Q5T1R4 · ZEP3_HUMAN

  • Protein
    Transcription factor HIVEP3
  • Gene
    HIVEP3
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Plays a role of transcription factor; binds to recognition signal sequences (Rss heptamer) for somatic recombination of immunoglobulin and T-cell receptor gene segments; Binds also to the kappa-B motif of gene such as S100A4, involved in cell progression and differentiation. Kappa-B motif is a gene regulatory element found in promoters and enhancers of genes involved in immunity, inflammation, and growth and that responds to viral antigens, mitogens, and cytokines. Involvement of HIVEP3 in cell growth is strengthened by the fact that its down-regulation promotes cell cycle progression with ultimate formation of multinucleated giant cells. Strongly inhibits TNF-alpha-induced NF-kappa-B activation; Interferes with nuclear factor NF-kappa-B by several mechanisms: as transcription factor, by competing for Kappa-B motif and by repressing transcription in the nucleus; through a non transcriptional process, by inhibiting nuclear translocation of RELA by association with TRAF2, an adapter molecule in the tumor necrosis factor signaling, which blocks the formation of IKK complex. Interaction with TRAF proteins inhibits both NF-Kappa-B-mediated and c-Jun N-terminal kinase/JNK-mediated responses that include apoptosis and pro-inflammatory cytokine gene expression. Positively regulates the expression of IL2 in T-cell. Essential regulator of adult bone formation.

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 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 Processpositive regulation of DNA-templated transcription
Biological Processregulation of transcription by RNA polymerase II
Biological Processskeletal muscle cell differentiation

Keywords

Enzyme and pathway databases

Community curation (1)

The subsequence KKERKPQKPGKYICQYCSRPCAKPSVLQKHIRSHTGERPYPCGPCGFSFKTKSNLYKHRKSHAHRIKAGLASGMGGEMYP; the subsequence GSGSESGKERRTTSKEISVIQHTSSFEKSDSLEQPSGLEGEDKPLAQFPSPPPAPHGRSAHSLQPKLVRQPNIQVPEILV; and the subsequence VKKEDSKEQPDLPSLAPPSSLPLSETSSRPAKSQEGTDSKKVLQFPSLHTTTNVSWCYLNYIKPNHIQHADRRSSVYAGW show transcriptional repressor activity in a high-throughput recruitment assay.

Names & Taxonomy

Protein names

  • Recommended name
    Transcription factor HIVEP3
  • Alternative names
    • Human immunodeficiency virus type I enhancer-binding protein 3
    • Kappa-B and V(D)J recombination signal sequences-binding protein
    • Kappa-binding protein 1 (KBP-1)
    • Zinc finger protein ZAS3

Gene names

    • Name
      HIVEP3
    • Synonyms
      KBP1, KIAA1555, KRC, ZAS3
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
    Q5T1R4
  • Secondary accessions
    • A7YY91
    • Q5T1R5
    • Q9BZS0
    • Q9HCL7

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_04291035in dbSNP:rs2146315
Natural variantVAR_042911484in a colorectal cancer sample; somatic mutation; dbSNP:rs780211835
Natural variantVAR_042912575in dbSNP:rs2810566
Natural variantVAR_0429131087in dbSNP:rs17363472
Natural variantVAR_0429142023in dbSNP:rs2483689
Natural variantVAR_0429152109in dbSNP:rs2991344
Natural variantVAR_0429162272in dbSNP:rs11809423
Natural variantVAR_0429172339in dbSNP:rs9439043
Natural variantVAR_0878912348in dbSNP:rs543298786

Variants

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

The viewer provides 2,739 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_00003316271-2406UniProtTranscription factor HIVEP3
Modified residue (large scale data)382PRIDEPhosphoserine
Modified residue (large scale data)542PRIDEPhosphoserine
Modified residue (large scale data)682PRIDEPhosphoserine
Modified residue (large scale data)720PRIDEPhosphoserine
Modified residue (large scale data)732PRIDEPhosphoserine
Modified residue (large scale data)733PRIDEPhosphothreonine
Modified residue (large scale data)739PRIDEPhosphoserine
Modified residue (large scale data)804PRIDEPhosphoserine
Modified residue (large scale data)805PRIDEPhosphoserine
Modified residue (large scale data)809PRIDEPhosphoserine
Modified residue (large scale data)811PRIDEPhosphoserine
Modified residue (large scale data)830PRIDEPhosphoserine
Modified residue (large scale data)931PRIDEPhosphoserine
Modified residue (large scale data)933PRIDEPhosphoserine
Modified residue (large scale data)993PRIDEPhosphoserine
Modified residue (large scale data)1012PRIDEPhosphoserine
Modified residue (large scale data)1050PRIDEPhosphoserine
Modified residue (large scale data)1433PRIDEPhosphoserine
Modified residue (large scale data)1437PRIDEPhosphoserine
Modified residue (large scale data)1964PRIDEPhosphoserine
Modified residue (large scale data)2006PRIDEPhosphoserine
Modified residue (large scale data)2009PRIDEPhosphoserine
Modified residue (large scale data)2034PRIDEPhosphoserine
Modified residue (large scale data)2067PRIDEPhosphoserine
Modified residue (large scale data)2127PRIDEPhosphoserine
Modified residue (large scale data)2245PRIDEPhosphoserine
Modified residue (large scale data)2255PRIDEPhosphoserine
Modified residue (large scale data)2354PRIDEPhosphoserine
Modified residue (large scale data)2382PRIDEPhosphoserine

Post-translational modification

Phosphorylated on threonine and serine residues.

Keywords

Proteomic databases

PTM databases

Expression

Induction

By 12-O-tetradecanoylphorbol-13 acetate (TPA).

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with TRAF1 and TRAF2 as well as with JUN. Forms a multimeric complex with RUNX2 and E3 ubiquitin ligase WWP1 (By similarity).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q5T1R4SFN P319475EBI-28989979, EBI-476295
BINARY Q5T1R4YWHAG P619812EBI-28989979, EBI-359832

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for compositional bias, region, zinc finger, motif, coiled coil, repeat.

TypeIDPosition(s)Description
Compositional bias1-21Basic and acidic residues
Region1-112Disordered
Compositional bias23-52Polar residues
Zinc finger192-214C2H2-type 1
Region192-242ZAS1
Region211-1074No DNA binding activity or transactivation activity, but complete prevention of TRAF-dependent NF-Kappa-B activation; associates with TRAF2 and JUN
Zinc finger220-242C2H2-type 2
Region264-287Acidic 1
Region272-358Disordered
Compositional bias306-336Polar residues
Region377-409Disordered
Compositional bias382-409Polar residues
Region481-540Disordered
Region597-633Disordered
Compositional bias615-633Basic and acidic residues
Zinc finger640-670CCHC HIVEP-type
Region677-696Disordered
Region706-1115Disordered
Compositional bias709-730Basic and acidic residues
Compositional bias797-812Polar residues
Compositional bias861-884Basic and acidic residues
Region862-883Acidic 2
Motif903-909Nuclear localization signal
Compositional bias914-946Polar residues
Compositional bias992-1019Polar residues
Compositional bias1069-1094Polar residues
Compositional bias1268-1283Polar residues
Region1268-1303Disordered
Compositional bias1406-1430Polar residues
Region1406-1459Disordered
Coiled coil1442-1466
Compositional bias1445-1459Basic and acidic residues
Region1472-1594Disordered
Compositional bias1476-1490Basic and acidic residues
Compositional bias1494-1508Polar residues
Compositional bias1569-1594Polar residues
Region1692-1727Disordered
Compositional bias1700-1724Basic and acidic residues
Zinc finger1754-1776C2H2-type 3
Region1754-1806ZAS2
Zinc finger1782-1806C2H2-type 4
Region1817-1872Acidic 3
Region1818-2033Disordered
Compositional bias1829-1848Basic and acidic residues
Compositional bias1849-1873Acidic residues
Compositional bias1910-1937Polar residues
Repeat1964-19671
Repeat1970-19732
Compositional bias1986-2002Polar residues
Repeat1993-19963
Repeat1998-20014
Region2052-2113Disordered
Region2053-21486 X 4 AA tandem repeats of S-P-X-[RK]
Repeat2067-20705
Repeat2079-20826
Region2125-2151Disordered
Compositional bias2129-2149Polar residues
Region2224-2406Disordered
Compositional bias2244-2262Polar residues
Compositional bias2304-2318Pro residues

Domain

The ZAS2 domain binds DNA as dimers, tetramers, and multiple of tetramers and readily forms highly ordered DNA-protein structures.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing. Additional isoforms can be generated by alternative splicing or polyadenylation. HIVEP3L transcript may lack exon 7 leading to a premature codon stop.

Q5T1R4-1

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
    HIVEP3S
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    2,406
  • Mass (Da)
    259,465
  • Last updated
    2004-12-21 v1
  • Checksum
    AFCCFDAF87014A7D
MDPEQSVKGTKKAEGSPRKRLTKGEAIQTSVSSSVPYPGSGTAATQESPAQELLAPQPFPGPSSVLREGSQEKTGQQQKPPKRPPIEASVHISQLPQHPLTPAFMSPGKPEHLLEGSTWQLVDPMRPGPSGSFVAPGLHPQSQLLPSHASIIPPEDLPGVPKVFVPRPSQVSLKPTEEAHKKERKPQKPGKYICQYCSRPCAKPSVLQKHIRSHTGERPYPCGPCGFSFKTKSNLYKHRKSHAHRIKAGLASGMGGEMYPHGLEMERIPGEEFEEPTEGESTDSEEETSATSGHPAELSPRPKQPLLSSGLYSSGSHSSSHERCSLSQSSTAQSLEDPPPFVEPSSEHPLSHKPEDTHTIKQKLALRLSERKKVIDEQAFLSPGSKGSTESGYFSRSESAEQQVSPPNTNAKSYAEIIFGKCGRIGQRTAMLTATSTQPLLPLSTEDKPSLVPLSVPRTQVIEHITKLITINEAVVDTSEIDSVKPRRSSLSRRSSMESPKSSLYREPLSSHSEKTKPEQSLLSLQHPPSTAPPVPLLRSHSMPSAACTISTPHHPFRGSYSFDDHITDSEALSHSSHVFTSHPRMLKRQPAIELPLGGEYSSEEPGPSSKDTASKPSDEVEPKESELTKKTKKGLKTKGVIYECNICGARYKKRDNYEAHKKYYCSELQIAKPISAGTHTSPEAEKSQIEHEPWSQMMHYKLGTTLELTPLRKRRKEKSLGDEEEPPAFESTKSQFGSPGPSDAARNLPLESTKSPAEPSKSVPSLEGPTGFQPRTPKPGSGSESGKERRTTSKEISVIQHTSSFEKSDSLEQPSGLEGEDKPLAQFPSPPPAPHGRSAHSLQPKLVRQPNIQVPEILVTEEPDRPDTEPEPPPKEPEKTEEFQWPQRSQTLAQLPAEKLPPKKKRLRLAEMAQSSGESSFESSVPLSRSPSQESNVSLSGSSRSASFERDDHGKAEAPSPSSDMRPKPLGTHMLTVPSHHPHAREMRRSASEQSPNVSHSAHMTETRSKSFDYGSLSLTGPSAPAPVAPPARVAPPERRKCFLVRQASLSRPPESELEVAPKGRQESEEPQPSSSKPSAKSSLSQISSAATSHGGPPGGKGPGQDRPPLGPTVPYTEALQVFHHPVAQTPLHEKPYLPPPVSLFSFQHLVQHEPGQSPEFFSTQAMSSLLSSPYSMPPLPPSLFQAPPLPLQPTVLHPGQLHLPQLMPHPANIPFRQPPSFLPMPYPTSSALSSGFFLPLQSQFALQLPGDVESHLPQIKTSLAPLATGSAGLSPSTEYSSDIRLPPVAPPASSSAPTSAPPLALPACPDTMVSLVVPVRVQTNMPSYGSAMYTTLSQILVTQSQGSSATVALPKFEEPPSKGTTVCGADVHEVGPGPSGLSEEQSRAFPTPYLRVPVTLPERKGTSLSSESILSLEGSSSTAGGSKRVLSPAGSLELTMETQQQKRVKEEEASKADEKLELVKPCSVVLTSTEDGKRPEKSHLGNQGQGRRELEMLSSLSSDPSDTKEIPPLPHPALSHGTAPGSEALKEYPQPSGKPHRRGLTPLSVKKEDSKEQPDLPSLAPPSSLPLSETSSRPAKSQEGTDSKKVLQFPSLHTTTNVSWCYLNYIKPNHIQHADRRSSVYAGWCISLYNPNLPGVSTKAALSLLRSKQKVSKETYTMATAPHPEAGRLVPSSSRKPRMTEVHLPSLVSPEGQKDLARVEKEEERRGEPEEDAPASQRGEPARIKIFEGGYKSNEEYVYVRGRGRGKYVCEECGIRCKKPSMLKKHIRTHTDVRPYVCKHCHFAFKTKGNLTKHMKSKAHSKKCQETGVLEELEAEEGTSDDLFQDSEGREGSEAVEEHQFSDLEDSDSDSDLDEDEDEDEEESQDELSRPSSEAPPPGPPHALRADSSPILGPQPPDAPASGTEATRGSSVSEAERLTASSCSMSSQSMPGLPWLGPAPLGSVEKDTGSALSYKPVSPRRPWSPSKEAGSRPPLARKHSLTKNDSSPQRCSPAREPQASAPSPPGLHVDPGRGMGALPCGSPRLQLSPLTLCPLGRELAPRAHVLSKLEGTTDPGLPRYSPTRRWSPGQAESPPRSAPPGKWALAGPGSPSAGEHGPGLGLDPRVLFPPAPLPHKLLSRSPETCASPWQKAESRSPSCSPGPAHPLSSRPFSALHDFHGHILARTEENIFSHLPLHSQHLTRAPCPLIPIGGIQMVQARPGAHPTLLPGPTAAWVSGFSGGGSDLTGAREAQERGRWSPTESSSASVSPVAKVSKFTLSSELEGGDYPKERERTGGGPGRPPDWTPHGTGAPAEPTPTHSPCTPPDTLPRPPQGRRAAQSWSPRLESPRAPTNPEPSATPPLDRSSSVGCLAEASARFPARTRNLSGEPRTRQDSPKPSGSGEPRAHPHQPEDRVPPNA

Q5T1R4-2

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

Sequence caution

The sequence BAB13381.2 differs from that shown. Reason: Erroneous initiation

Features

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

TypeIDPosition(s)Description
Compositional bias1-21Basic and acidic residues
Compositional bias23-52Polar residues
Sequence conflict44in Ref. 1; AAK01082
Sequence conflict94-95in Ref. 1; AAK01082
Sequence conflict123in Ref. 1; AAK01082
Sequence conflict127in Ref. 1; AAK01082
Sequence conflict133-134in Ref. 1; AAK01082
Compositional bias306-336Polar residues
Compositional bias382-409Polar residues
Sequence conflict589in Ref. 1; AAK01082
Compositional bias615-633Basic and acidic residues
Compositional bias709-730Basic and acidic residues
Compositional bias797-812Polar residues
Compositional bias861-884Basic and acidic residues
Sequence conflict901in Ref. 1; AAK01082
Compositional bias914-946Polar residues
Sequence conflict961in Ref. 1; AAK01082
Compositional bias992-1019Polar residues
Sequence conflict1034-1035in Ref. 1; AAK01082
Sequence conflict1048-1049in Ref. 1; AAK01082
Compositional bias1069-1094Polar residues
Sequence conflict1110in Ref. 1; AAK01082
Sequence conflict1180in Ref. 2; BAB13381 and 5; AAI52564
Compositional bias1268-1283Polar residues
Sequence conflict1279in Ref. 1; AAK01082
Compositional bias1406-1430Polar residues
Compositional bias1445-1459Basic and acidic residues
Compositional bias1476-1490Basic and acidic residues
Compositional bias1494-1508Polar residues
Sequence conflict1524in Ref. 1; AAK01082
Compositional bias1569-1594Polar residues
Compositional bias1700-1724Basic and acidic residues
Compositional bias1829-1848Basic and acidic residues
Compositional bias1849-1873Acidic residues
Compositional bias1910-1937Polar residues
Compositional bias1986-2002Polar residues
Compositional bias2129-2149Polar residues
Alternative sequenceVSP_0332792136in isoform 2
Compositional bias2244-2262Polar residues
Compositional bias2304-2318Pro residues
Sequence conflict2376in Ref. 1; AAK01082

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF278765
EMBL· GenBank· DDBJ
AAK01082.1
EMBL· GenBank· DDBJ
mRNA
AB046775
EMBL· GenBank· DDBJ
BAB13381.2
EMBL· GenBank· DDBJ
mRNA Different initiation
AL445933
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC152563
EMBL· GenBank· DDBJ
AAI52564.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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