Q8N7M2 · ZN283_HUMAN

  • Protein
    Zinc finger protein 283
  • Gene
    ZNF283
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

May be involved in transcriptional regulation.

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 Componentnucleus
Molecular FunctionDNA-binding transcription factor activity, RNA polymerase II-specific
Molecular Functionmetal ion binding
Molecular FunctionRNA polymerase II cis-regulatory region sequence-specific DNA binding
Biological Processregulation of transcription by RNA polymerase II

Keywords

Enzyme and pathway databases

Community curation (1)

Community annotation

The subsequence EESHGALISSCNSRTMTDGLVTFRDVAIDFSQEEWECLDPAQRDLYVDVMLENYSNLVSLDLESKTYETKKIFSENDIFE, which contains the KRAB domain, shows transcriptional repressor activity in a high-throughput recruitment assay.

SourceSubmission dateContributor
PubMed:333267460000-0002-4108-0575

Names & Taxonomy

Protein names

  • Recommended name
    Zinc finger protein 283
  • Alternative names
    • Zinc finger protein HZF19

Gene names

    • Name
      ZNF283

Organism names

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

Accessions

  • Primary accession
    Q8N7M2
  • Secondary accessions
    • B4DGZ5
    • B7WP04
    • Q6RFR9
    • Q86WM6

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_060605314in dbSNP:rs2195980
Natural variantVAR_057416629in dbSNP:rs1061768
Natural variantVAR_060606638in dbSNP:rs2356437
Natural variantVAR_060607638in dbSNP:rs1061769
Natural variantVAR_057417646in dbSNP:rs10417624

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 851 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

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

Type
IDPosition(s)Source
Description
ChainPRO_00000475071-679UniProtZinc finger protein 283
Modified residue (large scale data)145PTMeXchangeSumoylated lysine
Modified residue (large scale data)168PTMeXchangeSumoylated lysine
Modified residue (large scale data)192PTMeXchangeSumoylated lysine
Modified residue (large scale data)221PTMeXchangeSumoylated lysine
Cross-link280UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)280PTMeXchangeSumoylated lysine
Modified residue (large scale data)289PTMeXchangeSumoylated lysine
Modified residue (large scale data)298PTMeXchangeSumoylated lysine
Modified residue (large scale data)345PTMeXchangeSumoylated lysine
Modified residue (large scale data)354PTMeXchangeSumoylated lysine
Modified residue (large scale data)378PTMeXchangeSumoylated lysine
Modified residue (large scale data)429PTMeXchangeSumoylated lysine
Modified residue (large scale data)438PTMeXchangeSumoylated lysine
Modified residue (large scale data)457PTMeXchangeSumoylated lysine
Cross-link476UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)476PTMeXchangeSumoylated lysine
Modified residue (large scale data)541PTMeXchangeSumoylated lysine
Modified residue (large scale data)550PTMeXchangeSumoylated lysine
Cross-link588UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)588PTMeXchangeSumoylated lysine
Modified residue (large scale data)625PTMeXchangeSumoylated lysine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Detected in prostate, testis, and pancreas.

Gene expression databases

Organism-specific databases

Interaction

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain, zinc finger.

Type
IDPosition(s)Description
Domain73-152KRAB
Zinc finger205-227C2H2-type 1
Zinc finger233-255C2H2-type 2
Zinc finger261-283C2H2-type 3
Zinc finger289-311C2H2-type 4
Zinc finger317-339C2H2-type 5
Zinc finger345-367C2H2-type 6
Zinc finger373-395C2H2-type 7
Zinc finger401-423C2H2-type 8
Zinc finger429-451C2H2-type 9
Zinc finger457-479C2H2-type 10
Zinc finger485-507C2H2-type 11
Zinc finger513-535C2H2-type 12
Zinc finger541-563C2H2-type 13
Zinc finger569-591C2H2-type 14
Zinc finger597-619C2H2-type 15

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    679
  • Mass (Da)
    77,942
  • Last updated
    2009-11-24 v4
  • MD5 Checksum
    2063BD88040DC1AAADDBADE7FBBA7F03
MESRSVAQAGVQWCDLGSLQAPPPGFTLFSCLSLLSSWDYSSGFSGFCASPIEESHGALISSCNSRTMTDGLVTFRDVAIDFSQEEWECLDPAQRDLYVDVMLENYSNLVSLDLESKTYETKKIFSENDIFEINFSQWEMKDKSKTLGLEASIFRNNWKCKSIFEGLKGHQEGYFSQMIISYEKIPSYRKSKSLTPHQRIHNTEKSYVCKECGKACSHGSKLVQHERTHTAEKHFECKECGKNYLSAYQLNVHQRFHTGEKPYECKECGKTFSWGSSLVKHERIHTGEKPYECKECGKAFSRGYHLTQHQKIHTGVKSYKCKECGKAFFWGSSLAKHEIIHTGEKPYKCKECGKAFSRGYQLTQHQKIHTGKKPYECKICGKAFCWGYQLTRHQIFHTGEKPYECKECGKAFNCGSSLIQHERIHTGEKPYECKECGKAFSRGYHLSQHQKIHTGEKPFECKECGKAFSWGSSLVKHERVHTGEKSHECKECGKTFCSGYQLTRHQVFHTGEKPYECKECGKAFNCGSSLVQHERIHTGEKPYECKECGKAFSRGYHLTQHQKIHTGEKPFKCKECGKAFSWGSSLVKHERVHTNEKSYECKDCGKAFGSGYQLSVHQRFHTGEKLYQRKEFGKTFTCGSKLVHERTHSNDKPYKYNECGEAFLWTTYSNEKIDTDETL

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
Q4G0N1Q4G0N1_HUMANZNF28383
A0A494C0U8A0A494C0U8_HUMANZNF283643
K7EL69K7EL69_HUMANZNF28345
K7ESH0K7ESH0_HUMANZNF28354

Sequence caution

The sequence BAC05251.1 differs from that shown. Reason: Miscellaneous discrepancy Compared to the genome, the sequence lacks 6 bp for unexplained reasons.

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict139-140in Ref. 1; BAG57956
Sequence conflict172in Ref. 4; AAS55109
Sequence conflict432in Ref. 4; AAS55109
Sequence conflict638in Ref. 1; BAC05251/BAG57956 and 4; AAS55109

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK098175
EMBL· GenBank· DDBJ
BAC05251.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.
AK294852
EMBL· GenBank· DDBJ
BAG57956.1
EMBL· GenBank· DDBJ
mRNA
AC011508
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AY166784
EMBL· GenBank· DDBJ
AAO45833.1
EMBL· GenBank· DDBJ
mRNA
AY500359
EMBL· GenBank· DDBJ
AAS55109.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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