O75475 · PSIP1_HUMAN
- ProteinPC4 and SFRS1-interacting protein
- GenePSIP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids530 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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 | euchromatin | |
Cellular Component | heterochromatin | |
Cellular Component | nuclear periphery | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | chromatin binding | |
Molecular Function | DNA-binding transcription factor binding | |
Molecular Function | RNA binding | |
Molecular Function | supercoiled DNA binding | |
Molecular Function | transcription coactivator activity | |
Biological Process | chromatin remodeling | |
Biological Process | mRNA 5'-splice site recognition | |
Biological Process | positive regulation of transcription by RNA polymerase II | |
Biological Process | response to heat | |
Biological Process | response to oxidative stress |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePC4 and SFRS1-interacting protein
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO75475
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 360 | Reduced interaction with POGZ, CDCA7L and human HIV-1 integrase. | ||||
Sequence: K → A | ||||||
Mutagenesis | 365 | Loss of interaction with human HIV-1 integrase; reduced interaction with POGZ and CDCA7L. | ||||
Sequence: I → A | ||||||
Mutagenesis | 366 | Loss of interaction with human HIV-1 integrase; no effect on interaction with CDCA7L and POGZ. | ||||
Sequence: D → A | ||||||
Mutagenesis | 366 | Loss of interaction with human HIV-1 integrase; no effect on interaction with KMT2A. | ||||
Sequence: D → N | ||||||
Mutagenesis | 368 | Reduced interaction with KMT2A. Significant loss of interaction with KMT2A; when associated with D-407. | ||||
Sequence: L → A | ||||||
Mutagenesis | 370 | Reduced interaction with POGZ, CDCA7L and human HIV-1 integrase. | ||||
Sequence: V → A | ||||||
Mutagenesis | 404 | Significant loss of interaction with KMT2A; when associated with D-405. | ||||
Sequence: R → D | ||||||
Mutagenesis | 405 | Significant loss of interaction with KMT2A; when associated with D-404. | ||||
Sequence: R → D | ||||||
Mutagenesis | 406 | Loss of interaction with human HIV-1 integrase and POGZ; reduced interaction with CDCA7L. | ||||
Sequence: F → A | ||||||
Mutagenesis | 407 | Reduced interaction with KMT2A. Significant loss of interaction with KMT2A; when associated with A-368. | ||||
Sequence: K → D | ||||||
Mutagenesis | 408 | Reduced interaction with human HIV-1 integrase; no effect on interaction with POGZ and CDCA7L. | ||||
Sequence: V → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 672 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
Protein family/group databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), cross-link, modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000191708 | 1-530 | UniProt | PC4 and SFRS1-interacting protein | |||
Sequence: MTRDFKPGDLIFAKMKGYPHWPARVDEVPDGAVKPPTNKLPIFFFGTHETAFLGPKDIFPYSENKEKYGKPNKRKGFNEGLWEIDNNPKVKFSSQQAATKQSNASSDVEVEEKETSVSKEDTDHEEKASNEDVTKAVDITTPKAARRGRKRKAEKQVETEEAGVVTTATASVNLKVSPKRGRPAATEVKIPKPRGRPKMVKQPCPSESDIITEEDKSKKKGQEEKQPKKQPKKDEEGQKEEDKPRKEPDKKEGKKEVESKRKNLAKTGVTSTSDSEEEGDDQEGEKKRKGGRNFQTAHRRNMLKGQHEKEAADRKRKQEEQMETEQQNKDEGKKPEVKKVEKKRETSMDSRLQRIHAEIKNSLKIDNLDVNRCIEALDELASLQVTMQQAQKHTEMITTLKKIRRFKVSQVIMEKSTMLYNKFKNMFLVGEGDSVITQVLNKSLAEQRQHEEANKTKDQGKKGPNKKLEKEQTGSKTLNGGSDAQDGNQPQHNGESNEDSKDNHEASTKKKPSSEERETEISLKDSTLDN | |||||||
Modified residue (large scale data) | 62 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 75 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 99 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 102 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 102 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 105 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 105 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 106 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 106 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 115 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 115 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 116 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 118 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 122 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 122 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 129 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 129 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 141 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 141 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 167 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 171 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 177 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 177 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 206 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 206 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 208 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 212 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 270 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 271 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 271 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 272 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 272 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 273 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 273 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 275 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 275 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 347 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 434 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 434 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 437 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 437 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 443 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 443 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 482 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 496 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 500 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 513 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 514 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 514 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 517 | UniProt | Citrulline | ||||
Sequence: R | |||||||
Modified residue | 522 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 522 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 527 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 527 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with IFRD1/PC4 (PubMed:9822615).
Isoform 2 interacts with SFRS1 (PubMed:9885563).
Isoform 1 interacts (via IBD domain) with POGZ (via IBM motif) and CDCA7L (via IBM motifs) (PubMed:19244240, PubMed:25082813, PubMed:29997176).
Interacts (via IBD domain) with KMT2A (via IBM motifs) with a moderate affinity whereas interacts with the KMT2A-MEN1 complex with a greater affinity; MEN1 enhances interaction of KMT2A with PSIP1 (PubMed:22327296, PubMed:25082813, PubMed:25305204, PubMed:29997176).
Interacts with fusion protein KMT2A-MLLT3 (PubMed:25305204).
Interacts (via IBD domain) with IWS1 (via IBM motif), MED1 (via IBM motif) and DBF4 (via IBM motifs) (PubMed:29997176).
Isoform 1
Isoform 1
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | O75475 | gag-pol P04585 | 21 | EBI-1801773, EBI-3989067 | |
BINARY | O75475 | RBBP8 Q99708 | 4 | EBI-1801773, EBI-745715 | |
BINARY | O75475 | SUMO1 P63165 | 4 | EBI-1801773, EBI-80140 | |
XENO | O75475-1 | gag-pol PRO_0000042447 P04585 | 2 | EBI-5279836, EBI-9872653 | |
XENO | O75475-1 | gag-pol PRO_0000042402 P12497 | 3 | EBI-5279836, EBI-10131955 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region, motif, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-64 | PWWP | ||||
Sequence: MTRDFKPGDLIFAKMKGYPHWPARVDEVPDGAVKPPTNKLPIFFFGTHETAFLGPKDIFPYSEN | ||||||
Compositional bias | 88-105 | Polar residues | ||||
Sequence: PKVKFSSQQAATKQSNAS | ||||||
Region | 88-349 | Disordered | ||||
Sequence: PKVKFSSQQAATKQSNASSDVEVEEKETSVSKEDTDHEEKASNEDVTKAVDITTPKAARRGRKRKAEKQVETEEAGVVTTATASVNLKVSPKRGRPAATEVKIPKPRGRPKMVKQPCPSESDIITEEDKSKKKGQEEKQPKKQPKKDEEGQKEEDKPRKEPDKKEGKKEVESKRKNLAKTGVTSTSDSEEEGDDQEGEKKRKGGRNFQTAHRRNMLKGQHEKEAADRKRKQEEQMETEQQNKDEGKKPEVKKVEKKRETSMD | ||||||
Compositional bias | 106-133 | Basic and acidic residues | ||||
Sequence: SDVEVEEKETSVSKEDTDHEEKASNEDV | ||||||
Motif | 146-156 | Nuclear localization signal | ||||
Sequence: RRGRKRKAEKQ | ||||||
Compositional bias | 208-263 | Basic and acidic residues | ||||
Sequence: SDIITEEDKSKKKGQEEKQPKKQPKKDEEGQKEEDKPRKEPDKKEGKKEVESKRKN | ||||||
Compositional bias | 301-349 | Basic and acidic residues | ||||
Sequence: NMLKGQHEKEAADRKRKQEEQMETEQQNKDEGKKPEVKKVEKKRETSMD | ||||||
Coiled coil | 306-334 | |||||
Sequence: QHEKEAADRKRKQEEQMETEQQNKDEGKK | ||||||
Region | 340-417 | Integrase-binding domain (IBD) | ||||
Sequence: VEKKRETSMDSRLQRIHAEIKNSLKIDNLDVNRCIEALDELASLQVTMQQAQKHTEMITTLKKIRRFKVSQVIMEKST | ||||||
Coiled coil | 371-395 | |||||
Sequence: NRCIEALDELASLQVTMQQAQKHTE | ||||||
Compositional bias | 446-473 | Basic and acidic residues | ||||
Sequence: EQRQHEEANKTKDQGKKGPNKKLEKEQT | ||||||
Region | 446-530 | Disordered | ||||
Sequence: EQRQHEEANKTKDQGKKGPNKKLEKEQTGSKTLNGGSDAQDGNQPQHNGESNEDSKDNHEASTKKKPSSEERETEISLKDSTLDN | ||||||
Compositional bias | 474-494 | Polar residues | ||||
Sequence: GSKTLNGGSDAQDGNQPQHNG | ||||||
Compositional bias | 495-530 | Basic and acidic residues | ||||
Sequence: ESNEDSKDNHEASTKKKPSSEERETEISLKDSTLDN |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
O75475-1
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
- Synonymsp75, PSIP1
- NoteLess active than isoform 2 as transcriptional coactivator, but more abundant in cells.
- Length530
- Mass (Da)60,103
- Last updated1998-11-01 v1
- Checksum4B653D02B1D0E174
O75475-2
- Name2
- Synonymsp52, PSIP2
O75475-3
- Name3
- Differences from canonical
- 326-530: QQNKDEGKKPEVKKVEKKRETSMDSRLQRIHAEIKNSLKIDNLDVNRCIEALDELASLQVTMQQAQKHTEMITTLKKIRRFKVSQVIMEKSTMLYNKFKNMFLVGEGDSVITQVLNKSLAEQRQHEEANKTKDQGKKGPNKKLEKEQTGSKTLNGGSDAQDGNQPQHNGESNEDSKDNHEASTKKKPSSEERETEISLKDSTLDN → HFAL
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
V9GYT7 | V9GYT7_HUMAN | PSIP1 | 65 |
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 88-105 | Polar residues | ||||
Sequence: PKVKFSSQQAATKQSNAS | ||||||
Compositional bias | 106-133 | Basic and acidic residues | ||||
Sequence: SDVEVEEKETSVSKEDTDHEEKASNEDV | ||||||
Sequence conflict | 153-161 | in Ref. 7; AAH64135 | ||||
Sequence: Missing | ||||||
Compositional bias | 208-263 | Basic and acidic residues | ||||
Sequence: SDIITEEDKSKKKGQEEKQPKKQPKKDEEGQKEEDKPRKEPDKKEGKKEVESKRKN | ||||||
Sequence conflict | 224 | in Ref. 1; AAC97946/AAC97945 | ||||
Sequence: E → G | ||||||
Sequence conflict | 272 | in Ref. 8; AAB52589 | ||||
Sequence: T → P | ||||||
Compositional bias | 301-349 | Basic and acidic residues | ||||
Sequence: NMLKGQHEKEAADRKRKQEEQMETEQQNKDEGKKPEVKKVEKKRETSMD | ||||||
Alternative sequence | VSP_014297 | 326-333 | in isoform 2 | |||
Sequence: QQNKDEGK → HQTTCNLQ | ||||||
Alternative sequence | VSP_044435 | 326-530 | in isoform 3 | |||
Sequence: QQNKDEGKKPEVKKVEKKRETSMDSRLQRIHAEIKNSLKIDNLDVNRCIEALDELASLQVTMQQAQKHTEMITTLKKIRRFKVSQVIMEKSTMLYNKFKNMFLVGEGDSVITQVLNKSLAEQRQHEEANKTKDQGKKGPNKKLEKEQTGSKTLNGGSDAQDGNQPQHNGESNEDSKDNHEASTKKKPSSEERETEISLKDSTLDN → HFAL | ||||||
Alternative sequence | VSP_014298 | 334-530 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 420 | in Ref. 1; AAC97946 and 8; AAB52589 | ||||
Sequence: Y → F | ||||||
Compositional bias | 446-473 | Basic and acidic residues | ||||
Sequence: EQRQHEEANKTKDQGKKGPNKKLEKEQT | ||||||
Compositional bias | 474-494 | Polar residues | ||||
Sequence: GSKTLNGGSDAQDGNQPQHNG | ||||||
Compositional bias | 495-530 | Basic and acidic residues | ||||
Sequence: ESNEDSKDNHEASTKKKPSSEERETEISLKDSTLDN |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF098483 EMBL· GenBank· DDBJ | AAC97946.1 EMBL· GenBank· DDBJ | mRNA | ||
AF098482 EMBL· GenBank· DDBJ | AAC97945.1 EMBL· GenBank· DDBJ | mRNA | ||
AF063020 EMBL· GenBank· DDBJ | AAC25167.1 EMBL· GenBank· DDBJ | mRNA | ||
AF199339 EMBL· GenBank· DDBJ | AAF25870.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF199339 EMBL· GenBank· DDBJ | AAF25871.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF432220 EMBL· GenBank· DDBJ | AAL99926.1 EMBL· GenBank· DDBJ | mRNA | ||
AL359998 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL441925 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL513423 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471071 EMBL· GenBank· DDBJ | EAW58677.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471071 EMBL· GenBank· DDBJ | EAW58678.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471071 EMBL· GenBank· DDBJ | EAW58679.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC044568 EMBL· GenBank· DDBJ | AAH44568.2 EMBL· GenBank· DDBJ | mRNA | ||
BC064135 EMBL· GenBank· DDBJ | AAH64135.1 EMBL· GenBank· DDBJ | mRNA | ||
U94319 EMBL· GenBank· DDBJ | AAB52589.1 EMBL· GenBank· DDBJ | mRNA |