O95785 · WIZ_HUMAN

  • Protein
    Protein Wiz
  • Gene
    WIZ
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

May link EHMT1 and EHMT2 histone methyltransferases to the CTBP corepressor machinery. May be involved in EHMT1-EHMT2 heterodimer formation and stabilization (By similarity).

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 Componentextracellular exosome
Cellular Componentmidbody
Cellular Componentnucleoplasm
Cellular Componentnucleus
Molecular FunctionDNA-binding transcription factor activity, RNA polymerase II-specific
Molecular Functionhistone methyltransferase binding
Molecular Functionmetal ion binding
Molecular Functionprotein-containing complex binding
Molecular FunctionRNA polymerase II cis-regulatory region sequence-specific DNA binding
Molecular Functiontranscription corepressor binding
Biological Processpositive regulation of nuclear cell cycle DNA replication
Biological Processprotein stabilization
Biological Processregulation of transcription by RNA polymerase II

Keywords

Enzyme and pathway databases

Community curation (1)

The subsequence LQQKLEEVRQPPPRVRPVPSLVPRPPQTSLVKFVGNIYTLKCRFCEVEFQGPLSIQEEWVRHLQRHILEMNFSKADPPPE shows transcriptional repressor activity in a high-throughput recruitment assay.

Names & Taxonomy

Protein names

  • Recommended name
    Protein Wiz
  • Alternative names
    • Widely-interspaced zinc finger-containing protein
    • Zinc finger protein 803

Gene names

    • Name
      WIZ
    • Synonyms
      ZNF803
Community curation (1)

Organism names

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

Accessions

  • Primary accession
    O95785
  • Secondary accessions
    • B3KVH1
    • B7ZM82
    • M0QY21
    • Q4G0E0
    • Q6P6B0

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Disease & Variants

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

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

TypeIDPosition(s)SourceDescription
ChainPRO_00002860541-1651UniProtProtein Wiz
Cross-link11UniProtIn isoform O95785-3; Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link14UniProtIn isoform O95785-4; Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link29UniProtIn isoform O95785-3; Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link32UniProtIn isoform O95785-4; Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link39UniProtIn isoform O95785-3; Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link42UniProtIn isoform O95785-4; Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link258UniProtIn isoform O95785-3; Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link313UniProtIn isoform O95785-3; Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link883UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link939UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link955UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link967UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)968PRIDEPhosphoserine
Modified residue (large scale data)982PRIDEPhosphoserine
Modified residue (large scale data)983PRIDEPhosphoserine
Cross-link988UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)989PRIDEPhosphothreonine
Modified residue996UniProtPhosphoserine
Modified residue (large scale data)996PRIDEPhosphoserine
Modified residue998UniProtPhosphothreonine
Modified residue (large scale data)998PRIDEPhosphothreonine
Cross-link1000UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link1005UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue1006UniProtPhosphoserine
Modified residue (large scale data)1006PRIDEPhosphoserine
Modified residue (large scale data)1010PRIDEPhosphoserine
Modified residue1012UniProtPhosphoserine
Modified residue (large scale data)1012PRIDEPhosphoserine
Modified residue1017UniProtPhosphoserine
Modified residue (large scale data)1017PRIDEPhosphoserine
Modified residue1025UniProtPhosphoserine
Modified residue (large scale data)1025PRIDEPhosphoserine
Cross-link1056UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue1079UniProtPhosphoserine
Modified residue (large scale data)1079PRIDEPhosphoserine
Modified residue1106UniProtPhosphoserine
Modified residue (large scale data)1106PRIDEPhosphoserine
Cross-link1108UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link1112UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)1121PRIDEPhosphoserine
Modified residue1122UniProtPhosphoserine
Modified residue (large scale data)1122PRIDEPhosphoserine
Modified residue1127UniProtPhosphoserine
Modified residue (large scale data)1127PRIDEPhosphoserine
Modified residue (large scale data)1129PRIDEPhosphoserine
Modified residue1134UniProtPhosphoserine
Modified residue (large scale data)1134PRIDEPhosphoserine
Cross-link1138UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link1139UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue1146UniProtPhosphoserine
Modified residue (large scale data)1146PRIDEPhosphoserine
Modified residue1151UniProtPhosphoserine
Modified residue (large scale data)1151PRIDEPhosphoserine
Modified residue (large scale data)1153PRIDEPhosphothreonine
Modified residue (large scale data)1155PRIDEPhosphoserine
Modified residue1162UniProtN6,N6,N6-trimethyllysine; by EHMT2; alternate
Modified residue1162UniProtN6,N6-dimethyllysine; by EHMT2; alternate
Cross-link1177UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)1218PRIDEPhosphoserine
Cross-link1240UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue1263UniProtPhosphoserine
Modified residue (large scale data)1263PRIDEPhosphoserine
Cross-link1282UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue1309UniProtPhosphoserine
Modified residue (large scale data)1309PRIDEPhosphoserine
Modified residue1314UniProtPhosphoserine
Modified residue (large scale data)1314PRIDEPhosphoserine
Modified residue (large scale data)1335PRIDEPhosphoserine
Modified residue (large scale data)1337PRIDEPhosphothreonine
Cross-link1343UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)1352PRIDEPhosphoserine
Cross-link1356UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link1370UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link1372UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link1382UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link1448UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link1464UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link1477UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue1480UniProtPhosphoserine
Modified residue (large scale data)1480PRIDEPhosphoserine
Modified residue1517UniProtPhosphoserine
Modified residue (large scale data)1517PRIDEPhosphoserine
Cross-link1523UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate
Cross-link1523UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Cross-link1534UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link1560UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)1629PRIDEPhosphoserine
Cross-link1630UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with EHMT1, EHMT2, CTBP1 and CTBP2 (By similarity).
Part of a complex containing at least CDYL, REST, WIZ, SETB1, EHMT1 and EHMT2

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, zinc finger, compositional bias.

TypeIDPosition(s)Description
Region1-79Disordered
Zinc finger267-289C2H2-type 1
Zinc finger304-326C2H2-type 2
Zinc finger353-375C2H2-type 3
Region376-399Disordered
Zinc finger416-439C2H2-type 4
Region546-578Disordered
Zinc finger701-723C2H2-type 5
Zinc finger769-791C2H2-type 6
Region819-843Disordered
Zinc finger870-892C2H2-type 7
Region972-1038Disordered
Compositional bias1001-1019Polar residues
Region1030-1034Interaction with CTBP1 and CTBP2 1
Zinc finger1043-1065C2H2-type 8
Region1091-1174Disordered
Compositional bias1137-1154Pro residues
Region1214-1218Interaction with CTBP1 and CTBP2 2
Zinc finger1227-1249C2H2-type 9
Region1283-1331Disordered
Compositional bias1303-1317Pro residues
Zinc finger1397-1419C2H2-type 10
Region1463-1554Disordered
Compositional bias1527-1543Basic and acidic residues
Zinc finger1596-1622C2H2-type 11
Region1629-1651Disordered

Domain

The C2H2-type zinc finger 11 mediates interaction with EHMT1 and EHMT2.

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (4)
  • Sequence status
    Complete

This entry describes 4 isoforms produced by Alternative splicing.

O95785-1

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
    1,651
  • Mass (Da)
    178,674
  • Last updated
    2007-05-01 v2
  • Checksum
    9DB0485964578310
MEGSLAGSLAAPDRPQGPERLPGPAPRENIEGGAEAAEGEGGIFRSTRYLPVTKEGPRDILDGRGGISGTPDGRGPWEHPLVQEAGEGILSERRFEDSVIVRTMKPHAELEGSRRFLHHRGEPRLLEKHAQGRPRFDWLQDEDEQGSPQDAGLHLDLPAQPPPLAPFRRVFVPVEDTPKTLDMAVVGGREDLEDLEGLAQPSEWGLPTSASEVATQTWTVNSEASVERLQPLLPPIRTGPYLCELLEEVAEGVASPDEDEDEEPAVFPCIECSIYFKQKEHLLEHMSQHRRAPGQEPPADLAPLACGECGWAFADPTALEQHRQLHQASREKIIEEIQKLKQVPGDEGREARLQCPKCVFGTNSSRAYVQHAKLHMREPPGQTTKEPFGGSSGAGSPSPEASALLYQPYGAAVGLSACVFCGFPAPSESLLREHVRLVHAHPHWEEDGEAYEEDPASQPGTSQDAHACFPDTAVDYFGKAEPSLAPMWRENPAGYDPSLAFGPGCQQLSIRDFPLSKPLLHGTGQRPLGRLAFPSTLASTPYSLQLGRNKSTVHPQGLGERRRPWSEEEEEEEEEEDVVLTSEMDFSPENGVFSPLATPSLIPQAALELKQAFREALQAVEATQGQQQQLRGMVPIVLVAKLGPQVMAAARVPPRLQPEELGLAGAHPLDFLLLDAPLGGPLGLDTLLDGDPAMALKHEERKCPYCPDRFHNGIGLANHVRGHLNRVGVSYNVRHFISAEEVKAIERRFSFQKKKKKVANFDPGTFSLMRCDFCGAGFDTRAGLSSHARAHLRDFGITNWELTVSPINILQELLATSAAEQPPSPLGREPGGPPGSFLTSRRPRLPLTVPFPPTWAEDPGPAYGDAQSLTTCEVCGACFETRKGLSSHARSHLRQLGVAESESSGAPIDLLYELVKQKGLPDAHLGLPPGLAKKSSSLKEVVAGAPRPGLLSLAKPLDAPAVNKAIKSPPGFSAKGLGHPPSSPLLKKTPLALAGSPTPKNPEDKSPQLSLSPRPASPKAQWPQSEDEGPLNLTSGPEPARDIRCEFCGEFFENRKGLSSHARSHLRQMGVTEWYVNGSPIDTLREILKRRTQSRPGGPPNPPGPSPKALAKMMGGAGPGSSLEARSPSDLHISPLAKKLPPPPGSPLGHSPTASPPPTARKMFPGLAAPSLPKKLKPEQIRVEIKREMLPGALHGELHPSEGPWGAPREDMTPLNLSSRAEPVRDIRCEFCGEFFENRKGLSSHARSHLRQMGVTEWSVNGSPIDTLREILKKKSKPCLIKKEPPAGDLAPALAEDGPPTVAPGPVQSPLPLSPLAGRPGKPGAGPAQVPRELSLTPITGAKPSATGYLGSVAAKRPLQEDRLLPAEVKAKTYIQTELPFKAKTLHEKTSHSSTEACCELCGLYFENRKALASHARAHLRQFGVTEWCVNGSPIETLSEWIKHRPQKVGAYRSYIQGGRPFTKKFRSAGHGRDSDKRPSLGLAPGGLAVVGRSAGGEPGPEAGRAADGGERPLAASPPGTVKAEEHQRQNINKFERRQARPPDASAARGGEDTNDLQQKLEEVRQPPPRVRPVPSLVPRPPQTSLVKFVGNIYTLKCRFCEVEFQGPLSIQEEWVRHLQRHILEMNFSKADPPPEESQAPQAQTAAAEAP

O95785-2

O95785-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-46: MEGSLAGSLAAPDRPQGPERLPGPAPRENIEGGAEAAEGEGGIFRS → MDLGSPSLPKKSLPVPGALEQVASRLSSKVAAEVPHGSKQELQDLK
    • 47-865: Missing
    • 1034-1034: T → TLDSDGGRELDCQLCGAWFETRKGLSSHARAHLRHLGVSDPDAKGSPIDVLHGLIRRDGVQIRLPPRRGALAHPGRPPPTSAALSLLPPPPPAKKAKLKAAGMASPWGKQDLSAAAAAGIFWASDVEPSPLNLS

O95785-4

  • Name
    4
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-49: MEGSLAGSLAAPDRPQGPERLPGPAPRENIEGGAEAAEGEGGIFRSTRY → MVAMDLGSPSLPKKSLPVPGALEQVASRLSSKVAAEVPHGSKQELQDLK
    • 50-865: Missing

Computationally mapped potential isoform sequences

There are 8 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A2R8YFV2A0A2R8YFV2_HUMANWIZ1699
M0QXA7M0QXA7_HUMANWIZ968
M0QXF8M0QXF8_HUMANWIZ133
A0A3B3IS05A0A3B3IS05_HUMANWIZ96
A0A669KBG4A0A669KBG4_HUMANWIZ933
A0A669KBH9A0A669KBH9_HUMANWIZ1066
A0A669KAV7A0A669KAV7_HUMANWIZ1889
B9EGQ5B9EGQ5_HUMANWIZ832

Sequence caution

The sequence BAB55234.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

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

TypeIDPosition(s)Description
Alternative sequenceVSP_0545091-46in isoform 3
Alternative sequenceVSP_0572071-49in isoform 4
Alternative sequenceVSP_05451047-865in isoform 3
Alternative sequenceVSP_05720850-865in isoform 4
Alternative sequenceVSP_02495169-757in isoform 2
Alternative sequenceVSP_024952867-1034in isoform 2
Compositional bias1001-1019Polar residues
Alternative sequenceVSP_0545111034in isoform 3
Compositional bias1137-1154Pro residues
Compositional bias1303-1317Pro residues
Sequence conflict1373in Ref. 2; BAD18551
Compositional bias1527-1543Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK027615
EMBL· GenBank· DDBJ
BAB55234.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK122890
EMBL· GenBank· DDBJ
BAG53783.1
EMBL· GenBank· DDBJ
mRNA
AK131404
EMBL· GenBank· DDBJ
BAD18551.1
EMBL· GenBank· DDBJ
mRNA
AC006128
EMBL· GenBank· DDBJ
AAC97985.1
EMBL· GenBank· DDBJ
Genomic DNA
AC007059
EMBL· GenBank· DDBJ
AAD19817.1
EMBL· GenBank· DDBJ
Genomic DNA
AC007059
EMBL· GenBank· DDBJ
AAD19818.1
EMBL· GenBank· DDBJ
Genomic DNA
AC011492
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC002329
EMBL· GenBank· DDBJ
AAH02329.2
EMBL· GenBank· DDBJ
mRNA
BC007551
EMBL· GenBank· DDBJ
AAH07551.1
EMBL· GenBank· DDBJ
mRNA
BC062360
EMBL· GenBank· DDBJ
AAH62360.1
EMBL· GenBank· DDBJ
mRNA
BC098445
EMBL· GenBank· DDBJ
AAH98445.1
EMBL· GenBank· DDBJ
mRNA
BC144332
EMBL· GenBank· DDBJ
AAI44333.1
EMBL· GenBank· DDBJ
mRNA
AL390184
EMBL· GenBank· DDBJ
CAB99102.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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