GBRA4_HUMAN - dbPTM
GBRA4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GBRA4_HUMAN
UniProt AC P48169
Protein Name Gamma-aminobutyric acid receptor subunit alpha-4
Gene Name GABRA4
Organism Homo sapiens (Human).
Sequence Length 554
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 MVSAKKVPAIALSAGVSFALLRFLCLAVCLNESPGQNQKEEKLCTENFTRILDSLLDGYDNRLRPGFGGPVTEVKTDIYVTSFGPVSDVEMEYTMDVFFRQTWIDKRLKYDGPIEILRLNNMMVTKVWTPDTFFRNGKKSVSHNMTAPNKLFRIMRNGTILYTMRLTISAECPMRLVDFPMDGHACPLKFGSYAYPKSEMIYTWTKGPEKSVEVPKESSSLVQYDLIGQTVSSETIKSITGEYIVMTVYFHLRRKMGYFMIQTYIPCIMTVILSQVSFWINKESVPARTVFGITTVLTMTTLSISARHSLPKVSYATAMDWFIAVCFAFVFSALIEFAAVNYFTNIQMEKAKRKTSKPPQEVPAAPVQREKHPEAPLQNTNANLNMRKRTNALVHSESDVGNRTEVGNHSSKSSTVVQESSKGTPRSYLASSPNPFSRANAAETISAARALPSASPTSIRTGYMPRKASVGSASTRHVFGSRLQRIKTTVNTIGATGKLSATPPPSAPPPSGSGTSKIDKYARILFPVTFGAFNMVYWVVYLSKDTMEKSESLM
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
47N-linked_GlycosylationEEKLCTENFTRILDS
HHHHHHHHHHHHHHH		25.99UniProtKB CARBOHYD
76PhosphorylationGPVTEVKTDIYVTSF
CCCCEEEEEEEEEEE		32.57-
79PhosphorylationTEVKTDIYVTSFGPV
CEEEEEEEEEEECCC		10.65-
110PhosphorylationWIDKRLKYDGPIEIL
HHCHHCCCCCCEEEE		30.6226074081
125PhosphorylationRLNNMMVTKVWTPDT
EECCCEEEEEECCCC		11.2826074081
140PhosphorylationFFRNGKKSVSHNMTA
CCCCCCCCCCCCCCC		32.1322115753
142PhosphorylationRNGKKSVSHNMTAPN
CCCCCCCCCCCCCCC		19.0822115753
144N-linked_GlycosylationGKKSVSHNMTAPNKL
CCCCCCCCCCCCCHH		23.22UniProtKB CARBOHYD
146PhosphorylationKSVSHNMTAPNKLFR
CCCCCCCCCCCHHHH		44.2622115753
157N-linked_GlycosylationKLFRIMRNGTILYTM
HHHHHHCCCEEEEEE		34.28UniProtKB CARBOHYD
169PhosphorylationYTMRLTISAECPMRL
EEEEEEEEEECCEEE		16.8728509920
202PhosphorylationYPKSEMIYTWTKGPE
ECCHHEEEEEECCCC		8.56-
218PhosphorylationSVEVPKESSSLVQYD
CEECCCCCCCCEEEE		31.2130576142
233PhosphorylationLIGQTVSSETIKSIT
ECCCCCCHHHHHHHC		34.1330576142
235PhosphorylationGQTVSSETIKSITGE
CCCCCHHHHHHHCCC		35.3430576142
238PhosphorylationVSSETIKSITGEYIV
CCHHHHHHHCCCEEE		22.8725072903
240PhosphorylationSETIKSITGEYIVMT
HHHHHHHCCCEEEEE		30.9325072903
243PhosphorylationIKSITGEYIVMTVYF
HHHHCCCEEEEEEHH		10.5225072903
247PhosphorylationTGEYIVMTVYFHLRR
CCCEEEEEEHHHHHH		10.9325072903
249PhosphorylationEYIVMTVYFHLRRKM
CEEEEEEHHHHHHHH		3.9825072903
289PhosphorylationKESVPARTVFGITTV
CCCCCHHHHCCEEEE		23.4630206219
294PhosphorylationARTVFGITTVLTMTT
HHHHCCEEEEEEEHH		15.9527732954
295PhosphorylationRTVFGITTVLTMTTL
HHHCCEEEEEEEHHC		16.1727732954
298PhosphorylationFGITTVLTMTTLSIS
CCEEEEEEEHHCCHH		14.2427732954
300PhosphorylationITTVLTMTTLSISAR
EEEEEEEHHCCHHHH		21.2527732954
301PhosphorylationTTVLTMTTLSISARH
EEEEEEHHCCHHHHC		14.0027732954
303PhosphorylationVLTMTTLSISARHSL
EEEEHHCCHHHHCCC		16.6527732954
305PhosphorylationTMTTLSISARHSLPK
EEHHCCHHHHCCCCC		18.8427732954
309PhosphorylationLSISARHSLPKVSYA
CCHHHHCCCCCCCHH		40.5929449344
380PhosphorylationPEAPLQNTNANLNMR
CCCCCCCCCCCCCHH		23.8126091039
410PhosphorylationRTEVGNHSSKSSTVV
CCEECCCCCCCCCEE		43.3824719451
411PhosphorylationTEVGNHSSKSSTVVQ
CEECCCCCCCCCEEE		29.0724719451
414PhosphorylationGNHSSKSSTVVQESS
CCCCCCCCCEEECCC		29.02-
427PhosphorylationSSKGTPRSYLASSPN
CCCCCCHHHHCCCCC		26.2129116813
428PhosphorylationSKGTPRSYLASSPNP
CCCCCHHHHCCCCCC		13.9429978859
431PhosphorylationTPRSYLASSPNPFSR
CCHHHHCCCCCCCCC		43.6729978859
432PhosphorylationPRSYLASSPNPFSRA
CHHHHCCCCCCCCCC		24.0829116813
437PhosphorylationASSPNPFSRANAAET
CCCCCCCCCCCHHHH		31.5730576142
444PhosphorylationSRANAAETISAARAL
CCCCHHHHHHHHHHC		18.5930624053
446PhosphorylationANAAETISAARALPS
CCHHHHHHHHHHCCC		24.2430576142
455PhosphorylationARALPSASPTSIRTG
HHHCCCCCCCCCCCC		32.8024076635
458PhosphorylationLPSASPTSIRTGYMP
CCCCCCCCCCCCCCC		17.2922985185
474PhosphorylationKASVGSASTRHVFGS
CCCCCCHHHHHHHHH		27.8922817900
475PhosphorylationASVGSASTRHVFGSR
CCCCCHHHHHHHHHH		25.2221712546
481PhosphorylationSTRHVFGSRLQRIKT
HHHHHHHHHHHHHEE		20.5321712546
502PhosphorylationATGKLSATPPPSAPP
CCCCCCCCCCCCCCC		32.7124260401
515PhosphorylationPPPSGSGTSKIDKYA
CCCCCCCCCHHCCCH		28.6624260401
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 GBRA4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GBRA4_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 GBRA4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
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
D00058 Gamma-Aminobutyric acid (JAN); Gammalon (TN)
D00225 Alprazolam (JP16/USP/INN); Xanax (TN)
D00267 Chlordiazepoxide (JP16/USP/INN); Libritabs (TN)
D00280 Clonazepam (JP16/USP/INN); Klonopin (TN)
D00293 Diazepam (JP16/USP/INN); Diastat (TN); Valium (TN)
D00311 Estazolam (JP16/USAN/INN); ProSom (TN)
D00329 Flurazepam (JAN/INN); Insumin (TN)
D00331 Furosemide (JP16/USP/INN); Frusemide; Lasix (TN)
D00365 Lorazepam (JP16/USP/INN); Ativan (TN)
D00370 Temazepam (USP/INN); Restoril (TN)
D00376 Meprobamate (JAN/USP/INN); Equanil (TN); Miltown (TN)
D00387 Triazolam (JAN/USP/INN); Halcion (TN)
D00430 Secobarbital (USP/INN); Seconal (TN)
D00457 Quazepam (JAN/USP/INN); Doral (TN)
D00470 Prazepam (JP16/USAN/INN); Centrax (TN)
D00499 Pentobarbital (USP/INN); Nembutal (TN)
D00500 Pentobarbital sodium (JAN/USP); Nembutal sodium (TN)
D00506 Phenobarbital (JP16/USP/INN); Luminal (TN)
D00531 Nitrazepam (JP16/USAN/INN); Benzalin (TN); Nitrazepam (TN)
D00532 Glutethimide (JAN/INN); Doriden (TN)
D00549 Propofol (JAN/USAN/INN); Diprivan (TN)
D00550 Midazolam (JAN/USP/INN); Dormicum (TN); Buccolam (TN)
D00555 Amobarbital (JP16/INN); Isomytal (TN)
D00557 Methaqualone (JAN/USAN/INN)
D00693 Chlordiazepoxide hydrochloride (JAN/USP); Librium (TN)
D00694 Clorazepate dipotassium (JP16/USP); Tranxene (TN)
D00695 Flurazepam hydrochloride (USP); Flurazepam dihydrochloride; Dalmane (TN)
D00696 Midazolam hydrochloride (USAN); Versed (TN)
D00697 Flumazenil (JAN/USP/INN); Romazicon (TN)
D00700 Mephobarbital (JAN/USP); Methylphenobarbital (INN); Mebaral (TN)
D00701 Phenobarbital sodium (JAN/USP/INN); Luminal sodium (TN)
D00706 Zolpidem tartrate (JP16/USAN); Ambien (TN); Intermezzo (TN)
D00713 Thiamylal sodium (JP16); Surital (TN)
D00714 Thiopental sodium (JP16/USP/INN); Pentothal (TN)
D01071 Hexobarbital (JAN/INN)
D01230 Flunitrazepam (JP16/USAN/INN); Rohypnol (TN)
D01245 Bromazepam (JP16/USAN/INN); Lectopam (TN)
D01253 Clobazam (JAN/USAN/INN); Mystan (TN); Onfi (TN)
D01254 Tofisopam (JP16/INN); Emandaxin (TN)
D01268 Cloxazolam (JP16/INN); Sepazon (TN)
D01278 Oxazolam (JP16/INN); Serenal (TN)
D01279 Flutoprazepam (JP16/INN); Restas (TN)
D01286 Flutazolam (JAN/INN); Coreminal (TN)
D01292 Medazepam (JP16/INN); Pamnace (TN)
D01293 Ethyl loflazepate (JAN/INN); Meilax (TN)
D01310 Secobarbital sodium (JAN/USP); Seconal sodium (TN)
D01316 Mexazolam (JAN/INN); Melex (TN)
D01328 Clotiazepam (JP16/INN); Rize (TN)
D01354 Fludiazepam (JP16/INN); Erispan (TN)
D01372 Zopiclone (JAN/INN); Amoban (TN); Zopiclone (TN)
D01408 Flurazepam hydrochloride (JP16); Flurazepam monohydrochloride; Dalmate (TN)
D01514 Etizolam (JP16/INN); Sedekopan (TN)
D01564 Rilmazafone hydrochloride hydrate (JAN); Rilmazafone hydrochloride dihydrate; Rilmazafone hydrochlor
D01593 Nimetazepam (JAN/INN); Erimin (TN)
D01657 Lormetazepam (JAN/USAN/INN); Loramet (TN)
D01740 Barbital (JP16/INN); Barbital (TN)
D01744 Brotizolam (JP16/USAN/INN); Lendormin (TN)
D01758 Haloxazolam (JP16/INN); Somelin (TN)
D02252 Amobarbital sodium (JAN/USP); Amytal sodium (TN)
D02253 Pentobarbital calcium (JP16); Ravona (TN)
D02283 Iomazenil (123I) (JAN/INN); Benzodine (TN)
D02594 Abecarnil (INN)
D02616 Pagoclone (USAN/INN); Bextra (TN)
D02617 Ocinaplon (USAN/INN)
D02624 Eszopiclone (JAN/USAN/INN); Estorra (TN); Lunesta (TN)
D02833 Alpidem (USAN/INN)
D03155 Bretazenil (USAN/INN)
D03562 Clorazepate monopotassium (USAN)
D03737 Dextofisopam (USAN/INN)
D04257 Fospropofol disodium (USAN); Aquavan (TN); Lusedra (TN)
D04282 Gaboxadol (USAN/INN)
D04300 Ganaxolone (USAN/INN)
D04721 Levotofisopam (USAN/INN)
D04882 Medazepam hydrochloride (USAN); Nobrium (TN)
D05028 Midazolam maleate (USAN)
D06106 Thiamylal
D07326 Loprazolam (INN); Dormonoct (TN)
D07409 Pentetrazol (INN); Pentylenetetrazol; Coryvet [veterinary] (TN)
D07784 Delorazepam (INN); Dadumir (TN)
D07999 Sodium furosemide; Frosemide sodium; Lasix (TN)
D08001 Furosemide diolamine; Furosemide diethanolamine salt; Nuriban (TN)
D08145 Loprazolam mesilate; Loprazolam mesylate; Loprazolam methanesulfonate; Havlane (TN)
D08283 Nordazepam (INN); Calmday (TN)
D08356 Phenobarbital diethylamine; Gratusminal (TN)
D08481 Rilmazafone (INN)
D08507 Sarmazenil (INN); Sarmazol [veterinary] (TN)
D08690 Zolpidem (INN); Sanval (TN)
D08840 Adipiplon (USAN)
D10194 Remimazolam besilate (JAN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GBRA4_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction.";
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
Mol. Cell. Proteomics 6:1952-1967(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140 AND SER-142, ANDMASS SPECTROMETRY.

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