P63092 · GNAS2_HUMAN
- ProteinGuanine nucleotide-binding protein G(s) subunit alpha isoforms short
- GeneGNAS
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids394 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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).
Miscellaneous
Catalytic activity
- GTP + H2O = GDP + H+ + phosphateThis reaction proceeds in the forward direction.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 47-55 | GTP (UniProtKB | ChEBI) | ||||
Sequence: GAGESGKST | ||||||
Binding site | 54 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 197-204 | GTP (UniProtKB | ChEBI) | ||||
Sequence: LLRCRVLT | ||||||
Binding site | 204 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 223-227 | GTP (UniProtKB | ChEBI) | ||||
Sequence: DVGGQ | ||||||
Binding site | 292-295 | GTP (UniProtKB | ChEBI) | ||||
Sequence: NKQD | ||||||
Binding site | 366 | GTP (UniProtKB | ChEBI) | ||||
Sequence: A |
GO annotations
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameGuanine nucleotide-binding protein G(s) subunit alpha isoforms short
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP63092
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Albright hereditary osteodystrophy (AHO)
- Note
- DescriptionA disorder characterized by short stature, obesity, round facies, brachydactyly and subcutaneous calcification. It is often associated with pseudohypoparathyoidism, hypocalcemia and elevated PTH levels.
- See alsoMIM:103580
Natural variants in AHO
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_003439 | 99 | L>P | in AHO; dbSNP:rs137854531 | |
VAR_017843 | 115 | P>L | in AHO; dbSNP:rs137854539 | |
VAR_003440 | 165 | R>C | in AHO; dbSNP:rs137854532 | |
VAR_017848 | 231 | R>H | in AHO; impairs the ability to mediate hormonal stimulation; dbSNP:rs137854538 | |
VAR_031875 | 242 | T>I | in AHO; dbSNP:rs2146284332 | |
VAR_031876 | 246 | F>S | in AHO | |
VAR_017849 | 250 | S>R | in AHO; may alter guanine nucleotide binding which could lead to thermolability and impaired function; dbSNP:rs137854534 | |
VAR_015388 | 258 | R>W | in AHO; defective GDP binding resulting in increased thermolability and decreased activation; dbSNP:rs137854535 | |
VAR_031877 | 259 | E>V | in AHO | |
VAR_003444 | 385 | R>H | in AHO; uncouples receptors from adenylyl cyclases; dbSNP:rs2146306727 |
Pseudohypoparathyroidism 1A (PHP1A)
- Note
- DescriptionA 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.
- See alsoMIM:103580
Natural variants in PHP1A
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_031873 | 156 | D>N | in PHP1A | |
VAR_031874 | 159 | V>M | in PHP1A; dbSNP:rs2146209716 | |
VAR_031878 | 280 | R>G | in PHP1A | |
VAR_031879 | 280 | R>K | in PHP1A | |
VAR_031881 | 338 | K>N | in PHP1A; dbSNP:rs1165430006 | |
VAR_017850 | 366 | A>S | in PHP1A; the patient also shows testotoxicosis; constitutively activates adenylyl cyclase in vitro; rapidly degraded at 37 degrees resulting in loss of Gs activity; dbSNP:rs137854537 |
McCune-Albright syndrome (MAS)
- Note
- DescriptionCharacterized 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.
- See alsoMIM:174800
Natural variants in MAS
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_003442 | 201 | R>C | in MAS; also found in somatotrophinoma; dbSNP:rs11554273 | |
VAR_017844 | 201 | R>G | in MAS; dbSNP:rs11554273 | |
VAR_003441 | 201 | R>H | in MAS and AIMAH1; also found in somatotrophinoma; dbSNP:rs121913495 |
Progressive osseous heteroplasia (POH)
- Note
- DescriptionRare autosomal dominant disorder characterized by extensive dermal ossification during childhood, followed by disabling and widespread heterotopic ossification of skeletal muscle and deep connective tissue.
- See alsoMIM:166350
Natural variants in POH
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_031880 | 281 | W>R | in POH |
ACTH-independent macronodular adrenal hyperplasia 1 (AIMAH1)
- Note
- DescriptionA 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.
- See alsoMIM:219080
Natural variants in AIMAH1
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_003441 | 201 | R>H | in MAS and AIMAH1; also found in somatotrophinoma; dbSNP:rs121913495 | |
VAR_017846 | 201 | R>S | in AIMAH1; also found in pituitary tumor and polyostotic fibrous dysplasia; dbSNP:rs11554273 |
Pseudohypoparathyroidism 1B (PHP1B)
- Note
- DescriptionA 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.
- See alsoMIM:603233
GNAS hyperfunction (GNASHYP)
- Note
- DescriptionThis condition is 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.
- See alsoMIM:139320
Pseudohypoparathyroidism 1C (PHP1C)
- Note
- DescriptionA 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.
- See alsoMIM:612462
Natural variants in PHP1C
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_066387 | 388 | L>R | in PHP1C; significantly reduces receptor-mediated activation; displays normal receptor-independent activation; dbSNP:rs397514457 | |
VAR_066388 | 392 | E>K | in PHP1C; significantly reduces receptor-mediated activation; displays normal receptor-independent activation; dbSNP:rs397514456 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_003439 | 99 | in AHO; dbSNP:rs137854531 | |||
Sequence: L → P | ||||||
Natural variant | VAR_031872 | 106 | in AHO/PHP1A | |||
Sequence: I → S | ||||||
Natural variant | VAR_017843 | 115 | in AHO; dbSNP:rs137854539 | |||
Sequence: P → L | ||||||
Natural variant | VAR_031873 | 156 | in PHP1A | |||
Sequence: D → N | ||||||
Natural variant | VAR_031874 | 159 | in PHP1A; dbSNP:rs2146209716 | |||
Sequence: V → M | ||||||
Natural variant | VAR_003440 | 165 | in AHO; dbSNP:rs137854532 | |||
Sequence: R → C | ||||||
Mutagenesis | 170 | Increases GDP release but does not affect receptor-mediated activation. | ||||
Sequence: Q → A | ||||||
Natural variant | VAR_003442 | 201 | in MAS; also found in somatotrophinoma; dbSNP:rs11554273 | |||
Sequence: R → C | ||||||
Natural variant | VAR_017844 | 201 | in MAS; dbSNP:rs11554273 | |||
Sequence: R → G | ||||||
Natural variant | VAR_003441 | 201 | in MAS and AIMAH1; also found in somatotrophinoma; dbSNP:rs121913495 | |||
Sequence: R → H | ||||||
Natural variant | VAR_017845 | 201 | in non-MAS endocrine tumors; dbSNP:rs121913495 | |||
Sequence: R → L | ||||||
Natural variant | VAR_017846 | 201 | in AIMAH1; also found in pituitary tumor and polyostotic fibrous dysplasia; dbSNP:rs11554273 | |||
Sequence: R → S | ||||||
Natural variant | VAR_017847 | 227 | in pituitary adenomas; also found in a patient with severe Cushing syndrome; dbSNP:rs137854533 | |||
Sequence: Q → H | ||||||
Natural variant | VAR_003443 | 227 | in somatotrophinoma; dbSNP:rs121913494 | |||
Sequence: Q → R | ||||||
Mutagenesis | 227 | Increases binding to GAS2L2; when associated with N-295. | ||||
Sequence: Q → L | ||||||
Natural variant | VAR_017848 | 231 | in AHO; impairs the ability to mediate hormonal stimulation; dbSNP:rs137854538 | |||
Sequence: R → H | ||||||
Natural variant | VAR_031875 | 242 | in AHO; dbSNP:rs2146284332 | |||
Sequence: T → I | ||||||
Natural variant | VAR_031876 | 246 | in AHO | |||
Sequence: F → S | ||||||
Natural variant | VAR_017849 | 250 | in AHO; may alter guanine nucleotide binding which could lead to thermolability and impaired function; dbSNP:rs137854534 | |||
Sequence: S → R | ||||||
Natural variant | VAR_015388 | 258 | in AHO; defective GDP binding resulting in increased thermolability and decreased activation; dbSNP:rs137854535 | |||
Sequence: R → W | ||||||
Mutagenesis | 258 | Increases GDP release and impairs receptor-mediated activation; markedly elevated intrinsic GTPase rate which will lead to more rapid inactivation. | ||||
Sequence: R → A | ||||||
Natural variant | VAR_031877 | 259 | in AHO | |||
Sequence: E → V | ||||||
Natural variant | VAR_031878 | 280 | in PHP1A | |||
Sequence: R → G | ||||||
Natural variant | VAR_031879 | 280 | in PHP1A | |||
Sequence: R → K | ||||||
Natural variant | VAR_031880 | 281 | in POH | |||
Sequence: W → R | ||||||
Mutagenesis | 295 | Increases binding to GAS2L2; when associated with L-227. | ||||
Sequence: D → N | ||||||
Natural variant | VAR_031881 | 338 | in PHP1A; dbSNP:rs1165430006 | |||
Sequence: K → N | ||||||
Natural variant | VAR_017850 | 366 | in PHP1A; the patient also shows testotoxicosis; constitutively activates adenylyl cyclase in vitro; rapidly degraded at 37 degrees resulting in loss of Gs activity; dbSNP:rs137854537 | |||
Sequence: A → S | ||||||
Natural variant | VAR_049358 | 380 | in dbSNP:rs8986 | |||
Sequence: R → L | ||||||
Natural variant | VAR_034744 | 382 | unable to interact with the receptor for PTH | |||
Sequence: Missing | ||||||
Natural variant | VAR_003444 | 385 | in AHO; uncouples receptors from adenylyl cyclases; dbSNP:rs2146306727 | |||
Sequence: R → H | ||||||
Natural variant | VAR_066387 | 388 | in PHP1C; significantly reduces receptor-mediated activation; displays normal receptor-independent activation; dbSNP:rs397514457 | |||
Sequence: L → R | ||||||
Natural variant | VAR_066388 | 392 | in PHP1C; significantly reduces receptor-mediated activation; displays normal receptor-independent activation; dbSNP:rs397514456 | |||
Sequence: E → K |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 978 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, lipidation, chain, modified residue (large scale data), modified residue, cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Lipidation | 2 | UniProt | N-palmitoyl glycine | ||||
Sequence: G | |||||||
Chain | PRO_0000203721 | 2-394 | UniProt | Guanine nucleotide-binding protein G(s) subunit alpha isoforms short | |||
Sequence: GCLGNSKTEDQRNEEKAQREANKKIEKQLQKDKQVYRATHRLLLLGAGESGKSTIVKQMRILHVNGFNGEGGEEDPQAARSNSDGEKATKVQDIKNNLKEAIETIVAAMSNLVPPVELANPENQFRVDYILSVMNVPDFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLDKIDVIKQADYVPSDQDLLRCRVLTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSYNMVIREDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDLLAEKVLAGKSKIEDYFPEFARYTTPEDATPEPGEDPRVTRAKYFIRDEFLRISTASGDGRHYCYPHFTCAVDTENIRRVFNDCRDIIQRMHLRQYELL | |||||||
Lipidation | 3 | UniProt | S-palmitoyl cysteine | ||||
Sequence: C | |||||||
Modified residue (large scale data) | 54 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 201 | UniProt | ADP-ribosylarginine; by cholera toxin | ||||
Sequence: R | |||||||
Cross-link | 300 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue | 352 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 352 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with ADCY5 and stimulates its adenylyl cyclase activity (PubMed:17110384, PubMed:26206488).
Interacts with ADCY6 and stimulates its adenylyl cyclase activity (PubMed:17110384).
Interacts with ADCY2 (By similarity).
Interaction with SASH1 (PubMed:23333244).
Interacts with GAS2L2 (PubMed:23994616).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | P63092 | Coro1a O89053 | 2 | EBI-1047114, EBI-6665847 | |
XENO | P63092-2 | Oprm1 P42866 | 2 | EBI-7607528, EBI-5282656 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-23 | Disordered | ||||
Sequence: MGCLGNSKTEDQRNEEKAQREAN | ||||||
Compositional bias | 9-23 | Basic and acidic residues | ||||
Sequence: TEDQRNEEKAQREAN | ||||||
Domain | 39-394 | G-alpha | ||||
Sequence: ATHRLLLLGAGESGKSTIVKQMRILHVNGFNGEGGEEDPQAARSNSDGEKATKVQDIKNNLKEAIETIVAAMSNLVPPVELANPENQFRVDYILSVMNVPDFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLDKIDVIKQADYVPSDQDLLRCRVLTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSYNMVIREDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDLLAEKVLAGKSKIEDYFPEFARYTTPEDATPEPGEDPRVTRAKYFIRDEFLRISTASGDGRHYCYPHFTCAVDTENIRRVFNDCRDIIQRMHLRQYELL | ||||||
Region | 42-55 | G1 motif | ||||
Sequence: RLLLLGAGESGKST | ||||||
Region | 68-91 | Disordered | ||||
Sequence: FNGEGGEEDPQAARSNSDGEKATK | ||||||
Region | 196-204 | G2 motif | ||||
Sequence: DLLRCRVLT | ||||||
Region | 219-228 | G3 motif | ||||
Sequence: FHMFDVGGQR | ||||||
Region | 288-295 | G4 motif | ||||
Sequence: ILFLNKQD | ||||||
Region | 364-369 | G5 motif | ||||
Sequence: TCAVDT |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 8 isoforms produced by Alternative splicing.
P63092-1
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.
- NameGnas-1
- SynonymsAlpha-S2, GNASl, Alpha-S-long
- Length394
- Mass (Da)45,665
- Last updated1987-08-13 v1
- ChecksumCD541181FC4412EF
P63092-2
- NameGnas-2
- SynonymsAlpha-S1, GNASs, Alpha-S-short
P63092-3
- Name3
Q5JWF2-1
The sequence of this isoform can be found in the external entry linked below. Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
View isoform- NameXLas-1
Q5JWF2-2
The sequence of this isoform can be found in the external entry linked below. Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
View isoform- NameXLas-2
Q5JWF2-3
The sequence of this isoform can be found in the external entry linked below. Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
View isoform- NameXLas-3
O95467-1
The sequence of this isoform can be found in the external entry linked below. Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
View isoform- NameNesp55
P63092-4
- Name4
- Differences from canonical
- 86-86: G → GS
Computationally mapped potential isoform sequences
There are 25 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q5JWF2 | GNAS1_HUMAN | GNAS | 1037 | ||
O95467 | GNAS3_HUMAN | GNAS | 245 | ||
Q5JWD1 | Q5JWD1_HUMAN | GNAS | 87 | ||
Q5JWE9 | Q5JWE9_HUMAN | GNAS | 1022 | ||
H0Y7E8 | H0Y7E8_HUMAN | GNAS | 730 | ||
H0Y7Z6 | H0Y7Z6_HUMAN | GNAS | 113 | ||
A0A804HIH4 | A0A804HIH4_HUMAN | GNAS | 285 | ||
A0A590UJY2 | A0A590UJY2_HUMAN | GNAS | 237 | ||
A0A590UJS2 | A0A590UJS2_HUMAN | GNAS | 368 | ||
A0A590UJQ9 | A0A590UJQ9_HUMAN | GNAS | 336 | ||
A0A590UJX3 | A0A590UJX3_HUMAN | GNAS | 28 | ||
A0A590UJX6 | A0A590UJX6_HUMAN | GNAS | 725 | ||
A0A590UK28 | A0A590UK28_HUMAN | GNAS | 321 | ||
A0A590UK00 | A0A590UK00_HUMAN | GNAS | 451 | ||
A0A590UJC9 | A0A590UJC9_HUMAN | GNAS | 91 | ||
A0A590UJF0 | A0A590UJF0_HUMAN | GNAS | 320 | ||
A0A590UJ46 | A0A590UJ46_HUMAN | GNAS | 285 | ||
A0A590UJ47 | A0A590UJ47_HUMAN | GNAS | 13 | ||
A0A0A0MR13 | A0A0A0MR13_HUMAN | GNAS | 362 | ||
B0AZR9 | B0AZR9_HUMAN | GNAS | 335 | ||
A0A8I5F5B5 | A0A8I5F5B5_HUMAN | GNAS | 690 | ||
A2A2R6 | A2A2R6_HUMAN | GNAS | 72 | ||
A2A2S1 | A2A2S1_HUMAN | GNAS | 166 | ||
P84996 | ALEX_HUMAN | GNAS | 626 | ||
A0A7I2V5R6 | A0A7I2V5R6_HUMAN | GNAS | 1038 |
Features
Showing features for sequence conflict, compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 3 | in Ref. 8; AAH66923 | ||||
Sequence: C → Y | ||||||
Sequence conflict | 6 | in Ref. 3; CAA30084 | ||||
Sequence: N → T | ||||||
Compositional bias | 9-23 | Basic and acidic residues | ||||
Sequence: TEDQRNEEKAQREAN | ||||||
Alternative sequence | VSP_026616 | 71 | in isoform 3 | |||
Sequence: E → D | ||||||
Alternative sequence | VSP_001833 | 71-72 | in isoform Gnas-2 | |||
Sequence: EG → DS | ||||||
Sequence conflict | 72 | in Ref. 8; AAH66923 | ||||
Sequence: Missing | ||||||
Alternative sequence | VSP_026617 | 72-86 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_001834 | 73-86 | in isoform Gnas-2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_047325 | 86 | in isoform 4 | |||
Sequence: G → GS | ||||||
Sequence conflict | 167 | in Ref. 8; AAH22875 | ||||
Sequence: N → D | ||||||
Sequence conflict | 230 | in Ref. 9; AAA52583 | ||||
Sequence: E → Q |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X04408 EMBL· GenBank· DDBJ | CAA27996.1 EMBL· GenBank· DDBJ | mRNA | ||
X04409 EMBL· GenBank· DDBJ | CAA27997.1 EMBL· GenBank· DDBJ | mRNA | ||
M21142 EMBL· GenBank· DDBJ | AAA53147.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M21139 EMBL· GenBank· DDBJ | AAA53147.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M21740 EMBL· GenBank· DDBJ | AAA53147.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M21140 EMBL· GenBank· DDBJ | AAA53147.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M21741 EMBL· GenBank· DDBJ | AAA53147.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M21141 EMBL· GenBank· DDBJ | AAA53147.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M21142 EMBL· GenBank· DDBJ | AAA53146.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M21139 EMBL· GenBank· DDBJ | AAA53146.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M21740 EMBL· GenBank· DDBJ | AAA53146.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M21140 EMBL· GenBank· DDBJ | AAA53146.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M21741 EMBL· GenBank· DDBJ | AAA53146.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M21141 EMBL· GenBank· DDBJ | AAA53146.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M21142 EMBL· GenBank· DDBJ | AAA53148.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M21139 EMBL· GenBank· DDBJ | AAA53148.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M21141 EMBL· GenBank· DDBJ | AAA53148.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M21740 EMBL· GenBank· DDBJ | AAA53148.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M21741 EMBL· GenBank· DDBJ | AAA53148.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M21142 EMBL· GenBank· DDBJ | AAA53149.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M21139 EMBL· GenBank· DDBJ | AAA53149.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M21740 EMBL· GenBank· DDBJ | AAA53149.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M21741 EMBL· GenBank· DDBJ | AAA53149.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M21141 EMBL· GenBank· DDBJ | AAA53149.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U12466 EMBL· GenBank· DDBJ | AAB60334.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
X07036 EMBL· GenBank· DDBJ | CAA30084.1 EMBL· GenBank· DDBJ | mRNA | ||
AF493897 EMBL· GenBank· DDBJ | AAM12611.1 EMBL· GenBank· DDBJ | mRNA | ||
AF493898 EMBL· GenBank· DDBJ | AAM12612.1 EMBL· GenBank· DDBJ | mRNA | ||
BT009905 EMBL· GenBank· DDBJ | AAP88907.1 EMBL· GenBank· DDBJ | mRNA | ||
AL109840 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL121917 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL132655 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471077 EMBL· GenBank· DDBJ | EAW75468.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471077 EMBL· GenBank· DDBJ | EAW75460.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471077 EMBL· GenBank· DDBJ | EAW75463.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC002722 EMBL· GenBank· DDBJ | AAH02722.1 EMBL· GenBank· DDBJ | mRNA | ||
BC008855 EMBL· GenBank· DDBJ | AAH08855.1 EMBL· GenBank· DDBJ | mRNA | ||
BC066923 EMBL· GenBank· DDBJ | AAH66923.1 EMBL· GenBank· DDBJ | mRNA | ||
BC022875 EMBL· GenBank· DDBJ | AAH22875.1 EMBL· GenBank· DDBJ | mRNA | ||
BC104928 EMBL· GenBank· DDBJ | AAI04929.1 EMBL· GenBank· DDBJ | mRNA | ||
BC108315 EMBL· GenBank· DDBJ | AAI08316.2 EMBL· GenBank· DDBJ | mRNA | ||
M14631 EMBL· GenBank· DDBJ | AAA52583.1 EMBL· GenBank· DDBJ | mRNA |