GSA
entrez
2778
canonical
uniprot
O95467
canonical
uniprot
P63092
canonical
uniprot
P84996
canonical
uniprot
Q5JWF2
canonical
ensembl
ENSG00000087460
resolver
ensp
ENSP00000265620
resolver
ensp
ENSP00000265621
resolver
ensp
ENSP00000302237
resolver
ensp
ENSP00000304472
resolver
ensp
ENSP00000323571
resolver
ensp
ENSP00000346328
resolver
ensp
ENSP00000360115
resolver
ensp
ENSP00000360122
resolver
ensp
ENSP00000360126
resolver
ensp
ENSP00000360136
resolver
ensp
ENSP00000360139
resolver
ensp
ENSP00000360141
resolver
ensp
ENSP00000360143
resolver
ensp
ENSP00000392000
resolver
ensp
ENSP00000416234
resolver
ensp
ENSP00000474219
resolver
ensp
ENSP00000474802
resolver
ensp
ENSP00000499239
resolver
ensp
ENSP00000499293
resolver
ensp
ENSP00000499332
resolver
ensp
ENSP00000499334
resolver
ensp
ENSP00000499353
resolver
ensp
ENSP00000499380
resolver
ensp
ENSP00000499392
resolver
ensp
ENSP00000499409
resolver
ensp
ENSP00000499435
resolver
ensp
ENSP00000499443
resolver
ensp
ENSP00000499523
resolver
ensp
ENSP00000499545
resolver
ensp
ENSP00000499552
resolver
ensp
ENSP00000499654
resolver
ensp
ENSP00000499660
resolver
ensp
ENSP00000499673
resolver
ensp
ENSP00000499681
resolver
ensp
ENSP00000499758
resolver
ensp
ENSP00000499762
resolver
ensp
ENSP00000499767
resolver
ensp
ENSP00000499794
resolver
ensp
ENSP00000504675
resolver
enst
ENST00000306090
resolver
enst
ENST00000313949
resolver
enst
ENST00000349036
resolver
enst
ENST00000371075
resolver
enst
ENST00000371081
resolver
enst
ENST00000371098
resolver
enst
ENST00000419558
resolver
enst
ENST00000453292
resolver
enst
ENST00000462499
resolver
enst
ENST00000464788
resolver
enst
ENST00000467227
resolver
enst
ENST00000467321
resolver
enst
ENST00000469431
resolver
enst
ENST00000470512
resolver
enst
ENST00000472183
resolver
enst
ENST00000476935
resolver
enst
ENST00000477931
resolver
enst
ENST00000478585
resolver
enst
ENST00000480232
resolver
enst
ENST00000480975
resolver
enst
ENST00000481039
resolver
enst
ENST00000482112
resolver
enst
ENST00000485673
resolver
enst
ENST00000488546
resolver
enst
ENST00000488652
resolver
enst
ENST00000492907
resolver
enst
ENST00000603546
resolver
enst
ENST00000604005
resolver
enst
ENST00000657090
resolver
enst
ENST00000663479
resolver
enst
ENST00000667293
resolver
enst
ENST00000676826
resolver
genesymbol
GNAS
resolver
genesymbol
GSA
resolver
genesymbol_syn
GNAS1
resolver
genesymbol_syn
GSP
resolver
hgnc
HGNC:4392
resolver
uniprot
A0A0A0MR13
resolver
uniprot
A0A0S2Z3H8
resolver
uniprot
A0A0S2Z3S5
resolver
uniprot
A0A590UJ22
resolver
uniprot
A0A590UJ58
resolver
uniprot
A0A590UJA5
resolver
uniprot
A0A590UJB0
resolver
uniprot
A0A590UJB7
resolver
uniprot
A0A590UJF0
resolver
uniprot
A0A590UJG5
resolver
uniprot
A0A590UJI6
resolver
uniprot
A0A590UJJ0
resolver
uniprot
A0A590UJQ2
resolver
uniprot
A0A590UJQ9
resolver
uniprot
A0A590UJR6
resolver
uniprot
A0A590UJY8
resolver
uniprot
A0A590UK28
resolver
uniprot
A0A590UKA1
resolver
uniprot
A0A590UKA4
resolver
uniprot
A0A590UKA9
resolver
uniprot
A0A590UKB4
resolver
uniprot
A0A7I2V5R6
resolver
uniprot
A0A9K3Y787
resolver
uniprot
A0ACM8QBN8
resolver
uniprot
A2A2S3
resolver
uniprot
A2A2S4
resolver
uniprot
A6NI00
resolver
uniprot
B0AZR9
resolver
uniprot
B2RB88
resolver
uniprot
E1P5G2
resolver
uniprot
E1P5G3
resolver
uniprot
E1P5G5
resolver
uniprot
O75684
resolver
uniprot
O75685
resolver
uniprot
O95417
resolver
uniprot
P04895
resolver
uniprot
Q12927
resolver
uniprot
Q14433
resolver
uniprot
Q14455
resolver
uniprot
Q32P26
resolver
uniprot
Q5FWY2
resolver
uniprot
Q5JW67
resolver
uniprot
Q5JWD1
resolver
uniprot
Q5JWD2
resolver
uniprot
Q5JWD4
resolver
uniprot
Q5JWD5
resolver
uniprot
Q5JWE9
resolver
uniprot
Q5JWF1
resolver
uniprot
Q6NR75
resolver
uniprot
Q6NXS0
resolver
uniprot
Q8TBC0
resolver
uniprot
Q96H70
resolver
uniprot
Q9NY42
resolver
uniprot
S4R3E3
resolver
uniprot
S4R3V9
resolver
uniprot_entry
A0A0A0MR13_HUMAN
resolver
uniprot_entry
A0A0S2Z3H8_HUMAN
resolver
uniprot_entry
A0A0S2Z3S5_HUMAN
resolver
uniprot_entry
A0A590UJF0_HUMAN
resolver
uniprot_entry
A0A590UJQ9_HUMAN
resolver
uniprot_entry
A0A590UK28_HUMAN
resolver
uniprot_entry
A0A7I2V5R6_HUMAN
resolver
uniprot_entry
A0ACM8QBN8_HUMAN
resolver
uniprot_entry
ALEX_HUMAN
resolver
uniprot_entry
B0AZR9_HUMAN
resolver
uniprot_entry
GNAS1_HUMAN
resolver
uniprot_entry
GNAS2_HUMAN
resolver
uniprot_entry
GNAS3_HUMAN
resolver
uniprot_entry
Q14455_HUMAN
resolver
uniprot_entry
Q5FWY2_HUMAN
resolver
uniprot_entry
Q5JWD1_HUMAN
resolver
uniprot_entry
Q5JWE9_HUMAN
resolver
uniprot_sec
A0A590UJ22
resolver
uniprot_sec
A0A590UJ58
resolver
uniprot_sec
A0A590UJA5
resolver
uniprot_sec
A0A590UJB0
resolver
uniprot_sec
A0A590UJB7
resolver
uniprot_sec
A0A590UJG5
resolver
uniprot_sec
A0A590UJI6
resolver
uniprot_sec
A0A590UJJ0
resolver
uniprot_sec
A0A590UJQ2
resolver
uniprot_sec
A0A590UJR6
resolver
uniprot_sec
A0A590UJY8
resolver
uniprot_sec
A0A590UKA1
resolver
uniprot_sec
A0A590UKA4
resolver
uniprot_sec
A0A590UKA9
resolver
uniprot_sec
A0A590UKB4
resolver
uniprot_sec
A0A9K3Y787
resolver
uniprot_sec
A2A2S3
resolver
uniprot_sec
A2A2S4
resolver
uniprot_sec
A6NI00
resolver
uniprot_sec
B2RB88
resolver
uniprot_sec
E1P5G2
resolver
uniprot_sec
E1P5G3
resolver
uniprot_sec
E1P5G5
resolver
uniprot_sec
O75684
resolver
uniprot_sec
O75685
resolver
uniprot_sec
O95417
resolver
uniprot_sec
P04895
resolver
uniprot_sec
Q12927
resolver
uniprot_sec
Q14433
resolver
uniprot_sec
Q32P26
resolver
uniprot_sec
Q5JW67
resolver
uniprot_sec
Q5JWD2
resolver
uniprot_sec
Q5JWD4
resolver
uniprot_sec
Q5JWD5
resolver
uniprot_sec
Q5JWF1
resolver
uniprot_sec
Q6NR75
resolver
uniprot_sec
Q6NXS0
resolver
uniprot_sec
Q8TBC0
resolver
uniprot_sec
Q96H70
resolver
uniprot_sec
Q9NY42
resolver
uniprot_sec
S4R3E3
resolver
uniprot_sec
S4R3V9
resolver
amino_acid_sequence
MDRRSRAQQWRRARHNYNDLCPPIGRRAATALLWLSCSIALLRALATSNARAQQRAAAQQRRSFLNAHHRSGAQVFPESPESESDHEHEEADLELSLPECLEYEEEFDYETESETESEIESETDFETEPETAPTTEPETEPEDDRGPVVPKHSTFGQSLTQRLHALKLRSPDASPSRAPPSTQEPQSPREGEELKPEDKDPRDPEESKEPKEEKQRRRCKPKKPTRRDASPESPSKKGPIPIRRH
uniprot
proteins
amino_acid_sequence
MGCLGNSKTEDQRNEEKAQREANKKIEKQLQKDKQVYRATHRLLLLGAGESGKSTIVKQMRILHVNGFNGEGGEEDPQAARSNSDGEKATKVQDIKNNLKEAIETIVAAMSNLVPPVELANPENQFRVDYILSVMNVPDFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLDKIDVIKQADYVPSDQDLLRCRVLTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSYNMVIREDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDLLAEKVLAGKSKIEDYFPEFARYTTPEDATPEPGEDPRVTRAKYFIRDEFLRISTASGDGRHYCYPHFTCAVDTENIRRVFNDCRDIIQRMHLRQYELL
uniprot
proteins
amino_acid_sequence
MGVRNCLYGNNMSGQRDIPPEIGEQPEQPPLEAPGAAAPGAGPSPAEEMETEPPHNEPIPVENDGEACGPPEVSRPNFQVLNPAFREAGAHGSYSPPPEEAMPFEAEQPSLGGFWPTLEQPGFPSGVHAGLEAFGPALMEPGAFSGARPGLGGYSPPPEEAMPFEFDQPAQRGCSQLLLQVPDLAPGGPGAAGVPGAPPEEPQALRPAKAGSRGGYSPPPEETMPFELDGEGFGDDSPPPGLSRVIAQVDGSSQFAAVAASSAVRLTPAANAPPLWVPGAIGSPSQEAVRPPSNFTGSSPWMEISGPPFEIGSAPAGVDDTPVNMDSPPIALDGPPIKVSGAPDKRERAERPPVEEEAAEMEGAADAAEGGKVPSPGYGSPAAGAASADTAARAAPAAPADPDSGATPEDPDSGTAPADPDSGAFAADPDSGAAPAAPADPDSGAAPDAPADPDSGAAPDAPADPDAGAAPEAPAAPAAAETRAAHVAPAAPDAGAPTAPAASATRAAQVRRAASAAPASGARRKIHLRPPSPEIQAADPPTPRPTRASAWRGKSESSRGRRVYYDEGVASSDDDSSGDESDDGTSGCLRWFQHRRNRRRRKPQRNLLRNFLVQAFGGCFGRSESPQPKASRSLKVKKVPLAEKRRQMRKEALEKRAQKRAEKKRSKLIDKQLQDEKMGYMCTHRLLLLGAGESGKSTIVKQMRILHVNGFNGEGGEEDPQAARSNSDGEKATKVQDIKNNLKEAIETIVAAMSNLVPPVELANPENQFRVDYILSVMNVPDFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLDKIDVIKQADYVPSDQDLLRCRVLTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSYNMVIREDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDLLAEKVLAGKSKIEDYFPEFARYTTPEDATPEPGEDPRVTRAKYFIRDEFLRISTASGDGRHYCYPHFTCAVDTENIRRVFNDCRDIIQRMHLRQYELL
uniprot
proteins
amino_acid_sequence
MMARPVDPQRSPDPTFRSSTRHSGKLEPMEATAHLLRKQCPSRLNSPAWEASGLHWSSLDSPVGSMQALRPSAQHSWSPEPSVVPDQAWEDTALHQKKLCPLSLTSLPREAAVNFSYRSQTLLQEAQVLQGSPELLPRSPKPSGLQRLAPEEATALPLRRLCHLSLMEKDLGTTAHPRGFPELSHKSTAAASSRQSRPRVRSASLPPRTRLPSGSQAPSAAHPKRLSDLLLTSRAAAPGWRSPDPRSRLAAPPLGSTTLPSTWTAPQSRLTARPSRSPEPQIRESEQRDPQLRRKQQRWKEPLMPRREEKYPLRGTDPLPPGQPQRIPLPGQPLQPQPILTPGQPQKIPTPGQHQPILTPGHSQPIPTPGQPLPPQPIPTPGRPLTPQPIPTPGRPLTPQPIQMPGRPLRLPPPLRLLRPGQPMSPQLRQTQGLPLPQPLLPPGQPKSAGRPLQPLPPGPDARSISDPPAPRSRLPIRLLRGLLARLPGGASPRAAAAAACTTMKGWPAATMTPAETSPTMGPPDASAGFSIGEIAAAESPSATYSATFSCKPSGAASVDLRVPSPKPRALSRSRRYPWRRSADRCAKKPWRSGPRSAQRRNAVSSSTNNSRTKRWATCVRTACCF
uniprot
proteins
disease_involvement
DISEASE: ACTH-independent macronodular adrenal hyperplasia 1 (AIMAH1) [MIM:219080]: A rare adrenal defect characterized by multiple, bilateral, non-pigmented, benign, adrenocortical nodules. It results in excessive production of cortisol leading to ACTH-independent Cushing syndrome. Clinical manifestations of Cushing syndrome include facial and truncal obesity, abdominal striae, muscular weakness, osteoporosis, arterial hypertension, diabetes. {ECO:0000269|PubMed:12727968}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Pseudohypoparathyroidism 1B (PHP1B) [MIM:603233]: A disorder characterized by end-organ resistance to parathyroid hormone, hypocalcemia and hyperphosphatemia. Patients affected with PHP1B lack developmental defects characteristic of Albright hereditary osteodystrophy, and typically show no other endocrine abnormalities besides resistance to PTH. {ECO:0000269|PubMed:11029463, ECO:0000269|PubMed:11067869, ECO:0000269|PubMed:11294659, ECO:0000269|PubMed:12858292, ECO:0000269|PubMed:14561710, ECO:0000269|PubMed:15592469, ECO:0000269|PubMed:15800843}. Note=The disease is caused by variants affecting the gene represented in this entry. Most affected individuals have defects in methylation of the gene. In some cases microdeletions involving the STX16 appear to cause loss of methylation at exon A/B of GNAS, resulting in PHP1B. Paternal uniparental isodisomy have also been observed.; DISEASE: Note=Genetic variation affecting the GNAS locus is associated with GNAS hyperfunction, a condition characterized by increased trauma-related bleeding tendency, prolonged bleeding time, brachydactyly and intellectual disability. Both the XLas isoforms and the ALEX protein are mutated which strongly reduces the interaction between them and this may allow unimpeded activation of the XLas isoforms. {ECO:0000305}.
uniprot
proteins
disease_involvement
DISEASE: Albright hereditary osteodystrophy (AHO) [MIM:103580]: A disorder characterized by short stature, obesity, round facies, brachydactyly and subcutaneous calcification. It is often associated with pseudohypoparathyoidism, hypocalcemia and elevated PTH levels. {ECO:0000269|PubMed:11450852, ECO:0000269|PubMed:11600516, ECO:0000269|PubMed:12624854, ECO:0000269|PubMed:15817905, ECO:0000269|PubMed:7523385, ECO:0000269|PubMed:8388883, ECO:0000269|PubMed:8702665, ECO:0000269|PubMed:9159128, ECO:0000269|PubMed:9328353, ECO:0000269|PubMed:9727013}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Pseudohypoparathyroidism 1A (PHP1A) [MIM:103580]: A disorder characterized by end-organ resistance to parathyroid hormone, hypocalcemia and hyperphosphatemia. It is commonly associated with Albright hereditary osteodystrophy whose features are short stature, obesity, round facies, short metacarpals and ectopic calcification. {ECO:0000269|PubMed:21488135}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: McCune-Albright syndrome (MAS) [MIM:174800]: Characterized by polyostotic fibrous dysplasia, cafe-au-lait lesions, and a variety of endocrine disorders, including precocious puberty, hyperthyroidism, hypercortisolism, growth hormone excess, and hyperprolactinemia. The mutations producing MAS lead to constitutive activation of GS alpha. {ECO:0000269|PubMed:10571700, ECO:0000269|PubMed:1594625, ECO:0000269|PubMed:1944469, ECO:0000269|PubMed:7751320}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Progressive osseous heteroplasia (POH) [MIM:166350]: Rare autosomal dominant disorder characterized by extensive dermal ossification during childhood, followed by disabling and widespread heterotopic ossification of skeletal muscle and deep connective tissue. {ECO:0000269|PubMed:14723729}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: ACTH-independent macronodular adrenal hyperplasia 1 (AIMAH1) [MIM:219080]: A rare adrenal defect characterized by multiple, bilateral, non-pigmented, benign, adrenocortical nodules. It results in excessive production of cortisol leading to ACTH-independent Cushing syndrome. Clinical manifestations of Cushing syndrome include facial and truncal obesity, abdominal striae, muscular weakness, osteoporosis, arterial hypertension, diabetes. {ECO:0000269|PubMed:12727968}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Pseudohypoparathyroidism 1B (PHP1B) [MIM:603233]: A disorder characterized by end-organ resistance to parathyroid hormone, hypocalcemia and hyperphosphatemia. Patients affected with PHP1B lack developmental defects characteristic of Albright hereditary osteodystrophy, and typically show no other endocrine abnormalities besides resistance to PTH. {ECO:0000269|PubMed:11029463, ECO:0000269|PubMed:11067869, ECO:0000269|PubMed:11294659, ECO:0000269|PubMed:12858292, ECO:0000269|PubMed:14561710, ECO:0000269|PubMed:15592469, ECO:0000269|PubMed:15800843}. Note=The disease is caused by variants affecting the gene represented in this entry. Most affected individuals have defects in methylation of the gene. In some cases microdeletions involving the STX16 appear to cause loss of methylation at exon A/B of GNAS, resulting in PHP1B. Paternal uniparental isodisomy have also been observed.; DISEASE: Note=Genetic variation affecting the GNAS locus is associated with GNAS hyperfunction, a condition characterized by increased trauma-related bleeding tendency, prolonged bleeding time, brachydactyly and intellectual disability. Both the XLas isoforms and the ALEX protein are mutated which strongly reduces the interaction between them and this may allow unimpeded activation of the XLas isoforms. {ECO:0000305}.; DISEASE: Pseudohypoparathyroidism 1C (PHP1C) [MIM:612462]: A disorder characterized by end-organ resistance to parathyroid hormone, hypocalcemia and hyperphosphatemia. It is commonly associated with Albright hereditary osteodystrophy whose features are short stature, obesity, round facies, short metacarpals and ectopic calcification. {ECO:0000269|PubMed:21488135}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
disease_involvement
DISEASE: Note=Genetic variation affecting the GNAS locus is associated with GNAS hyperfunction, a condition characterized by increased trauma-related bleeding tendency, prolonged bleeding time, brachydactyly and intellectual disability. Both the XLas isoforms and the ALEX protein are mutated which strongly reduces the interaction between them and this may allow unimpeded activation of the XLas isoforms. {ECO:0000269|PubMed:11583302, ECO:0000269|PubMed:12719376}.; DISEASE: ACTH-independent macronodular adrenal hyperplasia 1 (AIMAH1) [MIM:219080]: A rare adrenal defect characterized by multiple, bilateral, non-pigmented, benign, adrenocortical nodules. It results in excessive production of cortisol leading to ACTH-independent Cushing syndrome. Clinical manifestations of Cushing syndrome include facial and truncal obesity, abdominal striae, muscular weakness, osteoporosis, arterial hypertension, diabetes. {ECO:0000269|PubMed:12727968}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Pseudohypoparathyroidism 1B (PHP1B) [MIM:603233]: A disorder characterized by end-organ resistance to parathyroid hormone, hypocalcemia and hyperphosphatemia. Patients affected with PHP1B lack developmental defects characteristic of Albright hereditary osteodystrophy, and typically show no other endocrine abnormalities besides resistance to PTH. {ECO:0000269|PubMed:11029463, ECO:0000269|PubMed:11067869, ECO:0000269|PubMed:11294659, ECO:0000269|PubMed:12858292, ECO:0000269|PubMed:14561710, ECO:0000269|PubMed:15592469, ECO:0000269|PubMed:15800843}. Note=The disease is caused by variants affecting the gene represented in this entry. Most affected individuals have defects in methylation of the gene. In some cases microdeletions involving the STX16 appear to cause loss of methylation at exon A/B of GNAS, resulting in PHP1B. Paternal uniparental isodisomy have also been observed.; DISEASE: Pseudohypoparathyroidism 1C (PHP1C) [MIM:612462]: A disorder characterized by end-organ resistance to parathyroid hormone, hypocalcemia and hyperphosphatemia. It is commonly associated with Albright hereditary osteodystrophy whose features are short stature, obesity, round facies, short metacarpals and ectopic calcification. {ECO:0000269|PubMed:11788646}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
disease_involvement
DISEASE: Note=Genetic variation affecting the GNAS locus is associated with GNAS hyperfunction, a condition characterized by increased trauma-related bleeding tendency, prolonged bleeding time, brachydactyly and intellectual disability. Both the XLas isoforms and the ALEX protein are mutated which strongly reduces the interaction between them and this may allow unimpeded activation of the XLas isoforms. {ECO:0000269|PubMed:12719376}.; DISEASE: ACTH-independent macronodular adrenal hyperplasia 1 (AIMAH1) [MIM:219080]: A rare adrenal defect characterized by multiple, bilateral, non-pigmented, benign, adrenocortical nodules. It results in excessive production of cortisol leading to ACTH-independent Cushing syndrome. Clinical manifestations of Cushing syndrome include facial and truncal obesity, abdominal striae, muscular weakness, osteoporosis, arterial hypertension, diabetes. {ECO:0000269|PubMed:12727968}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Pseudohypoparathyroidism 1B (PHP1B) [MIM:603233]: A disorder characterized by end-organ resistance to parathyroid hormone, hypocalcemia and hyperphosphatemia. Patients affected with PHP1B lack developmental defects characteristic of Albright hereditary osteodystrophy, and typically show no other endocrine abnormalities besides resistance to PTH. {ECO:0000269|PubMed:11029463, ECO:0000269|PubMed:11067869, ECO:0000269|PubMed:11294659, ECO:0000269|PubMed:12858292, ECO:0000269|PubMed:14561710, ECO:0000269|PubMed:15592469, ECO:0000269|PubMed:15800843}. Note=The disease is caused by variants affecting the gene represented in this entry. Most affected individuals have defects in methylation of the gene. In some cases microdeletions involving the STX16 appear to cause loss of methylation at exon A/B of GNAS, resulting in PHP1B. Paternal uniparental isodisomy have also been observed.; DISEASE: Colorectal cancer (CRC) [MIM:114500]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history. Note=The disease may be 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 in numerous signaling pathways controlled by G protein-coupled receptors (GPCRs) (PubMed:12391161, PubMed:17110384, PubMed:21488135, PubMed:26206488, PubMed:8702665, PubMed:10200251). The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state (PubMed:12391161, PubMed:17110384, PubMed:10200251). Signaling by an activated GPCR promotes GDP release and GTP binding (PubMed:12391161, PubMed:17110384, PubMed:10200251). The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal (PubMed:12391161, PubMed:17110384, PubMed:10200251). Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (PubMed:12391161, PubMed:17110384, PubMed:10200251). Signaling involves the activation of adenylyl cyclases, resulting in increased levels of the signaling molecule cAMP (PubMed:17110384, PubMed:26206488, PubMed:26206488, PubMed:8702665). Functions downstream of beta-adrenergic receptors (PubMed:21488135). Stimulates the Ras signaling pathway via RAPGEF2 (PubMed:12391161). {ECO:0000269|PubMed:10200251, ECO:0000269|PubMed:12391161, ECO:0000269|PubMed:17110384, ECO:0000269|PubMed:21488135, ECO:0000269|PubMed:26206488, ECO:0000269|PubMed:8702665}.
uniprot
proteins
function
FUNCTION: Guanine nucleotide-binding proteins (G proteins) function as transducers in numerous signaling pathways controlled by G protein-coupled receptors (GPCRs). 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. 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 involves the activation of adenylyl cyclases, resulting in increased levels of the signaling molecule cAMP. GNAS functions downstream of several GPCRs, including beta-adrenergic receptors. XLas isoforms interact with the same set of receptors as Gnas isoforms. {ECO:0000250|UniProtKB:Q6R0H7}.
uniprot
proteins
function
FUNCTION: May inhibit the adenylyl cyclase-stimulating activity of guanine nucleotide-binding protein G(s) subunit alpha which is produced from the same locus in a different open reading frame. {ECO:0000269|PubMed:12719376}.
uniprot
proteins
mass_dalton
111025
uniprot
proteins
mass_dalton
28029
uniprot
proteins
mass_dalton
45665
uniprot
proteins
mass_dalton
67948
uniprot
proteins
mutagenesis
MUTAGEN 3..6; /note="CLGN->STLS: Creates a myristoylation site and abolishes palmitoylation, impairing localization to the plasma membrane."; /evidence="ECO:0000269|PubMed:12135370"; MUTAGEN 4..6; /note="LGN->TLS: Creates a myristoylation site without affecting palmitoylation. Does not affect localization to the plasma membrane."; /evidence="ECO:0000269|PubMed:12135370"; MUTAGEN 6; /note="N->S: Does not create a myristoylation site. Does not affect palmitoylation."; /evidence="ECO:0000269|PubMed:12135370"; MUTAGEN 170; /note="Q->A: Increases GDP release but does not affect receptor-mediated activation."; /evidence="ECO:0000269|PubMed:10200251"; MUTAGEN 227; /note="Q->L: Increases binding to GAS2L2; when associated with N-295."; /evidence="ECO:0000269|PubMed:23994616"; MUTAGEN 258; /note="R->A: Increases GDP release and impairs receptor-mediated activation; markedly elevated intrinsic GTPase rate which will lead to more rapid inactivation."; /evidence="ECO:0000269|PubMed:10200251, ECO:0000269|PubMed:9727013"; MUTAGEN 295; /note="D->N: Increases binding to GAS2L2; when associated with L-227."; /evidence="ECO:0000269|PubMed:23994616
uniprot
proteins
post_translational_modification
PTM: Binds keratan sulfate chains. {ECO:0000250|UniProtKB:O18979}.; PTM: May be proteolytically processed to give rise to a number of active peptides. {ECO:0000269|PubMed:10729789}.
uniprot
proteins
protein_family
ALEX family
uniprot
proteins
protein_family
G(s) subfamily
uniprot
proteins
protein_family
G-alpha family
uniprot
proteins
protein_family
NESP55 family
uniprot
proteins
pubmed
10200251
uniprot
proteins
pubmed
10571700
uniprot
proteins
pubmed
10729789
uniprot
proteins
pubmed
10749992
uniprot
proteins
pubmed
11029463
uniprot
proteins
pubmed
11067869
uniprot
proteins
pubmed
11294659
uniprot
proteins
pubmed
11450852
uniprot
proteins
pubmed
11583302
uniprot
proteins
pubmed
11600516
uniprot
proteins
pubmed
11780052
uniprot
proteins
pubmed
11788646
uniprot
proteins
pubmed
11926205
uniprot
proteins
pubmed
12135370
uniprot
proteins
pubmed
12391161
uniprot
proteins
pubmed
12624854
uniprot
proteins
pubmed
12656668
uniprot
proteins
pubmed
12719376
uniprot
proteins
pubmed
12727968
uniprot
proteins
pubmed
12858292
uniprot
proteins
pubmed
14561710
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14723729
uniprot
proteins
pubmed
15148396
uniprot
proteins
pubmed
15242332
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15592469
uniprot
proteins
pubmed
15800843
uniprot
proteins
pubmed
15817905
uniprot
proteins
pubmed
1594625
uniprot
proteins
pubmed
16110341
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17110384
uniprot
proteins
pubmed
1944469
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20852621
uniprot
proteins
pubmed
21044946
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21488135
uniprot
proteins
pubmed
23333244
uniprot
proteins
pubmed
23994616
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
2549426
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26206488
uniprot
proteins
pubmed
27120771
uniprot
proteins
pubmed
3024154
uniprot
proteins
pubmed
3093273
uniprot
proteins
pubmed
3127824
uniprot
proteins
pubmed
3131741
uniprot
proteins
pubmed
32193322
uniprot
proteins
pubmed
35418677
uniprot
proteins
pubmed
35418678
uniprot
proteins
pubmed
35418679
uniprot
proteins
pubmed
35714614
uniprot
proteins
pubmed
35982227
uniprot
proteins
pubmed
36593162
uniprot
proteins
pubmed
36720854
uniprot
proteins
pubmed
36931277
uniprot
proteins
pubmed
37327704
uniprot
proteins
pubmed
37935376
uniprot
proteins
pubmed
37935377
uniprot
proteins
pubmed
38287118
uniprot
proteins
pubmed
38346960
uniprot
proteins
pubmed
38376112
uniprot
proteins
pubmed
38647423
uniprot
proteins
pubmed
38776963
uniprot
proteins
pubmed
39626010
uniprot
proteins
pubmed
7523385
uniprot
proteins
pubmed
7737262
uniprot
proteins
pubmed
7751320
uniprot
proteins
pubmed
8072545
uniprot
proteins
pubmed
8388883
uniprot
proteins
pubmed
8702665
uniprot
proteins
pubmed
8766942
uniprot
proteins
pubmed
9159128
uniprot
proteins
pubmed
9267696
uniprot
proteins
pubmed
9328353
uniprot
proteins
pubmed
9707596
uniprot
proteins
pubmed
9727013
uniprot
proteins
pubmed
9860993
uniprot
proteins
sequence_length
1037
uniprot
proteins
sequence_length
245
uniprot
proteins
sequence_length
394
uniprot
proteins
sequence_length
626
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12135370}; Peripheral membrane protein {ECO:0000269|PubMed:12135370}; Cytoplasmic side {ECO:0000269|PubMed:12135370}. Note=Associated to the plasma membrane via lipid-anchor. {ECO:0000269|PubMed:12135370}.
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27120771}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q63803}. Apical cell membrane {ECO:0000269|PubMed:27120771}. Note=Associated to the plasma membrane via lipid-anchor. {ECO:0000269|PubMed:27120771}.
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Cell projection, ruffle {ECO:0000250}. Note=Predominantly associated with cell membrane ruffles. {ECO:0000250}.
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle {ECO:0000250}. Secreted {ECO:0000250}. Note=Neuroendocrine secretory granules. {ECO:0000250}.
uniprot
proteins