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P12081

- SYHC_HUMAN

UniProt

P12081 - SYHC_HUMAN

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Protein

Histidine--tRNA ligase, cytoplasmic

Gene
HARS, HRS
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

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
Complete GO annotation...

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

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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 (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, cytoplasmicUniRule annotationPRO_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.

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.

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.

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. VSP_045118Add
BLAST
Alternative sequencei155 – 17420Missing in isoform 3 and isoform 4. VSP_046662Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61A → P in CAA28956. 1 Publication
Sequence conflicti126 – 1261S → P in BAG58213. 1 Publication
Sequence conflicti165 – 1651R → G in CAA28956. 1 Publication
Sequence conflicti181 – 1811N → Q in CAA28956. 1 Publication
Sequence conflicti186 – 1861I → N in CAA28956. 1 Publication
Sequence conflicti191 – 1911C → S in CAA28956. 1 Publication
Sequence conflicti206 – 2061D → N in CAA28956. 1 Publication
Sequence conflicti223 – 2231I → V in CAA28956. 1 Publication
Sequence conflicti227 – 2271S → P in CAA28956. 1 Publication
Sequence conflicti284 – 2841L → V in CAA28956. 1 Publication
Sequence conflicti347 – 3471A → E in CAA28956. 1 Publication
Sequence conflicti373 – 3742KG → QR in CAA28956. 1 Publication
Sequence conflicti375 – 3751R → L in BAG58213. 1 Publication
Sequence conflicti493 – 4931D → E in CAA28956. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 157 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

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