P17028 · ZNF24_HUMAN

  • Protein
    Zinc finger protein 24
  • Gene
    ZNF24
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Transcription factor required for myelination of differentiated oligodendrocytes. Required for the conversion of oligodendrocytes from the premyelinating to the myelinating state. In the developing central nervous system (CNS), involved in the maintenance in the progenitor stage by promoting the cell cycle. Specifically binds to the 5'-TCAT-3' DNA sequence (By similarity).
Has transcription repressor activity in vitro

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 Componentnucleoplasm
Cellular Componentnucleus
Molecular FunctionDNA-binding transcription activator activity, RNA polymerase II-specific
Molecular FunctionDNA-binding transcription factor activity, RNA polymerase II-specific
Molecular Functionidentical protein binding
Molecular Functionmetal ion binding
Molecular FunctionRNA polymerase II cis-regulatory region sequence-specific DNA binding
Molecular Functionsequence-specific DNA binding
Biological Processmyelination
Biological Processnegative regulation of DNA-templated transcription
Biological Processpositive regulation of transcription by RNA polymerase II
Biological Processregulation of transcription by RNA polymerase II

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Zinc finger protein 24
  • Alternative names
    • Retinoic acid suppression protein A (RSG-A)
    • Zinc finger and SCAN domain-containing protein 3
    • Zinc finger protein 191
    • Zinc finger protein KOX17

Gene names

    • Name
      ZNF24
    • Synonyms
      KOX17, ZNF191, ZSCAN3

Organism names

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

Accessions

  • Primary accession
    P17028
  • Secondary accessions
    • O14754
    • Q53YE4
    • Q6ICR5
    • Q8IZN4

Proteomes

Organism-specific databases

Subcellular Location

Nucleus

Keywords

Disease & Variants

Features

Showing features for natural variant, mutagenesis.

TypeIDPosition(s)Description
Natural variantVAR_012017220in dbSNP:rs2032729
Mutagenesis286Partial cytoplasmic accumulation.
Mutagenesis290Partial cytoplasmic accumulation.
Natural variantVAR_012018331in dbSNP:rs3568

Variants

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

The viewer provides 348 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, modified residue.

TypeIDPosition(s)SourceDescription
ChainPRO_00000473521-368UniProtZinc finger protein 24
Modified residue (large scale data)2PRIDEPhosphoserine
Modified residue (large scale data)5PRIDEPhosphoserine
Modified residue (large scale data)10PRIDEPhosphoserine
Cross-link22UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link27UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate
Cross-link27UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Modified residue (large scale data)38PRIDEPhosphoserine
Modified residue (large scale data)39PRIDEPhosphoserine
Modified residue (large scale data)63PRIDEPhosphoserine
Modified residue132UniProtPhosphoserine
Modified residue (large scale data)132PRIDEPhosphoserine
Modified residue142UniProtPhosphoserine
Modified residue (large scale data)142PRIDEPhosphoserine
Cross-link147UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)167PRIDEPhosphoserine
Cross-link177UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link236UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue274UniProtPhosphoserine
Modified residue (large scale data)274PRIDEPhosphoserine
Cross-link277UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)279PRIDEPhosphotyrosine
Cross-link286UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue292UniProtPhosphoserine
Modified residue (large scale data)292PRIDEPhosphoserine
Modified residue (large scale data)330PRIDEPhosphothreonine
Modified residue335UniProtPhosphotyrosine
Modified residue (large scale data)335PRIDEPhosphotyrosine
Cross-link361UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link367UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)

Post-translational modification

Sumoylated.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in many tissues except in heart.

Gene expression databases

Organism-specific databases

Interaction

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P17028AKT1 P317493EBI-707773, EBI-296087
BINARY P17028APLP1 P516932EBI-707773, EBI-74648
BINARY P17028APOE P026493EBI-707773, EBI-1222467
BINARY P17028APP P050673EBI-707773, EBI-77613
BINARY P17028DDX6 P261963EBI-707773, EBI-351257
BINARY P17028DMWD G5E9A73EBI-707773, EBI-10976677
BINARY P17028DZIP3 Q86Y135EBI-707773, EBI-948630
BINARY P17028FAM161A Q3B8203EBI-707773, EBI-719941
BINARY P17028LMO1 P258005EBI-707773, EBI-8639312
BINARY P17028LMO2 P257914EBI-707773, EBI-739696
BINARY P17028LMO2 P25791-33EBI-707773, EBI-11959475
BINARY P17028MAP1LC3C Q9BXW43EBI-707773, EBI-2603996
BINARY P17028MID2 Q9UJV3-23EBI-707773, EBI-10172526
BINARY P17028NEK6 Q9HC98-43EBI-707773, EBI-11750983
BINARY P17028PGBD1 Q96JS39EBI-707773, EBI-10290053
BINARY P17028PRPF31 Q8WWY33EBI-707773, EBI-1567797
BINARY P17028S100B P042713EBI-707773, EBI-458391
BINARY P17028SCAND1 P570868EBI-707773, EBI-745846
BINARY P17028SPRED1 Q7Z6993EBI-707773, EBI-5235340
BINARY P17028SQSTM1 Q135013EBI-707773, EBI-307104
BINARY P17028SYK P43405-23EBI-707773, EBI-25892332
BINARY P17028TCAF1 Q9Y4C23EBI-707773, EBI-750484
BINARY P17028UBE2I Q7KZS03EBI-707773, EBI-10180829
BINARY P17028YJU2B P139947EBI-707773, EBI-716093
BINARY P17028ZGPAT Q8N5A5-23EBI-707773, EBI-10183064
BINARY P17028ZKSCAN4 Q969J27EBI-707773, EBI-2818641
BINARY P17028ZNF165 P499103EBI-707773, EBI-741694
BINARY P17028ZNF174 Q15697-24EBI-707773, EBI-11158827
BINARY P17028ZNF232 Q9UNY54EBI-707773, EBI-749023
BINARY P17028ZNF24 P170284EBI-707773, EBI-707773
BINARY P17028ZNF396 Q96N95-35EBI-707773, EBI-12328453
BINARY P17028ZNF410 Q86VK4-33EBI-707773, EBI-11741890
BINARY P17028ZNF444 Q8N0Y2-26EBI-707773, EBI-12010736
BINARY P17028ZNF446 Q9NWS97EBI-707773, EBI-3925851
BINARY P17028ZNF446 Q9NWS9-213EBI-707773, EBI-740232
BINARY P17028ZNF483 Q6P0883EBI-707773, EBI-10196963
BINARY P17028ZNF620 Q6ZNG03EBI-707773, EBI-4395669
BINARY P17028ZSCAN12 O433093EBI-707773, EBI-1210440
BINARY P17028ZSCAN16 Q9H4T23EBI-707773, EBI-723596
BINARY P17028ZSCAN21 Q9Y5A68EBI-707773, EBI-10281938
BINARY P17028ZSCAN22 P100736EBI-707773, EBI-10178224
BINARY P17028ZSCAN23 Q3MJ624EBI-707773, EBI-5667532
BINARY P17028ZSCAN32 Q9NX6511EBI-707773, EBI-739949

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for domain, zinc finger, region.

TypeIDPosition(s)Description
Domain52-134SCAN box
Zinc finger251-273C2H2-type 1
Region251-301Necessary and sufficient for nuclear localization
Zinc finger279-301C2H2-type 2
Zinc finger307-329C2H2-type 3
Zinc finger335-357C2H2-type 4

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.

P17028-1

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
    368
  • Mass (Da)
    42,155
  • Last updated
    2007-10-23 v4
  • Checksum
    B890EDC512493E0E
MSAQSVEEDSILIIPTPDEEEKILRVKLEEDPDGEEGSSIPWNHLPDPEIFRQRFRQFGYQDSPGPREAVSQLRELCRLWLRPETHTKEQILELVVLEQFVAILPKELQTWVRDHHPENGEEAVTVLEDLESELDDPGQPVSLRRRKREVLVEDMVSQEEAQGLPSSELDAVENQLKWASWELHSLRHCDDDGRTENGALAPKQELPSALESHEVPGTLNMGVPQIFKYGETCFPKGRFERKRNPSRKKQHICDECGKHFSQGSALILHQRIHSGEKPYGCVECGKAFSRSSILVQHQRVHTGEKPYKCLECGKAFSQNSGLINHQRIHTGEKPYECVQCGKSYSQSSNLFRHQRRHNAEKLLNVVKV

P17028-2

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
K7EPL1K7EPL1_HUMANZNF24138
K7EQP8K7EQP8_HUMANZNF2496
K7EPZ8K7EPZ8_HUMANZNF24102

Features

Showing features for alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Alternative sequenceVSP_039219190-193in isoform 2
Alternative sequenceVSP_039220194-368in isoform 2
Sequence conflict367in Ref. 1; AAB37275 and 4; CAG29324

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U68536
EMBL· GenBank· DDBJ
AAB37275.1
EMBL· GenBank· DDBJ
mRNA
AF016052
EMBL· GenBank· DDBJ
AAB70216.1
EMBL· GenBank· DDBJ
Genomic DNA
AF542097
EMBL· GenBank· DDBJ
AAN40767.1
EMBL· GenBank· DDBJ
mRNA
AF038964
EMBL· GenBank· DDBJ
AAD19827.1
EMBL· GenBank· DDBJ
mRNA
AK291246
EMBL· GenBank· DDBJ
BAF83935.1
EMBL· GenBank· DDBJ
mRNA
BT006658
EMBL· GenBank· DDBJ
AAP35304.1
EMBL· GenBank· DDBJ
mRNA
CR450328
EMBL· GenBank· DDBJ
CAG29324.1
EMBL· GenBank· DDBJ
mRNA
AC116447
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH471088
EMBL· GenBank· DDBJ
EAX01348.1
EMBL· GenBank· DDBJ
Genomic DNA
CH471088
EMBL· GenBank· DDBJ
EAX01349.1
EMBL· GenBank· DDBJ
Genomic DNA
BC003566
EMBL· GenBank· DDBJ
AAH03566.1
EMBL· GenBank· DDBJ
mRNA
BC016801
EMBL· GenBank· DDBJ
AAH16801.1
EMBL· GenBank· DDBJ
mRNA
X52348
EMBL· GenBank· DDBJ
CAA36574.1
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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp