Q9UQR1 · ZN148_HUMAN
- ProteinZinc finger protein 148
- GeneZNF148
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids794 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in transcriptional regulation. Represses the transcription of a number of genes including gastrin, stromelysin and enolase. Binds to the G-rich box in the enhancer region of these genes.
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 | Golgi apparatus | |
Cellular Component | nucleoplasm | |
Molecular Function | DNA-binding transcription factor activity | |
Molecular Function | DNA-binding transcription repressor activity, RNA polymerase II-specific | |
Molecular Function | metal ion binding | |
Molecular Function | RNA polymerase II cis-regulatory region sequence-specific DNA binding | |
Molecular Function | sequence-specific DNA binding | |
Biological Process | cellular defense response | |
Biological Process | gamete generation | |
Biological Process | negative regulation of DNA-templated transcription | |
Biological Process | negative regulation of gene expression | |
Biological Process | negative regulation of transcription by RNA polymerase II | |
Biological Process | positive regulation of transcription by RNA polymerase II | |
Biological Process | regulation of transcription by RNA polymerase II | |
Biological Process | substantia nigra development |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameZinc finger protein 148
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9UQR1
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Global developmental delay, absent or hypoplastic corpus callosum, and dysmorphic facies (GDACCF)
- Note
- DescriptionAn autosomal dominant syndrome characterized by underdevelopment of the corpus callosum, mild to moderate developmental delay and intellectual disability, variable microcephaly or mild macrocephaly, short stature, feeding problems, facial dysmorphisms, and cardiac and renal malformations.
- See alsoMIM:617260
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 792 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, cross-link, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000047427 | 1-794 | UniProt | Zinc finger protein 148 | |||
Sequence: MNIDDKLEGLFLKCGGIDEMQSSRTMVVMGGVSGQSTVSGELQDSVLQDRSMPHQEILAADEVLQESEMRQQDMISHDELMVHEETVKNDEEQMETHERLPQGLQYALNVPISVKQEITFTDVSEQLMRDKKQIREPVDLQKKKKRKQRSPAKILTINEDGSLGLKTPKSHVCEHCNAAFRTNYHLQRHVFIHTGEKPFQCSQCDMRFIQKYLLQRHEKIHTGEKPFRCDECGMRFIQKYHMERHKRTHSGEKPYQCEYCLQYFSRTDRVLKHKRMCHENHDKKLNRCAIKGGLLTSEEDSGFSTSPKDNSLPKKKRQKTEKKSSGMDKESALDKSDLKKDKNDYLPLYSSSTKVKDEYMVAEYAVEMPHSSVGGSHLEDASGEIHPPKLVLKKINSKRSLKQPLEQNQTISPLSTYEESKVSKYAFELVDKQALLDSEGNADIDQVDNLQEGPSKPVHSSTNYDDAMQFLKKKRYLQAASNNSREYALNVGTIASQPSVTQAAVASVIDESTTASILESQALNVEIKSNHDKNVIPDEVLQTLLDHYSHKANGQHEISFSVADTEVTSSISINSSEVPEVTPSENVGSSSQASSSDKANMLQEYSKFLQQALDRTSQNDAYLNSPSLNFVTDNQTLPNQPAFSSIDKQVYATMPINSFRSGMNSPLRTTPDKSHFGLIVGDSQHSFPFSGDETNHASATSTQDFLDQVTSQKKAEAQPVHQAYQMSSFEQPFRAPYHGSRAGIATQFSTANGQVNLRGPGTSAEFSEFPLVNVNDNRAGMTSSPDATTGQTFG | |||||||
Cross-link | 6 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 51 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 88 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 115 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 132 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 194 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 194 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 250 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 250 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 291 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 296 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 297 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 301 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 301 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 304 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 305 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 306 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 306 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 308 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 311 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 336 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 356 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate | ||||
Sequence: K | |||||||
Cross-link | 356 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 400 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 402 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 412 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 412 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 415 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 421 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 424 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 438 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 607 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 661 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 665 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 665 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 669 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 670 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 728 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 782 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 783 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 784 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 784 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 788 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Sumoylated with SUMO2. Desumoylated by SENP3, resulting in the stimulation of transcription of its target genes (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with HNRNPDL (PubMed:15190078).
Interacts with the 5FMC complex; the interaction requires association with CHTOP. Interacts with CAVIN1 (By similarity).
Interacts with the 5FMC complex; the interaction requires association with CHTOP. Interacts with CAVIN1 (By similarity).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for zinc finger, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 171-193 | C2H2-type 1 | ||||
Sequence: HVCEHCNAAFRTNYHLQRHVFIH | ||||||
Zinc finger | 199-221 | C2H2-type 2 | ||||
Sequence: FQCSQCDMRFIQKYLLQRHEKIH | ||||||
Zinc finger | 227-249 | C2H2-type 3 | ||||
Sequence: FRCDECGMRFIQKYHMERHKRTH | ||||||
Zinc finger | 255-278 | C2H2-type 4 | ||||
Sequence: YQCEYCLQYFSRTDRVLKHKRMCH | ||||||
Region | 298-336 | Disordered | ||||
Sequence: EEDSGFSTSPKDNSLPKKKRQKTEKKSSGMDKESALDKS | ||||||
Compositional bias | 310-336 | Basic and acidic residues | ||||
Sequence: NSLPKKKRQKTEKKSSGMDKESALDKS | ||||||
Region | 574-596 | Disordered | ||||
Sequence: NSSEVPEVTPSENVGSSSQASSS |
Sequence similarities
Belongs to the krueppel C2H2-type zinc-finger protein family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9UQR1-1
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
- Length794
- Mass (Da)88,976
- Last updated2001-01-24 v2
- Checksum50413723459EBD1F
Q9UQR1-2
- Name2
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_055938 | 1-205 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_055939 | 233-690 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 287 | in Ref. 2; CAA15422 | ||||
Sequence: R → T | ||||||
Compositional bias | 310-336 | Basic and acidic residues | ||||
Sequence: NSLPKKKRQKTEKKSSGMDKESALDKS | ||||||
Sequence conflict | 348 | in Ref. 2; CAA15422 | ||||
Sequence: L → V | ||||||
Sequence conflict | 379 | in Ref. 6; AAB57692 | ||||
Sequence: E → K | ||||||
Sequence conflict | 495 | in Ref. 2; CAA15422 | ||||
Sequence: A → R | ||||||
Sequence conflict | 616 | in Ref. 6; AAB57692 | ||||
Sequence: T → N |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF039019 EMBL· GenBank· DDBJ | AAC39926.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ236885 EMBL· GenBank· DDBJ | CAA15422.1 EMBL· GenBank· DDBJ | mRNA | ||
AC108688 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471052 EMBL· GenBank· DDBJ | EAW79394.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471052 EMBL· GenBank· DDBJ | EAW79395.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471052 EMBL· GenBank· DDBJ | EAW79396.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471052 EMBL· GenBank· DDBJ | EAW79398.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC018971 EMBL· GenBank· DDBJ | AAH18971.1 EMBL· GenBank· DDBJ | mRNA | ||
BC050260 EMBL· GenBank· DDBJ | AAH50260.1 EMBL· GenBank· DDBJ | mRNA | ||
U96633 EMBL· GenBank· DDBJ | AAB57692.1 EMBL· GenBank· DDBJ | Genomic DNA |