GBRB2_HUMAN - dbPTM
GBRB2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GBRB2_HUMAN
UniProt AC P47870
Protein Name Gamma-aminobutyric acid receptor subunit beta-2
Gene Name GABRB2
Organism Homo sapiens (Human).
Sequence Length 512
Subcellular Localization Cell junction, synapse, postsynaptic cell membrane
Multi-pass membrane protein. Cell membrane
Multi-pass membrane protein . Cytoplasmic vesicle membrane .
Protein Description Component of the heteropentameric receptor for GABA, the major inhibitory neurotransmitter in the vertebrate brain. Functions also as histamine receptor and mediates cellular responses to histamine. Functions as receptor for diazepines and various anesthetics, such as pentobarbital; these are bound at a separate allosteric effector binding site. Functions as ligand-gated chloride channel..
Protein Sequence MWRVRKRGYFGIWSFPLIIAAVCAQSVNDPSNMSLVKETVDRLLKGYDIRLRPDFGGPPVAVGMNIDIASIDMVSEVNMDYTLTMYFQQAWRDKRLSYNVIPLNLTLDNRVADQLWVPDTYFLNDKKSFVHGVTVKNRMIRLHPDGTVLYGLRITTTAACMMDLRRYPLDEQNCTLEIESYGYTTDDIEFYWRGDDNAVTGVTKIELPQFSIVDYKLITKKVVFSTGSYPRLSLSFKLKRNIGYFILQTYMPSILITILSWVSFWINYDASAARVALGITTVLTMTTINTHLRETLPKIPYVKAIDMYLMGCFVFVFMALLEYALVNYIFFGRGPQRQKKAAEKAASANNEKMRLDVNKIFYKDIKQNGTQYRSLWDPTGNLSPTRRTTNYDFSLYTMDPHENILLSTLEIKNEMATSEAVMGLGDPRSTMLAYDASSIQYRKAGLPRHSFGRNALERHVAQKKSRLRRRASQLKITIPDLTDVNAIDRWSRIFFPVVFSFFNIVYWLYYVN
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
32N-linked_GlycosylationQSVNDPSNMSLVKET
HHCCCCCHHHHHHHH
29.47UniProtKB CARBOHYD
45UbiquitinationETVDRLLKGYDIRLR
HHHHHHHCCCCEEEC
61.0822817900
98PhosphorylationWRDKRLSYNVIPLNL
HHCCCCCEEEEECEE
20.3125884760
104N-linked_GlycosylationSYNVIPLNLTLDNRV
CEEEEECEEEECCCH
26.14UniProtKB CARBOHYD
126UbiquitinationDTYFLNDKKSFVHGV
CEEECCCCCCEEEEE
49.6022505724
127UbiquitinationTYFLNDKKSFVHGVT
EEECCCCCCEEEEEE
52.5723503661
157PhosphorylationYGLRITTTAACMMDL
EEEEEEHHHHHHHHH
12.0124260401
173N-linked_GlycosylationRYPLDEQNCTLEIES
CCCCCCCCCEEEEEE
20.77UniProtKB CARBOHYD
226PhosphorylationTKKVVFSTGSYPRLS
EEEEEEECCCCCCEE
20.7723532336
233PhosphorylationTGSYPRLSLSFKLKR
CCCCCCEEEEEECHH
24.2123090842
235PhosphorylationSYPRLSLSFKLKRNI
CCCCEEEEEECHHHC
19.5724719451
308PhosphorylationYVKAIDMYLMGCFVF
HHHHHHHHHHHHHHH
6.9818083107
347PhosphorylationKAAEKAASANNEKMR
HHHHHHHHCCCHHHE
36.07-
352UbiquitinationAASANNEKMRLDVNK
HHHCCCHHHEECHHH
31.2930230243
362PhosphorylationLDVNKIFYKDIKQNG
ECHHHHHHHHHHHCC
15.95-
370PhosphorylationKDIKQNGTQYRSLWD
HHHHHCCCEEEECCC
29.9424719451
372PhosphorylationIKQNGTQYRSLWDPT
HHHCCCEEEECCCCC
11.2924719451
389PhosphorylationLSPTRRTTNYDFSLY
CCCCCCCCCCCEEEE
29.9419763268
434PhosphorylationPRSTMLAYDASSIQY
CHHHHEEEEHHHHHH
14.211334482
441PhosphorylationYDASSIQYRKAGLPR
EEHHHHHHHHCCCCC
16.65-
472PhosphorylationSRLRRRASQLKITIP
HHHHHHHHHCCCCCC
33.951334482

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
434SPhosphorylationKinasePKC_GROUP-PhosphoELM
472SPhosphorylationKinasePKC-FAMILY-GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GBRB2_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 GBRB2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRAK2_HUMANTRAK2physical
12034717
GBRB3_HUMANGABRB3physical
28514442
ARHGP_HUMANARHGEF25physical
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
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)
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)
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 GBRB2_HUMAN

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Related Literatures of Post-Translational Modification
Ubiquitylation
ReferencePubMed
"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry.";
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
Proteomics 7:868-874(2007).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-45, AND MASSSPECTROMETRY.

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