Hemoglobin subunit gamma-1 (HBG1)

The protein contains 147 amino acids for an estimated molecular weight of 16140 Da.

 

Gamma chains make up the fetal hemoglobin F, in combination with alpha chains. (updated: March 4, 2015)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
  3. Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
  4. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  5. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
  6. Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.

Interpro domains
Total structural coverage: 99%
Model score: 100

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VariantDescription
Macedonia-I
Texas-1
Izumi/Kotobuki
Pordenone
Calluna
Kuala Lumpur
Xinjiang
Pendergrass
Cobb
Bonaire
Woodstock
Fukuyama
Beech island
Jamaica
Iwata
Xin-su
Forest Park
Sardinia/Forest Park
Dammam
Yamaguchi
Victoria jubilee
Dickinson
Siena/Hull
Baskent
Jiangsu

No binding partner found

The reference OMIM entry for this protein is 142200

Hemoglobin, gamma a; hbg1
Hemoglobin--gamma locus, 136 alanine

See 142250. Chang et al. (1978) demonstrated that the 5-prime untranslated region of the human gamma-globin mRNA contains 57 nucleotides, compared to 41 in alpha and 54 in beta. Both guanosine and cytidine were found at the 19th nucleotide position from the 5-prime end of the gamma mRNA. This heterogeneity may reflect differences in the A-gamma and G-gamma (142250) loci. Jeffreys (1979) found a restriction enzyme polymorphism of the DNA intervening sequence of the A-gamma gene. The frequency was estimated at 0.23. Puzzling was the finding of the same polymorphism in the G-gamma gene. See Slightom et al. (1980) and Shen et al. (1981) for a discussion of the possible mechanisms for suppression of allelic polymorphism. Gene conversion is 1 of the 2 classes of known mechanisms that can act on families of genes to maintain their sequence homology; the other is unequal crossing-over (Baltimore, 1981). The similarity of the 2 gamma-globin genes (e.g., identical restriction polymorphism in an intervening sequence) may owe its origin to this mechanism. Slightom et al. (1980) found that IVS-1 is highly conserved and has 122 bases between codons 30 and 31; IVS-2, which consists of conserved, nonconserved and simple sequence DNA and varies in length from 866 to 904 bases, is located between codons 104 and 105. The data of these authors suggested that gene conversion (intergenic exchanges in cis) is a frequent event, occurring in the germline. The gene conversion in the first example found in Smithies' laboratory (Slightom et al., 1980) involved more than a kilobase of DNA. Smithies and Powers (1986) referred to examples of much shorter gene conversions in the human fetal globin gene pair. They suggested that gene conversions are the consequence of a general mechanism whereby DNA strand invasions enable chromosomes to find their homologs during meiosis. The model they suggested had the following elements: In meiosis single-stranded 'feelers' are extruded from many sites along DNA molecules. These feelers can invade any DNA duplex they encounter and then can scan that duplex for homologous sequences with which to form a Watson-Crick double helix. Scanning is halted when a nucleotide sequence is found that can form a stable double helix. If nearby invasions have also been successful, a zipper effect will lead to pairing of homologs. If a stable heteroduplex is formed as a consequence of a related sequence being found at a nonhomologous chromosomal location, short gene conversions may result. Gene conversion is more likely to develop between closely linked genes than between widely separated ones. Papayannopoulou et al. (1982) demonstrated a humoral factor that induces switching from gamma-globin to beta-globin in neonatal and adult cells. Fetal cells are not responsive to the factor. Weinberg et al. (1983) studied the correlation between gamma-globin and beta-globin synthesis in cultures of erythroid progenitor cells from newborn infants and adults. The findings suggested a clonal model for hemoglobin switching. Lavett (1984) found an extensive stem-loop structure in the A-gamma-globin promoter region, with intron transcripts from epsilon-globin, A-gamma-globin, delta-globin and beta-globin showing sequences complementary to that of the loop. She proposed a model for globin-switching based on changes in DNA secondary structure and intron transcript pairing. Melis et al. (1987) presented evidence that the genes controlling the gamma-to-beta switch are ... More on the omim web site

Subscribe to this protein entry history

May 12, 2019: Protein entry updated
Automatic update: model status changed

Nov. 17, 2018: Protein entry updated
Automatic update: model status changed

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated

June 20, 2017: Protein entry updated
Automatic update: comparative model was added.

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 142200 was added.

Feb. 25, 2016: Protein entry updated
Automatic update: model status changed

Jan. 28, 2016: Protein entry updated
Automatic update: model status changed

Jan. 24, 2016: Protein entry updated
Automatic update: model status changed