P17181 · INAR1_HUMAN
- ProteinInterferon alpha/beta receptor 1
- GeneIFNAR1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids557 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Type I interferon binding activates the JAK-STAT signaling cascade, resulting in transcriptional activation or repression of interferon-regulated genes that encode the effectors of the interferon response (PubMed:10049744, PubMed:21854986, PubMed:7665574).
Mechanistically, type I interferon-binding brings the IFNAR1 and IFNAR2 subunits into close proximity with one another, driving their associated Janus kinases (JAKs) (TYK2 bound to IFNAR1 and JAK1 bound to IFNAR2) to cross-phosphorylate one another (PubMed:21854986, PubMed:32972995, PubMed:7665574, PubMed:7813427).
The activated kinases phosphorylate specific tyrosine residues on the intracellular domains of IFNAR1 and IFNAR2, forming docking sites for the STAT transcription factors (PubMed:21854986, PubMed:32972995, PubMed:7526154, PubMed:7665574, PubMed:7813427).
STAT proteins are then phosphorylated by the JAKs, promoting their translocation into the nucleus to regulate expression of interferon-regulated genes (PubMed:19561067, PubMed:21854986, PubMed:32972995, PubMed:7665574, PubMed:7813427, PubMed:9121453).
Can also act independently of IFNAR2: form an active IFNB1 receptor by itself and activate a signaling cascade that does not involve activation of the JAK-STAT pathway (By similarity).
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | late endosome | |
Cellular Component | lysosome | |
Cellular Component | plasma membrane | |
Molecular Function | cytokine binding | |
Molecular Function | JAK pathway signal transduction adaptor activity | |
Molecular Function | type I interferon binding | |
Molecular Function | type I interferon receptor activity | |
Biological Process | cell surface receptor signaling pathway via JAK-STAT | |
Biological Process | cellular response to interferon-alpha | |
Biological Process | cellular response to interferon-beta | |
Biological Process | cellular response to virus | |
Biological Process | positive regulation of cellular respiration | |
Biological Process | response to lipopolysaccharide | |
Biological Process | response to virus | |
Biological Process | type I interferon-mediated signaling pathway |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameInterferon alpha/beta receptor 1
- Short namesIFN-R-1; IFN-alpha/beta receptor 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP17181
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Isoform 1
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 28-436 | Extracellular | ||||
Sequence: KNLKSPQKVEVDIIDDNFILRWNRSDESVGNVTFSFDYQKTGMDNWIKLSGCQNITSTKCNFSSLKLNVYEEIKLRIRAEKENTSSWYEVDSFTPFRKAQIGPPEVHLEAEDKAIVIHISPGTKDSVMWALDGLSFTYSLVIWKNSSGVEERIENIYSRHKIYKLSPETTYCLKVKAALLTSWKIGVYSPVHCIKTTVENELPPPENIEVSVQNQNYVLKWDYTYANMTFQVQWLHAFLKRNPGNHLYKWKQIPDCENVKTTQCVFPQNVFQKGIYLLRVQASDGNNTSFWSEEIKFDTEIQAFLLPPVFNIRSLSDSFHIYIGAPKQSGNTPVIQDYPLIYEIIFWENTSNAERKIIEKKTDVTVPNLKPLTVYCVKARAHTMDEKLNKSSVFSDAVCEKTKPGNTSK | ||||||
Transmembrane | 437-457 | Helical | ||||
Sequence: IWLIVGICIALFALPFVIYAA | ||||||
Topological domain | 458-557 | Cytoplasmic | ||||
Sequence: KVFLRCINYVFFPSLKPSSSIDEYFSEQPLKNLLLSTSEEQIEKCFIIENISTIATVEETNQTDEDHKKYSSQTSQDSGNYSNEDESESKTSEELQQDFV |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Immunodeficiency 106, susceptibility to viral infections (IMD106)
- Note
- DescriptionAn autosomal recessive immunologic disorder characterized by increased susceptibility to viral infections beginning in infancy or early childhood. IMD106 affected individuals may demonstrate adverse reactions to vaccination with live attenuated viral vaccines, most notably measles, mumps and rubella (MMR) and yellow fever vaccines. A subset of IMD106 patients develop severe reactions, including excessive hyperinflammatory response, encephalopathy, acute respiratory distress syndrome, and multiorgan failure. IMD106 may also predispose to severe respiratory infection with SARS-CoV-2.
- See alsoMIM:619935
Natural variants in IMD106
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_087556 | 261-557 | missing | in IMD106; decreased protein abundance | |
VAR_087557 | 308-557 | missing | in IMD106; no protein detected in homozygous patient cells; loss of type I interferon receptor activity | |
VAR_087558 | 386-557 | missing | in IMD106; loss of localization at the plasma membrane; loss of type I interferon receptor activity |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_084085 | 24 | no effect on activation of STAT1 upon IFNA2 or IFNG binding; dbSNP:rs779701967 | |||
Sequence: A → V | ||||||
Natural variant | VAR_084086 | 57 | no effect on activation of STAT1 upon IFNA2 or IFNG binding; dbSNP:rs201532160 | |||
Sequence: G → R | ||||||
Natural variant | VAR_084087 | 73 | abolished STAT1 activation upon IFNA2 binding but no effect upon IFNG binding; dbSNP:rs181939581 | |||
Sequence: W → C | ||||||
Natural variant | VAR_084088 | 80 | no effect on activation of STAT1 upon IFNA2 or IFNG binding IFNG binding; dbSNP:rs1333470928 | |||
Sequence: Q → H | ||||||
Natural variant | VAR_084089 | 83 | no effect on activation of STAT1 upon IFNA2 or IFNG binding | |||
Sequence: T → A | ||||||
Natural variant | VAR_084090 | 88 | no effect on activation of STAT1 upon IFNA2 or IFNG binding; dbSNP:rs577823502 | |||
Sequence: N → S | ||||||
Natural variant | VAR_002717 | 168 | in dbSNP:rs2257167 | |||
Sequence: V → L | ||||||
Natural variant | VAR_084091 | 169 | no effect on activation of STAT1 upon IFNA2 or IFNG binding; dbSNP:rs747690835 | |||
Sequence: I → M | ||||||
Natural variant | VAR_084092 | 183 | no effect on activation of STAT1 upon IFNA2 or IFNG binding; dbSNP:rs770624214 | |||
Sequence: I → V | ||||||
Natural variant | VAR_087556 | 261-557 | in IMD106; decreased protein abundance | |||
Sequence: Missing | ||||||
Natural variant | VAR_084093 | 306 | no effect on activation of STAT1 upon IFNA2 or IFNG binding; dbSNP:rs201281365 | |||
Sequence: R → C | ||||||
Natural variant | VAR_020502 | 307 | no effect on activation of STAT1 upon IFNA2 or IFNG binding; dbSNP:rs17875833 | |||
Sequence: V → I | ||||||
Natural variant | VAR_087557 | 308-557 | in IMD106; no protein detected in homozygous patient cells; loss of type I interferon receptor activity | |||
Sequence: Missing | ||||||
Natural variant | VAR_084094 | 335 | decreased STAT1 activation upon IFNA2 binding but no effect upon IFNG binding | |||
Sequence: Missing | ||||||
Natural variant | VAR_020503 | 359 | in dbSNP:rs17875834 | |||
Sequence: T → M | ||||||
Natural variant | VAR_084095 | 386 | no effect on activation of STAT1 upon IFNA2 or IFNG binding; requires 2 nucleotide substitutions | |||
Sequence: E → L | ||||||
Natural variant | VAR_087558 | 386-557 | in IMD106; loss of localization at the plasma membrane; loss of type I interferon receptor activity | |||
Sequence: Missing | ||||||
Natural variant | VAR_084096 | 422 | abolished STAT1 activation upon IFNA2 binding but no effect upon IFNG binding; dbSNP:rs746291558 | |||
Sequence: S → R | ||||||
Natural variant | VAR_084097 | 424 | no effect on activation of STAT1 upon IFNA2 or IFNG binding; dbSNP:rs541858922 | |||
Sequence: A → T | ||||||
Mutagenesis | 466 | Impairs internalization in response to interferon. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 491-492 | Impairs interaction with TYK2. | ||||
Sequence: LL → AA | ||||||
Mutagenesis | 496-497 | Impairs interaction with TYK2. | ||||
Sequence: EE → AA | ||||||
Mutagenesis | 500 | Impairs interaction with TYK2. | ||||
Sequence: E → A | ||||||
Mutagenesis | 501 | Mildly reduces ubiquitination. Nearly abolishes ubiquitination and subsequent degradation; when associated with 525-R-R-526. | ||||
Sequence: K → R | ||||||
Natural variant | VAR_084098 | 515 | no effect on activation of STAT1 upon IFNA2 or IFNG binding; dbSNP:rs778182995 | |||
Sequence: E → K | ||||||
Mutagenesis | 525-526 | Reduces ubiquitination. Nearly abolishes ubiquitination and subsequent degradation; when associated with R-501. | ||||
Sequence: KK → RR | ||||||
Mutagenesis | 535 | Abolishes interaction with FBXW11 and decreases ubiquitination. | ||||
Sequence: S → A | ||||||
Mutagenesis | 535 | Abolishes phosphorylation at this site and interaction with SHMT2. | ||||
Sequence: S → A | ||||||
Mutagenesis | 539 | Abolishes interaction with FBXW11 and decreases ubiquitination. | ||||
Sequence: S → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 605 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, glycosylation, disulfide bond, lipidation, modified residue, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-27 | UniProt | |||||
Sequence: MMVVLLGATTLVLVAVAPWVLSAAAGG | |||||||
Chain | PRO_0000011001 | 28-557 | UniProt | Interferon alpha/beta receptor 1 | |||
Sequence: KNLKSPQKVEVDIIDDNFILRWNRSDESVGNVTFSFDYQKTGMDNWIKLSGCQNITSTKCNFSSLKLNVYEEIKLRIRAEKENTSSWYEVDSFTPFRKAQIGPPEVHLEAEDKAIVIHISPGTKDSVMWALDGLSFTYSLVIWKNSSGVEERIENIYSRHKIYKLSPETTYCLKVKAALLTSWKIGVYSPVHCIKTTVENELPPPENIEVSVQNQNYVLKWDYTYANMTFQVQWLHAFLKRNPGNHLYKWKQIPDCENVKTTQCVFPQNVFQKGIYLLRVQASDGNNTSFWSEEIKFDTEIQAFLLPPVFNIRSLSDSFHIYIGAPKQSGNTPVIQDYPLIYEIIFWENTSNAERKIIEKKTDVTVPNLKPLTVYCVKARAHTMDEKLNKSSVFSDAVCEKTKPGNTSKIWLIVGICIALFALPFVIYAAKVFLRCINYVFFPSLKPSSSIDEYFSEQPLKNLLLSTSEEQIEKCFIIENISTIATVEETNQTDEDHKKYSSQTSQDSGNYSNEDESESKTSEELQQDFV | |||||||
Glycosylation | 50 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 58 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 79↔87 | UniProt | |||||
Sequence: CQNITSTKC | |||||||
Glycosylation | 81 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 88 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 110 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 172 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 199↔220 | UniProt | |||||
Sequence: CLKVKAALLTSWKIGVYSPVHC | |||||||
Glycosylation | 254 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 283↔291 | UniProt | |||||
Sequence: CENVKTTQC | |||||||
Glycosylation | 313 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 314 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 376 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 403↔426 | UniProt | |||||
Sequence: CVKARAHTMDEKLNKSSVFSDAVC | |||||||
Glycosylation | 416 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 433 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Lipidation | 463 | UniProt | S-palmitoyl cysteine | ||||
Sequence: C | |||||||
Modified residue | 466 | UniProt | Phosphotyrosine; by TYK2 | ||||
Sequence: Y | |||||||
Modified residue | 481 | UniProt | Phosphotyrosine; by TYK2 | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 493 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 494 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 495 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 495 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 501 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Cross-link | 525 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Cross-link | 526 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue | 535 | UniProt | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Polyubiquitinated via 'Lys-48'-linked and 'Lys-63'-linked ubiquitin chains, leading to receptor internalization and lysosomal degradation (PubMed:18056411).
The 'Lys-63'-linked ubiquitin chains are cleaved off by the BRISC complex (PubMed:24075985).
Phosphorylated on serine residues in response to interferon binding; this promotes interaction with FBXW11 and ubiquitination (PubMed:14532120, PubMed:15337770, PubMed:24075985).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with TYK2 (PubMed:15337770, PubMed:24704786, PubMed:7526154).
Interacts with STAT1 and STAT2; the interaction requires its phosphorylation at Tyr-466 (PubMed:9121453).
Interacts (serine-phosphorylated form) with FBXW11, the substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex (PubMed:14532120, PubMed:15337770, PubMed:18056411).
Interacts with SHMT2; this promotes interaction with ABRAXAS2 and the BRISC complex (PubMed:24075985).
Interacts with TRIM10; this interaction prevents association between IFNAR1 and TYK2 (PubMed:33811647).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P17181 | FBXW11 Q9UKB1 | 9 | EBI-1547250, EBI-355189 | |
BINARY | P17181 | LAPTM4B Q86VI4 | 3 | EBI-1547250, EBI-3267258 | |
BINARY | P17181 | STAT1 P42224 | 2 | EBI-1547250, EBI-1057697 | |
BINARY | P17181 | STAT2 P52630 | 5 | EBI-1547250, EBI-1546963 | |
BINARY | P17181-1 | TYK2 P29597 | 3 | EBI-16099379, EBI-1383454 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 32-126 | Fibronectin type-III 1 | ||||
Sequence: SPQKVEVDIIDDNFILRWNRSDESVGNVTFSFDYQKTGMDNWIKLSGCQNITSTKCNFSSLKLNVYEEIKLRIRAEKENTSSWYEVDSFTPFRKA | ||||||
Domain | 127-227 | Fibronectin type-III 2 | ||||
Sequence: QIGPPEVHLEAEDKAIVIHISPGTKDSVMWALDGLSFTYSLVIWKNSSGVEERIENIYSRHKIYKLSPETTYCLKVKAALLTSWKIGVYSPVHCIKTTVEN | ||||||
Domain | 231-329 | Fibronectin type-III 3 | ||||
Sequence: PPENIEVSVQNQNYVLKWDYTYANMTFQVQWLHAFLKRNPGNHLYKWKQIPDCENVKTTQCVFPQNVFQKGIYLLRVQASDGNNTSFWSEEIKFDTEIQ | ||||||
Domain | 331-432 | Fibronectin type-III 4 | ||||
Sequence: FLLPPVFNIRSLSDSFHIYIGAPKQSGNTPVIQDYPLIYEIIFWENTSNAERKIIEKKTDVTVPNLKPLTVYCVKARAHTMDEKLNKSSVFSDAVCEKTKPG | ||||||
Region | 491-500 | Important for interaction with TYK2 | ||||
Sequence: LLSTSEEQIE | ||||||
Region | 516-557 | Disordered | ||||
Sequence: ETNQTDEDHKKYSSQTSQDSGNYSNEDESESKTSEELQQDFV | ||||||
Compositional bias | 540-557 | Basic and acidic residues | ||||
Sequence: NEDESESKTSEELQQDFV |
Sequence similarities
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 4 isoforms produced by Alternative splicing.
P17181-1
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
- Length557
- Mass (Da)63,525
- Last updated2006-03-07 v3
- Checksum24A01779DB7F356F
P17181-2
- Name2
- SynonymsSol-1, Soluble form 1
- NoteIncomplete sequence.
P17181-3
- Name3
- SynonymsSol-2, Soluble form 2
- NoteIncomplete sequence.
P17181-4
- Name4
- Differences from canonical
- 1-69: Missing
Computationally mapped potential isoform sequences
There are 13 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
C9J114 | C9J114_HUMAN | IFNAR1 | 458 | ||
A0A494BZU5 | A0A494BZU5_HUMAN | IFNAR1 | 236 | ||
A0A8V8TQJ9 | A0A8V8TQJ9_HUMAN | IFNAR1 | 78 | ||
A0A8V8TQK8 | A0A8V8TQK8_HUMAN | IFNAR1 | 303 | ||
A0A494C0E2 | A0A494C0E2_HUMAN | IFNAR1 | 270 | ||
A0A494C0K3 | A0A494C0K3_HUMAN | IFNAR1 | 67 | ||
A0A494C0P2 | A0A494C0P2_HUMAN | IFNAR1 | 128 | ||
A0A994J6V0 | A0A994J6V0_HUMAN | IFNAR1 | 381 | ||
A0A994J6F9 | A0A994J6F9_HUMAN | IFNAR1 | 184 | ||
A0A994J6F6 | A0A994J6F6_HUMAN | IFNAR1 | 552 | ||
A0A994J4B0 | A0A994J4B0_HUMAN | IFNAR1 | 135 | ||
A0A994J479 | A0A994J479_HUMAN | IFNAR1 | 227 | ||
A0A994J3P7 | A0A994J3P7_HUMAN | IFNAR1 | 395 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_055322 | 1-69 | in isoform 4 | |||
Sequence: Missing | ||||||
Sequence conflict | 17 | in Ref. 1; AAA52730 | ||||
Sequence: A → G | ||||||
Sequence conflict | 59 | in Ref. 4; BAD96532 | ||||
Sequence: V → M | ||||||
Sequence conflict | 279 | in Ref. 4; BAD96532 | ||||
Sequence: Q → R | ||||||
Sequence conflict | 344 | in Ref. 3; BAG35516 | ||||
Sequence: D → G | ||||||
Alternative sequence | VSP_029928 | 414-421 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_029930 | 428-434 | in isoform 2 | |||
Sequence: KTKPGNT → NISLNSH | ||||||
Alternative sequence | VSP_029929 | 428-480 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_029931 | 435-557 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 479 | in Ref. 4; BAD96532 | ||||
Sequence: D → N | ||||||
Compositional bias | 540-557 | Basic and acidic residues | ||||
Sequence: NEDESESKTSEELQQDFV |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
J03171 EMBL· GenBank· DDBJ | AAA52730.1 EMBL· GenBank· DDBJ | mRNA | ||
X60459 EMBL· GenBank· DDBJ | CAA42992.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK298051 EMBL· GenBank· DDBJ | BAG60345.1 EMBL· GenBank· DDBJ | mRNA | ||
AK312631 EMBL· GenBank· DDBJ | BAG35516.1 EMBL· GenBank· DDBJ | mRNA | ||
AK222770 EMBL· GenBank· DDBJ | BAD96490.1 EMBL· GenBank· DDBJ | mRNA | ||
AK222812 EMBL· GenBank· DDBJ | BAD96532.1 EMBL· GenBank· DDBJ | mRNA | ||
AY654286 EMBL· GenBank· DDBJ | AAT49100.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF039907 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AP000296 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AP000297 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AP000298 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471079 EMBL· GenBank· DDBJ | EAX09837.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471079 EMBL· GenBank· DDBJ | EAX09839.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC002590 EMBL· GenBank· DDBJ | AAH02590.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
BC021825 EMBL· GenBank· DDBJ | AAH21825.1 EMBL· GenBank· DDBJ | mRNA |