Q14790 · CASP8_HUMAN
- ProteinCaspase-8
- GeneCASP8
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids479 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Thiol protease that plays a key role in programmed cell death by acting as a molecular switch for apoptosis, necroptosis and pyroptosis, and is required to prevent tissue damage during embryonic development and adulthood (PubMed:23516580, PubMed:35338844, PubMed:35446120, PubMed:8681376, PubMed:8681377, PubMed:8962078, PubMed:9006941, PubMed:9184224).
Initiator protease that induces extrinsic apoptosis by mediating cleavage and activation of effector caspases responsible for FAS/CD95-mediated and TNFRSF1A-induced cell death (PubMed:23516580, PubMed:35338844, PubMed:35446120, PubMed:8681376, PubMed:8681377, PubMed:8962078, PubMed:9006941, PubMed:9184224).
Cleaves and activates effector caspases CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10 (PubMed:16916640, PubMed:8962078, PubMed:9006941).
Binding to the adapter molecule FADD recruits it to either receptor FAS/TNFRSF6 or TNFRSF1A (PubMed:8681376, PubMed:8681377).
The resulting aggregate called the death-inducing signaling complex (DISC) performs CASP8 proteolytic activation (PubMed:9184224).
The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases (PubMed:9184224).
Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC (PubMed:9184224).
In addition to extrinsic apoptosis, also acts as a negative regulator of necroptosis: acts by cleaving RIPK1 at 'Asp-324', which is crucial to inhibit RIPK1 kinase activity, limiting TNF-induced apoptosis, necroptosis and inflammatory response (PubMed:31827280, PubMed:31827281).
Also able to initiate pyroptosis by mediating cleavage and activation of gasdermin-C and -D (GSDMC and GSDMD, respectively): gasdermin cleavage promotes release of the N-terminal moiety that binds to membranes and forms pores, triggering pyroptosis (PubMed:32929201, PubMed:34012073).
Initiates pyroptosis following inactivation of MAP3K7/TAK1 (By similarity).
Also acts as a regulator of innate immunity by mediating cleavage and inactivation of N4BP1 downstream of TLR3 or TLR4, thereby promoting cytokine production (By similarity).
May participate in the Granzyme B (GZMB) cell death pathways (PubMed:8755496).
Cleaves PARP1 and PARP2 (PubMed:8681376).
Independent of its protease activity, promotes cell migration following phosphorylation at Tyr-380 (PubMed:18216014, PubMed:27109099).
Initiator protease that induces extrinsic apoptosis by mediating cleavage and activation of effector caspases responsible for FAS/CD95-mediated and TNFRSF1A-induced cell death (PubMed:23516580, PubMed:35338844, PubMed:35446120, PubMed:8681376, PubMed:8681377, PubMed:8962078, PubMed:9006941, PubMed:9184224).
Cleaves and activates effector caspases CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10 (PubMed:16916640, PubMed:8962078, PubMed:9006941).
Binding to the adapter molecule FADD recruits it to either receptor FAS/TNFRSF6 or TNFRSF1A (PubMed:8681376, PubMed:8681377).
The resulting aggregate called the death-inducing signaling complex (DISC) performs CASP8 proteolytic activation (PubMed:9184224).
The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases (PubMed:9184224).
Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC (PubMed:9184224).
In addition to extrinsic apoptosis, also acts as a negative regulator of necroptosis: acts by cleaving RIPK1 at 'Asp-324', which is crucial to inhibit RIPK1 kinase activity, limiting TNF-induced apoptosis, necroptosis and inflammatory response (PubMed:31827280, PubMed:31827281).
Also able to initiate pyroptosis by mediating cleavage and activation of gasdermin-C and -D (GSDMC and GSDMD, respectively): gasdermin cleavage promotes release of the N-terminal moiety that binds to membranes and forms pores, triggering pyroptosis (PubMed:32929201, PubMed:34012073).
Initiates pyroptosis following inactivation of MAP3K7/TAK1 (By similarity).
Also acts as a regulator of innate immunity by mediating cleavage and inactivation of N4BP1 downstream of TLR3 or TLR4, thereby promoting cytokine production (By similarity).
May participate in the Granzyme B (GZMB) cell death pathways (PubMed:8755496).
Cleaves PARP1 and PARP2 (PubMed:8681376).
Independent of its protease activity, promotes cell migration following phosphorylation at Tyr-380 (PubMed:18216014, PubMed:27109099).
Isoform 5
Lacks the catalytic site and may interfere with the pro-apoptotic activity of the complex.
Isoform 6
Lacks the catalytic site and may interfere with the pro-apoptotic activity of the complex.
Isoform 7
Lacks the catalytic site and may interfere with the pro-apoptotic activity of the complex (Probable). Acts as an inhibitor of the caspase cascade (PubMed:12010809).
Isoform 8
Lacks the catalytic site and may interfere with the pro-apoptotic activity of the complex.
Catalytic activity
Activity regulation
CASP8 activity is restricted by RIPK1 (By similarity).
Inhibited by the effector protein NleF that is produced by pathogenic E.coli; this inhibits apoptosis (PubMed:23516580).
Inhibited by the effector protein NleF that is produced by pathogenic E.coli; this inhibits apoptosis (PubMed:23516580).
Features
Showing features for site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 216-217 | Cleavage; by autocatalytic cleavage | ||||
Sequence: DS | ||||||
Active site | 317 | |||||
Sequence: H | ||||||
Active site | 360 | |||||
Sequence: C | ||||||
Site | 374-375 | Cleavage; by CASP6 | ||||
Sequence: DS | ||||||
Site | 384-385 | Cleavage; by autocatalytic cleavage | ||||
Sequence: DL |
GO annotations
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCaspase-8
- EC number
- Short namesCASP-8
- Alternative names
- Cleaved into 2 chains
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ14790
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Recruitment to lamellipodia of migrating cells is enhanced by phosphorylation at Tyr-380.
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Caspase-8 deficiency (CASP8D)
- Note
- DescriptionDisorder resembling autoimmune lymphoproliferative syndrome (ALPS). It is characterized by lymphadenopathy, splenomegaly, and defective CD95-induced apoptosis of peripheral blood lymphocytes (PBLs). It leads to defects in activation of T-lymphocytes, B-lymphocytes, and natural killer cells leading to immunodeficiency characterized by recurrent sinopulmonary and herpes simplex virus infections and poor responses to immunization.
- See alsoMIM:607271
Natural variants in CASP8D
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_014204 | 248 | R>W | in CASP8D; dbSNP:rs17860424 |
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 73 | Abolishes binding to FLASH. Induces NF-kappa-B activation. | ||||
Sequence: D → A | ||||||
Natural variant | VAR_025816 | 219 | in dbSNP:rs35976359 | |||
Sequence: S → T | ||||||
Natural variant | VAR_014204 | 248 | in CASP8D; dbSNP:rs17860424 | |||
Sequence: R → W | ||||||
Natural variant | VAR_020127 | 285 | associated with protection against breast cancer; also associated with a lower risk of cutaneous melanoma; dbSNP:rs1045485 | |||
Sequence: D → H | ||||||
Mutagenesis | 360 | Does not affect localization to lamellipodia of migrating cells. Prevents DISC-mediated processing of CASP8. | ||||
Sequence: C → A | ||||||
Mutagenesis | 360 | Abolishes interaction with UBR2. | ||||
Sequence: C → S | ||||||
Mutagenesis | 380 | Phosphomimetic mutant which does not affect interaction with PIK3R1 or DISC-mediated processing. | ||||
Sequence: Y → E | ||||||
Mutagenesis | 380 | Abolishes phosphorylation at this site. Lack of efficient localization to lamellipodia and lack of promotion of cell migration. Lack of interaction with the SH2 domain of SRC. Lack of interaction with PIK3R1. Impaired DISC-mediated processing. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 387 | Impaired CDK1-mediated phosphorylation and enhanced apoptosis. | ||||
Sequence: S → A | ||||||
Mutagenesis | 413 | Abolished ADP-riboxanation by C.violaceum CopC. | ||||
Sequence: R → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,378 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 propeptide, modified residue (large scale data), modified residue, chain.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Propeptide | PRO_0000004628 | 1-216 | UniProt | ||||
Sequence: MDFSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITYLNTRKEEMERELQTPGRAQISAYRVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQINKSLLKIINDYEEFSKERSSSLEGSPDEFSNGEELCGVMTISDSPREQD | |||||||
Modified residue (large scale data) | 21 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 26 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 188 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 211 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 211 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Chain | PRO_0000004629 | 217-374 | UniProt | Caspase-8 subunit p18 | |||
Sequence: SESQTLDKVYQMKSKPRGYCLIINNHNFAKAREKVPKLHSIRDRNGTHLDAGALTTTFEELHFEIKPHDDCTVEQIYEILKIYQLMDHSNMDCFICCILSHGDKGIIYGTDGQEAPIYELTSQFTGLKCPSLAGKPKVFFIQACQGDNYQKGIPVETD | |||||||
Modified residue | 224 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 334 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 334 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Propeptide | PRO_0000004630 | 375-384 | UniProt | ||||
Sequence: SEEQPYLEMD | |||||||
Modified residue | 380 | UniProt | Phosphotyrosine; by SRC | ||||
Sequence: Y | |||||||
Chain | PRO_0000004631 | 385-479 | UniProt | Caspase-8 subunit p10 | |||
Sequence: LSSPQTRYIPDEADFLLGMATVNNCVSYRNPAEGTWYIQSLCQSLRERCPRGDDILTILTEVNYEVSNKDDKKNMGKQMPQPTFTLRKKLVFPSD | |||||||
Modified residue | 387 | UniProt | Phosphoserine; by CDK1 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 387 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 413 | UniProt | (Microbial infection) ADP-riboxanated arginine | ||||
Sequence: R |
Post-translational modification
Generation of the p10 and p18 subunits requires association with the death-inducing signaling complex (DISC), whereas additional processing is likely due to the autocatalytic activity of the activated protease. GZMB and CASP10 can be involved in these processing events.
Phosphorylation on Ser-387 during mitosis by CDK1 inhibits activation by proteolysis and prevents apoptosis (PubMed:20937773).
Phosphorylation on Tyr-380 by SRC is mediated by interaction with the SRC SH2 domain and does not affect dimerization or recruitment to the death-inducing signaling complex (DISC) but negatively regulates DISC-mediated processing and activation of CASP8, down-regulating its proapoptotic function (PubMed:16619028, PubMed:27109099).
Phosphorylation on Tyr-380 also enhances localization to lamellipodia in migrating cells (PubMed:18216014).
Phosphorylation on Tyr-380 by SRC is mediated by interaction with the SRC SH2 domain and does not affect dimerization or recruitment to the death-inducing signaling complex (DISC) but negatively regulates DISC-mediated processing and activation of CASP8, down-regulating its proapoptotic function (PubMed:16619028, PubMed:27109099).
Phosphorylation on Tyr-380 also enhances localization to lamellipodia in migrating cells (PubMed:18216014).
(Microbial infection) ADP-riboxanation by C.violaceum CopC blocks CASP8 processing, preventing CASP8 activation and ability to mediate extrinsic apoptosis.
(Microbial infection) Proteolytically cleaved by the cowpox virus CRMA death inhibitory protein.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 18 kDa (p18) and a 10 kDa (p10) subunit (PubMed:10508784).
Component of the death-induced signaling complex (DISC) composed of cell surface receptor FAS/CD95 or TNFRSF1A, adapter protein FADD and the CASP8 protease; recruitment of CASP8 to the complex is required for processing of CASP8 into the p18 and p10 subunits (PubMed:8681376, PubMed:8681377, PubMed:9184224).
Component of the AIM2 PANoptosome complex, a multiprotein complex that drives inflammatory cell death (PANoptosis) (By similarity).
Interacts with CFLAR and PEA15 (PubMed:10442631).
Interacts with TNFAIP8L2 (By similarity).
Interacts with CASP8AP2 (PubMed:16378960).
Interacts with RFFL and RNF34; negatively regulate CASP8 through proteasomal degradation (PubMed:15069192).
Interacts with NOL3; decreases CASP8 activity in a mitochondria localization- and phosphorylation-dependent manner and this interaction is dissociated by calcium (PubMed:15509781).
Interacts with UBR2ca (PubMed:28602583).
Interacts with RIPK1 (By similarity).
Interacts with stimulated TNFRSF10B; this interaction is followed by CASP8 proteolytic cleavage and activation (PubMed:18846110).
Interacts (phosphorylated on Tyr-380) with PIK3R1 (PubMed:27109099).
Component of the death-induced signaling complex (DISC) composed of cell surface receptor FAS/CD95 or TNFRSF1A, adapter protein FADD and the CASP8 protease; recruitment of CASP8 to the complex is required for processing of CASP8 into the p18 and p10 subunits (PubMed:8681376, PubMed:8681377, PubMed:9184224).
Component of the AIM2 PANoptosome complex, a multiprotein complex that drives inflammatory cell death (PANoptosis) (By similarity).
Interacts with CFLAR and PEA15 (PubMed:10442631).
Interacts with TNFAIP8L2 (By similarity).
Interacts with CASP8AP2 (PubMed:16378960).
Interacts with RFFL and RNF34; negatively regulate CASP8 through proteasomal degradation (PubMed:15069192).
Interacts with NOL3; decreases CASP8 activity in a mitochondria localization- and phosphorylation-dependent manner and this interaction is dissociated by calcium (PubMed:15509781).
Interacts with UBR2ca (PubMed:28602583).
Interacts with RIPK1 (By similarity).
Interacts with stimulated TNFRSF10B; this interaction is followed by CASP8 proteolytic cleavage and activation (PubMed:18846110).
Interacts (phosphorylated on Tyr-380) with PIK3R1 (PubMed:27109099).
Isoform 9
Interacts at the endoplasmic reticulum with a complex containing BCAP31, BAP29, BCL2 and/or BCL2L1.
(Microbial infection) Interacts with human cytomegalovirus/HHV-5 protein vICA/UL36; this interaction inhibits CASP8 activation.
(Microbial infection) Interacts with NleF from pathogenic E.coli.
(Microbial infection) Interacts with molluscum contagiosum virus protein MC160.
(Microbial infection) Interacts (via RIP homotypic interaction motif) with herpes simplex virus 1/HHV-1 protein RIR1/ICP6 (via RIP homotypic interaction motif); this interaction prevents necroptosis activation.
(Microbial infection) Interacts (via RIP homotypic interaction motif) with herpes simplex virus 2/HHV-2 protein RIR1/ICP10 (via RIP homotypic interaction motif); this interaction prevents necroptosis activation.
Binary interactions
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-80 | DED 1 | ||||
Sequence: DFSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITYLN | ||||||
Domain | 100-177 | DED 2 | ||||
Sequence: AYRVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQINKSLLKIIND |
Domain
The catalytic domain is sufficient for recruitment to lamellipodia but catalytic activity is not necessary.
Isoform 9
Contains a N-terminal extension that is required for interaction with the BCAP31 complex.
Sequence similarities
Belongs to the peptidase C14A family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 9 isoforms produced by Alternative splicing.
Q14790-1
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.
- Name1
- SynonymsAlpha-1
- Length479
- Mass (Da)55,391
- Last updated1996-11-01 v1
- Checksum7A5FEAA6B39B582F
Q14790-2
- Name2
- SynonymsAlpha-2, MCH5-beta
- Differences from canonical
- 184-198: Missing
Q14790-3
- Name3
- SynonymsAlpha-3
- Differences from canonical
- 184-267: Missing
Q14790-4
- Name4
- SynonymsAlpha-4
Q14790-5
- Name5
- SynonymsBeta-1
Q14790-6
- Name6
- SynonymsBeta-2
Q14790-7
- Name7
- SynonymsBeta-3, 8L
- NoteMay be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Q14790-8
- Name8
- SynonymsBeta-4
Q14790-9
- Name9
- Synonyms8L
- Differences from canonical
- 1-1: M → MEGGRRARVVIESKRNFFLGAFPTPFPAEHVELGRLGDSETAMVPGKGGADYILLPFKKM
Computationally mapped potential isoform sequences
There are 10 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E7EVN1 | E7EVN1_HUMAN | CASP8 | 124 | ||
E7ETB7 | E7ETB7_HUMAN | CASP8 | 198 | ||
E7EQ01 | E7EQ01_HUMAN | CASP8 | 183 | ||
E7EQ06 | E7EQ06_HUMAN | CASP8 | 209 | ||
F8WF39 | F8WF39_HUMAN | CASP8 | 58 | ||
C9JB29 | C9JB29_HUMAN | CASP8 | 361 | ||
H7C0E2 | H7C0E2_HUMAN | CASP8 | 258 | ||
A0A8Q3WKY8 | A0A8Q3WKY8_HUMAN | CASP8 | 435 | ||
A0A8Q3SID9 | A0A8Q3SID9_HUMAN | CASP8 | 523 | ||
A0A8Q3SI66 | A0A8Q3SI66_HUMAN | CASP8 | 305 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_000808 | 1 | in isoform 9 | |||
Sequence: M → MEGGRRARVVIESKRNFFLGAFPTPFPAEHVELGRLGDSETAMVPGKGGADYILLPFKKM | ||||||
Sequence conflict | 14 | In isoform Q14790-9; in Ref. 8; AAL87628 | ||||
Sequence: K → R | ||||||
Alternative sequence | VSP_000809 | 102 | in isoform 4 | |||
Sequence: R → RFHFCRMSWAEANSQCQTQSVPFWRRVDHLLIR | ||||||
Alternative sequence | VSP_000810 | 184-198 | in isoform 2, isoform 4 and isoform 8 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_000811 | 184-220 | in isoform 6 | |||
Sequence: ERSSSLEGSPDEFSNGEELCGVMTISDSPREQDSESQ → DFGQSLPNEKQTSGILSDHQQSQFCKSTGESAQTSQH | ||||||
Alternative sequence | VSP_000813 | 184-267 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_000814 | 199-235 | in isoform 5 | |||
Sequence: GEELCGVMTISDSPREQDSESQTLDKVYQMKSKPRGY → DFGQSLPNEKQTSGILSDHQQSQFCKSTGESAQTSQH | ||||||
Alternative sequence | VSP_000812 | 221-479 | in isoform 6 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_000815 | 236-479 | in isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_000816 | 269-276 | in isoform 7 and isoform 8 | |||
Sequence: ALTTTFEE → TVEPKREK | ||||||
Alternative sequence | VSP_000817 | 277-479 | in isoform 7 and isoform 8 | |||
Sequence: Missing | ||||||
Sequence conflict | 294 | in Ref. 5; AAD24962 | ||||
Sequence: E → D | ||||||
Sequence conflict | 331 | in Ref. 2; AAC50602 and 5; AAD24962 | ||||
Sequence: A → P | ||||||
Sequence conflict | 343-344 | in Ref. 8; AAL87631 | ||||
Sequence: LK → FG |
Polymorphism
Genetic variations in CASP8 are associated with reduced risk of lung cancer [MIM:211980] in a population of Han Chinese subjects. Genetic variations are also associated with decreased risk of cancer of various other forms including esophageal, gastric, colorectal, cervical, and breast, acting in an allele dose-dependent manner.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X98172 EMBL· GenBank· DDBJ | CAA66853.1 EMBL· GenBank· DDBJ | mRNA | ||
X98173 EMBL· GenBank· DDBJ | CAA66854.1 EMBL· GenBank· DDBJ | mRNA | ||
X98174 EMBL· GenBank· DDBJ | CAA66855.1 EMBL· GenBank· DDBJ | mRNA | ||
X98175 EMBL· GenBank· DDBJ | CAA66856.1 EMBL· GenBank· DDBJ | mRNA | ||
X98176 EMBL· GenBank· DDBJ | CAA66857.1 EMBL· GenBank· DDBJ | mRNA | ||
X98177 EMBL· GenBank· DDBJ | CAA66858.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
X98178 EMBL· GenBank· DDBJ | CAA66859.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
U58143 EMBL· GenBank· DDBJ | AAC50602.1 EMBL· GenBank· DDBJ | mRNA | ||
U60520 EMBL· GenBank· DDBJ | AAC50645.1 EMBL· GenBank· DDBJ | mRNA | ||
AF009620 EMBL· GenBank· DDBJ | AAB70913.1 EMBL· GenBank· DDBJ | mRNA | ||
AF102146 EMBL· GenBank· DDBJ | AAD24962.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF102139 EMBL· GenBank· DDBJ | AAD24962.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF102140 EMBL· GenBank· DDBJ | AAD24962.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF102141 EMBL· GenBank· DDBJ | AAD24962.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF102142 EMBL· GenBank· DDBJ | AAD24962.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF102143 EMBL· GenBank· DDBJ | AAD24962.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF102144 EMBL· GenBank· DDBJ | AAD24962.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF102145 EMBL· GenBank· DDBJ | AAD24962.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB038985 EMBL· GenBank· DDBJ | BAB32555.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF380342 EMBL· GenBank· DDBJ | AAK57437.1 EMBL· GenBank· DDBJ | mRNA | ||
AF422925 EMBL· GenBank· DDBJ | AAL87628.1 EMBL· GenBank· DDBJ | mRNA | ||
AF422926 EMBL· GenBank· DDBJ | AAL87629.1 EMBL· GenBank· DDBJ | mRNA | ||
AF422927 EMBL· GenBank· DDBJ | AAL87630.1 EMBL· GenBank· DDBJ | mRNA | ||
AF422928 EMBL· GenBank· DDBJ | AAL87631.1 EMBL· GenBank· DDBJ | mRNA | ||
AF422929 EMBL· GenBank· DDBJ | AAL87632.1 EMBL· GenBank· DDBJ | mRNA | ||
DQ355026 EMBL· GenBank· DDBJ | ABC67468.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC007256 EMBL· GenBank· DDBJ | AAY24225.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC028223 EMBL· GenBank· DDBJ | - | mRNA | No translation available. |