P69892 · HBG2_HUMAN
- ProteinHemoglobin subunit gamma-2
- GeneHBG2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids147 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Gamma chains make up the fetal hemoglobin F, in combination with alpha chains.
Features
Showing features for binding site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | blood microparticle | |
Cellular Component | cytosol | |
Cellular Component | haptoglobin-hemoglobin complex | |
Cellular Component | hemoglobin complex | |
Molecular Function | heme binding | |
Molecular Function | hemoglobin alpha binding | |
Molecular Function | metal ion binding | |
Molecular Function | organic acid binding | |
Molecular Function | oxygen binding | |
Molecular Function | oxygen carrier activity | |
Biological Process | carbon dioxide transport | |
Biological Process | cellular oxidant detoxification | |
Biological Process | hydrogen peroxide catabolic process | |
Biological Process | oxygen transport |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHemoglobin subunit gamma-2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP69892
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Involvement in disease
Cyanosis transient neonatal (TNCY)
- Note
- 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 alsoMIM:613977
Natural variants in TNCY
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_003146 | 42 | F>S | in TNCY; hemoglobin Cincinnati; dbSNP:rs34878913 | |
VAR_025336 | 64 | H>L | in TNCY; hemoglobin M-Circleville | |
VAR_003154 | 64 | H>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; dbSNP:rs34474104 | |
VAR_065950 | 68 | V>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; dbSNP:rs587776864 | |
VAR_003166 | 93 | H>Y | in TNCY; hemoglobin Fort Ripley; dbSNP:rs35103459 | |
VAR_073159 | 106 | L>H | in TNCY; hemoglobin F-Brugine/Feldkirch; lowered affinity for oxygen |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_003123 | 2 | in Malaysia; dbSNP:rs36006195 | |||
Sequence: G → C | ||||||
Natural variant | VAR_003126 | 6 | in Meinohama; dbSNP:rs34263826 | |||
Sequence: E → G | ||||||
Natural variant | VAR_003129 | 8 | in Auckland; dbSNP:rs34501593 | |||
Sequence: D → N | ||||||
Natural variant | VAR_020643 | 9 | in Albaicin; dbSNP:rs35521813 | |||
Sequence: K → E | ||||||
Natural variant | VAR_020644 | 9 | in Albaicin; dbSNP:rs35521813 | |||
Sequence: K → Q | ||||||
Natural variant | VAR_020645 | 13 | in Heather; dbSNP:rs281864890 | |||
Sequence: T → R | ||||||
Natural variant | VAR_003131 | 16 | in Catalonia; dbSNP:rs34438981 | |||
Sequence: W → R | ||||||
Natural variant | VAR_003132 | 17 | in Melbourne; dbSNP:rs34907654 | |||
Sequence: G → R | ||||||
Natural variant | VAR_020646 | 18 | in Clamart; dbSNP:rs35621390 | |||
Sequence: K → N | ||||||
Natural variant | VAR_020647 | 20 | in Ouled Rabah; dbSNP:rs34018799 | |||
Sequence: N → K | ||||||
Natural variant | VAR_030496 | 21 | in Bron; dbSNP:rs63751196 | |||
Sequence: V → A | ||||||
Natural variant | VAR_003133 | 22 | in Saskatoon; dbSNP:rs33955330 | |||
Sequence: E → K | ||||||
Natural variant | VAR_003134 | 22 | in Fuchu; dbSNP:rs33955330 | |||
Sequence: E → Q | ||||||
Natural variant | VAR_020648 | 23 | in Urumqi; dbSNP:rs281864891 | |||
Sequence: D → G | ||||||
Natural variant | VAR_003136 | 23 | in Granada; dbSNP:rs281864891 | |||
Sequence: D → V | ||||||
Natural variant | VAR_003137 | 26 | in Cosenza; dbSNP:rs35687396 | |||
Sequence: G → E | ||||||
Natural variant | VAR_003139 | 27 | in Oakland; dbSNP:rs35654328 | |||
Sequence: E → K | ||||||
Natural variant | VAR_003140 | 35 | in Tokyo; dbSNP:rs35885783 | |||
Sequence: V → I | ||||||
Natural variant | VAR_030497 | 39 | in Bonheiden; causes severe hereditary hemolytic anemia; dbSNP:rs35799058 | |||
Sequence: T → P | ||||||
Natural variant | VAR_003144 | 41 | in Veleta; dbSNP:rs34532478 | |||
Sequence: R → G | ||||||
Natural variant | VAR_020649 | 41 | in Austell; dbSNP:rs281864892 | |||
Sequence: R → K | ||||||
Natural variant | VAR_003146 | 42 | in TNCY; hemoglobin Cincinnati; dbSNP:rs34878913 | |||
Sequence: F → S | ||||||
Natural variant | VAR_003148 | 45 | in Lodz; dbSNP:rs34017450 | |||
Sequence: S → R | ||||||
Natural variant | VAR_003150 | 56 | in Kingston; dbSNP:rs34915311 | |||
Sequence: M → R | ||||||
Natural variant | VAR_003151 | 60 | in Emirates; dbSNP:rs28933078 | |||
Sequence: K → E | ||||||
Natural variant | VAR_003152 | 60 | in Sacromonte; dbSNP:rs28933078 | |||
Sequence: K → Q | ||||||
Natural variant | VAR_025336 | 64 | in TNCY; hemoglobin M-Circleville | |||
Sequence: H → L | ||||||
Natural variant | VAR_003154 | 64 | 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; dbSNP:rs34474104 | |||
Sequence: H → Y | ||||||
Natural variant | VAR_003155 | 66 | in Clarke; dbSNP:rs34019507 | |||
Sequence: K → N | ||||||
Natural variant | VAR_003157 | 67 | in Brooklyn; dbSNP:rs34264694 | |||
Sequence: K → Q | ||||||
Natural variant | VAR_003156 | 67 | in Shanghai; dbSNP:rs35481866 | |||
Sequence: K → R | ||||||
Natural variant | VAR_065950 | 68 | 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; dbSNP:rs587776864 | |||
Sequence: V → M | ||||||
Natural variant | VAR_020650 | 73 | in Minoo; dbSNP:rs281860594 | |||
Sequence: G → R | ||||||
Natural variant | VAR_020651 | 76 | in LesVos/Waynesboro/Charlotte; dbSNP:rs104894225 | |||
Sequence: I → T | ||||||
Natural variant | VAR_030498 | 76 | in Coigneres; dbSNP:rs34363111 | |||
Sequence: I → V | ||||||
Natural variant | VAR_003162 | 78 | in Kennestone; dbSNP:rs34150306 | |||
Sequence: H → R | ||||||
Natural variant | VAR_020652 | 81 | in Marietta; dbSNP:rs63751148 | |||
Sequence: D → N | ||||||
Natural variant | VAR_003166 | 93 | in TNCY; hemoglobin Fort Ripley; dbSNP:rs35103459 | |||
Sequence: H → Y | ||||||
Natural variant | VAR_003167 | 95 | in Columbus-Ga; dbSNP:rs35812514 | |||
Sequence: D → N | ||||||
Natural variant | VAR_003169 | 102 | in La Grange; dbSNP:rs34876238 | |||
Sequence: E → K | ||||||
Natural variant | VAR_003170 | 105 | in Macedonia-II; dbSNP:rs35717854 | |||
Sequence: K → N | ||||||
Natural variant | VAR_073159 | 106 | in TNCY; hemoglobin F-Brugine/Feldkirch; lowered affinity for oxygen | |||
Sequence: L → H | ||||||
Natural variant | VAR_003171 | 118 | in Malta-1; dbSNP:rs36049074 | |||
Sequence: H → R | ||||||
Natural variant | VAR_015740 | 119 | in Calabria; dbSNP:rs35020253 | |||
Sequence: F → L | ||||||
Natural variant | VAR_003172 | 121 | in Caltech; dbSNP:rs34703519 | |||
Sequence: K → Q | ||||||
Natural variant | VAR_020653 | 122 | in Carlton; dbSNP:rs63750021 | |||
Sequence: E → K | ||||||
Natural variant | VAR_003174 | 126 | in Port-Royal; dbSNP:rs34997902 | |||
Sequence: E → A | ||||||
Natural variant | VAR_003176 | 131 | in Poole; unstable; dbSNP:rs35826780 | |||
Sequence: W → G | ||||||
Natural variant | VAR_003179 | 147 | in Onoda; O2 affinity up; dbSNP:rs34807671 | |||
Sequence: H → Y |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 217 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylglycine; in form Hb F1 | ||||
Sequence: G | |||||||
Chain | PRO_0000053254 | 2-147 | UniProt | Hemoglobin subunit gamma-2 | |||
Sequence: GHFTEEDKATITSLWGKVNVEDAGGETLGRLLVVYPWTQRFFDSFGNLSSASAIMGNPKVKAHGKKVLTSLGDAIKHLDDLKGTFAQLSELHCDKLHVDPENFKLLGNVLVTVLAIHFGKEFTPEVQASWQKMVTGVASALSSRYH | |||||||
Modified residue | 13 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 45 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 51 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 53 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 53 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 60 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 83 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 94 | UniProt | S-nitrosocysteine | ||||
Sequence: C | |||||||
Modified residue | 140 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 143 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 144 | UniProt | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Acetylation of Gly-2 converts Hb F to the minor Hb F1.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Red blood cells.
Developmental stage
Expressed until four or five weeks after birth.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Heterotetramer of two alpha chains and two gamma chains in fetal hemoglobin (Hb F).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P69892 | HBA2 P69905 | 3 | EBI-3910089, EBI-714680 | |
BINARY | P69892 | HBM Q6B0K9 | 6 | EBI-3910089, EBI-12805802 | |
BINARY | P69892 | HBQ1 P09105 | 3 | EBI-3910089, EBI-10193656 | |
BINARY | P69892 | XPNPEP1 Q9NQW7-3 | 3 | EBI-3910089, EBI-12079490 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 3-147 | Globin | ||||
Sequence: HFTEEDKATITSLWGKVNVEDAGGETLGRLLVVYPWTQRFFDSFGNLSSASAIMGNPKVKAHGKKVLTSLGDAIKHLDDLKGTFAQLSELHCDKLHVDPENFKLLGNVLVTVLAIHFGKEFTPEVQASWQKMVTGVASALSSRYH |
Sequence similarities
Belongs to the globin family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length147
- Mass (Da)16,126
- Last updated2007-01-23 v2
- Checksum8FCDC4441B416DDE
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M91036 EMBL· GenBank· DDBJ | AAB59428.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M91037 EMBL· GenBank· DDBJ | AAA58492.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U01317 EMBL· GenBank· DDBJ | AAA16331.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
V00515 EMBL· GenBank· DDBJ | CAA23773.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M15386 EMBL· GenBank· DDBJ | AAB50159.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AY662983 EMBL· GenBank· DDBJ | AAT98611.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK290492 EMBL· GenBank· DDBJ | BAF83181.1 EMBL· GenBank· DDBJ | mRNA | ||
BC010914 EMBL· GenBank· DDBJ | AAH10914.1 EMBL· GenBank· DDBJ | mRNA | ||
BC029387 EMBL· GenBank· DDBJ | AAH29387.1 EMBL· GenBank· DDBJ | mRNA | ||
BC130457 EMBL· GenBank· DDBJ | AAI30458.1 EMBL· GenBank· DDBJ | mRNA | ||
BC130459 EMBL· GenBank· DDBJ | AAI30460.1 EMBL· GenBank· DDBJ | mRNA | ||
M11427 EMBL· GenBank· DDBJ | AAA35957.1 EMBL· GenBank· DDBJ | mRNA |