O15062 · ZBTB5_HUMAN
- ProteinZinc finger and BTB domain-containing protein 5
- GeneZBTB5
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids677 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
May be involved in transcriptional regulation.
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 | nucleus | |
Molecular Function | DNA-binding transcription factor activity, RNA polymerase II-specific | |
Molecular Function | DNA-binding transcription repressor activity, RNA polymerase II-specific | |
Molecular Function | metal ion binding | |
Molecular Function | RNA polymerase II transcription regulatory region sequence-specific DNA binding | |
Biological Process | negative regulation of transcription by RNA polymerase II | |
Biological Process | regulation of transcription by RNA polymerase II |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameZinc finger and BTB domain-containing protein 5
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO15062
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_052915 | 300 | in dbSNP:rs17502738 | |||
Sequence: D → G |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 650 variants from UniProt as well as other sources including ClinVar and dbSNP.
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_0000047713 | 1-677 | UniProt | Zinc finger and BTB domain-containing protein 5 | |||
Sequence: MDFPGHFEQIFQQLNYQRLHGQLCDCVIVVGNRHFKAHRSVLAACSTHFRALFSVAEGDQTMNMIQLDSEVVTAEAFAALIDMMYTSTLMLGESNVMDVLLAASHLHLNSVVKACKHYLTTRTLPMSPPSERVQEQSARMQRSFMLQQLGLSIVSSALNSSQNGEEQPAPMSSSMRSNLDQRTPFPMRRLHKRKQSAEERARQRLRPSIDESAISDVTPENGPSGVHSREEFFSPDSLKIVDNPKADGMTDNQEDSAIMFDQSFGTQEDAQVPSQSDNSAGNMAQLSMASRATQVETSFDQEAAPEKSSFQCENPEVGLGEKEHMRVVVKSEPLSSPEPQDEVSDVTSQAEGSESVEVEGVVVSAEKIDLSPESSDRSFSDPQSSTDRVGDIHILEVTNNLEHKSTFSISNFLNKSRGNNFTANQNNDDNIPNTTSDCRLESEAPYLLSPEAGPAGGPSSAPGSHVENPFSEPADSHFVRPMQEVMGLPCVQTSGYQGGEQFGMDFSRSGLGLHSSFSRVMIGSPRGGASNFPYYRRIAPKMPVVTSVRSSQIPENSTSSQLMMNGATSSFENGHPSQPGPPQLTRASADVLSKCKKALSEHNVLVVEGARKYACKICCKTFLTLTDCKKHIRVHTGEKPYACLKCGKRFSQSSHLYKHSKTTCLRWQSSNLPSTLL | |||||||
Modified residue (large scale data) | 127 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 208 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 212 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 234 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 234 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 237 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 239 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 298 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 322 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 330 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 371 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 371 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 404 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 415 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 516 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 541 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 594 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 597 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 645 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 658 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O15062 | BAG4 O95429 | 3 | EBI-722671, EBI-2949658 | |
BINARY | O15062 | DCX O43602 | 4 | EBI-722671, EBI-8646694 | |
BINARY | O15062 | DCX O43602-2 | 3 | EBI-722671, EBI-14148644 | |
BINARY | O15062 | METTL5 Q9NRN9 | 3 | EBI-722671, EBI-12360031 | |
BINARY | O15062 | SWAP70 Q9UH65 | 3 | EBI-722671, EBI-310749 | |
BINARY | O15062 | ZBTB7B O15156 | 3 | EBI-722671, EBI-740434 | |
BINARY | O15062 | ZBTB7B O15156-2 | 3 | EBI-722671, EBI-11522250 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 24-93 | BTB | ||||
Sequence: CDCVIVVGNRHFKAHRSVLAACSTHFRALFSVAEGDQTMNMIQLDSEVVTAEAFAALIDMMYTSTLMLGE | ||||||
Compositional bias | 158-181 | Polar residues | ||||
Sequence: LNSSQNGEEQPAPMSSSMRSNLDQ | ||||||
Region | 158-252 | Disordered | ||||
Sequence: LNSSQNGEEQPAPMSSSMRSNLDQRTPFPMRRLHKRKQSAEERARQRLRPSIDESAISDVTPENGPSGVHSREEFFSPDSLKIVDNPKADGMTDN | ||||||
Compositional bias | 191-209 | Basic and acidic residues | ||||
Sequence: HKRKQSAEERARQRLRPSI | ||||||
Compositional bias | 287-308 | Polar residues | ||||
Sequence: SMASRATQVETSFDQEAAPEKS | ||||||
Region | 287-312 | Disordered | ||||
Sequence: SMASRATQVETSFDQEAAPEKSSFQC | ||||||
Region | 331-387 | Disordered | ||||
Sequence: SEPLSSPEPQDEVSDVTSQAEGSESVEVEGVVVSAEKIDLSPESSDRSFSDPQSSTD | ||||||
Compositional bias | 337-354 | Polar residues | ||||
Sequence: PEPQDEVSDVTSQAEGSE | ||||||
Region | 447-474 | Disordered | ||||
Sequence: LLSPEAGPAGGPSSAPGSHVENPFSEPA | ||||||
Compositional bias | 552-584 | Polar residues | ||||
Sequence: QIPENSTSSQLMMNGATSSFENGHPSQPGPPQL | ||||||
Region | 552-585 | Disordered | ||||
Sequence: QIPENSTSSQLMMNGATSSFENGHPSQPGPPQLT | ||||||
Zinc finger | 613-635 | C2H2-type 1 | ||||
Sequence: YACKICCKTFLTLTDCKKHIRVH | ||||||
Zinc finger | 641-664 | C2H2-type 2; atypical | ||||
Sequence: YACLKCGKRFSQSSHLYKHSKTTC |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length677
- Mass (Da)74,278
- Last updated1998-01-01 v1
- Checksum0F17A0AEE3FD827B
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 158-181 | Polar residues | ||||
Sequence: LNSSQNGEEQPAPMSSSMRSNLDQ | ||||||
Compositional bias | 191-209 | Basic and acidic residues | ||||
Sequence: HKRKQSAEERARQRLRPSI | ||||||
Compositional bias | 287-308 | Polar residues | ||||
Sequence: SMASRATQVETSFDQEAAPEKS | ||||||
Compositional bias | 337-354 | Polar residues | ||||
Sequence: PEPQDEVSDVTSQAEGSE | ||||||
Compositional bias | 552-584 | Polar residues | ||||
Sequence: QIPENSTSSQLMMNGATSSFENGHPSQPGPPQL |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB002352 EMBL· GenBank· DDBJ | BAA20811.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC010007 EMBL· GenBank· DDBJ | AAH10007.1 EMBL· GenBank· DDBJ | mRNA |