P00751 · CFAB_HUMAN
- ProteinComplement factor B
- GeneCFB
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids764 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Factor B which is part of the alternate pathway of the complement system is cleaved by factor D into 2 fragments: Ba and Bb. Bb, a serine protease, then combines with complement factor 3b to generate the C3 or C5 convertase. It has also been implicated in proliferation and differentiation of preactivated B-lymphocytes, rapid spreading of peripheral blood monocytes, stimulation of lymphocyte blastogenesis and lysis of erythrocytes. Ba inhibits the proliferation of preactivated B-lymphocytes.
Catalytic activity
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 526 | Charge relay system | ||||
Sequence: H | ||||||
Active site | 576 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 699 | Charge relay system | ||||
Sequence: S |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | blood microparticle | |
Cellular Component | extracellular exosome | |
Cellular Component | extracellular region | |
Cellular Component | extracellular space | |
Cellular Component | plasma membrane | |
Molecular Function | complement binding | |
Molecular Function | serine-type endopeptidase activity | |
Biological Process | complement activation | |
Biological Process | complement activation, alternative pathway | |
Biological Process | proteolysis | |
Biological Process | response to bacterium |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameComplement factor B
- EC number
- 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 accessionP00751
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Macular degeneration, age-related, 14 (ARMD14)
- Note
- DescriptionA form of age-related macular degeneration, a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.
- See alsoMIM:615489
Hemolytic uremic syndrome, atypical, 4 (AHUS4)
- Note
- DescriptionAn atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-stage renal disease.
- See alsoMIM:612924
Natural variants in AHUS4
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_063659 | 166 | S>P | in AHUS4 | |
VAR_063660 | 203 | R>Q | in AHUS4; dbSNP:rs745794224 | |
VAR_063661 | 242 | I>L | in AHUS4; dbSNP:rs144812066 | |
VAR_063221 | 286 | F>L | in AHUS4; gain-of-function mutation that results in enhanced formation of the C3bBb; dbSNP:rs117905900 | |
VAR_063222 | 323 | K>E | in AHUS4; gain-of-function mutation that results in enhanced formation of the C3bBb; dbSNP:rs121909748 | |
VAR_063662 | 323 | K>Q | in AHUS4 | |
VAR_063663 | 458 | M>I | in AHUS4; dbSNP:rs200837114 | |
VAR_063664 | 533 | K>R | in AHUS4; benign; dbSNP:rs149101394 |
Complement factor B deficiency (CFBD)
- Note
- DescriptionAn immunologic disorder characterized by increased susceptibility to bacterial infections, particularly Neisseria infections, due to a defect in the alternative complement pathway.
- See alsoMIM:615561
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_016274 | 9 | may be associated with a reduced risk for age-related macular degeneration; dbSNP:rs4151667 | |||
Sequence: L → H | ||||||
Natural variant | VAR_006493 | 28 | in allele FA; requires 2 nucleotide substitutions | |||
Sequence: W → Q | ||||||
Natural variant | VAR_006492 | 28 | in allele S | |||
Sequence: W → R | ||||||
Natural variant | VAR_006494 | 32 | in allele S; may be associated with a reduced risk for age-related macular degeneration; dbSNP:rs641153 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_016275 | 32 | in dbSNP:rs12614 | |||
Sequence: R → W | ||||||
Natural variant | VAR_063659 | 166 | in AHUS4 | |||
Sequence: S → P | ||||||
Natural variant | VAR_063660 | 203 | in AHUS4; dbSNP:rs745794224 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_063661 | 242 | in AHUS4; dbSNP:rs144812066 | |||
Sequence: I → L | ||||||
Natural variant | VAR_016276 | 252 | in dbSNP:rs4151651 | |||
Sequence: G → S | ||||||
Natural variant | VAR_063221 | 286 | in AHUS4; gain-of-function mutation that results in enhanced formation of the C3bBb; dbSNP:rs117905900 | |||
Sequence: F → L | ||||||
Natural variant | VAR_063222 | 323 | in AHUS4; gain-of-function mutation that results in enhanced formation of the C3bBb; dbSNP:rs121909748 | |||
Sequence: K → E | ||||||
Natural variant | VAR_063662 | 323 | in AHUS4 | |||
Sequence: K → Q | ||||||
Mutagenesis | 348-350 | Decreases binding to the pro-C3-convertase complex. Does not affect Complement C3 beta chain binding. | ||||
Sequence: KLK → AAA | ||||||
Natural variant | VAR_063663 | 458 | in AHUS4; dbSNP:rs200837114 | |||
Sequence: M → I | ||||||
Natural variant | VAR_063664 | 533 | in AHUS4; benign; dbSNP:rs149101394 | |||
Sequence: K → R | ||||||
Natural variant | VAR_016277 | 565 | in dbSNP:rs4151659 | |||
Sequence: K → E | ||||||
Natural variant | VAR_016278 | 651 | in dbSNP:rs4151660 | |||
Sequence: D → E | ||||||
Natural variant | VAR_006495 | 736 | in allele FA | |||
Sequence: A → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,283 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 signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-25 | |||||
Sequence: MGSNLSPQLCLMPFILGLLSGGVTT | ||||||
Chain | PRO_0000027546 | 26-259 | Complement factor B Ba fragment | |||
Sequence: TPWSLARPQGSCSLEGVEIKGGSFRLLQEGQALEYVCPSGFYPYPVQTRTCRSTGSWSTLKTQDQKTVRKAECRAIHCPRPHDFENGEYWPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAICDNGAGYCSNPGIPIGTRKVGSQYRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSCQDSFMYDTPQEVAEAFLSSLTETIEGVDAEDGHGPGEQQKR | ||||||
Chain | PRO_0000027545 | 26-764 | Complement factor B | |||
Sequence: TPWSLARPQGSCSLEGVEIKGGSFRLLQEGQALEYVCPSGFYPYPVQTRTCRSTGSWSTLKTQDQKTVRKAECRAIHCPRPHDFENGEYWPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAICDNGAGYCSNPGIPIGTRKVGSQYRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSCQDSFMYDTPQEVAEAFLSSLTETIEGVDAEDGHGPGEQQKRKIVLDPSGSMNIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSEADSSNADWVTKQLNEINYEDHKLKSGTNTKKALQAVYSMMSWPDDVPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPREDYLDVYVFGVGPLVNQVNINALASKKDNEQHVFKVKDMENLEDVFYQMIDESQSLSLCGMVWEHRKGTDYHKQPWQAKISVIRPSKGHESCMGAVVSEYFVLTAAHCFTVDDKEHSIKVSVGGEKRDLEIEVVLFHPNYNINGKKEAGIPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTTRALRLPPTTTCQQQKEELLPAQDIKALFVSEEEKKLTRKEVYIKNGDKKGSCERDAQYAPGYDKVKDISEVVTPRFLCTGGVSPYADPNTCRGDSGGPLIVHKRSRFIQVGVISWGVVDVCKNQKRQKQVPAHARDFHINLFQVLPWLKEKLQDEDLGFL | ||||||
Disulfide bond | 37↔76 | |||||
Sequence: CSLEGVEIKGGSFRLLQEGQALEYVCPSGFYPYPVQTRTC | ||||||
Disulfide bond | 62↔98 | |||||
Sequence: CPSGFYPYPVQTRTCRSTGSWSTLKTQDQKTVRKAEC | ||||||
Disulfide bond | 103↔145 | |||||
Sequence: CPRPHDFENGEYWPRSPYYNVSDEISFHCYDGYTLRGSANRTC | ||||||
Glycosylation | 122 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 131↔158 | |||||
Sequence: CYDGYTLRGSANRTCQVNGRWSGQTAIC | ||||||
Glycosylation | 142 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 165↔205 | |||||
Sequence: CSNPGIPIGTRKVGSQYRLEDSVTYHCSRGLTLRGSQRRTC | ||||||
Disulfide bond | 191↔218 | |||||
Sequence: CSRGLTLRGSQRRTCQEGGSWSGTEPSC | ||||||
Chain | PRO_0000027547 | 260-764 | Complement factor B Bb fragment | |||
Sequence: KIVLDPSGSMNIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSEADSSNADWVTKQLNEINYEDHKLKSGTNTKKALQAVYSMMSWPDDVPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPREDYLDVYVFGVGPLVNQVNINALASKKDNEQHVFKVKDMENLEDVFYQMIDESQSLSLCGMVWEHRKGTDYHKQPWQAKISVIRPSKGHESCMGAVVSEYFVLTAAHCFTVDDKEHSIKVSVGGEKRDLEIEVVLFHPNYNINGKKEAGIPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTTRALRLPPTTTCQQQKEELLPAQDIKALFVSEEEKKLTRKEVYIKNGDKKGSCERDAQYAPGYDKVKDISEVVTPRFLCTGGVSPYADPNTCRGDSGGPLIVHKRSRFIQVGVISWGVVDVCKNQKRQKQVPAHARDFHINLFQVLPWLKEKLQDEDLGFL | ||||||
Glycosylation | 285 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 291 | N-linked (Glc) (glycation) lysine | ||||
Sequence: K | ||||||
Glycosylation | 378 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 478↔596 | |||||
Sequence: CGMVWEHRKGTDYHKQPWQAKISVIRPSKGHESCMGAVVSEYFVLTAAHCFTVDDKEHSIKVSVGGEKRDLEIEVVLFHPNYNINGKKEAGIPEFYDYDVALIKLKNKLKYGQTIRPIC | ||||||
Disulfide bond | 511↔527 | |||||
Sequence: CMGAVVSEYFVLTAAHC | ||||||
Disulfide bond | 599↔615 | |||||
Sequence: CTEGTTRALRLPPTTTC | ||||||
Disulfide bond | 656↔682 | |||||
Sequence: CERDAQYAPGYDKVKDISEVVTPRFLC | ||||||
Disulfide bond | 695↔725 | |||||
Sequence: CRGDSGGPLIVHKRSRFIQVGVISWGVVDVC |
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Interaction
Subunit
Monomer (PubMed:19574954).
Part of the C3-convertase enzyme complex comprised of Complement C3 beta chain (C3b) and Complement factor B Bb fragment (Bb) and CFP (PubMed:28264884, PubMed:31507604).
Interacts to C3b; this interaction is dependent on the presence of Mg2+ (PubMed:28264884, PubMed:31507604).
Interacts to CFP; this interaction contributes to the stabilization of the active C3-convertase enzyme complex (PubMed:31507604).
Part of the C3-convertase enzyme complex comprised of Complement C3 beta chain (C3b) and Complement factor B Bb fragment (Bb) and CFP (PubMed:28264884, PubMed:31507604).
Interacts to C3b; this interaction is dependent on the presence of Mg2+ (PubMed:28264884, PubMed:31507604).
Interacts to CFP; this interaction contributes to the stabilization of the active C3-convertase enzyme complex (PubMed:31507604).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P00751 | C3 P01024 | 3 | EBI-1223668, EBI-905851 | |
BINARY | P00751 | CFHR4 Q92496-1 | 2 | EBI-1223668, EBI-22033617 | |
BINARY | P00751 | CFHR4 Q92496-3 | 2 | EBI-1223668, EBI-22033638 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 35-100 | Sushi 1 | ||||
Sequence: GSCSLEGVEIKGGSFRLLQEGQALEYVCPSGFYPYPVQTRTCRSTGSWSTLKTQDQKTVRKAECRA | ||||||
Domain | 101-160 | Sushi 2 | ||||
Sequence: IHCPRPHDFENGEYWPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAICDN | ||||||
Domain | 163-220 | Sushi 3 | ||||
Sequence: GYCSNPGIPIGTRKVGSQYRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSCQD | ||||||
Domain | 270-469 | VWFA | ||||
Sequence: NIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSEADSSNADWVTKQLNEINYEDHKLKSGTNTKKALQAVYSMMSWPDDVPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPREDYLDVYVFGVGPLVNQVNINALASKKDNEQHVFKVKDMENLEDVFYQMI | ||||||
Domain | 477-757 | Peptidase S1 | ||||
Sequence: LCGMVWEHRKGTDYHKQPWQAKISVIRPSKGHESCMGAVVSEYFVLTAAHCFTVDDKEHSIKVSVGGEKRDLEIEVVLFHPNYNINGKKEAGIPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTTRALRLPPTTTCQQQKEELLPAQDIKALFVSEEEKKLTRKEVYIKNGDKKGSCERDAQYAPGYDKVKDISEVVTPRFLCTGGVSPYADPNTCRGDSGGPLIVHKRSRFIQVGVISWGVVDVCKNQKRQKQVPAHARDFHINLFQVLPWLKEKLQ |
Domain
The unliganded VWA domain has an inactive 'locked' conformation whereby the scissile Arg-259|Lys-260 bond is protected from proteolytic activation.
Sequence similarities
Belongs to the peptidase S1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
P00751-1
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
- Length764
- Mass (Da)85,533
- Last updated1994-10-01 v2
- Checksum8BB6C101CC6AC200
P00751-2
- Name2
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F8WBL9 | F8WBL9_HUMAN | CFB | 86 | ||
H7C5H1 | H7C5H1_HUMAN | CFB | 692 | ||
A0A8V8TNU0 | A0A8V8TNU0_HUMAN | CFB | 687 | ||
A0A8V8TMI9 | A0A8V8TMI9_HUMAN | CFB | 483 | ||
A0A0G2JH38 | A0A0G2JH38_HUMAN | CFB | 589 |
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 297 | in Ref. 13; AA sequence | ||||
Sequence: I → T | ||||||
Sequence conflict | 300 | in Ref. 12; AAA36225 | ||||
Sequence: V → L | ||||||
Sequence conflict | 328 | in Ref. 12; AAA36225 | ||||
Sequence: D → V | ||||||
Sequence conflict | 356-357 | in Ref. 12; AAA36225 | ||||
Sequence: KK → EE | ||||||
Sequence conflict | 537 | in Ref. 15; AAA36219 | ||||
Sequence: I → T | ||||||
Alternative sequence | VSP_005380 | 543-621 | in isoform 2 | |||
Sequence: GEKRDLEIEVVLFHPNYNINGKKEAGIPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTTRALRLPPTTTCQQQKEE → KDATEGPGLHLCSPGNTSHFLQILHSTHPQCSPIPCTPDQSGMGEDVKLGMTRGQRQEAAHKEVVPTLLLQEGRSGTWR | ||||||
Alternative sequence | VSP_005381 | 622-764 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 764 | in Ref. 15; AAA36220 | ||||
Sequence: L → H |
Polymorphism
Two major variants, F and S, and 2 minor variants, as well as at least 14 very rare variants, have been identified.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X72875 EMBL· GenBank· DDBJ | CAA51389.1 EMBL· GenBank· DDBJ | mRNA | ||
S67310 EMBL· GenBank· DDBJ | AAD13989.1 EMBL· GenBank· DDBJ | mRNA | ||
L15702 EMBL· GenBank· DDBJ | AAA16820.1 EMBL· GenBank· DDBJ | mRNA | ||
X00284 EMBL· GenBank· DDBJ | CAA25077.1 EMBL· GenBank· DDBJ | mRNA | ||
AF349679 EMBL· GenBank· DDBJ | AAK30167.1 EMBL· GenBank· DDBJ | mRNA | ||
AF019413 EMBL· GenBank· DDBJ | AAB67977.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF551848 EMBL· GenBank· DDBJ | AAN71991.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL662849 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL844853 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BX005143 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CR388219 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CR759782 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AK223400 EMBL· GenBank· DDBJ | BAD97120.1 EMBL· GenBank· DDBJ | mRNA | ||
AL645922 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471081 EMBL· GenBank· DDBJ | EAX03550.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC004143 EMBL· GenBank· DDBJ | AAH04143.1 EMBL· GenBank· DDBJ | mRNA | ||
BC007990 EMBL· GenBank· DDBJ | AAH07990.1 EMBL· GenBank· DDBJ | mRNA | ||
K01566 EMBL· GenBank· DDBJ | AAA36225.2 EMBL· GenBank· DDBJ | mRNA | ||
J00125 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
J00126 EMBL· GenBank· DDBJ | AAA36226.1 EMBL· GenBank· DDBJ | mRNA | ||
J00185 EMBL· GenBank· DDBJ | AAA36219.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
J00186 EMBL· GenBank· DDBJ | AAA36220.1 EMBL· GenBank· DDBJ | mRNA | ||
M15082 EMBL· GenBank· DDBJ | AAA59625.1 EMBL· GenBank· DDBJ | Genomic DNA |