P01941 · HBA_TUPGL

Function

function

Involved in oxygen transport from the lung to the various peripheral tissues.

Hemopressin

Hemopressin acts as an antagonist peptide of the cannabinoid receptor CNR1. Hemopressin-binding efficiently blocks cannabinoid receptor CNR1 and subsequent signaling.

Features

Showing features for binding site.

1141102030405060708090100110120130140
TypeIDPosition(s)Description
Binding site58O2 (UniProtKB | ChEBI)
Binding site87Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); proximal binding residue

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 Componentblood microparticle
Cellular Componenthaptoglobin-hemoglobin complex
Cellular Componenthemoglobin complex
Molecular Functionhaptoglobin binding
Molecular Functionheme binding
Molecular Functioniron ion binding
Molecular Functionorganic acid binding
Molecular Functionoxygen binding
Molecular Functionoxygen carrier activity
Molecular Functionperoxidase activity
Biological Processhydrogen peroxide catabolic process

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Hemoglobin subunit alpha
  • Alternative names
    • Alpha-globin
    • Hemoglobin alpha chain
  • Cleaved into 1 chains

Gene names

    • Name
      HBA

Organism names

Accessions

  • Primary accession
    P01941

PTM/Processing

Features

Showing features for chain, modified residue, peptide.

TypeIDPosition(s)Description
ChainPRO_00000527931-141Hemoglobin subunit alpha
Modified residue3Phosphoserine
Modified residue7N6-succinyllysine
Modified residue11N6-succinyllysine
Modified residue16N6-acetyllysine; alternate
Modified residue16N6-succinyllysine; alternate
Modified residue24Phosphotyrosine
Modified residue35Phosphoserine
Modified residue40N6-succinyllysine
Modified residue49Phosphoserine
PeptidePRO_000045595595-103Hemopressin
Modified residue102Phosphoserine
Modified residue108Phosphothreonine
Modified residue124Phosphoserine
Modified residue134Phosphothreonine
Modified residue137Phosphothreonine
Modified residue138Phosphoserine

Keywords

Expression

Tissue specificity

Red blood cells.

Interaction

Subunit

Heterotetramer of two alpha chains and two beta chains.

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-141Globin

Sequence similarities

Belongs to the globin family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    141
  • Mass (Da)
    15,229
  • Last updated
    1986-07-21 v1
  • Checksum
    8D5B69010AE01AAF
VLSPGDKSNIKAAWGKIGGQAPQYGAEALERMFLSFPTTKTYFPHFDMSHGSAQIQAHGKKVADALSTAVGHLDDLPTALSALSDLHAHKLRVDPANFKLLSHCILVTLACHHPGDFTPEIHASLDKFLANVSTVLTSKYR

Keywords

Sequence databases

Similar Proteins

Disclaimer

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