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CHST9 (human)

Overview CHST9 Catalyzes the transfer of sulfate to position 4 of non- reducing N-acetylgalactosamine (GalNAc) residues in both N-glycans and O-glycans. Participates in biosynthesis of glycoprotein hormones lutropin and thyrotropin, by mediating sulfation of their carbohydrate structures. Has a higher activity toward carbonic anhydrase VI than toward lutropin. Only active against terminal GalNAcbeta1,GalNAcbeta. Isoform 2, but not isoform 1, is active toward chondroitin. Belongs to the sulfotransferase 2 family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB. Protein type: Membrane protein, integral; EC 2.8.2.-; Transferase Cellular Component: Golgi membrane; extracellular region; integral to membrane Molecular Function: N-acetylgalactosamine 4-O-sulfotransferase activity Biological Process: chondroitin sulfate metabolic process; sulfur metabolic process; chondroitin sulfate biosynthetic process; glycosaminoglycan metabolic process; proteoglycan biosynthetic process; carbohydrate metabolic process; hormone biosynthetic process; carbohydrate biosynthetic process Reference #:  Q7L1S5 (UniProtKB) Alt. Names/Synonyms: carbohydrate (N-acetylgalactosamine 4-0) sulfotransferase 9; Carbohydrate sulfotransferase 9; CHST9; FLJ42328; GalNAc-4-O-sulfotransferase 2; GalNAc-4-ST2; GalNAc-4-sulfotransferase 2; GalNAc4ST-2; N-acetylgalactosamine 4-O-sulfotransferase 2; N-acetylgalactosamine-4-O-sulfotransferase 2 Gene Symbols: CHST9 Molecular weight: 52,055 Da Basal Isoelectric point: 9.41  Predict pI for various phosphorylation states

Select Structure to View Below CHST9

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	Modification Sites and Domains

	Modification Sites in Parent Protein, Orthologs, and Isoforms

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
0	1		S122-p	QGGDQALsKSTGSPT
0	1		Y429-p	RQLIYDFyyLDyLMF
0	1		Y430-p	QLIYDFyyLDyLMFN
0	1		Y433-p	YDFyyLDyLMFNYTT

	mouse
-	under review
Y399	RQLIYDFYHLDYLMF
H400	QLIYDFYHLDYLMFN
Y403	YDFYHLDYLMFNYTT

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