Q15233 · NONO_HUMAN
- ProteinNon-POU domain-containing octamer-binding protein
- GeneNONO
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids471 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
DNA- and RNA binding protein, involved in several nuclear processes (PubMed:11525732, PubMed:12403470, PubMed:26571461).
Binds the conventional octamer sequence in double-stranded DNA (PubMed:11525732, PubMed:12403470, PubMed:26571461).
Also binds single-stranded DNA and RNA at a site independent of the duplex site (PubMed:11525732, PubMed:12403470, PubMed:26571461).
Involved in pre-mRNA splicing, probably as a heterodimer with SFPQ (PubMed:11525732, PubMed:12403470, PubMed:26571461).
Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b (PubMed:12403470).
Together with PSPC1, required for the formation of nuclear paraspeckles (PubMed:22416126).
The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs (PubMed:11525732).
The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1 (PubMed:10858305).
The SFPQ-NONO heteromer may be involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends (PubMed:15590677).
In vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex (PubMed:15590677).
NONO is involved in transcriptional regulation. The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional activity (PubMed:11897684).
NONO binds to an enhancer element in long terminal repeats of endogenous intracisternal A particles (IAPs) and activates transcription (By similarity).
Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer (By similarity).
Important for the functional organization of GABAergic synapses (By similarity).
Plays a specific and important role in the regulation of synaptic RNAs and GPHN/gephyrin scaffold structure, through the regulation of GABRA2 transcript (By similarity).
Plays a key role during neuronal differentiation by recruiting TET1 to genomic loci and thereby regulating 5-hydroxymethylcytosine levels (By similarity).
Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed:28712728, PubMed:30270045).
Promotes activation of the cGAS-STING pathway in response to HIV-2 infection: acts by interacting with HIV-2 Capsid protein p24, thereby promoting detection of viral DNA by CGAS, leading to CGAS-mediated inmmune activation (PubMed:30270045).
In contrast, the weak interaction with HIV-1 Capsid protein p24 does not allow activation of the cGAS-STING pathway (PubMed:30270045).
Binds the conventional octamer sequence in double-stranded DNA (PubMed:11525732, PubMed:12403470, PubMed:26571461).
Also binds single-stranded DNA and RNA at a site independent of the duplex site (PubMed:11525732, PubMed:12403470, PubMed:26571461).
Involved in pre-mRNA splicing, probably as a heterodimer with SFPQ (PubMed:11525732, PubMed:12403470, PubMed:26571461).
Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b (PubMed:12403470).
Together with PSPC1, required for the formation of nuclear paraspeckles (PubMed:22416126).
The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs (PubMed:11525732).
The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1 (PubMed:10858305).
The SFPQ-NONO heteromer may be involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends (PubMed:15590677).
In vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex (PubMed:15590677).
NONO is involved in transcriptional regulation. The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional activity (PubMed:11897684).
NONO binds to an enhancer element in long terminal repeats of endogenous intracisternal A particles (IAPs) and activates transcription (By similarity).
Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer (By similarity).
Important for the functional organization of GABAergic synapses (By similarity).
Plays a specific and important role in the regulation of synaptic RNAs and GPHN/gephyrin scaffold structure, through the regulation of GABRA2 transcript (By similarity).
Plays a key role during neuronal differentiation by recruiting TET1 to genomic loci and thereby regulating 5-hydroxymethylcytosine levels (By similarity).
Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed:28712728, PubMed:30270045).
Promotes activation of the cGAS-STING pathway in response to HIV-2 infection: acts by interacting with HIV-2 Capsid protein p24, thereby promoting detection of viral DNA by CGAS, leading to CGAS-mediated inmmune activation (PubMed:30270045).
In contrast, the weak interaction with HIV-1 Capsid protein p24 does not allow activation of the cGAS-STING pathway (PubMed:30270045).
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 377-378 | Breakpoint for translocation to form NONO-TFE3 | ||||
Sequence: AR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chromosome | |
Cellular Component | fibrillar center | |
Cellular Component | membrane | |
Cellular Component | nuclear matrix | |
Cellular Component | nuclear speck | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | paraspeckles | |
Cellular Component | RNA polymerase II transcription regulator complex | |
Molecular Function | chromatin binding | |
Molecular Function | DNA binding | |
Molecular Function | identical protein binding | |
Molecular Function | RNA binding | |
Biological Process | activation of innate immune response | |
Biological Process | circadian rhythm | |
Biological Process | DNA recombination | |
Biological Process | DNA repair | |
Biological Process | innate immune response | |
Biological Process | mRNA processing | |
Biological Process | negative regulation of DNA-templated transcription | |
Biological Process | negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway | |
Biological Process | regulation of circadian rhythm | |
Biological Process | regulation of DNA-templated transcription | |
Biological Process | RNA splicing |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNon-POU domain-containing octamer-binding protein
- Short namesNonO 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 accessionQ15233
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Detected in punctate subnuclear structures often located adjacent to splicing speckles, called paraspeckles.
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Intellectual developmental disorder, X-linked, syndromic 34 (MRXS34)
- Note
- DescriptionA syndrome characterized by intellectual deficit, delayed psychomotor development, poor speech, and dysmorphic features.
- See alsoMIM:300967
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 267 | Abolishes interaction with PSPC1 and localization in nuclear paraspeckles; when associated with A-271. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 271 | Abolishes interaction with PSPC1 and localization in nuclear paraspeckles; when associated with A-267. | ||||
Sequence: W → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 388 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 modified residue, chain, cross-link, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue | 1 | UniProt | N-acetylmethionine | ||||
Sequence: M | |||||||
Chain | PRO_0000081683 | 1-471 | UniProt | Non-POU domain-containing octamer-binding protein | |||
Sequence: MQSNKTFNLEKQNHTPRKHHQHHHQQQHHQQQQQQPPPPPIPANGQQASSQNEGLTIDLKNFRKPGEKTFTQRSRLFVGNLPPDITEEEMRKLFEKYGKAGEVFIHKDKGFGFIRLETRTLAEIAKVELDNMPLRGKQLRVRFACHSASLTVRNLPQYVSNELLEEAFSVFGQVERAVVIVDDRGRPSGKGIVEFSGKPAARKALDRCSEGSFLLTTFPRPVTVEPMDQLDDEEGLPEKLVIKNQQFHKEREQPPRFAQPGSFEYEYAMRWKALIEMEKQQQDQVDRNIKEAREKLEMEMEAARHEHQVMLMRQDLMRRQEELRRMEELHNQEVQKRKQLELRQEEERRRREEEMRRQQEEMMRRQQEGFKGTFPDAREQEIRMGQMAMGGAMGINNRGAMPPAPVPAGTPAPPGPATMMPDGTLGLTPPTTERFGQAATMEGIGAIGGTPPAFNRAAPGAEFAPNKRRRY | |||||||
Modified residue | 5 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 5 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue | 6 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 11 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 15 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 60 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 96 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 99 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 126 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 147 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 147 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 149 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 151 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 190 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 198 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 198 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 209 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 212 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 243 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 249 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 262 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 262 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 295 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 371 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 371 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 410 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 418 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 424 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 428 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 428 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 440 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 440 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 450 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 450 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 456 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Cross-link | 467 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K |
Post-translational modification
The N-terminus is blocked.
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Tissue specificity
Heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Also found in a number of breast tumor cell lines.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Monomer and component of the SFPQ-NONO complex, which is probably a heterotetramer of two 52 kDa (NONO) and two 100 kDa (SFPQ) subunits (PubMed:15590677, PubMed:8439294).
NONO is a component of spliceosome and U5.4/6 snRNP complexes (PubMed:12403470).
Interacts with CPNE4 (via VWFA domain) (By similarity).
Forms heterodimers with PSPC1; this involves formation of a coiled coil domain by helices from both proteins (PubMed:16148043, PubMed:22416126).
Part of complex consisting of SFPQ, NONO and MATR3 (PubMed:11525732).
Part of a complex consisting of SFPQ, NONO and NR5A1 (PubMed:11897684).
Part of a complex consisting of SFPQ, NONO and TOP1 (PubMed:9756848).
Interacts with SPI1 and SPIB (By similarity).
Interacts with RNF43 (PubMed:18655028).
Interacts with PER1 and PER2 (By similarity).
Part of the HDP-RNP complex composed of at least HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3) and NEAT1 RNA (PubMed:28712728).
Interacts (via second RRM domain) with WASL; the interaction is direct (PubMed:16767080).
Component of a multiprotein complex with WASL and SFPQ (PubMed:16767080).
Interacts with ERCC6 (PubMed:26030138).
Interacts (via DNA-binding domain) with TET1 (By similarity).
NONO is a component of spliceosome and U5.4/6 snRNP complexes (PubMed:12403470).
Interacts with CPNE4 (via VWFA domain) (By similarity).
Forms heterodimers with PSPC1; this involves formation of a coiled coil domain by helices from both proteins (PubMed:16148043, PubMed:22416126).
Part of complex consisting of SFPQ, NONO and MATR3 (PubMed:11525732).
Part of a complex consisting of SFPQ, NONO and NR5A1 (PubMed:11897684).
Part of a complex consisting of SFPQ, NONO and TOP1 (PubMed:9756848).
Interacts with SPI1 and SPIB (By similarity).
Interacts with RNF43 (PubMed:18655028).
Interacts with PER1 and PER2 (By similarity).
Part of the HDP-RNP complex composed of at least HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3) and NEAT1 RNA (PubMed:28712728).
Interacts (via second RRM domain) with WASL; the interaction is direct (PubMed:16767080).
Component of a multiprotein complex with WASL and SFPQ (PubMed:16767080).
Interacts with ERCC6 (PubMed:26030138).
Interacts (via DNA-binding domain) with TET1 (By similarity).
(Microbial infection) Interacts with HIV-2 Capsid protein p24; interacts with high affinity (PubMed:30270045).
Interacts with HIV-1 Capsid protein p24; interacts with low affinity (PubMed:30270045).
Interacts with HIV-1 Capsid protein p24; interacts with low affinity (PubMed:30270045).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q15233 | C11orf68 Q9H3H3 | 3 | EBI-350527, EBI-721765 | |
BINARY | Q15233 | C11orf68 Q9H3H3-3 | 3 | EBI-350527, EBI-12002214 | |
BINARY | Q15233 | CRTC2 Q53ET0 | 2 | EBI-350527, EBI-1181987 | |
XENO | Q15233 | EBNA-LP Q8AZK7 | 2 | EBI-350527, EBI-1185167 | |
BINARY | Q15233 | FXR1 P51114 | 2 | EBI-350527, EBI-713291 | |
BINARY | Q15233 | NONO Q15233 | 5 | EBI-350527, EBI-350527 | |
BINARY | Q15233 | PIN1 Q13526 | 4 | EBI-350527, EBI-714158 | |
BINARY | Q15233 | PSPC1 Q8WXF1 | 15 | EBI-350527, EBI-1392258 | |
BINARY | Q15233 | PSPC1 Q8WXF1-1 | 7 | EBI-350527, EBI-15974663 | |
BINARY | Q15233 | PSPC1 Q8WXF1-2 | 4 | EBI-350527, EBI-12135327 | |
BINARY | Q15233 | SFPQ P23246 | 9 | EBI-350527, EBI-355453 | |
BINARY | Q15233-2 | DDX6 P26196 | 3 | EBI-10203843, EBI-351257 | |
BINARY | Q15233-2 | LMO4 P61968 | 3 | EBI-10203843, EBI-2798728 | |
BINARY | Q15233-2 | PIN1 Q13526 | 3 | EBI-10203843, EBI-714158 | |
BINARY | Q15233-2 | PRKAA2 P54646 | 3 | EBI-10203843, EBI-1383852 | |
BINARY | Q15233-2 | PSPC1 Q8WXF1 | 3 | EBI-10203843, EBI-1392258 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-51 | Disordered | ||||
Sequence: MQSNKTFNLEKQNHTPRKHHQHHHQQQHHQQQQQQPPPPPIPANGQQASSQ | ||||||
Region | 54-373 | DBHS | ||||
Sequence: GLTIDLKNFRKPGEKTFTQRSRLFVGNLPPDITEEEMRKLFEKYGKAGEVFIHKDKGFGFIRLETRTLAEIAKVELDNMPLRGKQLRVRFACHSASLTVRNLPQYVSNELLEEAFSVFGQVERAVVIVDDRGRPSGKGIVEFSGKPAARKALDRCSEGSFLLTTFPRPVTVEPMDQLDDEEGLPEKLVIKNQQFHKEREQPPRFAQPGSFEYEYAMRWKALIEMEKQQQDQVDRNIKEAREKLEMEMEAARHEHQVMLMRQDLMRRQEELRRMEELHNQEVQKRKQLELRQEEERRRREEEMRRQQEEMMRRQQEGFKGT | ||||||
Domain | 74-141 | RRM 1 | ||||
Sequence: SRLFVGNLPPDITEEEMRKLFEKYGKAGEVFIHKDKGFGFIRLETRTLAEIAKVELDNMPLRGKQLRV | ||||||
Domain | 148-229 | RRM 2 | ||||
Sequence: ASLTVRNLPQYVSNELLEEAFSVFGQVERAVVIVDDRGRPSGKGIVEFSGKPAARKALDRCSEGSFLLTTFPRPVTVEPMDQ | ||||||
Coiled coil | 268-372 | |||||
Sequence: AMRWKALIEMEKQQQDQVDRNIKEAREKLEMEMEAARHEHQVMLMRQDLMRRQEELRRMEELHNQEVQKRKQLELRQEEERRRREEEMRRQQEEMMRRQQEGFKG | ||||||
Region | 443-471 | Disordered | ||||
Sequence: GIGAIGGTPPAFNRAAPGAEFAPNKRRRY |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q15233-1
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
- Length471
- Mass (Da)54,232
- Last updated2005-07-05 v4
- Checksum26BBD3828F5B9E49
Q15233-2
- Name2
- Differences from canonical
- 1-89: Missing
Computationally mapped potential isoform sequences
There are 14 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
C9IZL7 | C9IZL7_HUMAN | NONO | 207 | ||
A0A7P0MRW0 | A0A7P0MRW0_HUMAN | NONO | 515 | ||
C9J4X2 | C9J4X2_HUMAN | NONO | 124 | ||
C9JYS8 | C9JYS8_HUMAN | NONO | 247 | ||
C9JJ13 | C9JJ13_HUMAN | NONO | 65 | ||
H7C367 | H7C367_HUMAN | NONO | 234 | ||
A0A7I2YQK8 | A0A7I2YQK8_HUMAN | NONO | 130 | ||
A0A7I2V447 | A0A7I2V447_HUMAN | NONO | 56 | ||
A0A7I2V464 | A0A7I2V464_HUMAN | NONO | 360 | ||
A0A7I2V4K9 | A0A7I2V4K9_HUMAN | NONO | 411 | ||
A0A7I2V4J2 | A0A7I2V4J2_HUMAN | NONO | 468 | ||
A0A7I2V4N2 | A0A7I2V4N2_HUMAN | NONO | 360 | ||
A0A7I2V535 | A0A7I2V535_HUMAN | NONO | 501 | ||
A0A7I2V5Y7 | A0A7I2V5Y7_HUMAN | NONO | 476 |
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_045470 | 1-89 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 151 | in Ref. 1; AAC37578 | ||||
Sequence: T → H | ||||||
Sequence conflict | 358-359 | in Ref. 3; CAA72157 and 4; AAA03427 | ||||
Sequence: QQ → HE | ||||||
Sequence conflict | 366-367 | in Ref. 3; CAA72157 and 4; AAA03427 | ||||
Sequence: QQ → HE | ||||||
Sequence conflict | 387 | in Ref. 5; BAH12508 | ||||
Sequence: M → I |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L14599 EMBL· GenBank· DDBJ | AAC37578.1 EMBL· GenBank· DDBJ | mRNA | ||
U89867 EMBL· GenBank· DDBJ | AAC51852.1 EMBL· GenBank· DDBJ | mRNA | ||
Y11289 EMBL· GenBank· DDBJ | CAA72157.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y11290 EMBL· GenBank· DDBJ | CAA72157.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y11291 EMBL· GenBank· DDBJ | CAA72157.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y11292 EMBL· GenBank· DDBJ | CAA72157.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y11293 EMBL· GenBank· DDBJ | CAA72157.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y11294 EMBL· GenBank· DDBJ | CAA72157.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y11295 EMBL· GenBank· DDBJ | CAA72157.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y11296 EMBL· GenBank· DDBJ | CAA72157.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y11297 EMBL· GenBank· DDBJ | CAA72157.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y11298 EMBL· GenBank· DDBJ | CAA72157.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U02493 EMBL· GenBank· DDBJ | AAA03427.1 EMBL· GenBank· DDBJ | mRNA | ||
AK297144 EMBL· GenBank· DDBJ | BAH12508.1 EMBL· GenBank· DDBJ | mRNA | ||
CR456761 EMBL· GenBank· DDBJ | CAG33042.1 EMBL· GenBank· DDBJ | mRNA | ||
AL590762 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471132 EMBL· GenBank· DDBJ | EAX05298.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471132 EMBL· GenBank· DDBJ | EAX05299.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471132 EMBL· GenBank· DDBJ | EAX05300.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC002364 EMBL· GenBank· DDBJ | AAH02364.1 EMBL· GenBank· DDBJ | mRNA | ||
BC003129 EMBL· GenBank· DDBJ | AAH03129.1 EMBL· GenBank· DDBJ | mRNA | ||
BC012141 EMBL· GenBank· DDBJ | AAH12141.1 EMBL· GenBank· DDBJ | mRNA | ||
BC028299 EMBL· GenBank· DDBJ | AAH28299.1 EMBL· GenBank· DDBJ | mRNA | ||
BC069616 EMBL· GenBank· DDBJ | AAH69616.1 EMBL· GenBank· DDBJ | mRNA | ||
BC069639 EMBL· GenBank· DDBJ | AAH69639.1 EMBL· GenBank· DDBJ | mRNA |