CHSTE_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CHSTE_HUMAN
• UniProt AC: Q8NCH0
• Protein Name: Carbohydrate sulfotransferase 14
• Gene Name: CHST14
• Organism: Homo sapiens (Human).
• Sequence Length: 376
• Subcellular Localization: Golgi apparatus membrane; Single-pass type II membrane protein.
• Protein Description: Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of dermatan sulfate. Plays a pivotal role in the formation of 4-0-sulfated IdoA blocks in dermatan sulfate. Transfers sulfate to the C-4 hydroxyl of beta1,4-linked GalNAc that is substituted with an alpha-linked iduronic acid (IdoUA) at the C-3 hydroxyl. Transfers sulfate more efficiently to GalNAc residues in -IdoUA-GalNAc-IdoUA- than in -GlcUA-GalNAc-GlcUA-sequences. Has preference for partially desulfated dermatan sulfate. Addition of sulfate to GalNAc may occur immediately after epimerization of GlcUA to IdoUA. Appears to have an important role in the formation of the cerebellar neural network during postnatal brain development..
• Protein Sequence: MFPRPLTPLAAPNGAEPLGRALRRAPLGRARAGLGGPPLLLPSMLMFAVIVASSGLLLMIERGILAEMKPLPLHPPGREGTAWRGKAPKPGGLSLRAGDADLQVRQDVRNRTLRAVCGQPGMPRDPWDLPVGQRRTLLRHILVSDRYRFLYCYVPKVACSNWKRVMKVLAGVLDSVDVRLKMDHRSDLVFLADLRPEEIRYRLQHYFKFLFVREPLERLLSAYRNKFGEIREYQQRYGAEIVRRYRAGAGPSPAGDDVTFPEFLRYLVDEDPERMNEHWMPVYHLCQPCAVHYDFVGSYERLEADANQVLEWVRAPPHVRFPARQAWYRPASPESLHYHLCSAPRALLQDVLPKYILDFSLFAYPLPNVTKEACQQ

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
7	Phosphorylation	-MFPRPLTPLAAPNG -CCCCCCCCCCCCCC	20.95	28450419
86	Ubiquitination	EGTAWRGKAPKPGGL CCCCCCCCCCCCCCE	53.60	-
110	N-linked_Glycosylation	QVRQDVRNRTLRAVC HHHHHHHHCCHHHHH	40.93	UniProtKB CARBOHYD
147	Phosphorylation	HILVSDRYRFLYCYV HHHHCCCCEEEEECC	15.65	26657352
156	Ubiquitination	FLYCYVPKVACSNWK EEEECCCHHHCCCHH	32.21	-
186	Phosphorylation	RLKMDHRSDLVFLAD EECCCCCCCEEEEEC	31.70	-
226	Ubiquitination	LLSAYRNKFGEIREY HHHHHHHCHHHHHHH	45.83	-
245	Phosphorylation	GAEIVRRYRAGAGPS CHHHHHHHHCCCCCC	8.34	25278378
252	O-linked_Glycosylation	YRAGAGPSPAGDDVT HHCCCCCCCCCCCCC	26.85	31492838
259	Phosphorylation	SPAGDDVTFPEFLRY CCCCCCCCHHHHHHH	40.23	-
335	Phosphorylation	YRPASPESLHYHLCS CCCCCHHHHHHHHHH	24.67	30206219
338	Phosphorylation	ASPESLHYHLCSAPR CCHHHHHHHHHHHHH	11.20	30206219
342	Phosphorylation	SLHYHLCSAPRALLQ HHHHHHHHHHHHHHH	47.90	30206219
368	N-linked_Glycosylation	LFAYPLPNVTKEACQ HCCCCCCCCCHHHHC	62.87	UniProtKB CARBOHYD

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CHSTE_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 CHSTE_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
POTEE_HUMAN	POTEE	physical	28514442
GOGA5_HUMAN	GOLGA5	physical	28514442
FUT11_HUMAN	FUT11	physical	28514442
CALX_HUMAN	CANX	physical	28514442

Drug and Disease Associations

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