FICD_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FICD_HUMAN
• UniProt AC: Q9BVA6
• Protein Name: Adenosine monophosphate-protein transferase FICD {ECO:0000305}
• Gene Name: FICD {ECO:0000312|HGNC:HGNC:18416}
• Organism: Homo sapiens (Human).
• Sequence Length: 458
• Subcellular Localization: Endoplasmic reticulum membrane ; Single-pass type II membrane protein .
• Protein Description: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-231 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (By similarity). Acts as a key regulator of the ERN1/IRE1-mediated unfolded protein response (UPR) by mediating AMPylation or de-AMPylation of HSPA5/BiP. [PubMed: 25601083 In unstressed cells, acts as an adenylyltransferase by mediating AMPylation of HSPA5/BiP at 'Thr-518', thereby inactivating it (By similarity In response to endoplasmic reticulum stress, acts as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from HSPA5/BiP at 'Thr-518', leading to restore HSPA5/BiP activity (By similarity Although it is able to AMPylate RhoA, Rac and Cdc42 Rho GTPases in vitro, Rho GTPases do not constitute physiological substrates]
• Protein Sequence: MMLIPMASVMAVTEPKWVSVWSRFLWVTLLSMVLGSLLALLLPLGAVEEQCLAVLKGLYLLRSKPDRAQHAATKCTSPSTELSITSRGATLLVAKTKASPAGKLEARAALNQALEMKRQGKREKAQKLFMHALKMDPDFVDALTEFGIFSEEDKDIIQADYLYTRALTISPYHEKALVNRDRTLPLVEEIDQRYFSIIDSKVKKVMSIPKGNSALRRVMEETYYHHIYHTVAIEGNTLTLSEIRHILETRYAVPGKSLEEQNEVIGMHAAMKYINTTLVSRIGSVTISDVLEIHRRVLGYVDPVEAGRFRTTQVLVGHHIPPHPQDVEKQMQEFVQWLNSEEAMNLHPVEFAALAHYKLVYIHPFIDGNGRTSRLLMNLILMQAGYPPITIRKEQRSDYYHVLEAANEGDVRPFIRFIAKCTETTLDTLLFATTEYSVALPEAQPNHSGFKETLPVKP

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
1	Acetylation	-------MMLIPMAS -------CCCCCCCC	4.44	-
79	AMPylation	ATKCTSPSTELSITS HHHCCCCCCCEEEEC	33.99	25601083
80	AMPylation	TKCTSPSTELSITSR HHCCCCCCCEEEECC	44.31	25601083
168	O-linked_Glycosylation	YLYTRALTISPYHEK EEEEEEEECCCCCHH	20.58	55826265
183	Phosphorylation	ALVNRDRTLPLVEEI HHCCCCCCCCCHHHH	36.70	26270265
183	AMPylation	ALVNRDRTLPLVEEI HHCCCCCCCCCHHHH	36.70	25601083
194	Phosphorylation	VEEIDQRYFSIIDSK HHHHHHHHHHHHCHH	8.95	26270265
196	Phosphorylation	EIDQRYFSIIDSKVK HHHHHHHHHHCHHHH	15.08	26270265
200	Phosphorylation	RYFSIIDSKVKKVMS HHHHHHCHHHHHHHH	29.01	26270265
241	Phosphorylation	EGNTLTLSEIRHILE ECCEEEHHHHHHHHH	26.24	24719451
275	N-linked_Glycosylation	HAAMKYINTTLVSRI HHHHHHHHHHHHHCC	24.74	25601083
276	Phosphorylation	AAMKYINTTLVSRIG HHHHHHHHHHHHCCC	16.37	-
286	Phosphorylation	VSRIGSVTISDVLEI HHCCCCEEHHHHHHH	19.23	-
446	N-linked_Glycosylation	ALPEAQPNHSGFKET CCCCCCCCCCCCCCC	29.85	25601083

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

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

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
275	N	Glycosylation	N-glycosylated; predominantly glycosylated at Asn-275.	25601083

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of FICD_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of FICD_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

Acetylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
PubMed: 19413330