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måndag 6 juli 2020

Rakenneaminohapoilla on omat tRNA syntetaasinsa AARS ja niille kehitellään inhibiittoreita (thesis 2012)

Hain tähän blogiin aminohappojen tRNA transferaasien luettelon, sillä aloin lukea erästä  teesiä vuodelta 2012 ja siinä  kehiteltiin perusteita mahdollisten aminohappo-tRNA-syntaasien inhibiittoreille, joten ensinnäkin minun piti  alkaa ottaa selville näiden kahdenkymmenen rakenneaminohapon tRNA syntaasien olemassaolosta ja geeneistä, mutten kirja jää puolitiehen lukematta. Aminohappotransferaaseja AARS  on sytoplasminen ja mitokondriaalinen muoto.  Useimmat näyttävät omaavan  nukleaarisen genomin koodauksen ja geenituote etsiytyy miokondriaan,  mutta mitokondriaalisestakin genomista  tulee niitä  ainakin 9:lle aminohappolle multifunktionaalisina komplekseina ja varsinkin glutamaatin osalta on erityissäätelyä, johon tulee monen geenin taholta osallistumista.   Thesis josta sain inspiraation katsoa nmä AARS geenit  nyt  on  lääkekemian alueelta

Itedale Namro Redwan: Design and the synthesis of potential aminoacyl-tRNA synthetase inhibitors.  Dep. of Chemistry and molecular biology, University of Gothenburg. Kemigården. ISBN: 978-91-628-8445-1. http://hdl.handle.net/2077/28794

Teesisn avainsanat   ( Tänään 5-6.6. 2020  olen ktsonut  geenit  aminohappojen tRNA syntetaaseista AARS ja maininut samassa yhteydessä  aminohapot ( aa, aminoacids)

KEY WORDS: Aminoacyl tRNA synthetases (AARS)
Aminoacyl-AMP
Bioisosteres
Amino Acids  (a a)
Solution-Phase
Protective Groups
Solid-Phase Chemistry
Molecular Modelling
Biological Evaluation

Väitöstilaisuus oli kemian laitoksella. Vastaväittelijä oli Barcelonan biomedisiinisen tutkimuksen instituutista Ramon Eritja  tokokuussa  2012;  kävin kuuntelemassa väitöstilaisuuden ja siksi minulla on ollut  tämä  thesis  kirjahyllyssä aikaansa odottamassa.   Asia alkoi kiinnostaa, kun huomasin että nykyinen pandeminen virus SARS2  CoV nsp8  ja M -propteiini  tekevät   interaktion  myös ihmisen aminohappo-tRNA syntetaaseihin kuten asparaginyyli-tRNA syntetaasiin NARS ja vastaavasti  threonyyli-tRNA-syntetaasiin  TARS. 

  • AARS geeneistä PubMed haku 5-6.  7.2020


GLYSIINI aminohappo , Glycine,  (Gly, G)
Glycyl-tRNA synthetases GARS  1 and 2

Aliases: CMT2D, DSMAV, GARS, GlyRS, HMN5, SMAD1 GARS;
Summary: This gene encodes glycyl-tRNA synthetase, one of the aminoacyl-tRNA synthetases that charge tRNAs with their cognate amino acids. The encoded enzyme is an (alpha)2 dimer which belongs to the class II family of tRNA synthetases. It has been shown to be a target of autoantibodies in the human autoimmune diseases, polymyositis or dermatomyositis. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Oct 2015]
Preferred Names glycine--tRNA ligase
Names : AP-4-A synthetase
Charcot-Marie-Tooth neuropathy 2D
Charcot-Marie-Tooth neuropathy, neuronal type, D
ap4A synthetase
diadenosine tetraphosphate synthetase
GARS1P1, pseudogene 17q22), Alias: GARSP1 

GARS2: (en löydä).

ALANIINI aminohappo, Alanine, (Ala, A)
Alanyl-tRNA-synthetases AARS1 and 2:

Aliases: AARS; CMT2N; EIEE29 Preferred Names: alanine--tRNA ligase, cytoplasmic
Names : alaRS ; alanine tRNA ligase 1, cytoplasmic
alanyl-tRNA synthetase, cytoplasmic ; renal carcinoma antigen NY-REN-42.
Summary: The human alanyl-tRNA synthetase (AARS) belongs to a family of tRNA synthases, of the class II enzymes. Class II tRNA synthases evolved early in evolution and are highly conserved. This is reflected by the fact that 498 of the 968-residue polypeptide human AARS shares 41% identity witht the E.coli protein. tRNA synthases are the enzymes that interpret the RNA code and attach specific aminoacids to the tRNAs that contain the cognate trinucleotide anticodons. They consist of a catalytic domain which interacts with the amino acid acceptor-T psi C helix of the tRNA, and a second domain which interacts with the rest of the tRNA structure. [provided by RefSeq, Jul 2008] Expression: Ubiquitous expression in brain (RPKM 59.4), thyroid (RPKM 56.4) and 25 other tissues
Aliases: AARSL; LKENP; COXPD8; MTALARS; MT-ALARS
Summary: The protein encoded by this gene belongs to the class-II aminoacyl-tRNA synthetase family. Aminoacyl-tRNA synthetases play critical roles in mRNA translation by charging tRNAs with their cognate amino acids. The encoded protein is a mitochondrial enzyme that specifically aminoacylates alanyl-tRNA. Mutations in this gene are a cause of combined oxidative phosphorylation deficiency 8. [provided by RefSeq, Dec 2011]
Expression: Ubiquitous expression in small intestine (RPKM 2.7), ovary (RPKM 2.7) and 25 other tissues

ASPARTAATTI aminohappo, Aspartate, (Asp. D)
Aspartyl-tRNA synthetases DARS 1 and 2 :

Aliases: DARS; HBSL; aspRSSummary: This gene encodes a member of a multienzyme complex that functions in mediating the attachment of amino acids to their cognate tRNAs. The encoded protein ligates L-aspartate to tRNA(Asp). Mutations in this gene have been found in patients showing hypomyelination with brainstem and spinal cord involvement and leg spasticity. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jun 2014]Expression. Ubiquitous expression in thyroid (RPKM 24.7), lymph node (RPKM 20.9) and 25 other tissues

Aliases: LBSL; ASPRS; mtAspRS; MT-ASPRSSummary: The protein encoded by this gene belongs to the class-II aminoacyl-tRNA synthetase family. It is a mitochondrial enzyme that specifically aminoacylates aspartyl-tRNA. Mutations in this gene are associated with leukoencephalopathy with brainstem and spinal cord involvement and lactate elevation (LBSL). [provided by RefSeq, Nov 2009]Expression: Ubiquitous expression in kidney (RPKM 7.7), colon (RPKM 6.8) and 25 other tissues

ASPARAGIINI aminohappo, Asparagine, (Asn, N)
Asparaginyl-tRNA synthetasis NARS1 and 2

NARS1, https://www.ncbi.nlm.nih.gov/gene/4677
aliases: NARS; ASNRS.
 Unique N-terminal extension domain of human asparaginyl-tRNA synthetase elicits CCR3-mediated chemokine activity. Park JS, et al. Int J Biol Macromol, 2018 Dec. PMID 30171954
HIV-1 Rev interacting protein, asparaginyl-tRNA synthetase (NARS), is identified by the in-vitro binding experiments involving cytosolic or nuclear extracts from HeLa cells. The interaction of Rev with NARS is decreased by RRE

NARS2 , (11q14.1)
ALIASES: SLM5; asnRS; DFNB94
Summary: This gene encodes a putative member of the class II family of aminoacyl-tRNA synthetases. These enzymes play a critical role in protein biosynthesis by charging tRNAs with their cognate amino acids. This protein is encoded by the nuclear genome but is likely to be imported to the mitochondrion where it is thought to catalyze the ligation of asparagine to tRNA molecules. Mutations in this gene have been associated with combined oxidative phosphorylation deficiency 24 (COXPD24). [provided by RefSeq, Mar 2015] Expression Ubiquitous expression in kidney (RPKM 4.7), thyroid (RPKM 3.7) and 25 other tissues See more
H IV-1 MA is identified to have a physical interaction with asparaginyl-tRNA synthetase 2, mitochondrial (NARS2) in human HEK293 and/or Jurkat cell lines by using affinity tagging and purification mass spectrometry analyses
 
VALIINI aminohappo,  Valine,  (Val, V)
Valyl- tRNA synthetases VARS 1 and 2:

Aliases: G7A; VARS; VARS2; NDMSCASummary: Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAs, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. The protein encoded by this gene belongs to class-I aminoacyl-tRNA synthetase family and is located in the class III region of the major histocompatibility complex. [provided by RefSeq, Jul 2008] Preferred Names: valine--tRNA ligase. Names: protein G7a , valRS, valine tRNA ligase 1, cytoplasmic.

Aliases: VALRS; VARSL; VARS2L; COXPD20Summary: This gene encodes a mitochondrial aminoacyl-tRNA synthetase, which catalyzes the attachment of valine to tRNA(Val) for mitochondrial translation. Mutations in this gene cause combined oxidative phosphorylation deficiency-20, and are also associated with early-onset mitochondrial encephalopathies. Alternative splicing of this gene results in multiple transcript variants. [provided by RefSeq, Aug 2014]Expression Ubiquitous expression in brain (RPKM 7.4), esophagus (RPKM 6.1) and 25 other tissues

LEUSIINI aminohappo, Leucine, (Leu, L)
Leucyl-tRNA synthetases LARS1 and 2: 

Aliases: LRS; LARS; LEUS; LFIS; ILFS1; LEURS; PIG44; RNTLS; HSPC192; hr025Cl
Summary: This gene encodes a cytosolic leucine-tRNA synthetase, a member of the class I aminoacyl-tRNA synthetase family. The encoded enzyme catalyzes the ATP-dependent ligation of L-leucine to tRNA(Leu). It is found in the cytoplasm as part of a multisynthetase complex and interacts with the arginine tRNA synthetase through its C-terminal domain. A mutation in this gene was found in affected individuals with infantile liver failure syndrome 1. Alternatively spliced transcript variants of this gene have been observed. [provided by RefSeq, Dec 2015] Expression Ubiquitous expression in thyroid (RPKM 24.0), brain (RPKM 19.6) and 25 other tissuesTandem affinity purification and mass spectrometry analysis identify leucyl-Trna synthetase (LARS), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells

Aliases: HLASA; LEURS; PRLTS4; mtLeuRSSummary: This gene encodes a class 1 aminoacyl-tRNA synthetase, mitochondrial leucyl-tRNA synthetase. Each of the twenty aminoacyl-tRNA synthetases catalyzes the aminoacylation of a specific tRNA or tRNA isoaccepting family with the cognate amino acid. [provided by RefSeq, Jul 2008] Expression : Ubiquitous expression in kidney (RPKM 6.2), brain (RPKM 5.0) and 25 other tissues .

ISOLEUSIINI aminohappo, Isoleucine (ILE, I)
Isoleucyl-tRNA synthetases IARS 1 and 2:

Aliases: GRIDHH, IARS, ILERS, ILRS, IRS, Pro0785
Tandem affinity purification and mass spectrometry analysis identify isoleucyl-tRNA synthetase (IARS), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells 

Aliases: CAGSSS, ILERS. Mitochondrial. Class I aa-tRNA synthetase.
Hiv-1 vif interaction with IARS2.


SERIINI aminohappo, Serine,  (Ser, S)
Seryl-tRNA synthetases SERS1 and 2:

( En käytä tässä kohtaa SARS vaan SERS -vaihtoehtoa, etti sekoitu tuohon virukseen) 
Aliases: (SARS errorprone name ); SERS; SERRS; NEDMASSummary. This gene belongs to the class II amino-acyl tRNA family. The encoded enzyme catalyzes the transfer of L-serine to tRNA (Ser) and is related to bacterial and yeast counterparts. Multiple alternatively spliced transcript variants have been described but the biological validity of all variants is unknown
HIV-1 has a physical interaction with seryl-tRNA synthetase SERS. 

Aliases: SYS; (SARS error prone name); SERS; SARSM; SerRS; SerRSmt; mtSerRSSummary: This gene encodes the mitochondrial seryl-tRNA synthethase precursor, a member of the class II tRNA synthetase family. The mature enzyme catalyzes the ligation of Serine to tRNA(Ser) and participates in the biosynthesis of selenocysteinyl-tRNA(sec) in mitochondria. The enzyme contains an N-terminal tRNA binding domain and a core catalytic domain. It functions in a homodimeric form, which is stabilized by tRNA binding. This gene is regulated by a bidirectional promoter that also controls the expression of mitochondrial ribosomal protein S12. Both genes are within the critical interval for the autosomal dominant deafness locus DFNA4 and might be linked to this disease. Multiple transcript variants encoding different isoforms have been identified for this gene. [provided by RefSeq, Mar 2009] Expression Ubiquitous expression in thyroid (RPKM 6.7), placenta (RPKM 5.6) and 25 other tissues .


THREONIINI aminohappo, Threonine,  (Thr, T)
Threonyl-tRNA synthetases TARS1 and 2:

Aliases TTD7, ThrRS, cytoplasmic threonyl-tRNA synthetase
HIV-1 MA makes physical interaction with this protein.
(Also nCoV-19 has an interaction with this protein). 

mitochondrial. Aliases: COXPD21, TARSL1, thrRS. Class II aaRS.
Kidney, heart , 25 other tissues.
(TARS2P1 pseudogene kr.4)

GLUMAATTI aminohappo (E)( sekä PROLIINI (Pro, P)
Glutamyl-prolyl-tRNA synthetase 1, multifunctional 

(EARS), EPRS1, (1q41), https://www.ncbi.nlm.nih.gov/gene/2058 Alias EARS; EPRS; PARS; QARS; QPRS; HLD15; PIG32; GLUPRORSSummary: Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene is a multifunctional aminoacyl-tRNA synthetase that catalyzes the aminoacylation of glutamic acid and proline tRNA species. Alternative splicing has been observed for this gene, but the full-length nature and biological validity of the variant have not been determined. [provided by RefSeq, Jul 2008]Expression: Ubiquitous expression in thyroid (RPKM 31.6), appendix (RPKM 22.6) and 25 other tissues

GLUTAMAATTI eli ,GLUTAMIINIHAPPO, ( Glutamate, glutamic acid, Glu, E)
Glutamyl-tRNA synthases EARS/EPRS1 and EARS2.
Alias: MSE1; gluRS; COXPD12; mtGlnRS. Preferred Names: probable glutamate--tRNA ligase, mitochondrial. Names: glutamate tRNA ligase 2, mitochondrial; glutamate--tRNA ligase; probable glutamyl-tRNA synthetase, mitochondrial.
Summary: This gene encodes a member of the class I family of aminoacyl-tRNA synthetases. These enzymes play a critical role in protein biosynthesis by charging tRNAs with their cognate amino acids. This protein is encoded by the nuclear genome but is likely to be imported to the mitochondrion where it is thought to catalyze the ligation of glutamate to tRNA molecules. Mutations in this gene have been associated with combined oxidative phosphorylation deficiency 12 (COXPD12). Alternative splicing results in multiple transcript variants. [provided by RefSeq, Mar 2015] Expression: Ubiquitous expression in thyroid (RPKM 6.6), testis (RPKM 6.4) and 25 other tissues.

GATC (12q24.31),Glutamyl-tRNA-amidotransferase subunitC
Aliases: 15E1.2; COXPD42 . Expression: Ubiquitous expression in thyroid (RPKM 15.5), lymph node (RPKM 14.0) and 25 other tissues DOI: 10.1042/BJ20131107 Glutamyl-tRNAGln amidotransferase is essential for mammalian mitochondrial translation in vivo. Echevarría L, et al. Biochem J, 2014 May 15. PMID 24579914 Biogenesis of glutaminyl-mt tRNAGln in human mitochondria. Nagao A, et al. Proc Natl Acad Sci U S A, 2009 Sep 22. PMID 19805282, Free PMC Article
 
GATB (4q31.3) Glutamyl-tRNA-amidotransferase subunit B
PET112, COXPD41, HSPC199, PET112L.


(*) Biogenesis of Glutaminyl-Mt tRNAGln in Human Mitochondria:
Mammalian mitochondrial (mt) tRNAs, which are required for mitochondrial protein synthesis, are all encoded in the mitochondrial genome, while mt aminoacyl-tRNA synthetases (aaRSs) are encoded in the nuclear genome. However, no mitochondrial homolog of glutaminyl-tRNA synthetase (GlnRS) has been identified in mammalian genomes  , implying that Gln-tRNA(Gln) is synthesized via an indirect pathway in the mammalian mitochondria. We demonstrate here that human mt glutamyl-tRNA synthetase (mtGluRS efficiently misaminoacylates mt tRNA(Gln) to form Glu-tRNA(Gln). In addition, we have identified a human homolog of the Glu-tRNA(Gln) amidotransferase, the hGatCAB heterotrimer. When any of the hGatCAB subunits were inactivated by siRNA-mediated knock down in human cells, the Glu-charged form of tRNA(Gln) accumulated and defects in respiration could be observed. We successfully reconstituted in vitro Gln-tRNA(Gln) formation catalyzed by the recombinant mtGluRS and hGatCAB. The misaminoacylated form of tRNA(Gln) has a weak binding affinity to the mt elongation factor Tu (mtEF-Tu), indicating that the misaminoacylated form of tRNA(Gln) is rejected from the translational apparatus to maintain the accuracy of mitochondrial protein synthesis.



GLUTAMIINI, Glutamine, , (Gln, Q)
Glutaminyl-tRNA synthetase QARS1 and 2:

Aliases: QARS; GLNRS; MSCCA; PRO2195.
Summary: Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAs, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. In metazoans, 9 aminoacyl-tRNA synthetases specific for glutamine (gln), glutamic acid (glu), and 7 other amino acids are associated within a multienzyme complex. Although present in eukaryotes, glutaminyl-tRNA synthetase (QARS) is absent from many prokaryotes, mitochondria, and chloroplasts, in which Gln-tRNA(Gln) is formed by transamidation (*)of the misacylated Glu-tRNA(Gln). Glutaminyl-tRNA synthetase belongs to the class-I aminoacyl-tRNA synthetase family. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2013]
Expression: Ubiquitous expression in colon (RPKM 48.6), skin (RPKM 46.9) and 25 other tissues
Interaction of HIV-1 Gag with glutaminyl-tRNA synthetase (QARS) is identified in a series of six affinity purification/mass spectrometry screens.
HIV-1 MA is identified to have a physical interaction with glutaminyl-tRNA synthetase (QARS) in human HEK293 and/or Jurkat cell lines by using affinity tagging and purification mass spectrometry analyses .
QARS2  encoded by nuclear genome    is  absent in mitochondria, Mitokondrial entsyme  Gln-tRNA(Gln) is formed by transamidation (*).

CYSTEIINI aminohappo,  Cystein, i (Cys, C)
Cysteinyl-tRNA synthetases CARS1 and 2: 

Aliases: CARS; MDBH; CYSRS; MCDDBH; MGC:11246Summary: This gene encodes a class 1 aminoacyl-tRNA synthetase, cysteinyl-tRNA synthetase. Each of the twenty aminoacyl-tRNA synthetases catalyzes the aminoacylation of a specific tRNA or tRNA isoaccepting family with the cognate amino acid. This gene is one of several located near the imprinted gene domain on chromosome 11p15.5, an important tumor-suppressor gene region. Alterations in this region have been associated with Beckwith-Wiedemann syndrome, Wilms tumor, rhabdomyosarcoma, adrenocortical carcinoma, and lung, ovarian and breast cancers. Alternative splicing of this gene results in multiple transcript variants. [provided by RefSeq, Aug 2010]Expression: Ubiquitous expression in thyroid (RPKM 12.8), brain (RPKM 10.8) and 25 other tissues .

Alias: cysRS; COXPD27. Summary: This gene encodes a putative member of the class I family of aminoacyl-tRNA synthetases. These enzymes play a critical role in protein biosynthesis by charging tRNAs with their cognate amino acids. This protein is encoded by the nuclear genome but is likely to be imported to the mitochondrion where it is thought to catalyze the ligation of cysteine to tRNA molecules. A splice-site mutation in this gene has been associated with a novel progressive myoclonic epilepsy disease with similar symptoms to MERRF syndrome. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jun 2017] Expression: Ubiquitous expression in spleen (RPKM 6.3), bone marrow (RPKM 6.0) and 25 other tissue.

METIONIINI aminohappo, Methionine, (Met, M)
Methionyl-tRNA synthetases MARS 1 and 2:
Aliases: MRS; ILLD; MARS; CMT2U; ILFS2; METRS; MTRNS; SPG70Summary This gene encodes a member of the class I family of aminoacyl-tRNA synthetases. These enzymes play a critical role in protein biosynthesis by charging tRNAs with their cognate amino acids. The encoded protein is a component of the multi-tRNA synthetase complex and catalyzes the ligation of methionine to tRNA molecules. [provided by RefSeq, Jan 2011]Expression: Ubiquitous expression in testis (RPKM 31.8), appendix (RPKM 28.7) and 25 other tissues
HIV-1 interaction: Interaction of HIV-1 Gag with methionyl-tRNA synthetase (MARS) is identified in a series of six affinity purification/mass spectrometry screens
HIV-1 MA is identified to have a physical interaction with methionyl-tRNA synthetase (MARS) in human HEK293 and/or Jurkat cell lines by using affinity tagging and purification mass spectrometry analyses  https://pubmed.ncbi.nlm.nih.gov/29775242/

Aliases: MetRS; COXPD25; mtMetRSSummary: This gene produces a mitochondrial methionyl-tRNA synthetase protein that is encoded by the nuclear genome and imported to the mitochondrion. This protein likely functions as a monomer and is predicted to localize to the mitochondrial matrix. Mutations in this gene are associated with the autosomal recessive neurodegenerative disease spastic ataxia-3 (SPAX3). [provided by RefSeq, Apr 2014]

LYSIINI aminohaapo, Lysine,( Lys, K)
 Lysyl-tRNA synthetases KARS1(KARS2):

Aliases; KRS; KARS; KARS2; CMTRIB; DFNB89 Summary: Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. Lysyl-tRNA synthetase is a homodimer localized to the cytoplasm which belongs to the class II family of tRNA synthetases. It has been shown to be a target of autoantibodies in the human autoimmune diseases, polymyositis or dermatomyositis. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008] Expression: Ubiquitous expression in testis (RPKM 57.5), lymph node (RPKM 40.9) and 25 other tissues 

KARS2: See KARS1 (KARS2) lysyl-tRNA synthetase 1 in the Gene database


ARGINIINI aminohappo, Arginine,  (Arg, R)
Arginyl-tRNA syntethasis RARS1 and 2:

Alias: HLD9; RARS; ArgRS; DALRD1Summary: Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAs, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. Arginyl-tRNA synthetase belongs to the class-I aminoacyl-tRNA synthetase family. [provided by RefSeq, Jul 2008] Expression Ubiquitous expression in duodenum (RPKM 28.0), small intestine (RPKM 25.9) and 25 other tissues . https://pubmed.ncbi.nlm.nih.gov/20923763/ Interaction of HIV-1 Gag with arginyl-tRNA synthetase (RARS) is identified in a series of six affinity purification/mass spectrometry screens. HIV-1 MA is identified to have a physical interaction with arginyl-tRNA synthetase (RARS) in human HEK293 and/or Jurkat cell lines by using affinity tagging and purification mass spectrometry analyses

Aliases: PCH6; ArgRS; RARSL; DALRD2; PRO1992
Summary: This nuclear gene encodes a protein that localizes to the mitochondria, where it catalyzes the transfer of L-arginine to its cognate tRNA, an important step in translation of mitochondrially-encoded proteins. Defects in this gene are a cause of pontocerebellar hypoplasia type 6 (PCH6). Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2016]Expression: Ubiquitous expression in adrenal (RPKM 9.8), testis (RPKM 8.4) and 25 other tissues

TYROSIINI aminohappo, Tyrosine,  (Tyr, Y)
Tyrosinyl-tRNA synthetasis YARS 1 and 2:

Alias:YRS; YTS; YARS; TYRRS; CMTDIC. Summary:Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAs, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. Tyrosyl-tRNA synthetase belongs to the class I tRNA synthetase family. Cytokine activities have also been observed for the human tyrosyl-tRNA synthetase, after it is split into two parts, an N-terminal fragment that harbors the catalytic site and a C-terminal fragment found only in the mammalian enzyme. The N-terminal fragment is an interleukin-8-like cytokine, whereas the released C-terminal fragment is an EMAP II-like cytokine. [provided by RefSeq, Jul 2008] Expression:Ubiquitous expression in thyroid (RPKM 25.7), brain (RPKM 24.4) and 25 other tissues
Oncogenic protein. HIV-1 gp120 upregulates the expression of tyrosyl-tRNA synthetase in T-cell lines .
Aliases:TYRRS; CGI-04; MLASA2; MT-TYRRS.Summary: This gene encodes a mitochondrial protein that catalyzes the attachment of tyrosine to tRNA(Tyr). Mutations in this gene are associated with myopathy with lactic acidosis and sideroblastic anemia type 2 (MLASA2). [provided by RefSeq, Jan 2011] Expression: Ubiquitous expression in brain (RPKM 10.0), endometrium (RPKM 8.1) and 25 other tissues https://pubmed.ncbi.nlm.nih.gov/30026338/
TRYPTOFAANI aminohappo, Tryptophane,  (Trp.W)
Tryptophanyl-tRNA synthetasis WARS1 and 2 

Alias: GAMMA-2, HMN9, IFI53, IFP53, WARS
Sytoplasminen. Interferoni indusoi tätä. Expressiota placentassa ja appendixissa eniten.
Evoluution varhaisinta. ( Trp on ihmiselle essentielli aminohappo) WARS1P1  pseudogeeni kromosomissa 11.
WARSP2 (1p12).
Alias: NEMMLAS, TrpPS, mtTrpPSA. Mitokondriaalinen.
WARSP2P1 pseudogeeni on kromosomissa 10.

HISTIDIINI aminohappo, Histidine  (His, H)
Histidyl-tRNA synthetases HARS 1 and 2:

HARS1, (5q31.3)Histidyl-tRNA sythetase 1 (5q31.3)
Sytoplasminen
Alias: HARS1, CMT2W, HARS, HRS, USH3B, HisRS,Jo-1 antigen, Histidine translase.

HARS2 (5q31.3), mitochondrial
Alias: HO3; HARSL; HARSR; HisRS; PRLTS2 SummaryAminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene is an enzyme belonging to the class II family of aminoacyl-tRNA synthetases. Functioning in the synthesis of histidyl-transfer RNA, the enzyme plays an accessory role in the regulation of protein biosynthesis. The gene is located in a head-to-head orientation with HARS on chromosome five, where the homologous genes likely share a bidirectional promoter. Mutations in this gene are associated with the pathogenesis of Perrault syndrome, which involves ovarian dysgenesis and sensorineural hearing loss. Alternative splicing results in multiple transcript variants of this gene. [provided by RefSeq, Jul 2013] Expression Ubiquitous expression in colon (RPKM 9.6), endometrium (RPKM 9.1) and 25 other tissues

 PROLIINI aminohappo, proline (Pro, P)
Prolyl-tRNA synthetases PARS (EPRS1) and PARS2
EPRS1 (1q419 Glutamyl-Prolyl-tRNA synthetase, multifunctional

ALIASES: proRS; EIEE75; MT-PRORS Summary: This gene encodes a putative member of the class II family of aminoacyl-tRNA synthetases. These enzymes play a critical role in protein biosynthesis by charging tRNAs with their cognate amino acids. This protein is encoded by the nuclear genome but is likely to be imported to the mitochondrion where it is thought to catalyze the ligation of proline to tRNA molecules. Mutations have been found in this gene in some patients with Alpers syndrome. [provided by RefSeq, Mar 2015] Expression: Ubiquitous expression in testis (RPKM 3.4), ovary (RPKM 2.8) and 24 other. https://doi.org/10.1371/journal.pone.0158202

Muistiin 6.7.2020
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