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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: Annotation score: 5 out of 5-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.1 Publication

GO - Molecular functioni

  • GTPase activity Source: MGI
  • GTPase binding Source: UniProtKB
  • protein complex binding Source: MGI
  • signal transducer activity Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transducer

Enzyme and pathway databases

ReactomeiREACT_15457. G-protein activation.
REACT_15488. Olfactory Signaling Pathway.
REACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_163932. Activation of the phototransduction cascade.
REACT_1665. Glucagon signaling in metabolic regulation.
REACT_18274. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
REACT_18283. G alpha (q) signalling events.
REACT_18339. Adrenaline,noradrenaline inhibits insulin secretion.
REACT_18377. Glucagon-type ligand receptors.
REACT_18407. G alpha (12/13) signalling events.
REACT_19140. ADP signalling through P2Y purinoceptor 1.
REACT_19145. G beta:gamma signalling through PLC beta.
REACT_19231. G alpha (i) signalling events.
REACT_19290. G beta:gamma signalling through PI3Kgamma.
REACT_19327. G alpha (s) signalling events.
REACT_19333. G alpha (z) signalling events.
REACT_20647. Thromboxane signalling through TP receptor.
REACT_20653. ADP signalling through P2Y purinoceptor 12.
REACT_21254. Presynaptic function of Kainate receptors.
REACT_21384. Thrombin signalling through proteinase activated receptors (PARs).
REACT_23946. Prostacyclin signalling through prostacyclin receptor.
REACT_24023. Vasopressin regulates renal water homeostasis via Aquaporins.
REACT_25004. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
REACT_263982. Ca2+ pathway.
REACT_75831. Activation of G protein gated Potassium channels.
SignaLinkiP62873.

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:GNB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:4396. GNB1.

Subcellular locationi

GO - Cellular componenti

  • cell body Source: Ensembl
  • cytosol Source: GOC
  • dendrite Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • extracellular vesicle Source: UniProtKB
  • heterotrimeric G-protein complex Source: MGI
  • intracellular Source: BHF-UCL
  • lysosomal membrane Source: UniProtKB
  • membrane Source: BHF-UCL
  • photoreceptor disc membrane Source: Reactome
  • photoreceptor inner segment Source: Ensembl
  • photoreceptor outer segment membrane Source: Ensembl
  • plasma membrane Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi47 – 471T → A: Abolishes interaction with PTH1R and signaling in response to PTH1R agonist; when associated with A-337 and A-339. 1 Publication
Mutagenesisi337 – 3371K → A: Abolishes interaction with PTH1R and signaling in response to PTH1R agonist; when associated with A-47 and A-339. 1 Publication
Mutagenesisi339 – 3391W → A: Abolishes interaction with PTH1R and signaling in response to PTH1R agonist; when associated with A-47 and A-337. 1 Publication

Organism-specific databases

PharmGKBiPA28776.

Polymorphism and mutation databases

DMDMi51317302.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed4 Publications
Chaini2 – 340339Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1PRO_0000127687Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine4 Publications
Modified residuei266 – 2661PhosphohistidineBy similarity

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

MaxQBiP62873.
PaxDbiP62873.
PRIDEiP62873.

2D gel databases

OGPiP62873.
REPRODUCTION-2DPAGEIPI00026268.

PTM databases

PhosphoSiteiP62873.

Expressioni

Gene expression databases

BgeeiP62873.
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. The heterodimer formed by GNB1 and GNG2 interacts with PTH1R (via C-terminus).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NCF2P198782EBI-357130,EBI-489611

Protein-protein interaction databases

BioGridi109044. 76 interactions.
DIPiDIP-599N.
IntActiP62873. 31 interactions.
MINTiMINT-94562.
STRINGi9606.ENSP00000367869.

Structurei

Secondary structure

1
340
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 2321Combined sources
Helixi30 – 334Combined sources
Beta strandi35 – 373Combined sources
Beta strandi47 – 515Combined sources
Beta strandi58 – 636Combined sources
Beta strandi67 – 748Combined sources
Turni75 – 773Combined sources
Beta strandi78 – 836Combined sources
Turni84 – 863Combined sources
Beta strandi89 – 946Combined sources
Beta strandi96 – 983Combined sources
Beta strandi100 – 1056Combined sources
Beta strandi109 – 1168Combined sources
Beta strandi120 – 1278Combined sources
Beta strandi135 – 1406Combined sources
Beta strandi146 – 1538Combined sources
Beta strandi156 – 1616Combined sources
Beta strandi166 – 1705Combined sources
Turni171 – 1733Combined sources
Beta strandi176 – 1805Combined sources
Beta strandi187 – 1926Combined sources
Beta strandi196 – 2038Combined sources
Beta strandi208 – 2125Combined sources
Turni213 – 2164Combined sources
Beta strandi217 – 2226Combined sources
Beta strandi229 – 2346Combined sources
Beta strandi238 – 2458Combined sources
Beta strandi250 – 2545Combined sources
Turni255 – 2584Combined sources
Beta strandi259 – 2646Combined sources
Beta strandi273 – 2786Combined sources
Beta strandi284 – 2896Combined sources
Beta strandi294 – 2985Combined sources
Turni299 – 3013Combined sources
Beta strandi304 – 3085Combined sources
Beta strandi315 – 3206Combined sources
Beta strandi327 – 3315Combined sources
Beta strandi336 – 3394Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4KFMX-ray3.45B1-340[»]
4PNKX-ray2.56B1-340[»]
ProteinModelPortaliP62873.
SMRiP62873. Positions 2-340.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62873.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati53 – 8331WD 1Add
BLAST
Repeati95 – 12531WD 2Add
BLAST
Repeati141 – 17030WD 3Add
BLAST
Repeati182 – 21231WD 4Add
BLAST
Repeati224 – 25431WD 5Add
BLAST
Repeati268 – 29831WD 6Add
BLAST
Repeati310 – 34031WD 7Add
BLAST

Sequence similaritiesi

Belongs to the WD repeat G protein beta family.Curated
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00760000119239.
HOGENOMiHOG000176356.
HOVERGENiHBG000188.
InParanoidiP62873.
KOiK04536.
OMAiRIVMRPR.
OrthoDBiEOG7GN2N5.
PhylomeDBiP62873.
TreeFamiTF106149.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR001632. Gprotein_B.
IPR016346. Guanine_nucleotide-bd_bsu.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR19850. PTHR19850. 1 hit.
PfamiPF00400. WD40. 7 hits.
[Graphical view]
PRINTSiPR00319. GPROTEINB.
PR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

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

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei329 – 34012TGSWD…LKIWN → SVLG in isoform 2. 1 PublicationVSP_055232Add
BLAST

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, AL109917 Genomic DNA. Translation: CAI20029.1.
AL109917, AL031282 Genomic DNA. Translation: CAI95654.1.
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]
UniGeneiHs.430425.
Hs.721030.

Genome annotation databases

EnsembliENST00000378609; ENSP00000367872; ENSG00000078369. [P62873-1]
ENST00000610897; ENSP00000481878; ENSG00000078369. [P62873-1]
GeneIDi2782.
KEGGihsa:2782.
UCSCiuc001aif.3. human. [P62873-1]

Keywords - Coding sequence diversityi

Alternative splicing

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, AL109917 Genomic DNA. Translation: CAI20029.1.
AL109917, AL031282 Genomic DNA. Translation: CAI95654.1.
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]
UniGeneiHs.430425.
Hs.721030.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4KFMX-ray3.45B1-340[»]
4PNKX-ray2.56B1-340[»]
ProteinModelPortaliP62873.
SMRiP62873. Positions 2-340.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109044. 76 interactions.
DIPiDIP-599N.
IntActiP62873. 31 interactions.
MINTiMINT-94562.
STRINGi9606.ENSP00000367869.

PTM databases

PhosphoSiteiP62873.

Polymorphism and mutation databases

DMDMi51317302.

2D gel databases

OGPiP62873.
REPRODUCTION-2DPAGEIPI00026268.

Proteomic databases

MaxQBiP62873.
PaxDbiP62873.
PRIDEiP62873.

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.3. human. [P62873-1]

Organism-specific databases

CTDi2782.
GeneCardsiGC01M001748.
HGNCiHGNC:4396. GNB1.
HPAiHPA040736.
MIMi139380. gene.
neXtProtiNX_P62873.
PharmGKBiPA28776.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00760000119239.
HOGENOMiHOG000176356.
HOVERGENiHBG000188.
InParanoidiP62873.
KOiK04536.
OMAiRIVMRPR.
OrthoDBiEOG7GN2N5.
PhylomeDBiP62873.
TreeFamiTF106149.

Enzyme and pathway databases

ReactomeiREACT_15457. G-protein activation.
REACT_15488. Olfactory Signaling Pathway.
REACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_163932. Activation of the phototransduction cascade.
REACT_1665. Glucagon signaling in metabolic regulation.
REACT_18274. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
REACT_18283. G alpha (q) signalling events.
REACT_18339. Adrenaline,noradrenaline inhibits insulin secretion.
REACT_18377. Glucagon-type ligand receptors.
REACT_18407. G alpha (12/13) signalling events.
REACT_19140. ADP signalling through P2Y purinoceptor 1.
REACT_19145. G beta:gamma signalling through PLC beta.
REACT_19231. G alpha (i) signalling events.
REACT_19290. G beta:gamma signalling through PI3Kgamma.
REACT_19327. G alpha (s) signalling events.
REACT_19333. G alpha (z) signalling events.
REACT_20647. Thromboxane signalling through TP receptor.
REACT_20653. ADP signalling through P2Y purinoceptor 12.
REACT_21254. Presynaptic function of Kainate receptors.
REACT_21384. Thrombin signalling through proteinase activated receptors (PARs).
REACT_23946. Prostacyclin signalling through prostacyclin receptor.
REACT_24023. Vasopressin regulates renal water homeostasis via Aquaporins.
REACT_25004. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
REACT_263982. Ca2+ pathway.
REACT_75831. Activation of G protein gated Potassium channels.
SignaLinkiP62873.

Miscellaneous databases

ChiTaRSiGNB1. human.
EvolutionaryTraceiP62873.
GeneWikiiGNB1.
GenomeRNAii2782.
NextBioi10959.
PROiP62873.
SOURCEiSearch...

Gene expression databases

BgeeiP62873.
CleanExiHS_GNB1.
ExpressionAtlasiP62873. baseline and differential.
GenevisibleiP62873. HS.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR001632. Gprotein_B.
IPR016346. Guanine_nucleotide-bd_bsu.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR19850. PTHR19850. 1 hit.
PfamiPF00400. WD40. 7 hits.
[Graphical view]
PRINTSiPR00319. GPROTEINB.
PR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Beta-subunits of the human liver Gs/Gi signal-transducing proteins and those of bovine retinal rod cell transducin are identical."
    Codina J., Stengel D., Woo S.L.C., Birnbaumer L.
    FEBS Lett. 207:187-192(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  2. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
    Puhl H.L. III, Ikeda S.R., Aronstam R.S.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Brain, Muscle and Uterus.
  8. Bienvenut W.V., Quadroni M.
    Submitted (JUL-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-15; 58-89; 284-301 AND 305-314, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma and Melanoma.
  9. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-8; 69-78 AND 90-96, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Ovarian carcinoma.
  10. Lubec G., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 23-42; 58-78; 138-150; 198-209 AND 315-337, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fetal brain cortex.
  11. "G Protein betagamma subunits stimulate p114RhoGEF, a guanine nucleotide exchange factor for RhoA and Rac1: regulation of cell shape and reactive oxygen species production."
    Niu J., Profirovic J., Pan H., Vaiskunaite R., Voyno-Yasenetskaya T.
    Circ. Res. 93:848-856(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARHGEF18.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  13. "The cationic region of Rhes mediates its interactions with specific Gbeta subunits."
    Hill C., Goddard A., Ladds G., Davey J.
    Cell. Physiol. Biochem. 23:1-8(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RASD2.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  16. "Structure of the parathyroid hormone receptor C terminus bound to the G-protein dimer Gbeta1gamma2."
    Johnston C.A., Kimple A.J., Giguere P.M., Siderovski D.P.
    Structure 16:1086-1094(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEXES WITH GNG2 AND PTH1R, FUNCTION, SUBUNIT, MUTAGENESIS OF THR-47; LYS-337 AND TRP-339.
  17. Cited for: RETRACTION.

Entry informationi

Entry nameiGBB1_HUMAN
AccessioniPrimary (citable) accession number: P62873
Secondary accession number(s): B1AJZ7
, P04697, P04901, Q1RMY8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 130 of the entry and version 3 of the sequence. [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

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.