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Protein

Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1

Gene

GNB1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransducer

Enzyme and pathway databases

ReactomeiR-HSA-1296041 Activation of G protein gated Potassium channels
R-HSA-163359 Glucagon signaling in metabolic regulation
R-HSA-202040 G-protein activation
R-HSA-2485179 Activation of the phototransduction cascade
R-HSA-2514859 Inactivation, recovery and regulation of the phototransduction cascade
R-HSA-381676 Glucagon-like Peptide-1 (GLP1) regulates insulin secretion
R-HSA-381753 Olfactory Signaling Pathway
R-HSA-392170 ADP signalling through P2Y purinoceptor 12
R-HSA-392451 G beta:gamma signalling through PI3Kgamma
R-HSA-392851 Prostacyclin signalling through prostacyclin receptor
R-HSA-400042 Adrenaline,noradrenaline inhibits insulin secretion
R-HSA-4086398 Ca2+ pathway
R-HSA-416476 G alpha (q) signalling events
R-HSA-416482 G alpha (12/13) signalling events
R-HSA-418217 G beta:gamma signalling through PLC beta
R-HSA-418555 G alpha (s) signalling events
R-HSA-418592 ADP signalling through P2Y purinoceptor 1
R-HSA-418594 G alpha (i) signalling events
R-HSA-418597 G alpha (z) signalling events
R-HSA-420092 Glucagon-type ligand receptors
R-HSA-428930 Thromboxane signalling through TP receptor
R-HSA-432040 Vasopressin regulates renal water homeostasis via Aquaporins
R-HSA-456926 Thrombin signalling through proteinase activated receptors (PARs)
R-HSA-500657 Presynaptic function of Kainate receptors
R-HSA-6814122 Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding
R-HSA-997272 Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits
SignaLinkiP62873
SIGNORiP62873

Protein family/group databases

TCDBi8.A.92.1.1 the g-protein AlphaBetaGama complex (gpc) family

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Alternative name(s):
Transducin beta chain 1
Gene namesi
Name:GNB1Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000078369.17
HGNCiHGNC:4396 GNB1
MIMi139380 gene
neXtProtiNX_P62873

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Pathology & Biotechi

Involvement in diseasei

Mental retardation, autosomal dominant 42 (MRD42)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of mental retardation, a disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD42 patients manifest global developmental delay commonly accompanied by hypotonia, seizures of various types, ophthalmological manifestations, and poor growth.
See also OMIM:616973
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07827930L → F in MRD42; unknown pathological significance; no effect on protein abundance; no effect on complex formation with gamma subunit; no effect on trimer formation with alpha and gamma subunits; no effect on receptor-driven G protein activation. 1 PublicationCorresponds to variant dbSNP:rs764997309Ensembl.1
Natural variantiVAR_07828052R → G in MRD42; decreases receptor-driven G protein activation; no effect on protein abundance; no effect on complex formation with gamma subunit; decreases trimer formation with alpha and gamma subunit. 1 Publication1
Natural variantiVAR_07828164G → V in MRD42; decreases receptor-driven G protein activation; decreases protein abundance; decreases complex formation with gamma subunit; decreases trimer formation with alpha and gamma subunit. 1 Publication1
Natural variantiVAR_07664476D → E in MRD42. 1 PublicationCorresponds to variant dbSNP:rs869312822EnsemblClinVar.1
Natural variantiVAR_07664376D → G in MRD42. 1 PublicationCorresponds to variant dbSNP:rs869312821EnsemblClinVar.1
Natural variantiVAR_07664577G → S in MRD42. 1 PublicationCorresponds to variant dbSNP:rs758432471EnsemblClinVar.1
Natural variantiVAR_07664678K → R in MRD42. 1 PublicationCorresponds to variant dbSNP:rs869312823EnsemblClinVar.1
Natural variantiVAR_07664780I → N in MRD42; also found in patients with acute lymphoblastic T-cell leukemia; reduces interaction with GNAI2, GNAI3, GNA13 and GNA11; induces activation of PI3K-AKT-mTOR and MAPK pathways. 2 PublicationsCorresponds to variant dbSNP:rs752746786EnsemblClinVar.1
Natural variantiVAR_07664880I → T in MRD42; also found in patient with hematologic malignancies; reduces interaction with GNAI2, GNAI3, GNA13 and GNA11; induces activation of PI3K-AKT-mTOR and MAPK pathways. 2 PublicationsCorresponds to variant dbSNP:rs752746786EnsemblClinVar.1
Natural variantiVAR_07828291H → R in MRD42; unknown pathological significance; no effect on protein abundance; no effect on complex formation with gamma subunit; no effect on trimer formation with apha and gamma subunits; no effect on receptor-driven G protein activation. 1 Publication1
Natural variantiVAR_07828392A → T in MRD42; decreases receptor-driven G protein activation; increases trimer formation with alpha and gamma subunits; no effect on protein abundance; no effect on complex formation with gamma subunit. 1 Publication1
Natural variantiVAR_07828494P → S in MRD42; decreases receptor-driven G protein activation; decreases trimer formation with alpha and gamma subunit; no effect on protein abundance;no effect on complex formation with gamma subunit. 1 Publication1
Natural variantiVAR_07664995L → P in MRD42. 1 PublicationCorresponds to variant dbSNP:rs869312824EnsemblClinVar.1
Natural variantiVAR_07828596R → L in MRD42; decreases receptor-driven G protein activation; decreases trimer formation with alpha and gamma subunit; no effect on protein abundance; no effect on complex formation with gamma subunit. 1 Publication1
Natural variantiVAR_076650101M → V in MRD42. 1 PublicationCorresponds to variant dbSNP:rs869312825EnsemblClinVar.1
Natural variantiVAR_078286106A → T in MRD42; decreases receptor-driven G protein activation; decreases complex formation with gamma subunit; decreases trimer formation with alpha and gamma subunit; no effect on protein abundance. 1 Publication1
Natural variantiVAR_078287118D → G in MRD42; decreases receptor-driven G protein activation; no effect on protein abundance; no effect on complex formation with gamma subunit; no effect on trimer formation with alpha and gamma subunits. 2 Publications1
Natural variantiVAR_076651326A → T in MRD42. 1 PublicationCorresponds to variant dbSNP:rs869312826EnsemblClinVar.1
Natural variantiVAR_078288337K → Q in MRD42; unknown pathological significance; no effect on protein abundance; no effect on complex formation with gamma subunit; no effect on trimer formation with alpha and gamma subunits; no effect on receptor-driven G protein activation. 1 Publication1

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNETi2782
MalaCardsiGNB1
MIMi616973 phenotype
OpenTargetsiENSG00000078369
PharmGKBiPA28776

Chemistry databases

ChEMBLiCHEMBL3883319

Polymorphism and mutation databases

DMDMi51317302

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources2 Publications
ChainiPRO_00001276872 – 340Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1Add BLAST339

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources2 Publications1
Modified residuei2PhosphoserineCombined sources1
Modified residuei266PhosphohistidineBy similarity1

Post-translational modificationi

Phosphorylation at His-266 by NDKB contributes to G protein activation by increasing the high energetic phosphate transfer onto GDP.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP62873
MaxQBiP62873
PaxDbiP62873
PeptideAtlasiP62873
PRIDEiP62873
ProteomicsDBi57441

2D gel databases

OGPiP62873
REPRODUCTION-2DPAGEiIPI00026268

PTM databases

iPTMnetiP62873
PhosphoSitePlusiP62873
SwissPalmiP62873

Expressioni

Gene expression databases

BgeeiENSG00000078369 Expressed in 239 organ(s), highest expression level in putamen
CleanExiHS_GNB1
ExpressionAtlasiP62873 baseline and differential
GenevisibleiP62873 HS

Organism-specific databases

HPAiHPA040736

Interactioni

Subunit structurei

G proteins are composed of 3 units, alpha, beta and gamma. Interacts with ARHGEF18 and RASD2 (PubMed:14512443, PubMed:19255495). The heterodimer formed by GNB1 and GNG2 interacts with ARHGEF5 (PubMed:19713215).3 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi109044, 109 interactors
CORUMiP62873
DIPiDIP-599N
IntActiP62873, 54 interactors
MINTiP62873
STRINGi9606.ENSP00000367869

Structurei

Secondary structure

1340
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP62873
SMRiP62873
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62873

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati53 – 83WD 1Add BLAST31
Repeati95 – 125WD 2Add BLAST31
Repeati141 – 170WD 3Add BLAST30
Repeati182 – 212WD 4Add BLAST31
Repeati224 – 254WD 5Add BLAST31
Repeati268 – 298WD 6Add BLAST31
Repeati310 – 340WD 7Add BLAST31

Sequence similaritiesi

Belongs to the WD repeat G protein beta family.Curated

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG0286 Eukaryota
ENOG410XQUX LUCA
GeneTreeiENSGT00760000119239
HOGENOMiHOG000176356
HOVERGENiHBG000188
InParanoidiP62873
KOiK04536
OMAiTCNVWDT
OrthoDBiEOG091G0A7T
PhylomeDBiP62873
TreeFamiTF106149

Family and domain databases

Gene3Di2.130.10.10, 1 hit
InterProiView protein in InterPro
IPR020472 G-protein_beta_WD-40_rep
IPR001632 Gprotein_B
IPR016346 Guanine_nucleotide-bd_bsu
IPR015943 WD40/YVTN_repeat-like_dom_sf
IPR001680 WD40_repeat
IPR019775 WD40_repeat_CS
IPR017986 WD40_repeat_dom
IPR036322 WD40_repeat_dom_sf
PANTHERiPTHR19850 PTHR19850, 1 hit
PfamiView protein in Pfam
PF00400 WD40, 7 hits
PRINTSiPR00319 GPROTEINB
PR00320 GPROTEINBRPT
SMARTiView protein in SMART
SM00320 WD40, 7 hits
SUPFAMiSSF50978 SSF50978, 1 hit
PROSITEiView protein in PROSITE
PS00678 WD_REPEATS_1, 3 hits
PS50082 WD_REPEATS_2, 6 hits
PS50294 WD_REPEATS_REGION, 1 hit

Sequences (2+)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.iShow all

Isoform 1 (identifier: P62873-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MSELDQLRQE AEQLKNQIRD ARKACADATL SQITNNIDPV GRIQMRTRRT
60 70 80 90 100
LRGHLAKIYA MHWGTDSRLL VSASQDGKLI IWDSYTTNKV HAIPLRSSWV
110 120 130 140 150
MTCAYAPSGN YVACGGLDNI CSIYNLKTRE GNVRVSRELA GHTGYLSCCR
160 170 180 190 200
FLDDNQIVTS SGDTTCALWD IETGQQTTTF TGHTGDVMSL SLAPDTRLFV
210 220 230 240 250
SGACDASAKL WDVREGMCRQ TFTGHESDIN AICFFPNGNA FATGSDDATC
260 270 280 290 300
RLFDLRADQE LMTYSHDNII CGITSVSFSK SGRLLLAGYD DFNCNVWDAL
310 320 330 340
KADRAGVLAG HDNRVSCLGV TDDGMAVATG SWDSFLKIWN
Length:340
Mass (Da):37,377
Last modified:January 23, 2007 - v3
Checksum:i896CBD32D2686598
GO
Isoform 2 (identifier: P62873-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     329-340: TGSWDSFLKIWN → SVLG

Note: No experimental confirmation available.
Show »
Length:332
Mass (Da):36,298
Checksum:iB974CB3B43FEFFC4
GO

Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B1AKQ8B1AKQ8_HUMAN
Guanine nucleotide-binding protein ...
GNB1
107Annotation score:
F6UT28F6UT28_HUMAN
Guanine nucleotide-binding protein ...
GNB1
165Annotation score:
F6X3N5F6X3N5_HUMAN
Guanine nucleotide-binding protein ...
GNB1
163Annotation score:
B3KVK2B3KVK2_HUMAN
Guanine nucleotide-binding protein ...
GNB1
240Annotation score:

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07827930L → F in MRD42; unknown pathological significance; no effect on protein abundance; no effect on complex formation with gamma subunit; no effect on trimer formation with alpha and gamma subunits; no effect on receptor-driven G protein activation. 1 PublicationCorresponds to variant dbSNP:rs764997309Ensembl.1
Natural variantiVAR_07828052R → G in MRD42; decreases receptor-driven G protein activation; no effect on protein abundance; no effect on complex formation with gamma subunit; decreases trimer formation with alpha and gamma subunit. 1 Publication1
Natural variantiVAR_07828164G → V in MRD42; decreases receptor-driven G protein activation; decreases protein abundance; decreases complex formation with gamma subunit; decreases trimer formation with alpha and gamma subunit. 1 Publication1
Natural variantiVAR_07664476D → E in MRD42. 1 PublicationCorresponds to variant dbSNP:rs869312822EnsemblClinVar.1
Natural variantiVAR_07664376D → G in MRD42. 1 PublicationCorresponds to variant dbSNP:rs869312821EnsemblClinVar.1
Natural variantiVAR_07664577G → S in MRD42. 1 PublicationCorresponds to variant dbSNP:rs758432471EnsemblClinVar.1
Natural variantiVAR_07664678K → R in MRD42. 1 PublicationCorresponds to variant dbSNP:rs869312823EnsemblClinVar.1
Natural variantiVAR_07664780I → N in MRD42; also found in patients with acute lymphoblastic T-cell leukemia; reduces interaction with GNAI2, GNAI3, GNA13 and GNA11; induces activation of PI3K-AKT-mTOR and MAPK pathways. 2 PublicationsCorresponds to variant dbSNP:rs752746786EnsemblClinVar.1
Natural variantiVAR_07664880I → T in MRD42; also found in patient with hematologic malignancies; reduces interaction with GNAI2, GNAI3, GNA13 and GNA11; induces activation of PI3K-AKT-mTOR and MAPK pathways. 2 PublicationsCorresponds to variant dbSNP:rs752746786EnsemblClinVar.1
Natural variantiVAR_07828291H → R in MRD42; unknown pathological significance; no effect on protein abundance; no effect on complex formation with gamma subunit; no effect on trimer formation with apha and gamma subunits; no effect on receptor-driven G protein activation. 1 Publication1
Natural variantiVAR_07828392A → T in MRD42; decreases receptor-driven G protein activation; increases trimer formation with alpha and gamma subunits; no effect on protein abundance; no effect on complex formation with gamma subunit. 1 Publication1
Natural variantiVAR_07828494P → S in MRD42; decreases receptor-driven G protein activation; decreases trimer formation with alpha and gamma subunit; no effect on protein abundance;no effect on complex formation with gamma subunit. 1 Publication1
Natural variantiVAR_07664995L → P in MRD42. 1 PublicationCorresponds to variant dbSNP:rs869312824EnsemblClinVar.1
Natural variantiVAR_07828596R → L in MRD42; decreases receptor-driven G protein activation; decreases trimer formation with alpha and gamma subunit; no effect on protein abundance; no effect on complex formation with gamma subunit. 1 Publication1
Natural variantiVAR_076650101M → V in MRD42. 1 PublicationCorresponds to variant dbSNP:rs869312825EnsemblClinVar.1
Natural variantiVAR_078286106A → T in MRD42; decreases receptor-driven G protein activation; decreases complex formation with gamma subunit; decreases trimer formation with alpha and gamma subunit; no effect on protein abundance. 1 Publication1
Natural variantiVAR_078287118D → G in MRD42; decreases receptor-driven G protein activation; no effect on protein abundance; no effect on complex formation with gamma subunit; no effect on trimer formation with alpha and gamma subunits. 2 Publications1
Natural variantiVAR_076651326A → T in MRD42. 1 PublicationCorresponds to variant dbSNP:rs869312826EnsemblClinVar.1
Natural variantiVAR_078288337K → Q in MRD42; unknown pathological significance; no effect on protein abundance; no effect on complex formation with gamma subunit; no effect on trimer formation with alpha and gamma subunits; no effect on receptor-driven G protein activation. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_055232329 – 340TGSWD…LKIWN → SVLG in isoform 2. 1 PublicationAdd BLAST12

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04526 mRNA Translation: CAA28207.1
AF501882 mRNA Translation: AAM15918.1
BT007305 mRNA Translation: AAP35969.1
CR456784 mRNA Translation: CAG33065.1
AL031282 Genomic DNA No translation available.
AL109917 Genomic DNA No translation available.
CH471183 Genomic DNA Translation: EAW56147.1
BC004186 mRNA Translation: AAH04186.1
BC005888 mRNA Translation: AAH05888.1
BC008991 mRNA Translation: AAH08991.1
BC114618 mRNA Translation: AAI14619.1
M36430 mRNA Translation: AAA63265.1
CCDSiCCDS34.1 [P62873-1]
PIRiA24853 RGHUB1
RefSeqiNP_001269467.1, NM_001282538.1
NP_001269468.1, NM_001282539.1 [P62873-1]
NP_002065.1, NM_002074.4 [P62873-1]
XP_016856548.1, XM_017001059.1 [P62873-1]
XP_016856549.1, XM_017001060.1 [P62873-1]
XP_016856550.1, XM_017001061.1 [P62873-1]
UniGeneiHs.430425
Hs.721030

Genome annotation databases

EnsembliENST00000378609; ENSP00000367872; ENSG00000078369 [P62873-1]
ENST00000610897; ENSP00000481878; ENSG00000078369 [P62873-1]
GeneIDi2782
KEGGihsa:2782
UCSCiuc001aif.5 human [P62873-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04526 mRNA Translation: CAA28207.1
AF501882 mRNA Translation: AAM15918.1
BT007305 mRNA Translation: AAP35969.1
CR456784 mRNA Translation: CAG33065.1
AL031282 Genomic DNA No translation available.
AL109917 Genomic DNA No translation available.
CH471183 Genomic DNA Translation: EAW56147.1
BC004186 mRNA Translation: AAH04186.1
BC005888 mRNA Translation: AAH05888.1
BC008991 mRNA Translation: AAH08991.1
BC114618 mRNA Translation: AAI14619.1
M36430 mRNA Translation: AAA63265.1
CCDSiCCDS34.1 [P62873-1]
PIRiA24853 RGHUB1
RefSeqiNP_001269467.1, NM_001282538.1
NP_001269468.1, NM_001282539.1 [P62873-1]
NP_002065.1, NM_002074.4 [P62873-1]
XP_016856548.1, XM_017001059.1 [P62873-1]
XP_016856549.1, XM_017001060.1 [P62873-1]
XP_016856550.1, XM_017001061.1 [P62873-1]
UniGeneiHs.430425
Hs.721030

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4KFMX-ray3.45B1-340[»]
4PNKX-ray2.56B1-340[»]
5HE0X-ray2.56B2-340[»]
5HE1X-ray3.15B2-340[»]
5HE2X-ray2.79B2-340[»]
5HE3X-ray2.74B2-340[»]
5UKKX-ray2.60B2-340[»]
5UKLX-ray2.15B2-340[»]
5UKMX-ray3.03B2-340[»]
5UZ7electron microscopy4.10B2-340[»]
6B3Jelectron microscopy3.30B2-340[»]
6D9Helectron microscopy3.60B2-340[»]
6DDEelectron microscopy3.50B2-340[»]
6DDFelectron microscopy3.50B2-340[»]
6G79electron microscopy3.78B2-340[»]
6GDGelectron microscopy4.11B2-340[»]
ProteinModelPortaliP62873
SMRiP62873
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109044, 109 interactors
CORUMiP62873
DIPiDIP-599N
IntActiP62873, 54 interactors
MINTiP62873
STRINGi9606.ENSP00000367869

Chemistry databases

ChEMBLiCHEMBL3883319

Protein family/group databases

TCDBi8.A.92.1.1 the g-protein AlphaBetaGama complex (gpc) family

PTM databases

iPTMnetiP62873
PhosphoSitePlusiP62873
SwissPalmiP62873

Polymorphism and mutation databases

DMDMi51317302

2D gel databases

OGPiP62873
REPRODUCTION-2DPAGEiIPI00026268

Proteomic databases

EPDiP62873
MaxQBiP62873
PaxDbiP62873
PeptideAtlasiP62873
PRIDEiP62873
ProteomicsDBi57441

Protocols and materials databases

DNASUi2782
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000378609; ENSP00000367872; ENSG00000078369 [P62873-1]
ENST00000610897; ENSP00000481878; ENSG00000078369 [P62873-1]
GeneIDi2782
KEGGihsa:2782
UCSCiuc001aif.5 human [P62873-1]

Organism-specific databases

CTDi2782
DisGeNETi2782
EuPathDBiHostDB:ENSG00000078369.17
GeneCardsiGNB1
HGNCiHGNC:4396 GNB1
HPAiHPA040736
MalaCardsiGNB1
MIMi139380 gene
616973 phenotype
neXtProtiNX_P62873
OpenTargetsiENSG00000078369
PharmGKBiPA28776
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0286 Eukaryota
ENOG410XQUX LUCA
GeneTreeiENSGT00760000119239
HOGENOMiHOG000176356
HOVERGENiHBG000188
InParanoidiP62873
KOiK04536
OMAiTCNVWDT
OrthoDBiEOG091G0A7T
PhylomeDBiP62873
TreeFamiTF106149

Enzyme and pathway databases

ReactomeiR-HSA-1296041 Activation of G protein gated Potassium channels
R-HSA-163359 Glucagon signaling in metabolic regulation
R-HSA-202040 G-protein activation
R-HSA-2485179 Activation of the phototransduction cascade
R-HSA-2514859 Inactivation, recovery and regulation of the phototransduction cascade
R-HSA-381676 Glucagon-like Peptide-1 (GLP1) regulates insulin secretion
R-HSA-381753 Olfactory Signaling Pathway
R-HSA-392170 ADP signalling through P2Y purinoceptor 12
R-HSA-392451 G beta:gamma signalling through PI3Kgamma
R-HSA-392851 Prostacyclin signalling through prostacyclin receptor
R-HSA-400042 Adrenaline,noradrenaline inhibits insulin secretion
R-HSA-4086398 Ca2+ pathway
R-HSA-416476 G alpha (q) signalling events
R-HSA-416482 G alpha (12/13) signalling events
R-HSA-418217 G beta:gamma signalling through PLC beta
R-HSA-418555 G alpha (s) signalling events
R-HSA-418592 ADP signalling through P2Y purinoceptor 1
R-HSA-418594 G alpha (i) signalling events
R-HSA-418597 G alpha (z) signalling events
R-HSA-420092 Glucagon-type ligand receptors
R-HSA-428930 Thromboxane signalling through TP receptor
R-HSA-432040 Vasopressin regulates renal water homeostasis via Aquaporins
R-HSA-456926 Thrombin signalling through proteinase activated receptors (PARs)
R-HSA-500657 Presynaptic function of Kainate receptors
R-HSA-6814122 Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding
R-HSA-997272 Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits
SignaLinkiP62873
SIGNORiP62873

Miscellaneous databases

ChiTaRSiGNB1 human
EvolutionaryTraceiP62873
GeneWikiiGNB1
GenomeRNAii2782
PROiPR:P62873
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000078369 Expressed in 239 organ(s), highest expression level in putamen
CleanExiHS_GNB1
ExpressionAtlasiP62873 baseline and differential
GenevisibleiP62873 HS

Family and domain databases

Gene3Di2.130.10.10, 1 hit
InterProiView protein in InterPro
IPR020472 G-protein_beta_WD-40_rep
IPR001632 Gprotein_B
IPR016346 Guanine_nucleotide-bd_bsu
IPR015943 WD40/YVTN_repeat-like_dom_sf
IPR001680 WD40_repeat
IPR019775 WD40_repeat_CS
IPR017986 WD40_repeat_dom
IPR036322 WD40_repeat_dom_sf
PANTHERiPTHR19850 PTHR19850, 1 hit
PfamiView protein in Pfam
PF00400 WD40, 7 hits
PRINTSiPR00319 GPROTEINB
PR00320 GPROTEINBRPT
SMARTiView protein in SMART
SM00320 WD40, 7 hits
SUPFAMiSSF50978 SSF50978, 1 hit
PROSITEiView protein in PROSITE
PS00678 WD_REPEATS_1, 3 hits
PS50082 WD_REPEATS_2, 6 hits
PS50294 WD_REPEATS_REGION, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiGBB1_HUMAN
AccessioniPrimary (citable) accession number: P62873
Secondary accession number(s): B1AJZ7
, P04697, P04901, Q1RMY8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: September 12, 2018
This is version 164 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health

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