FETUB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FETUB_HUMAN
• UniProt AC: Q9UGM5
• Protein Name: Fetuin-B
• Gene Name: FETUB
• Organism: Homo sapiens (Human).
• Sequence Length: 382
• Subcellular Localization: Secreted.
• Protein Description: Protease inhibitor required for egg fertilization. Required to prevent premature zona pellucida hardening before fertilization, probably by inhibiting the protease activity of ASTL, a protease that mediates the cleavage of ZP2 and triggers zona pellucida hardening (By similarity)..
• Protein Sequence: MGLLLPLALCILVLCCGAMSPPQLALNPSALLSRGCNDSDVLAVAGFALRDINKDRKDGYVLRLNRVNDAQEYRRGGLGSLFYLTLDVLETDCHVLRKKAWQDCGMRIFFESVYGQCKAIFYMNNPSRVLYLAAYNCTLRPVSKKKIYMTCPDCPSSIPTDSSNHQVLEAATESLAKYNNENTSKQYSLFKVTRASSQWVVGPSYFVEYLIKESPCTKSQASSCSLQSSDSVPVGLCKGSLTRTHWEKFVSVTCDFFESQAPATGSENSAVNQKPTNLPKVEESQQKNTPPTDSPSKAGPRGSVQYLPDLDDKNSQEKGPQEAFPVHLDLTTNPQGETLDISFLFLEPMEEKLVVLPFPKEKARTAECPGPAQNASPLVLPP

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
33	Phosphorylation	LNPSALLSRGCNDSD CCHHHHHHCCCCHHH	27.72	24505115
37	N-linked_Glycosylation	ALLSRGCNDSDVLAV HHHHCCCCHHHHHHH	55.43	17623646
37	N-linked_Glycosylation	ALLSRGCNDSDVLAV HHHHCCCCHHHHHHH	55.43	16335952
60	Phosphorylation	NKDRKDGYVLRLNRV CCCCCCCEEEEEECC	13.37	-
136	N-linked_Glycosylation	VLYLAAYNCTLRPVS HEEEEEECCEECCCC	13.94	16335952
160	O-linked_Glycosylation	DCPSSIPTDSSNHQV CCCCCCCCCCCCHHH	47.01	OGP
182	N-linked_Glycosylation	LAKYNNENTSKQYSL HHHHCCCCCCCEEEE	52.34	UniProtKB CARBOHYD
188	Phosphorylation	ENTSKQYSLFKVTRA CCCCCEEEEEEEEEC	25.49	24719451
204	Phosphorylation	SQWVVGPSYFVEYLI CCEEECHHHHHHHHH	25.85	23401153
205	Phosphorylation	QWVVGPSYFVEYLIK CEEECHHHHHHHHHH	18.12	23401153
209	Phosphorylation	GPSYFVEYLIKESPC CHHHHHHHHHHCCCC	14.39	23401153
222	O-linked_Glycosylation	PCTKSQASSCSLQSS CCCHHHCCCCCCCCC	25.00	OGP
223	Phosphorylation	CTKSQASSCSLQSSD CCHHHCCCCCCCCCC	15.67	24505115
223	O-linked_Glycosylation	CTKSQASSCSLQSSD CCHHHCCCCCCCCCC	15.67	OGP
240	Phosphorylation	PVGLCKGSLTRTHWE CEEECCCCCCHHHHH	16.44	23401153
266	O-linked_Glycosylation	SQAPATGSENSAVNQ CCCCCCCCCCCCCCC	29.29	OGP
276	O-linked_Glycosylation	SAVNQKPTNLPKVEE CCCCCCCCCCCCHHH	57.32	OGP
289	O-linked_Glycosylation	EESQQKNTPPTDSPS HHHHHCCCCCCCCCC	37.37	UniProtKB CARBOHYD
292	O-linked_Glycosylation	QQKNTPPTDSPSKAG HHCCCCCCCCCCCCC	50.76	UniProtKB CARBOHYD
303	Phosphorylation	SKAGPRGSVQYLPDL CCCCCCCCCEECCCC	13.82	24275569
315	Phosphorylation	PDLDDKNSQEKGPQE CCCCCCCCCCCCCCC	45.52	26657352
376	Phosphorylation	PGPAQNASPLVLPP- CCCCCCCCCCCCCC-	26.73	24719451

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of FETUB_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 FETUB_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of FETUB_HUMAN !!

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

"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-37 AND ASN-136, AND MASSSPECTROMETRY.
PubMed: 16335952