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P26639

- SYTC_HUMAN

UniProt

P26639 - SYTC_HUMAN

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Protein

Threonine--tRNA ligase, cytoplasmic

Gene

TARS

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

Functioni

Catalytic activityi

ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr).

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein homodimerization activity Source: UniProtKB
  3. threonine-tRNA ligase activity Source: UniProtKB

GO - Biological processi

  1. gene expression Source: Reactome
  2. threonyl-tRNA aminoacylation Source: UniProtKB
  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

ReactomeiREACT_15306. Cytosolic tRNA aminoacylation.

Names & Taxonomyi

Protein namesi
Recommended name:
Threonine--tRNA ligase, cytoplasmic (EC:6.1.1.3)
Alternative name(s):
Threonyl-tRNA synthetase
Short name:
ThrRS
Gene namesi
Name:TARS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:11572. TARS.

Subcellular locationi

GO - Cellular componenti

  1. actin cytoskeleton Source: HPA
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: Reactome
  4. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36337.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 723723Threonine--tRNA ligase, cytoplasmicPRO_0000101119Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki222 – 222Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei243 – 2431N6-acetyllysine1 Publication
Modified residuei298 – 2981PhosphotyrosineBy similarity

Post-translational modificationi

ISGylated.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP26639.
PaxDbiP26639.
PeptideAtlasiP26639.
PRIDEiP26639.

PTM databases

PhosphoSiteiP26639.

Expressioni

Gene expression databases

BgeeiP26639.
CleanExiHS_TARS.
ExpressionAtlasiP26639. baseline and differential.
GenevestigatoriP26639.

Organism-specific databases

HPAiHPA037425.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi112760. 54 interactions.
IntActiP26639. 13 interactions.
MINTiMINT-3010570.
STRINGi9606.ENSP00000265112.

Structurei

Secondary structure

1
723
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi82 – 865Combined sources
Beta strandi92 – 965Combined sources
Turni97 – 993Combined sources
Helixi102 – 1087Combined sources
Turni111 – 1133Combined sources
Helixi114 – 1163Combined sources
Beta strandi120 – 1278Combined sources
Beta strandi129 – 1313Combined sources
Beta strandi135 – 1417Combined sources
Helixi323 – 3297Combined sources
Beta strandi332 – 3343Combined sources
Helixi347 – 36620Combined sources
Beta strandi376 – 3794Combined sources
Helixi380 – 3856Combined sources
Helixi388 – 3914Combined sources
Helixi393 – 3953Combined sources
Beta strandi398 – 4014Combined sources
Beta strandi404 – 4085Combined sources
Helixi413 – 4219Combined sources
Helixi427 – 4293Combined sources
Beta strandi431 – 4366Combined sources
Beta strandi439 – 4413Combined sources
Helixi446 – 4483Combined sources
Turni451 – 4533Combined sources
Beta strandi456 – 4594Combined sources
Beta strandi462 – 4676Combined sources
Helixi469 – 4713Combined sources
Helixi472 – 49019Combined sources
Beta strandi493 – 4997Combined sources
Helixi509 – 52517Combined sources
Beta strandi530 – 5334Combined sources
Beta strandi543 – 5497Combined sources
Beta strandi555 – 56511Combined sources
Helixi566 – 5705Combined sources
Beta strandi587 – 5959Combined sources
Helixi597 – 60711Combined sources
Turni608 – 6103Combined sources
Helixi614 – 6163Combined sources
Beta strandi621 – 6277Combined sources
Helixi628 – 6303Combined sources
Helixi631 – 64212Combined sources
Turni643 – 6453Combined sources
Beta strandi648 – 6503Combined sources
Helixi658 – 66710Combined sources
Beta strandi671 – 6766Combined sources
Helixi678 – 6836Combined sources
Beta strandi685 – 6906Combined sources
Beta strandi695 – 7006Combined sources
Helixi701 – 71313Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WWTNMR-A79-153[»]
4HWTX-ray2.30A/B321-723[»]
ProteinModelPortaliP26639.
SMRiP26639. Positions 81-722.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26639.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0441.
GeneTreeiENSGT00390000002149.
HOGENOMiHOG000003878.
HOVERGENiHBG059513.
InParanoidiP26639.
KOiK01868.
OMAiYNSKLWQ.
OrthoDBiEOG7JDQX3.
PhylomeDBiP26639.
TreeFamiTF300858.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
3.40.50.800. 1 hit.
HAMAPiMF_00184. Thr_tRNA_synth.
InterProiIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR012675. Beta-grasp_dom.
IPR004095. TGS.
IPR012676. TGS-like.
IPR002320. Thr-tRNA-ligase_IIa.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]
PfamiPF03129. HGTP_anticodon. 1 hit.
PF02824. TGS. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSiPR01047. TRNASYNTHTHR.
SMARTiSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMiSSF52954. SSF52954. 1 hit.
SSF55186. SSF55186. 1 hit.
SSF81271. SSF81271. 1 hit.
TIGRFAMsiTIGR00418. thrS. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P26639-1) [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

        10         20         30         40         50
MFEEKASSPS GKMGGEEKPI GAGEEKQKEG GKKKNKEGSG DGGRAELNPW
60 70 80 90 100
PEYIYTRLEM YNILKAEHDS ILAEKAEKDS KPIKVTLPDG KQVDAESWKT
110 120 130 140 150
TPYQIACGIS QGLADNTVIA KVNNVVWDLD RPLEEDCTLE LLKFEDEEAQ
160 170 180 190 200
AVYWHSSAHI MGEAMERVYG GCLCYGPPIE NGFYYDMYLE EGGVSSNDFS
210 220 230 240 250
SLEALCKKII KEKQAFERLE VKKETLLAMF KYNKFKCRIL NEKVNTPTTT
260 270 280 290 300
VYRCGPLIDL CRGPHVRHTG KIKALKIHKN SSTYWEGKAD METLQRIYGI
310 320 330 340 350
SFPDPKMLKE WEKFQEEAKN RDHRKIGRDQ ELYFFHELSP GSCFFLPKGA
360 370 380 390 400
YIYNALIEFI RSEYRKRGFQ EVVTPNIFNS RLWMTSGHWQ HYSENMFSFE
410 420 430 440 450
VEKELFALKP MNCPGHCLMF DHRPRSWREL PLRLADFGVL HRNELSGALT
460 470 480 490 500
GLTRVRRFQQ DDAHIFCAME QIEDEIKGCL DFLRTVYSVF GFSFKLNLST
510 520 530 540 550
RPEKFLGDIE VWDQAEKQLE NSLNEFGEKW ELNSGDGAFY GPKIDIQIKD
560 570 580 590 600
AIGRYHQCAT IQLDFQLPIR FNLTYVSHDG DDKKRPVIVH RAILGSVERM
610 620 630 640 650
IAILTENYGG KWPFWLSPRQ VMVVPVGPTC DEYAQKVRQQ FHDAKFMADI
660 670 680 690 700
DLDPGCTLNK KIRNAQLAQY NFILVVGEKE KISGTVNIRT RDNKVHGERT
710 720
ISETIERLQQ LKEFRSKQAE EEF
Length:723
Mass (Da):83,435
Last modified:February 15, 2005 - v3
Checksum:i885745118972C5A9
GO
Isoform 2 (identifier: P26639-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     110-110: S → SHTASCKNLSSLASLLASVAIPSSGMPWPPLFFL

Show »
Length:756
Mass (Da):86,861
Checksum:iE3516F3A14CBC746
GO

Sequence cautioni

The sequence AAB04939.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti164 – 1641A → G in AAB04939. (PubMed:2033077)Curated
Sequence conflicti350 – 3501A → V in AAB04939. (PubMed:2033077)Curated
Sequence conflicti417 – 4171C → S in AAB04939. (PubMed:2033077)Curated
Sequence conflicti439 – 4391V → G in AAB04939. (PubMed:2033077)Curated
Sequence conflicti453 – 4531T → I in AAH10578. (PubMed:15489334)Curated
Sequence conflicti581 – 5811D → E in AAB04939. (PubMed:2033077)Curated
Sequence conflicti612 – 6121W → LA in AAB04939. (PubMed:2033077)Curated
Sequence conflicti636 – 6361K → N in AAB04939. (PubMed:2033077)Curated
Sequence conflicti683 – 6831S → T in AAB04939. (PubMed:2033077)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti21 – 211G → D.
Corresponds to variant rs34334786 [ dbSNP | Ensembl ].
VAR_034533

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei110 – 1101S → SHTASCKNLSSLASLLASVA IPSSGMPWPPLFFL in isoform 2. 1 PublicationVSP_045114

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63180 mRNA. Translation: AAB04939.1. Different initiation.
AK292346 mRNA. Translation: BAF85035.1.
AK293620 mRNA. Translation: BAG57079.1.
AC025441 Genomic DNA. No translation available.
AC034231 Genomic DNA. No translation available.
CH471118 Genomic DNA. Translation: EAX10804.1.
BC000517 mRNA. Translation: AAH00517.2.
BC010578 mRNA. Translation: AAH10578.2.
CCDSiCCDS3899.1. [P26639-1]
CCDS58943.1. [P26639-2]
PIRiA38867. YSHUT.
RefSeqiNP_001245366.1. NM_001258437.1. [P26639-1]
NP_001245367.1. NM_001258438.1. [P26639-2]
NP_689508.3. NM_152295.4. [P26639-1]
UniGeneiHs.481860.

Genome annotation databases

EnsembliENST00000265112; ENSP00000265112; ENSG00000113407. [P26639-1]
ENST00000455217; ENSP00000387710; ENSG00000113407. [P26639-2]
ENST00000502553; ENSP00000424387; ENSG00000113407. [P26639-1]
GeneIDi6897.
KEGGihsa:6897.
UCSCiuc003jhy.4. human. [P26639-1]
uc011coc.3. human.

Polymorphism databases

DMDMi60267755.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63180 mRNA. Translation: AAB04939.1 . Different initiation.
AK292346 mRNA. Translation: BAF85035.1 .
AK293620 mRNA. Translation: BAG57079.1 .
AC025441 Genomic DNA. No translation available.
AC034231 Genomic DNA. No translation available.
CH471118 Genomic DNA. Translation: EAX10804.1 .
BC000517 mRNA. Translation: AAH00517.2 .
BC010578 mRNA. Translation: AAH10578.2 .
CCDSi CCDS3899.1. [P26639-1 ]
CCDS58943.1. [P26639-2 ]
PIRi A38867. YSHUT.
RefSeqi NP_001245366.1. NM_001258437.1. [P26639-1 ]
NP_001245367.1. NM_001258438.1. [P26639-2 ]
NP_689508.3. NM_152295.4. [P26639-1 ]
UniGenei Hs.481860.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WWT NMR - A 79-153 [» ]
4HWT X-ray 2.30 A/B 321-723 [» ]
ProteinModelPortali P26639.
SMRi P26639. Positions 81-722.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112760. 54 interactions.
IntActi P26639. 13 interactions.
MINTi MINT-3010570.
STRINGi 9606.ENSP00000265112.

Chemistry

BindingDBi P26639.
ChEMBLi CHEMBL3391.
DrugBanki DB00156. L-Threonine.

PTM databases

PhosphoSitei P26639.

Polymorphism databases

DMDMi 60267755.

Proteomic databases

MaxQBi P26639.
PaxDbi P26639.
PeptideAtlasi P26639.
PRIDEi P26639.

Protocols and materials databases

DNASUi 6897.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265112 ; ENSP00000265112 ; ENSG00000113407 . [P26639-1 ]
ENST00000455217 ; ENSP00000387710 ; ENSG00000113407 . [P26639-2 ]
ENST00000502553 ; ENSP00000424387 ; ENSG00000113407 . [P26639-1 ]
GeneIDi 6897.
KEGGi hsa:6897.
UCSCi uc003jhy.4. human. [P26639-1 ]
uc011coc.3. human.

Organism-specific databases

CTDi 6897.
GeneCardsi GC05P033440.
H-InvDB HIX0004790.
HGNCi HGNC:11572. TARS.
HPAi HPA037425.
MIMi 187790. gene.
neXtProti NX_P26639.
PharmGKBi PA36337.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0441.
GeneTreei ENSGT00390000002149.
HOGENOMi HOG000003878.
HOVERGENi HBG059513.
InParanoidi P26639.
KOi K01868.
OMAi YNSKLWQ.
OrthoDBi EOG7JDQX3.
PhylomeDBi P26639.
TreeFami TF300858.

Enzyme and pathway databases

Reactomei REACT_15306. Cytosolic tRNA aminoacylation.

Miscellaneous databases

ChiTaRSi TARS. human.
EvolutionaryTracei P26639.
GeneWikii TARS_(gene).
GenomeRNAii 6897.
NextBioi 26959.
PROi P26639.
SOURCEi Search...

Gene expression databases

Bgeei P26639.
CleanExi HS_TARS.
ExpressionAtlasi P26639. baseline and differential.
Genevestigatori P26639.

Family and domain databases

Gene3Di 3.10.20.30. 1 hit.
3.40.50.800. 1 hit.
HAMAPi MF_00184. Thr_tRNA_synth.
InterProi IPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR012675. Beta-grasp_dom.
IPR004095. TGS.
IPR012676. TGS-like.
IPR002320. Thr-tRNA-ligase_IIa.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view ]
Pfami PF03129. HGTP_anticodon. 1 hit.
PF02824. TGS. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view ]
PRINTSi PR01047. TRNASYNTHTHR.
SMARTi SM00863. tRNA_SAD. 1 hit.
[Graphical view ]
SUPFAMi SSF52954. SSF52954. 1 hit.
SSF55186. SSF55186. 1 hit.
SSF81271. SSF81271. 1 hit.
TIGRFAMsi TIGR00418. thrS. 1 hit.
PROSITEi PS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide and deduced amino acid sequence of human threonyl-tRNA synthetase reveals extensive homology to the Escherichia coli and yeast enzymes."
    Cruzen M.E., Arfin S.M.
    J. Biol. Chem. 266:9919-9923(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "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 1 AND 2).
    Tissue: Cerebellum and Testis.
  3. "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].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Cervix and Lung.
  6. Cited for: ISGYLATION.
  7. "The proteomic reactor facilitates the analysis of affinity-purified proteins by mass spectrometry: application for identifying ubiquitinated proteins in human cells."
    Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M., Haines D.S., Figeys D.
    J. Proteome Res. 6:298-305(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-222.
    Tissue: Lung adenocarcinoma.
  8. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-243, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Solution structure of the TGS domain from human threonyl-tRNA synthetase."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUL-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 79-153.

Entry informationi

Entry nameiSYTC_HUMAN
AccessioniPrimary (citable) accession number: P26639
Secondary accession number(s): A8K8I1
, B4DEG8, Q96FP5, Q9BWA6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: February 15, 2005
Last modified: November 26, 2014
This is version 162 of the entry and version 3 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

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