Entry - *615258 - EEF1A LYSINE METHYLTRANSFERASE 3; EEF1AKMT3 - OMIM

 
 
* 615258

EEF1A LYSINE METHYLTRANSFERASE 3; EEF1AKMT3


Alternative titles; symbols

METHYLTRANSFERASE-LIKE 21B; METTL21B
FAMILY WITH SEQUENCE SIMILARITY 119, MEMBER B; FAM119B


HGNC Approved Gene Symbol: EEF1AKMT3

Cytogenetic location: 12q14.1     Genomic coordinates (GRCh38): 12:57,772,614-57,782,541 (from NCBI)


TEXT

▼ Description

Methyltransferases catalyze the transfer of a methyl group from a donor, generally S-adenosyl-L-methionine (AdoMet), to acceptor molecules, including proteins, DNA, RNA, lipids, and small metabolites. METTL21B belongs to a family of protein lysine methyltransferases that methylate nonhistone proteins (Cloutier et al., 2013).


▼ Cloning and Expression

By searching databases for sequences similar to METTL22 (615261), Cloutier et al. (2013) identified METTL21B. The deduced protein is made up predominantly of a Rossmann fold of alternating beta strands and alpha helices, with a conserved AdoMet-binding site near the N terminus. Epitope-tagged METTL21B was predominantly expressed in a diffuse cytoplasmic distribution in transfected HeLa cells.


▼ Gene Function

By affinity purification, SDS-PAGE, and mass spectrometry, Cloutier et al. (2013) found that METTL21B expressed in HEK293 cells interacted with HSP90 (see 140571), HSP70 (see 140550), STIP1 (605063), CCT (see 605139), and tubulin (see 602529).


▼ Mapping

Hartz (2013) mapped the METTL21B gene to chromosome 12q14.1 based on an alignment of the METTL21B sequence (GenBank AK024983) with the genomic sequence (GRCh37).

▼ REFERENCES

  1. Cloutier, P., Lavallee-Adam, M., Faubert, D., Blanchette, M., Coulombe, B. A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity. PLoS Genet. 9: e1003210, 2013. Note: Electronic Article. [PubMed: 23349634, images, related citations] [Full Text]

  2. Hartz, P. A. Personal Communication. Baltimore, Md. 5/29/2013.


Creation Date:
Patricia A. Hartz : 5/29/2013
Edit History:
mgross : 11/30/2017
mgross : 05/31/2013

* 615258

EEF1A LYSINE METHYLTRANSFERASE 3; EEF1AKMT3


Alternative titles; symbols

METHYLTRANSFERASE-LIKE 21B; METTL21B
FAMILY WITH SEQUENCE SIMILARITY 119, MEMBER B; FAM119B


HGNC Approved Gene Symbol: EEF1AKMT3

Cytogenetic location: 12q14.1     Genomic coordinates (GRCh38): 12:57,772,614-57,782,541 (from NCBI)


TEXT

Description

Methyltransferases catalyze the transfer of a methyl group from a donor, generally S-adenosyl-L-methionine (AdoMet), to acceptor molecules, including proteins, DNA, RNA, lipids, and small metabolites. METTL21B belongs to a family of protein lysine methyltransferases that methylate nonhistone proteins (Cloutier et al., 2013).


Cloning and Expression

By searching databases for sequences similar to METTL22 (615261), Cloutier et al. (2013) identified METTL21B. The deduced protein is made up predominantly of a Rossmann fold of alternating beta strands and alpha helices, with a conserved AdoMet-binding site near the N terminus. Epitope-tagged METTL21B was predominantly expressed in a diffuse cytoplasmic distribution in transfected HeLa cells.


Gene Function

By affinity purification, SDS-PAGE, and mass spectrometry, Cloutier et al. (2013) found that METTL21B expressed in HEK293 cells interacted with HSP90 (see 140571), HSP70 (see 140550), STIP1 (605063), CCT (see 605139), and tubulin (see 602529).


Mapping

Hartz (2013) mapped the METTL21B gene to chromosome 12q14.1 based on an alignment of the METTL21B sequence (GenBank AK024983) with the genomic sequence (GRCh37).

REFERENCES

  1. Cloutier, P., Lavallee-Adam, M., Faubert, D., Blanchette, M., Coulombe, B. A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity. PLoS Genet. 9: e1003210, 2013. Note: Electronic Article. [PubMed: 23349634] [Full Text: https://doi.org/10.1371/journal.pgen.1003210]

  2. Hartz, P. A. Personal Communication. Baltimore, Md. 5/29/2013.


Creation Date:
Patricia A. Hartz : 5/29/2013

Edit History:
mgross : 11/30/2017
mgross : 05/31/2013



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OMIM® and Online Mendelian Inheritance in Man® are registered trademarks of the Johns Hopkins University.
Copyright® 1966-2024 Johns Hopkins University.

NOTE: OMIM is intended for use primarily by physicians and other professionals concerned with genetic disorders, by genetics researchers, and by advanced students in science and medicine. While the OMIM database is open to the public, users seeking information about a personal medical or genetic condition are urged to consult with a qualified physician for diagnosis and for answers to personal questions.
OMIM® and Online Mendelian Inheritance in Man® are registered trademarks of the Johns Hopkins University.
Copyright® 1966-2024 Johns Hopkins University.
Printed: June 3, 2024