Reviewed, UniProtKB/Swiss-Prot P02008 (HBAZ_HUMAN)

Names and origin

Protein names

Recommended name:
Hemoglobin subunit zeta

Alternative name(s):
Hemoglobin zeta chain
Zeta-globin
HBAZ

Gene names

Name:	HBZ
Synonyms:	HBZ2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	142 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	The zeta chain is an alpha-type chain of mammalian embryonic hemoglobin, synthesized primarily in the yolk sac.
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 hemoglobin Portland-1.
Tissue specificity	Red blood cells.
Sequence similarities	Belongs to the globin family.

Ontologies

Keywords
Biological process	Oxygen transport Transport
Ligand	Heme Iron Metal-binding
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	oxygen transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	hemoglobin complex Traceable author statement. Source: ProtInc
Molecular function	heme binding Inferred from electronic annotation. Source: InterPro oxygen binding Inferred from electronic annotation. Source: InterPro oxygen transporter activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.8 Ref.9

Chain

2 – 142

141

Hemoglobin subunit zeta

PRO_0000052851

Sites

Metal binding

59

1

Iron (heme distal ligand)

Metal binding

88

1

Iron (heme proximal ligand)

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.10

Secondary structure

1

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.

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.

.

142

Helix Strand Turn

Details...

Helix

5 – 18

14

Helix

22 – 36

15

Helix

38 – 43

6

Helix

54 – 72

19

Turn

73 – 75

3

Helix

77 – 80

4

Helix

82 – 90

9

Helix

97 – 113

17

Turn

115 – 117

3

Helix

120 – 138

19

Helix

139 – 141

3

Sequences

	Sequence		Length	Mass (Da)
	P02008-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: B62A9B825743A155	FASTA	142	15,637
	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

References

	« Hide 'large scale' referencesShow '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: 6297773] [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: 6963223] [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: 9054936] [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: 11157797] [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. , 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: 15489334] [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: 6179844] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-142.
[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: 6171809] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-142.
[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: 6172357] [Abstract] Cited for: ACETYLATION AT SER-2.
[11]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

GeneReviews

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.

IPI

IPI00217473.

PIR

HZHU. A90832.

RefSeq

NP_005323.1.

UniGene

Hs.585357

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JEB	X-ray	2.10	A/C	2-141	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P02008. 1 interaction.

STRING

P02008.

PTM databases

PhosphoSite

P02008.

Proteomic databases

PeptideAtlas

P02008.

PRIDE

P02008.

Genome annotation databases

Ensembl

ENST00000252951; ENSP00000252951; ENSG00000130656; Homo sapiens. [Genome view]

GeneID

3050.

KEGG

hsa:3050.

UCSC

uc002cft.1. human.

Organism-specific databases

CTD

3050.

GeneCards

GC16P000142.

H-InvDB

HIX0059559.

HGNC

HGNC:4835. HBZ.

MIM

142310. gene.

Orphanet

846. Alpha-thalassemia.
93615. Hemoglobin Constant Spring.
93616. Hemoglobin H disease.
163596. Hydrops fetalis of Barts.

PharmGKB

PA29212.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG20154.

HOGENOM

HBG715197.

HOVERGEN

HBG009709.

InParanoid

P02008.

OMA

LFASYPQ.

OrthoDB

EOG9X9B31.

Gene expression databases

ArrayExpress

P02008.

Bgee

P02008.

CleanEx

HS_HBZ.

Genevestigator

P02008.

GermOnline

ENSG00000130656. Homo sapiens.

Family and domain databases

InterPro

IPR009050. Globin-like.
IPR000971. Globin_subset.
IPR002338. Haemoglobin_a.
IPR002340. Haemoglobin_zeta.
[Graphical view]

Pfam

PF00042. Globin. 1 hit.
[Graphical view]

PRINTS

PR00612. ALPHAHAEM.
PR00816. ZETAHAEM.

SUPFAM

SSF46458. Globin_like. 1 hit.

PROSITE

PS01033. GLOBIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

12075.

SOURCE

Search...

Entry information

Entry name

HBAZ_HUMAN

Accession

Primary (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:	March 2, 2010
This is version 111 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.