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P01959

- HBA_EQUAS

UniProt

P01959 - HBA_EQUAS

Protein

Hemoglobin subunit alpha

Gene

HBA1

more
Organism
Equus asinus (Donkey)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi59 – 591Iron (heme distal ligand)
    Metal bindingi88 – 881Iron (heme proximal ligand)

    GO - Molecular functioni

    1. heme binding Source: InterPro
    2. iron ion binding Source: InterPro
    3. oxygen binding Source: InterPro
    4. oxygen transporter activity Source: UniProtKB-KW

    Keywords - Biological processi

    Oxygen transport, Transport

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hemoglobin subunit alpha
    Alternative name(s):
    Alpha-globin
    Hemoglobin alpha chain
    Gene namesi
    Name:HBA1
    AND
    Name:HBA2
    OrganismiEquus asinus (Donkey)
    Taxonomic identifieri9793 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaPerissodactylaEquidaeEquus

    Subcellular locationi

    GO - Cellular componenti

    1. hemoglobin complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 142141Hemoglobin subunit alphaPRO_0000052624Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei8 – 81N6-succinyllysineBy similarity
    Modified residuei12 – 121N6-succinyllysineBy similarity
    Modified residuei17 – 171N6-acetyllysine; alternateBy similarity
    Modified residuei17 – 171N6-succinyllysine; alternateBy similarity
    Modified residuei41 – 411N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Expressioni

    Tissue specificityi

    Red blood cells.

    Interactioni

    Subunit structurei

    Heterotetramer of two alpha chains and two beta chains.

    Structurei

    Secondary structure

    1
    142
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 1814
    Helixi19 – 213
    Helixi22 – 3615
    Helixi38 – 436
    Helixi54 – 7219
    Helixi74 – 763
    Helixi77 – 804
    Helixi82 – 887
    Turni89 – 924
    Helixi97 – 11317
    Turni115 – 1173
    Helixi120 – 13617
    Turni137 – 1415

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1S0HX-ray3.00A2-142[»]
    ProteinModelPortaliP01959.
    SMRiP01959. Positions 2-142.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP01959.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the globin family.PROSITE-ProRule annotation

    Phylogenomic databases

    HOVERGENiHBG009709.

    Family and domain databases

    Gene3Di1.10.490.10. 1 hit.
    InterProiIPR000971. Globin.
    IPR009050. Globin-like.
    IPR012292. Globin_dom.
    IPR002338. Haemoglobin_a.
    IPR002339. Haemoglobin_pi.
    [Graphical view]
    PfamiPF00042. Globin. 1 hit.
    [Graphical view]
    PRINTSiPR00612. ALPHAHAEM.
    PR00815. PIHAEM.
    SUPFAMiSSF46458. SSF46458. 1 hit.
    PROSITEiPS01033. GLOBIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P01959-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVLSAADKTN VKAAWSKVGG NAGEFGAEAL ERMFLGFPTT KTYFPHFDLS    50
    HGSAQVKAHG KKVGDALTLA VGHLDDLPGA LSNLSDLHAH KLRVDPVNFK 100
    LLSHCLLSTL AVHLPNDFTP AVHASLDKFL STVSTVLTSK YR 142
    Length:142
    Mass (Da):15,220
    Last modified:January 23, 2007 - v3
    Checksum:i93B837BC15C1D175
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti132 – 1321T → S AA sequence (PubMed:6030605)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U69894 Genomic DNA. Translation: AAD13640.1.
    U69895 Genomic DNA. Translation: AAD13641.1.
    PIRiA02282. HAHOD.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U69894 Genomic DNA. Translation: AAD13640.1 .
    U69895 Genomic DNA. Translation: AAD13641.1 .
    PIRi A02282. HAHOD.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1S0H X-ray 3.00 A 2-142 [» ]
    ProteinModelPortali P01959.
    SMRi P01959. Positions 2-142.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG009709.

    Miscellaneous databases

    EvolutionaryTracei P01959.

    Family and domain databases

    Gene3Di 1.10.490.10. 1 hit.
    InterProi IPR000971. Globin.
    IPR009050. Globin-like.
    IPR012292. Globin_dom.
    IPR002338. Haemoglobin_a.
    IPR002339. Haemoglobin_pi.
    [Graphical view ]
    Pfami PF00042. Globin. 1 hit.
    [Graphical view ]
    PRINTSi PR00612. ALPHAHAEM.
    PR00815. PIHAEM.
    SUPFAMi SSF46458. SSF46458. 1 hit.
    PROSITEi PS01033. GLOBIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Phylogenetic relationships within the genus Equus and the evolution of alpha and theta globin genes."
      Oakenfull E.A., Clegg J.B.
      J. Mol. Evol. 47:772-783(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA1 AND HBA2).
    2. "Amino-acid replacements in horse haemoglobin."
      Kilmartin J.V., Clegg J.B.
      Nature 213:269-271(1967) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-142.
    3. "Crystal structure of haemoglobin from donkey (Equus asinus) at 3A resolution."
      Balasundaresan D., Saraboji K., Ponnuswamy M.N.
      Biochimie 88:719-723(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).

    Entry informationi

    Entry nameiHBA_EQUAS
    AccessioniPrimary (citable) accession number: P01959
    Secondary accession number(s): P82988
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 91 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3