P37275 · ZEB1_HUMAN
- ProteinZinc finger E-box-binding homeobox 1
- GeneZEB1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1124 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Features
Showing features for dna binding.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
DNA binding | 581-640 | Homeobox; atypical | ||||
Sequence: NLSPSQPPLKNLLSLLKAYYALNAQPSAEELSKIADSVNLPLDVVKKWFEKMQAGQISVQ |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameZinc finger E-box-binding homeobox 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 accessionP37275
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Corneal dystrophy, posterior polymorphous, 3 (PPCD3)
- Note
- DescriptionA subtype of posterior corneal dystrophy, a disease characterized by alterations of Descemet membrane presenting as vesicles, opacities or band-like lesions on slit-lamp examination and specular microscopy. Affected patient typically are asymptomatic.
- See alsoMIM:609141
Corneal dystrophy, Fuchs endothelial, 6 (FECD6)
- Note
- DescriptionA corneal disease caused by loss of endothelium of the central cornea. It is characterized by focal wart-like guttata that arise from Descemet membrane and develop in the central cornea, epithelial blisters, reduced vision and pain. Descemet membrane is thickened by abnormal collagenous deposition.
- See alsoMIM:613270
Natural variants in FECD6
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_063759 | 78 | N>T | in FECD6; no effect on protein expression; no effect on nuclear localization; dbSNP:rs80194531 | |
VAR_072898 | 640 | Q>H | in FECD6; down-regulation of several collagen genes expression; dbSNP:rs779148597 | |
VAR_063760 | 649 | P>A | in FECD6; no effect on protein expression; no effect on nuclear localization; dbSNP:rs781750314 | |
VAR_072899 | 696 | N>S | in FECD6; no effect on protein expression; no effect on nuclear localization; dbSNP:rs567252241 | |
VAR_063761 | 810 | Q>P | in FECD6; no effect on protein expression; no effect on nuclear localization; dbSNP:rs199944415 | |
VAR_063762 | 840 | Q>P | in FECD6; no effect on protein expression; no effect on nuclear localization; dbSNP:rs118020901 | |
VAR_072900 | 905 | A>G | in FECD6; no effect on protein expression; no effect on nuclear localization; dbSNP:rs78449005 | |
VAR_063763 | 905 | A>T | in FECD6 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_063759 | 78 | in FECD6; no effect on protein expression; no effect on nuclear localization; dbSNP:rs80194531 | |||
Sequence: N → T | ||||||
Natural variant | VAR_052731 | 90 | in dbSNP:rs12217419 | |||
Sequence: G → R | ||||||
Natural variant | VAR_072897 | 525 | found in a patient with FECD6 | |||
Sequence: G → E | ||||||
Natural variant | VAR_031824 | 553 | in dbSNP:rs35753967 | |||
Sequence: K → R | ||||||
Natural variant | VAR_072898 | 640 | in FECD6; down-regulation of several collagen genes expression; dbSNP:rs779148597 | |||
Sequence: Q → H | ||||||
Natural variant | VAR_063760 | 649 | in FECD6; no effect on protein expression; no effect on nuclear localization; dbSNP:rs781750314 | |||
Sequence: P → A | ||||||
Natural variant | VAR_072899 | 696 | in FECD6; no effect on protein expression; no effect on nuclear localization; dbSNP:rs567252241 | |||
Sequence: N → S | ||||||
Natural variant | VAR_063761 | 810 | in FECD6; no effect on protein expression; no effect on nuclear localization; dbSNP:rs199944415 | |||
Sequence: Q → P | ||||||
Natural variant | VAR_063762 | 840 | in FECD6; no effect on protein expression; no effect on nuclear localization; dbSNP:rs118020901 | |||
Sequence: Q → P | ||||||
Natural variant | VAR_072900 | 905 | in FECD6; no effect on protein expression; no effect on nuclear localization; dbSNP:rs78449005 | |||
Sequence: A → G | ||||||
Natural variant | VAR_063763 | 905 | in FECD6 | |||
Sequence: A → T |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,492 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 chain, modified residue (large scale data), modified residue, cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000047231 | 1-1124 | UniProt | Zinc finger E-box-binding homeobox 1 | |||
Sequence: MADGPRCKRRKQANPRRNNVTNYNTVVETNSDSDDEDKLHIVEEESVTDAADCEGVPEDDLPTDQTVLPGRSSEREGNAKNCWEDDRKEGQEILGPEAQADEAGCTVKDDECESDAENEQNHDPNVEEFLQQQDTAVIFPEAPEEDQRQGTPEASGHDENGTPDAFSQLLTCPYCDRGYKRFTSLKEHIKYRHEKNEDNFSCSLCSYTFAYRTQLERHMTSHKSGRDQRHVTQSGCNRKFKCTECGKAFKYKHHLKEHLRIHSGEKPYECPNCKKRFSHSGSYSSHISSKKCISLIPVNGRPRTGLKTSQCSSPSLSASPGSPTRPQIRQKIENKPLQEQLSVNQIKTEPVDYEFKPIVVASGINCSTPLQNGVFTGGGPLQATSSPQGMVQAVVLPTVGLVSPISINLSDIQNVLKVAVDGNVIRQVLENNQANLASKEQETINASPIQQGGHSVISAISLPLVDQDGTTKIIINYSLEQPSQLQVVPQNLKKENPVATNSCKSEKLPEDLTVKSEKDKSFEGGVNDSTCLLCDDCPGDINALPELKHYDLKQPTQPPPLPAAEAEKPESSVSSATGDGNLSPSQPPLKNLLSLLKAYYALNAQPSAEELSKIADSVNLPLDVVKKWFEKMQAGQISVQSSEPSSPEPGKVNIPAKNNDQPQSANANEPQDSTVNLQSPLKMTNSPVLPVGSTTNGSRSSTPSPSPLNLSSSRNTQGYLYTAEGAQEEPQVEPLDLSLPKQQGELLERSTITSVYQNSVYSVQEEPLNLSCAKKEPQKDSCVTDSEPVVNVIPPSANPINIAIPTVTAQLPTIVAIADQNSVPCLRALAANKQTILIPQVAYTYSTTVSPAVQEPPLKVIQPNGNQDERQDTSSEGVSNVEDQNDSDSTPPKKKMRKTENGMYACDLCDKIFQKSSSLLRHKYEHTGKRPHECGICKKAFKHKHHLIEHMRLHSGEKPYQCDKCGKRFSHSGSYSQHMNHRYSYCKREAEERDSTEQEEAGPEILSNEHVGARASPSQGDSDERESLTREEDEDSEKEEEEEDKEMEELQEEKECEKPQGDEEEEEEEEEVEEEEVEEAENEGEEAKTEGLMKDDRAESQASSLGQKVGESSEQVSEEKTNEA | |||||||
Modified residue (large scale data) | 29 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 31 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 31 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 33 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 33 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 46 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 151 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 186 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 195 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 263 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 307 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 312 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 313 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 313 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 315 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 317 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 319 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 322 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 322 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 324 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 331 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 335 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 342 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 347 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate | ||||
Sequence: K | |||||||
Cross-link | 347 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Cross-link | 439 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 443 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 447 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 493 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 504 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 515 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 521 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 530 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 548 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 553 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 583 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 638 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 641 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 642 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 642 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 645 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 646 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 679 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 679 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 686 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 686 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 693 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 698 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 700 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 700 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 701 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 702 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 702 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 704 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 704 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 706 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 774 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate | ||||
Sequence: K | |||||||
Cross-link | 774 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 887 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 889 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 890 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 955 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 995 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 996 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1016 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1022 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1027 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1036 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1100 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-124 | Disordered | ||||
Sequence: MADGPRCKRRKQANPRRNNVTNYNTVVETNSDSDDEDKLHIVEEESVTDAADCEGVPEDDLPTDQTVLPGRSSEREGNAKNCWEDDRKEGQEILGPEAQADEAGCTVKDDECESDAENEQNHDP | ||||||
Compositional bias | 31-47 | Basic and acidic residues | ||||
Sequence: SDSDDEDKLHIVEEESV | ||||||
Compositional bias | 77-95 | Basic and acidic residues | ||||
Sequence: GNAKNCWEDDRKEGQEILG | ||||||
Region | 142-163 | Disordered | ||||
Sequence: APEEDQRQGTPEASGHDENGTP | ||||||
Zinc finger | 170-193 | C2H2-type 1 | ||||
Sequence: LTCPYCDRGYKRFTSLKEHIKYRH | ||||||
Zinc finger | 200-222 | C2H2-type 2 | ||||
Sequence: FSCSLCSYTFAYRTQLERHMTSH | ||||||
Zinc finger | 240-262 | C2H2-type 3 | ||||
Sequence: FKCTECGKAFKYKHHLKEHLRIH | ||||||
Zinc finger | 268-292 | C2H2-type 4; atypical | ||||
Sequence: YECPNCKKRFSHSGSYSSHISSKKC | ||||||
Region | 304-327 | Disordered | ||||
Sequence: TGLKTSQCSSPSLSASPGSPTRPQ | ||||||
Region | 551-586 | Disordered | ||||
Sequence: DLKQPTQPPPLPAAEAEKPESSVSSATGDGNLSPSQ | ||||||
Compositional bias | 570-586 | Polar residues | ||||
Sequence: ESSVSSATGDGNLSPSQ | ||||||
Region | 636-714 | Disordered | ||||
Sequence: QISVQSSEPSSPEPGKVNIPAKNNDQPQSANANEPQDSTVNLQSPLKMTNSPVLPVGSTTNGSRSSTPSPSPLNLSSSR | ||||||
Compositional bias | 656-714 | Polar residues | ||||
Sequence: AKNNDQPQSANANEPQDSTVNLQSPLKMTNSPVLPVGSTTNGSRSSTPSPSPLNLSSSR | ||||||
Region | 856-898 | Disordered | ||||
Sequence: PPLKVIQPNGNQDERQDTSSEGVSNVEDQNDSDSTPPKKKMRK | ||||||
Compositional bias | 860-886 | Polar residues | ||||
Sequence: VIQPNGNQDERQDTSSEGVSNVEDQND | ||||||
Zinc finger | 904-926 | C2H2-type 5 | ||||
Sequence: YACDLCDKIFQKSSSLLRHKYEH | ||||||
Zinc finger | 932-954 | C2H2-type 6 | ||||
Sequence: HECGICKKAFKHKHHLIEHMRLH | ||||||
Zinc finger | 960-981 | C2H2-type 7; atypical | ||||
Sequence: YQCDKCGKRFSHSGSYSQHMNH | ||||||
Compositional bias | 989-1004 | Basic and acidic residues | ||||
Sequence: EAEERDSTEQEEAGPE | ||||||
Region | 989-1124 | Disordered | ||||
Sequence: EAEERDSTEQEEAGPEILSNEHVGARASPSQGDSDERESLTREEDEDSEKEEEEEDKEMEELQEEKECEKPQGDEEEEEEEEEVEEEEVEEAENEGEEAKTEGLMKDDRAESQASSLGQKVGESSEQVSEEKTNEA | ||||||
Compositional bias | 1027-1050 | Acidic residues | ||||
Sequence: SLTREEDEDSEKEEEEEDKEMEEL | ||||||
Compositional bias | 1058-1085 | Acidic residues | ||||
Sequence: KPQGDEEEEEEEEEVEEEEVEEAENEGE |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 5 isoforms produced by Alternative splicing.
P37275-1
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
- Length1,124
- Mass (Da)124,074
- Last updated1999-07-15 v2
- Checksum0A2714CC37C848D1
P37275-2
- Name2
- Differences from canonical
- 87-87: R → TG
P37275-3
- Name3
- Differences from canonical
- 20-87: VTNYNTVVETNSDSDDEDKLHIVEEESVTDAADCEGVPEDDLPTDQTVLPGRSSEREGNAKNCWEDDR → G
P37275-4
- Name4
- Differences from canonical
- 87-107: RKEGQEILGPEAQADEAGCTV → I
P37275-5
- Name5
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_047279 | 1-19 | in isoform 5 | |||
Sequence: MADGPRCKRRKQANPRRNN → MK | ||||||
Sequence conflict | 12 | in Ref. 3; BAC03673 | ||||
Sequence: Q → R | ||||||
Alternative sequence | VSP_047280 | 20-87 | in isoform 3 | |||
Sequence: VTNYNTVVETNSDSDDEDKLHIVEEESVTDAADCEGVPEDDLPTDQTVLPGRSSEREGNAKNCWEDDR → G | ||||||
Compositional bias | 31-47 | Basic and acidic residues | ||||
Sequence: SDSDDEDKLHIVEEESV | ||||||
Compositional bias | 77-95 | Basic and acidic residues | ||||
Sequence: GNAKNCWEDDRKEGQEILG | ||||||
Sequence conflict | 81 | in Ref. 3; BAC03673 | ||||
Sequence: N → S | ||||||
Sequence conflict | 84 | in Ref. 3; BAC03673 | ||||
Sequence: E → K | ||||||
Alternative sequence | VSP_045184 | 87 | in isoform 2 and isoform 5 | |||
Sequence: R → TG | ||||||
Alternative sequence | VSP_047281 | 87-107 | in isoform 4 | |||
Sequence: RKEGQEILGPEAQADEAGCTV → I | ||||||
Sequence conflict | 220 | in Ref. 3; BAG62481 | ||||
Sequence: T → A | ||||||
Sequence conflict | 390 | in Ref. 3; BAG62481 | ||||
Sequence: M → T | ||||||
Sequence conflict | 420 | in Ref. 2; AAA20602 | ||||
Sequence: V → I | ||||||
Sequence conflict | 472 | in Ref. 3; BAG58962 | ||||
Sequence: K → R | ||||||
Compositional bias | 570-586 | Polar residues | ||||
Sequence: ESSVSSATGDGNLSPSQ | ||||||
Sequence conflict | 609 | in Ref. 7; M81699 | ||||
Sequence: E → Q | ||||||
Sequence conflict | 654 | in Ref. 2; AAA20602 | ||||
Sequence: I → T | ||||||
Compositional bias | 656-714 | Polar residues | ||||
Sequence: AKNNDQPQSANANEPQDSTVNLQSPLKMTNSPVLPVGSTTNGSRSSTPSPSPLNLSSSR | ||||||
Sequence conflict | 672 | in Ref. 7; M81699 | ||||
Sequence: D → H | ||||||
Sequence conflict | 681 | in Ref. 7; M81699 | ||||
Sequence: L → S | ||||||
Sequence conflict | 775 | in Ref. 3; BAG62481 | ||||
Sequence: K → T | ||||||
Sequence conflict | 793-794 | in Ref. 3; BAG58962 | ||||
Sequence: IP → KY | ||||||
Sequence conflict | 797 | in Ref. 3; BAG58962 | ||||
Sequence: A → N | ||||||
Sequence conflict | 818 | in Ref. 3; BAG62481 | ||||
Sequence: A → V | ||||||
Sequence conflict | 838 | in Ref. 3; BAC03673 | ||||
Sequence: I → T | ||||||
Compositional bias | 860-886 | Polar residues | ||||
Sequence: VIQPNGNQDERQDTSSEGVSNVEDQND | ||||||
Compositional bias | 989-1004 | Basic and acidic residues | ||||
Sequence: EAEERDSTEQEEAGPE | ||||||
Compositional bias | 1027-1050 | Acidic residues | ||||
Sequence: SLTREEDEDSEKEEEEEDKEMEEL | ||||||
Compositional bias | 1058-1085 | Acidic residues | ||||
Sequence: KPQGDEEEEEEEEEVEEEEVEEAENEGE | ||||||
Sequence conflict | 1066 | in Ref. 3; BAC03673 | ||||
Sequence: E → G |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D15050 EMBL· GenBank· DDBJ | BAA03646.1 EMBL· GenBank· DDBJ | mRNA | ||
U12170 EMBL· GenBank· DDBJ | AAA20602.1 EMBL· GenBank· DDBJ | mRNA | ||
AK091478 EMBL· GenBank· DDBJ | BAC03673.1 EMBL· GenBank· DDBJ | mRNA | ||
AK296244 EMBL· GenBank· DDBJ | BAG58962.1 EMBL· GenBank· DDBJ | mRNA | ||
AK300830 EMBL· GenBank· DDBJ | BAG62481.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AL158080 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL161935 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL117340 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL355148 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471072 EMBL· GenBank· DDBJ | EAW85989.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC112392 EMBL· GenBank· DDBJ | AAI12393.1 EMBL· GenBank· DDBJ | mRNA | ||
M81699 EMBL· GenBank· DDBJ | - | mRNA | No translation available. |