FUCO2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FUCO2_HUMAN
• UniProt AC: Q9BTY2
• Protein Name: Plasma alpha-L-fucosidase
• Gene Name: FUCA2
• Organism: Homo sapiens (Human).
• Sequence Length: 467
• Subcellular Localization: Secreted .
• Protein Description: Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins..
• Protein Sequence: MRPQELPRLAFPLLLLLLLLLPPPPCPAHSATRFDPTWESLDARQLPAWFDQAKFGIFIHWGVFSVPSFGSEWFWWYWQKEKIPKYVEFMKDNYPPSFKYEDFGPLFTAKFFNANQWADIFQASGAKYIVLTSKHHEGFTLWGSEYSWNWNAIDEGPKRDIVKELEVAIRNRTDLRFGLYYSLFEWFHPLFLEDESSSFHKRQFPVSKTLPELYELVNNYQPEVLWSDGDGGAPDQYWNSTGFLAWLYNESPVRGTVVTNDRWGAGSICKHGGFYTCSDRYNPGHLLPHKWENCMTIDKLSWGYRREAGISDYLTIEELVKQLVETVSCGGNLLMNIGPTLDGTISVVFEERLRQMGSWLKVNGEAIYETHTWRSQNDTVTPDVWYTSKPKEKLVYAIFLKWPTSGQLFLGHPKAILGATEVKLLGHGQPLNWISLEQNGIMVELPQLTIHQMPCKWGWALALTNVI

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
30	Phosphorylation	PPPCPAHSATRFDPT CCCCCCCCCCCCCCC	33.18	-
32	Phosphorylation	PCPAHSATRFDPTWE CCCCCCCCCCCCCHH	34.58	-
80	Ubiquitination	WFWWYWQKEKIPKYV CHHHHHCCCCCCHHH	46.99	22817900
82	Ubiquitination	WWYWQKEKIPKYVEF HHHHCCCCCCHHHHH	71.93	22817900
85	Ubiquitination	WQKEKIPKYVEFMKD HCCCCCCHHHHHHHH	66.46	22817900
85	Ubiquitination	WQKEKIPKYVEFMKD HCCCCCCHHHHHHHH	66.46	21890473
99	Ubiquitination	DNYPPSFKYEDFGPL HCCCCCCCCCCCCHH	52.66	-
108	Phosphorylation	EDFGPLFTAKFFNAN CCCCHHEEEEECCHH	36.30	-
171	N-linked_Glycosylation	ELEVAIRNRTDLRFG HHHHHHHCCCHHHHH	45.12	UniProtKB CARBOHYD
207	Phosphorylation	HKRQFPVSKTLPELY HHCCCCCCCCHHHHH	21.84	22817900
239	N-linked_Glycosylation	GAPDQYWNSTGFLAW CCCHHHCCCCCHHHH	25.43	19159218
301	Phosphorylation	CMTIDKLSWGYRREA CEEEEECCCCCCCCC	24.97	22167270
304	Phosphorylation	IDKLSWGYRREAGIS EEECCCCCCCCCCCC	10.55	24702127
377	N-linked_Glycosylation	THTWRSQNDTVTPDV EEEECCCCCEECCCC	48.44	UniProtKB CARBOHYD
391	Acetylation	VWYTSKPKEKLVYAI CEECCCCHHHEEEEE	71.82	19666675
414	Ubiquitination	QLFLGHPKAILGATE CEECCCHHHEEECCE	42.24	-

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
301	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of FUCO2_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 FUCO2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MEOX2_HUMAN	MEOX2	physical	25416956
MA2B2_HUMAN	MAN2B2	physical	28514442
CLD12_HUMAN	CLDN12	physical	28514442
QCR6_HUMAN	UQCRH	physical	28514442
GRP78_HUMAN	HSPA5	physical	28514442
CALX_HUMAN	CANX	physical	28514442
NAT14_HUMAN	NAT14	physical	28514442
RAB21_HUMAN	RAB21	physical	28514442
TV23C_HUMAN	TVP23C	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.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"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-239, AND MASSSPECTROMETRY.
PubMed: 19159218