P08235 · MCR_HUMAN
- ProteinMineralocorticoid receptor
- GeneNR3C2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids984 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Features
Showing features for binding site, dna binding.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 603 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
DNA binding | 603-668 | Nuclear receptor | ||||
Sequence: CLVCGDEASGCHYGVVTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRLQKCLQAGM | ||||||
Binding site | 606 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 620 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 623 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 639 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 645 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 655 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 658 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 770 | 21-hydroxyprogesterone (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 770 | aldosterone (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 770 | progesterone (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 776 | 21-hydroxyprogesterone (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 776 | aldosterone (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 776 | progesterone (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 817 | 21-hydroxyprogesterone (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 817 | aldosterone (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 817 | progesterone (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 945 | 21-hydroxyprogesterone (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 945 | aldosterone (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 945 | progesterone (UniProtKB | ChEBI) | ||||
Sequence: T |
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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Aspect | Term | |
---|---|---|
Cellular Component | chromatin | |
Cellular Component | cytosol | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | nucleoplasm | |
Cellular Component | receptor complex | |
Molecular Function | DNA-binding transcription factor activity | |
Molecular Function | DNA-binding transcription factor activity, RNA polymerase II-specific | |
Molecular Function | estrogen response element binding | |
Molecular Function | nuclear receptor activity | |
Molecular Function | nuclear steroid receptor activity | |
Molecular Function | sequence-specific double-stranded DNA binding | |
Molecular Function | steroid binding | |
Molecular Function | TBP-class protein binding | |
Molecular Function | zinc ion binding | |
Biological Process | nuclear receptor-mediated steroid hormone signaling pathway | |
Biological Process | positive regulation of non-canonical NF-kappaB signal transduction | |
Biological Process | regulation of transcription by RNA polymerase II | |
Biological Process | signal transduction |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMineralocorticoid receptor
- Short namesMR
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP08235
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Pseudohypoaldosteronism 1, autosomal dominant (PHA1A)
- Note
- DescriptionA salt wasting disease resulting from target organ unresponsiveness to mineralocorticoids. PHA1A is a mild form characterized by target organ defects confined to kidney. Patients may present with neonatal renal salt wasting with hyperkalaemic acidosis despite high aldosterone levels. These patients improve with age and usually become asymptomatic without treatment.
- See alsoMIM:177735
Natural variants in PHA1A
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_031268 | 633 | G>R | in PHA1A; reduces transcription transactivation upon aldosterone binding; dbSNP:rs121912566 | |
VAR_031269 | 645 | C>S | in PHA1A | |
VAR_031270 | 659 | R>S | in PHA1A | |
VAR_031271 | 759 | P>S | in PHA1A | |
VAR_031272 | 769 | L>P | in PHA1A | |
VAR_031273 | 770 | N>K | in PHA1A | |
VAR_031274 | 776 | Q>R | in PHA1A; reduces aldosterone binding; dbSNP:rs121912565 | |
VAR_031275 | 805 | S>P | in PHA1A | |
VAR_031276 | 815 | S>R | in PHA1A | |
VAR_031277 | 818 | S>L | in PHA1A; abolishes translocation to the nucleus and transcription transactivation upon aldosterone binding; dbSNP:rs121912573 | |
VAR_015627 | 924 | L>P | in PHA1A; abolishes transcription transactivation upon aldosterone binding; dbSNP:rs121912563 | |
VAR_031278 | 972 | E>G | in PHA1A; reduces affinity for aldosterone and transcription transactivation; dbSNP:rs121912574 | |
VAR_031279 | 979 | L>P | in PHA1A; loss of aldosterone binding and transcription transactivation; dbSNP:rs121912567 |
Early-onset hypertension with severe exacerbation in pregnancy (EOHSEP)
- Note
- DescriptionInheritance is autosomal dominant. The disease is characterized by the onset of severe hypertension before the age of 20, and by suppression of aldosterone secretion.
- See alsoMIM:605115
Natural variants in EOHSEP
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_015626 | 810 | S>L | in EOHSEP; alters receptor specificity and leads to constitutive activation; dbSNP:rs41511344 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_036063 | 7 | in a colorectal cancer sample; somatic mutation | |||
Sequence: H → Q | ||||||
Natural variant | VAR_014623 | 180 | decreased mineralocorticoid receptor activity; dbSNP:rs5522 | |||
Sequence: V → I | ||||||
Natural variant | VAR_015625 | 241 | changed mineralocorticoid receptor activity; changed response curve to aldosterone stimulation | |||
Sequence: V → A | ||||||
Natural variant | VAR_014624 | 444 | in dbSNP:rs5523 | |||
Sequence: N → T | ||||||
Natural variant | VAR_014625 | 537 | in dbSNP:rs5526 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_014626 | 554 | in dbSNP:rs5527 | |||
Sequence: N → S | ||||||
Natural variant | VAR_031268 | 633 | in PHA1A; reduces transcription transactivation upon aldosterone binding; dbSNP:rs121912566 | |||
Sequence: G → R | ||||||
Natural variant | VAR_031269 | 645 | in PHA1A | |||
Sequence: C → S | ||||||
Natural variant | VAR_031270 | 659 | in PHA1A | |||
Sequence: R → S | ||||||
Natural variant | VAR_031271 | 759 | in PHA1A | |||
Sequence: P → S | ||||||
Mutagenesis | 767 | Loss of transcription transactivation. | ||||
Sequence: S → N | ||||||
Mutagenesis | 767 | Strong decrease of transcription transactivation. | ||||
Sequence: S → Q | ||||||
Natural variant | VAR_031272 | 769 | in PHA1A | |||
Sequence: L → P | ||||||
Natural variant | VAR_031273 | 770 | in PHA1A | |||
Sequence: N → K | ||||||
Mutagenesis | 770 | Abolishes aldosterone binding and transcription transactivation. | ||||
Sequence: N → A, D, H, Q, S, or T | ||||||
Natural variant | VAR_031274 | 776 | in PHA1A; reduces aldosterone binding; dbSNP:rs121912565 | |||
Sequence: Q → R | ||||||
Mutagenesis | 776 | Reduces aldosterone binding and transcription transactivation. | ||||
Sequence: Q → A | ||||||
Mutagenesis | 782 | Decreased coactivator binding. | ||||
Sequence: K → E | ||||||
Mutagenesis | 785 | Loss of coactivator binding. | ||||
Sequence: K → E | ||||||
Mutagenesis | 796 | Decreased coactivator binding. | ||||
Sequence: E → R | ||||||
Natural variant | VAR_031275 | 805 | in PHA1A | |||
Sequence: S → P | ||||||
Mutagenesis | 808 | Increases aldosterone-binding. | ||||
Sequence: C → S | ||||||
Natural variant | VAR_015626 | 810 | in EOHSEP; alters receptor specificity and leads to constitutive activation; dbSNP:rs41511344 | |||
Sequence: S → L | ||||||
Mutagenesis | 810 | Alters receptor specificity. | ||||
Sequence: S → M | ||||||
Natural variant | VAR_031276 | 815 | in PHA1A | |||
Sequence: S → R | ||||||
Mutagenesis | 817 | Reduces aldosterone binding and transcription transactivation. | ||||
Sequence: R → A | ||||||
Natural variant | VAR_031277 | 818 | in PHA1A; abolishes translocation to the nucleus and transcription transactivation upon aldosterone binding; dbSNP:rs121912573 | |||
Sequence: S → L | ||||||
Natural variant | VAR_029311 | 826 | in dbSNP:rs13306592 | |||
Sequence: F → Y | ||||||
Mutagenesis | 849 | Strongly decreases affinity for aldosterone and transcription transactivation. | ||||
Sequence: C → S | ||||||
Natural variant | VAR_015627 | 924 | in PHA1A; abolishes transcription transactivation upon aldosterone binding; dbSNP:rs121912563 | |||
Sequence: L → P | ||||||
Mutagenesis | 942 | Abolishes steroid binding and transcription transactivation. | ||||
Sequence: C → S | ||||||
Mutagenesis | 945 | Decreases aldosterone-binding and cortisol-binding. | ||||
Sequence: T → A | ||||||
Mutagenesis | 952 | Reduces transcription transactivation. | ||||
Sequence: L → A | ||||||
Mutagenesis | 953 | Slightly reduces aldosterone binding and abolishes transcription transactivation. | ||||
Sequence: K → A | ||||||
Mutagenesis | 954 | Reduces aldosterone binding and abolishes transcription transactivation. | ||||
Sequence: V → A | ||||||
Mutagenesis | 956 | Abolishes aldosterone binding and transcription transactivation. | ||||
Sequence: F → A | ||||||
Mutagenesis | 957 | Slightly reduces aldosterone binding and transcription transactivation. | ||||
Sequence: P → A | ||||||
Natural variant | VAR_031278 | 972 | in PHA1A; reduces affinity for aldosterone and transcription transactivation; dbSNP:rs121912574 | |||
Sequence: E → G | ||||||
Natural variant | VAR_031279 | 979 | in PHA1A; loss of aldosterone binding and transcription transactivation; dbSNP:rs121912567 | |||
Sequence: L → P |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,390 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, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000053682 | 1-984 | UniProt | Mineralocorticoid receptor | |||
Sequence: METKGYHSLPEGLDMERRWGQVSQAVERSSLGPTERTDENNYMEIVNVSCVSGAIPNNSTQGSSKEKQELLPCLQQDNNRPGILTSDIKTELESKELSATVAESMGLYMDSVRDADYSYEQQNQQGSMSPAKIYQNVEQLVKFYKGNGHRPSTLSCVNTPLRSFMSDSGSSVNGGVMRAVVKSPIMCHEKSPSVCSPLNMTSSVCSPAGINSVSSTTASFGSFPVHSPITQGTPLTCSPNVENRGSRSHSPAHASNVGSPLSSPLSSMKSSISSPPSHCSVKSPVSSPNNVTLRSSVSSPANINNSRCSVSSPSNTNNRSTLSSPAASTVGSICSPVNNAFSYTASGTSAGSSTLRDVVPSPDTQEKGAQEVPFPKTEEVESAISNGVTGQLNIVQYIKPEPDGAFSSSCLGGNSKINSDSSFSVPIKQESTKHSCSGTSFKGNPTVNPFPFMDGSYFSFMDDKDYYSLSGILGPPVPGFDGNCEGSGFPVGIKQEPDDGSYYPEASIPSSAIVGVNSGGQSFHYRIGAQGTISLSRSARDQSFQHLSSFPPVNTLVESWKSHGDLSSRRSDGYPVLEYIPENVSSSTLRSVSTGSSRPSKICLVCGDEASGCHYGVVTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRLQKCLQAGMNLGARKSKKLGKLKGIHEEQPQQQQPPPPPPPPQSPEEGTTYIAPAKEPSVNTALVPQLSTISRALTPSPVMVLENIEPEIVYAGYDSSKPDTAENLLSTLNRLAGKQMIQVVKWAKVLPGFKNLPLEDQITLIQYSWMCLSSFALSWRSYKHTNSQFLYFAPDLVFNEEKMHQSAMYELCQGMHQISLQFVRLQLTFEEYTIMKVLLLLSTIPKDGLKSQAAFEEMRTNYIKELRKMVTKCPNNSGQSWQRFYQLTKLLDSMHDLVSDLLEFCFYTFRESHALKVEFPAMLVEIISDQLPKVESGNAKPLYFHRK | |||||||
Modified residue | 250 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 250 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 259 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 259 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 283 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 283 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 287 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 287 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 298 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 299 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 299 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 361 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 703 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, zinc finger, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-602 | Modulating | ||||
Sequence: METKGYHSLPEGLDMERRWGQVSQAVERSSLGPTERTDENNYMEIVNVSCVSGAIPNNSTQGSSKEKQELLPCLQQDNNRPGILTSDIKTELESKELSATVAESMGLYMDSVRDADYSYEQQNQQGSMSPAKIYQNVEQLVKFYKGNGHRPSTLSCVNTPLRSFMSDSGSSVNGGVMRAVVKSPIMCHEKSPSVCSPLNMTSSVCSPAGINSVSSTTASFGSFPVHSPITQGTPLTCSPNVENRGSRSHSPAHASNVGSPLSSPLSSMKSSISSPPSHCSVKSPVSSPNNVTLRSSVSSPANINNSRCSVSSPSNTNNRSTLSSPAASTVGSICSPVNNAFSYTASGTSAGSSTLRDVVPSPDTQEKGAQEVPFPKTEEVESAISNGVTGQLNIVQYIKPEPDGAFSSSCLGGNSKINSDSSFSVPIKQESTKHSCSGTSFKGNPTVNPFPFMDGSYFSFMDDKDYYSLSGILGPPVPGFDGNCEGSGFPVGIKQEPDDGSYYPEASIPSSAIVGVNSGGQSFHYRIGAQGTISLSRSARDQSFQHLSSFPPVNTLVESWKSHGDLSSRRSDGYPVLEYIPENVSSSTLRSVSTGSSRPSKI | ||||||
Region | 231-329 | Disordered | ||||
Sequence: QGTPLTCSPNVENRGSRSHSPAHASNVGSPLSSPLSSMKSSISSPPSHCSVKSPVSSPNNVTLRSSVSSPANINNSRCSVSSPSNTNNRSTLSSPAAST | ||||||
Region | 347-373 | Disordered | ||||
Sequence: GTSAGSSTLRDVVPSPDTQEKGAQEVP | ||||||
Zinc finger | 603-623 | NR C4-type | ||||
Sequence: CLVCGDEASGCHYGVVTCGSC | ||||||
Zinc finger | 639-663 | NR C4-type | ||||
Sequence: CAGRNDCIIDKIRRKNCPACRLQKC | ||||||
Region | 669-725 | Hinge | ||||
Sequence: NLGARKSKKLGKLKGIHEEQPQQQQPPPPPPPPQSPEEGTTYIAPAKEPSVNTALVP | ||||||
Region | 684-710 | Disordered | ||||
Sequence: IHEEQPQQQQPPPPPPPPQSPEEGTTY | ||||||
Compositional bias | 690-706 | Pro residues | ||||
Sequence: QQQQPPPPPPPPQSPEE | ||||||
Domain | 726-964 | NR LBD | ||||
Sequence: QLSTISRALTPSPVMVLENIEPEIVYAGYDSSKPDTAENLLSTLNRLAGKQMIQVVKWAKVLPGFKNLPLEDQITLIQYSWMCLSSFALSWRSYKHTNSQFLYFAPDLVFNEEKMHQSAMYELCQGMHQISLQFVRLQLTFEEYTIMKVLLLLSTIPKDGLKSQAAFEEMRTNYIKELRKMVTKCPNNSGQSWQRFYQLTKLLDSMHDLVSDLLEFCFYTFRESHALKVEFPAMLVEII | ||||||
Region | 782-785 | Important for coactivator binding | ||||
Sequence: KWAK |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing. Additional isoforms seem to exist.
P08235-1
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
- Length984
- Mass (Da)107,082
- Last updated2018-09-12 v2
- Checksum833D900F2CB27390
P08235-2
- Name2
- NoteLacks steroid-binding activity and acts as ligand-independent transactivator.
P08235-3
- Name3
- Differences from canonical
- 633-633: G → GKCSW
P08235-4
- Name4
- SynonymsDelta
- Differences from canonical
- 672-788: Missing
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_007357 | 633 | in isoform 3 | |||
Sequence: G → GKCSW | ||||||
Alternative sequence | VSP_007358 | 672-706 | in isoform 2 | |||
Sequence: ARKSKKLGKLKGIHEEQPQQQQPPPPPPPPQSPEE → ERRCISLPCMNYARGCTKSAFSSFDCSSPLKNTPS | ||||||
Alternative sequence | VSP_007360 | 672-788 | in isoform 4 | |||
Sequence: Missing | ||||||
Compositional bias | 690-706 | Pro residues | ||||
Sequence: QQQQPPPPPPPPQSPEE | ||||||
Alternative sequence | VSP_007359 | 707-984 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 946 | in Ref. 5; AAI11759 | ||||
Sequence: F → I |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M16801 EMBL· GenBank· DDBJ | AAA59571.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ315514 EMBL· GenBank· DDBJ | CAC67405.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ315515 EMBL· GenBank· DDBJ | CAC67406.1 EMBL· GenBank· DDBJ | mRNA | ||
EU326312 EMBL· GenBank· DDBJ | ACA05924.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
EU326312 EMBL· GenBank· DDBJ | ACA05925.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FJ515829 EMBL· GenBank· DDBJ | ACS13716.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FJ515829 EMBL· GenBank· DDBJ | ACS13717.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC069272 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC093678 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC093881 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC104691 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC106899 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC111758 EMBL· GenBank· DDBJ | AAI11759.1 EMBL· GenBank· DDBJ | mRNA | ||
AH006913 EMBL· GenBank· DDBJ | AAC63513.1 EMBL· GenBank· DDBJ | Genomic DNA |