CHST3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CHST3_HUMAN
• UniProt AC: Q7LGC8
• Protein Name: Carbohydrate sulfotransferase 3
• Gene Name: CHST3
• Organism: Homo sapiens (Human).
• Sequence Length: 479
• 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 the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Can also sulfate Gal residues of keratan sulfate, another glycosaminoglycan, and the Gal residues in sialyl N-acetyllactosamine (sialyl LacNAc) oligosaccharides. May play a role in the maintenance of naive T-lymphocytes in the spleen..
• Protein Sequence: MEKGLTLPQDCRDFVHSLKMRSKYALFLVFVVIVFVFIEKENKIISRVSDKLKQIPQALADANSTDPALILAENASLLSLSELDSAFSQLQSRLRNLSLQLGVEPAMEAAGEEEEEQRKEEEPPRPAVAGPRRHVLLMATTRTGSSFVGEFFNQQGNIFYLFEPLWHIERTVSFEPGGANAAGSALVYRDVLKQLFLCDLYVLEHFITPLPEDHLTQFMFRRGSSRSLCEDPVCTPFVKKVFEKYHCKNRRCGPLNVTLAAEACRRKEHMALKAVRIRQLEFLQPLAEDPRLDLRVIQLVRDPRAVLASRMVAFAGKYKTWKKWLDDEGQDGLREEEVQRLRGNCESIRLSAELGLRQPAWLRGRYMLVRYEDVARGPLQKAREMYRFAGIPLTPQVEDWIQKNTQAAHDGSGIYSTQKNSSEQFEKWRFSMPFKLAQVVQAACGPAMRLFGYKLARDAAALTNRSVSLLEERGTFWVT

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
17	Phosphorylation	DCRDFVHSLKMRSKY HHHHHHHHHHHHHHH	25.12	22985185
63	N-linked_Glycosylation	PQALADANSTDPALI HHHHHHCCCCCHHHH	46.09	UniProtKB CARBOHYD
74	N-linked_Glycosylation	PALILAENASLLSLS HHHHHHCCHHHCCHH	29.26	UniProtKB CARBOHYD
96	N-linked_Glycosylation	QLQSRLRNLSLQLGV HHHHHHHHHHHHHCC	38.28	UniProtKB CARBOHYD
140	Phosphorylation	RHVLLMATTRTGSSF CEEEEEEEECCCCHH	11.66	24719451
239	Acetylation	PVCTPFVKKVFEKYH CCCCHHHHHHHHHHC	43.53	7966127
256	N-linked_Glycosylation	NRRCGPLNVTLAAEA CCCCCCCHHHHHHHH	28.06	UniProtKB CARBOHYD
273	Methylation	RKEHMALKAVRIRQL CCCCHHHHHHHHHHH	34.98	23644510
309	Phosphorylation	DPRAVLASRMVAFAG CHHHHHHHHHHHHHC	19.42	22964224
342	Methylation	EEEVQRLRGNCESIR HHHHHHHHCCHHHHH	36.15	-
386	Phosphorylation	LQKAREMYRFAGIPL HHHHHHHHHHCCCCC	9.60	22210691
394	Phosphorylation	RFAGIPLTPQVEDWI HHCCCCCCHHHHHHH	13.30	22210691
419	Ubiquitination	SGIYSTQKNSSEQFE CCCCCCCCCCHHHHH	59.91	21963094
420	N-linked_Glycosylation	GIYSTQKNSSEQFEK CCCCCCCCCHHHHHH	40.73	UniProtKB CARBOHYD
427	Ubiquitination	NSSEQFEKWRFSMPF CCHHHHHHHHHCCHH	44.98	29967540
464	N-linked_Glycosylation	RDAAALTNRSVSLLE HHHHHHHHCCCHHHH	34.77	UniProtKB CARBOHYD
468	Phosphorylation	ALTNRSVSLLEERGT HHHHCCCHHHHHCCC	28.60	26437602

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

Oops, there are no upstream regulatory protein records of CHST3_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CHST3_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 CHST3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
OFD1_HUMAN	OFD1	physical	27173435

Drug and Disease Associations

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