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P02008

- HBAZ_HUMAN

UniProt

P02008 - HBAZ_HUMAN

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Protein

Hemoglobin subunit zeta

Gene
HBZ, HBZ2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29212.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 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.

Miscellaneous databases

EvolutionaryTraceiP02008.

Family & Domainsi

Sequence similaritiesi

Belongs to the globin family.

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 151 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

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