Q96EP0 · RNF31_HUMAN
- ProteinE3 ubiquitin-protein ligase RNF31
- GeneRNF31
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1072 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways (PubMed:17006537, PubMed:19136968, PubMed:20005846, PubMed:21455173, PubMed:21455180, PubMed:21455181, PubMed:22863777, PubMed:28189684).
Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation (PubMed:21455173, PubMed:28189684).
LUBAC is recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex (PubMed:20005846, PubMed:27458237).
The LUBAC complex is also involved in innate immunity by conjugating linear polyubiquitin chains at the surface of bacteria invading the cytosol to form the ubiquitin coat surrounding bacteria (PubMed:28481331, PubMed:34012115).
LUBAC is not able to initiate formation of the bacterial ubiquitin coat, and can only promote formation of linear polyubiquitins on pre-existing ubiquitin (PubMed:28481331).
Recruited to the surface of bacteria by RNF213, which initiates the bacterial ubiquitin coat (PubMed:34012115).
The bacterial ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B activation (PubMed:28481331, PubMed:34012115).
Together with OTULIN, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis (PubMed:23708998).
RNF31 is required for linear ubiquitination of BCL10, thereby promoting TCR-induced NF-kappa-B activation (PubMed:27777308).
Binds polyubiquitin of different linkage types (PubMed:23708998).
Catalytic activity
Pathway
Features
Showing features for site, binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 390-391 | Cleavage; by caspase | ||||
Sequence: DA | ||||||
Binding site | 699 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 702 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 717 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 719 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 722 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 725 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 744 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 747 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 799 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 802 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 817 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 820 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 825 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 828 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 836 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 841 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 871 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 874 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Active site | 885 | |||||
Sequence: C | ||||||
Binding site | 890 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 893 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 898 | Zn2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 901 | Zn2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 916 | Zn2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 925 | Zn2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
RNF31 (LUBAC) mediates NOD2 signaling and is recruited to the signaling complex by XIAP (BIRC4).
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin-protein ligase RNF31
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ96EP0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Immunodeficiency 115 with autoinflammation (IMD115)
- Note
- DescriptionAn autosomal recessive immunologic disorder manifesting in early infancy and characterized by combined immunodeficiency, recurrent bacterial, viral, and fungal infections, as well as autoinflammatory features, including arthritis and dermatitis.
- See alsoMIM:620632
Natural variants in IMD115
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_089148 | 72 | L>P | in IMD115; likely pathogenic; may affect protein expression level; linear ubiquitination and NF-kappa-B activation are impaired in the patient's fibroblasts stimulated by IL1B or TNF, a phenotype that can be restored by the reintroduction of the wild-type protein; the genetic variation producing this missense variant does not affect splicing; dbSNP:rs794729666 | |
VAR_089149 | 399 | Q>H | in IMD115; uncertain significance; decreased interaction with SHARPIN; does not affect interaction with RBCK1; the genetic variation producing this missense variant predominantly affects splicing, leading to in-frame skipping of exon 9 and lack of 84 amino acids from residue 496 to 579 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_089148 | 72 | in IMD115; likely pathogenic; may affect protein expression level; linear ubiquitination and NF-kappa-B activation are impaired in the patient's fibroblasts stimulated by IL1B or TNF, a phenotype that can be restored by the reintroduction of the wild-type protein; the genetic variation producing this missense variant does not affect splicing; dbSNP:rs794729666 | |||
Sequence: L → P | ||||||
Mutagenesis | 82 | Abolished interaction with OTULIN. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 82 | Reduced interaction with OTULIN. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 85 | Reduced interaction with OTULIN. | ||||
Sequence: N → A | ||||||
Mutagenesis | 99 | Reduced interaction with OTULIN. | ||||
Sequence: K → E | ||||||
Mutagenesis | 101 | Does not affect interaction with OTULIN. | ||||
Sequence: N → R | ||||||
Mutagenesis | 102 | Abolished interaction with SPATA2. | ||||
Sequence: N → A | ||||||
Mutagenesis | 102 | Abolished interaction with OTULIN. | ||||
Sequence: N → D | ||||||
Mutagenesis | 104 | Reduced interaction with OTULIN. | ||||
Sequence: V → A | ||||||
Mutagenesis | 360 | Decreased ubiquitin-binding and ability to promote formation of the bacterial ubiquitin coat. | ||||
Sequence: T → A | ||||||
Mutagenesis | 390 | Abolishes cleavage by caspase. | ||||
Sequence: D → A | ||||||
Natural variant | VAR_089149 | 399 | in IMD115; uncertain significance; decreased interaction with SHARPIN; does not affect interaction with RBCK1; the genetic variation producing this missense variant predominantly affects splicing, leading to in-frame skipping of exon 9 and lack of 84 amino acids from residue 496 to 579 | |||
Sequence: Q → H | ||||||
Mutagenesis | 699 | Abolishes polyubiquitination activity of LUBAC; when associated with S-702. | ||||
Sequence: C → S | ||||||
Mutagenesis | 702 | Abolishes polyubiquitination activity of LUBAC; when associated with S-699. | ||||
Sequence: C → S | ||||||
Mutagenesis | 735 | Reduced ubiquitination; when associated with R-783 and R-875. | ||||
Sequence: K → R | ||||||
Mutagenesis | 783 | Reduced ubiquitination; when associated with R-735 and R-875. | ||||
Sequence: K → R | ||||||
Mutagenesis | 871 | Abolishes polyubiquitination activity of LUBAC; when associated with S-874. | ||||
Sequence: C → S | ||||||
Mutagenesis | 874 | Abolishes polyubiquitination activity of LUBAC; when associated with S-871. | ||||
Sequence: C → S | ||||||
Mutagenesis | 875 | Reduced ubiquitination; when associated with R-735 and R-783. | ||||
Sequence: K → R | ||||||
Mutagenesis | 885 | Abolished E3 ubiquitin-protein ligase activity and ability to promote formation of the bacterial ubiquitin coat; when associated with A-935 and A-983. | ||||
Sequence: C → A | ||||||
Mutagenesis | 935 | Abolished E3 ubiquitin-protein ligase activity and ability to promote formation of the bacterial ubiquitin coat; when associated with A-885 and A-983. | ||||
Sequence: R → A | ||||||
Mutagenesis | 983 | Abolished E3 ubiquitin-protein ligase activity and ability to promote formation of the bacterial ubiquitin coat; when associated with A-885 and A-935. | ||||
Sequence: D → A | ||||||
Natural variant | VAR_052102 | 1061 | in dbSNP:rs2277484 | |||
Sequence: V → I |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,851 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue, cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000056069 | 1-1072 | UniProt | E3 ubiquitin-protein ligase RNF31 | |||
Sequence: MPGEEEERAFLVAREELASALRRDSGQAFSLEQLRPLLASSLPLAARYLQLDAARLVRCNAHGEPRNYLNTLSTALNILEKYGRNLLSPQRPRYWRGVKFNNPVFRSTVDAVQGGRDVLRLYGYTEEQPDGLSFPEGQEEPDEHQVATVTLEVLLLRTELSLLLQNTHPRQQALEQLLEDKVEDDMLQLSEFDPLLREIAPGPLTTPSVPGSTPGPCFLCGSAPGTLHCPSCKQALCPACDHLFHGHPSRAHHLRQTLPGVLQGTHLSPSLPASAQPRPQSTSLLALGDSSLSSPNPASAHLPWHCAACAMLNEPWAVLCVACDRPRGCKGLGLGTEGPQGTGGLEPDLARGRWACQSCTFENEAAAVLCSICERPRLAQPPSLVVDSRDAGICLQPLQQGDALLASAQSQVWYCIHCTFCNSSPGWVCVMCNRTSSPIPAQHAPRPYASSLEKGPPKPGPPRRLSAPLPSSCGDPEKQRQDKMREEGLQLVSMIREGEAAGACPEEIFSALQYSGTEVPLQWLRSELPYVLEMVAELAGQQDPGLGAFSCQEARRAWLDRHGNLDEAVEECVRTRRRKVQELQSLGFGPEEGSLQALFQHGGDVSRALTELQRQRLEPFRQRLWDSGPEPTPSWDGPDKQSLVRRLLAVYALPSWGRAELALSLLQETPRNYELGDVVEAVRHSQDRAFLRRLLAQECAVCGWALPHNRMQALTSCECTICPDCFRQHFTIALKEKHITDMVCPACGRPDLTDDTQLLSYFSTLDIQLRESLEPDAYALFHKKLTEGVLMRDPKFLWCAQCSFGFIYEREQLEATCPQCHQTFCVRCKRQWEEQHRGRSCEDFQNWKRMNDPEYQAQGLAMYLQENGIDCPKCKFSYALARGGCMHFHCTQCRHQFCSGCYNAFYAKNKCPEPNCRVKKSLHGHHPRDCLFYLRDWTALRLQKLLQDNNVMFNTEPPAGARAVPGGGCRVIEQKEVPNGLRDEACGKETPAGYAGLCQAHYKEYLVSLINAHSLDPATLYEVEELETATERYLHVRPQPLAGEDPPAYQARLLQKLTEEVPLGQSIPRRRK | |||||||
Modified residue (large scale data) | 265 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 383 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 383 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 436 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 437 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 451 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 466 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 466 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 472 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 735 | UniProt | (Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Cross-link | 783 | UniProt | (Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 840 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 875 | UniProt | (Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K |
Post-translational modification
Interaction with OTULIN is required to suppress formation of 'Met-1'-linked polyubiquitin chains and prevent subsequent inactivation of the LUBAC complex (PubMed:24726323).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
LUBAC has a MW of approximately 600 kDa suggesting a heteromultimeric assembly of its subunits (PubMed:17006537, PubMed:21455173, PubMed:21455180, PubMed:21455181).
Associates with the TNF-R1 signaling complex (TNF-RSC) in a stimulation-dependent manner (PubMed:20005846).
Interacts (via the PUB domain) with OTULIN (via the PIM motif); the interaction is direct (PubMed:23708998, PubMed:24726323, PubMed:24726327).
Interacts (via the PUB domain) with VCP (via the PIM motif) (PubMed:24726327).
Interacts (via the PUB domain) with SPATA2 (via the PIM motif); interaction is direct and bridges RNF31 and CYLD (PubMed:27458237, PubMed:27545878, PubMed:27591049, PubMed:28189684).
Interacts with CYLD; the interaction is indirect and is mediated via SPATA2 (PubMed:26997266, PubMed:27458237, PubMed:27545878).
Interacts with MUSK (By similarity).
Interacts with CARD11, promoting linear ubiquitination of BCL10 (PubMed:27777308).
Binary interactions
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, zinc finger, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-485 | Polyubiquitin-binding | ||||
Sequence: MPGEEEERAFLVAREELASALRRDSGQAFSLEQLRPLLASSLPLAARYLQLDAARLVRCNAHGEPRNYLNTLSTALNILEKYGRNLLSPQRPRYWRGVKFNNPVFRSTVDAVQGGRDVLRLYGYTEEQPDGLSFPEGQEEPDEHQVATVTLEVLLLRTELSLLLQNTHPRQQALEQLLEDKVEDDMLQLSEFDPLLREIAPGPLTTPSVPGSTPGPCFLCGSAPGTLHCPSCKQALCPACDHLFHGHPSRAHHLRQTLPGVLQGTHLSPSLPASAQPRPQSTSLLALGDSSLSSPNPASAHLPWHCAACAMLNEPWAVLCVACDRPRGCKGLGLGTEGPQGTGGLEPDLARGRWACQSCTFENEAAAVLCSICERPRLAQPPSLVVDSRDAGICLQPLQQGDALLASAQSQVWYCIHCTFCNSSPGWVCVMCNRTSSPIPAQHAPRPYASSLEKGPPKPGPPRRLSAPLPSSCGDPEKQRQDKMR | ||||||
Domain | 71-142 | PUB | ||||
Sequence: TLSTALNILEKYGRNLLSPQRPRYWRGVKFNNPVFRSTVDAVQGGRDVLRLYGYTEEQPDGLSFPEGQEEPD | ||||||
Region | 263-290 | Disordered | ||||
Sequence: QGTHLSPSLPASAQPRPQSTSLLALGDS | ||||||
Zinc finger | 299-329 | RanBP2-type 1 | ||||
Sequence: SAHLPWHCAACAMLNEPWAVLCVACDRPRGC | ||||||
Zinc finger | 350-379 | RanBP2-type 2 | ||||
Sequence: ARGRWACQSCTFENEAAAVLCSICERPRLA | ||||||
Zinc finger | 409-438 | RanBP2-type 3 | ||||
Sequence: QSQVWYCIHCTFCNSSPGWVCVMCNRTSSP | ||||||
Region | 443-484 | Disordered | ||||
Sequence: HAPRPYASSLEKGPPKPGPPRRLSAPLPSSCGDPEKQRQDKM | ||||||
Compositional bias | 452-466 | Pro residues | ||||
Sequence: LEKGPPKPGPPRRLS | ||||||
Region | 563-616 | Interaction with RBCK1 | ||||
Sequence: GNLDEAVEECVRTRRRKVQELQSLGFGPEEGSLQALFQHGGDVSRALTELQRQR | ||||||
Domain | 564-615 | UBA | ||||
Sequence: NLDEAVEECVRTRRRKVQELQSLGFGPEEGSLQALFQHGGDVSRALTELQRQ | ||||||
Region | 695-929 | TRIAD supradomain | ||||
Sequence: LAQECAVCGWALPHNRMQALTSCECTICPDCFRQHFTIALKEKHITDMVCPACGRPDLTDDTQLLSYFSTLDIQLRESLEPDAYALFHKKLTEGVLMRDPKFLWCAQCSFGFIYEREQLEATCPQCHQTFCVRCKRQWEEQHRGRSCEDFQNWKRMNDPEYQAQGLAMYLQENGIDCPKCKFSYALARGGCMHFHCTQCRHQFCSGCYNAFYAKNKCPEPNCRVKKSLHGHHPRD | ||||||
Zinc finger | 699-749 | RING-type 1 | ||||
Sequence: CAVCGWALPHNRMQALTSCECTICPDCFRQHFTIALKEKHITDMVCPACGR | ||||||
Zinc finger | 779-841 | IBR-type | ||||
Sequence: ALFHKKLTEGVLMRDPKFLWCAQCSFGFIYEREQLEATCPQCHQTFCVRCKRQWEEQHRGRSC | ||||||
Zinc finger | 871-901 | RING-type 2; atypical | ||||
Sequence: CPKCKFSYALARGGCMHFHCTQCRHQFCSGC | ||||||
Region | 910-1072 | LDD domain | ||||
Sequence: KCPEPNCRVKKSLHGHHPRDCLFYLRDWTALRLQKLLQDNNVMFNTEPPAGARAVPGGGCRVIEQKEVPNGLRDEACGKETPAGYAGLCQAHYKEYLVSLINAHSLDPATLYEVEELETATERYLHVRPQPLAGEDPPAYQARLLQKLTEEVPLGQSIPRRRK |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q96EP0-1
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
- Length1,072
- Mass (Da)119,652
- Last updated2001-12-01 v1
- ChecksumCFAD183A14F764BA
Q96EP0-2
- Name2
Q96EP0-3
- Name3
Computationally mapped potential isoform sequences
There are 18 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0AAG2TRQ6 | A0AAG2TRQ6_HUMAN | RNF31 | 161 | ||
H0YNT1 | H0YNT1_HUMAN | RNF31 | 140 | ||
H0YNK5 | H0YNK5_HUMAN | RNF31 | 887 | ||
H0YMN0 | H0YMN0_HUMAN | RNF31 | 143 | ||
H0YMK6 | H0YMK6_HUMAN | RNF31 | 32 | ||
H0YNC1 | H0YNC1_HUMAN | RNF31 | 60 | ||
H0YNJ0 | H0YNJ0_HUMAN | RNF31 | 56 | ||
H0YM57 | H0YM57_HUMAN | RNF31 | 52 | ||
H0YM13 | H0YM13_HUMAN | RNF31 | 170 | ||
H0YMG4 | H0YMG4_HUMAN | RNF31 | 623 | ||
H0YMG8 | H0YMG8_HUMAN | RNF31 | 494 | ||
H0YKI4 | H0YKI4_HUMAN | RNF31 | 165 | ||
H0YKX0 | H0YKX0_HUMAN | RNF31 | 917 | ||
A0A8V8TQD3 | A0A8V8TQD3_HUMAN | RNF31 | 1055 | ||
A0A8V8TQR2 | A0A8V8TQR2_HUMAN | RNF31 | 286 | ||
A0A8V8TPI3 | A0A8V8TPI3_HUMAN | RNF31 | 203 | ||
A0AAG2TKA8 | A0AAG2TKA8_HUMAN | RNF31 | 149 | ||
A0AAG2TIY5 | A0AAG2TIY5_HUMAN | RNF31 | 152 |
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_014006 | 1-151 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_009647 | 73-630 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_014007 | 152-164 | in isoform 3 | |||
Sequence: EVLLLRTELSLLL → MDLCTRAGEPSLT | ||||||
Compositional bias | 452-466 | Pro residues | ||||
Sequence: LEKGPPKPGPPRRLS | ||||||
Sequence conflict | 529 | in Ref. 1; AAP12522 | ||||
Sequence: P → S | ||||||
Sequence conflict | 800 | in Ref. 3; BAA91450 | ||||
Sequence: A → V | ||||||
Alternative sequence | VSP_009648 | 833-841 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 925 | in Ref. 3; BAB15675 | ||||
Sequence: H → R | ||||||
Sequence conflict | 1005 | in Ref. 3; BAB15675 | ||||
Sequence: Y → N | ||||||
Sequence conflict | 1018 | in Ref. 3; BAB15675 | ||||
Sequence: A → S | ||||||
Sequence conflict | 1021 | in Ref. 3; BAB15675 | ||||
Sequence: Y → D |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY256461 EMBL· GenBank· DDBJ | AAP12522.1 EMBL· GenBank· DDBJ | mRNA | ||
AB265810 EMBL· GenBank· DDBJ | BAF35583.1 EMBL· GenBank· DDBJ | mRNA | ||
AK000973 EMBL· GenBank· DDBJ | BAA91450.1 EMBL· GenBank· DDBJ | mRNA | ||
AK027154 EMBL· GenBank· DDBJ | BAB15675.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AK055542 EMBL· GenBank· DDBJ | BAB70948.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK291247 EMBL· GenBank· DDBJ | BAF83936.1 EMBL· GenBank· DDBJ | mRNA | ||
AL136295 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471078 EMBL· GenBank· DDBJ | EAW66098.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC009821 EMBL· GenBank· DDBJ | AAH09821.3 EMBL· GenBank· DDBJ | mRNA | ||
BC012077 EMBL· GenBank· DDBJ | AAH12077.1 EMBL· GenBank· DDBJ | mRNA | ||
BC017376 EMBL· GenBank· DDBJ | AAH17376.3 EMBL· GenBank· DDBJ | mRNA | ||
AK074144 EMBL· GenBank· DDBJ | BAB84970.1 EMBL· GenBank· DDBJ | mRNA |