P25799 · NFKB1_MOUSE
- ProteinNuclear factor NF-kappa-B p105 subunit
- GeneNfkb1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids971 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric p65-p50 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric p65-p50 and RelB-p50 complexes are transcriptional activators. The NF-kappa-B p50-p50 homodimer is a transcriptional repressor, but can act as a transcriptional activator when associated with BCL3. NFKB1 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p105 and generation of p50 by a cotranslational processing. The proteasome-mediated process ensures the production of both p50 and p105 and preserves their independent function, although processing of NFKB1/p105 also appears to occur post-translationally. p50 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. Plays a role in the regulation of apoptosis. In a complex with MAP3K8, NFKB1/p105 represses MAP3K8-induced MAPK signaling; active MAP3K8 is released by proteasome-dependent degradation of NFKB1/p105.
Nuclear factor NF-kappa-B p105 subunit
P105 is the precursor of the active p50 subunit (Nuclear factor NF-kappa-B p50 subunit) of the nuclear factor NF-kappa-B. Acts as a cytoplasmic retention of attached NF-kappa-B proteins by p105.
Nuclear factor NF-kappa-B p50 subunit
Constitutes the active form, which associates with RELA/p65 to form the NF-kappa-B p65-p50 complex to form a transcription factor. Together with RELA/p65, binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions.
Isoform 3
Isoform 3 (p98) (but not p84 or p105) acts as a transactivator of NF-kappa-B-regulated gene expression.
Isoform 5
Act as inhibitors of transactivation of p50 NF-kappa-B subunit, probably by sequestering it in the cytoplasm.
Isoform 6
Act as inhibitors of transactivation of p50 NF-kappa-B subunit, probably by sequestering it in the cytoplasm.
Isoform 7
Act as inhibitors of transactivation of p50 NF-kappa-B subunit, probably by sequestering it in the cytoplasm.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 431-432 | Cleavage (when cotranslationally processed) | ||||
Sequence: GT |
GO annotations
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNuclear factor NF-kappa-B p105 subunit
- Alternative names
- Cleaved into 1 chains
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP25799
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Nuclear factor NF-kappa-B p105 subunit
Nuclear factor NF-kappa-B p50 subunit
Note: Association with NFKBIA inhibitor (I-kappa-B), promotes its retention in the cytoplasm in an inactive form. Translocates into the nucleus following NFKBIA degradation.
Isoform 5
Isoform 6
Isoform 7
Keywords
- Cellular component
Phenotypes & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 44 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue, lipidation, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000030313 | 1-431 | Nuclear factor NF-kappa-B p50 subunit | |||
Sequence: MADDDPYGTGQMFHLNTALTHSIFNAELYSPEIPLSTDGPYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDGVCTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACIRGYNPGLLVHSDLAYLQAEGGGDRQLTDREKEIIRQAAVQQTKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSKAPNASNLKIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVHRQFAIVFKTPKYKDVNITKPASVFVQLRRKSDLETSEPKPFLYYPEIKDKEEVQRKRQKLMPNFSDSFGGGSGAGAGGGGMFGSGGGGGSTGSPGPGYGYSNYGFPPYGGITFHPGVTKSNAGVTHG | ||||||
Chain | PRO_0000030312 | 1-971 | Nuclear factor NF-kappa-B p105 subunit | |||
Sequence: MADDDPYGTGQMFHLNTALTHSIFNAELYSPEIPLSTDGPYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDGVCTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACIRGYNPGLLVHSDLAYLQAEGGGDRQLTDREKEIIRQAAVQQTKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSKAPNASNLKIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVHRQFAIVFKTPKYKDVNITKPASVFVQLRRKSDLETSEPKPFLYYPEIKDKEEVQRKRQKLMPNFSDSFGGGSGAGAGGGGMFGSGGGGGSTGSPGPGYGYSNYGFPPYGGITFHPGVTKSNAGVTHGTINTKFKNGPKDCAKSDDEESLTLPEKETEGEGPSLPMACTKTEPIALASTMEDKEQDMGFQDNLFLEKALQLARRHANALFDYAVTGDVKMLLAVQRHLTAVQDENGDSVLHLAIIHLHAQLVRDLLEVTSGLISDDIINMRNDLYQTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDRILSILLKSRKAAPLIDHPNGEGLNAIHIAVMSNSLPCLLLLVAAGAEVNAQEQKSGRTALHLAVEYDNISLAGCLLLEGDAHVDSTTYDGTTPLHIAAGRGSTRLAALLKAAGADPLVENFEPLYDLDDSWEKAGEDEGVVPGTTPLDMAANWQVFDILNGKPYEPVFTSDDILPQGDMKQLTEDTRLQLCKLLEIPDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEVSGGTIKELMEALQQMGYTEAIEVIQAAFRTPATTASSPVTTAQVHCLPLSSSSTRQHIDELRDSDSVCDSGVETSFRKLSFTESLTGDSPLLSLNKMPHGYGQEGPIEGKI | ||||||
Modified residue | 59 | S-nitrosocysteine; alternate | ||||
Sequence: C | ||||||
Lipidation | 59 | S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine; alternate | ||||
Sequence: C | ||||||
Cross-link | 323 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 335 | Phosphoserine; by PKA | ||||
Sequence: S | ||||||
Modified residue | 438 | N6-acetyllysine; by EP300 | ||||
Sequence: K | ||||||
Modified residue | 447 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 674 | (3S)-3-hydroxyasparagine; by HIF1AN | ||||
Sequence: N | ||||||
Modified residue | 755 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 896 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 910 | Phosphoserine; by GSK3-beta; in vitro | ||||
Sequence: S | ||||||
Modified residue | 926 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 930 | Phosphoserine; by IKKB | ||||
Sequence: S | ||||||
Modified residue | 935 | Phosphoserine; by IKKB | ||||
Sequence: S | ||||||
Modified residue | 940 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 946 | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Generation of the NF-kappa-B p50 (Nuclear factor NF-kappa-B p50 subunit) transcription factor takes place both cotranslationally and post-translationally via non-mutually exclusive mechanisms (By similarity).
A cotranslational processing allows the production of both p50 and p105 (Nuclear factor NF-kappa-B p105 subunit) from a single NFKB1 mRNA (PubMed:9529257).
While translation occurs, the particular unfolded structure after the GRR repeat region acts as a substrate for the proteasome, promoting degradation of the C-terminus (PubMed:9529257).
The GRR acts as a proteasomal 'stop signal', protecting the region upstream of the GRR from degradation and promoting generation of p50 (PubMed:9529257).
It is unclear if limited proteasome degradation during cotranslational processing depends on ubiquitination (PubMed:9529257).
NF-kappa-B p50 is also generated post-translationally following ubiquitination by the KPC complex, leading to limited processing by the proteasome downstream of the GRR region, thereby generating p50 (By similarity).
A cotranslational processing allows the production of both p50 and p105 (Nuclear factor NF-kappa-B p105 subunit) from a single NFKB1 mRNA (PubMed:9529257).
While translation occurs, the particular unfolded structure after the GRR repeat region acts as a substrate for the proteasome, promoting degradation of the C-terminus (PubMed:9529257).
The GRR acts as a proteasomal 'stop signal', protecting the region upstream of the GRR from degradation and promoting generation of p50 (PubMed:9529257).
It is unclear if limited proteasome degradation during cotranslational processing depends on ubiquitination (PubMed:9529257).
NF-kappa-B p50 is also generated post-translationally following ubiquitination by the KPC complex, leading to limited processing by the proteasome downstream of the GRR region, thereby generating p50 (By similarity).
Nuclear factor NF-kappa-B p105 subunit
Phosphorylation at the C-terminus by IKBKB/IKKB acts as a signal for ubiquitination and promotes either complete degradation or processing to generate the NF-kappa-B p50 (Nuclear factor NF-kappa-B p50 subunit) (By similarity).
Phosphorylation at Ser-910 primes p105 for proteolytic processing in response to TNF-alpha stimulation (By similarity).
Phosphorylation at Ser-926, Ser-930 and Ser-935 are required for BTRC/BTRCP-mediated ubiquitination and proteolysis (By similarity).
Phosphorylation at Ser-930 is also required for ubiquitination by the KPC complex and limited processing to generate NF-kappa-B p50 (Nuclear factor NF-kappa-B p50 subunit) (By similarity).
Phosphorylation at Ser-910 primes p105 for proteolytic processing in response to TNF-alpha stimulation (By similarity).
Phosphorylation at Ser-926, Ser-930 and Ser-935 are required for BTRC/BTRCP-mediated ubiquitination and proteolysis (By similarity).
Phosphorylation at Ser-930 is also required for ubiquitination by the KPC complex and limited processing to generate NF-kappa-B p50 (Nuclear factor NF-kappa-B p50 subunit) (By similarity).
Nuclear factor NF-kappa-B p105 subunit
Polyubiquitinated at multiple Lys residues in the C-terminus (By similarity).
Polyubiquitinated by the SCF(FBXW11) and SCF(BTRC) complexes following phosphorylation at Ser-926, Ser-930 and Ser-935, leading to its complete degradation (By similarity).
In contrast, polyubiquitination by the KPC complex following phosphorylation at Ser-930 leads to limited proteosomal processing and generation of the active NF-kappa-B p50 (Nuclear factor NF-kappa-B p50 subunit) (By similarity).
Polyubiquitinated by the SCF(FBXW11) and SCF(BTRC) complexes following phosphorylation at Ser-926, Ser-930 and Ser-935, leading to its complete degradation (By similarity).
In contrast, polyubiquitination by the KPC complex following phosphorylation at Ser-930 leads to limited proteosomal processing and generation of the active NF-kappa-B p50 (Nuclear factor NF-kappa-B p50 subunit) (By similarity).
S-nitrosylation of Cys-59 affects DNA binding.
The covalent modification of cysteine by 15-deoxy-Delta12,14-prostaglandin-J2 is autocatalytic and reversible. It may occur as an alternative to other cysteine modifications, such as S-nitrosylation and S-palmitoylation.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Component of the NF-kappa-B p65-p50 complex (By similarity).
Homodimer; component of the NF-kappa-B p50-p50 complex (By similarity).
Component of the NF-kappa-B p105-p50 complex (By similarity).
Component of the NF-kappa-B p50-c-Rel complex (By similarity).
Component of a complex consisting of the NF-kappa-B p50-p50 homodimer and BCL3 (By similarity).
Also interacts with MAP3K8 (By similarity).
NF-kappa-B p50 subunit interacts with NCOA3 coactivator, which may coactivate NF-kappa-B dependent expression via its histone acetyltransferase activity (By similarity).
Interacts with TSC22D3; this interaction prevents nuclear translocation and DNA-binding (By similarity).
Interacts with SPAG9 and UNC5CL (By similarity).
NFKB1/p105 interacts with CFLAR; the interaction inhibits p105 processing into p50 (By similarity).
NFKB1/p105 forms a ternary complex with MAP3K8 and TNIP2 (By similarity).
Interacts with GSK3B; the interaction prevents processing of p105 to p50 (By similarity).
NFKB1/p50 interacts with NFKBIE (By similarity).
NFKB1/p50 interacts with NFKBIZ (PubMed:11356851, PubMed:15241416).
Nuclear factor NF-kappa-B p50 subunit interacts with NFKBID (PubMed:11931770).
Directly interacts with MEN1 (By similarity).
Interacts with HIF1AN (By similarity).
Interacts with FEM1AA; interaction is direct (PubMed:18270204).
Homodimer; component of the NF-kappa-B p50-p50 complex (By similarity).
Component of the NF-kappa-B p105-p50 complex (By similarity).
Component of the NF-kappa-B p50-c-Rel complex (By similarity).
Component of a complex consisting of the NF-kappa-B p50-p50 homodimer and BCL3 (By similarity).
Also interacts with MAP3K8 (By similarity).
NF-kappa-B p50 subunit interacts with NCOA3 coactivator, which may coactivate NF-kappa-B dependent expression via its histone acetyltransferase activity (By similarity).
Interacts with TSC22D3; this interaction prevents nuclear translocation and DNA-binding (By similarity).
Interacts with SPAG9 and UNC5CL (By similarity).
NFKB1/p105 interacts with CFLAR; the interaction inhibits p105 processing into p50 (By similarity).
NFKB1/p105 forms a ternary complex with MAP3K8 and TNIP2 (By similarity).
Interacts with GSK3B; the interaction prevents processing of p105 to p50 (By similarity).
NFKB1/p50 interacts with NFKBIE (By similarity).
NFKB1/p50 interacts with NFKBIZ (PubMed:11356851, PubMed:15241416).
Nuclear factor NF-kappa-B p50 subunit interacts with NFKBID (PubMed:11931770).
Directly interacts with MEN1 (By similarity).
Interacts with HIF1AN (By similarity).
Interacts with FEM1AA; interaction is direct (PubMed:18270204).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P25799 | Akap8 Q9DBR0 | 4 | EBI-643958, EBI-4285802 | |
BINARY | P25799 | Hdac1 O09106 | 2 | EBI-643958, EBI-301912 | |
XENO | P25799 | NCOA1 Q15788 | 2 | EBI-643958, EBI-455189 | |
BINARY | P25799 | Rela Q04207 | 6 | EBI-643958, EBI-644400 | |
BINARY | P25799-1 | Rela Q04207 | 6 | EBI-643974, EBI-644400 | |
BINARY | PRO_0000030313 | Ankrd42 Q3V096 | 3 | EBI-1209141, EBI-15861272 | |
BINARY | PRO_0000030313 | Relb Q04863 | 2 | EBI-1209141, EBI-1209145 | |
BINARY | PRO_0000030312 | Rela Q04207 | 3 | EBI-1209193, EBI-644400 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, motif, region, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 40-365 | RHD | ||||
Sequence: PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDGVCTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACIRGYNPGLLVHSDLAYLQAEGGGDRQLTDREKEIIRQAAVQQTKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSKAPNASNLKIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVHRQFAIVFKTPKYKDVNITKPASVFVQLRRKSDLETSEPKPFLYYPEIKDKEEVQRKRQKLM | ||||||
Motif | 358-363 | Nuclear localization signal | ||||
Sequence: QRKRQK | ||||||
Region | 370-392 | GRR | ||||
Sequence: DSFGGGSGAGAGGGGMFGSGGGG | ||||||
Region | 433-971 | Interaction with CFLAR | ||||
Sequence: INTKFKNGPKDCAKSDDEESLTLPEKETEGEGPSLPMACTKTEPIALASTMEDKEQDMGFQDNLFLEKALQLARRHANALFDYAVTGDVKMLLAVQRHLTAVQDENGDSVLHLAIIHLHAQLVRDLLEVTSGLISDDIINMRNDLYQTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDRILSILLKSRKAAPLIDHPNGEGLNAIHIAVMSNSLPCLLLLVAAGAEVNAQEQKSGRTALHLAVEYDNISLAGCLLLEGDAHVDSTTYDGTTPLHIAAGRGSTRLAALLKAAGADPLVENFEPLYDLDDSWEKAGEDEGVVPGTTPLDMAANWQVFDILNGKPYEPVFTSDDILPQGDMKQLTEDTRLQLCKLLEIPDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEVSGGTIKELMEALQQMGYTEAIEVIQAAFRTPATTASSPVTTAQVHCLPLSSSSTRQHIDELRDSDSVCDSGVETSFRKLSFTESLTGDSPLLSLNKMPHGYGQEGPIEGKI | ||||||
Region | 439-470 | Disordered | ||||
Sequence: NGPKDCAKSDDEESLTLPEKETEGEGPSLPMA | ||||||
Repeat | 538-567 | ANK 1 | ||||
Sequence: NGDSVLHLAIIHLHAQLVRDLLEVTSGLIS | ||||||
Repeat | 577-606 | ANK 2 | ||||
Sequence: LYQTPLHLAVITKQEDVVEDLLRVGADLSL | ||||||
Repeat | 610-639 | ANK 3 | ||||
Sequence: WGNSVLHLAAKEGHDRILSILLKSRKAAPL | ||||||
Repeat | 646-675 | ANK 4 | ||||
Sequence: EGLNAIHIAVMSNSLPCLLLLVAAGAEVNA | ||||||
Region | 646-680 | Essential for interaction with HIF1AN | ||||
Sequence: EGLNAIHIAVMSNSLPCLLLLVAAGAEVNAQEQKS | ||||||
Repeat | 680-710 | ANK 5 | ||||
Sequence: SGRTALHLAVEYDNISLAGCLLLEGDAHVDS | ||||||
Repeat | 714-743 | ANK 6 | ||||
Sequence: DGTTPLHIAAGRGSTRLAALLKAAGADPLV | ||||||
Repeat | 767-797 | ANK 7 | ||||
Sequence: PGTTPLDMAANWQVFDILNGKPYEPVFTSDD | ||||||
Domain | 801-888 | Death | ||||
Sequence: QGDMKQLTEDTRLQLCKLLEIPDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEVSGGTIKELMEALQQMGYTEAIEVIQAAF |
Domain
The C-terminus of p105 might be involved in cytoplasmic retention, inhibition of DNA-binding, and transcription activation.
Glycine-rich region (GRR) is a critical element in the generation of p50 (Nuclear factor NF-kappa-B p50 subunit) by acting as a proteasomal 'stop signal', which leads to limited proteasomal degradation of the C-terminus, while generating p50.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 7 isoforms produced by Alternative splicing.
P25799-1
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
- Synonymsp105
- Length971
- Mass (Da)105,615
- Last updated2011-07-27 v2
- Checksum91EA9C595E375C30
P25799-2
- Name2
- Synonymsp84
- Differences from canonical
- 780-971: VFDILNGKPYEPVFTSDDILPQGDMKQLTEDTRLQLCKLLEIPDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEVSGGTIKELMEALQQMGYTEAIEVIQAAFRTPATTASSPVTTAQVHCLPLSSSSTRQHIDELRDSDSVCDSGVETSFRKLSFTESLTGDSPLLSLNKMPHGYGQEGPIEGKI → GT
P25799-3
- Name3
- Synonymsp98
- Differences from canonical
- 860-971: VSGGTIKELMEALQQMGYTEAIEVIQAAFRTPATTASSPVTTAQVHCLPLSSSSTRQHIDELRDSDSVCDSGVETSFRKLSFTESLTGDSPLLSLNKMPHGYGQEGPIEGKI → MNSGIVTASVTVVWRHPSANSALQSLLLETAHCYL
P25799-4
- Name4
P25799-5
- Name5
- SynonymsP70, I-kappa-B gamma
- Differences from canonical
- 1-364: Missing
P25799-6
- Name6
- Synonymsp63, I-kappa-B gamma-1
P25799-7
- Name7
- Synonymsp55, I-kappa-B gamma-2
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
V9GX90 | V9GX90_MOUSE | Nfkb1 | 270 | ||
F6Z9G5 | F6Z9G5_MOUSE | Nfkb1 | 534 | ||
A0A0G2JGK6 | A0A0G2JGK6_MOUSE | Nfkb1 | 128 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_017236 | 1-364 | in isoform 5, isoform 6 and isoform 7 | |||
Sequence: Missing | ||||||
Sequence conflict | 111 | in Ref. 9; AAR00341 | ||||
Sequence: L → P | ||||||
Sequence conflict | 265 | in Ref. 10; BAC35117 | ||||
Sequence: E → G | ||||||
Alternative sequence | VSP_017237 | 353-356 | in isoform 4 | |||
Sequence: DKEE → GTWV | ||||||
Alternative sequence | VSP_017238 | 357-971 | in isoform 4 | |||
Sequence: Missing | ||||||
Sequence conflict | 530 | in Ref. 10; BAE34261 | ||||
Sequence: H → D | ||||||
Sequence conflict | 546 | in Ref. 10; BAE34261 | ||||
Sequence: A → G | ||||||
Sequence conflict | 684 | in Ref. 1; AAA40415, 2; AAB21851 and 3; AAB28573 | ||||
Sequence: A → P | ||||||
Sequence conflict | 732 | in Ref. 10; BAE34261 | ||||
Sequence: A → T | ||||||
Alternative sequence | VSP_005583 | 780-971 | in isoform 2 and isoform 7 | |||
Sequence: VFDILNGKPYEPVFTSDDILPQGDMKQLTEDTRLQLCKLLEIPDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEVSGGTIKELMEALQQMGYTEAIEVIQAAFRTPATTASSPVTTAQVHCLPLSSSSTRQHIDELRDSDSVCDSGVETSFRKLSFTESLTGDSPLLSLNKMPHGYGQEGPIEGKI → GT | ||||||
Alternative sequence | VSP_005584 | 860-971 | in isoform 3 and isoform 6 | |||
Sequence: VSGGTIKELMEALQQMGYTEAIEVIQAAFRTPATTASSPVTTAQVHCLPLSSSSTRQHIDELRDSDSVCDSGVETSFRKLSFTESLTGDSPLLSLNKMPHGYGQEGPIEGKI → MNSGIVTASVTVVWRHPSANSALQSLLLETAHCYL | ||||||
Sequence conflict | 950 | in Ref. 10; BAE43399 | ||||
Sequence: P → A |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M57999 EMBL· GenBank· DDBJ | AAA40415.1 EMBL· GenBank· DDBJ | mRNA | ||
S89033 EMBL· GenBank· DDBJ | AAB21851.1 EMBL· GenBank· DDBJ | mRNA | ||
S66656 EMBL· GenBank· DDBJ | AAB28573.1 EMBL· GenBank· DDBJ | mRNA | ||
AB119195 EMBL· GenBank· DDBJ | BAC84979.1 EMBL· GenBank· DDBJ | mRNA | ||
AY521462 EMBL· GenBank· DDBJ | AAS00547.1 EMBL· GenBank· DDBJ | mRNA | ||
AY521463 EMBL· GenBank· DDBJ | AAS00548.1 EMBL· GenBank· DDBJ | mRNA | ||
CH466532 EMBL· GenBank· DDBJ | EDL12143.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC050841 EMBL· GenBank· DDBJ | AAH50841.1 EMBL· GenBank· DDBJ | mRNA | ||
BC138535 EMBL· GenBank· DDBJ | AAI38536.1 EMBL· GenBank· DDBJ | mRNA | ||
BC138536 EMBL· GenBank· DDBJ | AAI38537.1 EMBL· GenBank· DDBJ | mRNA | ||
AY423849 EMBL· GenBank· DDBJ | AAR00341.1 EMBL· GenBank· DDBJ | mRNA | ||
AK052726 EMBL· GenBank· DDBJ | BAC35117.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK089660 EMBL· GenBank· DDBJ | BAE43399.1 EMBL· GenBank· DDBJ | mRNA | ||
AK157915 EMBL· GenBank· DDBJ | BAE34261.1 EMBL· GenBank· DDBJ | mRNA |