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P54577

- SYYC_HUMAN

UniProt

P54577 - SYYC_HUMAN

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Protein

Tyrosine--tRNA ligase, cytoplasmic

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

Functioni

Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr) By similarity.

Catalytic activityi

ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei39 – 391Tyrosine
Binding sitei166 – 1661Tyrosine
Binding sitei170 – 1701Tyrosine
Binding sitei173 – 1731Tyrosine
Binding sitei188 – 1881Tyrosine

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. interleukin-8 receptor binding Source: ProtInc
  3. poly(A) RNA binding Source: UniProtKB
  4. signal transducer activity Source: ProtInc
  5. tRNA binding Source: UniProtKB-KW
  6. tyrosine-tRNA ligase activity Source: Reactome

GO - Biological processi

  1. apoptotic process Source: ProtInc
  2. gene expression Source: Reactome
  3. signal transduction Source: GOC
  4. tRNA aminoacylation for protein translation Source: Reactome
  5. tyrosyl-tRNA aminoacylation Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding, tRNA-binding

Enzyme and pathway databases

ReactomeiREACT_15306. Cytosolic tRNA aminoacylation.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine--tRNA ligase, cytoplasmic (EC:6.1.1.1)
Alternative name(s):
Tyrosyl-tRNA synthetase
Short name:
TyrRS
Cleaved into the following chain:
Gene namesi
Name:YARS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:12840. YARS.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. extracellular space Source: ProtInc
  4. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Charcot-Marie-Tooth disease, dominant, intermediate type, C (CMTDIC) [MIM:608323]: A form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. The dominant intermediate type C is characterized by clinical and pathologic features intermediate between demyelinating and axonal peripheral neuropathies, and motor median nerve conduction velocities ranging from 25 to 45 m/sec.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti41 – 411G → R in CMTDIC; partial loss of activity. 1 Publication
VAR_026681
Natural varianti153 – 1564Missing in CMTDIC.
VAR_026682
Natural varianti196 – 1961E → K in CMTDIC; partial loss of activity. 1 Publication
VAR_026684

Keywords - Diseasei

Charcot-Marie-Tooth disease, Disease mutation, Neurodegeneration, Neuropathy

Organism-specific databases

MIMi608323. phenotype.
Orphaneti100045. Autosomal dominant intermediate Charcot-Marie-Tooth disease type C.
PharmGKBiPA37431.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 528528Tyrosine--tRNA ligase, cytoplasmicPRO_0000423285Add
BLAST
Initiator methioninei1 – 11Removed; alternate2 Publications
Chaini2 – 528527Tyrosine--tRNA ligase, cytoplasmic, N-terminally processedPRO_0000055673Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei2 – 21N-acetylglycine; in Tyrosine--tRNA ligase, cytoplasmic, N-terminally processed2 Publications
Modified residuei197 – 1971N6-acetyllysine1 Publication
Modified residuei206 – 2061N6-acetyllysine1 Publication
Modified residuei474 – 4741N6-acetyllysine1 Publication
Modified residuei482 – 4821N6-acetyllysine1 Publication
Modified residuei490 – 4901N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP54577.
PaxDbiP54577.
PeptideAtlasiP54577.
PRIDEiP54577.

2D gel databases

REPRODUCTION-2DPAGEIPI00007074.

PTM databases

PhosphoSiteiP54577.

Miscellaneous databases

PMAP-CutDBP54577.

Expressioni

Gene expression databases

BgeeiP54577.
CleanExiHS_YARS.
GenevestigatoriP54577.

Organism-specific databases

HPAiHPA017936.
HPA018950.
HPA018954.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi114134. 15 interactions.
IntActiP54577. 1 interaction.
STRINGi9606.ENSP00000362576.

Structurei

Secondary structure

1
528
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 159
Beta strandi19 – 224
Helixi24 – 318
Beta strandi37 – 426
Helixi50 – 523
Helixi53 – 6412
Beta strandi68 – 736
Helixi75 – 806
Turni81 – 844
Helixi87 – 10822
Beta strandi115 – 1195
Helixi120 – 1223
Turni123 – 1253
Helixi127 – 13711
Helixi142 – 1487
Turni149 – 1524
Helixi161 – 17616
Beta strandi180 – 1856
Helixi186 – 1883
Helixi189 – 19810
Helixi199 – 2024
Beta strandi208 – 2125
Helixi238 – 2469
Beta strandi247 – 2493
Helixi259 – 2668
Turni267 – 2737
Beta strandi275 – 2773
Helixi281 – 2833
Beta strandi287 – 2915
Helixi292 – 3009
Helixi306 – 32722
Helixi331 – 34010
Helixi365 – 3673
Beta strandi370 – 38011
Beta strandi388 – 3936
Beta strandi395 – 3984
Beta strandi400 – 4056
Turni407 – 4093
Helixi412 – 4143
Turni415 – 4173
Beta strandi419 – 4235
Beta strandi429 – 4313
Beta strandi434 – 4363
Beta strandi442 – 45413
Beta strandi466 – 4694
Beta strandi479 – 4813
Helixi483 – 4853
Helixi487 – 4926
Beta strandi495 – 4973
Beta strandi501 – 5055
Beta strandi508 – 5125
Beta strandi526 – 5283

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N3LX-ray1.18A1-364[»]
1NTGX-ray2.21A/B/C/D359-528[»]
1Q11X-ray1.60A1-364[»]
ProteinModelPortaliP54577.
SMRiP54577. Positions 4-342, 360-528.

Miscellaneous databases

EvolutionaryTraceiP54577.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini364 – 468105tRNA-bindingAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi44 – 529"HIGH" region
Motifi222 – 2265"KMSKS" region

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0162.
HOGENOMiHOG000228237.
HOVERGENiHBG080113.
InParanoidiP54577.
KOiK01866.
OMAiNRQVEPL.
OrthoDBiEOG79CXZ2.
PhylomeDBiP54577.
TreeFamiTF300898.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
3.40.50.620. 1 hit.
InterProiIPR002305. aa-tRNA-synth_Ic.
IPR012340. NA-bd_OB-fold.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002547. tRNA-bd_dom.
IPR002307. Tyr-tRNA-ligase.
[Graphical view]
PfamiPF00579. tRNA-synt_1b. 1 hit.
PF01588. tRNA_bind. 1 hit.
[Graphical view]
PRINTSiPR01040. TRNASYNTHTYR.
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00234. tyrS. 1 hit.
PROSITEiPS50886. TRBD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P54577-1 [UniParc]FASTAAdd to Basket

« Hide

MGDAPSPEEK LHLITRNLQE VLGEEKLKEI LKERELKIYW GTATTGKPHV    50
AYFVPMSKIA DFLKAGCEVT ILFADLHAYL DNMKAPWELL ELRVSYYENV 100
IKAMLESIGV PLEKLKFIKG TDYQLSKEYT LDVYRLSSVV TQHDSKKAGA 150
EVVKQVEHPL LSGLLYPGLQ ALDEEYLKVD AQFGGIDQRK IFTFAEKYLP 200
ALGYSKRVHL MNPMVPGLTG SKMSSSEEES KIDLLDRKED VKKKLKKAFC 250
EPGNVENNGV LSFIKHVLFP LKSEFVILRD EKWGGNKTYT AYVDLEKDFA 300
AEVVHPGDLK NSVEVALNKL LDPIREKFNT PALKKLASAA YPDPSKQKPM 350
AKGPAKNSEP EEVIPSRLDI RVGKIITVEK HPDADSLYVE KIDVGEAEPR 400
TVVSGLVQFV PKEELQDRLV VVLCNLKPQK MRGVESQGML LCASIEGINR 450
QVEPLDPPAG SAPGEHVFVK GYEKGQPDEE LKPKKKVFEK LQADFKISEE 500
CIAQWKQTNF MTKLGSISCK SLKGGNIS 528
Length:528
Mass (Da):59,143
Last modified:January 23, 2007 - v4
Checksum:i00C7E88843905780
GO

Sequence cautioni

The sequence AAB39406.1 differs from that shown. Reason: Frameshift at position 354.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti41 – 411G → R in CMTDIC; partial loss of activity. 1 Publication
VAR_026681
Natural varianti153 – 1564Missing in CMTDIC.
VAR_026682
Natural varianti170 – 1701Q → H.
Corresponds to variant rs2128600 [ dbSNP | Ensembl ].
VAR_026683
Natural varianti196 – 1961E → K in CMTDIC; partial loss of activity. 1 Publication
VAR_026684

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti143 – 1431H → R in BAD97328. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U40714 mRNA. Translation: AAB39406.1. Frameshift.
U89436 mRNA. Translation: AAB88409.1.
AK125213 mRNA. Translation: BAG54166.1.
AK223608 mRNA. Translation: BAD97328.1.
CH471059 Genomic DNA. Translation: EAX07506.1.
CH471059 Genomic DNA. Translation: EAX07507.1.
BC001933 mRNA. Translation: AAH01933.1.
BC004151 mRNA. Translation: AAH04151.1.
BC016689 mRNA. Translation: AAH16689.1.
CCDSiCCDS368.1.
RefSeqiNP_003671.1. NM_003680.3.
UniGeneiHs.213264.

Genome annotation databases

EnsembliENST00000373477; ENSP00000362576; ENSG00000134684.
GeneIDi8565.
KEGGihsa:8565.
UCSCiuc001bvy.1. human.

Polymorphism databases

DMDMi13638438.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U40714 mRNA. Translation: AAB39406.1 . Frameshift.
U89436 mRNA. Translation: AAB88409.1 .
AK125213 mRNA. Translation: BAG54166.1 .
AK223608 mRNA. Translation: BAD97328.1 .
CH471059 Genomic DNA. Translation: EAX07506.1 .
CH471059 Genomic DNA. Translation: EAX07507.1 .
BC001933 mRNA. Translation: AAH01933.1 .
BC004151 mRNA. Translation: AAH04151.1 .
BC016689 mRNA. Translation: AAH16689.1 .
CCDSi CCDS368.1.
RefSeqi NP_003671.1. NM_003680.3.
UniGenei Hs.213264.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1N3L X-ray 1.18 A 1-364 [» ]
1NTG X-ray 2.21 A/B/C/D 359-528 [» ]
1Q11 X-ray 1.60 A 1-364 [» ]
ProteinModelPortali P54577.
SMRi P54577. Positions 4-342, 360-528.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114134. 15 interactions.
IntActi P54577. 1 interaction.
STRINGi 9606.ENSP00000362576.

Chemistry

BindingDBi P54577.
ChEMBLi CHEMBL3179.
DrugBanki DB00135. L-Tyrosine.

PTM databases

PhosphoSitei P54577.

Polymorphism databases

DMDMi 13638438.

2D gel databases

REPRODUCTION-2DPAGE IPI00007074.

Proteomic databases

MaxQBi P54577.
PaxDbi P54577.
PeptideAtlasi P54577.
PRIDEi P54577.

Protocols and materials databases

DNASUi 8565.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000373477 ; ENSP00000362576 ; ENSG00000134684 .
GeneIDi 8565.
KEGGi hsa:8565.
UCSCi uc001bvy.1. human.

Organism-specific databases

CTDi 8565.
GeneCardsi GC01M033240.
HGNCi HGNC:12840. YARS.
HPAi HPA017936.
HPA018950.
HPA018954.
MIMi 603623. gene.
608323. phenotype.
neXtProti NX_P54577.
Orphaneti 100045. Autosomal dominant intermediate Charcot-Marie-Tooth disease type C.
PharmGKBi PA37431.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0162.
HOGENOMi HOG000228237.
HOVERGENi HBG080113.
InParanoidi P54577.
KOi K01866.
OMAi NRQVEPL.
OrthoDBi EOG79CXZ2.
PhylomeDBi P54577.
TreeFami TF300898.

Enzyme and pathway databases

Reactomei REACT_15306. Cytosolic tRNA aminoacylation.

Miscellaneous databases

ChiTaRSi YARS. human.
EvolutionaryTracei P54577.
GeneWikii YARS.
GenomeRNAii 8565.
NextBioi 32113.
PMAP-CutDB P54577.
PROi P54577.
SOURCEi Search...

Gene expression databases

Bgeei P54577.
CleanExi HS_YARS.
Genevestigatori P54577.

Family and domain databases

Gene3Di 2.40.50.140. 1 hit.
3.40.50.620. 1 hit.
InterProi IPR002305. aa-tRNA-synth_Ic.
IPR012340. NA-bd_OB-fold.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002547. tRNA-bd_dom.
IPR002307. Tyr-tRNA-ligase.
[Graphical view ]
Pfami PF00579. tRNA-synt_1b. 1 hit.
PF01588. tRNA_bind. 1 hit.
[Graphical view ]
PRINTSi PR01040. TRNASYNTHTYR.
SUPFAMi SSF50249. SSF50249. 1 hit.
TIGRFAMsi TIGR00234. tyrS. 1 hit.
PROSITEi PS50886. TRBD. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Evidence that two present-day components needed for the genetic code appeared after nucleated cells separated from eubacteria."
    Ribas de Pouplana L., Frugier M., Quinn C.L., Schimmel P.
    Proc. Natl. Acad. Sci. U.S.A. 93:166-170(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Human tyrosyl-tRNA synthetase shares amino acid sequence homology with a putative cytokine."
    Kleeman T.A., Wei D., Simpson K.L., First E.A.
    J. Biol. Chem. 272:14420-14425(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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].
    Tissue: Brain.
  4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. 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].
    Tissue: Bone and Lung.
  7. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-16.
    Tissue: Platelet.
  8. Bienvenut W.V.
    Submitted (OCT-2004) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-16, ACETYLATION AT GLY-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  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 MET-1 AND GLY-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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-197; LYS-206; LYS-474; LYS-482 AND LYS-490, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Crystal structure of a human aminoacyl-tRNA synthetase cytokine."
    Yang X.-L., Skene R.J., McRee D.E., Schimmel P.
    Proc. Natl. Acad. Sci. U.S.A. 99:15369-15374(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.18 ANGSTROMS) OF 1-342, SUBUNIT.
  13. "Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains."
    Yang X.-L., Otero F.J., Skene R.J., McRee D.E., Schimmel P., Ribas de Pouplana L.
    Proc. Natl. Acad. Sci. U.S.A. 100:15376-15380(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1-364 IN COMPLEX WITH TYROSINE.
  14. Cited for: SUBCELLULAR LOCATION, VARIANTS CMTDIC 153-VAL--VAL-156 DEL; ARG-41 AND LYS-196, CHARACTERIZATION OF VARIANTS CMTDIC ARG-41 AND LYS-196.

Entry informationi

Entry nameiSYYC_HUMAN
AccessioniPrimary (citable) accession number: P54577
Secondary accession number(s): B3KWK4
, D3DPQ4, O43276, Q53EN1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 156 of the entry and version 4 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, Direct protein sequencing, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Human chromosome 1
    Human chromosome 1: 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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