GNAI1
entrez
2770
canonical
uniprot
P63096
canonical
ensembl
ENSG00000127955
resolver
ensp
ENSP00000410572
resolver
ensp
ENSP00000497260
resolver
genesymbol
GNAI1
resolver
hgnc
HGNC:4384
resolver
uniprot
A8KA88
resolver
uniprot
B4E2V1
resolver
uniprot
C9J3A4
resolver
uniprot
P04898
resolver
uniprot
P11015
resolver
uniprot
P31871
resolver
uniprot
Q5U074
resolver
uniprot
Q8TAN5
resolver
uniprot
Q9UGA4
resolver
uniprot_entry
GNAI1_HUMAN
resolver
uniprot_sec
A8KA88
resolver
uniprot_sec
B4E2V1
resolver
uniprot_sec
C9J3A4
resolver
uniprot_sec
P04898
resolver
uniprot_sec
P11015
resolver
uniprot_sec
P31871
resolver
uniprot_sec
Q5U074
resolver
uniprot_sec
Q8TAN5
resolver
uniprot_sec
Q9UGA4
resolver
amino_acid_sequence
MGCTLSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDSARADDARQLFVLAGAAEEGFMTAELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF
uniprot
proteins
disease_involvement
DISEASE: Neurodevelopmental disorder with hypotonia, impaired speech, and behavioral abnormalities (NEDHISB) [MIM:619854]: An autosomal dominant disorder characterized by global developmental delay, impaired intellectual development, delayed or absent speech, hypotonia, behavioral abnormalities, and epilepsy that ranges from self-limiting to intractable. More variable features include non-specific dysmorphic facial features, distal skeletal anomalies, and brain imaging abnormalities. {ECO:0000269|PubMed:33473207, ECO:0000269|PubMed:34685729, ECO:0000269|PubMed:34819662}. Note=The disease is caused by variants affecting the gene represented in this entry.
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 (PubMed:18434541, PubMed:33762731, PubMed:34239069, PubMed:35610220, PubMed:37935376, PubMed:37935377, PubMed:37963465, PubMed:38552625, PubMed:8774883, PubMed:38918398, PubMed:40080544). The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state (PubMed:18434541, PubMed:8774883). Signaling by an activated GPCR promotes GDP release and GTP binding (PubMed:18434541, PubMed:8774883). The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal (PubMed:18434541, PubMed:8774883). Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (PubMed:18434541, PubMed:8774883). 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 (PubMed:8119955). The inactive GDP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. Required for normal cytokinesis during mitosis (PubMed:17635935). Required for cortical dynein-dynactin complex recruitment during metaphase (PubMed:22327364). {ECO:0000250|UniProtKB:P10824, ECO:0000269|PubMed:17635935, ECO:0000269|PubMed:18434541, ECO:0000269|PubMed:22327364, ECO:0000269|PubMed:33762731, ECO:0000269|PubMed:34239069, ECO:0000269|PubMed:35610220, ECO:0000269|PubMed:37935376, ECO:0000269|PubMed:37935377, ECO:0000269|PubMed:37963465, ECO:0000269|PubMed:38552625, ECO:0000269|PubMed:38918398, ECO:0000269|PubMed:40080544, ECO:0000269|PubMed:8119955, ECO:0000269|PubMed:8774883}.
uniprot
proteins
mass_dalton
40361
uniprot
proteins
mutagenesis
MUTAGEN 42; /note="G->R: Abolishes switch to an activated conformation and dissociation from beta and gamma subunits upon GTP binding. Abolishes interaction with RGS family members."; /evidence="ECO:0000269|PubMed:22383884"; MUTAGEN 116; /note="E->L: Enhances interaction (inactive GDP-bound) with RGS14."; /evidence="ECO:0000269|PubMed:17603074, ECO:0000269|PubMed:21115486"; MUTAGEN 147; /note="Q->L: Enhances interaction (inactive GDP-bound) with RGS14."; /evidence="ECO:0000269|PubMed:17603074, ECO:0000269|PubMed:21115486"; MUTAGEN 245; /note="E->L: Enhances interaction (inactive GDP-bound) with RGS14."; /evidence="ECO:0000269|PubMed:21115486
uniprot
proteins
post_translational_modification
PTM: Myristoylation at Gly-2 is required for membrane anchoring before palmitoylation. {ECO:0000250|UniProtKB:P10824}.; PTM: Palmitoylation at Cys-3 varies with membrane lipid composition. {ECO:0000250|UniProtKB:P10824}.; PTM: (Microbial infection) Deamidated at Gln-204 by Photorhabdus asymbiotica toxin PAU_02230, blocking GTP hydrolysis of heterotrimeric GNAQ or GNA11 and G-alphai (GNAI1, GNAI2 or GNAI3) proteins, thereby activating RhoA. {ECO:0000269|PubMed:24141704}.
uniprot
proteins
protein_family
G(i/o/t/z) subfamily
uniprot
proteins
protein_family
G-alpha family
uniprot
proteins
pubmed
11230166
uniprot
proteins
pubmed
11976690
uniprot
proteins
pubmed
12135370
uniprot
proteins
pubmed
12853948
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15242332
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16004878
uniprot
proteins
pubmed
17264214
uniprot
proteins
pubmed
17603074
uniprot
proteins
pubmed
17635935
uniprot
proteins
pubmed
18434541
uniprot
proteins
pubmed
19211784
uniprot
proteins
pubmed
20213681
uniprot
proteins
pubmed
21115486
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22327364
uniprot
proteins
pubmed
22383884
uniprot
proteins
pubmed
22408789
uniprot
proteins
pubmed
22952234
uniprot
proteins
pubmed
24141704
uniprot
proteins
pubmed
25255805
uniprot
proteins
pubmed
26126266
uniprot
proteins
pubmed
26766442
uniprot
proteins
pubmed
2834384
uniprot
proteins
pubmed
3110783
uniprot
proteins
pubmed
32126208
uniprot
proteins
pubmed
32193322
uniprot
proteins
pubmed
33473207
uniprot
proteins
pubmed
33762731
uniprot
proteins
pubmed
34239069
uniprot
proteins
pubmed
34685729
uniprot
proteins
pubmed
34819662
uniprot
proteins
pubmed
35061538
uniprot
proteins
pubmed
35217703
uniprot
proteins
pubmed
35501348
uniprot
proteins
pubmed
35610220
uniprot
proteins
pubmed
36064945
uniprot
proteins
pubmed
37935376
uniprot
proteins
pubmed
37935377
uniprot
proteins
pubmed
37963465
uniprot
proteins
pubmed
38552625
uniprot
proteins
pubmed
38600377
uniprot
proteins
pubmed
38776963
uniprot
proteins
pubmed
38918398
uniprot
proteins
pubmed
40080544
uniprot
proteins
pubmed
8119955
uniprot
proteins
pubmed
8774883
uniprot
proteins
sequence_length
354
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12135370, ECO:0000269|PubMed:17635935, ECO:0000269|PubMed:26766442}; Peripheral membrane protein {ECO:0000305|PubMed:12135370}; Cytoplasmic side {ECO:0000305|PubMed:12135370}. Nucleus {ECO:0000250|UniProtKB:P10824}. Cytoplasm {ECO:0000269|PubMed:17635935}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17635935}. Cytoplasm, cell cortex {ECO:0000269|PubMed:22327364}. Note=Associated to the plasma membrane via lipid-anchor (PubMed:20213681). Localizes in the centrosomes of interphase and mitotic cells, but not in centrosomes during cytokinesis. Detected at the cleavage furrow or the midbody (PubMed:17635935). Localized at the plasma membrane throughout mitosis (PubMed:17635935). {ECO:0000269|PubMed:17635935, ECO:0000269|PubMed:20213681}.
uniprot
proteins