CHST7_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CHST7_HUMAN
• UniProt AC: Q9NS84
• Protein Name: Carbohydrate sulfotransferase 7
• Gene Name: CHST7
• Organism: Homo sapiens (Human).
• Sequence Length: 486
• Subcellular Localization: Golgi apparatus membrane; Single-pass type II membrane protein.
• Protein Description: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues. Preferentially acts on mannose-linked GlcNAc. Also able to catalyze the transfer of sulfate to position 6 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Also acts on core 2 mucin-type oligosaccharide and N-acetyllactosamine oligomer with a lower efficiency. Has weak or no activity toward keratan sulfate and oligosaccharides containing the Galbeta1-4GlcNAc. Catalyzes 6-O-sulfation of beta-benzyl GlcNAc but not alpha- or beta-benzyl GalNAc..
• Protein Sequence: MKGRRRRRREYCKFALLLVLYTLVLLLVPSVLDGGRDGDKGAEHCPGLQRSLGVWSLEAAAAGEREQGAEARAAEEGGANQSPRFPSNLSGAVGEAVSREKQHIYVHATWRTGSSFLGELFNQHPDVFYLYEPMWHLWQALYPGDAESLQGALRDMLRSLFRCDFSVLRLYAPPGDPAARAPDTANLTTAALFRWRTNKVICSPPLCPGAPRARAEVGLVEDTACERSCPPVAIRALEAECRKYPVVVIKDVRLLDLGVLVPLLRDPGLNLKVVQLFRDPRAVHNSRLKSRQGLLRESIQVLRTRQRGDRFHRVLLAHGVGARPGGQSRALPAAPRADFFLTGALEVICEAWLRDLLFARGAPAWLRRRYLRLRYEDLVRQPRAQLRRLLRFSGLRALAALDAFALNMTRGAAYGADRPFHLSARDAREAVHAWRERLSREQVRQVEAACAPAMRLLAYPRSGEEGDAEQPREGETPLEMDADGAT

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
82	Phosphorylation	EEGGANQSPRFPSNL HHCCCCCCCCCCCCC	20.18	28290473
88	N-linked_Glycosylation	QSPRFPSNLSGAVGE CCCCCCCCCCHHHHH	38.16	UniProtKB CARBOHYD
184	Phosphorylation	PAARAPDTANLTTAA HHHCCCCCCCCCHHH	19.18	-
186	N-linked_Glycosylation	ARAPDTANLTTAALF HCCCCCCCCCHHHHH	39.76	UniProtKB CARBOHYD
244	Phosphorylation	LEAECRKYPVVVIKD HHHHHHCCCEEEEEC	5.06	-
272	Ubiquitination	RDPGLNLKVVQLFRD HCCCCCEEEEEHHCC	39.01	21890473
328	Phosphorylation	GARPGGQSRALPAAP CCCCCCCCCCCCCCC	23.85	23403867
407	N-linked_Glycosylation	ALDAFALNMTRGAAY HHHHHHHHCCCHHHH	26.75	16335952
459	Phosphorylation	PAMRLLAYPRSGEEG HHHHHHHCCCCCCCC	10.11	22817900
462	Phosphorylation	RLLAYPRSGEEGDAE HHHHCCCCCCCCCCC	46.16	16335952

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of CHST7_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CHST7_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of CHST7_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of CHST7_HUMAN !!

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-407, AND MASSSPECTROMETRY.
PubMed: 16335952