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Protein

Hemoglobin subunit gamma-2

Gene

HBG2

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

Functioni

Gamma chains make up the fetal hemoglobin F, in combination with alpha chains.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi64Iron (heme distal ligand)By similarity1
Metal bindingi93Iron (heme proximal ligand)Combined sources1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywordsi

Biological processOxygen transport, Transport
LigandHeme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:G66-32215-MONOMER.
ReactomeiR-HSA-983231. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
Hemoglobin subunit gamma-2
Alternative name(s):
Gamma-2-globin
Hb F Ggamma
Hemoglobin gamma-2 chain
Hemoglobin gamma-G chain
Gene namesi
Name:HBG2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:4832. HBG2.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • cytosol Source: Reactome
  • hemoglobin complex Source: InterPro

Pathology & Biotechi

Involvement in diseasei

Cyanosis transient neonatal (TNCY)6 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by cyanosis in the fetus and neonate, due to a defect in the fetal hemoglobin chain which has reduced affinity for oxygen. Some patients develop anemia resulting from increased destruction of red cells containing abnormal or unstable hemoglobin. The cyanosis resolves spontaneously by 5 to 6 months of age or earlier, as the adult beta-globin chain is produced and replaces the fetal gamma-globin chain.
See also OMIM:613977
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00314642F → S in TNCY; hemoglobin Cincinnati. Corresponds to variant dbSNP:rs348789131 PublicationEnsembl.1
Natural variantiVAR_02533664H → L in TNCY; hemoglobin M-Circleville. 2 Publications1
Natural variantiVAR_00315464H → Y in TNCY; hemoglobin Osaka; the presence of a tyrosine causes the formation of a covalent link with heme iron, so that the iron is stabilized in the ferric form; when this occurs methemoglobin is formed, oxygen can no longer bind to heme and cyanosis occurs. Corresponds to variant dbSNP:rs344741042 PublicationsEnsembl.1
Natural variantiVAR_06595068V → M in TNCY; hemoglobin Toms River; the side chain of methionine decreases both the affinity of oxygen for binding to the mutant hemoglobin subunit via steric hindrance and the rate at which it does so; the mutant methionine is converted to aspartic acid post-translationally. Corresponds to variant dbSNP:rs5877768641 PublicationEnsembl.1
Natural variantiVAR_00316693H → Y in TNCY; hemoglobin Fort Ripley. Corresponds to variant dbSNP:rs351034591 PublicationEnsembl.1
Natural variantiVAR_073159106L → H in TNCY; hemoglobin F-Brugine/Feldkirch; lowered affinity for oxygen. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi3048.
MalaCardsiHBG2.
MIMi613977. phenotype.
OpenTargetsiENSG00000196565.
Orphaneti280615. Hemoglobinopathy Toms River.
46532. Hereditary persistence of fetal hemoglobin - beta-thalassemia.
251380. Hereditary persistence of fetal hemoglobin - sickle cell disease.
PharmGKBiPA29207.

Polymorphism and mutation databases

BioMutaiHBG2.
DMDMi56749861.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved3 Publications
ChainiPRO_00000532542 – 147Hemoglobin subunit gamma-2Add BLAST146

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylglycine; in form Hb F11 Publication1
Modified residuei45PhosphoserineCombined sources1
Modified residuei51PhosphoserineCombined sources1
Modified residuei53PhosphoserineCombined sources1
Modified residuei140PhosphoserineCombined sources1
Modified residuei143PhosphoserineCombined sources1
Modified residuei144PhosphoserineCombined sources1

Post-translational modificationi

Acetylation of Gly-2 converts Hb F to the minor Hb F1.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP69892.
MaxQBiP69892.
PaxDbiP69892.
PeptideAtlasiP69892.
PRIDEiP69892.

PTM databases

iPTMnetiP69892.
PhosphoSitePlusiP69892.

Expressioni

Tissue specificityi

Red blood cells.

Developmental stagei

Expressed until four or five weeks after birth.

Gene expression databases

BgeeiENSG00000196565.
CleanExiHS_HBG2.
ExpressionAtlasiP69892. baseline and differential.
GenevisibleiP69892. HS.

Organism-specific databases

HPAiCAB016143.
HPA043234.

Interactioni

Subunit structurei

Heterotetramer of two alpha chains and two gamma chains in fetal hemoglobin (Hb F).1 Publication

Protein-protein interaction databases

BioGridi109298. 8 interactors.
IntActiP69892. 7 interactors.
MINTiMINT-1200269.
STRINGi9606.ENSP00000338082.

Structurei

Secondary structure

1147
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 18Combined sources13
Helixi21 – 35Combined sources15
Helixi37 – 42Combined sources6
Helixi44 – 46Combined sources3
Helixi52 – 56Combined sources5
Helixi59 – 76Combined sources18
Helixi77 – 81Combined sources5
Helixi82 – 85Combined sources4
Helixi87 – 95Combined sources9
Helixi102 – 119Combined sources18
Helixi120 – 122Combined sources3
Helixi125 – 142Combined sources18
Helixi143 – 146Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FDHX-ray2.50G/H2-147[»]
4MQJX-ray1.80B/D/F/H3-147[»]
4MQKX-ray2.24B/D/F/H2-147[»]
ProteinModelPortaliP69892.
SMRiP69892.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP69892.

Family & Domainsi

Sequence similaritiesi

Belongs to the globin family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3378. Eukaryota.
COG1018. LUCA.
GeneTreeiENSGT00760000119197.
HOVERGENiHBG009709.
InParanoidiP69892.
KOiK13824.
PhylomeDBiP69892.
TreeFamiTF333268.

Family and domain databases

CDDicd08925. Hb-beta_like. 1 hit.
Gene3Di1.10.490.10. 1 hit.
InterProiIPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin/Proto.
IPR002337. Haemoglobin_b.
[Graphical view]
PfamiPF00042. Globin. 1 hit.
[Graphical view]
PRINTSiPR00814. BETAHAEM.
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.

P69892-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGHFTEEDKA TITSLWGKVN VEDAGGETLG RLLVVYPWTQ RFFDSFGNLS
60 70 80 90 100
SASAIMGNPK VKAHGKKVLT SLGDAIKHLD DLKGTFAQLS ELHCDKLHVD
110 120 130 140
PENFKLLGNV LVTVLAIHFG KEFTPEVQAS WQKMVTGVAS ALSSRYH
Length:147
Mass (Da):16,126
Last modified:January 23, 2007 - v2
Checksum:i8FCDC4441B416DDE
GO

Sequence cautioni

The sequence AAB50159 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0031232G → C in Malaysia. Corresponds to variant dbSNP:rs360061951 PublicationEnsembl.1
Natural variantiVAR_0031266E → G in Meinohama. Corresponds to variant dbSNP:rs342638261 PublicationEnsembl.1
Natural variantiVAR_0031298D → N in Auckland. Corresponds to variant dbSNP:rs345015931 PublicationEnsembl.1
Natural variantiVAR_0206439K → E in Albaicin. Corresponds to variant dbSNP:rs355218131 PublicationEnsembl.1
Natural variantiVAR_0206449K → Q in Albaicin. Corresponds to variant dbSNP:rs355218131 PublicationEnsembl.1
Natural variantiVAR_02064513T → R in Heather. Corresponds to variant dbSNP:rs281864890Ensembl.1
Natural variantiVAR_00313116W → R in Catalonia. Corresponds to variant dbSNP:rs344389811 PublicationEnsembl.1
Natural variantiVAR_00313217G → R in Melbourne. Corresponds to variant dbSNP:rs349076541 PublicationEnsembl.1
Natural variantiVAR_02064618K → N in Clamart. Corresponds to variant dbSNP:rs356213901 PublicationEnsembl.1
Natural variantiVAR_02064720N → K in Ouled Rabah. Corresponds to variant dbSNP:rs340187991 PublicationEnsembl.1
Natural variantiVAR_03049621V → A in Bron. Corresponds to variant dbSNP:rs637511961 PublicationEnsembl.1
Natural variantiVAR_00313322E → K in Saskatoon. Corresponds to variant dbSNP:rs339553301 PublicationEnsembl.1
Natural variantiVAR_00313422E → Q in Fuchu. Corresponds to variant dbSNP:rs339553301 PublicationEnsembl.1
Natural variantiVAR_02064823D → G in Urumqi. Corresponds to variant dbSNP:rs2818648912 PublicationsEnsembl.1
Natural variantiVAR_00313623D → V in Granada. Corresponds to variant dbSNP:rs2818648911 PublicationEnsembl.1
Natural variantiVAR_00313726G → E in Cosenza. Corresponds to variant dbSNP:rs356873961 PublicationEnsembl.1
Natural variantiVAR_00313927E → K in Oakland. Corresponds to variant dbSNP:rs356543281 PublicationEnsembl.1
Natural variantiVAR_00314035V → I in Tokyo. Corresponds to variant dbSNP:rs358857831 PublicationEnsembl.1
Natural variantiVAR_03049739T → P in Bonheiden; causes severe hereditary hemolytic anemia. Corresponds to variant dbSNP:rs357990581 PublicationEnsembl.1
Natural variantiVAR_00314441R → G in Veleta. Corresponds to variant dbSNP:rs34532478Ensembl.1
Natural variantiVAR_02064941R → K in Austell. Corresponds to variant dbSNP:rs2818648921 PublicationEnsembl.1
Natural variantiVAR_00314642F → S in TNCY; hemoglobin Cincinnati. Corresponds to variant dbSNP:rs348789131 PublicationEnsembl.1
Natural variantiVAR_00314845S → R in Lodz. Corresponds to variant dbSNP:rs340174501 PublicationEnsembl.1
Natural variantiVAR_00315056M → R in Kingston. Corresponds to variant dbSNP:rs349153111 PublicationEnsembl.1
Natural variantiVAR_00315160K → E in Emirates. Corresponds to variant dbSNP:rs289330781 PublicationEnsembl.1
Natural variantiVAR_00315260K → Q in Sacromonte. Corresponds to variant dbSNP:rs289330781 PublicationEnsembl.1
Natural variantiVAR_02533664H → L in TNCY; hemoglobin M-Circleville. 2 Publications1
Natural variantiVAR_00315464H → Y in TNCY; hemoglobin Osaka; the presence of a tyrosine causes the formation of a covalent link with heme iron, so that the iron is stabilized in the ferric form; when this occurs methemoglobin is formed, oxygen can no longer bind to heme and cyanosis occurs. Corresponds to variant dbSNP:rs344741042 PublicationsEnsembl.1
Natural variantiVAR_00315566K → N in Clarke. Corresponds to variant dbSNP:rs340195071 PublicationEnsembl.1
Natural variantiVAR_00315767K → Q in Brooklyn. Corresponds to variant dbSNP:rs342646941 PublicationEnsembl.1
Natural variantiVAR_00315667K → R in Shanghai. Corresponds to variant dbSNP:rs354818661 PublicationEnsembl.1
Natural variantiVAR_06595068V → M in TNCY; hemoglobin Toms River; the side chain of methionine decreases both the affinity of oxygen for binding to the mutant hemoglobin subunit via steric hindrance and the rate at which it does so; the mutant methionine is converted to aspartic acid post-translationally. Corresponds to variant dbSNP:rs5877768641 PublicationEnsembl.1
Natural variantiVAR_02065073G → R in Minoo. Corresponds to variant dbSNP:rs2818605941 PublicationEnsembl.1
Natural variantiVAR_02065176I → T in LesVos/Waynesboro/Charlotte. Corresponds to variant dbSNP:rs10612343 PublicationsEnsembl.1
Natural variantiVAR_03049876I → V in Coigneres. Corresponds to variant dbSNP:rs343631111 PublicationEnsembl.1
Natural variantiVAR_00316278H → R in Kennestone. Corresponds to variant dbSNP:rs341503061 PublicationEnsembl.1
Natural variantiVAR_02065281D → N in Marietta. Corresponds to variant dbSNP:rs63751148Ensembl.1
Natural variantiVAR_00316693H → Y in TNCY; hemoglobin Fort Ripley. Corresponds to variant dbSNP:rs351034591 PublicationEnsembl.1
Natural variantiVAR_00316795D → N in Columbus-Ga. Corresponds to variant dbSNP:rs358125141 PublicationEnsembl.1
Natural variantiVAR_003169102E → K in La Grange. Corresponds to variant dbSNP:rs348762381 PublicationEnsembl.1
Natural variantiVAR_003170105K → N in Macedonia-II. Corresponds to variant dbSNP:rs357178541 PublicationEnsembl.1
Natural variantiVAR_073159106L → H in TNCY; hemoglobin F-Brugine/Feldkirch; lowered affinity for oxygen. 1 Publication1
Natural variantiVAR_003171118H → R in Malta-1. Corresponds to variant dbSNP:rs360490741 PublicationEnsembl.1
Natural variantiVAR_015740119F → L in Calabria. Corresponds to variant dbSNP:rs350202531 PublicationEnsembl.1
Natural variantiVAR_003172121K → Q in Caltech. Corresponds to variant dbSNP:rs347035191 PublicationEnsembl.1
Natural variantiVAR_020653122E → K in Carlton. Corresponds to variant dbSNP:rs637500211 PublicationEnsembl.1
Natural variantiVAR_003174126E → A in Port-Royal. Corresponds to variant dbSNP:rs349979021 PublicationEnsembl.1
Natural variantiVAR_003176131W → G in Poole; unstable. Corresponds to variant dbSNP:rs358267801 PublicationEnsembl.1
Natural variantiVAR_003179147H → Y in Onoda; O(2) affinity up. Corresponds to variant dbSNP:rs348076711 PublicationEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M91036 Genomic DNA. Translation: AAB59428.1.
M91037 Genomic DNA. Translation: AAA58492.1.
U01317 Genomic DNA. Translation: AAA16331.1.
V00515 Genomic DNA. Translation: CAA23773.1.
M15386 mRNA. Translation: AAB50159.1. Different initiation.
AY662983 Genomic DNA. Translation: AAT98611.1.
AK290492 mRNA. Translation: BAF83181.1.
BC010914 mRNA. Translation: AAH10914.1.
BC029387 mRNA. Translation: AAH29387.1.
BC130457 mRNA. Translation: AAI30458.1.
BC130459 mRNA. Translation: AAI30460.1.
M11427 mRNA. Translation: AAA35957.1.
CCDSiCCDS7755.1.
PIRiA90803. HGHUA.
RefSeqiNP_000175.1. NM_000184.2.
UniGeneiHs.302145.
Hs.702189.

Genome annotation databases

EnsembliENST00000336906; ENSP00000338082; ENSG00000196565.
ENST00000380259; ENSP00000369609; ENSG00000196565.
GeneIDi3048.
KEGGihsa:3048.
UCSCiuc001maj.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

HbVar

Human hemoglobin variants and thalassemias

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M91036 Genomic DNA. Translation: AAB59428.1.
M91037 Genomic DNA. Translation: AAA58492.1.
U01317 Genomic DNA. Translation: AAA16331.1.
V00515 Genomic DNA. Translation: CAA23773.1.
M15386 mRNA. Translation: AAB50159.1. Different initiation.
AY662983 Genomic DNA. Translation: AAT98611.1.
AK290492 mRNA. Translation: BAF83181.1.
BC010914 mRNA. Translation: AAH10914.1.
BC029387 mRNA. Translation: AAH29387.1.
BC130457 mRNA. Translation: AAI30458.1.
BC130459 mRNA. Translation: AAI30460.1.
M11427 mRNA. Translation: AAA35957.1.
CCDSiCCDS7755.1.
PIRiA90803. HGHUA.
RefSeqiNP_000175.1. NM_000184.2.
UniGeneiHs.302145.
Hs.702189.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FDHX-ray2.50G/H2-147[»]
4MQJX-ray1.80B/D/F/H3-147[»]
4MQKX-ray2.24B/D/F/H2-147[»]
ProteinModelPortaliP69892.
SMRiP69892.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109298. 8 interactors.
IntActiP69892. 7 interactors.
MINTiMINT-1200269.
STRINGi9606.ENSP00000338082.

PTM databases

iPTMnetiP69892.
PhosphoSitePlusiP69892.

Polymorphism and mutation databases

BioMutaiHBG2.
DMDMi56749861.

Proteomic databases

EPDiP69892.
MaxQBiP69892.
PaxDbiP69892.
PeptideAtlasiP69892.
PRIDEiP69892.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000336906; ENSP00000338082; ENSG00000196565.
ENST00000380259; ENSP00000369609; ENSG00000196565.
GeneIDi3048.
KEGGihsa:3048.
UCSCiuc001maj.2. human.

Organism-specific databases

CTDi3048.
DisGeNETi3048.
GeneCardsiHBG2.
HGNCiHGNC:4832. HBG2.
HPAiCAB016143.
HPA043234.
MalaCardsiHBG2.
MIMi142250. gene.
613977. phenotype.
neXtProtiNX_P69892.
OpenTargetsiENSG00000196565.
Orphaneti280615. Hemoglobinopathy Toms River.
46532. Hereditary persistence of fetal hemoglobin - beta-thalassemia.
251380. Hereditary persistence of fetal hemoglobin - sickle cell disease.
PharmGKBiPA29207.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3378. Eukaryota.
COG1018. LUCA.
GeneTreeiENSGT00760000119197.
HOVERGENiHBG009709.
InParanoidiP69892.
KOiK13824.
PhylomeDBiP69892.
TreeFamiTF333268.

Enzyme and pathway databases

BioCyciZFISH:G66-32215-MONOMER.
ReactomeiR-HSA-983231. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

ChiTaRSiHBG2. human.
EvolutionaryTraceiP69892.
GeneWikiiHBG2.
GenomeRNAii3048.
PROiP69892.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000196565.
CleanExiHS_HBG2.
ExpressionAtlasiP69892. baseline and differential.
GenevisibleiP69892. HS.

Family and domain databases

CDDicd08925. Hb-beta_like. 1 hit.
Gene3Di1.10.490.10. 1 hit.
InterProiIPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin/Proto.
IPR002337. Haemoglobin_b.
[Graphical view]
PfamiPF00042. Globin. 1 hit.
[Graphical view]
PRINTSiPR00814. BETAHAEM.
SUPFAMiSSF46458. SSF46458. 1 hit.
PROSITEiPS01033. GLOBIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHBG2_HUMAN
AccessioniPrimary (citable) accession number: P69892
Secondary accession number(s): A8MZE0
, P02096, P62027, Q14491, Q68NH9, Q96FH6, Q96FH7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 134 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

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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 one 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.