Q9UQR1 · ZN148_HUMAN

  • Protein
    Zinc finger protein 148
  • Gene
    ZNF148
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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 annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular ComponentGolgi apparatus
Cellular Componentnucleoplasm
Molecular FunctionDNA-binding transcription factor activity
Molecular FunctionDNA-binding transcription repressor activity, RNA polymerase II-specific
Molecular Functionmetal ion binding
Molecular FunctionRNA polymerase II cis-regulatory region sequence-specific DNA binding
Molecular Functionsequence-specific DNA binding
Biological Processcellular defense response
Biological Processgamete generation
Biological Processnegative regulation of DNA-templated transcription
Biological Processnegative regulation of gene expression
Biological Processnegative regulation of transcription by RNA polymerase II
Biological Processpositive regulation of transcription by RNA polymerase II
Biological Processregulation of transcription by RNA polymerase II
Biological Processsubstantia nigra development

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Zinc finger protein 148
  • Alternative names
    • Transcription factor ZBP-89
    • Zinc finger DNA-binding protein 89

Gene names

    • Name
      ZNF148
    • Synonyms
      ZBP89

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q9UQR1
  • Secondary accessions
    • D3DN27
    • O00389
    • O43591
    • Q58EY5
    • Q6PJ98

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Disease & Variants

Involvement in disease

Global developmental delay, absent or hypoplastic corpus callosum, and dysmorphic facies (GDACCF)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    An 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 also
    MIM: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.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain, cross-link, modified residue, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
ChainPRO_00000474271-794UniProtZinc finger protein 148
Cross-link6UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue51UniProtPhosphoserine
Cross-link88UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link115UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link132UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue194UniProtPhosphothreonine
Modified residue (large scale data)194PRIDEPhosphothreonine
Modified residue250UniProtPhosphoserine
Modified residue (large scale data)250PRIDEPhosphoserine
Cross-link291UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)296PRIDEPhosphothreonine
Modified residue (large scale data)297PRIDEPhosphoserine
Modified residue301UniProtPhosphoserine
Modified residue (large scale data)301PRIDEPhosphoserine
Modified residue (large scale data)304PRIDEPhosphoserine
Modified residue (large scale data)305PRIDEPhosphothreonine
Modified residue306UniProtPhosphoserine
Modified residue (large scale data)306PRIDEPhosphoserine
Cross-link308UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)311PRIDEPhosphoserine
Modified residue (large scale data)336PRIDEPhosphoserine
Cross-link356UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate
Cross-link356UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Modified residue (large scale data)400PRIDEPhosphoserine
Cross-link402UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue412UniProtPhosphoserine
Modified residue (large scale data)412PRIDEPhosphoserine
Modified residue (large scale data)415PRIDEPhosphoserine
Cross-link421UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link424UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)438PRIDEPhosphoserine
Modified residue607UniProtN6-acetyllysine
Modified residue (large scale data)661PRIDEPhosphoserine
Modified residue665UniProtPhosphoserine
Modified residue (large scale data)665PRIDEPhosphoserine
Modified residue (large scale data)669PRIDEPhosphothreonine
Modified residue (large scale data)670PRIDEPhosphothreonine
Modified residue (large scale data)728PRIDEPhosphoserine
Modified residue (large scale data)782PRIDEPhosphothreonine
Modified residue (large scale data)783PRIDEPhosphoserine
Modified residue784UniProtPhosphoserine
Modified residue (large scale data)784PRIDEPhosphoserine
Modified residue (large scale data)788PRIDEPhosphothreonine

Post-translational modification

Sumoylated with SUMO2. Desumoylated by SENP3, resulting in the stimulation of transcription of its target genes (By similarity).

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with HNRNPDL (PubMed:15190078).
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.

TypeIDPosition(s)Description
Zinc finger171-193C2H2-type 1
Zinc finger199-221C2H2-type 2
Zinc finger227-249C2H2-type 3
Zinc finger255-278C2H2-type 4
Region298-336Disordered
Compositional bias310-336Basic and acidic residues
Region574-596Disordered

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

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.

  • Length
    794
  • Mass (Da)
    88,976
  • Last updated
    2001-01-24 v2
  • Checksum
    50413723459EBD1F
MNIDDKLEGLFLKCGGIDEMQSSRTMVVMGGVSGQSTVSGELQDSVLQDRSMPHQEILAADEVLQESEMRQQDMISHDELMVHEETVKNDEEQMETHERLPQGLQYALNVPISVKQEITFTDVSEQLMRDKKQIREPVDLQKKKKRKQRSPAKILTINEDGSLGLKTPKSHVCEHCNAAFRTNYHLQRHVFIHTGEKPFQCSQCDMRFIQKYLLQRHEKIHTGEKPFRCDECGMRFIQKYHMERHKRTHSGEKPYQCEYCLQYFSRTDRVLKHKRMCHENHDKKLNRCAIKGGLLTSEEDSGFSTSPKDNSLPKKKRQKTEKKSSGMDKESALDKSDLKKDKNDYLPLYSSSTKVKDEYMVAEYAVEMPHSSVGGSHLEDASGEIHPPKLVLKKINSKRSLKQPLEQNQTISPLSTYEESKVSKYAFELVDKQALLDSEGNADIDQVDNLQEGPSKPVHSSTNYDDAMQFLKKKRYLQAASNNSREYALNVGTIASQPSVTQAAVASVIDESTTASILESQALNVEIKSNHDKNVIPDEVLQTLLDHYSHKANGQHEISFSVADTEVTSSISINSSEVPEVTPSENVGSSSQASSSDKANMLQEYSKFLQQALDRTSQNDAYLNSPSLNFVTDNQTLPNQPAFSSIDKQVYATMPINSFRSGMNSPLRTTPDKSHFGLIVGDSQHSFPFSGDETNHASATSTQDFLDQVTSQKKAEAQPVHQAYQMSSFEQPFRAPYHGSRAGIATQFSTANGQVNLRGPGTSAEFSEFPLVNVNDNRAGMTSSPDATTGQTFG

Q9UQR1-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
C9J6Y6C9J6Y6_HUMANZNF14883
C9K0U4C9K0U4_HUMANZNF14875
C9JRX0C9JRX0_HUMANZNF14825
G5E9X2G5E9X2_HUMANZNF148144

Features

Showing features for alternative sequence, sequence conflict, compositional bias.

TypeIDPosition(s)Description
Alternative sequenceVSP_0559381-205in isoform 2
Alternative sequenceVSP_055939233-690in isoform 2
Sequence conflict287in Ref. 2; CAA15422
Compositional bias310-336Basic and acidic residues
Sequence conflict348in Ref. 2; CAA15422
Sequence conflict379in Ref. 6; AAB57692
Sequence conflict495in Ref. 2; CAA15422
Sequence conflict616in Ref. 6; AAB57692

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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