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Protein

Hemoglobin subunit zeta

Gene

HBZ

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi59Iron (heme distal ligand)1
Metal bindingi88Iron (heme proximal ligand)1

GO - Molecular functioni

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

GO - Biological processi

Keywordsi

Biological processOxygen transport, Transport
LigandHeme, 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
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

EuPathDBiHostDB:ENSG00000130656.4
HGNCiHGNC:4835 HBZ
MIMi142310 gene
neXtProtiNX_P02008

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Pathology & Biotechi

Organism-specific databases

DisGeNETi3050
GeneReviewsiHBZ
MalaCardsiHBZ
OpenTargetsiENSG00000130656
PharmGKBiPA29212

Polymorphism and mutation databases

DMDMi122335

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved4 Publications
ChainiPRO_00000528512 – 142Hemoglobin subunit zetaAdd BLAST141

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine2 Publications1
Modified residuei29PhosphothreonineCombined sources1
Modified residuei53PhosphoserineCombined sources1
Modified residuei73PhosphoserineCombined sources1
Modified residuei82PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP02008
PaxDbiP02008
PeptideAtlasiP02008
PRIDEiP02008

PTM databases

iPTMnetiP02008
PhosphoSitePlusiP02008

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

BgeeiENSG00000130656
CleanExiHS_HBZ
GenevisibleiP02008 HS

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

Show more details

Protein-protein interaction databases

BioGridi10930023 interactors.
IntActiP02008 23 interactors.
STRINGi9606.ENSP00000252951

Structurei

Secondary structure

1142
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 19Combined sources15
Helixi22 – 36Combined sources15
Helixi38 – 43Combined sources6
Helixi54 – 72Combined sources19
Helixi74 – 76Combined sources3
Helixi77 – 80Combined sources4
Helixi82 – 89Combined sources8
Turni90 – 92Combined sources3
Helixi97 – 113Combined sources17
Turni115 – 117Combined sources3
Helixi120 – 137Combined sources18
Helixi139 – 141Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP02008

Family & Domainsi

Sequence similaritiesi

Belongs to the globin family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3378 Eukaryota
COG1018 LUCA
GeneTreeiENSGT00760000119197
HOGENOMiHOG000036867
HOVERGENiHBG009709
InParanoidiP02008
KOiK13826
OMAiHFDLHAG
OrthoDBiEOG091G0S0X
PhylomeDBiP02008
TreeFamiTF332328

Family and domain databases

CDDicd08927 Hb-alpha_like, 1 hit
Gene3Di1.10.490.101 hit
InterProiView protein in InterPro
IPR000971 Globin
IPR009050 Globin-like_sf
IPR012292 Globin/Proto
IPR002338 Haemoglobin_a-typ
IPR002340 Haemoglobin_zeta
PfamiView protein in Pfam
PF00042 Globin, 1 hit
PRINTSiPR00612 ALPHAHAEM
PR00816 ZETAHAEM
SUPFAMiSSF46458 SSF46458, 1 hit
PROSITEiView protein in PROSITE
PS01033 GLOBIN, 1 hit

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_005255288.3
UniGeneiHs.585357

Genome annotation databases

EnsembliENST00000252951; ENSP00000252951; ENSG00000130656
GeneIDi3050
KEGGihsa:3050
UCSCiuc002cft.2 human

Similar proteinsi

Entry informationi

Entry nameiHBAZ_HUMAN
AccessioniPrimary (citable) accession number: P02008
Secondary accession number(s): Q6IBF6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 25, 2018
This is version 180 of the entry and version 2 of the sequence. See 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