FCGR1_HUMAN - dbPTM
FCGR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FCGR1_HUMAN
UniProt AC P12314
Protein Name High affinity immunoglobulin gamma Fc receptor I
Gene Name FCGR1A
Organism Homo sapiens (Human).
Sequence Length 374
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Stabilized at the cell membrane through interaction with FCER1G.
Protein Description High affinity receptor for the Fc region of immunoglobulins gamma. Functions in both innate and adaptive immune responses..
Protein Sequence MWFLTTLLLWVPVDGQVDTTKAVITLQPPWVSVFQEETVTLHCEVLHLPGSSSTQWFLNGTATQTSTPSYRITSASVNDSGEYRCQRGLSGRSDPIQLEIHRGWLLLQVSSRVFTEGEPLALRCHAWKDKLVYNVLYYRNGKAFKFFHWNSNLTILKTNISHNGTYHCSGMGKHRYTSAGISVTVKELFPAPVLNASVTSPLLEGNLVTLSCETKLLLQRPGLQLYFSFYMGSKTLRGRNTSSEYQILTARREDSGLYWCEAATEDGNVLKRSPELELQVLGLQLPTPVWFHVLFYLAVGIMFLVNTVLWVTIRKELKRKKKWDLEISLDSGHEKKVISSLQEDRHLEEELKCQEQKEEQLQEGVHRKEPQGAT
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
5Phosphorylation---MWFLTTLLLWVP
---CCEEEEEEEECC
13.1127732954
6Phosphorylation--MWFLTTLLLWVPV
--CCEEEEEEEECCC
19.9727732954
19PhosphorylationPVDGQVDTTKAVITL
CCCCCCCCCEEEEEE
31.1927732954
20PhosphorylationVDGQVDTTKAVITLQ
CCCCCCCCEEEEEEC
16.7327732954
59N-linked_GlycosylationSSTQWFLNGTATQTS
CCCEEEECCEEECCC
35.9721965667
73PhosphorylationSTPSYRITSASVNDS
CCCCEEEEEEEECCC
14.83-
74PhosphorylationTPSYRITSASVNDSG
CCCEEEEEEEECCCC
19.04-
76PhosphorylationSYRITSASVNDSGEY
CEEEEEEEECCCCCE
22.63-
78N-linked_GlycosylationRITSASVNDSGEYRC
EEEEEEECCCCCEEE
34.9221965667
133PhosphorylationAWKDKLVYNVLYYRN
ECCCCEEEEEEEEEC
15.2522817900
137PhosphorylationKLVYNVLYYRNGKAF
CEEEEEEEEECCEEE
8.97-
138PhosphorylationLVYNVLYYRNGKAFK
EEEEEEEEECCEEEE
8.0822817900
152N-linked_GlycosylationKFFHWNSNLTILKTN
EEEEECCCEEEEEEE
37.6821965667
159N-linked_GlycosylationNLTILKTNISHNGTY
CEEEEEEEECCCCEE
31.9821965667
163N-linked_GlycosylationLKTNISHNGTYHCSG
EEEEECCCCEEEECC
37.4021965667
195N-linked_GlycosylationLFPAPVLNASVTSPL
HCCCCCCCEECCCCC
30.3321965667
209PhosphorylationLLEGNLVTLSCETKL
CCCCCEEEEEEEHHH
19.0022468782
211PhosphorylationEGNLVTLSCETKLLL
CCCEEEEEEEHHHHH
10.6722468782
240N-linked_GlycosylationSKTLRGRNTSSEYQI
CCEECCCCCCCCEEE
47.32UniProtKB CARBOHYD
328PhosphorylationKKWDLEISLDSGHEK
CCCCEEEECCCCCHH
19.4227251275
331PhosphorylationDLEISLDSGHEKKVI
CEEEECCCCCHHHHH
47.5524247654
335AcetylationSLDSGHEKKVISSLQ
ECCCCCHHHHHHHHH
46.8220167786
339PhosphorylationGHEKKVISSLQEDRH
CCHHHHHHHHHHHHH
28.1627251275
340PhosphorylationHEKKVISSLQEDRHL
CHHHHHHHHHHHHHH
23.9728450419

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 FCGR1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FCGR1_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 FCGR1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FCAR_HUMANFCARphysical
8530370
HCK_HUMANHCKphysical
8064233
LAT_HUMANLATphysical
10781611
ITIH2_HUMANITIH2physical
28514442
PCD17_HUMANPCDH17physical
28514442
PCD12_HUMANPCDH12physical
28514442
FREM2_HUMANFREM2physical
28514442
PCDH7_HUMANPCDH7physical
28514442
MRCKA_HUMANCDC42BPAphysical
28514442
ULBP3_HUMANULBP3physical
28514442
ACAD8_HUMANACAD8physical
28514442
FRAS1_HUMANFRAS1physical
28514442
SNTB2_HUMANSNTB2physical
28514442
PCD20_HUMANPCDH20physical
28514442

Drug and Disease Associations
Kegg Disease
H00003 Acute myeloid leukemia (AML)
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 FCGR1_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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-78, 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-133 AND TYR-138, ANDMASS SPECTROMETRY.

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