Q14587 · ZN268_HUMAN

  • Protein
    Zinc finger protein 268
  • Gene
    ZNF268
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Isoform 1

Acts as a transcriptional repressor. Inhibits erythroid differentiation and tumor cell proliferation. Plays a role during ovarian cancer development and progression.

Isoform 2

Contributes to cervical carcinogenesis in part through the TNF-alpha-induced NF-kappa-B signaling pathway by interacting with the I-kappa-B-kinase (IKK) core complex.

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 Componentcytoplasm
Cellular Componentcytosol
Cellular Componentnucleus
Molecular FunctionDNA binding
Molecular FunctionDNA-binding transcription activator activity, RNA polymerase II-specific
Molecular FunctionDNA-binding transcription factor activity
Molecular Functionmetal ion binding
Molecular FunctionRNA polymerase II cis-regulatory region sequence-specific DNA binding
Biological Processcell differentiation
Biological Processcellular response to tumor necrosis factor
Biological Processnegative regulation of apoptotic process
Biological Processnegative regulation of cell population proliferation
Biological Processnegative regulation of transcription by RNA polymerase II
Biological Processpositive regulation of apoptotic process
Biological Processpositive regulation of cell differentiation
Biological Processpositive regulation of cell migration
Biological Processpositive regulation of cell population proliferation
Biological Processpositive regulation of non-canonical NF-kappaB signal transduction
Biological Processpositive regulation of protein catabolic process
Biological Processpositive regulation of protein homodimerization activity
Biological Processpositive regulation of protein phosphorylation
Biological Processpositive regulation of transcription by RNA polymerase II
Biological Processregulation of cell cycle
Biological Processregulation of DNA-templated transcription
Biological Processregulation of mitotic cell cycle
Biological Processregulation of protein heterodimerization activity
Biological Processregulation of transcription by RNA polymerase II

Keywords

Enzyme and pathway databases

Community curation (1)

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

Names & Taxonomy

Protein names

  • Recommended name
    Zinc finger protein 268
  • Alternative names
    • Zinc finger protein HZF3

Gene names

    • Name
      ZNF268
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
    Q14587
  • Secondary accessions
    • Q8TDG8
    • Q96RH4
    • Q9BZJ9

Proteomes

Organism-specific databases

Subcellular Location

Isoform 1

Nucleus

Isoform 2

Nucleus
Cytoplasm

Keywords

Disease & Variants

Features

Showing features for mutagenesis, natural variant.

TypeIDPosition(s)Description
Mutagenesis85Strongly reduces nuclear localization and interaction with TRIM28; when associated with A-86.
Mutagenesis86Reduces nuclear localization. Strongly reduces nuclear localization and interaction with TRIM28; when associated with A-85.
Mutagenesis88Reduces nuclear localization.
Mutagenesis90Reduces nuclear localization.
Mutagenesis93Reduces nuclear localization. Strongly reduces nuclear localization; when associated with A-94 and A-95.
Mutagenesis94Reduces nuclear localization. Inhibits nuclear localization; when associated with A-93 and A-95.
Mutagenesis95Reduces nuclear localization. Inhibits nuclear localization; when associated with A-93 and A-94.
Natural variantVAR_033562175in dbSNP:rs7975069

Variants

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

The viewer provides 1,276 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).

TypeIDPosition(s)SourceDescription
ChainPRO_00000474951-947UniProtZinc finger protein 268
Modified residue (large scale data)48PRIDEPhosphothreonine
Modified residue (large scale data)747PRIDEPhosphothreonine
Modified residue (large scale data)752PRIDEPhosphotyrosine

Proteomic databases

PTM databases

Expression

Tissue specificity

Overexpressed in ovarian cancer tissues compared to normal ovarian tissues. Isoform 1 and isoform 2 are expressed in squamous epithelium tissues. Isoform 2 is overexpressed in squamous cervical cancer (at protein level). Expressed in blood cells. Isoform 1 is expressed in pancreas, lung, skeletal muscle, heart, placenta, liver, kidney and brain. Isoform 2 expressed in chronic lymphocytic leukemia (CLL) and several tumor cell lines. Isoform 3 is expressed in several tumor cells. Isoform 5 is expressed in fetal liver and several tumor cells. Isoform 6 is weakly expressed in brain, lung amd small intestin and in several tumor cells. Isoform 7 is expressed in fetal liver and several tumor cells.

Induction

Down-regulated during erythroid differentiation by GATA1. Down-regulated by HTLV-1 Tax through the CREB/ATF pathway. Up-regulated by the regulator of nonsense transcript UPF1. Up-regulated by the cyclic AMP-dependent transcription factor ATF4.

Developmental stage

Expressed in fetal liver from 5 weeks until 4 months but drastically reduced by 6 months and became non-detectable by 7 months. Expressed in hematopoietic stem cells in 3 weeks and 5 weeks (at protein level). Expressed in fetal liver.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts (via the KRAB domain) with TRIM28 (via the RBCC domain); the interaction increases ZNF268 nuclear localization activity. Isoform 2 interacts with CHUK and IKBKB; the interaction is further increased in a TNF-alpha-dependent manner.

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for domain, zinc finger.

TypeIDPosition(s)Description
Domain81-152KRAB
Zinc finger276-298C2H2-type 1
Zinc finger304-326C2H2-type 2
Zinc finger332-354C2H2-type 3
Zinc finger360-382C2H2-type 4
Zinc finger388-410C2H2-type 5
Zinc finger416-438C2H2-type 6
Zinc finger444-466C2H2-type 7
Zinc finger472-494C2H2-type 8
Zinc finger500-522C2H2-type 9
Zinc finger528-550C2H2-type 10
Zinc finger556-578C2H2-type 11
Zinc finger584-606C2H2-type 12
Zinc finger612-634C2H2-type 13
Zinc finger640-662C2H2-type 14
Zinc finger668-690C2H2-type 15
Zinc finger696-718C2H2-type 16
Zinc finger724-746C2H2-type 17
Zinc finger752-774C2H2-type 18
Zinc finger780-802C2H2-type 19
Zinc finger808-830C2H2-type 20
Zinc finger836-858C2H2-type 21
Zinc finger864-886C2H2-type 22
Zinc finger892-914C2H2-type 23
Zinc finger920-942C2H2-type 24

Domain

The KRAB domain functions to reinforce the nuclear localization of isoform 1 in addition to its transcription repression activity.

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (7)
  • Sequence status
    Complete

This entry describes 7 isoforms produced by Alternative splicing.

Q14587-1

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.

  • Name
    1
  • Synonyms
    ZNF268a, KW-4 variant-1
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    947
  • Mass (Da)
    108,374
  • Last updated
    2001-08-29 v2
  • Checksum
    AC78F4824F4BE1A0
MATRVRTASIWVPPLQERNSSWDRIRKLQGQESILGQGTPGLQPLPGTPRQKQKSRRIEKVLEWLFISQEQPKITKSWGPLSFMDVFVDFTWEEWQLLDPAQKCLYRSVMLENYSNLVSLGYQHTKPDIIFKLEQGEELCMVQAQVPNQTCPNTVWKIDDLMDWHQENKDKLGSTAKSFECTTFGKLCLLSTKYLSRQKPHKCGTHGKSLKYIDFTSDYARNNPNGFQVHGKSFFHSKHEQTVIGIKYCESIESGKTVNKKSQLMCQQMYMGEKPFGCSCCEKAFSSKSYLLVHQQTHAEEKPYGCNECGKDFSSKSYLIVHQRIHTGEKLHECSECRKTFSFHSQLVIHQRIHTGENPYECCECGKVFSRKDQLVSHQKTHSGQKPYVCNECGKAFGLKSQLIIHERIHTGEKPYECNECQKAFNTKSNLMVHQRTHTGEKPYVCSDCGKAFTFKSQLIVHQGIHTGVKPYGCIQCGKGFSLKSQLIVHQRSHTGMKPYVCNECGKAFRSKSYLIIHTRTHTGEKLHECNNCGKAFSFKSQLIIHQRIHTGENPYECHECGKAFSRKYQLISHQRTHAGEKPYECTDCGKAFGLKSQLIIHQRTHTGEKPFECSECQKAFNTKSNLIVHQRTHTGEKPYSCNECGKAFTFKSQLIVHKGVHTGVKPYGCSQCAKTFSLKSQLIVHQRSHTGVKPYGCSECGKAFRSKSYLIIHMRTHTGEKPHECRECGKSFSFNSQLIVHQRIHTGENPYECSECGKAFNRKDQLISHQRTHAGEKPYGCSECGKAFSSKSYLIIHMRTHSGEKPYECNECGKAFIWKSLLIVHERTHAGVNPYKCSQCEKSFSGKLRLLVHQRMHTREKPYECSECGKAFIRNSQLIVHQRTHSGEKPYGCNECGKTFSQKSILSAHQRTHTGEKPCKCTECGKAFCWKSQLIMHQRTHVDDKH

Q14587-2

  • Name
    2
  • Synonyms
    ZNF268s, KW-4 variant-2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q14587-3

  • Name
    3
  • Synonyms
    ZNF268c
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q14587-4

  • Name
    4
  • Synonyms
    ZNF268d
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 12-99: VPPLQERNSSWDRIRKLQGQESILGQGTPGLQPLPGTPRQKQKSRRIEKVLEWLFISQEQPKITKSWGPLSFMDVFVDFTWEEWQLLD → GTNTPNLISSSSWNKEKSCVWCRPKFQIRPVQTQSGKLMILWIGIRKIKTSWEVWQKALNALHLENYVFLVQSIFQDKNLINVARMERV
    • 100-947: Missing

Q14587-6

  • Name
    5
  • Synonyms
    ZNF268e
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 79-135: GPLSFMDVFVDFTWEEWQLLDPAQKCLYRSVMLENYSNLVSLGYQHTKPDIIFKLEQ → TQSGKLMILWIGIRKIKTSWEVRQKALNALHLENYVFLVQSIFQDKNLINVARMERV
    • 136-947: Missing

Q14587-7

  • Name
    6
  • Synonyms
    ZNF268f
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 12-44: VPPLQERNSSWDRIRKLQGQESILGQGTPGLQP → GTNTPNLISSSSWNKEKSCVWCRPKFQIRPVQF
    • 45-947: Missing

Q14587-8

  • Name
    7
  • Synonyms
    ZNF268g
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 12-78: Missing
    • 153-183: NTVWKIDDLMDWHQENKDKLGSTAKSFECTT → ILKAGKSKAKVLAGLVSGEGPLCASKMTPCC
    • 184-947: Missing

Computationally mapped potential isoform sequences

There are 12 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A075B6T9A0A075B6T9_HUMANZNF268193
E7EV44E7EV44_HUMANZNF268188
K7EIF0K7EIF0_HUMANZNF268111
K7EMS6K7EMS6_HUMANZNF26894
K7EQP6K7EQP6_HUMANZNF268126
A0A087WV54A0A087WV54_HUMANZNF268121
F5H7L3F5H7L3_HUMANZNF268167
F5H6R9F5H6R9_HUMANZNF26838
F5H848F5H848_HUMANZNF268178
F5H670F5H670_HUMANZNF268100
F5H467F5H467_HUMANZNF26835
F5H1T2F5H1T2_HUMANZNF26868

Features

Showing features for alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Alternative sequenceVSP_0534611-140in isoform 3
Alternative sequenceVSP_0069091-161in isoform 2
Alternative sequenceVSP_05346412-44in isoform 6
Alternative sequenceVSP_05346312-78in isoform 7
Alternative sequenceVSP_05346212-99in isoform 4
Alternative sequenceVSP_05346545-947in isoform 6
Alternative sequenceVSP_05346679-135in isoform 5
Alternative sequenceVSP_053467100-947in isoform 4
Alternative sequenceVSP_053468136-947in isoform 5
Alternative sequenceVSP_053469153-183in isoform 7
Alternative sequenceVSP_053470184-947in isoform 7
Alternative sequenceVSP_053471222-947in isoform 3
Sequence conflict323in Ref. 2; AAL99923
Sequence conflict335-336in Ref. 2; AAL99923
Sequence conflict340in Ref. 2; AAL99923
Sequence conflict344in Ref. 2; AAL99923
Sequence conflict363in Ref. 2; AAL99923
Sequence conflict409in Ref. 2; AAL99923
Sequence conflict860in Ref. 2; AAL99923 and 6; CAA55526

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF317549
EMBL· GenBank· DDBJ
AAG59817.1
EMBL· GenBank· DDBJ
mRNA
AF385187
EMBL· GenBank· DDBJ
AAK69307.1
EMBL· GenBank· DDBJ
mRNA
AF432217
EMBL· GenBank· DDBJ
AAL99923.1
EMBL· GenBank· DDBJ
mRNA
AC026785
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
DQ057356
EMBL· GenBank· DDBJ
-mRNA No translation available.
DQ057357
EMBL· GenBank· DDBJ
-mRNA No translation available.
DQ057358
EMBL· GenBank· DDBJ
-mRNA No translation available.
DQ057359
EMBL· GenBank· DDBJ
-mRNA No translation available.
DQ057360
EMBL· GenBank· DDBJ
-mRNA No translation available.
X78926
EMBL· GenBank· DDBJ
CAA55526.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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