FCERA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FCERA_HUMAN
• UniProt AC: P12319
• Protein Name: High affinity immunoglobulin epsilon receptor subunit alpha
• Gene Name: FCER1A
• Organism: Homo sapiens (Human).
• Sequence Length: 257
• Subcellular Localization: Cell membrane; Single-pass type I membrane protein.
• Protein Description: Binds to the Fc region of immunoglobulins epsilon. High affinity receptor. Responsible for initiating the allergic response. Binding of allergen to receptor-bound IgE leads to cell activation and the release of mediators (such as histamine) responsible for the manifestations of allergy. The same receptor also induces the secretion of important lymphokines..
• Protein Sequence: MAPAMESPTLLCVALLFFAPDGVLAVPQKPKVSLNPPWNRIFKGENVTLTCNGNNFFEVSSTKWFHNGSLSEETNSSLNIVNAKFEDSGEYKCQHQQVNESEPVYLEVFSDWLLLQASAEVVMEGQPLFLRCHGWRNWDVYKVIYYKDGEALKYWYENHNISITNATVEDSGTYYCTGKVWQLDYESEPLNITVIKAPREKYWLQFFIPLLVVILFAVDTGLFISTQQQVTFLLKIKRTRKGFRLLNPHPKPNPKNN

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
46	N-linked_Glycosylation	NRIFKGENVTLTCNG CCCCCCCCEEEEECC	40.52	11531339
67	N-linked_Glycosylation	SSTKWFHNGSLSEET ECCEEEECCCCCCCC	32.07	11531339
75	N-linked_Glycosylation	GSLSEETNSSLNIVN CCCCCCCCCCCEEEE	32.64	UniProtKB CARBOHYD
99	N-linked_Glycosylation	KCQHQQVNESEPVYL EEEEEECCCCCCEEH	42.62	11531339
160	N-linked_Glycosylation	KYWYENHNISITNAT HHEEHHCCEEEEECE	41.08	UniProtKB CARBOHYD
165	N-linked_Glycosylation	NHNISITNATVEDSG HCCEEEEECEEECCC	31.76	11531339
191	N-linked_Glycosylation	DYESEPLNITVIKAP ECCCCCCEEEEEECC	38.30	11531339
202	Phosphorylation	IKAPREKYWLQFFIP EECCHHHHHHHHHHH	13.44	24043423
220	Phosphorylation	VILFAVDTGLFISTQ HHHHHHHCCCCCCCH	29.23	24043423
225	Phosphorylation	VDTGLFISTQQQVTF HHCCCCCCCHHHHHH	16.90	24043423
226	Phosphorylation	DTGLFISTQQQVTFL HCCCCCCCHHHHHHH	26.11	24043423
231	Phosphorylation	ISTQQQVTFLLKIKR CCCHHHHHHHHEEEC	12.29	24043423
241	Acetylation	LKIKRTRKGFRLLNP HEEECCCCCCEECCC	62.88	7370167
251	Acetylation	RLLNPHPKPNPKNN- EECCCCCCCCCCCC-	55.16	7370175

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of FCERA_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 FCERA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KSYK_HUMAN	SYK	physical	9103201
ODPB_HUMAN	PDHB	physical	21988832

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

"The analysis of the human high affinity IgE receptor Fc epsilon Rialpha from multiple crystal forms.";
Garman S.C., Sechi S., Kinet J.P., Jardetzky T.S.;
J. Mol. Biol. 311:1049-1062(2001).
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 26-201, GLYCOSYLATION ATASN-46; ASN-67; ASN-99; ASN-165 AND ASN-191, AND DISULFIDE BONDS.
PubMed: 11531339

"Crystal structure of the human high-affinity IgE receptor.";
Garman S.C., Kinet J.P., Jardetzky T.S.;
Cell 95:951-961(1998).
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 26-201, GLYCOSYLATION ATASN-46; ASN-67 AND ASN-191, AND DISULFIDE BONDS.
PubMed: 9875849