P19838 · NFKB1_HUMAN
- ProteinNuclear factor NF-kappa-B p105 subunit
- GeneNFKB1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids968 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Nuclear factor NF-kappa-B p105 subunit
Acts as a cytoplasmic retention of attached NF-kappa-B proteins by p105 (PubMed:1423592).
Nuclear factor NF-kappa-B p50 subunit
Together with RELA/p65, binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions (PubMed:1740106, PubMed:7830764).
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 433-434 | Cleavage (when cotranslationally processed) | ||||
Sequence: GT |
GO annotations
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNuclear factor NF-kappa-B p105 subunit
- Alternative names
- Cleaved into 1 chains
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP19838
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Nuclear factor NF-kappa-B p105 subunit
Nuclear factor NF-kappa-B p50 subunit
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Immunodeficiency, common variable, 12, with autoimmunity (CVID12)
- Note
- DescriptionA primary immunodeficiency characterized by hypogammaglobulinemia and recurrent bacterial infections. About half of patients develop autoimmune features, including cytopenia, as well as generalized inflammation and lymphoproliferation manifest as lymphadenopathy or hepatosplenomegaly.
- See alsoMIM:616576
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 61 | Suppresses S-nitrosylation-induced inhibition of DNA-binding activity. Loss of S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine-induced inhibition of DNA-binding activity. | ||||
Sequence: C → S | ||||||
Natural variant | VAR_016268 | 489 | in dbSNP:rs4648065 | |||
Sequence: T → I | ||||||
Natural variant | VAR_016269 | 506 | in dbSNP:rs4648072 | |||
Sequence: M → V | ||||||
Natural variant | VAR_016270 | 566 | in dbSNP:rs4648085 | |||
Sequence: T → I | ||||||
Natural variant | VAR_016271 | 578 | in dbSNP:rs4648086 | |||
Sequence: R → K | ||||||
Mutagenesis | 678 | Fails to promote HIF1AN-dependent 2-oxoglutarate decarboxylation. | ||||
Sequence: N → A | ||||||
Natural variant | VAR_016272 | 711 | in dbSNP:rs4648099 | |||
Sequence: H → Q | ||||||
Natural variant | VAR_016273 | 901 | in dbSNP:rs4648118 | |||
Sequence: A → T | ||||||
Mutagenesis | 903 | Prevents p105 proteolysis in response to TNF-alpha. | ||||
Sequence: S → A | ||||||
Mutagenesis | 907 | Prevents p105 proteolysis in response to TNF-alpha. | ||||
Sequence: S → A | ||||||
Mutagenesis | 921 | Decrease in stimuli-induced phosphorylation. Loss of phosphorylation; when associated with A-923 and A-932. | ||||
Sequence: S → A | ||||||
Mutagenesis | 923 | Decrease in stimuli-induced phosphorylation. Loss of phosphorylation; when associated with A-921 and A-932. | ||||
Sequence: S → A | ||||||
Mutagenesis | 927 | Decreased phosphorylation by IKBKB/IKKB and decreased generation of the NF-kappa-B p50 subunit from p105. | ||||
Sequence: S → A | ||||||
Mutagenesis | 932 | Decrease in stimuli-induced phosphorylation. Loss of phosphorylation; when associated with A-921 and A-923. | ||||
Sequence: S → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 963 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, lipidation, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000030311 | 1-433 | UniProt | Nuclear factor NF-kappa-B p50 subunit | |||
Sequence: MAEDDPYLGRPEQMFHLDPSLTHTIFNPEVFQPQMALPTDGPYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDGICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACIRGYNPGLLVHPDLAYLQAEGGGDRQLGDREKELIRQAALQQTKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSKAPNASNLKIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVHRQFAIVFKTPKYKDINITKPASVFVQLRRKSDLETSEPKPFLYYPEIKDKEEVQRKRQKLMPNFSDSFGGGSGAGAGGGGMFGSGGGGGGTGSTGPGYSFPHYGFPTYGGITFHPGTTKSNAGMKHG | |||||||
Chain | PRO_0000030310 | 1-968 | UniProt | Nuclear factor NF-kappa-B p105 subunit | |||
Sequence: MAEDDPYLGRPEQMFHLDPSLTHTIFNPEVFQPQMALPTDGPYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDGICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACIRGYNPGLLVHPDLAYLQAEGGGDRQLGDREKELIRQAALQQTKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSKAPNASNLKIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVHRQFAIVFKTPKYKDINITKPASVFVQLRRKSDLETSEPKPFLYYPEIKDKEEVQRKRQKLMPNFSDSFGGGSGAGAGGGGMFGSGGGGGGTGSTGPGYSFPHYGFPTYGGITFHPGTTKSNAGMKHGTMDTESKKDPEGCDKSDDKNTVNLFGKVIETTEQDQEPSEATVGNGEVTLTYATGTKEESAGVQDNLFLEKAMQLAKRHANALFDYAVTGDVKMLLAVQRHLTAVQDENGDSVLHLAIIHLHSQLVRDLLEVTSGLISDDIINMRNDLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAALLLDHPNGDGLNAIHLAMMSNSLPCLLLLVAAGADVNAQEQKSGRTALHLAVEHDNISLAGCLLLEGDAHVDSTTYDGTTPLHIAAGRGSTRLAALLKAAGADPLVENFEPLYDLDDSWENAGEDEGVVPGTTPLDMATSWQVFDILNGKPYEPEFTSDDLLAQGDMKQLAEDVKLQLYKLLEIPDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEVSGGTVRELVEALRQMGYTEAIEVIQAASSPVKTTSQAHSLPLSPASTRQQIDELRDSDSVCDSGVETSFRKLSFTESLTSGASLLTLNKMPHDYGQEGPLEGKI | |||||||
Modified residue | 61 | UniProt | S-nitrosocysteine; alternate | ||||
Sequence: C | |||||||
Lipidation | 61 | UniProt | S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine; alternate | ||||
Sequence: C | |||||||
Modified residue (large scale data) | 240 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Cross-link | 325 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 337 | UniProt | Phosphoserine; by PKA | ||||
Sequence: S | |||||||
Modified residue | 431 | UniProt | N6-acetyllysine; by EP300 | ||||
Sequence: K | |||||||
Modified residue | 440 | UniProt | N6-acetyllysine; by EP300 | ||||
Sequence: K | |||||||
Modified residue | 441 | UniProt | N6-acetyllysine; by EP300 | ||||
Sequence: K | |||||||
Modified residue | 449 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 678 | UniProt | (3S)-3-hydroxyasparagine; by HIF1AN; partial | ||||
Sequence: N | |||||||
Modified residue | 759 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 851 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 892 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 893 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 899 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 903 | UniProt | Phosphoserine; by GSK3-beta; in vitro | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 903 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 907 | UniProt | Phosphoserine; by GSK3-beta; in vitro | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 907 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 910 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 911 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 923 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 923 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 927 | UniProt | Phosphoserine; by IKKB | ||||
Sequence: S | |||||||
Modified residue | 932 | UniProt | Phosphoserine; by IKKB | ||||
Sequence: S | |||||||
Modified residue | 937 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 937 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 939 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 941 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 943 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 943 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
A cotranslational processing allows the production of both p50 and p105 (Nuclear factor NF-kappa-B p105 subunit) from a single NFKB1 mRNA (PubMed:10970863, PubMed:8628291, PubMed:9529257).
While translation occurs, the particular unfolded structure after the GRR repeat region acts as a substrate for the proteasome, promoting degradation of the C-terminus (PubMed:10970863, PubMed:9529257).
The GRR acts as a proteasomal 'stop signal', protecting the region upstream of the GRR from degradation and promoting generation of p50 (PubMed:10970863, PubMed:9529257).
It is unclear if limited proteasome degradation during cotranslational processing depends on ubiquitination (PubMed:10970863, PubMed:9529257).
NF-kappa-B p50 is also generated post-translationally following ubiquitination by the KPC complex, leading to limited processing by the proteasome downstream of the GRR region, thereby generating p50 (PubMed:25860612).
Nuclear factor NF-kappa-B p105 subunit
Phosphorylation at Ser-903 and Ser-907 primes p105 for proteolytic processing in response to TNF-alpha stimulation (PubMed:12871932).
Phosphorylation at Ser-923, Ser-927 and Ser-932 are required for BTRC/BTRCP-mediated ubiquitination and proteolysis (PubMed:10835356, PubMed:11158290, PubMed:11297557, PubMed:12482991, PubMed:14673179).
Phosphorylation at Ser-927 is also required for ubiquitination by the KPC complex and limited processing to generate NF-kappa-B p50 (Nuclear factor NF-kappa-B p50 subunit) (PubMed:25860612).
Nuclear factor NF-kappa-B p105 subunit
Polyubiquitinated by the SCF(FBXW11) and SCF(BTRC) complexes following phosphorylation at Ser-923, Ser-927 and Ser-932, leading to its complete degradation (PubMed:11158290).
In contrast, polyubiquitination by the KPC complex following phosphorylation at Ser-927 leads to limited proteosomal processing and generation of the active NF-kappa-B p50 (Nuclear factor NF-kappa-B p50 subunit) (PubMed:25860612).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homodimer; component of the NF-kappa-B p50-p50 complex. Component of the NF-kappa-B p105-p50 complex (PubMed:1423592).
Component of the NF-kappa-B p50-c-Rel complex (PubMed:15102766, PubMed:8152812).
Component of a complex consisting of the NF-kappa-B p50-p50 homodimer and BCL3 (PubMed:10469655).
Also interacts with MAP3K8 (PubMed:15485931, PubMed:9950430).
NF-kappa-B p50 subunit interacts with NCOA3 coactivator, which may coactivate NF-kappa-B dependent expression via its histone acetyltransferase activity (PubMed:11094166).
Interacts with TSC22D3; this interaction prevents nuclear translocation and DNA-binding (PubMed:11468175, PubMed:12393603).
Interacts with SPAG9 and UNC5CL (PubMed:14743216, PubMed:14769797).
NFKB1/p105 interacts with CFLAR; the interaction inhibits p105 processing into p50 (PubMed:13679070).
NFKB1/p105 forms a ternary complex with MAP3K8 and TNIP2 (PubMed:15169888).
Interacts with GSK3B; the interaction prevents processing of p105 to p50 (PubMed:12871932).
NFKB1/p50 interacts with NFKBIE (PubMed:9315679).
NFKB1/p50 interacts with NFKBIZ (By similarity).
Nuclear factor NF-kappa-B p50 subunit interacts with NFKBID (By similarity).
Directly interacts with MEN1 (PubMed:11526476).
Interacts with HIF1AN (PubMed:17003112).
Interacts with FEM1A; interaction is direct (By similarity).
Binary interactions
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, motif, region, compositional bias, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 42-367 | RHD | ||||
Sequence: PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDGICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACIRGYNPGLLVHPDLAYLQAEGGGDRQLGDREKELIRQAALQQTKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSKAPNASNLKIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVHRQFAIVFKTPKYKDINITKPASVFVQLRRKSDLETSEPKPFLYYPEIKDKEEVQRKRQKLM | ||||||
Motif | 360-365 | Nuclear localization signal | ||||
Sequence: QRKRQK | ||||||
Region | 372-394 | GRR | ||||
Sequence: DSFGGGSGAGAGGGGMFGSGGGG | ||||||
Region | 425-453 | Disordered | ||||
Sequence: KSNAGMKHGTMDTESKKDPEGCDKSDDKN | ||||||
Compositional bias | 434-453 | Basic and acidic residues | ||||
Sequence: TMDTESKKDPEGCDKSDDKN | ||||||
Region | 435-968 | Interaction with CFLAR | ||||
Sequence: MDTESKKDPEGCDKSDDKNTVNLFGKVIETTEQDQEPSEATVGNGEVTLTYATGTKEESAGVQDNLFLEKAMQLAKRHANALFDYAVTGDVKMLLAVQRHLTAVQDENGDSVLHLAIIHLHSQLVRDLLEVTSGLISDDIINMRNDLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAALLLDHPNGDGLNAIHLAMMSNSLPCLLLLVAAGADVNAQEQKSGRTALHLAVEHDNISLAGCLLLEGDAHVDSTTYDGTTPLHIAAGRGSTRLAALLKAAGADPLVENFEPLYDLDDSWENAGEDEGVVPGTTPLDMATSWQVFDILNGKPYEPEFTSDDLLAQGDMKQLAEDVKLQLYKLLEIPDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEVSGGTVRELVEALRQMGYTEAIEVIQAASSPVKTTSQAHSLPLSPASTRQQIDELRDSDSVCDSGVETSFRKLSFTESLTSGASLLTLNKMPHDYGQEGPLEGKI | ||||||
Repeat | 542-571 | ANK 1 | ||||
Sequence: NGDSVLHLAIIHLHSQLVRDLLEVTSGLIS | ||||||
Repeat | 581-610 | ANK 2 | ||||
Sequence: LYQTPLHLAVITKQEDVVEDLLRAGADLSL | ||||||
Repeat | 614-643 | ANK 3 | ||||
Sequence: LGNSVLHLAAKEGHDKVLSILLKHKKAALL | ||||||
Repeat | 650-679 | ANK 4 | ||||
Sequence: DGLNAIHLAMMSNSLPCLLLLVAAGADVNA | ||||||
Region | 650-684 | Essential for interaction with HIF1AN | ||||
Sequence: DGLNAIHLAMMSNSLPCLLLLVAAGADVNAQEQKS | ||||||
Repeat | 684-714 | ANK 5 | ||||
Sequence: SGRTALHLAVEHDNISLAGCLLLEGDAHVDS | ||||||
Repeat | 718-747 | ANK 6 | ||||
Sequence: DGTTPLHIAAGRGSTRLAALLKAAGADPLV | ||||||
Repeat | 771-801 | ANK 7 | ||||
Sequence: PGTTPLDMATSWQVFDILNGKPYEPEFTSDD | ||||||
Domain | 805-892 | Death | ||||
Sequence: QGDMKQLAEDVKLQLYKLLEIPDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEVSGGTVRELVEALRQMGYTEAIEVIQAAS |
Domain
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
P19838-1
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
- Length968
- Mass (Da)105,356
- Last updated2002-06-20 v2
- Checksum2A7C8FF86A10D1A8
P19838-2
- Name2
- Differences from canonical
- 39-39: T → TA
P19838-3
- Name3
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
D6RH30 | D6RH30_HUMAN | NFKB1 | 977 | ||
D6RC45 | D6RC45_HUMAN | NFKB1 | 144 | ||
A0A494C1E9 | A0A494C1E9_HUMAN | NFKB1 | 511 | ||
A0A494C157 | A0A494C157_HUMAN | NFKB1 | 253 | ||
A0A8V8TLB2 | A0A8V8TLB2_HUMAN | NFKB1 | 72 |
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_042869 | 1-180 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_021025 | 39 | in isoform 2 | |||
Sequence: T → TA | ||||||
Alternative sequence | VSP_042870 | 181-189 | in isoform 3 | |||
Sequence: EGGGDRQLG → MNGLCCMAL | ||||||
Sequence conflict | 243 | in Ref. 4; CAB94757 | ||||
Sequence: K → SE | ||||||
Sequence conflict | 361 | in Ref. 7; CAH18336 | ||||
Sequence: R → G | ||||||
Compositional bias | 434-453 | Basic and acidic residues | ||||
Sequence: TMDTESKKDPEGCDKSDDKN | ||||||
Sequence conflict | 551-552 | in Ref. 4; CAB94757 | ||||
Sequence: II → SS | ||||||
Sequence conflict | 573 | in Ref. 6; BAF84139 | ||||
Sequence: D → G | ||||||
Sequence conflict | 726 | in Ref. 4; CAB94757 | ||||
Sequence: A → V | ||||||
Sequence conflict | 825 | in Ref. 7; CAH18336 | ||||
Sequence: I → T | ||||||
Sequence conflict | 869 | in Ref. 4; CAB94757 | ||||
Sequence: V → I | ||||||
Sequence conflict | 927 | in Ref. 1; AAA36361, 3; AAA36360 and 4; CAB94757 | ||||
Sequence: S → T |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M55643 EMBL· GenBank· DDBJ | AAA36361.1 EMBL· GenBank· DDBJ | mRNA | ||
M58603 EMBL· GenBank· DDBJ | AAA36360.1 EMBL· GenBank· DDBJ | mRNA | ||
Z47748 EMBL· GenBank· DDBJ | CAB94757.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z47749 EMBL· GenBank· DDBJ | CAB94757.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z47750 EMBL· GenBank· DDBJ | CAB94757.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z47751 EMBL· GenBank· DDBJ | CAB94757.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z47752 EMBL· GenBank· DDBJ | CAB94757.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z47753 EMBL· GenBank· DDBJ | CAB94757.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z47754 EMBL· GenBank· DDBJ | CAB94757.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z47755 EMBL· GenBank· DDBJ | CAB94757.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z47734 EMBL· GenBank· DDBJ | CAB94757.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z47735 EMBL· GenBank· DDBJ | CAB94757.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z47736 EMBL· GenBank· DDBJ | CAB94757.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z47737 EMBL· GenBank· DDBJ | CAB94757.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z47738 EMBL· GenBank· DDBJ | CAB94757.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z47739 EMBL· GenBank· DDBJ | CAB94757.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z47740 EMBL· GenBank· DDBJ | CAB94757.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z47741 EMBL· GenBank· DDBJ | CAB94757.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z47742 EMBL· GenBank· DDBJ | CAB94757.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z47743 EMBL· GenBank· DDBJ | CAB94757.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z47744 EMBL· GenBank· DDBJ | CAB94757.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF213884 EMBL· GenBank· DDBJ | AAF35232.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK122850 EMBL· GenBank· DDBJ | BAG53760.1 EMBL· GenBank· DDBJ | mRNA | ||
AK291450 EMBL· GenBank· DDBJ | BAF84139.1 EMBL· GenBank· DDBJ | mRNA | ||
CR749522 EMBL· GenBank· DDBJ | CAH18336.1 EMBL· GenBank· DDBJ | mRNA | ||
AY223820 EMBL· GenBank· DDBJ | AAO30127.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC033210 EMBL· GenBank· DDBJ | AAH33210.1 EMBL· GenBank· DDBJ | mRNA | ||
BC051765 EMBL· GenBank· DDBJ | AAH51765.1 EMBL· GenBank· DDBJ | mRNA |