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0SYHH_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameHARSL
DescriptionHistidyl-trna synthetase homolog (ec 6.1.1.21) (histidine--trna ligase homolog) (hisrs).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005737 cytoplasm (NAS)
0005524 ATP binding (NAS)
0004821 histidine-tRNA ligase activity (NAS)
0006412 protein biosynthesis (NAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
The aminoacyl-tRNA synthetases () catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction. These proteins differ widely in size and oligomeric state.nd have limited sequence homology . The 20 aminoacyl-tRNA synthetases are divided into two classes. and II. Class I aminoacyl-tRNA synthetases contain a characteristic Rossman fold and are mostly monomeric .hile class II aminoacyl-tRNA synthetases share an anti-parallel beta-sheet formation.lanked byalpha-helices .nd are mostly dimeric or multimeric. In reactions catalysed by the class I aminoacyl-tRNA synthetases.he aminoacyl group is coupled to the 2-hydroxyl of the tRNA.hile.nclass II reactions.he 3-hydroxyl site is preferred. The synthetases specific for arginine.ysteine.lutamic acid.lutamine.soleucine.eucine.ethionine.yrosine.ryptophan and valine belong to class I synthetases.The synthetases specific for alanine.sparagine.spartic acid.lycine.istidine.ysine.henylalanine.roline.erine.nd threonine belong to class-II synthetases .The 10 class I synthetases are considered to have in common the catalytic domain structure based on the Rossmann fold.hich is totally different from the class II catalytic domain structure. The class I synthetases are further divided into three subclasses.. and c.ccording to sequence homology. tRNA binding involves an alpha-helical structure that is conserved between class I and class II synthetases.Class-II tRNA synthetases do not share a high degree of similarity.owever at least three conserved regions are present . This domain includes the glycine.istidine.roline.hreonine and serine tRNA synthetases.
  IPR002314:tRNA synthetase, class II (G, H, P and S)
tRNA synthetases.r tRNA ligases are involved in protein synthesis. This domain is found in histidyl.lycyl.hreonyl and prolyl tRNA synthetases it is probably the anticodon binding domain .
  IPR004154:Anticodon-binding
The aminoacyl-tRNA synthetases () catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction. These proteins differ widely in size and oligomeric state.nd have limited sequence homology . The 20 aminoacyl-tRNA synthetases are divided into two classes. and II. Class I aminoacyl-tRNA synthetases contain a characteristic Rossman fold and are mostly monomeric .hile class II aminoacyl-tRNA synthetases share an anti-parallel beta-sheet formation.lanked byalpha-helices .nd are mostly dimeric or multimeric. In reactions catalysed by the class I aminoacyl-tRNA synthetases.he aminoacyl group is coupled to the 2-hydroxyl of the tRNA.hile.nclass II reactions.he 3-hydroxyl site is preferred. The synthetases specific for arginine.ysteine.lutamic acid.lutamine.soleucine.eucine.ethionine.yrosine.ryptophan and valine belong to class I synthetases.The synthetases specific for alanine.sparagine.spartic acid.lycine.istidine.ysine.henylalanine.roline.erine.nd threonine belong to class-II synthetases .The 10 class I synthetases are considered to have in common the catalytic domain structure based on the Rossmann fold.hich is totally different from the class II catalytic domain structure. The class I synthetases are further divided into three subclasses.. and c.ccording to sequence homology. tRNA binding involves an alpha-helical structure that is conserved between class I and class II synthetases.Class-II tRNA synthetases do not share a high degree of similarity.owever at least three conserved regions are present . Histidyl-tRNA synthetase () is an alpha2 dimer that belongs to class IIa. Every completed genome includes a histidyl-tRNA synthetase. Apparent second copies from Bacillus subtilis.ynechocystis sp..nd Aquifex aeolicus are slightly shorter.ore closely related to each other than to other hisS proteins.nd not demonstrated to act as histidyl-tRNA synthetases (see ). Theregulatory protein kinase GCN2 of Saccharomyces cerevisiae (YDR283c).nd related proteins from other species designated eIF-2 alpha kinase.ave a domain closely related to histidyl-tRNA synthetase that may serve to detect and respond to uncharged tRNA(his).n indicator of amino acid starvation.ut these regulatory proteins are not orthologous.
  IPR004516:Histidyl-tRNA synthetase, class IIa
IPR002314:tRNA-synt_2b 
Evalue:-35.9208183288574 
Location:73-235IPR004154:HGTP_anticodon 
Evalue:-23.9208183288574 
Location:411-502
SequencesProtein: SYHH_HUMAN (506 aa)
mRNA: NM_012208
Local Annotation
Synapse Ontology
Calcium release from RyR (Ryanodine Receptor) in the SR (Sarcoplasmic Reticulum) is activated by the calcium induced-calcium-release
sdb:0325 RyR-CICR  (Evidence:keywords)
KO assignmentK01891
  Level 3 annotation:
    histidyl-tRNA synthetase
  Level 2 annotation:
    Histidine metabolism
    Aminoacyl-tRNA biosynthesis
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 109 residues, 140051201-140051525Exon2: 27 residues, 140053359-140053434Exon3: 42 residues, 140053703-140053823Exon4: 34 residues, 140053953-140054049Exon5: 44 residues, 140055276-140055402Exon6: 38 residues, 140055506-140055614Exon7: 35 residues, 140055871-140055970Exon8: 33 residues, 140056289-140056383Exon9: 44 residues, 140056711-140056839Exon10: 83 residues, 140056932-140057175Exon11: 41 residues, 140057337-140057454Exon12: 51 residues, 140057700-140057847Exon13: 272 residues, 140058261-140059073Exon14: 2 residues, -Jump to SYHH_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3481 140051201-140059073 ~-8K 29557(HARSL)(+)Loci: 3482 140146059-140372113 ~-226K 29559(PCDHA1)(+)Loci: 3483 140411162-140413696 ~-3K 29584(PCDHB1)(+)Loci: 3484 140454420-140457146 ~-3K 29585(PCDHB2)(+)Loci: 3485 140460417-140463589 ~-3K 29586(PCDHB3)(+)Loci: 3486 140481764-140485385 ~-4K 29587(PCDHB4)(+)Loci: 3487 140494983-140497887 ~-3K 29588(PCDHB5)(+)Loci: 3488 140510022-140513050 ~-3K 29589(PCDHB6)(+)Loci: 3489 140532426-140536140 ~-4K 29592(PCDHB7)(+)Loci: 3490 140541163-140545979 ~-5K 29593(PCDHB16)(+)Loci: 3491 140552135-140555397 ~-3K 29594(PCDHB10)(+)Loci: 3492 140559531-140562801 ~-3K 29596(PCDHB11)(+)Loci: 3493 140568474-140571880 ~-3K 29597(PCDHB12)(+)Loci: 3494 140573692-140577177 ~-3K 29598(PCDHB13)(+)Loci: 3495 140583261-140586042 ~-3K 29599(PCDHB14)(+)Loci: 3496 140605330-140607983 ~-3K 29601(PCDHB15)(+)Loci: 4735 140662380-140663796 ~-1K 29602(SLC25A2)(-)Loci: 3497 140690435-140872730 ~-182K 29604(PCDHGA1)(+)Loci: 4736 140874772-140978691 ~-104K 29642(DIAPH1)(-)Loci: 4737 141013153-141041984 ~-29K 29650(CENTD3)(-)Loci: 4734 140033674-140051155 ~-17K 29556(HARS)(-)Link out to UCSC