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P62873

- GBB1_HUMAN

UniProt

P62873 - GBB1_HUMAN

Protein

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

Gene

GNB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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

    1. GTPase activity Source: MGI
    2. GTPase binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. protein complex binding Source: MGI
    5. signal transducer activity Source: UniProtKB-KW

    GO - Biological processi

    1. adenylate cyclase-activating dopamine receptor signaling pathway Source: BHF-UCL
    2. blood coagulation Source: Reactome
    3. cardiac muscle cell apoptotic process Source: Ensembl
    4. cell proliferation Source: Ensembl
    5. cellular response to catecholamine stimulus Source: BHF-UCL
    6. cellular response to glucagon stimulus Source: Reactome
    7. cellular response to hypoxia Source: Ensembl
    8. cellular response to prostaglandin E stimulus Source: BHF-UCL
    9. energy reserve metabolic process Source: Reactome
    10. G-protein coupled acetylcholine receptor signaling pathway Source: ProtInc
    11. GTP catabolic process Source: GOC
    12. phospholipase C-activating G-protein coupled receptor signaling pathway Source: Ensembl
    13. phototransduction, visible light Source: Reactome
    14. platelet activation Source: Reactome
    15. positive regulation of cytosolic calcium ion concentration Source: Ensembl
    16. Ras protein signal transduction Source: ProtInc
    17. regulation of rhodopsin mediated signaling pathway Source: Reactome
    18. retina development in camera-type eye Source: Ensembl
    19. rhodopsin mediated signaling pathway Source: Reactome
    20. sensory perception of taste Source: Ensembl
    21. signal transduction Source: ProtInc
    22. small molecule metabolic process Source: Reactome
    23. synaptic transmission Source: Reactome

    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_172761. Ca2+ pathway.
    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. Regulation of water balance by renal Aquaporins.
    REACT_25004. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
    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: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:4396. GNB1.

    Subcellular locationi

    GO - Cellular componenti

    1. cell body Source: Ensembl
    2. dendrite Source: Ensembl
    3. extracellular vesicular exosome Source: UniProt
    4. heterotrimeric G-protein complex Source: MGI
    5. intracellular Source: BHF-UCL
    6. lysosomal membrane Source: UniProtKB
    7. membrane Source: BHF-UCL
    8. photoreceptor disc membrane Source: Reactome
    9. photoreceptor inner segment Source: Ensembl
    10. photoreceptor outer segment membrane Source: Ensembl
    11. plasma membrane Source: Reactome

    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.

    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

    ArrayExpressiP62873.
    BgeeiP62873.
    CleanExiHS_GNB1.
    GenevestigatoriP62873.

    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. 70 interactions.
    DIPiDIP-599N.
    IntActiP62873. 30 interactions.
    MINTiMINT-94562.
    STRINGi9606.ENSP00000367872.

    Structurei

    Secondary structure

    1
    340
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 2523
    Helixi30 – 345
    Beta strandi47 – 515
    Beta strandi58 – 636
    Beta strandi67 – 748
    Beta strandi77 – 837
    Turni84 – 863
    Beta strandi89 – 946
    Beta strandi100 – 1056
    Beta strandi109 – 1168
    Beta strandi121 – 1277
    Beta strandi134 – 1396
    Beta strandi146 – 1538
    Beta strandi156 – 1616
    Beta strandi164 – 1707
    Turni171 – 1733
    Beta strandi176 – 1816
    Beta strandi187 – 1926
    Beta strandi196 – 2038
    Beta strandi208 – 2125
    Turni213 – 2164
    Beta strandi217 – 2226
    Beta strandi229 – 2346
    Beta strandi238 – 2458
    Beta strandi250 – 2545
    Turni255 – 2584
    Beta strandi259 – 2646
    Beta strandi273 – 2786
    Beta strandi284 – 2896
    Beta strandi292 – 2987
    Turni299 – 3013
    Beta strandi303 – 3097
    Beta strandi315 – 3206
    Beta strandi327 – 3315
    Beta strandi336 – 3394

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4KFMX-ray3.45B1-340[»]
    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.
    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]
    PfamiPF00400. WD40. 7 hits.
    [Graphical view]
    PIRSFiPIRSF002394. GN-bd_beta. 1 hit.
    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. Align

    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

    MSELDQLRQE AEQLKNQIRD ARKACADATL SQITNNIDPV GRIQMRTRRT    50
    LRGHLAKIYA MHWGTDSRLL VSASQDGKLI IWDSYTTNKV HAIPLRSSWV 100
    MTCAYAPSGN YVACGGLDNI CSIYNLKTRE GNVRVSRELA GHTGYLSCCR 150
    FLDDNQIVTS SGDTTCALWD IETGQQTTTF TGHTGDVMSL SLAPDTRLFV 200
    SGACDASAKL WDVREGMCRQ TFTGHESDIN AICFFPNGNA FATGSDDATC 250
    RLFDLRADQE LMTYSHDNII CGITSVSFSK SGRLLLAGYD DFNCNVWDAL 300
    KADRAGVLAG HDNRVSCLGV TDDGMAVATG SWDSFLKIWN 340
    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:
    EMBL
    GenBank
    DDBJ
    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.
    NP_002065.1. NM_002074.4.
    UniGeneiHs.430425.
    Hs.721030.

    Genome annotation databases

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

    Polymorphism databases

    DMDMi51317302.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS34.1. [P62873-1 ]
    PIRi A24853. RGHUB1.
    RefSeqi NP_001269467.1. NM_001282538.1.
    NP_001269468.1. NM_001282539.1.
    NP_002065.1. NM_002074.4.
    UniGenei Hs.430425.
    Hs.721030.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4KFM X-ray 3.45 B 1-340 [» ]
    ProteinModelPortali P62873.
    SMRi P62873. Positions 2-340.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109044. 70 interactions.
    DIPi DIP-599N.
    IntActi P62873. 30 interactions.
    MINTi MINT-94562.
    STRINGi 9606.ENSP00000367872.

    PTM databases

    PhosphoSitei P62873.

    Polymorphism databases

    DMDMi 51317302.

    2D gel databases

    OGPi P62873.
    REPRODUCTION-2DPAGE IPI00026268.

    Proteomic databases

    MaxQBi P62873.
    PaxDbi P62873.
    PRIDEi P62873.

    Protocols and materials databases

    DNASUi 2782.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000378609 ; ENSP00000367872 ; ENSG00000078369 . [P62873-1 ]
    GeneIDi 2782.
    KEGGi hsa:2782.
    UCSCi uc001aif.3. human. [P62873-1 ]

    Organism-specific databases

    CTDi 2782.
    GeneCardsi GC01M001748.
    HGNCi HGNC:4396. GNB1.
    HPAi HPA040736.
    MIMi 139380. gene.
    neXtProti NX_P62873.
    PharmGKBi PA28776.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2319.
    HOGENOMi HOG000176356.
    HOVERGENi HBG000188.
    InParanoidi P62873.
    KOi K04536.
    OMAi RIVMRPR.
    OrthoDBi EOG7GN2N5.
    PhylomeDBi P62873.
    TreeFami TF106149.

    Enzyme and pathway databases

    Reactomei REACT_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_172761. Ca2+ pathway.
    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. Regulation of water balance by renal Aquaporins.
    REACT_25004. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
    REACT_75831. Activation of G protein gated Potassium channels.
    SignaLinki P62873.

    Miscellaneous databases

    ChiTaRSi GNB1. human.
    EvolutionaryTracei P62873.
    GeneWikii GNB1.
    GenomeRNAii 2782.
    NextBioi 10959.
    PROi P62873.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P62873.
    Bgeei P62873.
    CleanExi HS_GNB1.
    Genevestigatori P62873.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    InterProi IPR020472. 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 ]
    Pfami PF00400. WD40. 7 hits.
    [Graphical view ]
    PIRSFi PIRSF002394. GN-bd_beta. 1 hit.
    PRINTSi PR00319. GPROTEINB.
    PR00320. GPROTEINBRPT.
    SMARTi SM00320. WD40. 7 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 1 hit.
    PROSITEi PS00678. WD_REPEATS_1. 3 hits.
    PS50082. WD_REPEATS_2. 6 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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].
    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].
    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: October 1, 2014
    This is version 122 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