P51812 · KS6A3_HUMAN
- ProteinRibosomal protein S6 kinase alpha-3
- GeneRPS6KA3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids740 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of the transcription factors CREB1, ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and EIF4B phosphorylation, and mediates cellular proliferation, survival, and differentiation by modulating mTOR signaling and repressing pro-apoptotic function of BAD and DAPK1 (PubMed:16213824, PubMed:16223362, PubMed:17360704, PubMed:9770464).
In fibroblast, is required for EGF-stimulated phosphorylation of CREB1 and histone H3 at 'Ser-10', which results in the subsequent transcriptional activation of several immediate-early genes (PubMed:10436156, PubMed:9770464).
In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP (PubMed:16223362).
Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity (PubMed:8250835).
Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the preinitiation complex (PubMed:17360704).
In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation (PubMed:18508509, PubMed:18813292).
Is involved in the mTOR nutrient-sensing pathway by directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2 ability to suppress mTOR signaling, and mediates phosphorylation of RPTOR, which regulates mTORC1 activity and may promote rapamycin-sensitive signaling independently of the PI3K/AKT pathway (PubMed:18722121).
Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic function (PubMed:16213824).
Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4) (PubMed:18508509, PubMed:18813292).
Is involved in cell cycle regulation by phosphorylating the CDK inhibitor CDKN1B, which promotes CDKN1B association with 14-3-3 proteins and prevents its translocation to the nucleus and inhibition of G1 progression (By similarity).
In LPS-stimulated dendritic cells, is involved in TLR4-induced macropinocytosis, and in myeloma cells, acts as effector of FGFR3-mediated transformation signaling, after direct phosphorylation at Tyr-529 by FGFR3 (By similarity).
Negatively regulates EGF-induced MAPK1/3 phosphorylation via phosphorylation of SOS1 (By similarity).
Phosphorylates SOS1 at 'Ser-1134' and 'Ser-1161' that create YWHAB and YWHAE binding sites and which contribute to the negative regulation of MAPK1/3 phosphorylation (By similarity).
Phosphorylates EPHA2 at 'Ser-897', the RPS6KA-EPHA2 signaling pathway controls cell migration (PubMed:26158630).
Acts as a regulator of osteoblast differentiation by mediating phosphorylation of ATF4, thereby promoting ATF4 transactivation activity (By similarity).
In fibroblast, is required for EGF-stimulated phosphorylation of CREB1 and histone H3 at 'Ser-10', which results in the subsequent transcriptional activation of several immediate-early genes (PubMed:10436156, PubMed:9770464).
In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP (PubMed:16223362).
Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity (PubMed:8250835).
Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the preinitiation complex (PubMed:17360704).
In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation (PubMed:18508509, PubMed:18813292).
Is involved in the mTOR nutrient-sensing pathway by directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2 ability to suppress mTOR signaling, and mediates phosphorylation of RPTOR, which regulates mTORC1 activity and may promote rapamycin-sensitive signaling independently of the PI3K/AKT pathway (PubMed:18722121).
Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic function (PubMed:16213824).
Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4) (PubMed:18508509, PubMed:18813292).
Is involved in cell cycle regulation by phosphorylating the CDK inhibitor CDKN1B, which promotes CDKN1B association with 14-3-3 proteins and prevents its translocation to the nucleus and inhibition of G1 progression (By similarity).
In LPS-stimulated dendritic cells, is involved in TLR4-induced macropinocytosis, and in myeloma cells, acts as effector of FGFR3-mediated transformation signaling, after direct phosphorylation at Tyr-529 by FGFR3 (By similarity).
Negatively regulates EGF-induced MAPK1/3 phosphorylation via phosphorylation of SOS1 (By similarity).
Phosphorylates SOS1 at 'Ser-1134' and 'Ser-1161' that create YWHAB and YWHAE binding sites and which contribute to the negative regulation of MAPK1/3 phosphorylation (By similarity).
Phosphorylates EPHA2 at 'Ser-897', the RPS6KA-EPHA2 signaling pathway controls cell migration (PubMed:26158630).
Acts as a regulator of osteoblast differentiation by mediating phosphorylation of ATF4, thereby promoting ATF4 transactivation activity (By similarity).
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Cofactor
Activity regulation
Upon extracellular signal or mitogen stimulation, phosphorylated at Thr-577 in the C-terminal kinase domain (CTKD) by MAPK1/ERK2 and MAPK3/ERK1. The activated CTKD then autophosphorylates Ser-386, allowing binding of PDPK1, which in turn phosphorylates Ser-227 in the N-terminal kinase domain (NTDK) leading to the full activation of the protein and subsequent phosphorylation of the substrates by the NTKD.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
3.56 μM | NFATC4 |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
11.5 μmol/min/ug | toward ATP |
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 74-82 | ATP (UniProtKB | ChEBI) | ||||
Sequence: LGQGSFGKV | ||||||
Binding site | 100 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 193 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 428-436 | ATP (UniProtKB | ChEBI) | ||||
Sequence: IGVGSYSVC | ||||||
Binding site | 451 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 539 | Proton acceptor | ||||
Sequence: D |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRibosomal protein S6 kinase alpha-3
- EC number
- Short namesS6K-alpha-3
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP51812
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Involvement in disease
Coffin-Lowry syndrome (CLS)
- Note
- DescriptionAn X-linked disorder characterized by intellectual disability associated with facial and digital dysmorphisms, progressive skeletal malformations, growth retardation, hearing deficit and paroxysmal movement disorders.
- See alsoMIM:303600
Natural variants in CLS
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_006189 | 75 | G>V | in CLS; dbSNP:rs122454124 | |
VAR_006190 | 82 | V>F | in CLS; dbSNP:rs122454126 | |
VAR_006191 | 114 | R>W | in CLS; dbSNP:rs122454127 | |
VAR_006192 | 127 | H>Q | in CLS | |
VAR_006193 | 154 | D>Y | in CLS | |
VAR_065894 | 189 | I>K | in CLS; dbSNP:rs122454130 | |
VAR_006194 | 225 | A>V | in CLS; dbSNP:rs879027948 | |
VAR_006195 | 227 | S>A | in CLS; dbSNP:rs122454125 | |
VAR_065896 | 268 | F>S | in CLS; dbSNP:rs122454131 | |
VAR_006196 | 431 | G>D | in CLS | |
VAR_065898 | 477 | missing | in CLS | |
VAR_006197 | 729 | R>Q | in CLS; dbSNP:rs28935171 |
Intellectual developmental disorder, X-linked 19 (XLID19)
- Note
- DescriptionA disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period.
- See alsoMIM:300844
Natural variants in XLID19
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_065892 | 115 | T>S | in XLID19; dbSNP:rs387906703 | |
VAR_065893 | 152 | missing | in XLID19; dbSNP:rs398122813 | |
VAR_065895 | 202 | missing | in XLID19 | |
VAR_065897 | 383 | R>W | in XLID19; kinase activity is decreased but not abolished; dbSNP:rs122454129 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_006188 | 38 | in dbSNP:rs56218010 | |||
Sequence: I → S | ||||||
Natural variant | VAR_006189 | 75 | in CLS; dbSNP:rs122454124 | |||
Sequence: G → V | ||||||
Natural variant | VAR_006190 | 82 | in CLS; dbSNP:rs122454126 | |||
Sequence: V → F | ||||||
Natural variant | VAR_006191 | 114 | in CLS; dbSNP:rs122454127 | |||
Sequence: R → W | ||||||
Natural variant | VAR_065892 | 115 | in XLID19; dbSNP:rs387906703 | |||
Sequence: T → S | ||||||
Natural variant | VAR_006192 | 127 | in CLS | |||
Sequence: H → Q | ||||||
Natural variant | VAR_065893 | 152 | in XLID19; dbSNP:rs398122813 | |||
Sequence: Missing | ||||||
Natural variant | VAR_006193 | 154 | in CLS | |||
Sequence: D → Y | ||||||
Natural variant | VAR_065894 | 189 | in CLS; dbSNP:rs122454130 | |||
Sequence: I → K | ||||||
Natural variant | VAR_065895 | 202 | in XLID19 | |||
Sequence: Missing | ||||||
Natural variant | VAR_006194 | 225 | in CLS; dbSNP:rs879027948 | |||
Sequence: A → V | ||||||
Natural variant | VAR_006195 | 227 | in CLS; dbSNP:rs122454125 | |||
Sequence: S → A | ||||||
Natural variant | VAR_065896 | 268 | in CLS; dbSNP:rs122454131 | |||
Sequence: F → S | ||||||
Natural variant | VAR_065897 | 383 | in XLID19; kinase activity is decreased but not abolished; dbSNP:rs122454129 | |||
Sequence: R → W | ||||||
Natural variant | VAR_035627 | 416 | in a breast cancer sample; somatic mutation; dbSNP:rs148050184 | |||
Sequence: I → V | ||||||
Natural variant | VAR_006196 | 431 | in CLS | |||
Sequence: G → D | ||||||
Natural variant | VAR_065898 | 477 | in CLS | |||
Sequence: Missing | ||||||
Natural variant | VAR_040629 | 483 | in a gastric adenocarcinoma sample; somatic mutation; dbSNP:rs1271090915 | |||
Sequence: Y → C | ||||||
Natural variant | VAR_040630 | 608 | in a glioblastoma multiforme sample; somatic mutation | |||
Sequence: L → F | ||||||
Natural variant | VAR_040631 | 723 | in dbSNP:rs35026425 | |||
Sequence: R → C | ||||||
Natural variant | VAR_006197 | 729 | in CLS; dbSNP:rs28935171 | |||
Sequence: R → Q |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 547 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 chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000086203 | 1-740 | UniProt | Ribosomal protein S6 kinase alpha-3 | |||
Sequence: MPLAQLADPWQKMAVESPSDSAENGQQIMDEPMGEEEINPQTEEVSIKEIAITHHVKEGHEKADPSQFELLKVLGQGSFGKVFLVKKISGSDARQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNPANRLGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKTPKDSPGIPPSANAHQLFRGFSFVAITSDDESQAMQTVGVHSIVQQLHRNSIQFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGKFSLSGGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHWDQLPQYQLNRQDAPHLVKGAMAATYSALNRNQSPVLEPVGRSTLAQRRGIKKITSTAL | |||||||
Modified residue (large scale data) | 17 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 19 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 78 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 226 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 227 | UniProt | Phosphoserine; by PDPK1 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 227 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 231 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 365 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 365 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 369 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 369 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 375 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 375 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 386 | UniProt | Phosphoserine; by autocatalysis and MAPKAPK2 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 386 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 415 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 415 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 529 | UniProt | Phosphotyrosine; by FGFR3 | ||||
Sequence: Y | |||||||
Modified residue | 556 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 577 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 580 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 581 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 707 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 715 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 715 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Activated by phosphorylation at Ser-227 by PDPK1. Autophosphorylated on Ser-386, as part of the activation process. May be phosphorylated at Thr-365 and Ser-369 by MAPK1/ERK2 and MAPK3/ERK1. Can also be activated via phosphorylation at Ser-386 by MAPKAPK2.
N-terminal myristoylation results in an activated kinase in the absence of added growth factors.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in many tissues, highest levels in skeletal muscle.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Forms a complex with either MAPK1/ERK2 or MAPK3/ERK1 in quiescent cells. Transiently dissociates following mitogenic stimulation (By similarity).
Interacts with NFATC4, ETV1/ER81 and FGFR1
Interacts with NFATC4, ETV1/ER81 and FGFR1
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P51812 | BAG6 P46379-2 | 3 | EBI-1046616, EBI-10988864 | |
BINARY | P51812 | CSNK2B P67870 | 7 | EBI-1046616, EBI-348169 | |
BINARY | P51812 | GNAO1 P09471 | 3 | EBI-1046616, EBI-715087 | |
BINARY | P51812 | HSP90AB1 P08238 | 3 | EBI-1046616, EBI-352572 | |
BINARY | P51812 | KLF11 O14901 | 3 | EBI-1046616, EBI-948266 | |
BINARY | P51812 | MAPK1 P28482 | 12 | EBI-1046616, EBI-959949 | |
BINARY | P51812 | NEK6 Q9HC98-4 | 3 | EBI-1046616, EBI-11750983 | |
BINARY | P51812 | PABIR3 Q6P4D5-2 | 3 | EBI-1046616, EBI-9091052 | |
BINARY | P51812 | PIK3R1 P27986-2 | 3 | EBI-1046616, EBI-9090282 | |
BINARY | P51812 | SPRED2 Q7Z698 | 4 | EBI-1046616, EBI-7082156 | |
XENO | P51812 | yopM A1JU68 | 2 | EBI-1046616, EBI-26365850 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-38 | Disordered | ||||
Sequence: MPLAQLADPWQKMAVESPSDSAENGQQIMDEPMGEEEI | ||||||
Domain | 68-327 | Protein kinase 1 | ||||
Sequence: FELLKVLGQGSFGKVFLVKKISGSDARQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNPANRLGAGPDGVEEIKRHSFF | ||||||
Domain | 328-397 | AGC-kinase C-terminal | ||||
Sequence: STIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKTPKDSPGIPPSANAHQLFRGFSFVAITSDDESQ | ||||||
Domain | 422-679 | Protein kinase 2 | ||||
Sequence: YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGKFSLSGGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length740
- Mass (Da)83,736
- Last updated1996-10-01 v1
- Checksum486AE8357CEAB6C8
Computationally mapped potential isoform sequences
There are 7 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2R8Y7S9 | A0A2R8Y7S9_HUMAN | RPS6KA3 | 144 | ||
A0A2R8Y603 | A0A2R8Y603_HUMAN | RPS6KA3 | 282 | ||
A0A2R8YGB7 | A0A2R8YGB7_HUMAN | RPS6KA3 | 81 | ||
B7ZB17 | B7ZB17_HUMAN | RPS6KA3 | 712 | ||
B4DG22 | B4DG22_HUMAN | RPS6KA3 | 711 | ||
B1AXG1 | B1AXG1_HUMAN | RPS6KA3 | 711 | ||
B1AXG2 | B1AXG2_HUMAN | RPS6KA3 | 65 |
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 89 | in Ref. 5; AAH96303 | ||||
Sequence: S → L | ||||||
Sequence conflict | 410 | in Ref. 3; BAD92170 | ||||
Sequence: Missing | ||||||
Sequence conflict | 424 | in Ref. 6; AAC82495 | ||||
Sequence: V → L | ||||||
Sequence conflict | 480 | in Ref. 6; AAC82495 | ||||
Sequence: K → N | ||||||
Sequence conflict | 494 | in Ref. 6; AAC82495 | ||||
Sequence: Missing |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U08316 EMBL· GenBank· DDBJ | AAA81952.1 EMBL· GenBank· DDBJ | mRNA | ||
AK313932 EMBL· GenBank· DDBJ | BAG36651.1 EMBL· GenBank· DDBJ | mRNA | ||
AB208933 EMBL· GenBank· DDBJ | BAD92170.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AL732366 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL807772 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC096301 EMBL· GenBank· DDBJ | AAH96301.1 EMBL· GenBank· DDBJ | mRNA | ||
BC096302 EMBL· GenBank· DDBJ | AAH96302.1 EMBL· GenBank· DDBJ | mRNA | ||
BC096303 EMBL· GenBank· DDBJ | AAH96303.1 EMBL· GenBank· DDBJ | mRNA | ||
L07599 EMBL· GenBank· DDBJ | AAC82495.1 EMBL· GenBank· DDBJ | mRNA | ||
AB102662 EMBL· GenBank· DDBJ | BAC81131.1 EMBL· GenBank· DDBJ | mRNA |