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P12081

- SYHC_HUMAN

UniProt

P12081 - SYHC_HUMAN

Protein

Histidine--tRNA ligase, cytoplasmic

Gene

HARS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 2 (01 May 1992)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. histidine-tRNA ligase activity Source: UniProtKB

    GO - Biological processi

    1. gene expression Source: Reactome
    2. histidyl-tRNA aminoacylation Source: InterPro
    3. translation Source: UniProtKB
    4. tRNA aminoacylation for protein translation Source: Reactome

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi6.1.1.21. 2681.
    ReactomeiREACT_15306. Cytosolic tRNA aminoacylation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histidine--tRNA ligase, cytoplasmic (EC:6.1.1.21)
    Alternative name(s):
    Histidyl-tRNA synthetase
    Short name:
    HisRS
    Gene namesi
    Name:HARS
    Synonyms:HRS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:4816. HARS.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Usher syndrome 3B (USH3B) [MIM:614504]: A syndrome characterized by progressive vision and hearing loss during early childhood. Some patients have the so-called 'Charles Bonnet syndrome,' involving decreased visual acuity and vivid visual hallucinations. USH is a genetically heterogeneous condition characterized by the association of retinitis pigmentosa with sensorineural deafness. Age at onset and differences in auditory and vestibular function distinguish Usher syndrome type 1 (USH1), Usher syndrome type 2 (USH2) and Usher syndrome type 3 (USH3). USH3 is characterized by postlingual, progressive hearing loss, variable vestibular dysfunction, and onset of retinitis pigmentosa symptoms, including nyctalopia, constriction of the visual fields, and loss of central visual acuity, usually by the second decade of life.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti454 – 4541Y → S in USH3B. 1 Publication
    VAR_067918
    HARS mutations may be involved in peripheral neuropathy, a disease mainly characterized by distal motor and sensory dysfunction. Inherited peripheral neuropathies are clinically and genetically heterogeneous with variable age of onset and reduced penetrance associated with specific loci. HARS mutations may directly predispose patients to peripheral neuropathy or may modify a peripheral neuropathy phenotype by contributing to the genetic and environmental load in a given patient (PubMed:22930593).1 Publication

    Keywords - Diseasei

    Deafness, Disease mutation, Neuropathy, Retinitis pigmentosa, Usher syndrome

    Organism-specific databases

    MIMi614504. phenotype.
    Orphaneti231183. Usher syndrome type 3.
    PharmGKBiPA29191.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 509508Histidine--tRNA ligase, cytoplasmicPRO_0000136332Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP12081.
    PaxDbiP12081.
    PeptideAtlasiP12081.
    PRIDEiP12081.

    PTM databases

    PhosphoSiteiP12081.

    Expressioni

    Tissue specificityi

    Brain, heart, liver and kidney.

    Gene expression databases

    ArrayExpressiP12081.
    BgeeiP12081.
    CleanExiHS_HARS.
    GenevestigatoriP12081.

    Organism-specific databases

    HPAiHPA036539.

    Interactioni

    Protein-protein interaction databases

    BioGridi109285. 29 interactions.
    DIPiDIP-37596N.
    IntActiP12081. 2 interactions.
    MINTiMINT-3007818.
    STRINGi9606.ENSP00000304668.

    Structurei

    Secondary structure

    1
    509
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi2 – 2322
    Helixi28 – 4518
    Helixi67 – 8620
    Beta strandi96 – 994
    Helixi100 – 1034
    Beta strandi125 – 1273
    Helixi132 – 14110
    Beta strandi147 – 15610
    Beta strandi169 – 18012
    Helixi186 – 20217
    Beta strandi207 – 2137
    Helixi214 – 22411
    Helixi228 – 23811
    Helixi239 – 2424
    Helixi246 – 25510
    Helixi261 – 27111
    Beta strandi274 – 2763
    Helixi277 – 2837
    Helixi287 – 2904
    Helixi293 – 31119
    Helixi315 – 3173
    Beta strandi318 – 3214
    Turni328 – 3303
    Beta strandi332 – 34211
    Beta strandi352 – 36211
    Helixi367 – 3693
    Beta strandi371 – 3733
    Beta strandi379 – 3846
    Helixi386 – 39813
    Turni399 – 4013
    Beta strandi411 – 4144
    Beta strandi416 – 4194
    Helixi421 – 43313
    Beta strandi438 – 4403
    Beta strandi442 – 4454
    Helixi448 – 45811
    Beta strandi462 – 4654
    Helixi468 – 4736
    Beta strandi475 – 4806
    Turni481 – 4833
    Beta strandi486 – 4905
    Helixi491 – 4933
    Helixi494 – 5029

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1X59NMR-A1-60[»]
    2LW7NMR-A2-509[»]
    4G84X-ray2.40A/B54-506[»]
    4G85X-ray3.11A/B1-506[»]
    ProteinModelPortaliP12081.
    SMRiP12081. Positions 1-508.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12081.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 5957WHEP-TRSAdd
    BLAST

    Sequence similaritiesi

    Contains 1 WHEP-TRS domain.Curated

    Phylogenomic databases

    eggNOGiCOG0124.
    HOGENOMiHOG000018075.
    HOVERGENiHBG002731.
    InParanoidiP12081.
    KOiK01892.
    OMAiIFSITKA.
    PhylomeDBiP12081.
    TreeFamiTF300652.

    Family and domain databases

    Gene3Di1.10.287.10. 1 hit.
    3.40.50.800. 1 hit.
    HAMAPiMF_00127. His_tRNA_synth.
    InterProiIPR002314. aa-tRNA-synt_IIb_cons-dom.
    IPR006195. aa-tRNA-synth_II.
    IPR004154. Anticodon-bd.
    IPR015807. His-tRNA-ligase.
    IPR004516. HisRS/HisZ.
    IPR009068. S15_NS1_RNA-bd.
    IPR000738. WHEP-TRS.
    [Graphical view]
    PANTHERiPTHR11476. PTHR11476. 1 hit.
    PfamiPF03129. HGTP_anticodon. 1 hit.
    PF00587. tRNA-synt_2b. 1 hit.
    PF00458. WHEP-TRS. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001549. His-tRNA_synth. 1 hit.
    SMARTiSM00991. WHEP-TRS. 1 hit.
    [Graphical view]
    SUPFAMiSSF47060. SSF47060. 1 hit.
    SSF52954. SSF52954. 1 hit.
    TIGRFAMsiTIGR00442. hisS. 1 hit.
    PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
    PS00762. WHEP_TRS_1. 1 hit.
    PS51185. WHEP_TRS_2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P12081-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAERAALEEL VKLQGERVRG LKQQKASAEL IEEEVAKLLK LKAQLGPDES    50
    KQKFVLKTPK GTRDYSPRQM AVREKVFDVI IRCFKRHGAE VIDTPVFELK 100
    ETLMGKYGED SKLIYDLKDQ GGELLSLRYD LTVPFARYLA MNKLTNIKRY 150
    HIAKVYRRDN PAMTRGRYRE FYQCDFDIAG NFDPMIPDAE CLKIMCEILS 200
    SLQIGDFLVK VNDRRILDGM FAICGVSDSK FRTICSSVDK LDKVSWEEVK 250
    NEMVGEKGLA PEVADRIGDY VQQHGGVSLV EQLLQDPKLS QNKQALEGLG 300
    DLKLLFEYLT LFGIDDKISF DLSLARGLDY YTGVIYEAVL LQTPAQAGEE 350
    PLGVGSVAAG GRYDGLVGMF DPKGRKVPCV GLSIGVERIF SIVEQRLEAL 400
    EEKIRTTETQ VLVASAQKKL LEERLKLVSE LWDAGIKAEL LYKKNPKLLN 450
    QLQYCEEAGI PLVAIIGEQE LKDGVIKLRS VTSREEVDVR REDLVEEIKR 500
    RTGQPLCIC 509
    Length:509
    Mass (Da):57,411
    Last modified:May 1, 1992 - v2
    Checksum:i65D8BB71CE79B1FF
    GO
    Isoform 2 (identifier: P12081-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         60-99: Missing.

    Show »
    Length:469
    Mass (Da):52,720
    Checksum:iB02783AB9FED1E1D
    GO
    Isoform 3 (identifier: P12081-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         60-99: Missing.
         155-174: Missing.

    Show »
    Length:449
    Mass (Da):50,156
    Checksum:i9B97F9CC4FE63BB9
    GO
    Isoform 4 (identifier: P12081-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         155-174: Missing.

    Show »
    Length:489
    Mass (Da):54,847
    Checksum:iE0C0825FF411F391
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61A → P in CAA28956. (PubMed:3554142)Curated
    Sequence conflicti126 – 1261S → P in BAG58213. (PubMed:14702039)Curated
    Sequence conflicti165 – 1651R → G in CAA28956. (PubMed:3554142)Curated
    Sequence conflicti181 – 1811N → Q in CAA28956. (PubMed:3554142)Curated
    Sequence conflicti186 – 1861I → N in CAA28956. (PubMed:3554142)Curated
    Sequence conflicti191 – 1911C → S in CAA28956. (PubMed:3554142)Curated
    Sequence conflicti206 – 2061D → N in CAA28956. (PubMed:3554142)Curated
    Sequence conflicti223 – 2231I → V in CAA28956. (PubMed:3554142)Curated
    Sequence conflicti227 – 2271S → P in CAA28956. (PubMed:3554142)Curated
    Sequence conflicti284 – 2841L → V in CAA28956. (PubMed:3554142)Curated
    Sequence conflicti347 – 3471A → E in CAA28956. (PubMed:3554142)Curated
    Sequence conflicti373 – 3742KG → QR in CAA28956. (PubMed:3554142)Curated
    Sequence conflicti375 – 3751R → L in BAG58213. (PubMed:14702039)Curated
    Sequence conflicti493 – 4931D → E in CAA28956. (PubMed:3554142)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti5 – 51A → E.1 Publication
    Corresponds to variant rs78741041 [ dbSNP | Ensembl ].
    VAR_069021
    Natural varianti137 – 1371R → Q Found in a patient with peripheral neuropathy; unknown pathological significance; results in loss of function; has a neurotoxic effect in an animal model. 1 Publication
    Corresponds to variant rs191391414 [ dbSNP | Ensembl ].
    VAR_069022
    Natural varianti205 – 2051G → D.1 Publication
    Corresponds to variant rs147288996 [ dbSNP | Ensembl ].
    VAR_069023
    Natural varianti238 – 2381V → A Found in a patient with peripheral neuropathy; unknown pathological role. 1 Publication
    VAR_069024
    Natural varianti376 – 3761K → R.1 Publication
    Corresponds to variant rs139447495 [ dbSNP | Ensembl ].
    VAR_069025
    Natural varianti399 – 3991A → V.
    Corresponds to variant rs34732372 [ dbSNP | Ensembl ].
    VAR_061908
    Natural varianti454 – 4541Y → S in USH3B. 1 Publication
    VAR_067918
    Natural varianti505 – 5051P → S Found in a patient with peripheral neuropathy; unknown pathological role. 1 Publication
    VAR_069026

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei60 – 9940Missing in isoform 2 and isoform 3. 1 PublicationVSP_045118Add
    BLAST
    Alternative sequencei155 – 17420Missing in isoform 3 and isoform 4. 2 PublicationsVSP_046662Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z11518 mRNA. Translation: CAA77607.1.
    X05345 mRNA. Translation: CAA28956.1. Frameshift.
    AK295219 mRNA. Translation: BAG58213.1.
    AK302295 mRNA. Translation: BAG63635.1.
    AK225776 mRNA. No translation available.
    AC116353 Genomic DNA. No translation available.
    BC011807 mRNA. Translation: AAH11807.1.
    BC080514 mRNA. Translation: AAH80514.1.
    M96646 Genomic DNA. Translation: AAA58668.1.
    U18936 Genomic DNA. Translation: AAA73973.1.
    CCDSiCCDS4237.1. [P12081-1]
    CCDS58976.1. [P12081-2]
    CCDS58977.1. [P12081-3]
    CCDS58978.1. [P12081-4]
    PIRiI37559. SYHUHT.
    RefSeqiNP_001244969.1. NM_001258040.2. [P12081-2]
    NP_001244970.1. NM_001258041.2. [P12081-4]
    NP_001244971.1. NM_001258042.2. [P12081-3]
    NP_002100.2. NM_002109.5. [P12081-1]
    UniGeneiHs.528050.

    Genome annotation databases

    EnsembliENST00000307633; ENSP00000304668; ENSG00000170445. [P12081-3]
    ENST00000438307; ENSP00000411511; ENSG00000170445. [P12081-2]
    ENST00000457527; ENSP00000387893; ENSG00000170445. [P12081-4]
    ENST00000504156; ENSP00000425634; ENSG00000170445. [P12081-1]
    GeneIDi3035.
    KEGGihsa:3035.
    UCSCiuc003lgu.3. human. [P12081-1]
    uc011czm.3. human.

    Polymorphism databases

    DMDMi135123.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z11518 mRNA. Translation: CAA77607.1 .
    X05345 mRNA. Translation: CAA28956.1 . Frameshift.
    AK295219 mRNA. Translation: BAG58213.1 .
    AK302295 mRNA. Translation: BAG63635.1 .
    AK225776 mRNA. No translation available.
    AC116353 Genomic DNA. No translation available.
    BC011807 mRNA. Translation: AAH11807.1 .
    BC080514 mRNA. Translation: AAH80514.1 .
    M96646 Genomic DNA. Translation: AAA58668.1 .
    U18936 Genomic DNA. Translation: AAA73973.1 .
    CCDSi CCDS4237.1. [P12081-1 ]
    CCDS58976.1. [P12081-2 ]
    CCDS58977.1. [P12081-3 ]
    CCDS58978.1. [P12081-4 ]
    PIRi I37559. SYHUHT.
    RefSeqi NP_001244969.1. NM_001258040.2. [P12081-2 ]
    NP_001244970.1. NM_001258041.2. [P12081-4 ]
    NP_001244971.1. NM_001258042.2. [P12081-3 ]
    NP_002100.2. NM_002109.5. [P12081-1 ]
    UniGenei Hs.528050.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1X59 NMR - A 1-60 [» ]
    2LW7 NMR - A 2-509 [» ]
    4G84 X-ray 2.40 A/B 54-506 [» ]
    4G85 X-ray 3.11 A/B 1-506 [» ]
    ProteinModelPortali P12081.
    SMRi P12081. Positions 1-508.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109285. 29 interactions.
    DIPi DIP-37596N.
    IntActi P12081. 2 interactions.
    MINTi MINT-3007818.
    STRINGi 9606.ENSP00000304668.

    Chemistry

    BindingDBi P12081.
    ChEMBLi CHEMBL4002.
    DrugBanki DB00117. L-Histidine.

    PTM databases

    PhosphoSitei P12081.

    Polymorphism databases

    DMDMi 135123.

    Proteomic databases

    MaxQBi P12081.
    PaxDbi P12081.
    PeptideAtlasi P12081.
    PRIDEi P12081.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000307633 ; ENSP00000304668 ; ENSG00000170445 . [P12081-3 ]
    ENST00000438307 ; ENSP00000411511 ; ENSG00000170445 . [P12081-2 ]
    ENST00000457527 ; ENSP00000387893 ; ENSG00000170445 . [P12081-4 ]
    ENST00000504156 ; ENSP00000425634 ; ENSG00000170445 . [P12081-1 ]
    GeneIDi 3035.
    KEGGi hsa:3035.
    UCSCi uc003lgu.3. human. [P12081-1 ]
    uc011czm.3. human.

    Organism-specific databases

    CTDi 3035.
    GeneCardsi GC05M140034.
    HGNCi HGNC:4816. HARS.
    HPAi HPA036539.
    MIMi 142810. gene.
    614504. phenotype.
    neXtProti NX_P12081.
    Orphaneti 231183. Usher syndrome type 3.
    PharmGKBi PA29191.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0124.
    HOGENOMi HOG000018075.
    HOVERGENi HBG002731.
    InParanoidi P12081.
    KOi K01892.
    OMAi IFSITKA.
    PhylomeDBi P12081.
    TreeFami TF300652.

    Enzyme and pathway databases

    BRENDAi 6.1.1.21. 2681.
    Reactomei REACT_15306. Cytosolic tRNA aminoacylation.

    Miscellaneous databases

    ChiTaRSi HARS. human.
    EvolutionaryTracei P12081.
    GeneWikii HARS.
    GenomeRNAii 3035.
    NextBioi 12014.
    PROi P12081.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P12081.
    Bgeei P12081.
    CleanExi HS_HARS.
    Genevestigatori P12081.

    Family and domain databases

    Gene3Di 1.10.287.10. 1 hit.
    3.40.50.800. 1 hit.
    HAMAPi MF_00127. His_tRNA_synth.
    InterProi IPR002314. aa-tRNA-synt_IIb_cons-dom.
    IPR006195. aa-tRNA-synth_II.
    IPR004154. Anticodon-bd.
    IPR015807. His-tRNA-ligase.
    IPR004516. HisRS/HisZ.
    IPR009068. S15_NS1_RNA-bd.
    IPR000738. WHEP-TRS.
    [Graphical view ]
    PANTHERi PTHR11476. PTHR11476. 1 hit.
    Pfami PF03129. HGTP_anticodon. 1 hit.
    PF00587. tRNA-synt_2b. 1 hit.
    PF00458. WHEP-TRS. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001549. His-tRNA_synth. 1 hit.
    SMARTi SM00991. WHEP-TRS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47060. SSF47060. 1 hit.
    SSF52954. SSF52954. 1 hit.
    TIGRFAMsi TIGR00442. hisS. 1 hit.
    PROSITEi PS50862. AA_TRNA_LIGASE_II. 1 hit.
    PS00762. WHEP_TRS_1. 1 hit.
    PS51185. WHEP_TRS_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
      Tissue: Caudate nucleus and Testis.
    4. "Homo sapiens protein coding cDNA."
      Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Brain.
    5. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Lung and Uterus.
    7. "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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
    8. "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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
    9. "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] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: POSSIBLE INVOLVEMENT IN PERIPHERAL NEUROPATHY, VARIANTS GLU-5; GLN-137; ASP-205; ALA-238; ARG-376 AND SER-505, CHARACTERIZATION OF VARIANT GLN-137.
    12. "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.
    13. Cited for: VARIANT USH3B SER-454.

    Entry informationi

    Entry nameiSYHC_HUMAN
    AccessioniPrimary (citable) accession number: P12081
    Secondary accession number(s): B4DHQ1
    , B4DY73, D6REN6, J3KNE5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: May 1, 1992
    Last modified: October 1, 2014
    This is version 158 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3