Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
GABRB1 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
GABRB1 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. Belongs to the ligand-gated ion channel (TC 1.A.9) family. Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily. GABRB1 sub-subfamily. Note: This description may include information from UniProtKB.
Protein type: Transporter; Membrane protein, integral; Channel, ligand-gated; Channel, chloride; Transporter, ion channel; Membrane protein, multi-pass
Cellular Component: postsynaptic membrane; integral to plasma membrane; plasma membrane; cell junction
Molecular Function: chloride channel activity; GABA-A receptor activity; extracellular ligand-gated ion channel activity
Biological Process: synaptic transmission; transport; signal transduction; transmembrane transport
Reference #:  P18505 (UniProtKB)
Alt. Names/Synonyms: GABA(A) receptor subunit beta-1; GABRB1; gamma-aminobutyric acid (GABA) A receptor, beta 1; Gamma-aminobutyric acid receptor subunit beta-1; GBRB1
Gene Symbols: GABRB1
Molecular weight: 54,235 Da
Basal Isoelectric point: 8.88  Predict pI for various phosphorylation states
Select Structure to View Below

GABRB1

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  Source  |  InnateDB  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
1 2 K46-u ETVDRLLkGYDIRLR
1 0 T227 SKKVEFTTGAYPRLS
1 0 Y230 VEFTTGAYPRLSLSF
1 0 T287 ITTVLTMTTISTHLR
1 0 T288 TTVLTMTTISTHLRE
1 0 S290 VLTMTTISTHLRETL
1 0 T291 LTMTTISTHLRETLP
1 0 S396 DPKATMYSYDSASIQ
1 0 S399 ATMYSYDSASIQYRK
1 1 S401 MYSYDSASIQYRKPL
1 0 Y404 YDSASIQYRKPLSSR
3 0 S409 IQYRKPLSSREAYGR
1 0 S410 QYRKPLSSREAYGRA
6 0 S434 GRIRRRASQLKVKIP
  mouse

 
K46-u ETVDRLLkGYDIRLR
T227-p SKKVEFTtGAyPRLS
Y230-p VEFTtGAyPRLSLSF
T287-p ITTVLTMttIstHLR
T288-p TTVLTMttIstHLRE
S290-p VLTMttIstHLRETL
T291-p LTMttIstHLRETLP
S396-p DPKATMYsYDsAsIQ
S399-p ATMYsYDsAsIQyRK
S401-p MYsYDsAsIQyRKPL
Y404-p YDsAsIQyRKPLssR
S409-p IQyRKPLssREGFGR
S410-p QyRKPLssREGFGRG
S434-p GRIRRRAsQLKVKIP
  rat

 
K46 ETVDRLLKGYDIRLR
T227 SKKVEFTTGAYPRLS
Y230 VEFTTGAYPRLSLSF
T287 ITTVLTMTTISTHLR
T288 TTVLTMTTISTHLRE
S290 VLTMTTISTHLRETL
T291 LTMTTISTHLRETLP
S396 DPKATMYSYDSASIQ
S399 ATMYSYDSASIQYRK
S401 MYSYDSASIQYRKPL
Y404 YDSASIQYRKPLSSR
S409 IQYRKPLSSREGFGR
S410 QYRKPLSSREGFGRG
S434-p GRIRRRAsQLKVKIP
  cow

 
K46 ETVDRLLKGYDIRLR
T227 SKKVEFTTGAYPRLS
Y230 VEFTTGAYPRLSLSF
T287 ITTVLTMTTISTHLR
T288 TTVLTMTTISTHLRE
S290 VLTMTTISTHLRETL
T291 LTMTTISTHLRETLP
S396 DPKTTMYSYDSASIQ
S399 TTMYSYDSASIQYRK
S401 MYSYDSASIQYRKPM
Y404 YDSASIQYRKPMSSR
S409 IQYRKPMSSREGYGR
S410 QYRKPMSSREGYGRA
S434 GRIRRRASQLKVKIP
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.