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P02008 (HBAZ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hemoglobin subunit zeta
Alternative name(s):
HBAZ
Hemoglobin zeta chain
Zeta-globin
Gene names
Name:HBZ
Synonyms:HBZ2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length142 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

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. Ref.9 Ref.11 Ref.13 Ref.15 Ref.16

Tissue specificity

Detected in fetal erythrocytes (at protein level). Ref.9 Ref.11

Developmental stage

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). Ref.8 Ref.9 Ref.11 Ref.12 Ref.13

Sequence similarities

Belongs to the globin family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HBBP688712EBI-719843,EBI-715554

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8 Ref.9 Ref.15
Chain2 – 142141Hemoglobin subunit zeta
PRO_0000052851

Sites

Metal binding591Iron (heme distal ligand)
Metal binding881Iron (heme proximal ligand)

Amino acid modifications

Modified residue21N-acetylserine Ref.10 Ref.15

Secondary structure

....................... 142
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02008 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: B62A9B825743A155

FASTA14215,637
        10         20         30         40         50         60 
MSLTKTERTI IVSMWAKIST QADTIGTETL ERLFLSHPQT KTYFPHFDLH PGSAQLRAHG 

        70         80         90        100        110        120 
SKVVAAVGDA VKSIDDIGGA LSKLSELHAY ILRVDPVNFK LLSHCLLVTL AARFPADFTA 

       130        140 
EAHAAWDKFL SVVSSVLTEK YR 

« Hide

References

« Hide 'large scale' references
[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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS10397.1.
PIRHZHU. A90832.
RefSeqNP_005323.1. NM_005332.2.
XP_005255345.1. XM_005255288.1.
UniGeneHs.585357.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JEBX-ray2.10A/C2-142[»]
3W4UX-ray1.95A/C/E1-142[»]
ProteinModelPortalP02008.
SMRP02008. Positions 2-142.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109300. 10 interactions.
IntActP02008. 6 interactions.
MINTMINT-1416153.
STRING9606.ENSP00000252951.

PTM databases

PhosphoSiteP02008.

Polymorphism databases

DMDM122335.

Proteomic databases

MaxQBP02008.
PaxDbP02008.
PeptideAtlasP02008.
PRIDEP02008.

Protocols and materials databases

DNASU3050.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000252951; ENSP00000252951; ENSG00000130656.
GeneID3050.
KEGGhsa:3050.
UCSCuc002cft.1. human.

Organism-specific databases

CTD3050.
GeneCardsGC16P000202.
GeneReviewsHBZ.
H-InvDBHIX0059565.
HGNCHGNC:4835. HBZ.
MIM142310. gene.
neXtProtNX_P02008.
PharmGKBPA29212.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG271358.
HOGENOMHOG000036867.
HOVERGENHBG009709.
InParanoidP02008.
KOK13826.
OMAVHAAWDK.
OrthoDBEOG7KH9MP.
PhylomeDBP02008.
TreeFamTF332328.

Gene expression databases

BgeeP02008.
CleanExHS_HBZ.
GenevestigatorP02008.

Family and domain databases

Gene3D1.10.490.10. 1 hit.
InterProIPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin_dom.
IPR002338. Haemoglobin_a.
IPR002340. Haemoglobin_zeta.
[Graphical view]
PfamPF00042. Globin. 1 hit.
[Graphical view]
PRINTSPR00612. ALPHAHAEM.
PR00816. ZETAHAEM.
SUPFAMSSF46458. SSF46458. 1 hit.
PROSITEPS01033. GLOBIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP02008.
GeneWikiHBZ.
GenomeRNAi3050.
NextBio12075.
PROP02008.
SOURCESearch...

Entry information

Entry nameHBAZ_HUMAN
AccessionPrimary (citable) accession number: P02008
Secondary accession number(s): Q6IBF6
Entry history
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 statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM