dbPTM

SIA10_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SIA10_HUMAN
UniProt AC	Q9Y274
Protein Name	Type 2 lactosamine alpha-2,3-sialyltransferase
Gene Name	ST3GAL6
Organism	Homo sapiens (Human).
Sequence Length	331
Subcellular Localization	Golgi apparatus membrane Single-pass type II membrane protein .
Protein Description	Involved in the synthesis of sialyl-paragloboside, a precursor of sialyl-Lewis X determinant. Has a alpha-2,3-sialyltransferase activity toward Gal-beta1,4-GlcNAc structure on glycoproteins and glycolipids. Has a restricted substrate specificity, it utilizes Gal-beta1,4-GlcNAc on glycoproteins, and neolactotetraosylceramide and neolactohexaosylceramide, but not lactotetraosylceramide, lactosylceramide or asialo-GM1..
Protein Sequence	MRGYLVAIFLSAVFLYYVLHCILWGTNVYWVAPVEMKRRNKIQPCLSKPAFASLLRFHQFHPFLCAADFRKIASLYGSDKFDLPYGMRTSAEYFRLALSKLQSCDLFDEFDNIPCKKCVVVGNGGVLKNKTLGEKIDSYDVIIRMNNGPVLGHEEEVGRRTTFRLFYPESVFSDPIHNDPNTTVILTAFKPHDLRWLLELLMGDKINTNGFWKKPALNLIYKPYQIRILDPFIIRTAAYELLHFPKVFPKNQKPKHPTTGIIAITLAFYICHEVHLAGFKYNFSDLKSPLHYYGNATMSLMNKNAYHNVTAEQLFLKDIIEKNLVINLTQD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
129	N-linked_Glycosylation	GNGGVLKNKTLGEKI CCCCEECCCCHHCCC	38.08	UniProtKB CARBOHYD
181	N-linked_Glycosylation	DPIHNDPNTTVILTA CCCCCCCCCEEEEEE	51.77	UniProtKB CARBOHYD
282	N-linked_Glycosylation	HLAGFKYNFSDLKSP HHCCCCCCHHHCCCC	30.45	UniProtKB CARBOHYD
295	N-linked_Glycosylation	SPLHYYGNATMSLMN CCCCCCCHHHHHHCC	19.00	UniProtKB CARBOHYD
306	Phosphorylation	SLMNKNAYHNVTAEQ HHCCCCCCCCCCHHH	11.88	-
308	N-linked_Glycosylation	MNKNAYHNVTAEQLF CCCCCCCCCCHHHHH	21.84	19159218
310	Phosphorylation	KNAYHNVTAEQLFLK CCCCCCCCHHHHHHH	29.78	-
327	N-linked_Glycosylation	IEKNLVINLTQD--- HHHCCEEECCCC---	29.56	UniProtKB CARBOHYD

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of SIA10_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SIA10_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of SIA10_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
A4_HUMAN	APP	physical	21832049

Drug and Disease Associations

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

Regulatory Network of SIA10_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-308, AND MASSSPECTROMETRY.	19159218 [Abstract]