P10070 · GLI2_HUMAN
- ProteinZinc finger protein GLI2
- GeneGLI2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1586 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Functions as a transcription regulator in the hedgehog (Hh) pathway (PubMed:18455992, PubMed:26565916).
Functions as a transcriptional activator (PubMed:19878745, PubMed:24311597, PubMed:9557682).
May also function as transcriptional repressor (By similarity).
Requires STK36 for full transcriptional activator activity. Required for normal embryonic development (PubMed:15994174, PubMed:20685856).
Functions as a transcriptional activator (PubMed:19878745, PubMed:24311597, PubMed:9557682).
May also function as transcriptional repressor (By similarity).
Requires STK36 for full transcriptional activator activity. Required for normal embryonic development (PubMed:15994174, PubMed:20685856).
Isoform 1
Involved in the smoothened (SHH) signaling pathway.
Isoform 2
Involved in the smoothened (SHH) signaling pathway.
Isoform 3
Involved in the smoothened (SHH) signaling pathway.
Isoform 4
Involved in the smoothened (SHH) signaling pathway.
Isoform 1
Acts as a transcriptional activator in T-cell leukemia virus type 1 (HTLV-1)-infected cells in a Tax-dependent manner. Binds to the DNA sequence 5'-GAACCACCCA-3' which is part of the Tax-responsive element (TRE-2S) regulatory element that augments the Tax-dependent enhancer of HTLV-1 (PubMed:9557682).
Isoform 2
(Microbial infection) Acts as a transcriptional activators in T-cell leukemia virus type 1 (HTLV-1)-infected cells in a Tax-dependent manner. Binds to the DNA sequence 5'-GAACCACCCA-3' which is part of the Tax-responsive element (TRE-2S) regulatory element that augments the Tax-dependent enhancer of HTLV-1 (PubMed:9557682).
Isoform 3
(Microbial infection) Acts as a transcriptional activators in T-cell leukemia virus type 1 (HTLV-1)-infected cells in a Tax-dependent manner. Binds to the DNA sequence 5'-GAACCACCCA-3' which is part of the Tax-responsive element (TRE-2S) regulatory element that augments the Tax-dependent enhancer of HTLV-1 (PubMed:9557682).
Isoform 4
(Microbial infection) Acts as a transcriptional activators in T-cell leukemia virus type 1 (HTLV-1)-infected cells in a Tax-dependent manner. Binds to the DNA sequence 5'-GAACCACCCA-3' which is part of the Tax-responsive element (TRE-2S) regulatory element that augments the Tax-dependent enhancer of HTLV-1 (PubMed:9557682).
Isoform 5
Acts as a transcriptional repressor.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameZinc finger protein GLI2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP10070
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: STK36 promotes translocation to the nucleus. In keratinocytes, it is sequestered in the cytoplasm by SUFU. In the absence of SUFU, it translocates to the nucleus.
Isoform 1
Isoform 2
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Holoprosencephaly 9 (HPE9)
- Note
- DescriptionA structural anomaly of the brain, in which the developing forebrain fails to correctly separate into right and left hemispheres. Holoprosencephaly is genetically heterogeneous and associated with several distinct facies and phenotypic variability. Holoprosencephaly type 9 is characterized by defective anterior pituitary formation and pan-hypopituitarism, with or without overt forebrain cleavage abnormalities, and holoprosencephaly-like midfacial hypoplasia.
- See alsoMIM:610829
Natural variants in HPE9
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_032975 | 479 | R>G | in HPE9; uncertain significance; dbSNP:rs121917708 | |
VAR_032976 | 932 | P>S | in HPE9; uncertain significance; dbSNP:rs1272759660 | |
VAR_032978 | 1554 | P>L | in HPE9; uncertain significance; dbSNP:rs767802807 |
Culler-Jones syndrome (CJS)
- Note
- DescriptionAn autosomal dominant disorder characterized by a wide range of clinical manifestations. Clinical features include hypothalamic hamartoma, pituitary dysfunction, central or postaxial polydactyly, and syndactyly. Malformations are frequent in the viscera, e.g. anal atresia, bifid uvula, congenital heart malformations, pulmonary or renal dysplasia.
- See alsoMIM:615849
Natural variants in CJS
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_075214 | 516 | R>P | in CJS; loss of DNA-binding; loss of transcription factor activity | |
VAR_071700 | 608 | P>L | in CJS; dbSNP:rs149800897 | |
VAR_075216 | 1444-1445 | ML>IF | in CJS; uncertain significance; decreased transcription factor activity |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_047303 | 449 | in dbSNP:rs13427953 | |||
Sequence: D → H | ||||||
Natural variant | VAR_032975 | 479 | in HPE9; uncertain significance; dbSNP:rs121917708 | |||
Sequence: R → G | ||||||
Natural variant | VAR_075214 | 516 | in CJS; loss of DNA-binding; loss of transcription factor activity | |||
Sequence: R → P | ||||||
Natural variant | VAR_047304 | 579 | in dbSNP:rs12618388 | |||
Sequence: S → I | ||||||
Natural variant | VAR_071700 | 608 | in CJS; dbSNP:rs149800897 | |||
Sequence: P → L | ||||||
Natural variant | VAR_047305 | 625 | in dbSNP:rs3099537 | |||
Sequence: P → S | ||||||
Natural variant | VAR_032976 | 932 | in HPE9; uncertain significance; dbSNP:rs1272759660 | |||
Sequence: P → S | ||||||
Natural variant | VAR_047306 | 1156 | in dbSNP:rs3738880 | |||
Sequence: A → S | ||||||
Natural variant | VAR_047307 | 1306 | in dbSNP:rs12711538 | |||
Sequence: D → N | ||||||
Natural variant | VAR_075215 | 1352 | found in Culler-Jones syndrome; when associated in cis with N-1520; decreased transcription factor activity when associated in cis with N-1520; dbSNP:rs149140724 | |||
Sequence: M → V | ||||||
Natural variant | VAR_032977 | 1444 | in dbSNP:rs146467786 | |||
Sequence: M → I | ||||||
Natural variant | VAR_075216 | 1444-1445 | in CJS; uncertain significance; decreased transcription factor activity | |||
Sequence: ML → IF | ||||||
Natural variant | VAR_075217 | 1520 | found in Culler-Jones syndrome; when associated in cis with V-1352 in Culler-Jones syndrome; decreased transcription factor activity when associated in cis with V-1352; dbSNP:rs114814747 | |||
Sequence: D → N | ||||||
Natural variant | VAR_075218 | 1543 | no effect on transcription factor activity; dbSNP:rs138987487 | |||
Sequence: R → H | ||||||
Natural variant | VAR_032978 | 1554 | in HPE9; uncertain significance; dbSNP:rs767802807 | |||
Sequence: P → L |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,914 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, cross-link, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000354050 | 1-1586 | UniProt | Zinc finger protein GLI2 | |||
Sequence: METSASATASEKQEAKSGILEAAGFPDPGKKASPLVVAAAAAAAVAAQGVPQHLLPPFHAPLPIDMRHQEGRYHYEPHSVHGVHGPPALSGSPVISDISLIRLSPHPAGPGESPFNAPHPYVNPHMEHYLRSVHSSPTLSMISAARGLSPADVAQEHLKERGLFGLPAPGTTPSDYYHQMTLVAGHPAPYGDLLMQSGGAASAPHLHDYLNPVDVSRFSSPRVTPRLSRKRALSISPLSDASLDLQRMIRTSPNSLVAYINNSRSSSAASGSYGHLSAGALSPAFTFPHPINPVAYQQILSQQRGLGSAFGHTPPLIQPSPTFLAQQPMALTSINATPTQLSSSSNCLSDTNQNKQSSESAVSSTVNPVAIHKRSKVKTEPEGLRPASPLALTQGQVSGHGSCGCALPLSQEQLADLKEDLDRDDCKQEAEVVIYETNCHWEDCTKEYDTQEQLVHHINNEHIHGEKKEFVCRWQACTREQKPFKAQYMLVVHMRRHTGEKPHKCTFEGCSKAYSRLENLKTHLRSHTGEKPYVCEHEGCNKAFSNASDRAKHQNRTHSNEKPYICKIPGCTKRYTDPSSLRKHVKTVHGPDAHVTKKQRNDVHLRTPLLKENGDSEAGTEPGGPESTEASSTSQAVEDCLHVRAIKTESSGLCQSSPGAQSSCSSEPSPLGSAPNNDSGVEMPGTGPGSLGDLTALDDTPPGADTSALAAPSAGGLQLRKHMTTMHRFEQLKKEKLKSLKDSCSWAGPTPHTRNTKLPPLPGSGSILENFSGSGGGGPAGLLPNPRLSELSASEVTMLSQLQERRDSSTSTVSSAYTVSRRSSGISPYFSSRRSSEASPLGAGRPHNASSADSYDPISTDASRRSSEASQCSGGSGLLNLTPAQQYSLRAKYAAATGGPPPTPLPGLERMSLRTRLALLDAPERTLPAGCPRPLGPRRGSDGPTYGHGHAGAAPAFPHEAPGGGARRASDPVRRPDALSLPRVQRFHSTHNVNPGPLPPCADRRGLRLQSHPSTDGGLARGAYSPRPPSISENVAMEAVAAGVDGAGPEADLGLPEDDLVLPDDVVQYIKAHASGALDEGTGQVYPTESTGFSDNPRLPSPGLHGQRRMVAADSNVGPSAPMLGGCQLGFGAPSSLNKNNMPVQWNEVSSGTVDALASQVKPPPFPQGNLAVVQQKPAFGQYPGYSPQGLQASPGGLDSTQPHLQPRSGAPSQGIPRVNYMQQLRQPVAGSQCPGMTTTMSPHACYGQVHPQLSPSTISGALNQFPQSCSNMPAKPGHLGHPQQTEVAPDPTTMGNRHRELGVPDSALAGVPPPHPVQSYPQQSHHLAASMSQEGYHQVPSLLPARQPGFMEPQTGPMGVATAGFGLVQPRPPLEPSPTGRHRGVRAVQQQLAYARATGHAMAAMPSSQETAEAVPKGAMGNMGSVPPQPPPQDAGGAPDHSMLYYYGQIHMYEQDGGLENLGSCQVMRSQPPQPQACQDSIQPQPLPSPGVNQVSSTVDSQLLEAPQIDFDAIMDDGDHSSLFSGALSPSLLHSLSQNSSRLTTPRNSLTLPSIPAGISNMAVGDMSSMLTSLAEESKFLNMMT | |||||||
Cross-link | 50 | UniProt | In isoform P10070-2; Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: V | |||||||
Cross-link | 50 | UniProt | In isoform P10070-4; Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: V | |||||||
Modified residue (large scale data) | 92 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 132 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 136 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 149 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 234 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 234 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 236 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 236 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 242 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 388 | UniProt | Phosphoserine; by DYRK2 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 388 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 725 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 757 | UniProt | N6-acetyllysine; by EP300 | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 808 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 823 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 824 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 866 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 941 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1011 | UniProt | Phosphoserine; by DYRK2 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1014 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1101 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1194 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated in vitro by ULK3. Phosphorylated by DYRK2; this inhibits GLI2 transcription factor activity and promotes proteasomal degradation of GLI2.
Acetylation at Lys-757 inhibits Hh target gene expression, probably by impeding entry into chromatin thus preventing promoter occupancy.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in breast cancers (at protein level) (PubMed:26565916).
Isoform 1 and isoform 4 are expressed in HTLV-1-infected T-cell lines (at protein level) (PubMed:9557682).
Isoform 1 and isoform 2 are strongly expressed in HTLV-1-infected T-cell lines (PubMed:9557682).
Isoform 3 and isoform 4 are weakly expressed in HTLV-1-infected T-cell lines (PubMed:9557682).
Isoform 1 and isoform 4 are expressed in HTLV-1-infected T-cell lines (at protein level) (PubMed:9557682).
Isoform 1 and isoform 2 are strongly expressed in HTLV-1-infected T-cell lines (PubMed:9557682).
Isoform 3 and isoform 4 are weakly expressed in HTLV-1-infected T-cell lines (PubMed:9557682).
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interaction with ZIC1 and ZIC2 (By similarity).
Interacts with STK36 (PubMed:10806483).
Interacts with SUFU; this inhibits transcriptional activation mediated by GLI2 (PubMed:24311597).
Interacts (via C-terminal internal region) with FOXC1 (via N-terminus); this interaction is direct and increases GLI2 DNA-binding and transcriptional activity through a smoothened (SMO)-independent Hedgehog (Hh) signaling pathway (PubMed:26565916).
Interacts with STK36 (PubMed:10806483).
Interacts with SUFU; this inhibits transcriptional activation mediated by GLI2 (PubMed:24311597).
Interacts (via C-terminal internal region) with FOXC1 (via N-terminus); this interaction is direct and increases GLI2 DNA-binding and transcriptional activity through a smoothened (SMO)-independent Hedgehog (Hh) signaling pathway (PubMed:26565916).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P10070 | BTRC Q9Y297 | 4 | EBI-10821567, EBI-307461 | |
BINARY | P10070 | SMAD3 P84022 | 4 | EBI-10821567, EBI-347161 | |
BINARY | P10070 | TSG101 Q99816 | 2 | EBI-10821567, EBI-346882 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-22 | Disordered | ||||
Sequence: METSASATASEKQEAKSGILEA | ||||||
Compositional bias | 342-370 | Polar residues | ||||
Sequence: SSSSNCLSDTNQNKQSSESAVSSTVNPVA | ||||||
Region | 342-389 | Disordered | ||||
Sequence: SSSSNCLSDTNQNKQSSESAVSSTVNPVAIHKRSKVKTEPEGLRPASP | ||||||
Zinc finger | 437-464 | C2H2-type 1 | ||||
Sequence: TNCHWEDCTKEYDTQEQLVHHINNEHIH | ||||||
Zinc finger | 475-497 | C2H2-type 2; degenerate | ||||
Sequence: QACTREQKPFKAQYMLVVHMRRH | ||||||
Zinc finger | 503-527 | C2H2-type 3 | ||||
Sequence: HKCTFEGCSKAYSRLENLKTHLRSH | ||||||
Zinc finger | 533-558 | C2H2-type 4 | ||||
Sequence: YVCEHEGCNKAFSNASDRAKHQNRTH | ||||||
Zinc finger | 564-589 | C2H2-type 5 | ||||
Sequence: YICKIPGCTKRYTDPSSLRKHVKTVH | ||||||
Compositional bias | 577-611 | Basic and acidic residues | ||||
Sequence: DPSSLRKHVKTVHGPDAHVTKKQRNDVHLRTPLLK | ||||||
Region | 577-636 | Disordered | ||||
Sequence: DPSSLRKHVKTVHGPDAHVTKKQRNDVHLRTPLLKENGDSEAGTEPGGPESTEASSTSQA | ||||||
Compositional bias | 650-680 | Polar residues | ||||
Sequence: SSGLCQSSPGAQSSCSSEPSPLGSAPNNDSG | ||||||
Region | 650-716 | Disordered | ||||
Sequence: SSGLCQSSPGAQSSCSSEPSPLGSAPNNDSGVEMPGTGPGSLGDLTALDDTPPGADTSALAAPSAGG | ||||||
Region | 742-879 | Disordered | ||||
Sequence: DSCSWAGPTPHTRNTKLPPLPGSGSILENFSGSGGGGPAGLLPNPRLSELSASEVTMLSQLQERRDSSTSTVSSAYTVSRRSSGISPYFSSRRSSEASPLGAGRPHNASSADSYDPISTDASRRSSEASQCSGGSGLL | ||||||
Compositional bias | 746-760 | Polar residues | ||||
Sequence: WAGPTPHTRNTKLPP | ||||||
Compositional bias | 790-838 | Polar residues | ||||
Sequence: ELSASEVTMLSQLQERRDSSTSTVSSAYTVSRRSSGISPYFSSRRSSEA | ||||||
Compositional bias | 852-879 | Polar residues | ||||
Sequence: ADSYDPISTDASRRSSEASQCSGGSGLL | ||||||
Region | 925-1030 | Disordered | ||||
Sequence: RTLPAGCPRPLGPRRGSDGPTYGHGHAGAAPAFPHEAPGGGARRASDPVRRPDALSLPRVQRFHSTHNVNPGPLPPCADRRGLRLQSHPSTDGGLARGAYSPRPPS | ||||||
Region | 1182-1215 | Disordered | ||||
Sequence: QYPGYSPQGLQASPGGLDSTQPHLQPRSGAPSQG | ||||||
Compositional bias | 1187-1209 | Polar residues | ||||
Sequence: SPQGLQASPGGLDSTQPHLQPRS | ||||||
Region | 1421-1441 | Disordered | ||||
Sequence: MGNMGSVPPQPPPQDAGGAPD | ||||||
Region | 1469-1498 | Disordered | ||||
Sequence: MRSQPPQPQACQDSIQPQPLPSPGVNQVSS |
Domain
The N-terminal domain confers transcriptional repressor activity, while the C-terminal domain mediates transcriptional activation.
Sequence similarities
Belongs to the GLI C2H2-type zinc-finger protein family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 5 isoforms produced by Alternative splicing.
P10070-5
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.
- Name5
- SynonymsGLI2
- Length1,586
- Mass (Da)167,783
- Last updated2008-11-25 v4
- Checksum86556112E13DE106
P10070-1
- Name1
- SynonymsAlpha, GLI2star, GLI2deltaN
- Differences from canonical
- 1-328: Missing
P10070-2
- Name2
- SynonymsBeta
P10070-3
- Name3
- SynonymsGamma
- Differences from canonical
- 1-328: Missing
- 1149-1157: VSSGTVDAL → ASATWLSGT
- 1158-1586: Missing
P10070-4
- Name4
- SynonymsDelta
- Differences from canonical
- 1-328: Missing
- 394-410: Missing
- 1149-1157: VSSGTVDAL → ASATWLSGT
- 1158-1586: Missing
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q1PSW9 | Q1PSW9_HUMAN | GLI2 | 82 | ||
A0A6Q8PH00 | A0A6Q8PH00_HUMAN | GLI2 | 152 | ||
F2Z2B4 | F2Z2B4_HUMAN | GLI2 | 67 | ||
H7C1U2 | H7C1U2_HUMAN | GLI2 | 56 | ||
A0A7I2PJA1 | A0A7I2PJA1_HUMAN | GLI2 | 1569 |
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_035708 | 1-328 | in isoform 1, isoform 2, isoform 3 and isoform 4 | |||
Sequence: Missing | ||||||
Compositional bias | 342-370 | Polar residues | ||||
Sequence: SSSSNCLSDTNQNKQSSESAVSSTVNPVA | ||||||
Alternative sequence | VSP_006877 | 394-410 | in isoform 2 and isoform 4 | |||
Sequence: Missing | ||||||
Sequence conflict | 456 | in Ref. 5; M20672 | ||||
Sequence: H → Q | ||||||
Compositional bias | 577-611 | Basic and acidic residues | ||||
Sequence: DPSSLRKHVKTVHGPDAHVTKKQRNDVHLRTPLLK | ||||||
Compositional bias | 650-680 | Polar residues | ||||
Sequence: SSGLCQSSPGAQSSCSSEPSPLGSAPNNDSG | ||||||
Sequence conflict | 718-719 | in Ref. 4; BAA03568/BAA03569 | ||||
Sequence: QL → HV | ||||||
Compositional bias | 746-760 | Polar residues | ||||
Sequence: WAGPTPHTRNTKLPP | ||||||
Compositional bias | 790-838 | Polar residues | ||||
Sequence: ELSASEVTMLSQLQERRDSSTSTVSSAYTVSRRSSGISPYFSSRRSSEA | ||||||
Compositional bias | 852-879 | Polar residues | ||||
Sequence: ADSYDPISTDASRRSSEASQCSGGSGLL | ||||||
Sequence conflict | 923-925 | in Ref. 1; BAA25665/BAA25667/BAA25666/BAA25668 | ||||
Sequence: PER → AEG | ||||||
Sequence conflict | 966 | in Ref. 1; BAA25665/BAA25667/BAA25666/BAA25668 | ||||
Sequence: A → T | ||||||
Alternative sequence | VSP_006878 | 1149-1157 | in isoform 3 and isoform 4 | |||
Sequence: VSSGTVDAL → ASATWLSGT | ||||||
Alternative sequence | VSP_006879 | 1158-1586 | in isoform 3 and isoform 4 | |||
Sequence: Missing | ||||||
Compositional bias | 1187-1209 | Polar residues | ||||
Sequence: SPQGLQASPGGLDSTQPHLQPRS |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB007295 EMBL· GenBank· DDBJ | BAA25665.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AB007296 EMBL· GenBank· DDBJ | BAA25666.1 EMBL· GenBank· DDBJ | mRNA | ||
AB007297 EMBL· GenBank· DDBJ | BAA25667.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AB007298 EMBL· GenBank· DDBJ | BAA25668.1 EMBL· GenBank· DDBJ | mRNA | ||
DQ086814 EMBL· GenBank· DDBJ | AAY87165.1 EMBL· GenBank· DDBJ | mRNA | ||
AC016764 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC017033 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
D14827 EMBL· GenBank· DDBJ | BAA03568.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
D14828 EMBL· GenBank· DDBJ | BAA03569.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
M20672 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
M20673 EMBL· GenBank· DDBJ | AAA35898.1 EMBL· GenBank· DDBJ | Genomic DNA |