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0HBB_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameHBB
DescriptionHemoglobin beta subunit (hemoglobin beta chain) (beta-globin).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005833 hemoglobin complex (NAS)
0030492 hemoglobin binding (IDA)
0019825 oxygen binding (IDA)
0005344 oxygen transporter activity (NAS)
0008430 selenium binding (IDA)
0030185 nitric oxide transport (NAS)
0015671 oxygen transport (NAS)
0045429 positive regulation of nitric oxide biosynt... (NAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Globins are heme-containing proteins involved in binding and/or transporting oxygen. They belong to a very large and well studied family which is widely distributed in many organisms. The major groups of globins arehemoglobins (Hb) and myoglobins (Mg) from vertebrates.nvertebrate globins.eghemoglobins from plants.nd flavohemoproteins from bacteria. Hb is the protein responsible for transporting oxygen from the lungs to other tissues.nd is a tetramer of two alpha and two beta chains. Most vertebrate species also expressspecific embryonic or fetal forms of hemoglobin where the alpha or the beta chains are replaced by a chain with higher oxygen affinity.s for the gamma.elta.psilon and zeta chains in mammals.or example.Mg is a monomeric protein responsible for oxygen storage in muscles. A wide variety of globins are found ininvertebrates . Molluscs generally have one or two muscle globins which are either monomeric or dimeric.hile insects.uch as the midge Chironomus thummi.ave a large set of extracellular globins. Nematodes and annelids have a variety of intracellular and extracellular globins.ome of them are multi-domain polypeptides (from two up to nine-domain globins).nd some produce large.isulphide-bonded aggregates. Leghemoglobins (Lg) from the root nodules of leguminous plants provides oxygen for bacteroids.Flavohemoproteins from bacteria (Escherichia coli hmpA) and fungi consist of two distinct domains.n N-terminal globin domain and a C-terminal FAD-containing reductase domain. In bacteria such as Vitreoscilla.he enzyme-associated globin is a single domain protein. All these globins seem to have evolved from a common ancestor.
  IPR000971:Globin
Globins are haem-containing proteins involved in dioxygen binding and/or transport. At present.ore than 700 globin sequences are known .It has been proposed that all globins have evolved from a family of ancestral.pproximately 17 kD haemoproteins that displayed the globin fold and functioned as redox proteins . The globin superfamily includes vertebrate haemoglobins (Hb); vertebrate myoglobins (Mb); invertebrate globins; plant leghaemoglobins; and bacterial flavohaemoglobins. The function of vertebrate haemoglobins (Hb) is transport of dioxygen inblood plasma. Hb binds O(2) in the reduced [Fe(II)] state. The Hb molecule exists as a tetramer.ypically of two alpha- and two beta-globin chains.hich form a well-defined quaternary structure. Each monomer binds iron protoporphyrin IX (haem). The 3D structures of a great number of haemoglobins in various statesare known. The protein is largely alpha-helical.ight conserved helices (A to H) providing the scaffold for a well-defined haem-binding pocket(Hb alpha subunits lack helix D ). The imidazole ring of the proximalHis residue provides the fifth haem iron ligand; the other axial haem iron position remains essentially free for O(2) coordination. Conserved distalHis and Val residues block an unhindered access to the sixth coordination site so that a controlled binding of small molecules may result only as a consequence of side-chain dynamics of the protein. O(2) binding resultsin a transition from high-spin to low-spin iron.ith accompanying changes in the Fe-N bond lengths and coordination geometry. In Hb.hese subtle changes lead to the well-known cooperative effect. On the quaternary structure level.(2) binding induces relative reorientation of the [alpha-1.eta-1] and [alpha-2.eta-2] dimers. Alpha- and beta-haemoglobins are highly similar; the sequence of beta-differs in length from that of alpha-haemoglobin on average by 5 residues(actual lengths 146 and 141 residues respectively). The major structuraldifference between alpha- and beta-forms is that beta-haemoglobins containan alpha-helix (the D helix) that is missing in alpha-forms.
  IPR002337:Beta haemoglobin
The globin-like family of proteins display the general structure of six helices in a partly opened.olded leaf topology. Members include the haemoglobins.hich occurs in all kingdoms of life. Vertebrate haemoglobins consist of a tetramer of alpha and beta chains .hile invertebrate haemoglobins can range from monomers to large multisubunit molecules. Different forms are found in bacteria (haemoglobins.runcated haemoglobins and flavohaemoglobins).lgae (truncated haemoglobin).rotozoa (truncated haemoglobin).lants (symbiotic haemoglobin and non-symbiotic leghaemoglobin).ematodes.nnelids (erythrocruorin).olluscs (haemoglobins I.I.nd III).nd crustaceans. Haemoglobins occur in red blood cells and in specific tissues. Vertebrate and many invertebrate haemoglobins function in oxygen transport. However.nvertebrate haemoglobins display a greater diversity of functional properties.ncluding roles in controlling nitric oxide levels in bacteria (flavohaemoglobins ).ydrogen sulphide binding in symbiotic molluscs (haemoglobin I ).xygen scavenging in plant roots to prevent the inhibition of nitrogen fixation in symbiotic bacteria (leghaemoglobin ).he detoxification of chlorinated material (dehaloperoxidase ).nd the phototrophism of worms. Several functionally different haemoglobins can coexist in the same species.Other globins include myoglobin in striated muscle and heart .he neuroprotective neuroglobin in vertebrates and nerve globin in invertebrates.he oxygen sensor cytoglobin.nd the phycobiliproteins (phycocyanin.llophycocyanin.hycoerythrin and phycoerythrocyanin) in red algae and cyanobacteria used for light-harvesting . Both the truncated haemoglobin and nerve globin lack the first helix found in other haemoglobins. The phycobiliproteins are oligomers of two different types of globin-like subunits that contain two extra helices at the N-terminus.nd which are use to bind a bilin chromophore.
  IPR009050:Globin-like
The globin-related family of proteins display the general structure of six helices in a partly opened.olded leaf topology that is found in the classical haem-binding globin family.uch as in haemoglobin.yoglobin.eghaemoglobin.rythrocruorin.lavohaemoglobin.ehaloperoxidase.nd others . This family also contains the truncated haemoglobins found in protozoa and bacteria that lack the first helix.nd neural globin that also lacks the first helix.ut which is closer to classical globins than the truncated ones .
  IPR012292:Globin-related
IPR000971:Globin 
Evalue:-58.8860549926758 
Location:7-141
SequencesProtein: HBB_HUMAN (146 aa)
mRNA: NM_000518
Local Annotation
Synapse Ontology
A process that increases long-term neuronal synaptic plasticity, the ability of neuronal synapses to change long-term as circumstances require. Long-term neuronal synaptic plasticity generally involves increase or decrease in actual synapse numbers.
sdb:0039 positive regulation of long-term neuronal synaptic plasticity  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 88 residues, 5203271-5203532Exon2: 76 residues, 5204382-5204605Exon3: 49 residues, 5204735-5204877Exon4: 2 residues, -Jump to HBB_HUMAN  
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