CHST1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CHST1_HUMAN
• UniProt AC: O43916
• Protein Name: Carbohydrate sulfotransferase 1
• Gene Name: CHST1
• Organism: Homo sapiens (Human).
• Sequence Length: 411
• 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 galactose (Gal) residues of keratan. Has a preference for sulfating keratan sulfate, but it also transfers sulfate to the unsulfated polymer. The sulfotransferase activity on sialyl LacNAc structures is much higher than the corresponding desialylated substrate, and only internal Gal residues are sulfated. May function in the sulfation of sialyl N-acetyllactosamine oligosaccharide chains attached to glycoproteins. Participates in biosynthesis of selectin ligands. Selectin ligands are present in high endothelial cells (HEVs) and play a central role in lymphocyte homing at sites of inflammation..
• Protein Sequence: MQCSWKAVLLLALASIAIQYTAIRTFTAKSFHTCPGLAEAGLAERLCEESPTFAYNLSRKTHILILATTRSGSSFVGQLFNQHLDVFYLFEPLYHVQNTLIPRFTQGKSPADRRVMLGASRDLLRSLYDCDLYFLENYIKPPPVNHTTDRIFRRGASRVLCSRPVCDPPGPADLVLEEGDCVRKCGLLNLTVAAEACRERSHVAIKTVRVPEVNDLRALVEDPRLNLKVIQLVRDPRGILASRSETFRDTYRLWRLWYGTGRKPYNLDVTQLTTVCEDFSNSVSTGLMRPPWLKGKYMLVRYEDLARNPMKKTEEIYGFLGIPLDSHVARWIQNNTRGDPTLGKHKYGTVRNSAATAEKWRFRLSYDIVAFAQNACQQVLAQLGYKIAASEEELKNPSVSLVEERDFRPFS

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
55	Phosphorylation	EESPTFAYNLSRKTH HCCCCEEEECCCCCE	16.67	21447384
56	N-linked_Glycosylation	ESPTFAYNLSRKTHI CCCCEEEECCCCCEE	28.27	UniProtKB CARBOHYD
120	Phosphorylation	RRVMLGASRDLLRSL HHHHHHCCHHHHHHH	25.24	-
126	Phosphorylation	ASRDLLRSLYDCDLY CCHHHHHHHHHCCHH	31.11	-
128	Phosphorylation	RDLLRSLYDCDLYFL HHHHHHHHHCCHHHH	18.77	-
145	N-linked_Glycosylation	YIKPPPVNHTTDRIF CCCCCCCCCCHHHHH	32.34	UniProtKB CARBOHYD
189	N-linked_Glycosylation	VRKCGLLNLTVAAEA HHHCCCHHHHHHHHH	38.41	UniProtKB CARBOHYD
297	Phosphorylation	PPWLKGKYMLVRYED CCCCCCCEEEEEHHH	12.35	20230923
334	N-linked_Glycosylation	HVARWIQNNTRGDPT HHHHHHHHCCCCCCC	42.58	UniProtKB CARBOHYD
356	Phosphorylation	TVRNSAATAEKWRFR CCCCCHHHHHHHHEE	34.76	-
390	Phosphorylation	LGYKIAASEEELKNP HCCHHHCCHHHHCCC	36.20	21815630
398	Phosphorylation	EEELKNPSVSLVEER HHHHCCCCCCCEECC	33.46	19664994
411	Phosphorylation	ERDFRPFS------- CCCCCCCC-------	41.83	21815630

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

Oops, there are no upstream regulatory protein records of CHST1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CHST1_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 CHST1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NH2L1_HUMAN	NHP2L1	physical	21988832

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.