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P02008

- HBAZ_HUMAN

UniProt

P02008 - HBAZ_HUMAN

Protein

Hemoglobin subunit zeta

Gene

HBZ

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    The zeta chain is an alpha-type chain of mammalian embryonic hemoglobin.

    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: ProtInc
    5. protein binding Source: IntAct

    GO - Biological processi

    1. erythrocyte maturation Source: Ensembl
    2. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl

    Keywords - Biological processi

    Oxygen transport, Transport

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hemoglobin subunit zeta
    Alternative name(s):
    HBAZ
    Hemoglobin zeta chain
    Zeta-globin
    Gene namesi
    Name:HBZ
    Synonyms:HBZ2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:4835. HBZ.

    Subcellular locationi

    GO - Cellular componenti

    1. hemoglobin complex Source: ProtInc

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29212.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 142141Hemoglobin subunit zetaPRO_0000052851Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP02008.
    PaxDbiP02008.
    PeptideAtlasiP02008.
    PRIDEiP02008.

    PTM databases

    PhosphoSiteiP02008.

    Expressioni

    Tissue specificityi

    Detected in fetal erythrocytes (at protein level).2 Publications

    Developmental stagei

    Detected in the yolk sac of the early embryo and in erythrocytes from fetal umbilical cord blood. Detected at low levels after 10 weeks of gestation. Hemoglobin Portland levels are increased in fetuses with homozygous alpha-thalassemia, but it constitutes only a minor proportion of total hemoglobin and its levels decrease steadily after 10 weeks of gestation. Hemoglobin Portland-2 is detected in blood from still-born neoneates with homozygous alpha-thalassemia (at protein level).5 Publications

    Gene expression databases

    BgeeiP02008.
    CleanExiHS_HBZ.
    GenevestigatoriP02008.

    Interactioni

    Subunit structurei

    Heterotetramer of two zeta chains and two epsilon chains in early embryonic hemoglobin Gower-1; two zeta chains and two gamma chains in fetal hemoglobin Portland-1. Heterotetramer of two zeta chains and two beta chains in hemoglobin Portland-2, detected in fetuses and neonates with homozygous alpha-thalassemia.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HBBP688712EBI-719843,EBI-715554

    Protein-protein interaction databases

    BioGridi109300. 10 interactions.
    IntActiP02008. 6 interactions.
    MINTiMINT-1416153.
    STRINGi9606.ENSP00000252951.

    Structurei

    Secondary structure

    1
    142
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 1915
    Helixi22 – 3615
    Helixi38 – 436
    Helixi54 – 7219
    Helixi74 – 763
    Helixi77 – 804
    Helixi82 – 898
    Turni90 – 923
    Helixi97 – 11317
    Turni115 – 1173
    Helixi120 – 13718
    Helixi139 – 1413

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JEBX-ray2.10A/C2-142[»]
    3W4UX-ray1.95A/C/E1-142[»]
    ProteinModelPortaliP02008.
    SMRiP02008. Positions 2-142.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02008.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the globin family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG271358.
    HOGENOMiHOG000036867.
    HOVERGENiHBG009709.
    InParanoidiP02008.
    KOiK13826.
    OMAiVHAAWDK.
    OrthoDBiEOG7KH9MP.
    PhylomeDBiP02008.
    TreeFamiTF332328.

    Family and domain databases

    Gene3Di1.10.490.10. 1 hit.
    InterProiIPR000971. Globin.
    IPR009050. Globin-like.
    IPR012292. Globin_dom.
    IPR002338. Haemoglobin_a.
    IPR002340. Haemoglobin_zeta.
    [Graphical view]
    PfamiPF00042. Globin. 1 hit.
    [Graphical view]
    PRINTSiPR00612. ALPHAHAEM.
    PR00816. ZETAHAEM.
    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.

    P02008-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSLTKTERTI IVSMWAKIST QADTIGTETL ERLFLSHPQT KTYFPHFDLH    50
    PGSAQLRAHG SKVVAAVGDA VKSIDDIGGA LSKLSELHAY ILRVDPVNFK 100
    LLSHCLLVTL AARFPADFTA EAHAAWDKFL SVVSSVLTEK YR 142
    Length:142
    Mass (Da):15,637
    Last modified:January 23, 2007 - v2
    Checksum:iB62A9B825743A155
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J00182 Genomic DNA. Translation: AAB59406.1.
    M24173 mRNA. Translation: AAA61306.1.
    Z84721 Genomic DNA. Translation: CAB06552.1.
    CR456848 mRNA. Translation: CAG33129.1.
    AE006462 Genomic DNA. Translation: AAK61214.1.
    CH471112 Genomic DNA. Translation: EAW85864.1.
    BC027892 mRNA. Translation: AAH27892.1.
    CCDSiCCDS10397.1.
    PIRiA90832. HZHU.
    RefSeqiNP_005323.1. NM_005332.2.
    XP_005255345.1. XM_005255288.1.
    UniGeneiHs.585357.

    Genome annotation databases

    EnsembliENST00000252951; ENSP00000252951; ENSG00000130656.
    GeneIDi3050.
    KEGGihsa:3050.
    UCSCiuc002cft.1. human.

    Polymorphism databases

    DMDMi122335.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J00182 Genomic DNA. Translation: AAB59406.1 .
    M24173 mRNA. Translation: AAA61306.1 .
    Z84721 Genomic DNA. Translation: CAB06552.1 .
    CR456848 mRNA. Translation: CAG33129.1 .
    AE006462 Genomic DNA. Translation: AAK61214.1 .
    CH471112 Genomic DNA. Translation: EAW85864.1 .
    BC027892 mRNA. Translation: AAH27892.1 .
    CCDSi CCDS10397.1.
    PIRi A90832. HZHU.
    RefSeqi NP_005323.1. NM_005332.2.
    XP_005255345.1. XM_005255288.1.
    UniGenei Hs.585357.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JEB X-ray 2.10 A/C 2-142 [» ]
    3W4U X-ray 1.95 A/C/E 1-142 [» ]
    ProteinModelPortali P02008.
    SMRi P02008. Positions 2-142.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109300. 10 interactions.
    IntActi P02008. 6 interactions.
    MINTi MINT-1416153.
    STRINGi 9606.ENSP00000252951.

    PTM databases

    PhosphoSitei P02008.

    Polymorphism databases

    DMDMi 122335.

    Proteomic databases

    MaxQBi P02008.
    PaxDbi P02008.
    PeptideAtlasi P02008.
    PRIDEi P02008.

    Protocols and materials databases

    DNASUi 3050.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000252951 ; ENSP00000252951 ; ENSG00000130656 .
    GeneIDi 3050.
    KEGGi hsa:3050.
    UCSCi uc002cft.1. human.

    Organism-specific databases

    CTDi 3050.
    GeneCardsi GC16P000202.
    GeneReviewsi HBZ.
    H-InvDB HIX0059565.
    HGNCi HGNC:4835. HBZ.
    MIMi 142310. gene.
    neXtProti NX_P02008.
    PharmGKBi PA29212.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG271358.
    HOGENOMi HOG000036867.
    HOVERGENi HBG009709.
    InParanoidi P02008.
    KOi K13826.
    OMAi VHAAWDK.
    OrthoDBi EOG7KH9MP.
    PhylomeDBi P02008.
    TreeFami TF332328.

    Miscellaneous databases

    EvolutionaryTracei P02008.
    GeneWikii HBZ.
    GenomeRNAii 3050.
    NextBioi 12075.
    PROi P02008.
    SOURCEi Search...

    Gene expression databases

    Bgeei P02008.
    CleanExi HS_HBZ.
    Genevestigatori P02008.

    Family and domain databases

    Gene3Di 1.10.490.10. 1 hit.
    InterProi IPR000971. Globin.
    IPR009050. Globin-like.
    IPR012292. Globin_dom.
    IPR002338. Haemoglobin_a.
    IPR002340. Haemoglobin_zeta.
    [Graphical view ]
    Pfami PF00042. Globin. 1 hit.
    [Graphical view ]
    PRINTSi PR00612. ALPHAHAEM.
    PR00816. ZETAHAEM.
    SUPFAMi SSF46458. SSF46458. 1 hit.
    PROSITEi PS01033. GLOBIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The structure of the human zeta-globin gene and a closely linked, nearly identical pseudogene."
      Proudfoot N.J., Gil A., Maniatis T.
      Cell 31:553-563(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Cloning and nucleotide sequence analysis of human embryonic zeta-globin cDNA."
      Cohen-Solal M., Authier B., Deriel J.K., Murnane M.J., Forget B.G.
      DNA 1:355-363(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "The relationship between chromosome structure and function at a human telomeric region."
      Flint J., Thomas K., Micklem G., Raynham H., Clark K., Doggett N.A., King A., Higgs D.R.
      Nat. Genet. 15:252-257(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16."
      Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.
      Hum. Mol. Genet. 10:339-352(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Pancreas and Spleen.
    8. "Human embryonic haemoglobins. The primary structure of the zeta chains."
      Aschauer H., Sanguansermsri T., Braunitzer G.
      Hoppe-Seyler's Z. Physiol. Chem. 362:1159-1162(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-142, DEVELOPMENTAL STAGE.
    9. "Structure of the zeta chain of human embryonic hemoglobin."
      Clegg J.B., Gagnon J.
      Proc. Natl. Acad. Sci. U.S.A. 78:6076-6080(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-142, DEVELOPMENTAL STAGE, SUBUNIT, TISSUE SPECIFICITY.
    10. "Human embryonic haemoglobins. Ac-Ser-Leu-Thr-is the N-terminal sequence of the zeta-chains."
      Aschauer H., Schaefer W., Sanguansermsri T., Braunitzer G.
      Hoppe-Seyler's Z. Physiol. Chem. 362:1657-1659(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT SER-2.
    11. "Human hemoglobin Portland II (zeta 2 beta 2). Isolation and characterization of Portland hemoglobin components and their constituent globin chains."
      Randhawa Z.I., Jones R.T., Lie-Injo L.E.
      J. Biol. Chem. 259:7325-7330(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
    12. "Quantities of adult, fetal and embryonic globin chains in the blood of eighteen- to twenty-week-old human fetuses."
      Kutlar F., Moscoso H., Kiefer C.R., Garver F.A., Beksac S., Onderoglu L., Gurgey A., Altay C., Huisman T.H.
      J. Chromatogr. B 567:359-368(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.
    13. "Haemoglobin level, proportion of haemoglobin Bart's and haemoglobin Portland in fetuses affected by homozygous alpha0-thalassemia from 12 to 40 weeks' gestation."
      Li T.K., Leung K.Y., Lam Y.H., Tang M.H., Chan V.
      Prenat. Diagn. 30:1126-1130(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, DEVELOPMENTAL STAGE.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "The role of beta chains in the control of the hemoglobin oxygen binding function: chimeric human/mouse proteins, structure, and function."
      Kidd R.D., Russell J.E., Watmough N.J., Baker E.N., Brittain T.
      Biochemistry 40:15669-15675(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH HEME AND MOUSE HBB, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, SUBUNIT.
    16. "Structure of fully liganded Hb zeta2beta2s trapped in a tense conformation."
      Safo M.K., Ko T.P., Abdulmalik O., He Z., Wang A.H., Schreiter E.R., Russell J.E.
      Acta Crystallogr. D 69:2061-2071(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH HEME; CARBON MONOXIDE AND HBB, SUBUNIT.

    Entry informationi

    Entry nameiHBAZ_HUMAN
    AccessioniPrimary (citable) accession number: P02008
    Secondary accession number(s): Q6IBF6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 152 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3