Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Hemoglobin subunit zeta

Gene

HBZ

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • heme binding Source: InterPro
  • iron ion binding Source: InterPro
  • oxygen binding Source: InterPro
  • oxygen transporter activity Source: ProtInc

GO - Biological processi

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 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:4835. HBZ.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • hemoglobin complex Source: ProtInc
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29212.

Polymorphism and mutation databases

DMDMi122335.

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
DOCK8Q8NF50-23EBI-719843,EBI-10174653
HBBP688712EBI-719843,EBI-715554
HBDP020423EBI-719843,EBI-6152722
KHDRBS2Q5VWX13EBI-719843,EBI-742808
KRT40Q6A1623EBI-719843,EBI-10171697
KRTAP10-7P604093EBI-719843,EBI-10172290
KRTAP10-9P604113EBI-719843,EBI-10172052
NOTCH2NLQ7Z3S93EBI-719843,EBI-945833

Protein-protein interaction databases

BioGridi109300. 18 interactions.
IntActiP02008. 13 interactions.
MINTiMINT-1416153.
STRINGi9606.ENSP00000252951.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000119197.
HOGENOMiHOG000036867.
HOVERGENiHBG009709.
InParanoidiP02008.
KOiK13826.
OMAiETHAAWD.
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

        10         20         30         40         50
MSLTKTERTI IVSMWAKIST QADTIGTETL ERLFLSHPQT KTYFPHFDLH
60 70 80 90 100
PGSAQLRAHG SKVVAAVGDA VKSIDDIGGA LSKLSELHAY ILRVDPVNFK
110 120 130 140
LLSHCLLVTL AARFPADFTA EAHAAWDKFL SVVSSVLTEK YR
Length:142
Mass (Da):15,637
Last modified:January 23, 2007 - v2
Checksum:iB62A9B825743A155
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_005255288.2.
UniGeneiHs.585357.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_005255288.2.
UniGeneiHs.585357.

3D structure databases

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

Protein-protein interaction databases

BioGridi109300. 18 interactions.
IntActiP02008. 13 interactions.
MINTiMINT-1416153.
STRINGi9606.ENSP00000252951.

PTM databases

PhosphoSiteiP02008.

Polymorphism and mutation databases

DMDMi122335.

Proteomic databases

MaxQBiP02008.
PaxDbiP02008.
PeptideAtlasiP02008.
PRIDEiP02008.

Protocols and materials databases

DNASUi3050.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3050.
GeneCardsiGC16P000202.
GeneReviewsiHBZ.
H-InvDBHIX0059565.
HGNCiHGNC:4835. HBZ.
MIMi142310. gene.
neXtProtiNX_P02008.
PharmGKBiPA29212.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG271358.
GeneTreeiENSGT00760000119197.
HOGENOMiHOG000036867.
HOVERGENiHBG009709.
InParanoidiP02008.
KOiK13826.
OMAiETHAAWD.
OrthoDBiEOG7KH9MP.
PhylomeDBiP02008.
TreeFamiTF332328.

Miscellaneous databases

EvolutionaryTraceiP02008.
GeneWikiiHBZ.
GenomeRNAii3050.
NextBioi12075.
PROiP02008.
SOURCEiSearch...

Gene expression databases

BgeeiP02008.
CleanExiHS_HBZ.
GenevestigatoriP02008.

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]
ProtoNetiSearch...

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: May 27, 2015
This is version 158 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.