGGTRSEVLLVSEDGKILAEADGLSTNHWLIGTDKCVERINEMVNRAKRKA
GVDPLVPLRSLGLSLSGGDQEDAGRILIEELRDRFPYLSESYLITTDAAGSIATATPDGG
VVLISGTGSNCRLINPDGSESGCGGWGHMMGDEGSAYWIAHQAVKIVFDSIDNLEAAPHD
IGYVKQAMFHYFQVPDRLGILTHLYRDFDKCRFAGFCRKIAEGAQQGDPLSRYIFRKAGE
MLGRHIVAVLPEIDPVLFQGKIGLPILCVGSVWKSWELLKEGFLLALTQGREIQAQNFFS
SFTLMKLRHSSALGGASLGARHIGHLLPMDYSANAIAFYSYTFS

• Aminosugars metabolism (map00530 )
• Glutamate Metabolism (map00251 )

• ATP + N-acetyl-D-glucosamine = ADP + N-acetyl-D-glucosamine 6-phosphate

• BcrAD_BadFG (PF01869 )

• None

• None

ATGGCCGCGATCTATGGGGGTGTAGAGGGGGGAGGCACACGATCCGAGGTCCTTTTAGTC
TCAGAGGATGGGAAGATCCTGGCAGAAGCAGATGGACTGAGCACAAACCACTGGCTGATC
GGGACAGACAAGTGTGTGGAGAGGATCAATGAGATGGTGAACAGGGCCAAACGGAAAGCA
GGGGTGGATCCTCTGGTACCGCTGCGAATTTTGGGCCTATCTCTGAGCGGTGGGGACCAG
GAGGACGCGGGGAGGATCCTGATCGAGGAGCTGAGGGACCGATTTCCCTACCTGAGTGAA
AGCTACTTAATCACCACCGATGCCGCCGGCTCCATCGCCACAGCTACACCGGATGGTGGG
ATTGTGCTCATATCTGGAACAGGCTCCAACTGCAGGCTCATCAACCCTGATGGCTCCGAG
AGTGGCTGCGGCGGCTGGGGCCATATGATGGGTGATGAGGGTTCAGCCTACTGGATCGCA
CACCAAGCAGTGAAAATAGTGTTTGACTCCATTGACAACCTAGAGGCGGCTCCTCATGAT
ATCGGCTACGTCAAACAGGCCATGTTCCACTATTTCCAGGTGCCAGATCGGCTAGGGATA
CTCACTCACCTGTATAGGGACTTTGATAAATGCAGGTTTGCTGGGTTTTGCCGGAAAATT
GCAGAAGGTGCTCAGCAGGGAGACCCCCTTTCCCGCTATATCTTCAGGAAGGCTGGGGAG
ATGCTGGGCAGACACATCGTAGCAGTGTTGCCCGAGATTGACCCGGTCTTGTTCCAGGGC
AAGATTGGACTCCCCATCCTGTGCGTGGGCTCTGTGTGGAAGAGCTGGGAGCTGCTGAAG
GAAGGTTTTCTTTTGGCGCTGACCCAGGGCAGAGAGATCCAGGCTCAGAACTTCTTCTCC
AGCTTCACCCTGATGAAGCTGAGGCACTCCTCCGCTCTGGGTGGGGCCAGCCTAGGGGCC
AGGCACATCGGGCACCTCCTCCCCATGGACTATAGCGCCAATGCCATTGCCTTCTATTCC
TACACCTTTTCCTAG

1. Hinderlich S, Berger M, Schwarzkopf M, Effertz K, Reutter W: Molecular cloning and characterization of murine and human N-acetylglucosamine kinase. Eur J Biochem. 2000 Jun;267(11):3301-8. [PubMed ]
2. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed ]
3. Maguire PB, Wynne KJ, Harney DF, O'Donoghue NM, Stephens G, Fitzgerald DJ: Identification of the phosphotyrosine proteome from thrombin activated platelets. Proteomics. 2002 Jun;2(6):642-8. [PubMed ]

1. AMCase
2. TSA1902

MTKLILLTGLVLILNLQLGSAYQLTCYFTNWAQYRPGLGRFMPDNIDPCLCTHLIYAFAG
RQNNEITTIEWNDVTLYQAFNGLKNKNSQLKTLLAIGGWNFGTAPFTAMVSTPENRQTFI
TSVIKFLRQYEFDGLDFDWEYPGSRGSPPQDKHLFTVLVQEMREAFEQEAKQINKPRLMV
TAAVAAGISNIQSGYEIPQLSQYLDYIHVMTYDLHGSWEGYTGENSPLYKYPTDTGSNAY
LNVDYVMNYWKDNGAPAEKLIVGFPTYGHNFILSNPSNTGIGAPTSGAGPAGPYAKESGI
WAYYEICTFLKNGATQGWDAPQEVPYAYQGNVWVGYDNIKSFDIKAQWLKHNKFGGAMVW
AIDLDDFTGTFCNQGKFPLISTLKKALGLQSASCTAPAQPIEPITAAPSGSGNGSGSSSS
GGSSGGSGFCAVRANGLYPVANNRNAFWHCVNGVTYQQNCQAGLVFDTSCDCCNWA

• Aminosugars metabolism (map00530 )

• Random hydrolysis of N-acetyl-beta-D-glucosaminide 1,4-beta-linkages in chitin and chitodextrins

• CBM_14 (PF01607 )
• Glyco_hydro_18 (PF00704 )

• 1-21

ATGGTTTCTACTCCTGAGAACCGCCAGACTTTCATCACCTCAGTCATCAAATTCCTGCGC
CAGTATGAGTTTGACGGGCTGGACTTTGACTGGGAGTACCCTGGCTCTCGTGGGAGCCCT
CCTCAGGACAAGCATCTCTTCACTGTCCTGGTGCAGGAAATGCGTGAAGCTTTTGAGCAG
GAGGCCAAGCAGATCAACAAGCCCAGGCTGATGGTCACTGCTGCAGTAGCTGCTGGCATC
TCCAATATCCAGTCTGGCTATGAGATCCCCCAACTGTCACAGTACCTGGACTACATCCAT
GTCATGACCTACGACCTCCATGGCTCCTGGGAGGGCTACACTGGAGAGAACAGCCCCCTC
TACAAATACCCGACTGACACCGGCAGCAACGCCTACCTCAATGTGGATTATGTCATGAAC
TACTGGAAGGACAATGGAGCACCAGCTGAGAAGCTCATCGTTGGATTCCCTACCTATGGA
CACAACTTCATCCTGAGCAACCCCTCCAACACTGGAATTGGTGCCCCCACCTCTGGTGCT
GGTCCTGCTGGGCCCTATGCCAAGGAGTCTGGGATCTGGGCTTACTACGAGATCTGTACC
TTCCTGAAAAATGGAGCCACTCAGGGATGGGATGCCCCTCAGGAAGTGCCTTATGCCTAT
CAGGGCAATGTGTGGGTTGGCTATGACAACGTCAAGAGCTTCGATATTAAGGCTCAATGG
CTTAAGCACAACAAATTTGGAGGCGCCATGGTCTGGGCCATTGATCTGGATGACTTCACT
GGCACTTTCTGCAACCAGGGCAAGTTTCCCCTAATCTCCACCCTGAAGAAGGCCCTTGGC
CTGCAGAGTGCAAGTTGCACGGCTCCAGCTCAGCCCATTGAGCCAATAACTGCTGCTCCC
AGTGGCAGCGGGAACGGGAGCGGGAGTAGCAGCTCTGGAGGCAGCTCGGGAGGCAGTGGA
TTCTGTGCTGGCAGAGCCAACGGCCTCTACCCCGTGGCAAATAACAGAAATGCCTTCTGG
CACTGCGTGAATGGAGTCACGTACCAGCAGAACTGCCAGGCCGGGCTTGTCTTCGACACC
AGCTGTGATTGCTGCAACTGGGCATAA

1. Saito A, Ozaki K, Fujiwara T, Nakamura Y, Tanigami A: Isolation and mapping of a human lung-specific gene, TSA1902, encoding a novel chitinase family member. Gene. 1999 Nov 1;239(2):325-31. [PubMed ]

1. Phosphodiester alpha-GlcNAcase
2. Mannose 6- phosphate-uncovering enzyme

MATSTGRWLLLRLALFGFLWEASGGLDSGASRDDDLLLPYPRARARLPRDCTRVRAGNRE
HESWPPPPATPGAGGLAVRTFVSHFRDRAVAGHLTRAVEPLRTFSVLEPGGPGGCAARRR
ATVEETARAADCRVAQNGGFFRMNSGECLGNVVSDERRVSSSGGLQNAQFGIRRDGTLVT
GYLSEEEVLDTENPFVQLLSGVVWLIRNGSIYINESQATECDETQETGSFSKFVNVISAR
TAIGHDRKGQLVLFHADGHTEQRGINLWEMAEFLLKQDVVNAINLDGGGSATFVLNGTLA
SYPSDHCQDNMWRCPRQVSTVVCVHEPRCQPPDCHGHGTCVDGHCQCTGHFWRGPGCDEL
DCGPSNCSQHGLCTETGCRCDAGWTGSNCSEECPLGWHGPGCQRRCKCEHHCPCDPKTGN
CSVSRVKQCLQPPEATLRAGELSFFTRTAWLALTLALAFLLLISIAANLSLLLSRAERNR
RLHGDYAYHPLQEMNGEPLAAEKEQPGGAHNPFKD

• glycoprotein N-acetyl-D-glucosaminyl-phospho-D-mannose + H2O = N-acetyl-D-glucosamine + glycoprotein phospho-D-mannose

• EGF (PF00008 )
• EGF_2 (PF07974 )

• 1-24

• 449-469

ATGGCGACCTCCACGGGTCGCTGGCTTCTCCTCCGGCTTGCACTATTCGGCTTCCTCTGG
GAAGCGTCCGGCGGCCTCGACTCGGGGGCCTCCCGCGACGACGACTTGCTACTGCCCTAT
CCACGCGCGCGCGCGCGCCTCCCCCGGGACTGCACACGGGTGCGCGCCGGCAACCGCGAG
CACGAGAGTTGGCCTCCGCCTCCCGCGACTCCCGGCGCCGGCGGTCTGGCCGTGCGCACC
TTCGTGTCGCACTTCAGGGACCGCGCGGTGGCCGGCCACCTGACGCGGGCCGTTGAGCCC
CTGCGCACCTTCTCGGTGCTGGAGCCCGGTGGACCCGGCGGCTGCGCGGCGAGACGACGC
GCCACCGTGGAGGAGACGGCGCGGGCGGCCGACTGCCGTGTCGCCCAGAACGGCGGCTTC
TTCCGCATGAACTCGGGCGAGTGCCTGGGGAACGTGGTGAGCGACGAGCGGCGGGTGAGC
AGCTCCGGGGGGCTGCAGAACGCGCAGTTCGGGATCCGCCGCGACGGGACCCTGGTCACC
GGGTACCTGTCTGAGGAGGAGGTGCTGGACACTGAGAACCCATTTGTGCAGCTGCTGAGT
GGGGTCGTGTGGCTGATTCGTAATGGAAGCATCTACATCAACGAGAGCCAAGCCACAGAG
TGTGACGAGACACAGGAGACAGGTTCCTTTAGCAAATTTGTGAATGTGATATCAGCCAGG
ACGGCCATTGGCCACGACCGGAAAGGGCAGCTGGTGCTCTTTCATGCAGACGGCCATACG
GAGCAGCGTGGCATCAACCTGTGGGAAATGGCGGAGTTCCTGCTGAAACAGGACGTGGTC
AACGCCATCAACCTGGATGGGGGTGGCTCTGCCACCTTTGTGCTCAACGGGACCTTGGCC
AGTTACCCGTCAGATCACTGCCAGGACAACATGTGGCGCTGTCCCCGCCAAGTGTCCACC
GTGGTGTGTGTGCACGAACCCCGCTGCCAGCCGCCTGACTGCCACGGCCACGGGACCTGC
GTGGACGGGCACTGCCAATGCACCGGGCACTTCTGGCGGGGTCCCGGCTGTGATGAGCTG
GACTGTGGCCCCTCTAACTGCAGCCAGCACGGACTGTGCACGGAGACCGGCTGCCGCTGT
GATGCCGGATGGACCGGGTCCAACTGCAGTGAAGAGTGTCCCCTTGGCTGGCATGGGCCG
GGCTGCCAGAGGCGTTGTAAGTGTGAGCACCATTGTCCCTGTGACCCCAAGACTGGCAAC
TGCAGCGTCTCCAGAGTAAAGCAGTGTCTCCAGCCACCTGAAGCCACCCTGAGGGCGGGA
GAACTCTCCTTTTTCACCAGGACCGCCTGGCTAGCCCTCACCCTGGCGCTGGCCTTCCTC
CTGCTGATCAGCATTGCAGCAAACCTGTCCTTGCTCCTGTCCAGAGCAGAGAGGAACCGG
CGCCTGCATGGGGACTATGCATACCACCCGCTGCAGGAGATGAACGGGGAGCCTCTGGCC
GCAGAGAAGGAGCAGCCAGGGGGCGCCCACAACCCCTTCAAGGACTGA

1. Kornfeld R, Bao M, Brewer K, Noll C, Canfield W: Molecular cloning and functional expression of two splice forms of human N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase. J Biol Chem. 1999 Nov 12;274(46):32778-85. [PubMed ]

1. Chitinase-1

MVRSVAWAGFMVLLMIPWGSAAKLVCYFTNWAQYRQGEARFLPKDLDPSLCTHLIYAFAG
MTNHQLSTTEWNDETLYQEFNGLKKMNPKLKTLLAIGGWNFGTQKFTDMVATANNRQTFV
NSAIRFLRKYSFDGLDLDWEYPGSQGSPAVDKERFTTLVQDLANAFQQEAQTSGKERLLL
SAAVPAGQTYVDAGYEVDKIAQNLDFVNLMAYDFHGSWEKVTGHNSPLYKRQEESGAAAS
LNVDAAVQQWLQKGTPASKLILGMPTYGRSFTLASSSDTRVGAPATGSGTPGPFTKEGGM
LAYYEVCSWKGATKQRIQDQKVPYIFRDNQWVGFDDVESFKTKVSYLKQKGLGGAMVWAL
DLDDFAGFSCNQGRYPLIQTLRQELSLPYLPSGTPELEVPKPGQPSEPEHGPSPGQDTFC
QGKADGLYPNPRERSSFYSCAAGRLFQQSCPTGLVFSNSCKCCTWN

• Aminosugars metabolism (map00530 )

• Random hydrolysis of N-acetyl-beta-D-glucosaminide 1,4-beta-linkages in chitin and chitodextrins

• CBM_14 (PF01607 )
• Glyco_hydro_18 (PF00704 )

• 1-21

ATGGTGCGGTCTGTGGCCTGGGCAGGTTTCATGGTCCTGCTGATGATCCCATGGGGCTCT
GCTGCAAAACTGGTCTGCTACTTCACCAACTGGGCCCAGTACAGACAGGGGGAGGCTCGC
TTCCTGCCCAAGGACTTGGACCCCAGCCTTTGCACCCACCTCATCTACGCCTTCGCTGGC
ATGACCAACCACCAGCTGAGCACCACTGAGTGGAATGACGAGACTCTCTACCAGGAGTTC
AATGGCCTGAAGAAGATGAATCCCAAGCTGAAGACCCTGTTAGCCATCGGAGGCTGGAAT
TTCGGCACTCAGAAGTTCACAGATATGGTAGCCACGGCCAACAACCGTCAGACCTTTGTC
AACTCGGCCATCAGGTTTCTGCGCAAATACAGCTTTGACGGCCTTGACCTTGACTGGGAG
TACCCAGGAAGCCAGGGGAGCCCTGCCGTAGACAAGGAGCGCTTCACAACCCTGGTACAG
GACTTGGCCAATGCCTTCCAGCAGGAAGCCCAGACCTCAGGGAAGGAACGCCTTCTTCTG
AGTGCAGCGGTTCCAGCTGGGCAGACCTATGTGGATGCTGGATACGAGGTGGACAAAATC
GCCCAGAACCTGGATTTTGTCAACCTTATGGCCTACGACTTCCATGGCTCTTGGGAGAAG
GTCACGGGACATAACAGCCCCCTCTACAAGAGGCAAGAAGAGAGTGGTGCAGCAGCCAGC
CTCAACGTGGATGCTGCTGTGCAACAGTGGCTGCAGAAGGGGACCCCTGCCAGCAAGCTG
ATCCTTGGCATGCCTACCTACGGACGCTCCTTCACACTGGCCTCCTCATCAGACACCAGA
GTGGGGGCCCCAGCCACAGGGTCTGGCACTCCAGGCCCCTTCACCAAGGAAGGAGGGATG
CTGGCCTACTATGAAGTCTGCTCCTGGAAGGGGGCCACCAAACAGAGAATCCAGGATCAG
AAGGTGCCCTACATCTTCCGGGACAACCAGTGGGTGGGCTTTGATGATGTGGAGAGCTTC
AAAACCAAGGTCAGCTATCTGAAGCAGAAGGGACTGGGCGGGGCCATGGTCTGGGCACTG
GACTTAGATGACTTTGCCGGCTTCTCCTGCAACCAGGGCCGATACCCCCTCATCCAGACG
CTACGGCAGGAACTGAGTCTTCCATACTTGCCTTCAGGCACCCCAGAGCTTGAAGTTCCA
AAACCAGGTCAGCCCTCTGAACCTGAGCATGGCCCCAGCCCTGGACAAGACACGTTCTGC
CAGGGCAAAGCTGATGGGCTCTATCCCAATCCTCGGGAACGGTCCAGCTTCTACAGCTGT
GCAGCGGGGCGGCTGTTCCAGCAAAGCTGCCCGACAGGCCTGGTGTTCAGCAACTCCTGC
AAATGCTGCACCTGGAATTGA

1. Boot RG, Renkema GH, Strijland A, van Zonneveld AJ, Aerts JM: Cloning of a cDNA encoding chitotriosidase, a human chitinase produced by macrophages. J Biol Chem. 1995 Nov 3;270(44):26252-6. [PubMed ]
2. Renkema GH, Boot RG, Muijsers AO, Donker-Koopman WE, Aerts JM: Purification and characterization of human chitotriosidase, a novel member of the chitinase family of proteins. J Biol Chem. 1995 Feb 3;270(5):2198-202. [PubMed ]
3. Boot RG, Renkema GH, Verhoek M, Strijland A, Bliek J, de Meulemeester TM, Mannens MM, Aerts JM: The human chitotriosidase gene. Nature of inherited enzyme deficiency. J Biol Chem. 1998 Oct 2;273(40):25680-5. [PubMed ]
4. Fusetti F, von Moeller H, Houston D, Rozeboom HJ, Dijkstra BW, Boot RG, Aerts JM, van Aalten DM: Structure of human chitotriosidase. Implications for specific inhibitor design and function of mammalian chitinase-like lectins. J Biol Chem. 2002 Jul 12;277(28):25537-44. Epub 2002 Apr 17. [PubMed ]

1. Beta-1,4-GalTase 3
2. Beta4Gal-T3
3. b4Gal-T3
4. UDP-galactose:beta-N-acetylglucosamine beta- 1,4-galactosyltransferase 3
5. UDP-Gal:beta-GlcNAc beta-1,4- galactosyltransferase 3[Includes: N-acetyllactosamine synthase
6. Nal synthetase
7. Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase

MLRRLLERPCTLALLVGSQLAVMMYLSLGGFRSLSALFGRDQGPTFDYSHPRDVYSNLSH
LPGAPGGPPAPQGLPYCPERSPLLVGPVSVSFSPVPSLAEIVERNPRVEPGGRYRPAGCE
PRSRTAIIVPHRAREHHLRLLLYHLHPFLQRQQLAYGIYVIHQAGNGTFNRAKLLNVGVR
EALRDEEWDCLFLHDVDLLPENDHNLYVCDPRGPRHVAVAMNKFGYSLPYPQYFGGVSAL
TPDQYLKMNGFPNEYWGWGGEDDDIATRVRLAGMKISRPPTSVGHYKMVKHRGDKGNEEN
PHRFDLLVRTQNSWTQDGMNSLTYQLLARELGPLYTNITADIGTDPRGPRAPSGPRYPPG
SSQAFRQEMLQRRPPARPGPLSTANHTALRGSH

• Keratan sulfate biosynthesis (map00533 )
• N-Glycan biosynthesis (map00510 )

• UDP-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine

• Galactosyl_T_2 (PF02709 )

• 1-36

ATGTTGCGGAGGCTGCTGGAGCGGCCTTGCACGCTGGCCCTGCTTGTGGGCTCCCAGCTG
GCTGTCATGATGTACCTGTCACTGGGGGGCTTCCGAAGTCTCAGTGCCCTATTTGGCCGA
GATCAGGGACCGACATTTGACTATTCTCACCCTCGTGATGTCTACAGTAACCTCAGTCAC
CTGCCTGGGGCCCCAGGGGGTCCTCCAGCTCCTCAAGGTCTGCCCTACTGTCCAGAACGA
TCTCCTCTCTTAGTGGGTCCTGTGTCGGTGTCCTTTAGCCCAGTGCCATCACTGGCAGAG
ATTGTGGAGCGGAATCCCCGGGTAGAACCAGGGGGCCGGTACCGCCCTGCAGGTTGTGAG
CCCCGCTCCCGAACAGCCATCATTGTGCCTCATCGTGCCCGGGAGCACCACCTGCGCCTG
CTGCTCTACCACCTGCACCCCTTCTTGCAGCGCCAGCAGCTTGCTTATGGCATCTATGTC
ATCCACCAGGCTGGAAATGGAACATTTAACAGGGCAAAACTGTTGAACGTTGGGGTGCGA
GAGGCCCTGCGTGATGAAGAGTGGGACTGCCTGTTCTTGCACGATGTGGACCTCTTGCCA
GAAAATGACCACAATCTGTATGTGTGTGACCCCCGGGGACCCCGCCATGTTGCCGTTGCT
ATGAACAAGTTTGGATACAGCCTCCCGTACCCCCAGTACTTCGGAGGAGTCTCAGCACTT
ACTCCTGACCAGTACCTGAAGATGAATGGCTTCCCCAATGAATACTGGGGCTGGGGTGGT
GAGGATGACGACATTGCTACCAGGGTGCGCCTGGCTGGGATGAAGATCTCTCGGCCCCCC
ACATCTGTAGGACACTATAAGATGGTGAAGCACCGAGGAGATAAGGGCAATGAGGAAAAT
CCCCACAGATTTGACCTCCTGGTCCGTACCCAGAATTCCTGGACGCAAGATGGGATGAAC
TCACTGACATACCAGTTGCTGGCTCGAGAGCTGGGGCCTCTTTATACCAACATCACAGCA
GACATTGGGACTGACCCTCGGGGTCCTCGGGCTCCTTCTGGGCCACGTTACCCACCTGGT
TCCTCCCAAGCCTTCCGTCAAGAGATGCTGCAACGCCGGCCCCCAGCCAGGCCTGGGCCT
CTATCTACTGCCAACCACACAGCCCTCCGAGGTTCACACTGA

1. Almeida R, Amado M, David L, Levery SB, Holmes EH, Merkx G, van Kessel AG, Rygaard E, Hassan H, Bennett E, Clausen H: A family of human beta4-galactosyltransferases. Cloning and expression of two novel UDP-galactose:beta-n-acetylglucosamine beta1, 4-galactosyltransferases, beta4Gal-T2 and beta4Gal-T3. J Biol Chem. 1997 Dec 19;272(51):31979-91. [PubMed ]
2. Lo NW, Shaper JH, Pevsner J, Shaper NL: The expanding beta 4-galactosyltransferase gene family: messages from the databanks. Glycobiology. 1998 May;8(5):517-26. [PubMed ]
3. Guo S, Sato T, Shirane K, Furukawa K: Galactosylation of N-linked oligosaccharides by human beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed in Sf-9 cells. Glycobiology. 2001 Oct;11(10):813-20. [PubMed ]
4. Amado M, Almeida R, Schwientek T, Clausen H: Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions. Biochim Biophys Acta. 1999 Dec 6;1473(1):35-53. [PubMed ]

1. Beta-1,4-GalTase 4
2. Beta4Gal-T4
3. b4Gal-T4
4. UDP-galactose:beta-N-acetylglucosamine beta- 1,4-galactosyltransferase 4
5. UDP-Gal:beta-GlcNAc beta-1,4- galactosyltransferase 4[Includes: N-acetyllactosamine synthase
6. Nal synthetase
7. Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase

MGFNLTFHLSYKFRLLLLLTLCLTVVGWATSNYFVGAIQEIPKAKEFMANFHKTLILGKG
KTLTNEASTKKVELDNCPSVSPYLRGQSKLIFKPDLTLEEVQAENPKVSRGRYRPQECKA
LQRVAILVPHRNREKHLMYLLEHLHPFLQRQQLDYGIYVIHQAEGKKFNRAKLLNVGYLE
ALKEENWDCFIFHDVDLVPENDFNLYKCEEHPKHLVVGRNSTGYRLRYSGYFGGVTALSR
EQFFKVNGFSNNYWGWGGEDDDLRLRVELQRMKISRPLPEVGKYTMVFHTRDKGNEVNAE
RMKLLHQVSRVWRTDGLSSCSYKLVSVEHNPLYINITVDFWFGA

• UDP-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine

• Galactosyl_T_2 (PF02709 )

• 1-29

ATGGGCTTCAACCTGACTTTCCACCTTTCCTACAAATTCCGATTACTGTTGCTGTTGACT
TTGTGCCTGACAGTGGTTGGGTGGGCCACCAGTAACTACTTCGTGGGTGCCATTCAAGAG
ATTCCTAAAGCAAAGGAGTTCATGGCTAATTTCCATAAGACCCTCATTTTGGGGAAGGGA
AAAACTCTGACTAATGAAGCATCCACGAAGAAGGTAGAACTTGACAACTGCCCTTCTGTG
TCTCCTTACCTCAGAGGCCAGAGCAAGCTCATTTTCAAACCAGATCTCACTTTGGAAGAG
GTACAGGCAGAAAATCCCAAAGTGTCCAGAGGCCGGTATCGCCCTCAGGAATGTAAAGCT
TTACAGAGGGTCGCCATCCTCGTTCCCCACCGGAACAGAGAGAAACACCTGATGTACCTG
CTGGAACATCTGCATCCCTTCCTGCAGAGGCAGCAGCTGGATTATGGCATCTACGTCATC
CACCAGGCTGAAGGTAAAAAGTTTAATCGAGCCAAACTCTTGAATGTGGGCTATCTAGAA
GCCCTCAAGGAAGAAAATTGGGACTGCTTTATATTCCACGATGTGGACCTGGTACCCGAG
AATGACTTTAACCTTTACAAGTGTGAGGAGCATCCCAAGCATCTGGTGGTTGGCAGGAAC
AGCACTGGGTACAGGTTACGTTACAGTGGATATTTTGGGGGTGTTACTGCCCTAAGCAGA
GAGCAGTTTTTCAAGGTGAATGGATTCTCTAACAACTACTGGGGATGGGGAGGCGAAGAC
GATGACCTCAGACTCAGGGTTGAGCTCCAAAGAATGAAAATTTCCCGGCCCCTGCCTGAA
GTGGGTAAATATACAATGGTCTTCCACACTAGAGACAAAGGCAATGAGGTGAACGCAGAA
CGGATGAAGCTCTTACACCAAGTGTCACGAGTCTGGAGAACAGATGGGTTGAGTAGTTGT
TCTTATAAATTAGTATCTGTGGAACACAATCCTTTATATATCAACATCACAGTGGATTTC
TGGTTTGGTGCATGA

1. Lo NW, Shaper JH, Pevsner J, Shaper NL: The expanding beta 4-galactosyltransferase gene family: messages from the databanks. Glycobiology. 1998 May;8(5):517-26. [PubMed ]
2. Schwientek T, Almeida R, Levery SB, Holmes EH, Bennett E, Clausen H: Cloning of a novel member of the UDP-galactose:beta-N-acetylglucosamine beta1,4-galactosyltransferase family, beta4Gal-T4, involved in glycosphingolipid biosynthesis. J Biol Chem. 1998 Nov 6;273(45):29331-40. [PubMed ]
3. Guo S, Sato T, Shirane K, Furukawa K: Galactosylation of N-linked oligosaccharides by human beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed in Sf-9 cells. Glycobiology. 2001 Oct;11(10):813-20. [PubMed ]
4. 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 ]
5. Amado M, Almeida R, Schwientek T, Clausen H: Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions. Biochim Biophys Acta. 1999 Dec 6;1473(1):35-53. [PubMed ]

1. N-acetyl-alpha- glucosaminidase
2. NAG[Contains: Alpha-N-acetylglucosaminidase 82 kDa form
3. Alpha-N-acetylglucosaminidase 77 kDa form]

MEAVAVAAAVGVLLLAGAGGAAGDEAREAAAVRALVARLLGPGPAADFSVSVERALAAKP
GLDTYSLGGGGAARVRVRGSTGVAAAAGLHRYLRDFCGCHVAWSGSQLRLPRPLPAVPGE
LTEATPNRYRYYQNVCTQSYSFVWWDWARWEREIDWMALNGINLALAWSGQEAIWQRVYL
ALGLTQAEINEFFTGPAFLAWGRMGNLHTWDGPLPPSWHIKQLYLQHRVLDQMRSFGMTP
VLPAFAGHVPEAVTRVFPQVNVTKMGSWGHFNCSYSCSFLLAPEDPIFPIIGSLFLRELI
KEFGTDHIYGADTFNEMQPPSSEPSYLAAATTAVYEAMTAVDTEAVWLLQGWLFQHQPQF
WGPAQIRAVLGAVPRGRLLVLDLFAESQPVYTRTASFQGQPFIWCMLHNFGGNHGLFGAL
EAVNGGPEAARLFPNSTMVGTGMAPEGISQNEVVYSLMAELGWRKDPVPDLAAWVTSFAA
RRYGVSHPDAGAAWRLLLRSVYNCSGEACRGHNRSPLVRRPSLQMNTSIWYNRSDVFEAW
RLLLTSAPSLATSPAFRYDLLDLTRQAVQELVSLYYEEARSAYLSKELASLLRAGGVLAY
ELLPALDEVLASDSRFLLGSWLEQARAAAVSEAEADFYEQNSRYQLTLWGPEGNILDYAN
KQLAGLVANYYTPRWRLFLEALVDSVAQGIPFQQHQFDKNVFQLEQAFVLSKQRYPSQPR
GDTVDLAKKIFLKYYPGWVAGSW

• Glycosaminoglycan degradation (map00531 )

• Hydrolysis of terminal non-reducing N-acetyl-D-glucosamine residues in N-acetyl-alpha-D-glucosaminides

• NAGLU (PF05089 )

• 1-23

ATGGAGGCGGTGGCGGTGGCCGCGGCGGTGGGGGTCCTTCTCCTGGCCGGGGCCGGGGGC
GCGGCAGGCGACGAGGCCCGGGAGGCGGCGGCCGTGCGGGCGCTCGTGGCCCGGCTGCTG
GGGCCAGGCCCCGCGGCCGACTTCTCCGTGTCGGTGGAGCGCGCTCTGGCTGCCAAGCCG
GGCTTGGACACCTACAGCCTGGGCGGCGGCGGCGCGGCGCGCGTGCGGGTGCGCGGCTCC
ACGGGCGTGGCGGCCGCCGCGGGGCTGCACCGCTACCTGCGCGACTTCTGTGGCTGCCAC
GTGGCCTGGTCCGGCTCTCAGCTGCGCCTGCCGCGGCCACTGCCAGCCGTGCCGGGGGAG
CTGACCGAGGCCACGCCCAACAGGTACCGCTATTACCAGAATGTGTGCACGCAAAGCTAC
TCCTTCGTGTGGTGGGACTGGGCCCGCTGGGAGCGAGAGATAGACTGGATGGCGCTGAAT
GGCATCAACCTGGCACTGGCCTGGAGCGGCCAGGAGGCCATCTGGCAGCGGGTGTACCTG
GCCTTGGGCCTGACCCAGGCAGAGATCAATGAGTTCTTTACTGGTCCTGCCTTCCTGGCC
TGGGGGCGAATGGGCAACCTGCACACCTGGGATGGCCCCCTGCCCCCCTCCTGGCACATC
AAGCAGCTTTACCTGCAGCACCGGGTCCTGGACCAGATGCGCTCCTTCGGCATGACCCCA
GTGCTGCCTGCATTCGCGGGGCATGTTCCCGAGGCTGTCACCAGGGTGTTCCCTCAGGTC
AATGTCACGAAGATGGGCAGTTGGGGCCACTTTAACTGTTCCTACTCCTGCTCCTTCCTT
CTGGCTCCGGAAGACCCCATATTCCCCATCATCGGGAGCCTCTTCCTGCGAGAGCTGATC
AAAGAGTTTGGCACAGACCACATCTATGGGGCCGACACTTTCAATGAGATGCAGCCACCT
TCCTCAGAGCCCTCCTACCTTGCCGCAGCCACCACTGCCGTCTATGAGGCCATGACTGCA
GTGGATACTGAGGCTGTGTGGCTGCTCCAAGGCTGGCTCTTCCAGCACCAGCCGCAGTTC
TGGGGGCCCGCCCAGATCAGGGCTGTGCTGGGAGCTGTGCCCCGTGGCCGCCTCCTGGTT
CTGGACCTGTTTGCTGAGAGCCAGCCTGTGTATACCCGCACTGCCTCCTTCCAGGGCCAG
CCCTTCATCTGGTGCATGCTGCACAACTTTGGGGGAAACCATGGTCTTTTTGGAGCCCTA
GAGGCTGTGAACGGAGGCCCAGAAGCTGCCCGCCTCTTCCCCAACTCCACCATGGTAGGC
ACGGGCATGGCCCCCGAGGGCATCAGCCAGAACGAAGTGGTCTATTCCCTCATGGCTGAG
CTGGGCTGGCGAAAGGACCCAGTGCCAGATTTGGCAGCCTGGGTGACCAGCTTTGCCGCC
CGGCGGTATGGGGTCTCCCACCCGGACGCAGGGGCAGCGTGGAGGCTACTGCTCCGGAGT
GTGTACAACTGCTCCGGGGAGGCCTGCAGGGGCCACAATCGTAGCCCGCTGGTCAGGCGG
CCGTCCCTACAGATGAATACCAGCATCTGGTACAACCGATCTGATGTGTTTGAGGCCTGG
CGGCTGCTGCTCACATCTGCTCCCTCCCTGGCCACCAGCCCCGCCTTCCGCTACGACCTG
CTGGACCTCACTCGGCAGGCAGTGCAGGAGCTGGTCAGCTTGTACTATGAGGAGGCAAGA
AGCGCCTACCTGAGCAAGGAGCTGGCCTCCCTGTTGAGGGCTGGAGGCGTCCTGGCCTAT
GAGCTGCTGCCGGCACTGGACGAGGTGCTGGCTAGTGACAGCCGCTTCTTGCTGGGCAGC
TGGCTAGAGCAGGCCCGAGCAGCGGCAGTCAGTGAGGCCGAGGCCGATTTCTACGAGCAG
AACAGCCGCTACCAGCTGACCTTGTGGGGGCCAGAAGGCAACATCCTGGACTATGCCAAC
AAGCAGCTGGCGGGGTTGGTGGCCAACTACTACACCCCTCGCTGGCGGCTTTTCCTGGAG
GCGCTGGTTGACAGTGTGGCCCAGGGCATCCCTTTCCAACAGCACCAGTTTGACAAAAAT
GTCTTCCAACTGGAGCAGGCCTTCGTTCTCAGCAAGCAGAGGTACCCCAGCCAGCCGCGA
GGAGACACTGTGGACCTGGCCAAGAAGATCTTCCTCAAATATTACCCCGGCTGGGTGGCC
GGCTCTTGGTGA

1. Zhao HG, Li HH, Bach G, Schmidtchen A, Neufeld EF: The molecular basis of Sanfilippo syndrome type B. Proc Natl Acad Sci U S A. 1996 Jun 11;93(12):6101-5. [PubMed ]
2. Weber B, Blanch L, Clements PR, Scott HS, Hopwood JJ: Cloning and expression of the gene involved in Sanfilippo B syndrome (mucopolysaccharidosis III B). Hum Mol Genet. 1996 Jun;5(6):771-7. [PubMed ]
3. Schmidtchen A, Greenberg D, Zhao HG, Li HH, Huang Y, Tieu P, Zhao HZ, Cheng S, Zhao Z, Whitley CB, Di Natale P, Neufeld EF: NAGLU mutations underlying Sanfilippo syndrome type B. Am J Hum Genet. 1998 Jan;62(1):64-9. [PubMed ]
4. Bunge S, Knigge A, Steglich C, Kleijer WJ, van Diggelen OP, Beck M, Gal A: Mucopolysaccharidosis type IIIB (Sanfilippo B): identification of 18 novel alpha-N-acetylglucosaminidase gene mutations. J Med Genet. 1999 Jan;36(1):28-31. [PubMed ]

1. 1,4-beta-N-acetylmuramidase C

MKALIVLGLVLLSVTVQGKVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRA
TNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRD
PQGIRAWVAWRNRCQNRDVRQYVQGCGV

• Hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins

• Lys (PF00062 )

• 1-18

ATGAAGGCTCTCATTGTTCTGGGGCTTGTCCTCCTTTCTGTTACGGTCCAGGGCAAGGTC
TTTGAAAGGTGTGAGTTGGCCAGAACTCTGAAAAGATTGGGAATGGATGGCTACAGGGGA
ATCAGCCTAGCAAACTGGATGTGTTTGGCCAAATGGGAGAGTGGTTACAACACACGAGCT
ACAAACTACAATGCTGGAGACAGAAGCACTGATTATGGGATATTTCAGATCAATAGCCGC
TACTGGTGTAATGATGGCAAAACCCCAGGAGCAGTTAATGCCTGTCATTTATCCTGCAGT
GCTTTGCTGCAAGATAACATCGCTGATGCTGTAGCTTGTGCAAAGAGGGTTGTCCGTGAT
CCACAAGGCATTAGAGCATGGGTGGCATGGAGAAATCGTTGTCAAAACAGAGATGTCCGT
CAGTATGTTCAAGGTTGTGGAGTGTAA

1. Peters CW, Kruse U, Pollwein R, Grzeschik KH, Sippel AE: The human lysozyme gene. Sequence organization and chromosomal localization. Eur J Biochem. 1989 Jul 1;182(3):507-16. [PubMed ]
2. Castanon MJ, Spevak W, Adolf GR, Chlebowicz-Sledziewska E, Sledziewski A: Cloning of human lysozyme gene and expression in the yeast Saccharomyces cerevisiae. Gene. 1988 Jun 30;66(2):223-34. [PubMed ]
3. Chung LP, Keshav S, Gordon S: Cloning the human lysozyme cDNA: inverted Alu repeat in the mRNA and in situ hybridization for macrophages and Paneth cells. Proc Natl Acad Sci U S A. 1988 Sep;85(17):6227-31. [PubMed ]
4. Yoshimura K, Toibana A, Nakahama K: Human lysozyme: sequencing of a cDNA, and expression and secretion by Saccharomyces cerevisiae. Biochem Biophys Res Commun. 1988 Jan 29;150(2):794-801. [PubMed ]
5. Canfield RE, Kammerman S, Sobel JH, Morgan FJ: Primary structure of lysozymes from man and goose. Nat New Biol. 1971 Jul 7;232(27):16-7. [PubMed ]
6. Jolles J, Jolles P: Human milk lysozyme: unpublished data concerning the establishment of the complete primary structure; comparison with lysozymes of various origins. Helv Chim Acta. 1971;54(8):2668-75. [PubMed ]
7. Kanaya E, Ishihara K, Tsunasawa S, Nokihara K, Kikuchi M: Indication of possible post-translational formation of disulphide bonds in the beta-sheet domain of human lysozyme. Biochem J. 1993 Jun 1;292 ( Pt 2):469-76. [PubMed ]
8. Artymiuk PJ, Blake CC: Refinement of human lysozyme at 1.5 A resolution analysis of non-bonded and hydrogen-bond interactions. J Mol Biol. 1981 Nov 15;152(4):737-62. [PubMed ]
9. Blake CC, Pulford WC, Artymiuk PJ: X-ray studies of water in crystals of lysozyme. J Mol Biol. 1983 Jul 5;167(3):693-723. [PubMed ]
10. Inaka K, Taniyama Y, Kikuchi M, Morikawa K, Matsushima M: The crystal structure of a mutant human lysozyme C77/95A with increased secretion efficiency in yeast. J Biol Chem. 1991 Jul 5;266(19):12599-603. [PubMed ]
11. Steinrauf LK: Structures of monoclinic lysozyme iodide at 1.6 A and of triclinic lysozyme nitrate at 1.1 A. Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):767-80. [PubMed ]
12. Redfield C, Dobson CM: 1H NMR studies of human lysozyme: spectral assignment and comparison with hen lysozyme. Biochemistry. 1990 Aug 7;29(31):7201-14. [PubMed ]
13. Ohkubo T, Taniyama Y, Kikuchi M: 1H and 15N NMR study of human lysozyme. J Biochem. 1991 Dec;110(6):1022-9. [PubMed ]
14. Pepys MB, Hawkins PN, Booth DR, Vigushin DM, Tennent GA, Soutar AK, Totty N, Nguyen O, Blake CC, Terry CJ, et al.: Human lysozyme gene mutations cause hereditary systemic amyloidosis. Nature. 1993 Apr 8;362(6420):553-7. [PubMed ]

1. POMGnT1
2. UDP-GlcNAc:alpha-D-mannoside beta-1,2-N- acetylglucosaminyltransferase I.2
3. GnT I.2

MDDWKPSPLIKPFGARKKRSWYLTWKYKLTNQRALRRFCQTGAVLFLLVTVIVNIKLILD
TRRAISEANEDPEPEQDYDEALGRLEPPRRRGSGPRRVLDVEVYSSRSKVYVAVDGTTVL
EDEAREQGRGIHVIVLNQATGHVMAKRVFDTYSPHEDEAMVLFLNMVAPGRVLICTVKDE
GSFHLKDTAKALLRSLGSQAGPALGWRDTWAFVGRKGGPVFGEKHSKSPALSSWGDPVLL
KTDVPLSSAEEAECHWADTELNRRRRRFCSKVEGYGSVCSCKDPTPIEFSPDPLPDNKVL
NVPVAVIAGNRPNYLYRMLRSLLSAQGVSPQMITVFIDGYYEEPMDVVALFGLRGIQHTP
ISIKNARVSQHYKASLTATFNLFPEAKFAVVLEEDLDIAVDFFSFLSQSIHLLEEDDSLY
CISAWNDQGYEHTAEDPALLYRVETMPGLGWVLRRSLYKEELEPKWPTPEKLWDWDMWMR
MPEQRRGRECIIPDVSRSYHFGIVGLNMNGYFHEAYFKKHKFNTVPGVQLRNVDSLKKEA
YEVEVHRLLSEAEVLDHSKNPCEDSFLPDTEGHTYVAFIRMEKDDDFTTWTQLAKCLHIW
DLDVRGNHRGLWRLFRKKNHFLVVGVPASPYSVKKPPSVTPIFLEPPPKEEGAPGAPEQT

• GNT-I (PF03071 )

• None

• 38-58

ATGGACGACTGGAAGCCCAGCCCCCTCATCAAGCCCTTTGGGGCTCGGAAGAAGCGGAGC
TGGTACCTTACCTGGAAGTATAAACTGACAAACCAGCGGGCCCTGCGGAGATTCTGTCAG
ACAGGGGCCGTGCTTTTCCTGCTGGTGACTGTCATTGTCAATATCAAGTTGATCCTGGAC
ACTCGGCGAGCCATCAGTGAAGCCAATGAAGACCCAGAGCCAGAGCAAGACTATGATGAG
GCCCTAGGCCGCCTGGAGCCCCCACGGCGCAGAGGCAGTGGTCCCCGGCGGGTCCTGGAC
GTAGAGGTGTATTCAAGTCGCAGCAAAGTATATGTGGCAGTGGATGGCACCACGGTGCTG
GAGGATGAGGCCCGGGAGCAGGGCCGGGGCATCCATGTCATTGTCCTCAACCAGGCCACG
GGCCACGTGATGGCAAAACGTGTGTTTGACACGTACTCACCTCATGAGGATGAGGCCATG
GTGCTATTCCTCAACATGGTAGCGCCCGGCCGAGTGCTCATCTGCACTGTCAAGGATGAG
GGCTCCTTCCACCTCAAGGACACAGCCAAGGCTCTGCTGAGGAGCCTGGGCAGCCAGGCT
GGCCCTGCCCTGGGCTGGAGGGACACATGGGCCTTCGTGGGACGAAAAGGAGGTCCTGTC
TTCGGGGAGAAACATTCTAAATCACCTGCCCTCTCTTCCTGGGGGGACCCAGTCCTGCTG
AAGACAGATGTGCCATTGAGCTCAGCAGAAGAGGCAGAGTGCCACTGGGCAGACACAGAG
CTGAACCGTCGCCGCCGGCGCTTCTGCAGCAAAGTTGAGGGCTATGGAAGTGTATGCAGC
TGCAAGGACCCCACACCCATCGAGTTCAGCCCTGACCCACTCCCAGACAACAAGGTCCTC
AATGTGCCTGTGGCTGTCATTGCAGGGAACCGACCCAATTACCTGTACAGGATGCTGCGC
TCTCTGCTTTCAGCCCAGGGGGTGTCTCCTCAGATGATAACAGTTTTCATTGACGGCTAC
TATGAGGAACCCATGGATGTGGTGGCACTGTTTGGTCTGAGGGGCATCCAGCATACTCCC
ATCAGCATCAAGAATGCCCGCGTGTCTCAGCACTACAAGGCCAGCCTCACTGCCACTTTC
AACCTGTTTCCGGAGGCCAAGTTTGCTGTGGTTCTGGAAGAGGACCTGGACATTGCTGTG
GATTTTTTCAGTTTCCTGAGCCAATCCATCCACCTACTGGAGGAGGATGACAGCCTGTAC
TGCATCTCTGCCTGGAATGACCAGGGGTATGAACACACGGCTGAGGACCCAGCACTACTG
TACCGTGTGGAGACCATGCCTGGGCTGGGCTGGGTGCTCAGGAGGTCCTTGTACAAGGAG
GAGCTTGAGCCCAAGTGGCCTACACCGGAAAAGCTCTGGGATTGGGACATGTGGATGCGG
ATGCCTGAACAACGCCGGGGCCGAGAGTGCATCATCCCTGACGTTTCCCGATCCTACCAC
TTTGGCATCGTCGGCCTCAACATGAATGGCTACTTTCACGAGGCCTACTTCAAGAAGCAC
AAGTTCAACACGGTTCCAGGTGTCCAGCTCAGGAATGTGGACAGTCTGAAGAAAGAAGCT
TATGAAGTGGAAGTTCACAGGCTGCTCAGTGAGGCTGAGGTTCTGGACCACAGCAAGAAC
CCTTGTGAAGACTCTTTCCTGCCAGACACAGAGGGCCACACCTACGTGGCCTTTATTCGA
ATGGAGAAAGATGATGACTTCACCACCTGGACCCAGCTTGCCAAGTGCCTCCATATCTGG
GACCTGGATGTGCGTGGCAACCATCGGGGCCTGTGGAGATTGTTTCGGAAGAAGAACCAC
TTCCTGGTGGTGGGGGTCCCGGCTTCCCCCTACTCAGTGAAGAAGCCACCCTCAGTCACC
CCAATTTTCCTGGAGCCACCCCCAAAGGAGGAGGGAGCCCCAGGAGCCCCAGAACAGACA
TGA

1. Yoshida A, Kobayashi K, Manya H, Taniguchi K, Kano H, Mizuno M, Inazu T, Mitsuhashi H, Takahashi S, Takeuchi M, Herrmann R, Straub V, Talim B, Voit T, Topaloglu H, Toda T, Endo T: Muscular dystrophy and neuronal migration disorder caused by mutations in a glycosyltransferase, POMGnT1. Dev Cell. 2001 Nov;1(5):717-24. [PubMed ]
2. Taniguchi K, Kobayashi K, Saito K, Yamanouchi H, Ohnuma A, Hayashi YK, Manya H, Jin DK, Lee M, Parano E, Falsaperla R, Pavone P, Van Coster R, Talim B, Steinbrecher A, Straub V, Nishino I, Topaloglu H, Voit T, Endo T, Toda T: Worldwide distribution and broader clinical spectrum of muscle-eye-brain disease. Hum Mol Genet. 2003 Mar 1;12(5):527-34. [PubMed ]
3. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed ]
4. Zhang W, Betel D, Schachter H: Cloning and expression of a novel UDP-GlcNAc:alpha-D-mannoside beta1,2-N-acetylglucosaminyltransferase homologous to UDP-GlcNAc:alpha-3-D-mannoside beta1,2-N-acetylglucosaminyltransferase I. Biochem J. 2002 Jan 1;361(Pt 1):153-62. [PubMed ]
5. Manya H, Sakai K, Kobayashi K, Taniguchi K, Kawakita M, Toda T, Endo T: Loss-of-function of an N-acetylglucosaminyltransferase, POMGnT1, in muscle-eye-brain disease. Biochem Biophys Res Commun. 2003 Jun 20;306(1):93-7. [PubMed ]

MKAAGILTLIGCLVTGAESKIYTRCKLAKIFSRAGLDNYWGFSLGNWICMAYYESGYNTT
AQTVLDDGSIDYGIFQINSFAWCRRGKLKENNHCHVACSALITDDLTDAIICARKIVKET
QGMNYWQGWKKHCEGRDLSEWKKGCEVS

• Lys (PF00062 )

• 1-19

• None

1. 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 ]

MRLREPLLSGSAAMPGASLQRACRLLVAVCALHLGVTLVYYLAGRDLSRLPQLVGVSTPL
QGGSNSAAAIGQSSGELRTGGARPPPPLGASSQPRPGGDSSPVVDSGPGPASNLTSVPVP
HTTALSLPACPEESPLLVGPMLIEFNMPVDLELVAKQNPNVKMGGRYAPRDCVSPHKVAI
IIPFRNRQEHLKYWLYYLHPVLQRQQLDYGIYVINQAGDTIFNRAKLLNVGFQEALKDYD
YTCFVFSDVDLIPMNDHNAYRCFSQPRHISVAMDKFGFSLPYVQYFGGVSALSKQQFLTI
NGFPNNYWGWGGEDDDIFNRLVFRGMSISRPNAVVGRCRMIRHSRDKKNEPNPQRFDRIA
HTKETMLSDGLNSLTYQVLDVQRYPLYTQITVDIGTPS

• Galactosyl_T_2 (PF02709 )

• None

• None

1. SubName: UDP-Gal:betaGlcNAc beta 1,4-galactosyltransferase, polypeptide 2, isoform CRA_a

MSRLLGGTLERVCKAVLLLCLLHFLVAVILYFDVYAQHLAFFSRFSARGPAHALHPAASS
SSSSSNCSRPNATASSSGLPEVPSALPGPTAPTLPPCPDSPPGLVGRLLIEFTSPMPLER
VQRENPGVLMGGRYTPPDCTPAQTVAVIIPFRHREHHLRYWLHYLHPILRRQRLRYGVYV
INQHGEDTFNRAKLLNVGFLEALKEDAAYDCFIFSDVDLVPMDDRNLYRCGDQPRHFAIA
MDKFGFRLPYAGYFGGVSGLSKAQFLRINGFPNEYWGWGGEDDDIFNRISLTGMKISRPD
IRIGRYRMIKHDRDKHNEPNPQRFTKIQNTKLTMKRDGIGSVRYQVLEVSRQPLFTNITV
DIGRPPSWPPRG

• Galactosyl_T_2 (PF02709 )

• None

• None

MGFNLTFHLSYKFRLLLLLTLCLTVVGWATSNYFVGAIQEIPKAKEFMANFHKTLILGKG
KTLTNEASTKKVELDNCPSVSPYLRGQSKLIFKPDLTLEEVQAENPKVSRGRYRPQECKA
LQRVAILVPHRNREKHLMYLLEHLHPFLQRQQLDYGIYVIHQAEGKKFNRAKLLNVGYLE
ALKEENWDCFIFHDVDLVPENDFNLYKCEEHPKHLVVGRNSTGYRLRYSGYFGGVTALSR
EQFFKVNGFSNNYWGWGGEDDDLRLRVELQRMKISRPLPEVGKYTMVFHTRDKGNEVNAE
RMKLLHQVSRVWRTDGLSSCSYKLVSVEHNPLYINITVDFWFGA

• Galactosyl_T_2 (PF02709 )

• None

• None

1. SubName: N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase, isoform CRA_a
2. SubName: cDNA, FLJ95078, highly similar to Homo sapiens N-acetylglucosamine-1-phosphodiesteralpha-N-acetylglucosaminidase (NAGPA), mRNA

MATSTGRWLLLRLALFGFLWEASGGLDSGASRDDDLLLPYPRARARLPRDCTRVRAGNRE
HESWPPPPATPGAGGLAVRTFVSHFRDRAVAGHLTRAVEPLRTFSVLEPGGPGGCAARRR
ATVEETARAADCRVAQNGGFFRMNSGECLGNVVSDERRVSSSGGLQNAQFGIRRDGTLVT
GYLSEEEVLDTENPFVQLLSGVVWLIRNGSIYINESQATECDETQETGSFSKFVNVISAR
TAIGHDRKGQLVLFHADGQTEQRGINLWEMAEFLLKQDVVNAINLDGGGSATFVLNGTLA
SYPSDHCQDNMWRCPRQVSTVVCVHEPRCQPPDCHGHGTCVDGHCQCTGHFWRGPGCDEL
DCGPSNCSQHGLCTETGCRCDAGWTGSNCSEECPLGWHGPGCQRPCKCEHHCPCDPKTGN
CSVSRVKQCLQPPEATLRAGELSFFTRTAWLALTLALAFLLLISTAANLSLLLSRAERNR
RLHGDYAYHPLQEMNGEPLAAEKEQPGGAHNPFKD

• glycoprotein N-acetyl-D-glucosaminyl-phospho-D-mannose + H2O = N-acetyl-D-glucosamine + glycoprotein phospho-D-mannose [RN:R04373] ALL_REAC R04373

• EGF_2 (PF07974 )

• None

• None

1. Lysozyme-2

MKAAGILTLIGCLVTGAESKIYTRCKLAKIFSRAGLDNYWGFSLGNWICMAYYESGYNTT
AQTVLDDGSIDYGIFQINSFAWCRRGKLKENNHCHVACSALVTDDLTDAIICAKKIVKET
QGMNYWQGWKKHCEGRDLSDWKKDCEVS

• Lys (PF00062 )

• 1-19

• None

1. Lysozyme-like protein 5
2. Sperm-specific lysozyme-like protein X
3. SLLP-X

MKAWGTVVVTLATLMVVTVDAKIYERCELAARLERAGLNGYKGYGVGDWLCMAHYESGFD
TAFVDHNPDGSSEYGIFQLNSAWWCDNGITPTKNLCHMDCHDLLNRHILDDIRCAKQIVS
SQNGLSAWTSWRLHCSGHDLSEWLKGCDMHVKIDPKIHP

• Lys (PF00062 )

• 1-21

• None

1. 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 ]

MTKALLIYLVSSFLALNQASLISRCDLAQVLQLEDLDGFEGYSLSDWLCLAFVESKFNIS
KINENADGSFDYGLFQINSHYWCNDYKSYSENLCHVDCQDLLNPNLLAGIHCAKRIVSGA
RGMNNWVEWRLHCSGRPLFYWLTGCRLR

• Lys (PF00062 )

• 1-19

• None

1. Nomiyama H, Fukuda S, Iio M, Tanase S, Miura R, Yoshie O: Organization of the chemokine gene cluster on human chromosome 17q11.2 containing the genes for CC chemokine MPIF-1, HCC-2, HCC-1, LEC, and RANTES. J Interferon Cytokine Res. 1999 Mar;19(3):227-34. [PubMed ]
2. 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 ]