Protein:ZBTB17 |
Protein Summary |
 Gene summary |
| Gene name: ZBTB17 | ASpdb.0 ID: 7709 | Gene | Gene symbol | ZBTB17 | Gene ID | 7709 |
| Gene name | zinc finger and BTB domain containing 17 |
| Synonyms | MIZ-1|ZNF151|ZNF60|pHZ-67 |
| Cytomap | 1p36.13 |
| Type of gene | protein-coding |
| Description | zinc finger and BTB domain-containing protein 17Myc-interacting Zn finger protein-1zinc finger protein 151 (pHZ-67)zinc finger protein 60 |
| Modification date | 20240403 |
| UniProtAcc | Q13105 |
| Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | ZBTB17 | GO:0001046 | core promoter sequence-specific DNA binding | 19160485 |
| Gene | ZBTB17 | GO:0001228 | DNA-binding transcription activator activity, RNA polymerase II-specific | 9312026 |
| Gene | ZBTB17 | GO:0003700 | DNA-binding transcription factor activity | 12244100 |
| Gene | ZBTB17 | GO:0008285 | negative regulation of cell population proliferation | 19160485 |
| Gene | ZBTB17 | GO:0032991 | protein-containing complex | 19160485 |
| Gene | ZBTB17 | GO:0045944 | positive regulation of transcription by RNA polymerase II | 9312026 |
| Gene | ZBTB17 | GO:0070314 | G1 to G0 transition | 19160485 |
AS Summary |
| Information of the canonical protein with experimentally identified structure from PDB (2023). |
| UniProt Acc | File name | PDB ID | Method | Resolution | Chain | Start | End |
| Q13105-1 | Q13105-1_3m52_A.pdb | 3M52 | X-ray | 2.59 | A | 1 | 115 |
| ASpdb's canonical and alternatively spliced isoform information. |
| accession_id | gene_name | canonical_id | alternative_id | canonical_length | alternative_length | canonical_start | canonical_end | type | originalSEQ | variationSEQ | alternative_start | alternative_end |
| Q13105 | ZBTB17 | Q13105-1 | Q13105-2 | 803 | 810 | 679 | 679 | Substitution | T | TGPATLPA | 679 | 686 |
| Q13105 | ZBTB17 | Q13105-1 | Q13105-3 | 803 | 721 | 1 | 131 | Substitution | MDFPQHSQHVLEQLNQQRQLGLLCDCTFVVDGVHFKAHKAVLAACSEYFKMLFVDQKDVVHLDISNAAGLGQVLEFMYTAKLSLSPENVDDVLAVATFLQMQDIITACHALKSLAEPATSPGGNAEALATE | MMCWPWPLSSKCRTSSRPAMPSSHLLSRLPALGEMRRPWPQKVCPVPSP | 1 | 49 |
| Multiple sequence alignment of our canonical and alternatively spliced ZBTB17 |
| Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of ZBTB17 |
| UniProt-id | ENSG | ENST | ENSP |
| Q13105-1 | ENSG00000116809.12 | ENST00000375743.9 | ENSP00000364895.4 |
| Q13105-2 | ENSG00000116809.12 | ENST00000375733.6 | ENSP00000364885.2 |
| Q13105-3 | ENSG00000116809.12 | ENST00000537142.5 | ENSP00000438529.1 |
| UniProt-id | NM ID | NP ID |
| Q13105-1 | NM_003443.2 | NP_003434.2 |
| Q13105-2 | NM_001287603.1 | NP_001274532.1 |
| Q13105-3 | NM_001242884.1 | NP_001229813.1 |
| Amino acid sequences of our canonical and alternatively spliced ZBTB17 |
| accession_id | Protein sequence |
| Q13105-1 | MDFPQHSQHVLEQLNQQRQLGLLCDCTFVVDGVHFKAHKAVLAACSEYFKMLFVDQKDVVHLDISNAAGLGQVLEFMYTAKLSLSPENVD DVLAVATFLQMQDIITACHALKSLAEPATSPGGNAEALATEGGDKRAKEEKVATSTLSRLEQAGRSTPIGPSRDLKEERGGQAQSAASGA EQTEKADAPREPPPVELKPDPTSGMAAAEAEAALSESSEQEMEVEPARKGEEEQKEQEEQEEEGAGPAEVKEEGSQLENGEAPEENENEE SAGTDSGQELGSEARGLRSGTYGDRTESKAYGSVIHKCEDCGKEFTHTGNFKRHIRIHTGEKPFSCRECSKAFSDPAACKAHEKTHSPLK PYGCEECGKSYRLISLLNLHKKRHSGEARYRCEDCGKLFTTSGNLKRHQLVHSGEKPYQCDYCGRSFSDPTSKMRHLETHDTDKEHKCPH CDKKFNQVGNLKAHLKIHIADGPLKCRECGKQFTTSGNLKRHLRIHSGEKPYVCIHCQRQFADPGALQRHVRIHTGEKPCQCVMCGKAFT QASSLIAHVRQHTGEKPYVCERCGKRFVQSSQLANHIRHHDNIRPHKCSVCSKAFVNVGDLSKHIIIHTGEKPYLCDKCGRGFNRVDNLR SHVKTVHQGKAGIKILEPEEGSEVSVVTVDDMVTLATEALAATAVTQLTVVPVGAAVTADETEVLKAEISKAVKQVQEEDPNTHILYACD |
| Q13105-2 | MDFPQHSQHVLEQLNQQRQLGLLCDCTFVVDGVHFKAHKAVLAACSEYFKMLFVDQKDVVHLDISNAAGLGQVLEFMYTAKLSLSPENVD DVLAVATFLQMQDIITACHALKSLAEPATSPGGNAEALATEGGDKRAKEEKVATSTLSRLEQAGRSTPIGPSRDLKEERGGQAQSAASGA EQTEKADAPREPPPVELKPDPTSGMAAAEAEAALSESSEQEMEVEPARKGEEEQKEQEEQEEEGAGPAEVKEEGSQLENGEAPEENENEE SAGTDSGQELGSEARGLRSGTYGDRTESKAYGSVIHKCEDCGKEFTHTGNFKRHIRIHTGEKPFSCRECSKAFSDPAACKAHEKTHSPLK PYGCEECGKSYRLISLLNLHKKRHSGEARYRCEDCGKLFTTSGNLKRHQLVHSGEKPYQCDYCGRSFSDPTSKMRHLETHDTDKEHKCPH CDKKFNQVGNLKAHLKIHIADGPLKCRECGKQFTTSGNLKRHLRIHSGEKPYVCIHCQRQFADPGALQRHVRIHTGEKPCQCVMCGKAFT QASSLIAHVRQHTGEKPYVCERCGKRFVQSSQLANHIRHHDNIRPHKCSVCSKAFVNVGDLSKHIIIHTGEKPYLCDKCGRGFNRVDNLR SHVKTVHQGKAGIKILEPEEGSEVSVVTVDDMVTLATEALAATAVTQLTGPATLPAVVPVGAAVTADETEVLKAEISKAVKQVQEEDPNT HILYACDSCGDKFLDANSLAQHVRIHTAQALVMFQTDADFYQQYGPGGTWPAGQVLQAGELVFRPRDGAEGQPALAETSPTAPECPPPAE |
| Q13105-3 | MMCWPWPLSSKCRTSSRPAMPSSHLLSRLPALGEMRRPWPQKVCPVPSPGGDKRAKEEKVATSTLSRLEQAGRSTPIGPSRDLKEERGGQ AQSAASGAEQTEKADAPREPPPVELKPDPTSGMAAAEAEAALSESSEQEMEVEPARKGEEEQKEQEEQEEEGAGPAEVKEEGSQLENGEA PEENENEESAGTDSGQELGSEARGLRSGTYGDRTESKAYGSVIHKCEDCGKEFTHTGNFKRHIRIHTGEKPFSCRECSKAFSDPAACKAH EKTHSPLKPYGCEECGKSYRLISLLNLHKKRHSGEARYRCEDCGKLFTTSGNLKRHQLVHSGEKPYQCDYCGRSFSDPTSKMRHLETHDT DKEHKCPHCDKKFNQVGNLKAHLKIHIADGPLKCRECGKQFTTSGNLKRHLRIHSGEKPYVCIHCQRQFADPGALQRHVRIHTGEKPCQC VMCGKAFTQASSLIAHVRQHTGEKPYVCERCGKRFVQSSQLANHIRHHDNIRPHKCSVCSKAFVNVGDLSKHIIIHTGEKPYLCDKCGRG FNRVDNLRSHVKTVHQGKAGIKILEPEEGSEVSVVTVDDMVTLATEALAATAVTQLTVVPVGAAVTADETEVLKAEISKAVKQVQEEDPN THILYACDSCGDKFLDANSLAQHVRIHTAQALVMFQTDADFYQQYGPGGTWPAGQVLQAGELVFRPRDGAEGQPALAETSPTAPECPPPA |
Protein Functional Features |
| Main function of this protein. (from UniProt) |
| ZBTB17 (go to UniProt):Q13105 |
| Retention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at * Minus value of BPloci means that the break pointn is located before the CDS. |
| - Retained protein feature among the 13 regional features. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| Q13105 | Domain | 1 | 104 | Note=BTB;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00037 | Type=Substitution;Start=1;End=131 |
| Q13105 | Region | 116 | 295 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=1;End=131 |
| Q13105 | Region | 637 | 803 | Note=Interaction with HCFC1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12244100;Dbxref=PMID:12244100 | Type=Substitution;Start=679;End=679 |
| Q13105 | Region | 637 | 718 | Note=Interaction with MYC | Type=Substitution;Start=679;End=679 |
| Q13105 | Compositional bias | 131 | 145 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=1;End=131 |
Gene Isoform Structures and Expression Levels for ZBTB17 |
| Gene structures of our canonical and alternative spliced genes of ZBTB17 * Click on the image to open the UCSC genome browser with custom track showing this image in a new window. |
| Expression levels of gene isoforms across GTEx. |
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| Expression levels of gene isoforms across TCGA. |
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Protein Structures |
| PDB and CIF files of the predicted protein structures * Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format. |
| 3D view using mol* of Q13105-1 |
| 3D view using mol* of Q13105-2 |
| 3D view using mol* of Q13105-3 |
pLDDT Score Distribution |
| pLDDT score distribution of the predicted protein structures from AlphaFold2 * AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. |
| pLDDT distribution across the protein length of Q13105-1 |
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| pLDDT distribution across the protein length of Q13105-2 |
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| pLDDT distribution across the protein length of Q13105-3 |
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Ramachandran Plot of Protein Structures |
| Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide. |
| Ramachandran plot of Q13105-1 |
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| Ramachandran plot of Q13105-2 |
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| Ramachandran plot of Q13105-3 |
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Potential Active Site Information |
| The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite. |
| UniProt-id | Site score | Size | D score | Volume | Exposure | Enclosure | Contact | Phobic | Philic | Balance | Don/Acc | Residues |
| Q13105-1 | 0.918 | 66 | 0.956 | 215.061 | 0.681 | 0.662 | 0.782 | 1.163 | 0.627 | 1.853 | 1.125 | 11,14,15,18,23,25,28,35,36,37,38,41,74,78
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| Q13105-2 | 0.988 | 286 | 1.01 | 1212.162 | 0.572 | 0.676 | 0.866 | 0.457 | 1.028 | 0.444 | 0.586 | 204,205,206,207,208,209,210,211,481,483,491,492,49 4,495,498,499,500,507,509,510,511,512,513,516,519, 520,523,526,528,535,537,538,539,540,541,543,544,54 7,548,550,551,558,569,570,571,655,656,657,658,659, 660,661,662,663,666,667,670 |
| Q13105-3 | 0.559 | 15 | 0.517 | 46.305 | 0.741 | 0.588 | 0.812 | 0.782 | 0.613 | 1.275 | 4.991 | 272,275,277,279,280,290
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Protein Structure and Feature Comparision |
| Protein Structure Comparision Using Template Modeling Scores (TM-score). |
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| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green) |
| 3D view using mol* of Q13105-1_Q13105-1_3m52_A.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of Q13105-1_3m52_A_Q13105-2.pdb |
| 3D view using mol* of Q13105-1_3m52_A_Q13105-3.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of Q13105-1_Q13105-2.pdb |
| 3D view using mol* of Q13105-1_Q13105-3.pdb |
| Protein Feature Comparison of the protein sequendary structures among the protiens. |
| ./stats/secondary_structure/figure/Q13105-1_vs_Q13105-2.png |
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| ./stats/secondary_structure/figure/Q13105-1_vs_Q13105-3.png |
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| Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
| ./stats/relative_asa/Q13105-1_vs_Q13105-2.png |
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| ./stats/relative_asa/Q13105-1_vs_Q13105-3.png |
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Protein-Protein Interaction |
| Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| Q13105 | Region | 637 | 803 | Note=Interaction with HCFC1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12244100;Dbxref=PMID:12244100 | Type=Substitution;Start=679;End=679 |
| Q13105 | Region | 637 | 718 | Note=Interaction with MYC | Type=Substitution;Start=679;End=679 |
| Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to ZBTB17 |
| Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
Related Diseases to ZBTB17 |
| Previous studies relating to the alternative splicing of ZBTB17 and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| ZBTB17 | 25245946 | Two ZNF509 (ZBTB49) isoforms induce cell-cycle arrest by activating transcription of p21/CDKN1A and RB upon exposure to genotoxic stress. | ZNF509 is unique among POK family proteins in that four isoforms are generated by alternative splicing. Short ZNF509 (ZNF509S1, -S2 and -S3) isoforms contain one or two out of the seven zinc-fingers contained in long ZNF509 (ZNF509L). Here, we investigated the functions of ZNF509 isoforms in response to DNA damage, showing isoforms to be induced by p53. Intriguingly, to inhibit proliferation of HCT116 and HEK293 cells, we found that ZNF509L activates p21/CDKN1A transcription, while ZNF509S1 induces RB. ZNF509L binds to the p21/CDKN1A promoter either alone or by interacting with MIZ-1 to recruit the co-activator p300 to activate p21/CDKN1A transcription. In contrast, ZNF509S1 binds to the distal RB promoter to interact and interfere with the MIZF repressor, resulting in derepression and transcription of RB. Immunohistochemical analysis revealed that ZNF509 is highly expressed in normal epithelial cells, but was completely repressed in tumor tissues of the colon, lung and skin, indicating a possible role as a tumor suppressor. | D009369 | Neoplasms |
Clinically important variants in ZBTB17 |
| (ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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