Myeloid-associated differentiation marker (MYADM)

The protein contains 322 amino acids for an estimated molecular weight of 35274 Da.

 

No function (updated: Jan. 7, 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. 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.
  3. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  4. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.

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.
Protein sequence (FASTA)
Protein coevolution profile (FreeContact)
Multiple Sequence Alignment (Muscle)

This protein is annotated as membranous in Gene Ontology, is predicted to be membranous by TOPCONS.

Topcons

Interpro domains
Total structural coverage: 0%
Model score: 0
MODL_ROSETTA-3.4

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The reference OMIM entry for this protein is 609959

Myeloid-associated differentiation marker; myadm

CLONING

Using differential display analysis, Pettersson et al. (2000) identified mouse myeloid-associated differentiation marker (Myadm) based upon its varied expression during differentiation of an Il3 (147740)-dependent myeloid progenitor cell line established from mouse bone marrow. The deduced protein contains 8 potential transmembrane domains and several potential phosphorylation sites. Northern blot analysis on hematopoietic cell lines revealed restricted expression of Myadm to cells belonging to the myeloid lineage. Expression was also seen in mature granulocytes and macrophages. Tissue analysis showed high expression of Myadm in lung and more moderate expression in bone marrow and brain. RT-PCR experiments demonstrated expression of Myadm in multipotent cells (c-kit+Sca-1+Lin-), erythroid progenitors, and early lymphoid progenitors. By database searching with mouse Myadm as query, Cui et al. (2002) identified human MYADM and cloned a full-length MYADM sequence from a human bone marrow cDNA library. The deduced 298-amino acid protein has a predicted molecular mass of 32 kD. It contains 7 predicted transmembrane domains and shows sequence homology with the T-cell differentiation protein MAL (188860) and plasmolipin (PLMP; 600340). MYADM shares 75.8% overall sequence identity with mouse Myadm, with highest levels of conservation seen in the predicted transmembrane regions. Northern blot analysis detected 3.3- and 2.2-kb MYADM transcripts. Expression of the longer transcript was seen in all tissues tested except thymus; expression of the shorter transcript was seen in heart, placenta, lung, pancreas, testis, and peripheral blood leukocytes and was undetectable in all other tissues. Semiquantitative PCR assays showed that expression of MYADM was not only significantly higher in peripheral blood leukocytes than in bone marrow cells, but was also upregulated in NB4 cells (derived from a patient with acute promyelocytic leukemia) that were treated with the differentiation inducer all-trans retinoic acid (ATRA).

GENE FUNCTION

Using antisense Myadm oligonucleotides, Pettersson et al. (2000) showed that downregulation of mouse Myadm expression in pluripotent hematopoietic progenitor cells inhibited colony formation.

GENE STRUCTURE

Cui et al. (2002) determined that the MYADM gene contains 3 exons and spans 7.1 kb.

MAPPING

By radiation hybrid analysis, Cui et al. (2002) mapped the MYADM gene to chromosome 19q13.33-q13.4. ... 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

Oct. 27, 2017: Protein entry updated
Automatic update: model status changed

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 609959 was added.

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

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

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