FCAR_HUMAN - dbPTM
FCAR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FCAR_HUMAN
UniProt AC P24071
Protein Name Immunoglobulin alpha Fc receptor
Gene Name FCAR
Organism Homo sapiens (Human).
Sequence Length 287
Subcellular Localization Isoform A.1: Cell membrane
Single-pass type I membrane protein.
Isoform A.2: Cell membrane
Single-pass type I membrane protein.
Isoform A.3: Cell membrane
Single-pass type I membrane protein.
Isoform B: Secreted.
Isoform B-delta-S2: Secreted.
Protein Description Binds to the Fc region of immunoglobulins alpha. Mediates several functions including cytokine production..
Protein Sequence MDPKQTTLLCLVLCLGQRIQAQEGDFPMPFISAKSSPVIPLDGSVKIQCQAIREAYLTQLMIIKNSTYREIGRRLKFWNETDPEFVIDHMDANKAGRYQCQYRIGHYRFRYSDTLELVVTGLYGKPFLSADRGLVLMPGENISLTCSSAHIPFDRFSLAKEGELSLPQHQSGEHPANFSLGPVDLNVSGIYRCYGWYNRSPYLWSFPSNALELVVTDSIHQDYTTQNLIRMAVAGLVLVALLAILVENWHSHTALNKEASADVAEPSWSQQMCQPGLTFARTPSVCK
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 Orthologous
Protein Cluster
44PhosphorylationPVIPLDGSVKIQCQA
CEECCCCCEEEEHHH
21.6522210691
56PhosphorylationCQAIREAYLTQLMII
HHHHHHHHHHHHHHC
12.9119664995
58PhosphorylationAIREAYLTQLMIIKN
HHHHHHHHHHHHCCC
13.6429978859
65N-linked_GlycosylationTQLMIIKNSTYREIG
HHHHHCCCCCHHHHH
29.22UniProtKB CARBOHYD
66PhosphorylationQLMIIKNSTYREIGR
HHHHCCCCCHHHHHH
23.0922210691
67PhosphorylationLMIIKNSTYREIGRR
HHHCCCCCHHHHHHH
35.6729978859
68PhosphorylationMIIKNSTYREIGRRL
HHCCCCCHHHHHHHH
13.1829978859
79N-linked_GlycosylationGRRLKFWNETDPEFV
HHHHCCCCCCCCCCE
45.48UniProtKB CARBOHYD
141N-linked_GlycosylationLVLMPGENISLTCSS
EEEECCCCEEEEEEC
34.7612768205
177N-linked_GlycosylationQSGEHPANFSLGPVD
CCCCCCCCCEECCCC
31.3312768205
186N-linked_GlycosylationSLGPVDLNVSGIYRC
EECCCCCCCCCEEEE
22.80UniProtKB CARBOHYD
198N-linked_GlycosylationYRCYGWYNRSPYLWS
EEEECCCCCCCEEEE
31.29UniProtKB CARBOHYD
223Nitrated tyrosineTDSIHQDYTTQNLIR
CCCCCCCCHHHHHHH
12.71-
223NitrationTDSIHQDYTTQNLIR
CCCCCCCCHHHHHHH
12.71-

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 FCAR_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FCAR_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 FCAR_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FCGR1_HUMANFCGR1Aphysical
8530370
LYN_HUMANLYNphysical
9427690
FCGR1_HUMANFCGR1Aphysical
16517729
HUTH_HUMANHALphysical
26186194
EFR3B_HUMANEFR3Bphysical
26186194
FCERG_HUMANFCER1Gphysical
15096494
EFR3B_HUMANEFR3Bphysical
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.
Regulatory Network of FCAR_HUMAN

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Related Literatures of Post-Translational Modification
Nitration
ReferencePubMed
"The human pituitary nitroproteome: detection of nitrotyrosyl-proteinswith two-dimensional Western blotting, and amino acid sequencedetermination with mass spectrometry.";
Zhan X., Desiderio D.M.;
Biochem. Biophys. Res. Commun. 325:1180-1186(2004).
Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-223, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-56, AND MASSSPECTROMETRY.

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