TYS1/YGR185C Protein Information

Standard Name	Tys1p 1
Systematic Name	Ygr185cp
Alias	Tts1p 2
ORF Classification	Verified
Description	Cytoplasmic tyrosyl-tRNA synthetase; required for cytoplasmic protein synthesis; interacts with positions 34 and 35 of the tRNATyr anticodon; mutations in human ortholog YARS are associated with Charcot-Marie-Tooth (CMT) neuropathies; protein abundance increases in response to DNA replication stress (2, 3, 4, 5, 6, 7) Also known as: TyrRS 8
Name Description	TYrosyl-tRNA Synthetase 1

Experimental Data
Molecules/cell	2710 9

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	394
Molecular Weight (Da)	44,020
Isoelectric Point (pI)	8.75

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Tys1p (InterPro)
Physical Interactions	There are 30 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI0000136756 \| P36421 MIPS: YGR185C NCBI: 1323328 \| 1430951 \| 149241068 \| 173120 \| 398366063 \| 549037 \| 639701 \| NP_011701.3 GenBank/EMBL/DDBJ: DAA08279.1 \| L12221 \| U13015 \| X71998 \| X99074 \| Z72970
External Classifications	EC: 6.1.1.1 [Tyrosine--tRNA ligase]

Amino Acid Sequence (or in FASTA format)
1 MSSAATVDPN EAFGLITKNL QEVLNPQIIK DVLEVQKRHL KLYWGTAPTG 51 RPHCGYFVPM TKLADFLKAG CEVTVLLADL HAFLDNMKAP LEVVNYRAKY 101 YELTIKAILR SINVPIEKLK FVVGSSYQLT PDYTMDIFRL SNIVSQNDAK 151 RAGADVVKQV ANPLLSGLIY PLMQALDEQF LDVDCQFGGV DQRKIFVLAE 201 ENLPSLGYKK RAHLMNPMVP GLAQGGKMSA SDPNSKIDLL EEPKQVKKKI 251 NSAFCSPGNV EENGLLSFVQ YVIAPIQELK FGTNHFEFFI DRPEKFGGPI 301 TYKSFEEMKL AFKEEKLSPP DLKIGVADAI NELLEPIRQE FANNKEFQEA 351 SEKGYPVATP QKSKKAKKPK NKGTKYPGAT KTNEIATKLE ETKL*

Amino Acid Sequence (or in FASTA format)

       1  MSSAATVDPN EAFGLITKNL QEVLNPQIIK DVLEVQKRHL KLYWGTAPTG
      51  RPHCGYFVPM TKLADFLKAG CEVTVLLADL HAFLDNMKAP LEVVNYRAKY
     101  YELTIKAILR SINVPIEKLK FVVGSSYQLT PDYTMDIFRL SNIVSQNDAK
     151  RAGADVVKQV ANPLLSGLIY PLMQALDEQF LDVDCQFGGV DQRKIFVLAE
     201  ENLPSLGYKK RAHLMNPMVP GLAQGGKMSA SDPNSKIDLL EEPKQVKKKI
     251  NSAFCSPGNV EENGLLSFVQ YVIAPIQELK FGTNHFEFFI DRPEKFGGPI
     301  TYKSFEEMKL AFKEEKLSPP DLKIGVADAI NELLEPIRQE FANNKEFQEA
     351  SEKGYPVATP QKSKKAKKPK NKGTKYPGAT KTNEIATKLE ETKL*

external links for Tys1p

Homologs	Interaction Resources	Protein databases/Other	Localization Resources
BLASTP (NCBI)	BioGRID	SCOP Superfamily	Organelle DB
Ashbya (AGD)	BOND	GPMdb (Mass Spec.)	YPL+
Candida (CGD)	BioPIXIE	MIPS	YeastGFP
Candida (CandidaDB)	CYC2008 (complexes)	Pfam domains	YeastRC Public Image Repository
YGOB	Complexome	YeastRC Structure Prediction (Seattle)
YOGY	DIP
	GeneMANIA

References cited on this page View Complete Literature Guide for Tys1p

1)	Dagkessamanskaia A, et al. (2001) Interaction of Knr4 protein, a protein involved in cell wall synthesis, with tyrosine tRNA synthetase encoded by TYS1 in Saccharomyces cerevisiae. FEMS Microbiol Lett 200(1):53-8
2)	Guan MX (1997) Cytoplasmic tyrosyl-tRNA synthetase rescues the defect in mitochondrial genome maintenance caused by the nuclear mutation mgm104-1 in the yeast Saccharomyces cerevisiae. Mol Gen Genet 255(5):525-32
3)	Cavarelli J, et al. (1993) Yeast tRNA(Asp) recognition by its cognate class II aminoacyl-tRNA synthetase. Nature 362(6416):181-4
4)	Chow CM and RajBhandary UL (1993) Saccharomyces cerevisiae cytoplasmic tyrosyl-tRNA synthetase gene. Isolation by complementation of a mutant Escherichia coli suppressor tRNA defective in aminoacylation and sequence analysis. J Biol Chem 268(17):12855-63
5)	Bare LA and Uhlenbeck OC (1986) Specific substitution into the anticodon loop of yeast tyrosine transfer RNA. Biochemistry 25(19):5825-30
6)	Jordanova A, et al. (2006) Disrupted function and axonal distribution of mutant tyrosyl-tRNA synthetase in dominant intermediate Charcot-Marie-Tooth neuropathy. Nat Genet 38(2):197-202
7)	Tkach JM, et al. (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
8)	Smagowicz W, et al. (1983) Stimulation of transcription of the yeast tRNATyr gene in cell-free extracts by tyrosyl-tRNA synthetase. Nature 304(5928):747-9
9)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41