Q5TCZ1 · SPD2A_HUMAN
- ProteinSH3 and PX domain-containing protein 2A
- GeneSH3PXD2A
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1133 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Adapter protein involved in invadopodia and podosome formation, extracellular matrix degradation and invasiveness of some cancer cells. Binds matrix metalloproteinases (ADAMs), NADPH oxidases (NOXs) and phosphoinositides. Acts as an organizer protein that allows NOX1- or NOX3-dependent reactive oxygen species (ROS) generation and ROS localization. In association with ADAM12, mediates the neurotoxic effect of amyloid-beta peptide.
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 | anchoring junction | |
Cellular Component | cell projection | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | podosome | |
Molecular Function | phosphatidylinositol-3,4-bisphosphate binding | |
Molecular Function | phosphatidylinositol-3-phosphate binding | |
Molecular Function | phosphatidylinositol-4,5-bisphosphate binding | |
Molecular Function | phosphatidylinositol-4-phosphate binding | |
Molecular Function | phosphatidylinositol-5-phosphate binding | |
Molecular Function | protease binding | |
Molecular Function | superoxide-generating NADPH oxidase activator activity | |
Biological Process | in utero embryonic development | |
Biological Process | osteoclast fusion | |
Biological Process | superoxide anion generation | |
Biological Process | superoxide metabolic process |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSH3 and PX domain-containing protein 2A
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ5TCZ1
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Cytoplasmic in normal cells and localizes to podosomes in SRC-transformed cells.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 42 | Loss of binding to (PtdIns3P) and (PtdIns(3,4)P2). | ||||
Sequence: R → A | ||||||
Mutagenesis | 93 | Loss of binding to (PtdIns3P) and (PtdIns(3,4)P2). | ||||
Sequence: R → A | ||||||
Natural variant | VAR_030781 | 659 | in dbSNP:rs11818820 | |||
Sequence: K → Q | ||||||
Natural variant | VAR_030782 | 1035 | in dbSNP:rs3781365 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_056993 | 1073 | in dbSNP:rs12764700 | |||
Sequence: L → P |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,328 variants from UniProt as well as other sources including ClinVar and dbSNP.
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_0000278488 | 1-1133 | UniProt | SH3 and PX domain-containing protein 2A | |||
Sequence: MLAYCVQDATVVDVEKRRNPSKHYVYIINVTWSDSTSQTIYRRYSKFFDLQMQLLDKFPIEGGQKDPKQRIIPFLPGKILFRRSHIRDVAVKRLKPIDEYCRALVRLPPHISQCDEVFRFFEARPEDVNPPKEDYGSSKRKSVWLSSWAESPKKDVTGADATAEPMILEQYVVVSNYKKQENSELSLQAGEVVDVIEKNESGWWFVSTSEEQGWVPATYLEAQNGTRDDSDINTSKTGEVSKRRKAHLRRLDRRWTLGGMVNRQHSREEKYVTVQPYTSQSKDEIGFEKGVTVEVIRKNLEGWWYIRYLGKEGWAPASYLKKAKDDLPTRKKNLAGPVEIIGNIMEISNLLNKKASGDKETPPAEGEGHEAPIAKKEISLPILCNASNGSAVGVPDRTVSRLAQGSPAVARIAPQRAQISSPNLRTRPPPRRESSLGFQLPKPPEPPSVEVEYYTIAEFQSCISDGISFRGGQKAEVIDKNSGGWWYVQIGEKEGWAPASYIDKRKKPNLSRRTSTLTRPKVPPPAPPSKPKEAEEGPTGASESQDSPRKLKYEEPEYDIPAFGFDSEPELSEEPVEDRASGERRPAQPHRPSPASSLQRARFKVGESSEDVALEEETIYENEGFRPYAEDTLSARGSSGDSDSPGSSSLSLTRKNSPKSGSPKSSSLLKLKAEKNAQAEMGKNHSSASFSSSITINTTCCSSSSSSSSSLSKTSGDLKPRSASDAGIRGTPKVRAKKDADANAGLTSCPRAKPSVRPKPFLNRAESQSQEKMDISTLRRQLRPTGQLRGGLKGSKSEDSELPPQTASEAPSEGSRRSSSDLITLPATTPPCPTKKEWEGPATSYMTCSAYQKVQDSEISFPAGVEVQVLEKQESGWWYVRFGELEGWAPSHYLVLDENEQPDPSGKELDTVPAKGRQNEGKSDSLEKIERRVQALNTVNQSKKATPPIPSKPPGGFGKTSGTPAVKMRNGVRQVAVRPQSVFVSPPPKDNNLSCALRRNESLTATDGLRGVRRNSSFSTARSAAAEAKGRLAERAASQGSDSPLLPAQRNSIPVSPVRPKPIEKSQFIHNNLKDVYVSIADYEGDEETAGFQEGVSMEVLERNPNGWWYCQILDGVKPFKGWVPSNYLEKKN | |||||||
Modified residue (large scale data) | 186 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 256 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 256 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 361 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 379 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 406 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 406 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 420 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 421 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 421 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 515 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 544 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 547 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 547 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 553 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 558 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 567 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 567 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 572 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 593 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 593 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 596 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 597 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 608 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 634 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 638 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 642 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 644 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 644 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 649 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 651 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 653 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 662 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 722 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 724 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 731 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 731 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 748 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 767 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 767 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 769 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 795 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 797 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 800 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 819 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 819 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 829 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 946 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 981 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1002 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1002 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1016 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1016 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1017 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1017 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1038 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1038 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1041 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1043 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1052 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1056 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Tyrosine phosphorylated by SRC. Phosphorylation plays a regulatory role in the protein localization. The intramolecular interaction of the PX domain with the third SH3 domain maintains the protein in the cytoplasm and phosphorylation disrupts this interaction, resulting in the redistribution of the protein from cytoplasm to the perimembrane region. Phosphorylated on serine upon DNA damage, probably by ATM or ATR.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Found in several cancer cell lines, particularly invasive breast carcinomas and melanomas.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts (via N-terminus) with CYBA (By similarity).
Interacts with ADAM12, ADAM15 and ADAM19. Interacts with NOXO1. Interacts (via SH3 domains) with NOXA1. Interacts with FASLG
Interacts with ADAM12, ADAM15 and ADAM19. Interacts with NOXO1. Interacts (via SH3 domains) with NOXA1. Interacts with FASLG
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q5TCZ1 | ADAM15 Q13444 | 4 | EBI-2483234, EBI-77818 | |
BINARY | Q5TCZ1 | ADAM19 Q9H013 | 2 | EBI-2483234, EBI-8567699 | |
XENO | Q5TCZ1-2 | Dnm1 P21575 | 2 | EBI-7014859, EBI-80070 | |
BINARY | Q5TCZ1-2 | SOS1 Q07889 | 5 | EBI-7014859, EBI-297487 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-128 | PX | ||||
Sequence: YCVQDATVVDVEKRRNPSKHYVYIINVTWSDSTSQTIYRRYSKFFDLQMQLLDKFPIEGGQKDPKQRIIPFLPGKILFRRSHIRDVAVKRLKPIDEYCRALVRLPPHISQCDEVFRFFEARPEDV | ||||||
Domain | 166-225 | SH3 1 | ||||
Sequence: MILEQYVVVSNYKKQENSELSLQAGEVVDVIEKNESGWWFVSTSEEQGWVPATYLEAQNG | ||||||
Domain | 266-325 | SH3 2 | ||||
Sequence: SREEKYVTVQPYTSQSKDEIGFEKGVTVEVIRKNLEGWWYIRYLGKEGWAPASYLKKAKD | ||||||
Region | 415-446 | Disordered | ||||
Sequence: QRAQISSPNLRTRPPPRRESSLGFQLPKPPEP | ||||||
Domain | 448-507 | SH3 3 | ||||
Sequence: SVEVEYYTIAEFQSCISDGISFRGGQKAEVIDKNSGGWWYVQIGEKEGWAPASYIDKRKK | ||||||
Region | 505-840 | Disordered | ||||
Sequence: RKKPNLSRRTSTLTRPKVPPPAPPSKPKEAEEGPTGASESQDSPRKLKYEEPEYDIPAFGFDSEPELSEEPVEDRASGERRPAQPHRPSPASSLQRARFKVGESSEDVALEEETIYENEGFRPYAEDTLSARGSSGDSDSPGSSSLSLTRKNSPKSGSPKSSSLLKLKAEKNAQAEMGKNHSSASFSSSITINTTCCSSSSSSSSSLSKTSGDLKPRSASDAGIRGTPKVRAKKDADANAGLTSCPRAKPSVRPKPFLNRAESQSQEKMDISTLRRQLRPTGQLRGGLKGSKSEDSELPPQTASEAPSEGSRRSSSDLITLPATTPPCPTKKEWEG | ||||||
Compositional bias | 635-672 | Polar residues | ||||
Sequence: ARGSSGDSDSPGSSSLSLTRKNSPKSGSPKSSSLLKLK | ||||||
Compositional bias | 680-719 | Polar residues | ||||
Sequence: EMGKNHSSASFSSSITINTTCCSSSSSSSSSLSKTSGDLK | ||||||
Compositional bias | 762-783 | Polar residues | ||||
Sequence: LNRAESQSQEKMDISTLRRQLR | ||||||
Compositional bias | 799-827 | Polar residues | ||||
Sequence: DSELPPQTASEAPSEGSRRSSSDLITLPA | ||||||
Domain | 840-899 | SH3 4 | ||||
Sequence: GPATSYMTCSAYQKVQDSEISFPAGVEVQVLEKQESGWWYVRFGELEGWAPSHYLVLDEN | ||||||
Region | 899-924 | Disordered | ||||
Sequence: NEQPDPSGKELDTVPAKGRQNEGKSD | ||||||
Coiled coil | 917-946 | |||||
Sequence: RQNEGKSDSLEKIERRVQALNTVNQSKKAT | ||||||
Region | 941-964 | Disordered | ||||
Sequence: QSKKATPPIPSKPPGGFGKTSGTP | ||||||
Region | 1029-1059 | Disordered | ||||
Sequence: KGRLAERAASQGSDSPLLPAQRNSIPVSPVR | ||||||
Domain | 1072-1133 | SH3 5 | ||||
Sequence: NLKDVYVSIADYEGDEETAGFQEGVSMEVLERNPNGWWYCQILDGVKPFKGWVPSNYLEKKN |
Domain
The PX domain is required for podosome localization because of its ability to bind phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) and, to a lesser extent, phosphatidylinositol 4-phosphate (PtdIns4P), phosphatidylinositol 5-phosphate (PtdIns5P), and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Binds to the third intramolecular SH3 domain (By similarity).
The fifth SH3 domain mediates binding with ADAM12, ADAM15 and ADAM19.
Sequence similarities
Belongs to the SH3PXD2 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q5TCZ1-1
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
- Length1,133
- Mass (Da)125,289
- Last updated2004-12-21 v1
- ChecksumD485F49E9192359C
Q5TCZ1-2
- Name2
Q5TCZ1-3
- Name3
- NoteGene prediction based on similarity to mouse ortholog and partial transcript data.
- Differences from canonical
- 240-267: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I5KQW5 | A0A8I5KQW5_HUMAN | SH3PXD2A | 185 |
Sequence caution
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_023312 | 1-165 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_023313 | 240-267 | in isoform 2 and isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 635-672 | Polar residues | ||||
Sequence: ARGSSGDSDSPGSSSLSLTRKNSPKSGSPKSSSLLKLK | ||||||
Compositional bias | 680-719 | Polar residues | ||||
Sequence: EMGKNHSSASFSSSITINTTCCSSSSSSSSSLSKTSGDLK | ||||||
Compositional bias | 762-783 | Polar residues | ||||
Sequence: LNRAESQSQEKMDISTLRRQLR | ||||||
Compositional bias | 799-827 | Polar residues | ||||
Sequence: DSELPPQTASEAPSEGSRRSSSDLITLPA |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB007878 EMBL· GenBank· DDBJ | BAA24848.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AL121929 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL133355 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471066 EMBL· GenBank· DDBJ | EAW49623.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471066 EMBL· GenBank· DDBJ | EAW49624.1 EMBL· GenBank· DDBJ | Genomic DNA |