Q9NZI7 · UBIP1_HUMAN

  • Protein
    Upstream-binding protein 1
  • Gene
    UBP1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Functions as a transcriptional activator in a promoter context-dependent manner. Modulates the placental expression of CYP11A1. Involved in regulation of the alpha-globin gene in erythroid cells. Activation of the alpha-globin promoter in erythroid cells is via synergistic interaction with TFCP2 (By similarity).
Involved in regulation of the alpha-globin gene in erythroid cells. Binds strongly to sequences around the HIV-1 initiation site and weakly over the TATA-box. Represses HIV-1 transcription by inhibiting the binding of TFIID to the TATA-box

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 Componentchromatin
Cellular Componentcytosol
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 FunctionRNA polymerase II cis-regulatory region sequence-specific DNA binding
Molecular Functionsequence-specific double-stranded DNA binding
Biological Processangiogenesis
Biological Processnegative regulation of viral 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
    Upstream-binding protein 1
  • Alternative names
    • Transcription factor LBP-1

Gene names

    • Name
      UBP1
    • Synonyms
      LBP1

Organism names

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

Accessions

  • Primary accession
    Q9NZI7
  • Secondary accessions
    • Q68CT0
    • Q86Y57
    • Q9H8V0
    • Q9UD76
    • Q9UD78

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_049294109in dbSNP:rs3736563
Natural variantVAR_025730212in dbSNP:rs17854430

Variants

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

The viewer provides 460 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, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
ChainPRO_00002290261-540UniProtUpstream-binding protein 1
Modified residue22UniProtPhosphoserine
Modified residue (large scale data)194PRIDEPhosphothreonine
Modified residue390UniProtPhosphoserine
Modified residue (large scale data)390PRIDEPhosphoserine
Modified residue393UniProtPhosphoserine
Modified residue (large scale data)393PRIDEPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in adrenal tissue, JEG-3, NCI-H295A, Hep-G2 and HeLa cell lines.

Induction

By HIV-1 infection of lymphocytes.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with TFCP2. Interacts with PIAS1, and is probably part of a complex containing TFCP2, UBP1 and PIAS1 (By similarity).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q9NZI7LNX1 Q8TBB13EBI-2795133, EBI-739832
BINARY Q9NZI7MORF4L1 Q9UBU8-23EBI-2795133, EBI-10288852
BINARY Q9NZI7TFCP2 Q128003EBI-2795133, EBI-717422

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain, compositional bias, region.

TypeIDPosition(s)Description
Domain60-296Grh/CP2 DB
Compositional bias236-264Basic and acidic residues
Region236-270Disordered
Region285-368Disordered
Compositional bias316-368Polar residues

Sequence similarities

Belongs to the grh/CP2 family. CP2 subfamily.

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q9NZI7-1

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
    LBP-1b
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    540
  • Mass (Da)
    60,491
  • Last updated
    2000-10-01 v1
  • Checksum
    CD95819AA86A7F39
MAWVLKMDEVIESGLVHDFDASLSGIGQELGAGAYSMSDVLALPIFKQEDSSLPLDGETEHPPFQYVMCAATSPAVKLHDETLTYLNQGQSYEIRMLDNRKMGDMPEINGKLVKSIIRVVFHDRRLQYTEHQQLEGWKWNRPGDRLLDLDIPMSVGIIDTRTNPSQLNAVEFLWDPAKRTSAFIQVHCISTEFTPRKHGGEKGVPFRIQVDTFKQNENGEYTDHLHSASCQIKVFKPKGADRKQKTDREKMEKRTAHEKEKYQPSYDTTILTEMRLEPIIEDAVEHEQKKSSKRTLPADYGDSLAKRGSCSPWPDAPTAYVNNSPSPAPTFTSPQQSTCSVPDSNSSSPNHQGDGASQTSGEQIQPSATIQETQQWLLKNRFSSYTRLFSNFSGADLLKLTKEDLVQICGAADGIRLYNSLKSRSVRPRLTIYVCREQPSSTVLQGQQQAASSASENGSGAPYVYHAIYLEEMIASEVARKLALVFNIPLHQINQVYRQGPTGIHILVSDQMVQNFQDESCFLFSTVKAESSDGIHIILK

Q9NZI7-4

  • Name
    2
  • Synonyms
    LBP-1a
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
F8WEP8F8WEP8_HUMANUBP1164
C9JWL3C9JWL3_HUMANUBP1148

Features

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

TypeIDPosition(s)Description
Sequence conflict93-94in Ref. 3; BAB14501
Compositional bias236-264Basic and acidic residues
Sequence conflict273in Ref. 1
Alternative sequenceVSP_017730274-309in isoform 2
Sequence conflict291-297in Ref. 1
Compositional bias316-368Polar residues
Sequence conflict418in Ref. 1
Sequence conflict424in Ref. 5; CAH18658
Sequence conflict503in Ref. 1

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF198487
EMBL· GenBank· DDBJ
AAF32274.1
EMBL· GenBank· DDBJ
mRNA
AK023274
EMBL· GenBank· DDBJ
BAB14501.1
EMBL· GenBank· DDBJ
mRNA
BC047235
EMBL· GenBank· DDBJ
AAH47235.1
EMBL· GenBank· DDBJ
mRNA
CR749798
EMBL· GenBank· DDBJ
CAH18658.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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