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Identification
HMDB Protein ID HMDBP01105
Secondary Accession Numbers
  • 6394
Name Chondroitin sulfate synthase 1
Synonyms
  1. ChSy-1
  2. Chondroitin glucuronyltransferase 1
  3. Chondroitin synthase 1
  4. Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase 1
  5. N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase 1
  6. N-acetylgalactosaminyltransferase 1
Gene Name CHSY1
Protein Type Unknown
Biological Properties
General Function Involved in transferase activity, transferring hexosyl groups
Specific Function Has both beta-1,3-glucuronic acid and beta-1,4-N-acetylgalactosamine transferase activity. Transfers glucuronic acid (GlcUA) from UDP-GlcUA and N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of the elongating chondroitin polymer. Involved in the negative control of osteogenesis likely through the modulation of NOTCH signaling.
Pathways
  • Glycosaminoglycan biosynthesis - chondroitin sulfate / dermatan sulfate
Reactions
UDP-N-acetyl-alpha-D-galactosamine + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-proteoglycan → Uridine 5'-diphosphate + N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-proteoglycan details
Uridine diphosphate glucuronic acid + N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan → Uridine 5'-diphosphate + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan details
Uridine diphosphate-N-acetylgalactosamine + D-Glucuronyl-N-acetyl-1,3-beta-D-galactosaminylproteoglycan → Uridine 5'-diphosphate + N-Acetyl-beta-D-galactosaminyl-1,4-beta-D-glucuronyl-N-acetyl-1,3-beta-D-galactosaminylproteoglycan details
UDP-D-glucuronate + → UDP + details
UDP-N-acetyl-D-galactosamine + → UDP + details
UDP-D-glucuronate + → UDP + details
UDP-N-acetyl-D-galactosamine + → UDP + details
Uridine diphosphate glucuronic acid + N-Acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosylproteoglycan → Uridine 5'-diphosphate + beta-D-Glucuronosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosylproteoglycan details
GO Classification
Biological Process
chondroitin sulfate biosynthetic process
negative regulation of ossification
response to nutrient levels
carbohydrate metabolic process
Cellular Component
Golgi cisterna membrane
extracellular region
integral to membrane
Golgi membrane
Component
golgi membrane
membrane
cell part
organelle membrane
golgi cisterna membrane
Function
catalytic activity
transferase activity
transferase activity, transferring hexosyl groups
transferase activity, transferring glycosyl groups
Molecular Function
metal ion binding
glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase activity
N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase activity
Cellular Location
  1. Golgi apparatus
  2. Golgi stack membrane
  3. Single-pass type II membrane protein (Probable)
Gene Properties
Chromosome Location 15
Locus 15q26.3
SNPs CHSY1
Gene Sequence
>2409 bp
ATGGCCGCGCGCGGCCGGCGCGCCTGGCTCAGCGTGCTGCTCGGGCTCGTCCTGGGCTTC
GTGCTGGCCTCGCGGCTCGTCCTGCCCCGGGCTTCCGAGCTGAAGCGAGCGGGCCCACGG
CGCCGCGCCAGCCCCGAGGGCTGCCGGTCCGGGCAGGCGGCGGCTTCCCAGGCCGGCGGG
GCGCGCGGCGATGCGCGCGGGGCGCAGCTCTGGCCGCCCGGCTCGGACCCAGATGGCGGC
CCGCGCGACAGGAACTTTCTCTTCGTGGGAGTCATGACCGCCCAGAAATACCTGCAGACT
CGGGCCGTGGCCGCCTACAGAACATGGTCCAAGACAATTCCTGGGAAAGTTCAGTTCTTC
TCAAGTGAGGGTTCTGACACATCTGTACCAATTCCAGTAGTGCCACTACGGGGTGTGGAC
GACTCCTACCCGCCCCAGAAGAAGTCCTTCATGATGCTCAAGTACATGCACGACCACTAC
TTGGACAAGTATGAATGGTTTATGAGAGCAGATGATGACGTGTACATCAAAGGAGACCGT
CTGGAGAACTTCCTGAGGAGTTTGAACAGCAGCGAGCCCCTCTTTCTTGGGCAGACAGGC
CTGGGCACCACGGAAGAAATGGGAAAACTGGCCCTGGAGCCTGGTGAGAACTTCTGCATG
GGGGGGCCTGGCGTGATCATGAGCCGGGAGGTGCTTCGGAGAATGGTGCCGCACATTGGC
AAGTGTCTCCGGGAGATGTACACCACCCATGAGGACGTGGAGGTGGGAAGGTGTGTCCGG
AGGTTTGCAGGGGTGCAGTGTGTCTGGTCTTATGAGATGCAGCAGCTTTTTTATGAGAAT
TACGAGCAGAACAAAAAGGGGTACATTAGAGATCTCCATAACAGTAAAATTCACCAAGCT
ATCACATTACACCCCAACAAAAACCCACCCTACCAGTACAGGCTCCACAGCTACATGCTG
AGCCGCAAGATATCCGAGCTCCGCCATCGCACAATACAGCTGCACCGCGAAATTGTCCTG
ATGAGCAAATACAGCAACACAGAAATTCATAAAGAGGACCTCCAGCTGGGAATCCCTCCC
TCCTTCATGAGGTTTCAGCCCCGCCAGCGAGAGGAGATTCTGGAATGGGAGTTTCTGACT
GGAAAATACTTGTATTCGGCAGTTGACGGCCAGCCCCCTCGAAGAGGAATGGACTCCGCC
CAGAGGGAAGCCTTGGACGACATTGTCATGCAGGTCATGGAGATGATCAATGCCAACGCC
AAGACCAGAGGGCGCATCATTGACTTCAAAGAGATCCAGTACGGCTACCGCCGGGTGAAC
CCCATGTATGGGGCTGAGTACATCCTGGACCTGCTGCTTCTGTACAAAAAGCACAAAGGG
AAGAAAATGACGGTCCCTGTGAGGAGGCACGCGTATTTACAGCAGACTTTCAGCAAAATC
CAGTTTGTGGAGCATGAGGAGCTGGATGCACAAGAGTTGGCCAAGAGAATCAATCAGGAA
TCTGGATCCTTGTCCTTTCTCTCAAACTCCCTGAAGAAGCTCGTCCCCTTTCAGCTCCCT
GGGTCGAAGAGTGAGCACAAAGAACCCAAAGATAAAAAGATAAACATACTGATTCCTTTG
TCTGGGCGTTTCGACATGTTTGTGAGATTTATGGGAAACTTTGAGAAGACGTGTCTTATC
CCCAATCAGAACGTCAAGCTCGTGGTTCTGCTTTTCAATTCTGACTCCAACCCTGACAAG
GCCAAACAAGTTGAACTGATGAGAGATTACCGCATTAAGTACCCTAAAGCCGACATGCAG
ATTTTGCCTGTGTCTGGAGAGTTTTCAAGAGCCCTGGCCCTGGAAGTAGGATCCTCCCAG
TTTAACAATGAATCTTTGCTCTTCTTCTGCGACGTCGACCTCGTGTTTACTACAGAATTC
CTTCAGCGATGTCGAGCAAATACAGTTCTGGGCCAACAAATATATTTTCCAATCATCTTC
AGCCAGTATGACCCAAAGATTGTTTATAGTGGGAAAGTTCCCAGTGACAACCATTTTGCC
TTTACTCAGAAAACTGGCTTCTGGAGAAACTATGGGTTTGGCATCACGTGTATTTATAAG
GGAGATCTTGTCCGAGTGGGTGGCTTTGATGTTTCCATCCAAGGCTGGGGGCTGGAGGAT
GTGGACCTTTTCAACAAGGTTGTCCAGGCAGGTTTGAAGACGTTTAGGAGCCAGGAAGTA
GGAGTAGTCCACGTCCACCATCCTGTCTTTTGTGATCCCAATCTTGACCCCAAACAGTAC
AAAATGTGCTTGGGGTCCAAAGCATCGACCTATGGGTCCACCCAGCAGCTGGCTGAGATG
TGGCTGGAAAAAAATGATCCAAGTTACAGTAAAAGCAGCAATAATAATGGCTCAGTGAGG
ACAGCCTAA
Protein Properties
Number of Residues 802
Molecular Weight 91783.785
Theoretical pI 9.238
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Chondroitin sulfate synthase 1
MAARGRRAWLSVLLGLVLGFVLASRLVLPRASELKRAGPRRRASPEGCRSGQAAASQAGG
ARGDARGAQLWPPGSDPDGGPRDRNFLFVGVMTAQKYLQTRAVAAYRTWSKTIPGKVQFF
SSEGSDTSVPIPVVPLRGVDDSYPPQKKSFMMLKYMHDHYLDKYEWFMRADDDVYIKGDR
LENFLRSLNSSEPLFLGQTGLGTTEEMGKLALEPGENFCMGGPGVIMSREVLRRMVPHIG
KCLREMYTTHEDVEVGRCVRRFAGVQCVWSYEMQQLFYENYEQNKKGYIRDLHNSKIHQA
ITLHPNKNPPYQYRLHSYMLSRKISELRHRTIQLHREIVLMSKYSNTEIHKEDLQLGIPP
SFMRFQPRQREEILEWEFLTGKYLYSAVDGQPPRRGMDSAQREALDDIVMQVMEMINANA
KTRGRIIDFKEIQYGYRRVNPMYGAEYILDLLLLYKKHKGKKMTVPVRRHAYLQQTFSKI
QFVEHEELDAQELAKRINQESGSLSFLSNSLKKLVPFQLPGSKSEHKEPKDKKINILIPL
SGRFDMFVRFMGNFEKTCLIPNQNVKLVVLLFNSDSNPDKAKQVELMRDYRIKYPKADMQ
ILPVSGEFSRALALEVGSSQFNNESLLFFCDVDLVFTTEFLQRCRANTVLGQQIYFPIIF
SQYDPKIVYSGKVPSDNHFAFTQKTGFWRNYGFGITCIYKGDLVRVGGFDVSIQGWGLED
VDLFNKVVQAGLKTFRSQEVGVVHVHHPVFCDPNLDPKQYKMCLGSKASTYGSTQQLAEM
WLEKNDPSYSKSSNNNGSVRTA
GenBank ID Protein 31542309
UniProtKB/Swiss-Prot ID Q86X52
UniProtKB/Swiss-Prot Entry Name CHSS1_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_014918.4
GeneCard ID CHSY1
GenAtlas ID CHSY1
HGNC ID HGNC:17198
References
General References
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  3. Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Feb 26;6(1):63-70. [PubMed:10231032 ]
  4. Yada T, Sato T, Kaseyama H, Gotoh M, Iwasaki H, Kikuchi N, Kwon YD, Togayachi A, Kudo T, Watanabe H, Narimatsu H, Kimata K: Chondroitin sulfate synthase-3. Molecular cloning and characterization. J Biol Chem. 2003 Oct 10;278(41):39711-25. Epub 2003 Aug 7. [PubMed:12907687 ]
  5. Kitagawa H, Izumikawa T, Uyama T, Sugahara K: Molecular cloning of a chondroitin polymerizing factor that cooperates with chondroitin synthase for chondroitin polymerization. J Biol Chem. 2003 Jun 27;278(26):23666-71. Epub 2003 Apr 25. [PubMed:12716890 ]
  6. Kitagawa H, Uyama T, Sugahara K: Molecular cloning and expression of a human chondroitin synthase. J Biol Chem. 2001 Oct 19;276(42):38721-6. Epub 2001 Aug 20. [PubMed:11514575 ]