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P12081 (SYHC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histidine--tRNA ligase, cytoplasmic

EC=6.1.1.21
Alternative name(s):
Histidyl-tRNA synthetase
Short name=HisRS
Gene names
Name:HARS
Synonyms:HRS
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length509 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + L-histidine + tRNA(His) = AMP + diphosphate + L-histidyl-tRNA(His).

Subcellular location

Cytoplasm.

Tissue specificity

Brain, heart, liver and kidney.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family.

Contains 1 WHEP-TRS domain.

Sequence caution

The sequence CAA28956.1 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processhistidyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytosol

Traceable author statement. Source: Reactome

   Molecular functionATP binding

Non-traceable author statement. Source: UniProtKB

histidine-tRNA ligase activity

Non-traceable author statement Ref.1Ref.5. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 509508Histidine--tRNA ligase, cytoplasmic
PRO_0000136332

Regions

Domain3 – 5957WHEP-TRS

Amino acid modifications

Modified residue21N-acetylalanine Ref.6
Modified residue4431N6-acetyllysine Ref.7

Natural variations

Natural variant3991A → V.
Corresponds to variant rs34732372 [ dbSNP | Ensembl ].
VAR_061908

Experimental info

Sequence conflict61A → P in CAA28956. Ref.2
Sequence conflict1651R → G in CAA28956. Ref.2
Sequence conflict1811N → Q in CAA28956. Ref.2
Sequence conflict1861I → N in CAA28956. Ref.2
Sequence conflict1911C → S in CAA28956. Ref.2
Sequence conflict2061D → N in CAA28956. Ref.2
Sequence conflict2231I → V in CAA28956. Ref.2
Sequence conflict2271S → P in CAA28956. Ref.2
Sequence conflict2841L → V in CAA28956. Ref.2
Sequence conflict3471A → E in CAA28956. Ref.2
Sequence conflict373 – 3742KG → QR in CAA28956. Ref.2
Sequence conflict4931D → E in CAA28956. Ref.2

Secondary structure

..... 509
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12081 [UniParc].

Last modified May 1, 1992. Version 2.
Checksum: 65D8BB71CE79B1FF

FASTA50957,411
        10         20         30         40         50         60 
MAERAALEEL VKLQGERVRG LKQQKASAEL IEEEVAKLLK LKAQLGPDES KQKFVLKTPK 

        70         80         90        100        110        120 
GTRDYSPRQM AVREKVFDVI IRCFKRHGAE VIDTPVFELK ETLMGKYGED SKLIYDLKDQ 

       130        140        150        160        170        180 
GGELLSLRYD LTVPFARYLA MNKLTNIKRY HIAKVYRRDN PAMTRGRYRE FYQCDFDIAG 

       190        200        210        220        230        240 
NFDPMIPDAE CLKIMCEILS SLQIGDFLVK VNDRRILDGM FAICGVSDSK FRTICSSVDK 

       250        260        270        280        290        300 
LDKVSWEEVK NEMVGEKGLA PEVADRIGDY VQQHGGVSLV EQLLQDPKLS QNKQALEGLG 

       310        320        330        340        350        360 
DLKLLFEYLT LFGIDDKISF DLSLARGLDY YTGVIYEAVL LQTPAQAGEE PLGVGSVAAG 

       370        380        390        400        410        420 
GRYDGLVGMF DPKGRKVPCV GLSIGVERIF SIVEQRLEAL EEKIRTTETQ VLVASAQKKL 

       430        440        450        460        470        480 
LEERLKLVSE LWDAGIKAEL LYKKNPKLLN QLQYCEEAGI PLVAIIGEQE LKDGVIKLRS 

       490        500 
VTSREEVDVR REDLVEEIKR RTGQPLCIC 

« Hide

References

« Hide 'large scale' references
[1]"Human histidyl-tRNA synthetase: recognition of amino acid signature regions in class 2a aminoacyl-tRNA synthetases."
Raben N., Borriello F., Amin J., Horwitz R., Fraser D., Plotz P.
Nucleic Acids Res. 20:1075-1081(1992) [PubMed: 1549469] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Isolation, structure and expression of mammalian genes for histidyl-tRNA synthetase."
Tsui F.W.L., Siminovitch L.
Nucleic Acids Res. 15:3349-3367(1987) [PubMed: 3554142] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung and Uterus.
[4]"Transcriptional analyses of the gene region that encodes human histidyl-tRNA synthetase: identification of a novel bidirectional regulatory element."
Tsui H.W., Mok S., de Souza L., Martin A., Tsui F.W.L.
Gene 131:201-208(1993) [PubMed: 8406012] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
[5]"A novel gene oriented in a head-to-head configuration with the human histidyl-tRNA synthetase (HRS) gene encodes an mRNA that predicts a polypeptide homologous to HRS."
O'Hanlon T.P., Raben N., Miller F.W.
Biochem. Biophys. Res. Commun. 210:556-566(1995) [PubMed: 7755634] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
[6]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[7]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-443, MASS SPECTROMETRY.
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Solution structures of the WHEP-TRS domain of human histidyl-tRNA synthetase."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 1-60.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z11518 mRNA. Translation: CAA77607.1.
X05345 mRNA. Translation: CAA28956.1. Frameshift.
BC011807 mRNA. Translation: AAH11807.1.
BC080514 mRNA. Translation: AAH80514.1.
M96646 Genomic DNA. Translation: AAA58668.1.
U18936 Genomic DNA. Translation: AAA73973.1.
IPIIPI00021808.
PIRSYHUHT. I37559.
RefSeqNP_002100.2. NM_002109.3.
UniGeneHs.528050.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1X59NMR-A1-60[»]
ProteinModelPortalP12081.
SMRP12081. Positions 1-502.
ModBaseSearch...

Protein-protein interaction databases

IntActP12081. 1 interaction.
STRINGP12081.

PTM databases

PhosphoSiteP12081.

Polymorphism databases

DMDM135123.

Proteomic databases

PeptideAtlasP12081.
PRIDEP12081.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000307633; ENSP00000304668; ENSG00000170445.
GeneID3035.
KEGGhsa:3035.
NMPDRfig|9606.3.peg.25876.
UCSCuc003lgu.1. human.

Organism-specific databases

CTD3035.
GeneCardsGC05M140034.
H-InvDBHIX0005239.
HGNCHGNC:4816. HARS.
HPAHPA036539.
MIM142810. gene.
neXtProtNX_P12081.
PharmGKBPA29191.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG19383.
GeneTreeENSGT00390000005922.
HOGENOMHBG616575.
HOVERGENHBG002731.
InParanoidP12081.
OMALVSELWD.
PhylomeDBP12081.

Enzyme and pathway databases

BRENDA6.1.1.21. 2681.
ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressP12081.
BgeeP12081.
CleanExHS_HARS.
GenevestigatorP12081.
GermOnlineENSG00000170445. Homo sapiens.

Family and domain databases

InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR015807. His-tRNA-synth_IIa_subgr.
IPR004516. His-tRNA_synth_IIA.
IPR009068. S15_NS1_RNA-bd.
IPR000738. WHEP-TRS.
[Graphical view]
Gene3DG3DSA:3.40.50.800. Anticodon_bd. 1 hit.
G3DSA:1.10.287.10. S15_NS1_RNA_bd. 1 hit.
KOK01892.
PANTHERPTHR11476. His-tRNA_synth. 1 hit.
PfamPF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF00458. WHEP-TRS. 1 hit.
[Graphical view]
PIRSFPIRSF001549. His-tRNA_synth. 1 hit.
SMARTSM00991. WHEP-TRS. 1 hit.
[Graphical view]
SUPFAMSSF52954. Anticodon_bd. 1 hit.
SSF47060. S15/NS1_bind. 1 hit.
TIGRFAMsTIGR00442. HisS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
PS00762. WHEP_TRS_1. 1 hit.
PS51185. WHEP_TRS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

DrugBankDB00117. L-Histidine.
NextBio12014.
SOURCESearch...

Entry information

Entry nameSYHC_HUMAN
AccessionPrimary (citable) accession number: P12081
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: May 1, 1992
Last modified: January 25, 2012
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families