P31629 · ZEP2_HUMAN

  • Protein
    Transcription factor HIVEP2
  • Gene
    HIVEP2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

This protein specifically binds to the DNA sequence 5'-GGGACTTTCC-3' which is found in the enhancer elements of numerous viral promoters such as those of SV40, CMV, or HIV1. In addition, related sequences are found in the enhancer elements of a number of cellular promoters, including those of the class I MHC, interleukin-2 receptor, somatostatin receptor II, and interferon-beta genes. It may act in T-cell activation.

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
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

Names & Taxonomy

Protein names

  • Recommended name
    Transcription factor HIVEP2
  • Alternative names
    • Human immunodeficiency virus type I enhancer-binding protein 2 (HIV-EP2)
    • MHC-binding protein 2 (MBP-2)

Gene names

    • Name
      HIVEP2

Organism names

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

Accessions

  • Primary accession
    P31629
  • Secondary accessions
    • Q02646
    • Q5THT5
    • Q9NS05

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Disease & Variants

Involvement in disease

Intellectual developmental disorder, autosomal dominant 43 (MRD43)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD43 patients manifest developmental delay, intellectual disability, hypotonia, and dysmorphic features.
  • See also
    MIM:616977

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_05275446in dbSNP:rs17072013
Natural variantVAR_0527551041in dbSNP:rs34875559
Natural variantVAR_0527561293in dbSNP:rs35675714
Natural variantVAR_0527571538in dbSNP:rs109836

Variants

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

The viewer provides 2,878 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

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

TypeIDPosition(s)SourceDescription
ChainPRO_00000473711-2446UniProtTranscription factor HIVEP2
Modified residue (large scale data)41PRIDEPhosphoserine
Modified residue (large scale data)71PRIDEPhosphoserine
Modified residue (large scale data)166PRIDEPhosphoserine
Modified residue (large scale data)169PRIDEPhosphoserine
Modified residue (large scale data)296PRIDEPhosphoserine
Modified residue (large scale data)314PRIDEPhosphoserine
Modified residue (large scale data)374PRIDEPhosphoserine
Modified residue (large scale data)389PRIDEPhosphoserine
Modified residue (large scale data)412PRIDEPhosphoserine
Modified residue (large scale data)444PRIDEPhosphoserine
Modified residue (large scale data)563PRIDEPhosphoserine
Modified residue (large scale data)565PRIDEPhosphoserine
Modified residue (large scale data)619PRIDEPhosphoserine
Modified residue (large scale data)620PRIDEPhosphoserine
Modified residue (large scale data)702PRIDEPhosphoserine
Modified residue (large scale data)769PRIDEPhosphoserine
Modified residue (large scale data)771PRIDEPhosphoserine
Modified residue (large scale data)807PRIDEPhosphoserine
Modified residue (large scale data)813PRIDEPhosphoserine
Modified residue819UniProtPhosphoserine
Modified residue (large scale data)819PRIDEPhosphoserine
Modified residue (large scale data)926PRIDEPhosphothreonine
Modified residue950UniProtPhosphoserine
Modified residue (large scale data)950PRIDEPhosphoserine
Modified residue955UniProtPhosphoserine
Modified residue (large scale data)964PRIDEPhosphoserine
Modified residue (large scale data)1032PRIDEPhosphoserine
Modified residue1048UniProtPhosphoserine
Modified residue (large scale data)1050PRIDEPhosphoserine
Modified residue (large scale data)1070PRIDEPhosphoserine
Modified residue (large scale data)1085PRIDEPhosphoserine
Modified residue1443UniProtPhosphoserine
Modified residue (large scale data)1443PRIDEPhosphoserine
Modified residue1447UniProtPhosphoserine
Modified residue (large scale data)1447PRIDEPhosphoserine
Modified residue (large scale data)1613PRIDEPhosphoserine
Modified residue (large scale data)1937PRIDEPhosphoserine
Modified residue (large scale data)2059PRIDEPhosphoserine
Modified residue2118UniProtPhosphoserine
Modified residue (large scale data)2118PRIDEPhosphoserine
Modified residue2297UniProtPhosphoserine
Modified residue (large scale data)2297PRIDEPhosphoserine
Modified residue (large scale data)2298PRIDEPhosphothreonine
Modified residue (large scale data)2300PRIDEPhosphoserine
Modified residue2301UniProtPhosphoserine
Modified residue (large scale data)2301PRIDEPhosphoserine
Modified residue (large scale data)2311PRIDEPhosphoserine
Modified residue (large scale data)2402PRIDEPhosphothreonine
Modified residue2429UniProtPhosphoserine
Modified residue2431UniProtPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in brain and skeletal muscle.

Induction

By mitogens and phorbol ester.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with TCF4.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P31629YWHAG P619814EBI-2514157, EBI-359832

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

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

TypeIDPosition(s)Description
Region1-93Disordered
Compositional bias30-78Polar residues
Zinc finger189-211C2H2-type 1
Zinc finger217-239C2H2-type 2
Region272-303Disordered
Compositional bias340-360Polar residues
Region340-416Disordered
Compositional bias361-379Basic and acidic residues
Compositional bias380-416Polar residues
Compositional bias543-560Polar residues
Region543-563Disordered
Region751-985Disordered
Compositional bias799-820Polar residues
Compositional bias861-883Polar residues
Compositional bias889-919Basic and acidic residues
Compositional bias934-950Basic and acidic residues
Motif937-943Nuclear localization signal
Compositional bias951-985Polar residues
Region1485-1603Disordered
Compositional bias1505-1535Polar residues
Compositional bias1576-1590Polar residues
Zinc finger1799-1821C2H2-type 3
Zinc finger1827-1851C2H2-type 4
Region1882-1951Disordered
Compositional bias1900-1924Acidic residues
Compositional bias1930-1944Polar residues
Region2024-2129Disordered
Compositional bias2033-2054Polar residues
Repeat2053-20561
Region2053-214810 X 4 AA tandem repeats of S-P-[RGMKC]-[RK]
Repeat2059-20622
Compositional bias2067-2111Basic and acidic residues
Repeat2071-20743
Repeat2083-20864
Repeat2089-20925
Repeat2106-21096
Repeat2112-21157
Repeat2118-21218
Repeat2130-21339
Repeat2145-214810
Region2242-2325Disordered
Compositional bias2291-2313Polar residues
Region2371-2403Disordered
Region2423-2446Disordered

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    2,446
  • Mass (Da)
    269,053
  • Last updated
    2005-12-06 v2
  • Checksum
    482E2C577EF9449A
MDTGDTALGQKATSRSGETDKASGRWRQEQSAVIKMSTFGSHEGQRQPQIEPEQIGNTASAQLFGSGKLASPSEVVQQVAEKQYPPHRPSPYSCQHSLSFPQHSLPQGVMHSTKPHQSLEGPPWLFPGPLPSVASEDLFPFPIHGHSGGYPRKKISSLNPAYSQYSQKSIEQAEEAHKKEHKPKKPGKYICPYCSRACAKPSVLKKHIRSHTGERPYPCIPCGFSFKTKSNLYKHRKSHAHAIKAGLVPFTESAVSKLDLEAGFIDVEAEIHSDGEQSTDTDEESSLFAEASDKMSPGPPIPLDIASRGGYHGSLEESLGGPMKVPILIIPKSGIPLPNESSQYIGPDMLPNPSLNTKADDSHTVKQKLALRLSEKKGQDSEPSLNLLSPHSKGSTDSGYFSRSESAEQQISPPNTNAKSYEEIIFGKYCRLSPRNALSVTTTSQERAAMGRKGIMEPLPHVNTRLDVKMFEDPVSQLIPSKGDVDPSQTSMLKSTKFNSESRQPQIIPSSIRNEGKLYPANFQGSNPVLLEAPVDSSPLIRSNSVPTSSATNLTIPPSLRGSHSFDERMTGSDDVFYPGTVGIPPQRMLRRQAAFELPSVQEGHVEVEHHGRMLKGISSSSLKEKKLSPGDRVGYDYDVCRKPYKKWEDSETPKQNYRDISCLSSLKHGGEYFMDPVVPLQGVPSMFGTTCENRKRRKEKSVGDEEDTPMICSSIVSTPVGIMASDYDPKLQMQEGVRSGFAMAGHENLSHGHTERFDPCRPQLQPGSPSLVSEESPSAIDSDKMSDLGGRKPPGNVISVIQHTNSLSRPNSFERSESAELVACTQDKAPSPSETCDSEISEAPVSPEWAPPGDGAESGGKPSPSQQVQQQSYHTQPRLVRQHNIQVPEIRVTEEPDKPEKEKEAQSKEPEKPVEEFQWPQRSETLSQLPAEKLPPKKKRLRLADMEHSSGESSFESTGTGLSRSPSQESNLSHSSSFSMSFEREETSKLSALPKQDEFGKHSEFLTVPAGSYSLSVPGHHHQKEMRRCSSEQMPCPHPAEVPEVRSKSFDYGNLSHAPVSGAAASTVSPSRERKKCFLVRQASFSGSPEISQGEVGMDQSVKQEQLEHLHAGLRSGWHHGPPAVLPPLQQEDPGKQVAGPCPPLSSGPLHLAQPQIMHMDSQESLRNPLIQPTSYMTSKHLPEQPHLFPHQETIPFSPIQNALFQFQYPTVCMVHLPAQQPPWWQAHFPHPFAQHPQKSYGKPSFQTEIHSSYPLEHVAEHTGKKPAEYAHTKEQTYPCYSGASGLHPKNLLPKFPSDQSSKSTETPSEQVLQEDFASANAGSLQSLPGTVVPVRIQTHVPSYGSVMYTSISQILGQNSPAIVICKVDENMTQRTLVTNAAMQGIGFNIAQVLGQHAGLEKYPIWKAPQTLPLGLESSIPLCLPSTSDSVATLGGSKRMLSPASSLELFMETKQQKRVKEEKMYGQIVEELSAVELTNSDIKKDLSRPQKPQLVRQGCASEPKDGLQSGSSSFSSLSPSSSQDYPSVSPSSREPFLPSKEMLSGSRAPLPGQKSSGPSESKESSDELDIDETASDMSMSPQSSSLPAGDGQLEEEGKGHKRPVGMLVRMASAPSGNVADSTLLLTDMADFQQILQFPSLRTTTTVSWCFLNYTKPNYVQQATFKSSVYASWCISSCNPNPSGLNTKTTLALLRSKQKITAEIYTLAAMHRPGTGKLTSSSAWKQFTQMKPDASFLFGSKLERKLVGNILKERGKGDIHGDKDIGSKQTEPIRIKIFEGGYKSNEDYVYVRGRGRGKYICEECGIRCKKPSMLKKHIRTHTDVRPYVCKLCNFAFKTKGNLTKHMKSKAHMKKCLELGVSMTSVDDTETEEAENLEDLHKAAEKHSMSSISTDHQFSDAEESDGEDGDDNDDDDEDEDDFDDQGDLTPKTRSRSTSPQPPRFSSLPVNVGAVPHGVPSDSSLGHSSLISYLVTLPSIRVTQLMTPSDSCEDTQMTEYQRLFQSKSTDSEPDKDRLDIPSCMDEECMLPSEPSSSPRDFSPSSHHSSPGYDSSPCRDNSPKRYLIPKGDLSPRRHLSPRRDLSPMRHLSPRKEAALRREMSQRDVSPRRHLSPRRPVSPGKDITARRDLSPRRERRYMTTIRAPSPRRALYHNPPLSMGQYLQAEPIVLGPPNLRRGLPQVPYFSLYGDQEGAYEHPGSSLFPEGPNDYVFSHLPLHSQQQVRAPIPMVPVGGIQMVHSMPPALSSLHPSPTLPLPMEGFEEKKGASGESFSKDPYVLSKQHEKRGPHALQSSGPPSTPSSPRLLMKQSTSEDSLNATEREQEENIQTCTKAIASLRIATEEAALLGPDQPARVQEPHQNPLGSAHVSIRHFSRPEPGQPCTSATHPDLHDGEKDNFGTSQTPLAHSTFYSKSCVDDKQLDFHSSKELSSSTEESKDPSSEKSQLH

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A994J742A0A994J742_HUMANHIVEP2712
A0A994J6P4A0A994J6P4_HUMANHIVEP2717
A0A994J481A0A994J481_HUMANHIVEP21411
A0A994J411A0A994J411_HUMANHIVEP2416

Sequence caution

The sequence AAB88218.1 differs from that shown. Reason: Erroneous initiation
The sequence CAA46596.1 differs from that shown. Reason: Erroneous initiation

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias30-78Polar residues
Compositional bias340-360Polar residues
Compositional bias361-379Basic and acidic residues
Compositional bias380-416Polar residues
Compositional bias543-560Polar residues
Compositional bias799-820Polar residues
Compositional bias861-883Polar residues
Compositional bias889-919Basic and acidic residues
Compositional bias934-950Basic and acidic residues
Compositional bias951-985Polar residues
Compositional bias1505-1535Polar residues
Compositional bias1576-1590Polar residues
Compositional bias1900-1924Acidic residues
Compositional bias1930-1944Polar residues
Compositional bias2033-2054Polar residues
Compositional bias2067-2111Basic and acidic residues
Sequence conflict2091in Ref. 2; CAA46596
Compositional bias2291-2313Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M60119
EMBL· GenBank· DDBJ
AAB88218.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation
X65644
EMBL· GenBank· DDBJ
CAA46596.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AF153836
EMBL· GenBank· DDBJ
AAF81365.1
EMBL· GenBank· DDBJ
Genomic DNA
AL023584
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
M61744
EMBL· GenBank· DDBJ
AAA36202.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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