XYLK_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: XYLK_HUMAN
• UniProt AC: O75063
• Protein Name: Glycosaminoglycan xylosylkinase
• Gene Name: FAM20B {ECO:0000312|HGNC:HGNC:23017}
• Organism: Homo sapiens (Human).
• Sequence Length: 409
• Subcellular Localization: Golgi apparatus membrane ; Single-pass type II membrane protein .
• Protein Description: Responsible for the 2-O-phosphorylation of xylose in the glycosaminoglycan-protein linkage region of proteoglycans thereby regulating the amount of mature GAG chains. Sulfated glycosaminoglycans (GAGs), including heparan sulfate and chondroitin sulfate, are synthesized on the so-called common GAG-protein linkage region (GlcUAbeta1-3Galbeta1-3Galbeta1-4Xylbeta1-O-Ser) of core proteins, which is formed by the stepwise addition of monosaccharide residues by the respective specific glycosyltransferases. Xylose 2-O-phosphorylation may influence the catalytic activity of B3GAT3 (GlcAT-I) which completes the precursor tetrasaccharide of GAG-protein linkage regions on which the repeating disaccharide region is synthesized..
• Protein Sequence: MKLKQRVVLLAILLVIFIFTKVFLIDNLDTSAANREDQRAFHRMMTGLRVELAPKLDHTLQSPWEIAAQWVVPREVYPEETPELGAVMHAMATKKIIKADVGYKGTQLKALLILEGGQKVVFKPKRYSRDHVVEGEPYAGYDRHNAEVAAFHLDRILGFHRAPLVVGRFVNLRTEIKPVATEQLLSTFLTVGNNTCFYGKCYYCRETEPACADGDIMEGSVTLWLPDVWPLQKHRHPWGRTYREGKLARWEYDESYCDAVKKTSPYDSGPRLLDIIDTAVFDYLIGNADRHHYESFQDDEGASMLILLDNAKSFGNPSLDERSILAPLYQCCIIRVSTWNRLNYLKNGVLKSALKSAMAHDPISPVLSDPHLDAVDQRLLSVLATVKQCTDQFGMDTVLVEDRMPLSHL

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
104	Ubiquitination	IKADVGYKGTQLKAL HHHCCCCCCCCCEEE	49.94	-
138	Phosphorylation	HVVEGEPYAGYDRHN CEECCCCCCCCCCCC	14.35	21082442
141	Phosphorylation	EGEPYAGYDRHNAEV CCCCCCCCCCCCHHH	11.13	28152594
193	N-linked_Glycosylation	STFLTVGNNTCFYGK HHHCEECCCCEECCE	35.98	UniProtKB CARBOHYD
256	Phosphorylation	RWEYDESYCDAVKKT EEECCHHHHHHCHHC	7.72	22468782
263	Phosphorylation	YCDAVKKTSPYDSGP HHHHCHHCCCCCCCC	29.26	22468782
266	Phosphorylation	AVKKTSPYDSGPRLL HCHHCCCCCCCCHHH	23.62	22468782
268	Phosphorylation	KKTSPYDSGPRLLDI HHCCCCCCCCHHHHH	44.87	22468782
293	Phosphorylation	GNADRHHYESFQDDE CCCCHHHCHHHCCCC	13.72	22798277
303	Phosphorylation	FQDDEGASMLILLDN HCCCCCCEEEEEECC	25.61	22798277
313	Phosphorylation	ILLDNAKSFGNPSLD EEECCHHHHCCCCCC	35.66	22798277
364	Phosphorylation	AMAHDPISPVLSDPH HHHCCCCCCCCCCCC	17.84	-
385	Phosphorylation	RLLSVLATVKQCTDQ HHHHHHHHHHHHHHH	24.87	29396449

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of XYLK_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 XYLK_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ASPH2_HUMAN	ASPHD2	physical	28514442

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.