Q9NRA8 · 4ET_HUMAN
- ProteinEukaryotic translation initiation factor 4E transporter
- GeneEIF4ENIF1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids985 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
EIF4E-binding protein that regulates translation and stability of mRNAs in processing bodies (P-bodies) (PubMed:16157702, PubMed:24335285, PubMed:27342281, PubMed:32354837).
Plays a key role in P-bodies to coordinate the storage of translationally inactive mRNAs in the cytoplasm and prevent their degradation (PubMed:24335285, PubMed:32354837).
Acts as a binding platform for multiple RNA-binding proteins: promotes deadenylation of mRNAs via its interaction with the CCR4-NOT complex, and blocks decapping via interaction with eIF4E (EIF4E and EIF4E2), thereby protecting deadenylated and repressed mRNAs from degradation (PubMed:27342281, PubMed:32354837).
Component of a multiprotein complex that sequesters and represses translation of proneurogenic factors during neurogenesis (By similarity).
Promotes miRNA-mediated translational repression (PubMed:24335285, PubMed:27342281, PubMed:28487484).
Required for the formation of P-bodies (PubMed:16157702, PubMed:22966201, PubMed:27342281, PubMed:32354837).
Involved in mRNA translational repression mediated by the miRNA effector TNRC6B by protecting TNRC6B-targeted mRNAs from decapping and subsequent decay (PubMed:32354837).
Also acts as a nucleoplasmic shuttling protein, which mediates the nuclear import of EIF4E and DDX6 by a piggy-back mechanism (PubMed:10856257, PubMed:28216671).
Plays a key role in P-bodies to coordinate the storage of translationally inactive mRNAs in the cytoplasm and prevent their degradation (PubMed:24335285, PubMed:32354837).
Acts as a binding platform for multiple RNA-binding proteins: promotes deadenylation of mRNAs via its interaction with the CCR4-NOT complex, and blocks decapping via interaction with eIF4E (EIF4E and EIF4E2), thereby protecting deadenylated and repressed mRNAs from degradation (PubMed:27342281, PubMed:32354837).
Component of a multiprotein complex that sequesters and represses translation of proneurogenic factors during neurogenesis (By similarity).
Promotes miRNA-mediated translational repression (PubMed:24335285, PubMed:27342281, PubMed:28487484).
Required for the formation of P-bodies (PubMed:16157702, PubMed:22966201, PubMed:27342281, PubMed:32354837).
Involved in mRNA translational repression mediated by the miRNA effector TNRC6B by protecting TNRC6B-targeted mRNAs from decapping and subsequent decay (PubMed:32354837).
Also acts as a nucleoplasmic shuttling protein, which mediates the nuclear import of EIF4E and DDX6 by a piggy-back mechanism (PubMed:10856257, PubMed:28216671).
GO annotations
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEukaryotic translation initiation factor 4E transporter
- Short names4E-T ; eIF4E transporter
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9NRA8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 30 | Abolishes interaction with EIF4E and EIF4E2. Impaired ability to repress mRNA translation. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 30-36 | Abolished interaction with EIF4E2. | ||||
Sequence: YTKEELL → ATKEEAA | ||||||
Mutagenesis | 35-36 | Abolished interaction with EIF4E2. | ||||
Sequence: LL → AA | ||||||
Mutagenesis | 54-61 | Strongly reduced interaction with EIF4E and EIF4E2. | ||||
Sequence: KYDSDGVW → ADSDAA | ||||||
Mutagenesis | 195-196 | Abolishes the nuclear localization. | ||||
Sequence: RR → NS | ||||||
Mutagenesis | 301 | In S6A mutant; abolished phosphorylation by MAPK8/JNK1; impaired P-body assembly in response to oxidative stress when associated with A-374, A-513, A-587, A-693 and A-752. | ||||
Sequence: S → A | ||||||
Mutagenesis | 374 | In S6A mutant; abolished phosphorylation by MAPK8/JNK1; impaired P-body assembly in response to oxidative stress when associated with A-301, A-513, A-587, A-693 and A-752. | ||||
Sequence: S → A | ||||||
Mutagenesis | 513 | In S6A mutant; abolished phosphorylation by MAPK8/JNK1; impaired P-body assembly in response to oxidative stress when associated with A-301, A-374, A-587, A-693 and A-752. | ||||
Sequence: S → A | ||||||
Mutagenesis | 587 | In S6A mutant; abolished phosphorylation by MAPK8/JNK1; impaired P-body assembly in response to oxidative stress when associated with A-301, A-374, A-513, A-693 and A-752. | ||||
Sequence: S → A | ||||||
Mutagenesis | 693 | In S6A mutant; abolished phosphorylation by MAPK8/JNK1; impaired P-body assembly in response to oxidative stress when associated with A-301, A-374, A-513, A-587 and A-752. | ||||
Sequence: S → A | ||||||
Mutagenesis | 752 | In S6A mutant; abolished phosphorylation by MAPK8/JNK1; impaired P-body assembly in response to oxidative stress when associated with A-301, A-374, A-513, A-587 and A-693. | ||||
Sequence: S → A | ||||||
Mutagenesis | 955-958 | Abolished interaction with LSM14A. | ||||
Sequence: LAKW → AAKA | ||||||
Mutagenesis | 958 | Abolished interaction with LSM14A. | ||||
Sequence: W → A | ||||||
Mutagenesis | 959 | Abolished interaction with LSM14A. | ||||
Sequence: F → A | ||||||
Mutagenesis | 961 | Does not affect interaction with LSM14A. | ||||
Sequence: S → A | ||||||
Mutagenesis | 970 | Does not affect interaction with LSM14A. | ||||
Sequence: S → A | ||||||
Mutagenesis | 978 | Abolished interaction with LSM14A. | ||||
Sequence: V → A | ||||||
Mutagenesis | 978-981 | Abolished interaction with LSM14A. | ||||
Sequence: VDEL → ADEA | ||||||
Mutagenesis | 982 | Abolished interaction with LSM14A. | ||||
Sequence: E → K |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,043 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, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000064381 | 1-985 | UniProt | Eukaryotic translation initiation factor 4E transporter | |||
Sequence: MDRRSMGETESGDAFLDLKKPPASKCPHRYTKEELLDIKELPHSKQRPSCLSEKYDSDGVWDPEKWHASLYPASGRSSPVESLKKELDTDRPSLVRRIVDPRERVKEDDLDVVLSPQRRSFGGGCHVTAAVSSRRSGSPLEKDSDGLRLLGGRRIGSGRIISARTFEKDHRLSDKDLRDLRDRDRERDFKDKRFRREFGDSKRVFGERRRNDSYTEEEPEWFSAGPTSQSETIELTGFDDKILEEDHKGRKRTRRRTASVKEGIVECNGGVAEEDEVEVILAQEPAADQEVPRDAVLPEQSPGDFDFNEFFNLDKVPCLASMIEDVLGEGSVSASRFSRWFSNPSRSGSRSSSLGSTPHEELERLAGLEQAILSPGQNSGNYFAPIPLEDHAENKVDILEMLQKAKVDLKPLLSSLSANKEKLKESSHSGVVLSVEEVEAGLKGLKVDQQVKNSTPFMAEHLEETLSAVTNNRQLKKDGDMTAFNKLVSTMKASGTLPSQPKVSRNLESHLMSPAEIPGQPVPKNILQELLGQPVQRPASSNLLSGLMGSLEPTTSLLGQRAPSPPLSQVFQTRAASADYLRPRIPSPIGFTPGPQQLLGDPFQGMRKPMSPITAQMSQLELQQAALEGLALPHDLAVQAANFYQPGFGKPQVDRTRDGFRNRQQRVTKSPAPVHRGNSSSPAPAASITSMLSPSFTPTSVIRKMYESKEKSKEEPASGKAALGDSKEDTQKASEENLLSSSSVPSADRDSSPTTNSKLSALQRSSCSTPLSQANRYTKEQDYRPKATGRKTPTLASPVPTTPFLRPVHQVPLVPHVPMVRPAHQLHPGLVQRMLAQGVHPQHLPSLLQTGVLPPGMDLSHLQGISGPILGQPFYPLPAASHPLLNPRPGTPLHLAMVQQQLQRSVLHPPGSGSHAAAVSVQTTPQNVPSRSGLPHMHSQLEHRPSQRSSSPVGLAKWFGSDVLQQPLPSMPAKVISVDELEYRQ | |||||||
Modified residue | 5 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 5 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 9 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 11 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 71 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 74 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 74 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 77 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 78 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 78 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 115 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 115 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 120 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 120 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 136 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 136 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 138 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 138 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 213 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 301 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 301 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 345 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 345 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 351 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 352 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 353 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 353 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 356 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 357 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 374 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 374 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 379 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 410 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 414 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 417 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 417 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 455 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 486 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 499 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 513 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 513 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 541 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 564 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 564 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 568 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 577 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 587 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 587 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 592 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 611 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 668 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 670 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 681 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 687 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 689 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 693 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 693 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 697 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 746 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 751 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 752 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 752 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 757 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 768 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 769 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 792 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 891 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 920 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 950 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 951 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 951 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 977 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylation by MAPK8/JNK1 and or MAPK9/JNK2 in response to oxidative stress promotes P-body assembly (PubMed:22966201).
Phosphorylated during meiotic maturation (By similarity).
Phosphorylated during meiotic maturation (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts (via YXXXXLphi motif) with EIF4E (PubMed:10856257, PubMed:16157702, PubMed:23991149, PubMed:24335285, PubMed:25923732, PubMed:28487484).
Interacts (via YXXXXLphi motif) with EIF4E2 (PubMed:23991149, PubMed:28487484).
Interacts with DDX6 (PubMed:26027925, PubMed:26489469, PubMed:27342281, PubMed:28216671, PubMed:31422817, PubMed:31439631, PubMed:32354837).
Interacts with CSDE1/UNR (PubMed:27342281, PubMed:32354837).
Interacts with CNOT1; promoting association with the CCR4-NOT complex (PubMed:26027925, PubMed:26489469, PubMed:27342281, PubMed:32354837).
Interacts with LSM14A; promoting EIF4ENIF1 localization to P-bodies (PubMed:26027925, PubMed:29510985, PubMed:32354837).
Interacts with PATL1 (PubMed:26027925, PubMed:32354837).
Interacts with importin beta only in the presence of importin alpha, suggesting a direct interaction with importin alpha (PubMed:10856257).
Interacts with APOBEC3G in an RNA-dependent manner (PubMed:16699599).
Interacts (via YXXXXLphi motif) with EIF4E2 (PubMed:23991149, PubMed:28487484).
Interacts with DDX6 (PubMed:26027925, PubMed:26489469, PubMed:27342281, PubMed:28216671, PubMed:31422817, PubMed:31439631, PubMed:32354837).
Interacts with CSDE1/UNR (PubMed:27342281, PubMed:32354837).
Interacts with CNOT1; promoting association with the CCR4-NOT complex (PubMed:26027925, PubMed:26489469, PubMed:27342281, PubMed:32354837).
Interacts with LSM14A; promoting EIF4ENIF1 localization to P-bodies (PubMed:26027925, PubMed:29510985, PubMed:32354837).
Interacts with PATL1 (PubMed:26027925, PubMed:32354837).
Interacts with importin beta only in the presence of importin alpha, suggesting a direct interaction with importin alpha (PubMed:10856257).
Interacts with APOBEC3G in an RNA-dependent manner (PubMed:16699599).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-15 | Basic and acidic residues | ||||
Sequence: MDRRSMGETESGDAF | ||||||
Region | 1-24 | Disordered | ||||
Sequence: MDRRSMGETESGDAFLDLKKPPAS | ||||||
Motif | 30-36 | YXXXXLphi motif | ||||
Sequence: YTKEELL | ||||||
Region | 131-161 | Interaction with CSDE1 | ||||
Sequence: VSSRRSGSPLEKDSDGLRLLGGRRIGSGRII | ||||||
Motif | 195-211 | Nuclear localization signal | ||||
Sequence: RREFGDSKRVFGERRRN | ||||||
Region | 208-230 | Disordered | ||||
Sequence: RRRNDSYTEEEPEWFSAGPTSQS | ||||||
Region | 219-240 | Interaction with DDX6 | ||||
Sequence: PEWFSAGPTSQSETIELTGFDD | ||||||
Motif | 438-447 | Nuclear export signal | ||||
Sequence: VEAGLKGLKV | ||||||
Region | 448-490 | Interaction with LSM14A | ||||
Sequence: DQQVKNSTPFMAEHLEETLSAVTNNRQLKKDGDMTAFNKLVST | ||||||
Motif | 613-638 | Nuclear export signal | ||||
Sequence: ITAQMSQLELQQAALEGLALPHDLAV | ||||||
Region | 664-693 | Disordered | ||||
Sequence: QQRVTKSPAPVHRGNSSSPAPAASITSMLS | ||||||
Compositional bias | 665-693 | Polar residues | ||||
Sequence: QRVTKSPAPVHRGNSSSPAPAASITSMLS | ||||||
Region | 695-713 | Interaction with PATL1 | ||||
Sequence: SFTPTSVIRKMYESKEKSK | ||||||
Compositional bias | 707-734 | Basic and acidic residues | ||||
Sequence: ESKEKSKEEPASGKAALGDSKEDTQKAS | ||||||
Region | 707-803 | Disordered | ||||
Sequence: ESKEKSKEEPASGKAALGDSKEDTQKASEENLLSSSSVPSADRDSSPTTNSKLSALQRSSCSTPLSQANRYTKEQDYRPKATGRKTPTLASPVPTTP | ||||||
Compositional bias | 735-778 | Polar residues | ||||
Sequence: EENLLSSSSVPSADRDSSPTTNSKLSALQRSSCSTPLSQANRYT | ||||||
Region | 922-953 | Disordered | ||||
Sequence: QTTPQNVPSRSGLPHMHSQLEHRPSQRSSSPV | ||||||
Region | 940-985 | Interaction with LSM14A | ||||
Sequence: QLEHRPSQRSSSPVGLAKWFGSDVLQQPLPSMPAKVISVDELEYRQ |
Domain
Intrinsically disordered protein with multiple low-complexity regions that confer binding to multiple RNA translation, deadenylation and decapping factors.
The YXXXXLphi motif mediates interaction with eIF4E (EIF4E and EIF4E2).
Sequence similarities
Belongs to the 4E-T/EIF4E-T family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q9NRA8-1
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
- Length985
- Mass (Da)108,201
- Last updated2002-08-02 v2
- Checksum4C898E0488903C04
Q9NRA8-2
- Name2
Q9NRA8-3
- Name3
- Differences from canonical
- 616-616: Q → QQ
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-15 | Basic and acidic residues | ||||
Sequence: MDRRSMGETESGDAF | ||||||
Alternative sequence | VSP_003783 | 100-262 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 114 | in Ref. 1; AAF81693 | ||||
Sequence: L → F | ||||||
Alternative sequence | VSP_003784 | 493-504 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_047042 | 616 | in isoform 2 and isoform 3 | |||
Sequence: Q → QQ | ||||||
Compositional bias | 665-693 | Polar residues | ||||
Sequence: QRVTKSPAPVHRGNSSSPAPAASITSMLS | ||||||
Compositional bias | 707-734 | Basic and acidic residues | ||||
Sequence: ESKEKSKEEPASGKAALGDSKEDTQKAS | ||||||
Compositional bias | 735-778 | Polar residues | ||||
Sequence: EENLLSSSSVPSADRDSSPTTNSKLSALQRSSCSTPLSQANRYT | ||||||
Sequence conflict | 825 | in Ref. 6; AAH33028 | ||||
Sequence: Q → R |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF240775 EMBL· GenBank· DDBJ | AAF81693.1 EMBL· GenBank· DDBJ | mRNA | ||
CR456386 EMBL· GenBank· DDBJ | CAG30272.1 EMBL· GenBank· DDBJ | mRNA | ||
AK025254 EMBL· GenBank· DDBJ | BAB15092.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK074768 EMBL· GenBank· DDBJ | BAC11194.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK314636 EMBL· GenBank· DDBJ | BAG37198.1 EMBL· GenBank· DDBJ | mRNA | ||
AL096701 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471095 EMBL· GenBank· DDBJ | EAW59977.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC032941 EMBL· GenBank· DDBJ | AAH32941.1 EMBL· GenBank· DDBJ | mRNA | ||
BC033028 EMBL· GenBank· DDBJ | AAH33028.1 EMBL· GenBank· DDBJ | mRNA |