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Overview

Uniprot IDP62879
Protein NameGuanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2
Gene NameGNB2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
23 NQIRDARKACGDSTL

Function

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

Protein Sequence

10 MSELEQLRQE 20 AEQLRNQIRD 30 ARKACGDSTL 40 TQITAGLDPV 50 GRIQMRTRRT 60 LRGHLAKIYA 70 MHWGTDSRLL 80 VSASQDGKLI 90 IWDSYTTNKV 100 HAIPLRSSWV 110 MTCAYAPSGN 120 FVACGGLDNI 130 CSIYSLKTRE 140 GNVRVSRELP 150 GHTGYLSCCR 160 FLDDNQIITS 170 SGDTTCALWD 180 IETGQQTVGF 190 AGHSGDVMSL 200 SLAPDGRTFV 210 SGACDASIKL 220 WDVRDSMCRQ 230 TFIGHESDIN 240 AVAFFPNGYA 250 FTTGSDDATC 260 RLFDLRADQE 270 LLMYSHDNII 280 CGITSVAFSR 290 SGRLLLAGYD 300 DFNCNIWDAM 310 KGDRAGVLAG 320 HDNRVSCLGV 330 TDDGMAVATG 340 SWDSFLKIWN

Gene Ontology

Classification GO ID Description
Molecular Function GO:0003924 GTPase activity
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005615 extracellular space
Cellular Component GO:0005925 focal adhesion
Cellular Component GO:0005834 heterotrimeric G-protein complex
Cellular Component GO:0005765 lysosomal membrane
Cellular Component GO:0016020 membrane
Cellular Component GO:0048471 perinuclear region of cytoplasm
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0045202 synapse
Cellular Component GO:0031982 vesicle
Molecular Function GO:0051020 GTPase binding
Molecular Function GO:0044877 protein-containing complex binding
Molecular Function GO:0030159 signaling receptor complex adaptor activity
Biological Process GO:0007186 G protein-coupled receptor signaling pathway
Biological Process GO:1901379 regulation of potassium ion transmembrane transport

Reference

[1] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.