Tripartite motif-containing protein 10 (TRIM10)

The protein contains 481 amino acids for an estimated molecular weight of 55037 Da.

 

Seems to play an important role in erythropoiesis. (updated: Sept. 12, 2018)

Protein identification was indicated in the following studies:

  1. 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.
  2. Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
  3. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  4. 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: 0%
Model score: 0
No model available.

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VariantDescription
dbSNP:rs12212092
dbSNP:rs17194446

The reference OMIM entry for this protein is 605701

Tripartite motif-containing protein 10; trim10
Rfb30
Hematopoietic ring finger 1; herf1
Ring finger protein 9, formerly; rnf9, formerly

CLONING

By screening a human chromosome 6-specific library with a B30.2 domain-encoding exon that had been mapped to 6p21.3 as the probe, Henry et al. (1997) obtained a cDNA encoding RFB30. Sequence analysis predicted that the 481-amino acid protein contains a RING finger-B box domain encoded by exon 1, a coiled-coil domain encoded by exons 2 through 6, and a B30.2 domain encoded by exon 7. Harada et al. (1999) isolated a cDNA encoding mouse Herf1. Northern blot analysis of mouse tissue detected a 2.3-kb transcript only in spleen and bone marrow erythroid cells. In embryonic mice, expression was detected on day 11.5 at the beginning of erythropoiesis.

GENE STRUCTURE

Henry et al. (1997) determined that the TRIM10 gene contains at least 7 exons.

MAPPING

Henry et al. (1997) mapped the TRIM10 gene to chromosome 6p21.3. ... More on the omim web site

Subscribe to this protein entry history

June 30, 2020: Protein entry updated
Automatic update: OMIM entry 605701 was added.

Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).