GBRE_HUMAN - dbPTM
GBRE_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GBRE_HUMAN
UniProt AC P78334
Protein Name Gamma-aminobutyric acid receptor subunit epsilon
Gene Name GABRE
Organism Homo sapiens (Human).
Sequence Length 506
Subcellular Localization Cell junction, synapse, postsynaptic cell membrane
Multi-pass membrane protein. Cell membrane
Multi-pass membrane protein.
Protein Description GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel..
Protein Sequence MLSKVLPVLLGILLILQSRVEGPQTESKNEASSRDVVYGPQPQPLENQLLSEETKSTETETGSRVGKLPEASRILNTILSNYDHKLRPGIGEKPTVVTVEISVNSLGPLSILDMEYTIDIIFSQTWYDERLCYNDTFESLVLNGNVVSQLWIPDTFFRNSKRTHEHEITMPNQMVRIYKDGKVLYTIRMTIDAGCSLHMLRFPMDSHSCPLSFSSFSYPENEMIYKWENFKLEINEKNSWKLFQFDFTGVSNKTEIITTPVGDFMVMTIFFNVSRRFGYVAFQNYVPSSVTTMLSWVSFWIKTESAPARTSLGITSVLTMTTLGTFSRKNFPRVSYITALDFYIAICFVFCFCALLEFAVLNFLIYNQTKAHASPKLRHPRINSRAHARTRARSRACARQHQEAFVCQIVTTEGSDGEERPSCSAQQPPSPGSPEGPRSLCSKLACCEWCKRFKKYFCMVPDCEGSTWQQGRLCIHVYRLDNYSRVVFPVTFFFFNVLYWLVCLNL
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
82PhosphorylationLNTILSNYDHKLRPG
HHHHHHHCCCCCCCC
18.9529978859
134N-linked_GlycosylationYDERLCYNDTFESLV
CCCCEECCCCCHHHE
40.63UniProtKB CARBOHYD
163PhosphorylationFFRNSKRTHEHEITM
CCCCCCCCEEEEECC
35.04-
169PhosphorylationRTHEHEITMPNQMVR
CCEEEEECCCCCEEE
24.4824719451
178PhosphorylationPNQMVRIYKDGKVLY
CCCEEEEEECCEEEE
7.77-
185PhosphorylationYKDGKVLYTIRMTID
EECCEEEEEEEEEEE
11.7826552605
186PhosphorylationKDGKVLYTIRMTIDA
ECCEEEEEEEEEEEC
9.6524719451
190PhosphorylationVLYTIRMTIDAGCSL
EEEEEEEEEECCCEE
13.0726552605
196PhosphorylationMTIDAGCSLHMLRFP
EEEECCCEEEEEECC
22.0126552605
206PhosphorylationMLRFPMDSHSCPLSF
EEECCCCCCCCCCCC
15.8525850435
208PhosphorylationRFPMDSHSCPLSFSS
ECCCCCCCCCCCCCC
22.7525850435
212PhosphorylationDSHSCPLSFSSFSYP
CCCCCCCCCCCCCCC
14.2825850435
214PhosphorylationHSCPLSFSSFSYPEN
CCCCCCCCCCCCCCC
27.3925850435
215PhosphorylationSCPLSFSSFSYPENE
CCCCCCCCCCCCCCC
19.0525850435
217PhosphorylationPLSFSSFSYPENEMI
CCCCCCCCCCCCCEE
41.5525850435
218PhosphorylationLSFSSFSYPENEMIY
CCCCCCCCCCCCEEE
16.7425850435
225PhosphorylationYPENEMIYKWENFKL
CCCCCEEEEEECEEE
14.5625850435
252N-linked_GlycosylationFDFTGVSNKTEIITT
EEECCCCCCEEEEEE
53.51UniProtKB CARBOHYD
310PhosphorylationTESAPARTSLGITSV
CCCCCCCCCCCCEEE
30.3430576142
322PhosphorylationTSVLTMTTLGTFSRK
EEEEEECCCCCCCCC
16.6230576142

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 GBRE_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GBRE_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 GBRE_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SC11A_HUMANSEC11Aphysical
26186194
LSR_HUMANLSRphysical
26186194
1A02_HUMANHLA-Aphysical
26186194
1A03_HUMANHLA-Aphysical
26186194
1A01_HUMANHLA-Aphysical
26186194
1A26_HUMANHLA-Aphysical
26186194
PIGO_HUMANPIGOphysical
26186194
ALG9_HUMANALG9physical
26186194
GPAA1_HUMANGPAA1physical
26186194
B3A2_HUMANSLC4A2physical
26186194
TMTC3_HUMANTMTC3physical
26186194
CCPG1_HUMANCCPG1physical
26186194
TGO1_HUMANMIA3physical
26186194
HEM3_HUMANHMBSphysical
26186194
STIM1_HUMANSTIM1physical
26186194
TTC17_HUMANTTC17physical
26186194
SPCS2_HUMANSPCS2physical
26186194
POMT1_HUMANPOMT1physical
26186194
S39A6_HUMANSLC39A6physical
26186194
GHITM_HUMANGHITMphysical
26186194
CUX1_HUMANCUX1physical
26186194
CASP_HUMANCUX1physical
26186194
KCNQ5_HUMANKCNQ5physical
26186194
CLCC1_HUMANCLCC1physical
26186194
GRM1A_HUMANGRAMD1Aphysical
26186194
FZD2_HUMANFZD2physical
26186194
CTR2_HUMANSLC7A2physical
26186194
GPHRA_HUMANGPR89Bphysical
26186194
GPHRB_HUMANGPR89Bphysical
26186194
BSCL2_HUMANBSCL2physical
26186194
ERMP1_HUMANERMP1physical
26186194
FZD6_HUMANFZD6physical
26186194
CNNM1_HUMANCNNM1physical
26186194
PIGM_HUMANPIGMphysical
26186194
TMED7_HUMANTMED7physical
26186194
ABCB8_HUMANABCB8physical
26186194
KCNJ8_HUMANKCNJ8physical
26186194
EPHB4_HUMANEPHB4physical
26186194
GP1BB_HUMANGP1BBphysical
26186194
S47A1_HUMANSLC47A1physical
26186194
ENTP4_HUMANENTPD4physical
26186194
SGPP1_HUMANSGPP1physical
26186194
F189B_HUMANFAM189Bphysical
26186194
CJ035_HUMANC10orf35physical
26186194
LMF2_HUMANLMF2physical
26186194
FADS1_HUMANFADS1physical
26186194
HEM3_HUMANHMBSphysical
28514442
ERMP1_HUMANERMP1physical
28514442
ALG9_HUMANALG9physical
28514442
KCNQ5_HUMANKCNQ5physical
28514442
ENTP4_HUMANENTPD4physical
28514442
EPHB4_HUMANEPHB4physical
28514442
BSCL2_HUMANBSCL2physical
28514442
TTC17_HUMANTTC17physical
28514442
TGO1_HUMANMIA3physical
28514442
GRM1A_HUMANGRAMD1Aphysical
28514442
CTR2_HUMANSLC7A2physical
28514442
GP1BB_HUMANGP1BBphysical
28514442
FADS1_HUMANFADS1physical
28514442
CCPG1_HUMANCCPG1physical
28514442
FZD6_HUMANFZD6physical
28514442
TM39A_HUMANTMEM39Aphysical
28514442
S47A1_HUMANSLC47A1physical
28514442
LMF2_HUMANLMF2physical
28514442
CNNM1_HUMANCNNM1physical
28514442
ABCB8_HUMANABCB8physical
28514442
GPHRA_HUMANGPR89Bphysical
28514442
GPHRB_HUMANGPR89Bphysical
28514442
SGPP1_HUMANSGPP1physical
28514442
CJ035_HUMANC10orf35physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GBRE_HUMAN

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Related Literatures of Post-Translational Modification

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