P69906 · HBA_PANPA

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.

Miscellaneous

Gives blood its red color.

Features

Showing features for binding site.

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TypeIDPosition(s)Description
Binding site59O2 (UniProtKB | ChEBI)
Binding site88Fe (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
      HBA1
    • Name
      HBA2

Organism names

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

Accessions

  • Primary accession
    P69906
  • Secondary accessions
    • P01922

Proteomes

PTM/Processing

Features

Showing features for initiator methionine, chain, modified residue, peptide.

TypeIDPosition(s)Description
Initiator methionine1Removed
ChainPRO_00000527172-142Hemoglobin subunit alpha
Modified residue4Phosphoserine
Modified residue8N6-succinyllysine
Modified residue9Phosphothreonine
Modified residue12N6-succinyllysine
Modified residue17N6-acetyllysine; alternate
Modified residue17N6-succinyllysine; alternate
Modified residue25Phosphotyrosine
Modified residue36Phosphoserine
Modified residue41N6-succinyllysine
Modified residue50Phosphoserine
PeptidePRO_000045591796-104Hemopressin
Modified residue103Phosphoserine
Modified residue109Phosphothreonine
Modified residue125Phosphoserine
Modified residue132Phosphoserine
Modified residue135Phosphothreonine
Modified residue138Phosphothreonine
Modified residue139Phosphoserine

Keywords

Expression

Tissue specificity

Red blood cells.

Gene expression databases

Interaction

Subunit

Heterotetramer of two alpha chains and two beta chains in adult hemoglobin A (HbA); two alpha chains and two delta chains in adult hemoglobin A2 (HbA2); two alpha chains and two epsilon chains in early embryonic hemoglobin Gower-2; two alpha chains and two gamma chains in fetal hemoglobin F (HbF).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain2-142Globin

Sequence similarities

Belongs to the globin family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    142
  • Mass (Da)
    15,258
  • Last updated
    2007-01-23 v2
  • Checksum
    15E13666573BBBAE
MVLSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFDLSHGSAQVKGHGKKVADALTNAVAHVDDMPNALSALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPAVHASLDKFLASVSTVLTSKYR

Keywords

Sequence databases

Genome annotation databases

Similar Proteins

Disclaimer

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