Q9Y4B6 · DCAF1_HUMAN
- ProteinDDB1- and CUL4-associated factor 1
- GeneDCAF1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1507 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Acts both as a substrate recognition component of E3 ubiquitin-protein ligase complexes and as an atypical serine/threonine-protein kinase, playing key roles in various processes such as cell cycle, telomerase regulation and histone modification. Probable substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex, named CUL4A-RBX1-DDB1-DCAF1/VPRBP complex, which mediates ubiquitination and proteasome-dependent degradation of proteins such as NF2 (PubMed:23063525).
Involved in the turnover of methylated proteins: recognizes and binds methylated proteins via its chromo domain, leading to ubiquitination of target proteins by the RBX1-DDB1-DCAF1/VPRBP complex (PubMed:23063525).
The CUL4A-RBX1-DDB1-DCAF1/VPRBP complex is also involved in B-cell development: DCAF1 is recruited by RAG1 to ubiquitinate proteins, leading to limit error-prone repair during V(D)J recombination (By similarity).
Also part of the EDVP complex, an E3 ligase complex that mediates ubiquitination of proteins such as TERT, leading to TERT degradation and telomerase inhibition (PubMed:19287380, PubMed:23362280).
The EDVP complex also mediates ubiquitination and degradation of CCP110 (PubMed:28242748, PubMed:34259627).
Also acts as an atypical serine/threonine-protein kinase that specifically mediates phosphorylation of 'Thr-120' of histone H2A (H2AT120ph) in a nucleosomal context, thereby repressing transcription (PubMed:24140421).
H2AT120ph is present in the regulatory region of many tumor suppresor genes, down-regulates their transcription and is present at high level in a number of tumors (PubMed:24140421).
Involved in JNK-mediated apoptosis during cell competition process via its interaction with LLGL1 and LLGL2 (PubMed:20644714).
By acting on TET dioxygenses, essential for oocyte maintenance at the primordial follicle stage, hence essential for female fertility (By similarity).
Involved in the turnover of methylated proteins: recognizes and binds methylated proteins via its chromo domain, leading to ubiquitination of target proteins by the RBX1-DDB1-DCAF1/VPRBP complex (PubMed:23063525).
The CUL4A-RBX1-DDB1-DCAF1/VPRBP complex is also involved in B-cell development: DCAF1 is recruited by RAG1 to ubiquitinate proteins, leading to limit error-prone repair during V(D)J recombination (By similarity).
Also part of the EDVP complex, an E3 ligase complex that mediates ubiquitination of proteins such as TERT, leading to TERT degradation and telomerase inhibition (PubMed:19287380, PubMed:23362280).
The EDVP complex also mediates ubiquitination and degradation of CCP110 (PubMed:28242748, PubMed:34259627).
Also acts as an atypical serine/threonine-protein kinase that specifically mediates phosphorylation of 'Thr-120' of histone H2A (H2AT120ph) in a nucleosomal context, thereby repressing transcription (PubMed:24140421).
H2AT120ph is present in the regulatory region of many tumor suppresor genes, down-regulates their transcription and is present at high level in a number of tumors (PubMed:24140421).
Involved in JNK-mediated apoptosis during cell competition process via its interaction with LLGL1 and LLGL2 (PubMed:20644714).
By acting on TET dioxygenses, essential for oocyte maintenance at the primordial follicle stage, hence essential for female fertility (By similarity).
(Microbial infection) In case of infection by HIV-1 virus, it is recruited by HIV-1 Vpr in order to hijack the CUL4A-RBX1-DDB1-DCAF1/VPRBP function leading to arrest the cell cycle in G2 phase, and also to protect the viral protein from proteasomal degradation by another E3 ubiquitin ligase. The HIV-1 Vpr protein hijacks the CUL4A-RBX1-DDB1-DCAF1/VPRBP complex to promote ubiquitination and degradation of proteins such as TERT and ZIP/ZGPAT.
(Microbial infection) In case of infection by HIV-2 virus, it is recruited by HIV-2 Vpx in order to hijack the CUL4A-RBX1-DDB1-DCAF1/VPRBP function leading to enhanced efficiency of macrophage infection and promotion of the replication of cognate primate lentiviruses in cells of monocyte/macrophage lineage.
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Pathway
Protein modification; protein ubiquitination.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | Cul4-RING E3 ubiquitin ligase complex | |
Cellular Component | cytoplasm | |
Cellular Component | fibrillar center | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | ATP binding | |
Molecular Function | histone H2AT120 kinase activity | |
Molecular Function | nuclear estrogen receptor binding | |
Molecular Function | protein serine kinase activity | |
Molecular Function | ubiquitin-like ligase-substrate adaptor activity | |
Biological Process | B cell differentiation | |
Biological Process | cell competition in a multicellular organism | |
Biological Process | negative regulation of transcription by RNA polymerase II | |
Biological Process | positive regulation of protein catabolic process | |
Biological Process | post-translational protein modification | |
Biological Process | protein ubiquitination | |
Biological Process | V(D)J recombination |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDDB1- and CUL4-associated factor 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9Y4B6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Associated with chromatin in a DDB1-independent and cell cycle-dependent manner: recruited to chromatin as DNA is being replicated and is released from chromatin before mitosis (By similarity).
Homogenous pancellular distribution is observed outside S-phase and a slight cytoplasmic-to-nuclear translocation from early to late S-phase (By similarity).
Colocalizes with TET1 and PCNA at replicating heterochromatin during late S phase (By similarity).
More concentrated in nuclei than in cytoplasm in germinal vesicle (GV) stage oocytes, zygotes and the 2-cell stage, but distributed in the cytoplasm at the MII-stage oocytes (By similarity).
Localizes to centrosomes following interaction with CEP78 (PubMed:28242748, PubMed:34259627).
Homogenous pancellular distribution is observed outside S-phase and a slight cytoplasmic-to-nuclear translocation from early to late S-phase (By similarity).
Colocalizes with TET1 and PCNA at replicating heterochromatin during late S phase (By similarity).
More concentrated in nuclei than in cytoplasm in germinal vesicle (GV) stage oocytes, zygotes and the 2-cell stage, but distributed in the cytoplasm at the MII-stage oocytes (By similarity).
Localizes to centrosomes following interaction with CEP78 (PubMed:28242748, PubMed:34259627).
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 194 | Abolishes serine/threonine-protein kinase kinase activity. | ||||
Sequence: K → R | ||||||
Natural variant | VAR_051486 | 267 | in dbSNP:rs3749318 | |||
Sequence: N → D | ||||||
Mutagenesis | 361 | Abolishes serine/threonine-protein kinase kinase activity. | ||||
Sequence: D → A | ||||||
Mutagenesis | 363 | Abolishes serine/threonine-protein kinase kinase activity. | ||||
Sequence: K → A | ||||||
Natural variant | VAR_051487 | 378 | does not affect serine/threonine-protein kinase kinase activity; dbSNP:rs17712228 | |||
Sequence: L → F | ||||||
Natural variant | VAR_051488 | 1031 | in dbSNP:rs9835229 | |||
Sequence: L → P | ||||||
Mutagenesis | 1247 | Loss of interaction with DDB1, no effect on interaction with TET3; when associated with A-1283. | ||||
Sequence: R → A | ||||||
Mutagenesis | 1283 | Loss of interaction with DDB1, no effect on interaction with TET3; when associated with A-1247. | ||||
Sequence: R → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 995 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000287473 | 1-1507 | UniProt | DDB1- and CUL4-associated factor 1 | |||
Sequence: MTTVVVHVDSKAELTTLLEQWEKEHGSGQDMVPILTRMSQLIEKETEEYRKGDPDPFDDRHPGRADPECMLGHLLRILFKNDDFMNALVNAYVMTSREPPLNTAACRLLLDIMPGLETAVVFQEKEGIVENLFKWAREADQPLRTYSTGLLGGAMENQDIAANYRDENSQLVAIVLRRLRELQLQEVALRQENKRPSPRKLSSEPLLPLDEEAVDMDYGDMAVDVVDGDQEEASGDMEISFHLDSGHKTSSRVNSTTKPEDGGLKKNKSAKQGDRENFRKAKQKLGFSSSDPDRMFVELSNSSWSEMSPWVIGTNYTLYPMTPAIEQRLILQYLTPLGEYQELLPIFMQLGSRELMMFYIDLKQTNDVLLTFEALKHLASLLLHNKFATEFVAHGGVQKLLEIPRPSMAATGVSMCLYYLSYNQDAMERVCMHPHNVLSDVVNYTLWLMECSHASGCCHATMFFSICFSFRAVLELFDRYDGLRRLVNLISTLEILNLEDQGALLSDDEIFASRQTGKHTCMALRKYFEAHLAIKLEQVKQSLQRTEGGILVHPQPPYKACSYTHEQIVEMMEFLIEYGPAQLYWEPAEVFLKLSCVQLLLQLISIACNWKTYYARNDTVRFALDVLAILTVVPKIQLQLAESVDVLDEAGSTVSTVGISIILGVAEGEFFIHDAEIQKSALQIIINCVCGPDNRISSIGKFISGTPRRKLPQNPKSSEHTLAKMWNVVQSNNGIKVLLSLLSIKMPITDADQIRALACKALVGLSRSSTVRQIISKLPLFSSCQIQQLMKEPVLQDKRSDHVKFCKYAAELIERVSGKPLLIGTDVSLARLQKADVVAQSRISFPEKELLLLIRNHLISKGLGETATVLTKEADLPMTAASHSSAFTPVTAAASPVSLPRTPRIANGIATRLGSHAAVGASAPSAPTAHPQPRPPQGPLALPGPSYAGNSPLIGRISFIRERPSPCNGRKIRVLRQKSDHGAYSQSPAIKKQLDRHLPSPPTLDSIITEYLREQHARCKNPVATCPPFSLFTPHQCPEPKQRRQAPINFTSRLNRRASFPKYGGVDGGCFDRHLIFSRFRPISVFREANEDESGFTCCAFSARERFLMLGTCTGQLKLYNVFSGQEEASYNCHNSAITHLEPSRDGSLLLTSATWSQPLSALWGMKSVFDMKHSFTEDHYVEFSKHSQDRVIGTKGDIAHIYDIQTGNKLLTLFNPDLANNYKRNCATFNPTDDLVLNDGVLWDVRSAQAIHKFDKFNMNISGVFHPNGLEVIINTEIWDLRTFHLLHTVPALDQCRVVFNHTGTVMYGAMLQADDEDDLMEERMKSPFGSSFRTFNATDYKPIATIDVKRNIFDLCTDTKDCYLAVIENQGSMDALNMDTVCRLYEVGRQRLAEDEDEEEDQEEEEQEEEDDDEDDDDTDDLDELDTDQLLEAELEEDDNNENAGEDGDNDFSPSDEELANLLEEGEDGEDEDSDADEEVELILGDTDSSDNSDLEDDIILSLNE | |||||||
Modified residue | 202 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 255 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 255 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 288 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 289 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 290 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 701 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 706 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 828 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 828 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 888 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 888 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 895 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 895 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 898 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 898 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 902 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 915 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 951 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 979 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 979 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 984 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 985 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 987 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1000 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1000 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1003 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1006 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1328 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1328 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Component of the DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex, named CUL4A-RBX1-DDB1-DCAF1/VPRBP complex. Interacts with DDB1; the interaction is direct. Also forms a ternary complex with DDA1 and DDB1. Interacts with NF2 (via FERM domain). Component of the EDVP complex, a E3 ligase complex containing DYRK2, EDD/UBR5, DDB1 and DCAF1 (PubMed:19287380, PubMed:24357321, PubMed:28242748, PubMed:34259627).
Interacts with DYRK2; the interaction is direct. Interacts with RAG1; the interaction is direct. Interacts with LLGL1 and LLGL2. Interacts with histone H3. Interacts with ESR1 and LATS1; probably recruited by LATS1 to promote ESR1 ubiquitination and ubiquitin-mediated proteasomal degradation (PubMed:28068668).
Directly interacts with TET1, TET2 and TET3 (via C-terminus) (PubMed:24357321, PubMed:25557551).
Interacts with CEP78; promoting DCAF1 localization to centrosomes (PubMed:28242748, PubMed:34259627).
Interacts with DYRK2; the interaction is direct. Interacts with RAG1; the interaction is direct. Interacts with LLGL1 and LLGL2. Interacts with histone H3. Interacts with ESR1 and LATS1; probably recruited by LATS1 to promote ESR1 ubiquitination and ubiquitin-mediated proteasomal degradation (PubMed:28068668).
Directly interacts with TET1, TET2 and TET3 (via C-terminus) (PubMed:24357321, PubMed:25557551).
Interacts with CEP78; promoting DCAF1 localization to centrosomes (PubMed:28242748, PubMed:34259627).
(Microbial infection) Interacts with HIV-1 virus Vpr protein; the interaction is direct.
(Microbial infection) Interacts with HIV-2 virus Vpx protein; the interaction is direct and the complex recruits SAMHD1 to promote its ubiquitin-dependent proteasomal degradation.
(Microbial infection) Interacts (via C-terminus) with human cytomegalovirus protein UL35; this interaction induces the accumulation of cells in the G2 phase of the cell cycle.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9Y4B6 | DDB1 Q16531 | 4 | EBI-1996353, EBI-350322 | |
XENO | Q9Y4B6 | ERDMAN_2289 A0A0H3LAC5 | 2 | EBI-1996353, EBI-25401874 | |
BINARY | Q9Y4B6 | LATS1 O95835 | 4 | EBI-1996353, EBI-444209 | |
BINARY | Q9Y4B6 | LATS2 Q9NRM7 | 2 | EBI-1996353, EBI-3506895 | |
XENO | Q9Y4B6 | vpr P12520 | 5 | EBI-1996353, EBI-6164519 | |
XENO | Q9Y4B6 | vpx P18045 | 2 | EBI-1996353, EBI-6558105 | |
XENO | Q9Y4B6 | vpx P19508 | 4 | EBI-1996353, EBI-6558117 | |
BINARY | Q9Y4B6-3 | DDB1 Q16531 | 2 | EBI-9915372, EBI-350322 | |
BINARY | Q9Y4B6-3 | PRPS1 P60891 | 3 | EBI-9915372, EBI-749195 | |
XENO | Q9Y4B6-3 | vpr P05928 | 2 | EBI-9915372, EBI-9210238 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain, repeat, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 141-500 | Protein kinase-like | ||||
Sequence: QPLRTYSTGLLGGAMENQDIAANYRDENSQLVAIVLRRLRELQLQEVALRQENKRPSPRKLSSEPLLPLDEEAVDMDYGDMAVDVVDGDQEEASGDMEISFHLDSGHKTSSRVNSTTKPEDGGLKKNKSAKQGDRENFRKAKQKLGFSSSDPDRMFVELSNSSWSEMSPWVIGTNYTLYPMTPAIEQRLILQYLTPLGEYQELLPIFMQLGSRELMMFYIDLKQTNDVLLTFEALKHLASLLLHNKFATEFVAHGGVQKLLEIPRPSMAATGVSMCLYYLSYNQDAMERVCMHPHNVLSDVVNYTLWLMECSHASGCCHATMFFSICFSFRAVLELFDRYDGLRRLVNLISTLEILNLED | ||||||
Region | 242-288 | Disordered | ||||
Sequence: HLDSGHKTSSRVNSTTKPEDGGLKKNKSAKQGDRENFRKAKQKLGFS | ||||||
Compositional bias | 259-282 | Basic and acidic residues | ||||
Sequence: PEDGGLKKNKSAKQGDRENFRKAK | ||||||
Domain | 562-593 | Chromo | ||||
Sequence: SYTHEQIVEMMEFLIEYGPAQLYWEPAEVFLK | ||||||
Domain | 846-878 | LisH | ||||
Sequence: PEKELLLLIRNHLISKGLGETATVLTKEADLPM | ||||||
Region | 917-947 | Disordered | ||||
Sequence: AAVGASAPSAPTAHPQPRPPQGPLALPGPSY | ||||||
Compositional bias | 928-942 | Pro residues | ||||
Sequence: TAHPQPRPPQGPLAL | ||||||
Repeat | 1091-1130 | WD 1 | ||||
Sequence: EDESGFTCCAFSARERFLMLGTCTGQLKLYNVFSGQEEAS | ||||||
Region | 1091-1290 | WD repeat-like region | ||||
Sequence: EDESGFTCCAFSARERFLMLGTCTGQLKLYNVFSGQEEASYNCHNSAITHLEPSRDGSLLLTSATWSQPLSALWGMKSVFDMKHSFTEDHYVEFSKHSQDRVIGTKGDIAHIYDIQTGNKLLTLFNPDLANNYKRNCATFNPTDDLVLNDGVLWDVRSAQAIHKFDKFNMNISGVFHPNGLEVIINTEIWDLRTFHLLHT | ||||||
Repeat | 1133-1174 | WD 2 | ||||
Sequence: CHNSAITHLEPSRDGSLLLTSATWSQPLSALWGMKSVFDMKH | ||||||
Repeat | 1176-1213 | WD 3 | ||||
Sequence: FTEDHYVEFSKHSQDRVIGTKGDIAHIYDIQTGNKLLT | ||||||
Repeat | 1215-1247 | WD 4 | ||||
Sequence: FNPDLANNYKRNCATFNPTDDLVLNDGVLWDVR | ||||||
Motif | 1242-1249 | DWD box 1 | ||||
Sequence: VLWDVRSA | ||||||
Repeat | 1248-1290 | WD 5 | ||||
Sequence: SAQAIHKFDKFNMNISGVFHPNGLEVIINTEIWDLRTFHLLHT | ||||||
Motif | 1278-1285 | DWD box 2 | ||||
Sequence: EIWDLRTF | ||||||
Region | 1393-1507 | Disordered | ||||
Sequence: RLAEDEDEEEDQEEEEQEEEDDDEDDDDTDDLDELDTDQLLEAELEEDDNNENAGEDGDNDFSPSDEELANLLEEGEDGEDEDSDADEEVELILGDTDSSDNSDLEDDIILSLNE | ||||||
Compositional bias | 1395-1497 | Acidic residues | ||||
Sequence: AEDEDEEEDQEEEEQEEEDDDEDDDDTDDLDELDTDQLLEAELEEDDNNENAGEDGDNDFSPSDEELANLLEEGEDGEDEDSDADEEVELILGDTDSSDNSDL | ||||||
Region | 1418-1507 | Interaction with NF2 | ||||
Sequence: DDDTDDLDELDTDQLLEAELEEDDNNENAGEDGDNDFSPSDEELANLLEEGEDGEDEDSDADEEVELILGDTDSSDNSDLEDDIILSLNE |
Domain
The protein kinase-like region mediates the threonine-protein kinase activity.
The DWD boxes are required for interaction with DDB1.
The chromo domain with a restricted pocket directly recognizes monomethylated substrates.
Sequence similarities
Belongs to the VPRBP/DCAF1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q9Y4B6-1
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
- Length1,507
- Mass (Da)169,007
- Last updated2007-05-15 v3
- Checksum7E71AB2CAC4962C5
Q9Y4B6-2
- Name2
- Differences from canonical
- 87-87: Missing
Q9Y4B6-3
- Name3
- Differences from canonical
- 225-673: Missing
Sequence caution
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_025498 | 87 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_025499 | 225-673 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 259-282 | Basic and acidic residues | ||||
Sequence: PEDGGLKKNKSAKQGDRENFRKAK | ||||||
Compositional bias | 928-942 | Pro residues | ||||
Sequence: TAHPQPRPPQGPLAL | ||||||
Compositional bias | 1395-1497 | Acidic residues | ||||
Sequence: AEDEDEEEDQEEEEQEEEDDDEDDDDTDDLDELDTDQLLEAELEEDDNNENAGEDGDNDFSPSDEELANLLEEGEDGEDEDSDADEEVELILGDTDSSDNSDL |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB018343 EMBL· GenBank· DDBJ | BAA34520.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AC092037 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC022792 EMBL· GenBank· DDBJ | AAH22792.1 EMBL· GenBank· DDBJ | mRNA | ||
BC110371 EMBL· GenBank· DDBJ | AAI10372.1 EMBL· GenBank· DDBJ | mRNA | ||
AL080145 EMBL· GenBank· DDBJ | CAB45738.1 EMBL· GenBank· DDBJ | mRNA | ||
AF061935 EMBL· GenBank· DDBJ | AAG27134.1 EMBL· GenBank· DDBJ | mRNA |