P35609 · ACTN2_HUMAN
- ProteinAlpha-actinin-2
- GeneACTN2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids894 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 766 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 770 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 777 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 802 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 804 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 808 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: T |
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 | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAlpha-actinin-2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP35609
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Colocalizes with MYOZ1 and FLNC at the Z-lines of skeletal muscle.
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Cardiomyopathy, familial hypertrophic, 23, with or without left ventricular non-compaction (CMH23)
- Note
- DescriptionA hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.
- See alsoMIM:612158
Natural variants in CMH23
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_071970 | 119 | A>T | in CMH23 and CMD1AA; dbSNP:rs727502886 | |
VAR_074292 | 228 | M>T | in CMH23; dbSNP:rs786205144 | |
VAR_071971 | 495 | T>M | in CMH23; dbSNP:rs200248944 | |
VAR_071972 | 583 | E>A | in CMH23; dbSNP:rs200631005 | |
VAR_071973 | 628 | E>G | in CMH23; dbSNP:rs786204951 |
Cardiomyopathy, dilated, 1AA, with or without left ventricular non-compaction (CMD1AA)
- Note
- DescriptionA disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.
- See alsoMIM:612158
Natural variants in CMD1AA
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_054628 | 9 | Q>R | in CMD1AA; dbSNP:rs121434525 | |
VAR_071970 | 119 | A>T | in CMH23 and CMD1AA; dbSNP:rs727502886 |
Congenital myopathy 8 (CMYP8)
- Note
- DescriptionAn autosomal dominant muscular disorder characterized by progressive early-onset muscle weakness, gait difficulties, loss of ambulation, and respiratory insufficiency. Morphological and ultrastructural analyses of muscle biopsies reveal type 1 fiber predominance, multiple structured cores forming a circular arrangement beneath the sarcolemma, and jagged Z-lines.
- See alsoMIM:618654
Natural variants in CMYP8
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_083366 | 727 | L>R | in CMYP8; dbSNP:rs1572148902 | |
VAR_083367 | 732-742 | missing | in CMYP8; uncertain significance |
Myopathy, distal, 6, adult onset, autosomal dominant (MPD6)
- Note
- DescriptionAn autosomal dominant muscular disorder characterized by adult onset of asymmetric distal muscle weakness, primarily affecting the lower limbs and resulting in gait difficulties. Some patients develop involvement of proximal and upper limb muscles.
- See alsoMIM:618655
Natural variants in MPD6
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_083364 | 131 | L>P | in MPD6; uncertain significance; dbSNP:rs1572114611 | |
VAR_083365 | 487 | C>R | in MPD6; dbSNP:rs1572140109 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_054628 | 9 | in CMD1AA; dbSNP:rs121434525 | |||
Sequence: Q → R | ||||||
Natural variant | VAR_071970 | 119 | in CMH23 and CMD1AA; dbSNP:rs727502886 | |||
Sequence: A → T | ||||||
Natural variant | VAR_083364 | 131 | in MPD6; uncertain significance; dbSNP:rs1572114611 | |||
Sequence: L → P | ||||||
Natural variant | VAR_074292 | 228 | in CMH23; dbSNP:rs786205144 | |||
Sequence: M → T | ||||||
Natural variant | VAR_083365 | 487 | in MPD6; dbSNP:rs1572140109 | |||
Sequence: C → R | ||||||
Natural variant | VAR_071971 | 495 | in CMH23; dbSNP:rs200248944 | |||
Sequence: T → M | ||||||
Natural variant | VAR_071972 | 583 | in CMH23; dbSNP:rs200631005 | |||
Sequence: E → A | ||||||
Natural variant | VAR_033487 | 604 | in dbSNP:rs35997569 | |||
Sequence: M → V | ||||||
Natural variant | VAR_071973 | 628 | in CMH23; dbSNP:rs786204951 | |||
Sequence: E → G | ||||||
Natural variant | VAR_083366 | 727 | in CMYP8; dbSNP:rs1572148902 | |||
Sequence: L → R | ||||||
Natural variant | VAR_083367 | 732-742 | in CMYP8; uncertain significance | |||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,359 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000073435 | 1-894 | UniProt | Alpha-actinin-2 | |||
Sequence: MNQIEPGVQYNYVYDEDEYMIQEEEWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPKPDRGKMRFHKIANVNKALDYIASKGVKLVSIGAEEIVDGNVKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKHLDIPKMLDAEDIVNTPKPDERAIMTYVSCFYHAFAGAEQAETAANRICKVLAVNQENERLMEEYERLASELLEWIRRTIPWLENRTPEKTMQAMQKKLEDFRDYRRKHKPPKVQEKCQLEINFNTLQTKLRISNRPAFMPSEGKMVSDIAGAWQRLEQAEKGYEEWLLNEIRRLERLEHLAEKFRQKASTHETWAYGKEQILLQKDYESASLTEVRALLRKHEAFESDLAAHQDRVEQIAAIAQELNELDYHDAVNVNDRCQKICDQWDRLGTLTQKRREALERMEKLLETIDQLHLEFAKRAAPFNNWMEGAMEDLQDMFIVHSIEEIQSLITAHEQFKATLPEADGERQSIMAIQNEVEKVIQSYNIRISSSNPYSTVTMDELRTKWDKVKQLVPIRDQSLQEELARQHANERLRRQFAAQANAIGPWIQNKMEEIARSSIQITGALEDQMNQLKQYEHNIINYKNNIDKLEGDHQLIQEALVFDNKHTNYTMEHIRVGWELLLTTIARTINEVETQILTRDAKGITQEQMNEFRASFNHFDRRKNGLMDHEDFRACLISMGYDLGEAEFARIMTLVDPNGQGTVTFQSFIDFMTRETADTDTAEQVIASFRILASDKPYILAEELRRELPPDQAQYCIKRMPAYSGPGSVPGALDYAAFSSALYGESDL | |||||||
Modified residue (large scale data) | 50 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 57 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 109 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 147 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 178 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 201 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 237 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 237 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 308 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 347 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 411 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 412 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 415 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 418 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 431 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 433 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 435 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 449 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 574 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 589 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 594 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 595 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 596 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 603 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 609 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 624 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 681 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 688 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 715 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 716 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 744 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 751 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 761 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 840 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Ubiquitinated by FBXL22, leading to proteasomal degradation.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in both skeletal and cardiac muscle.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homodimer; antiparallel. Also forms heterodimers with ACTN3. Interacts with ADAM12, MYOZ1, MYOZ2 and MYOZ3. Interacts via its C-terminal region with the LDB3 PDZ domain. Interacts with XIRP2. Interacts with DST isoform 1 (via N-terminus). Interacts with PARVB. Interacts with SYNPO2.
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-254 | Actin-binding | ||||
Sequence: MNQIEPGVQYNYVYDEDEYMIQEEEWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPKPDRGKMRFHKIANVNKALDYIASKGVKLVSIGAEEIVDGNVKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKHLDIPKMLDAEDIVNTPKPDERAIMTYVSCFYH | ||||||
Domain | 38-142 | Calponin-homology (CH) 1 | ||||
Sequence: KQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPKPDRGKMRFHKIANVNKALDYIASKGVKLVSIGAEEIVDGNVKMTLGMIWTIILRFA | ||||||
Domain | 151-257 | Calponin-homology (CH) 2 | ||||
Sequence: TSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKHLDIPKMLDAEDIVNTPKPDERAIMTYVSCFYHAFA | ||||||
Repeat | 281-391 | Spectrin 1 | ||||
Sequence: RLMEEYERLASELLEWIRRTIPWLENRTPEKTMQAMQKKLEDFRDYRRKHKPPKVQEKCQLEINFNTLQTKLRISNRPAFMPSEGKMVSDIAGAWQRLEQAEKGYEEWLLN | ||||||
Repeat | 401-506 | Spectrin 2 | ||||
Sequence: HLAEKFRQKASTHETWAYGKEQILLQKDYESASLTEVRALLRKHEAFESDLAAHQDRVEQIAAIAQELNELDYHDAVNVNDRCQKICDQWDRLGTLTQKRREALER | ||||||
Repeat | 516-627 | Spectrin 3 | ||||
Sequence: QLHLEFAKRAAPFNNWMEGAMEDLQDMFIVHSIEEIQSLITAHEQFKATLPEADGERQSIMAIQNEVEKVIQSYNIRISSSNPYSTVTMDELRTKWDKVKQLVPIRDQSLQE | ||||||
Repeat | 637-740 | Spectrin 4 | ||||
Sequence: RLRRQFAAQANAIGPWIQNKMEEIARSSIQITGALEDQMNQLKQYEHNIINYKNNIDKLEGDHQLIQEALVFDNKHTNYTMEHIRVGWELLLTTIARTINEVET | ||||||
Domain | 753-788 | EF-hand 1 | ||||
Sequence: EQMNEFRASFNHFDRRKNGLMDHEDFRACLISMGYD | ||||||
Domain | 789-824 | EF-hand 2 | ||||
Sequence: LGEAEFARIMTLVDPNGQGTVTFQSFIDFMTRETAD |
Sequence similarities
Belongs to the alpha-actinin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
P35609-1
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
- Length894
- Mass (Da)103,854
- Last updated1994-06-01 v1
- Checksum7F612C1C3B3E2299
P35609-2
- Name2
- Differences from canonical
- 234-261: IVNTPKPDERAIMTYVSCFYHAFAGAEQ → LVYTARPDERAIMTYVSCYYHAFAGAQK
Computationally mapped potential isoform sequences
There are 8 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A804HI95 | A0A804HI95_HUMAN | ACTN2 | 863 | ||
A0A804HKG0 | A0A804HKG0_HUMAN | ACTN2 | 163 | ||
A0A494C031 | A0A494C031_HUMAN | ACTN2 | 61 | ||
A0A494C033 | A0A494C033_HUMAN | ACTN2 | 182 | ||
A0A494C166 | A0A494C166_HUMAN | ACTN2 | 263 | ||
A0A494C1A0 | A0A494C1A0_HUMAN | ACTN2 | 858 | ||
A0A494C0Q3 | A0A494C0Q3_HUMAN | ACTN2 | 131 | ||
A0A494C060 | A0A494C060_HUMAN | ACTN2 | 588 |
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_054923 | 234-261 | in isoform 2 | |||
Sequence: IVNTPKPDERAIMTYVSCFYHAFAGAEQ → LVYTARPDERAIMTYVSCYYHAFAGAQK |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M86406 EMBL· GenBank· DDBJ | AAA51583.1 EMBL· GenBank· DDBJ | mRNA | ||
M86804 EMBL· GenBank· DDBJ | AAA51584.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ249756 EMBL· GenBank· DDBJ | CAB61269.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ249757 EMBL· GenBank· DDBJ | CAB61269.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ249758 EMBL· GenBank· DDBJ | CAB61269.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ249759 EMBL· GenBank· DDBJ | CAB61269.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ249760 EMBL· GenBank· DDBJ | CAB61269.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ249761 EMBL· GenBank· DDBJ | CAB61269.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ249762 EMBL· GenBank· DDBJ | CAB61269.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ249763 EMBL· GenBank· DDBJ | CAB61269.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ249764 EMBL· GenBank· DDBJ | CAB61269.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ249765 EMBL· GenBank· DDBJ | CAB61269.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ249766 EMBL· GenBank· DDBJ | CAB61269.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ249767 EMBL· GenBank· DDBJ | CAB61269.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ249768 EMBL· GenBank· DDBJ | CAB61269.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ249769 EMBL· GenBank· DDBJ | CAB61269.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ249770 EMBL· GenBank· DDBJ | CAB61269.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ249771 EMBL· GenBank· DDBJ | CAB61269.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ249772 EMBL· GenBank· DDBJ | CAB61269.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ249773 EMBL· GenBank· DDBJ | CAB61269.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ249774 EMBL· GenBank· DDBJ | CAB61269.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ249775 EMBL· GenBank· DDBJ | CAB61269.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ249776 EMBL· GenBank· DDBJ | CAB61269.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK315250 EMBL· GenBank· DDBJ | BAG37672.1 EMBL· GenBank· DDBJ | mRNA | ||
AL359185 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL359921 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471098 EMBL· GenBank· DDBJ | EAW70064.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471098 EMBL· GenBank· DDBJ | EAW70065.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC047901 EMBL· GenBank· DDBJ | AAH47901.2 EMBL· GenBank· DDBJ | mRNA | ||
BC051770 EMBL· GenBank· DDBJ | AAH51770.2 EMBL· GenBank· DDBJ | mRNA |