O43353 · RIPK2_HUMAN
- ProteinReceptor-interacting serine/threonine-protein kinase 2
- GeneRIPK2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids540 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Acts as a key effector of NOD1 and NOD2 signaling pathways: upon activation by bacterial peptidoglycans, NOD1 and NOD2 oligomerize and recruit RIPK2 via CARD-CARD domains, leading to the formation of RIPK2 filaments (PubMed:17054981, PubMed:17562858, PubMed:21123652, PubMed:22607974, PubMed:28656966, PubMed:29452636, PubMed:30026309).
Once recruited, RIPK2 autophosphorylates and undergoes 'Lys-63'-linked polyubiquitination by E3 ubiquitin ligases XIAP, BIRC2 and BIRC3, as well as 'Met-1'-linked (linear) polyubiquitination by the LUBAC complex, becoming a scaffolding protein for downstream effectors (PubMed:22607974, PubMed:28545134, PubMed:29452636, PubMed:30026309, PubMed:30279485, PubMed:30478312).
'Met-1'-linked polyubiquitin chains attached to RIPK2 recruit IKBKG/NEMO, which undergoes 'Lys-63'-linked polyubiquitination in a RIPK2-dependent process (PubMed:17562858, PubMed:22607974, PubMed:29452636, PubMed:30026309).
'Lys-63'-linked polyubiquitin chains attached to RIPK2 serve as docking sites for TAB2 and TAB3 and mediate the recruitment of MAP3K7/TAK1 to IKBKG/NEMO, inducing subsequent activation of IKBKB/IKKB (PubMed:18079694).
In turn, NF-kappa-B is released from NF-kappa-B inhibitors and translocates into the nucleus where it activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis (PubMed:18079694).
The protein kinase activity is dispensable for the NOD1 and NOD2 signaling pathways (PubMed:29452636, PubMed:30026309).
Contributes to the tyrosine phosphorylation of the guanine exchange factor ARHGEF2 through Src tyrosine kinase leading to NF-kappa-B activation by NOD2 (PubMed:21887730).
Also involved in adaptive immunity: plays a role during engagement of the T-cell receptor (TCR) in promoting BCL10 phosphorylation and subsequent NF-kappa-B activation (PubMed:14638696).
Plays a role in the inactivation of RHOA in response to NGFR signaling (PubMed:26646181).
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Activity regulation
Upon activation, helix alphaC is displaced and the phosphorylated AS becomes disordered (PubMed:28545134).
Specifically inhibited by GSK583, which blocks NOD2 signaling by interfering with XIAP binding to RIPK2 (PubMed:29452636).
Specifically inhibited by CSLP37 and CSLP43, which blocks NOD2 signaling by interfering with XIAP binding to RIPK2 (PubMed:30026309).
Features
Showing features for binding site, active site.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameReceptor-interacting serine/threonine-protein kinase 2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO43353
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 47 | Abolishes protein-kinase activity without preventing ability to activate NF-kappa-B downstream of NOD2. | ||||
Sequence: K → A | ||||||
Mutagenesis | 47 | Abolishes protein-kinase activity. Reduces FAS-mediated apoptosis. | ||||
Sequence: K → M | ||||||
Mutagenesis | 95 | Abolished ability to activate NF-kappa-B downstream of NOD2. | ||||
Sequence: T → W | ||||||
Mutagenesis | 146 | Abolishes protein-kinase activity without preventing ability to activate NF-kappa-B downstream of NOD2. | ||||
Sequence: D → N | ||||||
Mutagenesis | 176 | Decreased phosphorylation and activation. Abolished phosphorylation by LRRK2. | ||||
Sequence: S → A | ||||||
Mutagenesis | 209 | Decreased polyubiquitination. | ||||
Sequence: K → R | ||||||
Natural variant | VAR_041045 | 259 | in dbSNP:rs2230801 | |||
Sequence: I → T | ||||||
Natural variant | VAR_041046 | 268 | in dbSNP:rs35004667 | |||
Sequence: L → V | ||||||
Natural variant | VAR_041047 | 313 | in dbSNP:rs35395048 | |||
Sequence: K → N | ||||||
Mutagenesis | 381 | Prevents phosphorylation. Reduces serine and threonine phosphorylation of ARHGEF2. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 410 | Reduced ubiquitination by XIAP and activation of NF-kappa-B; when associated with R-538. | ||||
Sequence: K → R | ||||||
Mutagenesis | 437 | Decreased interaction with NGFR. | ||||
Sequence: Q → E | ||||||
Mutagenesis | 444 | Abolishes interaction with NOD1. Abolished activation of NF-kappa-B. | ||||
Sequence: R → E | ||||||
Mutagenesis | 445 | Strongly decreased activation of NF-kappa-B. Does not affect activation of NF-kappa-B; when associated with E-458. | ||||
Sequence: E → R | ||||||
Mutagenesis | 449 | Strongly decreased activation of NF-kappa-B. | ||||
Sequence: N → D | ||||||
Mutagenesis | 450 | Increased activation of NF-kappa-B. | ||||
Sequence: Q → K | ||||||
Mutagenesis | 452 | Impaired interaction with NOD2 and decreased homooligomerization and ability to transmit NOD2 signaling. | ||||
Sequence: T → K | ||||||
Mutagenesis | 453 | Decreased homooligomerization and ability to transmit NOD2 signaling. | ||||
Sequence: E → K | ||||||
Mutagenesis | 455 | Decreased homooligomerization and ability to transmit NOD2 signaling. | ||||
Sequence: C → S | ||||||
Mutagenesis | 458 | Strongly decreased activation of NF-kappa-B. Does not affect activation of NF-kappa-B; when associated with R-445. | ||||
Sequence: Q → E | ||||||
Mutagenesis | 461 | Abolished activation of NF-kappa-B. | ||||
Sequence: D → R | ||||||
Mutagenesis | 467 | Decreased interaction with NGFR. | ||||
Sequence: D → R | ||||||
Mutagenesis | 470 | Decreased homooligomerization and ability to transmit NOD2 signaling. | ||||
Sequence: M → A or K | ||||||
Mutagenesis | 471 | Abolished activation of NF-kappa-B. | ||||
Sequence: K → D | ||||||
Mutagenesis | 471 | Decreased interaction with NGFR. | ||||
Sequence: K → E | ||||||
Mutagenesis | 472 | Abolished activation of NF-kappa-B. | ||||
Sequence: E → R | ||||||
Mutagenesis | 474 | Decreases interaction with NOD2. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 474 | Abolished activation of NF-kappa-B. | ||||
Sequence: Y → R | ||||||
Mutagenesis | 475 | Abolished activation of NF-kappa-B. | ||||
Sequence: E → R | ||||||
Mutagenesis | 483 | Abolished activation of NF-kappa-B. | ||||
Sequence: R → D | ||||||
Mutagenesis | 483 | Abolishes interaction with NOD1. | ||||
Sequence: R → E | ||||||
Mutagenesis | 488 | Abolishes interaction with NOD1. Abolished activation of NF-kappa-B. | ||||
Sequence: R → E | ||||||
Mutagenesis | 492 | Abolished activation of NF-kappa-B. | ||||
Sequence: D → K | ||||||
Mutagenesis | 496 | Decreased interaction with NGFR. | ||||
Sequence: I → A | ||||||
Mutagenesis | 497 | Increased activation of NF-kappa-B. | ||||
Sequence: Q → A or K | ||||||
Mutagenesis | 497 | Strongly decreased activation of NF-kappa-B. | ||||
Sequence: Q → E | ||||||
Mutagenesis | 500 | Decreased interaction with NGFR. | ||||
Sequence: E → R | ||||||
Mutagenesis | 503 | Abolished ubiquitination by ZNRF4. | ||||
Sequence: K → R | ||||||
Mutagenesis | 513 | Reduced formation of filaments and activation of NF-kappa-B. | ||||
Sequence: K → E | ||||||
Mutagenesis | 528 | Decreased interaction with NGFR. | ||||
Sequence: R → E | ||||||
Mutagenesis | 538 | Reduced ubiquitination by XIAP and activation of NF-kappa-B; when associated with R-410. | ||||
Sequence: K → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 493 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, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000086608 | 1-540 | UniProt | Receptor-interacting serine/threonine-protein kinase 2 | |||
Sequence: MNGEAICSALPTIPYHKLADLRYLSRGASGTVSSARHADWRVQVAVKHLHIHTPLLDSERKDVLREAEILHKARFSYILPILGICNEPEFLGIVTEYMPNGSLNELLHRKTEYPDVAWPLRFRILHEIALGVNYLHNMTPPLLHHDLKTQNILLDNEFHVKIADFGLSKWRMMSLSQSRSSKSAPEGGTIIYMPPENYEPGQKSRASIKHDIYSYAVITWEVLSRKQPFEDVTNPLQIMYSVSQGHRPVINEESLPYDIPHRARMISLIESGWAQNPDERPSFLKCLIELEPVLRTFEEITFLEAVIQLKKTKLQSVSSAIHLCDKKKMELSLNIPVNHGPQEESCGSSQLHENSGSPETSRSLPAPQDNDFLSRKAQDCYFMKLHHCPGNHSWDSTISGSQRAAFCDHKTTPCSSAIINPLSTAGNSERLQPGIAQQWIQSKREDIVNQMTEACLNQSLDALLSRDLIMKEDYELVSTKPTRTSKVRQLLDTTDIQGEEFAKVIVQKLKDNKQMGLQPYPEILVVSRSPSLNLLQNKSM | |||||||
Modified residue | 149 | UniProt | (Microbial infection) O-acetylthreonine; by Yersinia YopJ | ||||
Sequence: T | |||||||
Modified residue | 168 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 168 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 174 | UniProt | (Microbial infection) O-acetylserine; by Yersinia YopJ | ||||
Sequence: S | |||||||
Modified residue | 174 | UniProt | Phosphoserine; alternate | ||||
Sequence: S | |||||||
Modified residue | 176 | UniProt | (Microbial infection) O-acetylserine; by Yersinia YopJ; alternate | ||||
Sequence: S | |||||||
Modified residue | 176 | UniProt | Phosphoserine; by autocatalysis and LRRK2; alternate | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 176 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 178 | UniProt | (Microbial infection) O-acetylserine; by Yersinia YopJ | ||||
Sequence: S | |||||||
Modified residue | 178 | UniProt | Phosphoserine; alternate | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 178 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 180 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 181 | UniProt | (Microbial infection) O-acetylserine; by Yersinia YopJ | ||||
Sequence: S | |||||||
Modified residue | 181 | UniProt | Phosphoserine; alternate | ||||
Sequence: S | |||||||
Modified residue | 183 | UniProt | (Microbial infection) O-acetylserine; by Yersinia YopJ | ||||
Sequence: S | |||||||
Modified residue | 189 | UniProt | (Microbial infection) O-acetylthreonine; by Yersinia YopJ | ||||
Sequence: T | |||||||
Cross-link | 209 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 355 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 357 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 363 | UniProt | (Microbial infection) O-acetylserine; by Yersinia YopJ | ||||
Sequence: S | |||||||
Modified residue | 363 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 363 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 381 | UniProt | Phosphotyrosine; by CSK | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 381 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 393 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 393 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 397 | UniProt | (Microbial infection) O-acetylthreonine; by Yersinia YopJ | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 401 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 410 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue | 423 | UniProt | (Microbial infection) O-acetylserine; by Yersinia YopJ | ||||
Sequence: S | |||||||
Modified residue | 474 | UniProt | Phosphotyrosine; by autocatalysis | ||||
Sequence: Y | |||||||
Cross-link | 503 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue | 527 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 527 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 529 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 529 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 531 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 531 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 538 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue | 539 | UniProt | Phosphoserine | ||||
Sequence: S |
Post-translational modification
'Lys-63'-linked polyubiquitination by XIAP is essential for NOD2 signaling and promotes recruitment of the LUBAC complex (PubMed:22607974, PubMed:29452636, PubMed:30026309).
Also polyubiquitinated with 'Lys-63'-linked chains by PELI3, BIRC2/c-IAP1 and BIRC3/c-IAP2 (PubMed:19464198, PubMed:21931591).
Ubiquitinated on Lys-209 via 'Lys-63'-linked by ITCH (PubMed:18079694, PubMed:19592251).
Undergoes 'Lys-63'-linked deubiquitination by MYSM1 to attenuate NOD2-mediated inflammation and tissue damage (By similarity).
Polyubiquitinated with 'Lys-63'-linked chains in response to Shigella infection, promoting its SQSTM1/p62-dependent autophagic degradation (PubMed:36221902).
Undergoes 'Met-1'-linked polyubiquitination; the head-to-tail linear polyubiquitination is mediated by the LUBAC complex in response to NOD2 stimulation 'Met-1'-linked polyubiquitination (PubMed:23806334).
'Lys-63'-linked polyubiquitination by XIAP is required for recruimtent of the LUBAC complex and subsequent (PubMed:22607974).
Linear polyubiquitination is restricted by FAM105B/otulin, probably to limit NOD2-dependent pro-inflammatory signaling activation of NF-kappa-B (PubMed:23806334).
Ubiquitination at Lys-503 by ZNRF4 via 'Lys-48'-linked polyubiquitination promotes RIPK2 degradation by the proteasome; ubiquitination by ZNRF4 takes place during both acute and NOD2 tolerance conditions (PubMed:28656966).
Phosphorylated at Ser-176, either via autophosphorylation or by LRRK2, enhancing activity (PubMed:16824733, PubMed:27830463).
Autophosphorylation at Tyr-474 is required for effective NOD2 signaling (PubMed:21123652).
Autophosphorylation is however not essential for NOD2 signaling (PubMed:29452636).
Phosphorylation at Tyr-381 by Src kinase CSK occurs in a ARHGEF2-dependent manner and is required for NOD2-dependent innate immune activation (PubMed:21887730).
IRGM promotes NOD1/NOD2-RIPK2 RIPosome recruitment to autophagosome membranes (PubMed:36221902).
RIPK2 biquitinated via 'Lys-63'-linked chains is then recognized by SQSTM1/p62, leading to the SQSTM1/p62-dependent autophagic degradation of the NOD1/NOD2-RIPK2 RIPosome (PubMed:36221902).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts (via CARD domain) with NOD1 (via CARD domain) (PubMed:17054981, PubMed:30478312).
Homooligomer; following interaction with NOD1 or NOD2, homooligomerizes via its CARD domain and forms long filaments named RIPosomes (PubMed:30279485, PubMed:30478312).
Found in a signaling complex consisting of at least ARHGEF2, NOD2 and RIPK2 (PubMed:21887730).
Interacts with ARHGEF2; the interaction mediates tyrosine phosphorylation of RIPK2 by Src kinase CSK (PubMed:21887730).
Interacts with MAP3K4; this interaction sequesters RIPK2 from the NOD2 signaling pathway (PubMed:18775659).
Interacts with IKBKG/NEMO (PubMed:18079694).
The polyubiquitinated protein interacts with MAP3K7/TAK1; interaction is indirect and is mediated by TAB2 and TAB3 that bind to polyubiquitin chains attached to RIPK2 (PubMed:18079694).
Binds to CFLAR/CLARP and CASP1 via their CARD domains (PubMed:9575181).
Binds to BIRC3/c-IAP1 and BIRC2/c-IAP2, TRAF1, TRAF2, TRAF5 and TRAF6 (PubMed:21931591).
Interacts with NLRP10 (PubMed:22672233).
Interacts with CARD9 (By similarity).
Interacts with INAVA; the interaction takes place upon PRR stimulation (PubMed:28436939).
Interacts (via CARD domain) with NGFR (via death domain) (PubMed:26646181).
Interacts with IRGM; promoting RIPK2 degradation (PubMed:36221902).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O43353 | BIRC2 Q13490 | 3 | EBI-358522, EBI-514538 | |
BINARY | O43353 | BIRC3 Q13489 | 3 | EBI-358522, EBI-517709 | |
BINARY | O43353 | CARD6 Q9BX69 | 2 | EBI-358522, EBI-14405242 | |
BINARY | O43353 | MAVS Q7Z434 | 3 | EBI-358522, EBI-995373 | |
BINARY | O43353 | NOD1 Q9Y239 | 5 | EBI-358522, EBI-1051262 | |
BINARY | O43353 | NOD2 Q9HC29 | 3 | EBI-358522, EBI-7445625 | |
BINARY | O43353 | RIPK2 O43353 | 6 | EBI-358522, EBI-358522 | |
BINARY | O43353 | TRAF2 Q12933 | 2 | EBI-358522, EBI-355744 | |
BINARY | O43353 | TRAF3 Q13114 | 6 | EBI-358522, EBI-357631 | |
BINARY | O43353 | XIAP P98170 | 22 | EBI-358522, EBI-517127 | |
BINARY | O43353 | YWHAE P62258 | 2 | EBI-358522, EBI-356498 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 18-294 | Protein kinase | ||||
Sequence: LADLRYLSRGASGTVSSARHADWRVQVAVKHLHIHTPLLDSERKDVLREAEILHKARFSYILPILGICNEPEFLGIVTEYMPNGSLNELLHRKTEYPDVAWPLRFRILHEIALGVNYLHNMTPPLLHHDLKTQNILLDNEFHVKIADFGLSKWRMMSLSQSRSSKSAPEGGTIIYMPPENYEPGQKSRASIKHDIYSYAVITWEVLSRKQPFEDVTNPLQIMYSVSQGHRPVINEESLPYDIPHRARMISLIESGWAQNPDERPSFLKCLIELEPVL | ||||||
Region | 65-73 | Helix alphaC | ||||
Sequence: REAEILHKA | ||||||
Region | 167-193 | Activation segment (AS) | ||||
Sequence: LSKWRMMSLSQSRSSKSAPEGGTIIYM | ||||||
Compositional bias | 338-368 | Polar residues | ||||
Sequence: NHGPQEESCGSSQLHENSGSPETSRSLPAPQ | ||||||
Region | 338-369 | Disordered | ||||
Sequence: NHGPQEESCGSSQLHENSGSPETSRSLPAPQD | ||||||
Domain | 432-524 | CARD | ||||
Sequence: QPGIAQQWIQSKREDIVNQMTEACLNQSLDALLSRDLIMKEDYELVSTKPTRTSKVRQLLDTTDIQGEEFAKVIVQKLKDNKQMGLQPYPEIL |
Domain
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
O43353-1
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
- Length540
- Mass (Da)61,195
- Last updated1998-11-01 v2
- Checksum575A692239505792
O43353-2
- Name2
- Differences from canonical
- 1-137: Missing
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_013266 | 1-137 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 271 | in Ref. 5; BAH13484 | ||||
Sequence: S → G | ||||||
Compositional bias | 338-368 | Polar residues | ||||
Sequence: NHGPQEESCGSSQLHENSGSPETSRSLPAPQ | ||||||
Sequence conflict | 514 | in Ref. 5; BAH13484 | ||||
Sequence: Q → R |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF027706 EMBL· GenBank· DDBJ | AAC34970.1 EMBL· GenBank· DDBJ | mRNA | ||
AF078530 EMBL· GenBank· DDBJ | AAC27722.1 EMBL· GenBank· DDBJ | mRNA | ||
AF064824 EMBL· GenBank· DDBJ | AAC25668.1 EMBL· GenBank· DDBJ | mRNA | ||
AY358813 EMBL· GenBank· DDBJ | AAQ89172.1 EMBL· GenBank· DDBJ | mRNA | ||
AY358814 EMBL· GenBank· DDBJ | AAQ89173.1 EMBL· GenBank· DDBJ | mRNA | ||
AK301448 EMBL· GenBank· DDBJ | BAH13484.1 EMBL· GenBank· DDBJ | mRNA | ||
AC004003 EMBL· GenBank· DDBJ | AAC24561.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF117829 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC004553 EMBL· GenBank· DDBJ | AAH04553.1 EMBL· GenBank· DDBJ | mRNA |