P23276 · KELL_HUMAN
- ProteinKell blood group glycoprotein
- GeneKEL
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids732 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Zinc endopeptidase with endothelin-3-converting enzyme activity. Cleaves EDN1, EDN2 and EDN3, with a marked preference for EDN3.
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site, active site.
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 | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | Golgi apparatus | |
Cellular Component | membrane | |
Cellular Component | nucleoplasm | |
Cellular Component | plasma membrane | |
Molecular Function | metal ion binding | |
Molecular Function | metalloendopeptidase activity | |
Biological Process | establishment of localization in cell | |
Biological Process | intracellular calcium ion homeostasis | |
Biological Process | intracellular magnesium ion homeostasis | |
Biological Process | myelination | |
Biological Process | negative regulation of potassium ion transmembrane transport | |
Biological Process | potassium ion transmembrane transport | |
Biological Process | protein processing | |
Biological Process | regulation of axon diameter | |
Biological Process | regulation of cell size | |
Biological Process | skeletal muscle fiber development | |
Biological Process | vasoconstriction |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameKell blood group glycoprotein
- EC number
- CD Antigen Name
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP23276
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type II membrane protein
Note: Spans the erythrocyte membrane, and is attached to the underlying cytoskeleton.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-47 | Cytoplasmic | ||||
Sequence: MEGGDQSEEEPRERSQAGGMGTLWSQESTPEERLPVEGSRPWAVARR | ||||||
Transmembrane | 48-67 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: VLTAILILGLLLCFSVLLFY | ||||||
Topological domain | 68-732 | Extracellular | ||||
Sequence: NFQNCGPRPCETSVCLDLRDHYLASGNTSVAPCTDFFSFACGRAKETNNSFQELATKNKNRLRRILEVQNSWHPGSGEEKAFQFYNSCMDTLAIEAAGTGPLRQVIEELGGWRISGKWTSLNFNRTLRLLMSQYGHFPFFRAYLGPHPASPHTPVIQIDQPEFDVPLKQDQEQKIYAQIFREYLTYLNQLGTLLGGDPSKVQEHSSLSISITSRLFQFLRPLEQRRAQGKLFQMVTIDQLKEMAPAIDWLSCLQATFTPMSLSPSQSLVVHDVEYLKNMSQLVEEMLLKQRDFLQSHMILGLVVTLSPALDSQFQEARRKLSQKLRELTEQPPMPARPRWMKCVEETGTFFEPTLAALFVREAFGPSTRSAAMKLFTAIRDALITRLRNLPWMNEETQNMAQDKVAQLQVEMGASEWALKPELARQEYNDIQLGSSFLQSVLSCVRSLRARIVQSFLQPHPQHRWKVSPWDVNAYYSVSDHVVVFPAGLLQPPFFHPGYPRAVNFGAAGSIMAHELLHIFYQLLLPGGCLACDNHALQEAHLCLKRHYAAFPLPSRTSFNDSLTFLENAADVGGLAIALQAYSKRLLRHHGETVLPSLDLSPQQIFFRSYAQVMCRKPSPQDSHDTHSPPHLRVHGPLSSTPAFARYFRCARGALLNPSSRCQLW |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 72 | Loss of Kell-XK complex. | ||||
Sequence: C → S | ||||||
Natural variant | VAR_016265 | 163 | in dbSNP:rs8175974 | |||
Sequence: A → T | ||||||
Natural variant | VAR_006731 | 180 | in KEL24 antigen; dbSNP:rs61729039 | |||
Sequence: R → P | ||||||
Natural variant | VAR_006732 | 193 | in KEL1/K antigen; dbSNP:rs8176058 | |||
Sequence: T → M | ||||||
Natural variant | VAR_015120 | 248 | in KEL25 antigen; dbSNP:rs61729040 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_015121 | 249 | in KEL27 antigen; dbSNP:rs61729042 | |||
Sequence: E → K | ||||||
Natural variant | VAR_006734 | 281 | in KEL21/Kp(c) antigen; dbSNP:rs61729036 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_006733 | 281 | in KEL3/Kp(a) antigen; dbSNP:rs8176059 | |||
Sequence: R → W | ||||||
Natural variant | VAR_006735 | 302 | in KEL17 antigen; dbSNP:rs61729034 | |||
Sequence: V → A | ||||||
Mutagenesis | 319 | No loss of Kell-XK complex. | ||||
Sequence: C → S | ||||||
Natural variant | VAR_015122 | 322 | in KEL22 antigen; dbSNP:rs61729037 | |||
Sequence: A → V | ||||||
Natural variant | VAR_015123 | 382 | in KEL23 antigen; dbSNP:rs61729038 | |||
Sequence: Q → R | ||||||
Natural variant | VAR_015124 | 406 | in KEL26 antigen; dbSNP:rs61729041 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_015125 | 492 | in KEL19 antigen; dbSNP:rs61729035 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_006736 | 494 | in KEL10/Ul(a) antigen; dbSNP:rs61729032 | |||
Sequence: E → V | ||||||
Natural variant | VAR_015126 | 548 | in KEL12 antigen; dbSNP:rs61729033 | |||
Sequence: H → R | ||||||
Mutagenesis | 582 | Loss of catalytic activity. | ||||
Sequence: E → G | ||||||
Natural variant | VAR_006737 | 597 | in KEL6/Js(a) antigen; dbSNP:rs8176038 | |||
Sequence: L → P | ||||||
Natural variant | VAR_016266 | 726 | in dbSNP:rs8176048 | |||
Sequence: S → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,635 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, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000078227 | 1-732 | Kell blood group glycoprotein | |||
Sequence: MEGGDQSEEEPRERSQAGGMGTLWSQESTPEERLPVEGSRPWAVARRVLTAILILGLLLCFSVLLFYNFQNCGPRPCETSVCLDLRDHYLASGNTSVAPCTDFFSFACGRAKETNNSFQELATKNKNRLRRILEVQNSWHPGSGEEKAFQFYNSCMDTLAIEAAGTGPLRQVIEELGGWRISGKWTSLNFNRTLRLLMSQYGHFPFFRAYLGPHPASPHTPVIQIDQPEFDVPLKQDQEQKIYAQIFREYLTYLNQLGTLLGGDPSKVQEHSSLSISITSRLFQFLRPLEQRRAQGKLFQMVTIDQLKEMAPAIDWLSCLQATFTPMSLSPSQSLVVHDVEYLKNMSQLVEEMLLKQRDFLQSHMILGLVVTLSPALDSQFQEARRKLSQKLRELTEQPPMPARPRWMKCVEETGTFFEPTLAALFVREAFGPSTRSAAMKLFTAIRDALITRLRNLPWMNEETQNMAQDKVAQLQVEMGASEWALKPELARQEYNDIQLGSSFLQSVLSCVRSLRARIVQSFLQPHPQHRWKVSPWDVNAYYSVSDHVVVFPAGLLQPPFFHPGYPRAVNFGAAGSIMAHELLHIFYQLLLPGGCLACDNHALQEAHLCLKRHYAAFPLPSRTSFNDSLTFLENAADVGGLAIALQAYSKRLLRHHGETVLPSLDLSPQQIFFRSYAQVMCRKPSPQDSHDTHSPPHLRVHGPLSSTPAFARYFRCARGALLNPSSRCQLW | ||||||
Modified residue | 7 | Phosphoserine | ||||
Sequence: S | ||||||
Disulfide bond | 72 | Interchain (with C-347 in XK) | ||||
Sequence: C | ||||||
Disulfide bond | 77↔82 | |||||
Sequence: CETSVC | ||||||
Glycosylation | 94 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 100↔717 | |||||
Sequence: CTDFFSFACGRAKETNNSFQELATKNKNRLRRILEVQNSWHPGSGEEKAFQFYNSCMDTLAIEAAGTGPLRQVIEELGGWRISGKWTSLNFNRTLRLLMSQYGHFPFFRAYLGPHPASPHTPVIQIDQPEFDVPLKQDQEQKIYAQIFREYLTYLNQLGTLLGGDPSKVQEHSSLSISITSRLFQFLRPLEQRRAQGKLFQMVTIDQLKEMAPAIDWLSCLQATFTPMSLSPSQSLVVHDVEYLKNMSQLVEEMLLKQRDFLQSHMILGLVVTLSPALDSQFQEARRKLSQKLRELTEQPPMPARPRWMKCVEETGTFFEPTLAALFVREAFGPSTRSAAMKLFTAIRDALITRLRNLPWMNEETQNMAQDKVAQLQVEMGASEWALKPELARQEYNDIQLGSSFLQSVLSCVRSLRARIVQSFLQPHPQHRWKVSPWDVNAYYSVSDHVVVFPAGLLQPPFFHPGYPRAVNFGAAGSIMAHELLHIFYQLLLPGGCLACDNHALQEAHLCLKRHYAAFPLPSRTSFNDSLTFLENAADVGGLAIALQAYSKRLLRHHGETVLPSLDLSPQQIFFRSYAQVMCRKPSPQDSHDTHSPPHLRVHGPLSSTPAFARYFRC | ||||||
Disulfide bond | 108↔682 | |||||
Sequence: CGRAKETNNSFQELATKNKNRLRRILEVQNSWHPGSGEEKAFQFYNSCMDTLAIEAAGTGPLRQVIEELGGWRISGKWTSLNFNRTLRLLMSQYGHFPFFRAYLGPHPASPHTPVIQIDQPEFDVPLKQDQEQKIYAQIFREYLTYLNQLGTLLGGDPSKVQEHSSLSISITSRLFQFLRPLEQRRAQGKLFQMVTIDQLKEMAPAIDWLSCLQATFTPMSLSPSQSLVVHDVEYLKNMSQLVEEMLLKQRDFLQSHMILGLVVTLSPALDSQFQEARRKLSQKLRELTEQPPMPARPRWMKCVEETGTFFEPTLAALFVREAFGPSTRSAAMKLFTAIRDALITRLRNLPWMNEETQNMAQDKVAQLQVEMGASEWALKPELARQEYNDIQLGSSFLQSVLSCVRSLRARIVQSFLQPHPQHRWKVSPWDVNAYYSVSDHVVVFPAGLLQPPFFHPGYPRAVNFGAAGSIMAHELLHIFYQLLLPGGCLACDNHALQEAHLCLKRHYAAFPLPSRTSFNDSLTFLENAADVGGLAIALQAYSKRLLRHHGETVLPSLDLSPQQIFFRSYAQVMC | ||||||
Glycosylation | 115 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 155↔410 | |||||
Sequence: CMDTLAIEAAGTGPLRQVIEELGGWRISGKWTSLNFNRTLRLLMSQYGHFPFFRAYLGPHPASPHTPVIQIDQPEFDVPLKQDQEQKIYAQIFREYLTYLNQLGTLLGGDPSKVQEHSSLSISITSRLFQFLRPLEQRRAQGKLFQMVTIDQLKEMAPAIDWLSCLQATFTPMSLSPSQSLVVHDVEYLKNMSQLVEEMLLKQRDFLQSHMILGLVVTLSPALDSQFQEARRKLSQKLRELTEQPPMPARPRWMKC | ||||||
Glycosylation | 191 | N-linked (GlcNAc...) asparagine; in KEL2 antigen | ||||
Sequence: N | ||||||
Glycosylation | 345 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 610↔729 | |||||
Sequence: CLKRHYAAFPLPSRTSFNDSLTFLENAADVGGLAIALQAYSKRLLRHHGETVLPSLDLSPQQIFFRSYAQVMCRKPSPQDSHDTHSPPHLRVHGPLSSTPAFARYFRCARGALLNPSSRC | ||||||
Glycosylation | 627 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
N-glycosylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed at high levels in erythrocytes and testis (in Sertoli cells), and, at lower levels, in skeletal muscle, tonsils (in follicular dendritic cells), lymph node, spleen and appendix (at protein level). Also expressed in many adult and fetal nonerythroid tissues, including brain, spleen, lymph nodes and bone marrow.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Heterodimer with XK; disulfide-linked.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P23276 | ADIPOQ Q15848 | 3 | EBI-746662, EBI-10827839 | |
BINARY | P23276 | C5 P01031 | 3 | EBI-746662, EBI-8558308 | |
BINARY | P23276 | CLDN19 Q8N6F1-2 | 3 | EBI-746662, EBI-12256978 | |
BINARY | P23276 | PM20D2 Q8IYS1 | 3 | EBI-746662, EBI-11339910 | |
BINARY | P23276 | PRKACA P17612 | 3 | EBI-746662, EBI-476586 | |
BINARY | P23276 | SERPINH1 P50454 | 3 | EBI-746662, EBI-350723 | |
BINARY | P23276 | TGFBR2 P37173 | 3 | EBI-746662, EBI-296151 | |
BINARY | P23276 | TTMP Q5BVD1 | 3 | EBI-746662, EBI-10243654 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-15 | Basic and acidic residues | ||||
Sequence: MEGGDQSEEEPRERS | ||||||
Region | 1-37 | Disordered | ||||
Sequence: MEGGDQSEEEPRERSQAGGMGTLWSQESTPEERLPVE | ||||||
Domain | 76-732 | Peptidase M13 | ||||
Sequence: PCETSVCLDLRDHYLASGNTSVAPCTDFFSFACGRAKETNNSFQELATKNKNRLRRILEVQNSWHPGSGEEKAFQFYNSCMDTLAIEAAGTGPLRQVIEELGGWRISGKWTSLNFNRTLRLLMSQYGHFPFFRAYLGPHPASPHTPVIQIDQPEFDVPLKQDQEQKIYAQIFREYLTYLNQLGTLLGGDPSKVQEHSSLSISITSRLFQFLRPLEQRRAQGKLFQMVTIDQLKEMAPAIDWLSCLQATFTPMSLSPSQSLVVHDVEYLKNMSQLVEEMLLKQRDFLQSHMILGLVVTLSPALDSQFQEARRKLSQKLRELTEQPPMPARPRWMKCVEETGTFFEPTLAALFVREAFGPSTRSAAMKLFTAIRDALITRLRNLPWMNEETQNMAQDKVAQLQVEMGASEWALKPELARQEYNDIQLGSSFLQSVLSCVRSLRARIVQSFLQPHPQHRWKVSPWDVNAYYSVSDHVVVFPAGLLQPPFFHPGYPRAVNFGAAGSIMAHELLHIFYQLLLPGGCLACDNHALQEAHLCLKRHYAAFPLPSRTSFNDSLTFLENAADVGGLAIALQAYSKRLLRHHGETVLPSLDLSPQQIFFRSYAQVMCRKPSPQDSHDTHSPPHLRVHGPLSSTPAFARYFRCARGALLNPSSRCQLW | ||||||
Region | 684-703 | Disordered | ||||
Sequence: KPSPQDSHDTHSPPHLRVHG |
Sequence similarities
Belongs to the peptidase M13 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length732
- Mass (Da)82,824
- Last updated1996-02-01 v2
- Checksum604A168AD300EDB4
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E7ETW3 | E7ETW3_HUMAN | KEL | 47 | ||
H0Y8A1 | H0Y8A1_HUMAN | KEL | 156 | ||
A0A0J9YXC0 | A0A0J9YXC0_HUMAN | KEL | 186 | ||
A0A0J9YXV8 | A0A0J9YXV8_HUMAN | KEL | 204 | ||
E9PHG0 | E9PHG0_HUMAN | KEL | 184 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-15 | Basic and acidic residues | ||||
Sequence: MEGGDQSEEEPRERS |
Polymorphism
KEL is responsible for the Kell blood group system. The molecular basis of the K=KEL1/k=KEL2 blood group antigens is a single variation in position 193; Thr-193 corresponds to KEL2 and Met-193 to KEL1 (PubMed:7849312).
The molecular basis of the Kpa=KEL3/Kpb=KEL4/Kpc=KEL21 blood group antigens is a single variation in position 281; Arg-281 corresponds to KEL4, Trp-281 to KEL3 and Gln-281 to KEL21 (PubMed:8669078).
The molecular basis of the Jsa=KEL6/Jsb=KEL7 blood group antigens is a single variation in position 597; Leu-597 corresponds to KEL7 and Pro-597 to KEL6 (PubMed:7570911).
The molecular basis of the KEL11/KEL17 blood group antigens is a single variation in position 302; Val-302 corresponds to KEL11 and Ala-302 to KEL17 (PubMed:8669078).
The molecular basis of the KEL14/KEL24 blood group antigens is a single variation in position 180; Arg-180 corresponds to KEL14 and Pro-180 to KEL24 (PubMed:9354821).
The molecular basis of the Kpa=KEL3/Kpb=KEL4/Kpc=KEL21 blood group antigens is a single variation in position 281; Arg-281 corresponds to KEL4, Trp-281 to KEL3 and Gln-281 to KEL21 (PubMed:8669078).
The molecular basis of the Jsa=KEL6/Jsb=KEL7 blood group antigens is a single variation in position 597; Leu-597 corresponds to KEL7 and Pro-597 to KEL6 (PubMed:7570911).
The molecular basis of the KEL11/KEL17 blood group antigens is a single variation in position 302; Val-302 corresponds to KEL11 and Ala-302 to KEL17 (PubMed:8669078).
The molecular basis of the KEL14/KEL24 blood group antigens is a single variation in position 180; Arg-180 corresponds to KEL14 and Pro-180 to KEL24 (PubMed:9354821).
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M64934 EMBL· GenBank· DDBJ | AAA03192.1 EMBL· GenBank· DDBJ | mRNA | ||
AF172627 EMBL· GenBank· DDBJ | AAB33459.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF172609 EMBL· GenBank· DDBJ | AAB33459.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF172610 EMBL· GenBank· DDBJ | AAB33459.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF172611 EMBL· GenBank· DDBJ | AAB33459.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF172612 EMBL· GenBank· DDBJ | AAB33459.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF172613 EMBL· GenBank· DDBJ | AAB33459.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF172614 EMBL· GenBank· DDBJ | AAB33459.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF172615 EMBL· GenBank· DDBJ | AAB33459.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF172616 EMBL· GenBank· DDBJ | AAB33459.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF172617 EMBL· GenBank· DDBJ | AAB33459.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF172618 EMBL· GenBank· DDBJ | AAB33459.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF172619 EMBL· GenBank· DDBJ | AAB33459.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF172620 EMBL· GenBank· DDBJ | AAB33459.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF172621 EMBL· GenBank· DDBJ | AAB33459.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF172622 EMBL· GenBank· DDBJ | AAB33459.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF172623 EMBL· GenBank· DDBJ | AAB33459.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF172624 EMBL· GenBank· DDBJ | AAB33459.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF172625 EMBL· GenBank· DDBJ | AAB33459.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF172626 EMBL· GenBank· DDBJ | AAB33459.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY228336 EMBL· GenBank· DDBJ | AAO38053.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK314831 EMBL· GenBank· DDBJ | BAG37351.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471198 EMBL· GenBank· DDBJ | EAW51891.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC003135 EMBL· GenBank· DDBJ | AAH03135.1 EMBL· GenBank· DDBJ | mRNA | ||
BC050639 EMBL· GenBank· DDBJ | AAH50639.1 EMBL· GenBank· DDBJ | mRNA | ||
AF279657 EMBL· GenBank· DDBJ | AAK69488.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
S80081 EMBL· GenBank· DDBJ | AAB47018.1 EMBL· GenBank· DDBJ | Genomic DNA |