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Protein

Hemoglobin subunit gamma-2

Gene

HBG2

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

  • heme binding Source: GO_Central
  • metal ion binding Source: UniProtKB-KW
  • organic acid binding Source: GO_Central
  • oxygen binding Source: GO_Central
  • oxygen carrier activity Source: GO_Central

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

ReactomeiR-HSA-983231 Factors involved in megakaryocyte development and platelet production
SIGNORiP69892

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

EuPathDBiHostDB:ENSG00000196565.12
HGNCiHGNC:4832 HBG2
MIMi142250 gene
neXtProtiNX_P69892

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

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. 1 PublicationCorresponds to variant dbSNP:rs34878913EnsemblClinVar.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. 2 PublicationsCorresponds to variant dbSNP:rs34474104EnsemblClinVar.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. 1 PublicationCorresponds to variant dbSNP:rs587776864EnsemblClinVar.1
Natural variantiVAR_00316693H → Y in TNCY; hemoglobin Fort Ripley. 1 PublicationCorresponds to variant dbSNP:rs35103459EnsemblClinVar.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 syndrome
251380 Hereditary persistence of fetal hemoglobin-sickle cell disease syndrome
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 residuei13PhosphothreonineBy similarity1
Modified residuei45PhosphoserineCombined sources1
Modified residuei51PhosphoserineCombined sources1
Modified residuei53PhosphoserineCombined sources1
Modified residuei60N6-acetyllysineBy similarity1
Modified residuei83N6-acetyllysineBy similarity1
Modified residuei94S-nitrosocysteineBy similarity1
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, S-nitrosylation

Proteomic databases

EPDiP69892
MaxQBiP69892
PaxDbiP69892
PeptideAtlasiP69892
PRIDEiP69892
ProteomicsDBi57546

PTM databases

iPTMnetiP69892
PhosphoSitePlusiP69892

Expressioni

Tissue specificityi

Red blood cells.

Developmental stagei

Expressed until four or five weeks after birth.

Gene expression databases

BgeeiENSG00000196565 Expressed in 86 organ(s), highest expression level in stomach
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

Binary interactionsi

WithEntry#Exp.IntActNotes
HBMQ6B0K94EBI-3910089,EBI-12805802

Protein-protein interaction databases

BioGridi109298, 8 interactors
ComplexPortaliCPX-2931 Hemoglobin Portland-1 Variant 2 complex
CPX-2933 Hemoglobin HbF Variant 2 complex
CORUMiP69892
IntActiP69892, 10 interactors
MINTiP69892
STRINGi9606.ENSP00000338082

Structurei

Secondary structure

1147
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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
InterProiView protein in InterPro
IPR000971 Globin
IPR009050 Globin-like_sf
IPR012292 Globin/Proto
IPR002337 Haemoglobin_b
PfamiView protein in Pfam
PF00042 Globin, 1 hit
PRINTSiPR00814 BETAHAEM
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.

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. 1 PublicationCorresponds to variant dbSNP:rs36006195EnsemblClinVar.1
Natural variantiVAR_0031266E → G in Meinohama. 1 PublicationCorresponds to variant dbSNP:rs34263826EnsemblClinVar.1
Natural variantiVAR_0031298D → N in Auckland. 1 PublicationCorresponds to variant dbSNP:rs34501593EnsemblClinVar.1
Natural variantiVAR_0206439K → E in Albaicin. 1 PublicationCorresponds to variant dbSNP:rs35521813EnsemblClinVar.1
Natural variantiVAR_0206449K → Q in Albaicin. 1 PublicationCorresponds to variant dbSNP:rs35521813EnsemblClinVar.1
Natural variantiVAR_02064513T → R in Heather. Corresponds to variant dbSNP:rs281864890EnsemblClinVar.1
Natural variantiVAR_00313116W → R in Catalonia. 1 PublicationCorresponds to variant dbSNP:rs34438981EnsemblClinVar.1
Natural variantiVAR_00313217G → R in Melbourne. 1 PublicationCorresponds to variant dbSNP:rs34907654EnsemblClinVar.1
Natural variantiVAR_02064618K → N in Clamart. 1 PublicationCorresponds to variant dbSNP:rs35621390EnsemblClinVar.1
Natural variantiVAR_02064720N → K in Ouled Rabah. 1 PublicationCorresponds to variant dbSNP:rs34018799EnsemblClinVar.1
Natural variantiVAR_03049621V → A in Bron. 1 PublicationCorresponds to variant dbSNP:rs63751196Ensembl.1
Natural variantiVAR_00313322E → K in Saskatoon. 1 PublicationCorresponds to variant dbSNP:rs33955330EnsemblClinVar.1
Natural variantiVAR_00313422E → Q in Fuchu. 1 PublicationCorresponds to variant dbSNP:rs33955330EnsemblClinVar.1
Natural variantiVAR_02064823D → G in Urumqi. 2 PublicationsCorresponds to variant dbSNP:rs281864891EnsemblClinVar.1
Natural variantiVAR_00313623D → V in Granada. 1 PublicationCorresponds to variant dbSNP:rs281864891EnsemblClinVar.1
Natural variantiVAR_00313726G → E in Cosenza. 1 PublicationCorresponds to variant dbSNP:rs35687396EnsemblClinVar.1
Natural variantiVAR_00313927E → K in Oakland. 1 PublicationCorresponds to variant dbSNP:rs35654328EnsemblClinVar.1
Natural variantiVAR_00314035V → I in Tokyo. 1 PublicationCorresponds to variant dbSNP:rs35885783EnsemblClinVar.1
Natural variantiVAR_03049739T → P in Bonheiden; causes severe hereditary hemolytic anemia. 1 PublicationCorresponds to variant dbSNP:rs35799058Ensembl.1
Natural variantiVAR_00314441R → G in Veleta. Corresponds to variant dbSNP:rs34532478EnsemblClinVar.1
Natural variantiVAR_02064941R → K in Austell. 1 PublicationCorresponds to variant dbSNP:rs281864892EnsemblClinVar.1
Natural variantiVAR_00314642F → S in TNCY; hemoglobin Cincinnati. 1 PublicationCorresponds to variant dbSNP:rs34878913EnsemblClinVar.1
Natural variantiVAR_00314845S → R in Lodz. 1 PublicationCorresponds to variant dbSNP:rs34017450EnsemblClinVar.1
Natural variantiVAR_00315056M → R in Kingston. 1 PublicationCorresponds to variant dbSNP:rs34915311EnsemblClinVar.1
Natural variantiVAR_00315160K → E in Emirates. 1 PublicationCorresponds to variant dbSNP:rs28933078EnsemblClinVar.1
Natural variantiVAR_00315260K → Q in Sacromonte. 1 PublicationCorresponds to variant dbSNP:rs28933078EnsemblClinVar.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. 2 PublicationsCorresponds to variant dbSNP:rs34474104EnsemblClinVar.1
Natural variantiVAR_00315566K → N in Clarke. 1 PublicationCorresponds to variant dbSNP:rs34019507EnsemblClinVar.1
Natural variantiVAR_00315767K → Q in Brooklyn. 1 PublicationCorresponds to variant dbSNP:rs34264694EnsemblClinVar.1
Natural variantiVAR_00315667K → R in Shanghai. 1 PublicationCorresponds to variant dbSNP:rs35481866EnsemblClinVar.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. 1 PublicationCorresponds to variant dbSNP:rs587776864EnsemblClinVar.1
Natural variantiVAR_02065073G → R in Minoo. 1 PublicationCorresponds to variant dbSNP:rs281860594EnsemblClinVar.1
Natural variantiVAR_02065176I → T in LesVos/Waynesboro/Charlotte. 3 PublicationsCorresponds to variant dbSNP:rs1061234Ensembl.1
Natural variantiVAR_03049876I → V in Coigneres. 1 PublicationCorresponds to variant dbSNP:rs34363111Ensembl.1
Natural variantiVAR_00316278H → R in Kennestone. 1 PublicationCorresponds to variant dbSNP:rs34150306EnsemblClinVar.1
Natural variantiVAR_02065281D → N in Marietta. Corresponds to variant dbSNP:rs63751148EnsemblClinVar.1
Natural variantiVAR_00316693H → Y in TNCY; hemoglobin Fort Ripley. 1 PublicationCorresponds to variant dbSNP:rs35103459EnsemblClinVar.1
Natural variantiVAR_00316795D → N in Columbus-Ga. 1 PublicationCorresponds to variant dbSNP:rs35812514EnsemblClinVar.1
Natural variantiVAR_003169102E → K in La Grange. 1 PublicationCorresponds to variant dbSNP:rs34876238EnsemblClinVar.1
Natural variantiVAR_003170105K → N in Macedonia-II. 1 PublicationCorresponds to variant dbSNP:rs35717854EnsemblClinVar.1
Natural variantiVAR_073159106L → H in TNCY; hemoglobin F-Brugine/Feldkirch; lowered affinity for oxygen. 1 Publication1
Natural variantiVAR_003171118H → R in Malta-1. 1 PublicationCorresponds to variant dbSNP:rs36049074EnsemblClinVar.1
Natural variantiVAR_015740119F → L in Calabria. 1 PublicationCorresponds to variant dbSNP:rs35020253EnsemblClinVar.1
Natural variantiVAR_003172121K → Q in Caltech. 1 PublicationCorresponds to variant dbSNP:rs34703519EnsemblClinVar.1
Natural variantiVAR_020653122E → K in Carlton. 1 PublicationCorresponds to variant dbSNP:rs63750021EnsemblClinVar.1
Natural variantiVAR_003174126E → A in Port-Royal. 1 PublicationCorresponds to variant dbSNP:rs34997902EnsemblClinVar.1
Natural variantiVAR_003176131W → G in Poole; unstable. 1 PublicationCorresponds to variant dbSNP:rs35826780EnsemblClinVar.1
Natural variantiVAR_003179147H → Y in Onoda; O(2) affinity up. 1 PublicationCorresponds to variant dbSNP:rs34807671EnsemblClinVar.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
GeneIDi3048
KEGGihsa:3048
UCSCiuc001maj.2 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

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
ComplexPortaliCPX-2931 Hemoglobin Portland-1 Variant 2 complex
CPX-2933 Hemoglobin HbF Variant 2 complex
CORUMiP69892
IntActiP69892, 10 interactors
MINTiP69892
STRINGi9606.ENSP00000338082

PTM databases

iPTMnetiP69892
PhosphoSitePlusiP69892

Polymorphism and mutation databases

BioMutaiHBG2
DMDMi56749861

Proteomic databases

EPDiP69892
MaxQBiP69892
PaxDbiP69892
PeptideAtlasiP69892
PRIDEiP69892
ProteomicsDBi57546

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3048
DisGeNETi3048
EuPathDBiHostDB:ENSG00000196565.12
GeneCardsiENSG00000239920
HBG2
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 syndrome
251380 Hereditary persistence of fetal hemoglobin-sickle cell disease syndrome
PharmGKBiPA29207
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3378 Eukaryota
COG1018 LUCA
GeneTreeiENSGT00760000119197
HOVERGENiHBG009709
InParanoidiP69892
KOiK13824
PhylomeDBiP69892
TreeFamiTF333268

Enzyme and pathway databases

ReactomeiR-HSA-983231 Factors involved in megakaryocyte development and platelet production
SIGNORiP69892

Miscellaneous databases

ChiTaRSiHBG2 human
EvolutionaryTraceiP69892
GeneWikiiHBG2
GenomeRNAii3048
PROiPR:P69892
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000196565 Expressed in 86 organ(s), highest expression level in stomach
CleanExiHS_HBG2
ExpressionAtlasiP69892 baseline and differential
GenevisibleiP69892 HS

Family and domain databases

CDDicd08925 Hb-beta_like, 1 hit
Gene3Di1.10.490.10, 1 hit
InterProiView protein in InterPro
IPR000971 Globin
IPR009050 Globin-like_sf
IPR012292 Globin/Proto
IPR002337 Haemoglobin_b
PfamiView protein in Pfam
PF00042 Globin, 1 hit
PRINTSiPR00814 BETAHAEM
SUPFAMiSSF46458 SSF46458, 1 hit
PROSITEiView protein in PROSITE
PS01033 GLOBIN, 1 hit
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 7, 2018
This is version 151 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. SIMILARITY comments
    Index of protein domains and families
  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. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
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