Gnai2
entrez
81664
canonical
uniprot
P04897
canonical
ensembl
ENSRNOG00000016592
resolver
ensembl
ENSRNOG00055013363
resolver
ensembl
ENSRNOG00060029241
resolver
ensembl
ENSRNOG00065008318
resolver
ensp
ENSRNOP00000022550
resolver
ensp
ENSRNOP00055018581
resolver
ensp
ENSRNOP00060042319
resolver
ensp
ENSRNOP00065009777
resolver
enst
ENSRNOT00000022550
resolver
enst
ENSRNOT00055022918
resolver
enst
ENSRNOT00060050877
resolver
enst
ENSRNOT00065013208
resolver
genesymbol
Gnai2
resolver
genesymbol_syn
Gnai-2
resolver
uniprot
A6I2Z9
resolver
uniprot
Q45QN0
resolver
uniprot_entry
A6I2Z9_RAT
resolver
uniprot_entry
GNAI2_RAT
resolver
uniprot_sec
Q45QN0
resolver
amino_acid_sequence
MGCTVSAEDKAAAERSKMIDKNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEDGYSEEECRQYRAVVYSNTIQSIMAIVKAMGNLQIDFADPQRADDARQLFALSCAAEEQGMLPEDLSGVIRRLWADHGVQACFGRSREYQLNDSAAYYLNDLERIAQSDYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSAYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKITQSPLTICFPEYTGANKYDEAASYIQSKFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF
uniprot
proteins
ec_number
3.6.5.-
uniprot
proteins
function
FUNCTION: Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades. The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state. Signaling by an activated GPCR promotes GDP release and GTP binding. Examples of interacting GPCRs include the adenosine A1 receptor/ADORA1, CNR1, and FPR2. The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal. Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins. Signaling is mediated via effector proteins, such as adenylate cyclase: inhibits adenylate cyclase activity of ADCY1, ADCY5 and ADCY6, leading to decreased intracellular cAMP levels. Plays an important role in the activation of the transcription factor NFAT in endothelial cells to promote angiogenesis. The G(i) proteins are involved in hormonal regulation of adenylate cyclase: they inhibit the cyclase in response to beta-adrenergic stimuli. Plays an essential role for neutrophil recruitment in the context of acute inflammation suggesting a linked function of both GNAI2 in neutrophils and endothelial cells for polymorphonuclear neutrophils transmigration. {ECO:0000250|UniProtKB:P04899, ECO:0000250|UniProtKB:P08752}.
uniprot
proteins
mass_dalton
40499
uniprot
proteins
mutagenesis
MUTAGEN 82; /note="M->I: Increases sensitivity to RGS14 GTPase activity; when associated with I-85; R-86; R-90; K-92; G-96; A-98; A-99; A-111; G-112; T-121 and A-122. Does not increase sensitivity to RGS14 GTPase activity; when associated with I-85 and A-111."; /evidence="ECO:0000269|PubMed:15337739"; MUTAGEN 85; /note="V->I: Increases sensitivity to RGS14 GTPase activity; when associated with I-82; R-86; R-90; K-92; G-96; A-98; A-99; A-111; G-112; T-121 and A-122. Does not increase sensitivity to RGS14 GTPase activity; when associated with I-82 and A-111."; /evidence="ECO:0000269|PubMed:15337739"; MUTAGEN 86; /note="K->R: Increases sensitivity to RGS14 GTPase activity; when associated with I-82; I-85; R-90; K-92; G-96; A-98; A-99; A-111; G-112; T-121 and A-122."; /evidence="ECO:0000269|PubMed:15337739"; MUTAGEN 90; /note="N->R: Increases sensitivity to RGS14 GTPase activity; when associated with I-82; I-85; R-86; K-92; G-96; A-98; A-99; A-111; G-112; T-121 and A-122."; /evidence="ECO:0000269|PubMed:15337739"; MUTAGEN 92; /note="Q->K: Increases sensitivity to RGS14 GTPase activity; when associated with I-82; I-85; R-86; R-90; G-96; A-98; A-99; A-111; G-112; T-121 and A-122."; /evidence="ECO:0000269|PubMed:15337739"; MUTAGEN 96; /note="A->G: Increases sensitivity to RGS14 GTPase activity; when associated with I-82; I-85; R-86; R-90; K-92; A-98; A-99; A-111; G-112; T-121 and A-122."; /evidence="ECO:0000269|PubMed:15337739"; MUTAGEN 98; /note="P->A: Increases sensitivity to RGS14 GTPase activity; when associated with I-82; I-85; R-86; R-90; K-92; G-96; A-99; A-111; G-112; T-121 and A-122."; /evidence="ECO:0000269|PubMed:15337739"; MUTAGEN 99; /note="Q->A: Increases sensitivity to RGS14 GTPase activity; when associated with I-82; I-85; R-86; R-90; K-92; G-96; A-98; A-111; G-112; T-121 and A-122."; /evidence="ECO:0000269|PubMed:15337739"; MUTAGEN 111; /note="S->A: Increases sensitivity to RGS14 GTPase activity; when associated with I-82; I-85; R-86; R-90; K-92; G-96; A-98; A-99; G-112; T-121 and A-122. Does not increase sensitivity to RGS14 GTPase activity; when associated with G-112; T-121 and A-122. Does not increase sensitivity to RGS14 GTPase activity; when associated with I-82 and A-85."; /evidence="ECO:0000269|PubMed:15337739"; MUTAGEN 112; /note="C->G: Increases sensitivity to RGS14 GTPase activity; when associated with I-82; I-85; R-86; R-90; K-92; G-96; A-98; A-99; A-111; T-121 and A-122. Does not increase sensitivity to RGS14 GTPase activity; when associated with G-111; T-121 and A-122."; /evidence="ECO:0000269|PubMed:15337739"; MUTAGEN 117; /note="Missing: Increases sensitivity to RGS14 GTPase activity; when associated with I-82; I-85; R-86; R-90; K-92; G-96; A-98; A-99; A-111; G-112; T-121 and A-122. Does not increase sensitivity to RGS14 GTPase activity; when associated with G-111; G-112; T-121 and A-122."; MUTAGEN 121; /note="P->T: Increases sensitivity to RGS14 GTPase activity; when associated with I-82; I-85; R-86; R-90; K-92; G-96; A-98; A-99; A-111; G-112 and A-122. Does not increase sensitivity to RGS14 GTPase activity; when associated with G-111; G-112 and A-122."; /evidence="ECO:0000269|PubMed:15337739"; MUTAGEN 122; /note="E->A: Increases sensitivity to RGS14 GTPase activity; when associated with I-82; I-85; R-86; R-90; K-92; G-96; A-98; A-99; A-111; G-112 and T-121. Does not increase sensitivity to RGS14 GTPase activity; when associated with G-111; G-112 and T-121."; /evidence="ECO:0000269|PubMed:15337739
uniprot
proteins
protein_family
G(i/o/t/z) subfamily
uniprot
proteins
protein_family
G-alpha family
uniprot
proteins
pubmed
11121039
uniprot
proteins
pubmed
11387333
uniprot
proteins
pubmed
15337739
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16870394
uniprot
proteins
pubmed
17635935
uniprot
proteins
pubmed
19211784
uniprot
proteins
pubmed
2159473
uniprot
proteins
pubmed
21653697
uniprot
proteins
pubmed
2820999
uniprot
proteins
pubmed
3086867
uniprot
proteins
sequence_length
355
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04899}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P04899}. Cell membrane {ECO:0000250|UniProtKB:P04899}. Membrane {ECO:0000250|UniProtKB:P04899}; Lipid-anchor {ECO:0000250|UniProtKB:P04899}. Note=Localizes in the centrosomes of interphase and mitotic cells. Detected at the cleavage furrow and/or the midbody. {ECO:0000250|UniProtKB:P04899}.
uniprot
proteins