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Protein

Cytoplasmic tRNA 2-thiolation protein 2

Gene

NCS2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a central role in 2-thiolation of mcm5S2U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with NCS6 that ligates sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position. Prior mcm5 tRNA modification by the elongator complex is required for 2-thiolation. May also be involved in protein urmylation and in invasive and pseudohyphal growth. Inhibits replication of Brome mosaic virus.UniRule annotation6 Publications

Pathwayi: 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis

This protein is involved in the pathway 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis, which is part of tRNA modification.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis and in tRNA modification.

GO - Molecular functioni

GO - Biological processi

  • invasive growth in response to glucose limitation Source: SGD
  • protein urmylation Source: SGD
  • pseudohyphal growth Source: SGD
  • tRNA thio-modification Source: UniProtKB
  • tRNA wobble position uridine thiolation Source: SGD
  • tRNA wobble uridine modification Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

tRNA processing

Enzyme and pathway databases

BioCyciYEAST:G3O-33141-MONOMER.
UniPathwayiUPA00988.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytoplasmic tRNA 2-thiolation protein 2UniRule annotation
Alternative name(s):
Needs CLA4 to survive protein 2UniRule annotation
Thiolation of uridine in cytoplasmic tRNA protein 2UniRule annotation
Gene namesi
Name:NCS2UniRule annotation
Synonyms:CTU2UniRule annotation, TUC2UniRule annotation
Ordered Locus Names:YNL119W
ORF Names:N1913
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL119W.
SGDiS000005063. NCS2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 493493Cytoplasmic tRNA 2-thiolation protein 2PRO_0000203432Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei489 – 4891PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP53923.

PTM databases

iPTMnetiP53923.

Interactioni

Subunit structurei

Interacts with NCS6 and URM1. May act by forming a heterodimer with NCS6.UniRule annotation1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ARC1P466722EBI-28871,EBI-7224
MAGEA12P433653EBI-28871,EBI-749530From a different organism.

Protein-protein interaction databases

BioGridi35707. 88 interactions.
DIPiDIP-6649N.
IntActiP53923. 2 interactions.
MINTiMINT-635230.

Structurei

3D structure databases

ProteinModelPortaliP53923.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the CTU2/NCS2 family.UniRule annotation

Phylogenomic databases

InParanoidiP53923.
KOiK14169.
OMAiKQRKQMM.
OrthoDBiEOG7VB2RN.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
HAMAPiMF_03054. CTU2.
InterProiIPR019407. CTU2.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF10288. CTU2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53923-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MECQRCPASA RNPATVESRK EKFCDECFIK FVSTKQRKQM MKDEYFRNLF
60 70 80 90 100
KVIYPFEKEG SVSKILLPLS HSDSGSLVML DIVHDLLLEQ TKQHNNRTGF
110 120 130 140 150
TVDVLTVFTE ENVSVIKERM ESLINEKMSQ LNKISNIFNV HFIDVNEFFN
160 170 180 190 200
NASEVSTFII DNENFEIFSK SKSVDDSNIL TLKEILGKYC LNNSSRSDLI
210 220 230 240 250
SIIKTQLIKH FAYENGYNAI MWGHSMTKLS EVIISLVVKG KGSQIATFLD
260 270 280 290 300
SESFDTLNNK PCKYKNLYPM KDLLSVEIES FLQIRNLAQF LINVEETNVK
310 320 330 340 350
PNCLIARKSL PSLGQQKLVK NMTINEITNK YFQDIQNDYS NIISTVLRTA
360 370 380 390 400
DKLTQPKSSM AKPSQCQICQ SKIYTNPSNW LNRITVTSPY PVETTEEKYL
410 420 430 440 450
FKQWQDSKLG QSHTHYVELL NEIKQGASNS LDVEDGDVKL CYGCLILLNT
460 470 480 490
SIKDKNLVWP KVDTMDITAN ATNKNKELSQ ILDQFEINSD GEE
Length:493
Mass (Da):56,473
Last modified:October 1, 1996 - v1
Checksum:i420FE465B982C43E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti36 – 361Q → R in AAU09777 (PubMed:17322287).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti7 – 71P → S in strain: YJM230 and YJM320. 1 Publication
Natural varianti71 – 711H → L in strain: SK1, V1-09, YJM1129, YJM269, YJM270, YJM320, YJM326, YJM230, YJM339 and YJM627. 1 Publication
Natural varianti193 – 1931N → S in strain: SK1, V1-09, YJM230, YJM320 and YJM339. 1 Publication
Natural varianti409 – 4091L → S in strain: YJM627. 1 Publication
Natural varianti428 – 4281S → G in strain: YJM627. 1 Publication
Natural varianti436 – 4361G → S in strain: YJM230 and YJM320. 1 Publication
Natural varianti474 – 4741K → N in strain: YJM1129, YJM269, YJM270, YJM326 and YJM627. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF125216 Genomic DNA. Translation: ABN58538.1.
EF125217 Genomic DNA. Translation: ABN58547.1.
EF125218 Genomic DNA. Translation: ABN58556.1.
EF125219 Genomic DNA. Translation: ABN58565.1.
EF125220 Genomic DNA. Translation: ABN58574.1.
EF125221 Genomic DNA. Translation: ABN58583.1.
EF125222 Genomic DNA. Translation: ABN58592.1.
EF125223 Genomic DNA. Translation: ABN58601.1.
EF125224 Genomic DNA. Translation: ABN58610.1.
EF125225 Genomic DNA. Translation: ABN58619.1.
EF125226 Genomic DNA. Translation: ABN58628.1.
EF125228 Genomic DNA. Translation: ABN58646.1.
Z69382 Genomic DNA. Translation: CAA93388.1.
Z71396 Genomic DNA. Translation: CAA96001.1.
AY723860 Genomic DNA. Translation: AAU09777.1.
BK006947 Genomic DNA. Translation: DAA10429.1.
PIRiS63060.
RefSeqiNP_014280.3. NM_001182957.3.

Genome annotation databases

EnsemblFungiiYNL119W; YNL119W; YNL119W.
GeneIDi855603.
KEGGisce:YNL119W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF125216 Genomic DNA. Translation: ABN58538.1.
EF125217 Genomic DNA. Translation: ABN58547.1.
EF125218 Genomic DNA. Translation: ABN58556.1.
EF125219 Genomic DNA. Translation: ABN58565.1.
EF125220 Genomic DNA. Translation: ABN58574.1.
EF125221 Genomic DNA. Translation: ABN58583.1.
EF125222 Genomic DNA. Translation: ABN58592.1.
EF125223 Genomic DNA. Translation: ABN58601.1.
EF125224 Genomic DNA. Translation: ABN58610.1.
EF125225 Genomic DNA. Translation: ABN58619.1.
EF125226 Genomic DNA. Translation: ABN58628.1.
EF125228 Genomic DNA. Translation: ABN58646.1.
Z69382 Genomic DNA. Translation: CAA93388.1.
Z71396 Genomic DNA. Translation: CAA96001.1.
AY723860 Genomic DNA. Translation: AAU09777.1.
BK006947 Genomic DNA. Translation: DAA10429.1.
PIRiS63060.
RefSeqiNP_014280.3. NM_001182957.3.

3D structure databases

ProteinModelPortaliP53923.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35707. 88 interactions.
DIPiDIP-6649N.
IntActiP53923. 2 interactions.
MINTiMINT-635230.

PTM databases

iPTMnetiP53923.

Proteomic databases

MaxQBiP53923.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL119W; YNL119W; YNL119W.
GeneIDi855603.
KEGGisce:YNL119W.

Organism-specific databases

EuPathDBiFungiDB:YNL119W.
SGDiS000005063. NCS2.

Phylogenomic databases

InParanoidiP53923.
KOiK14169.
OMAiKQRKQMM.
OrthoDBiEOG7VB2RN.

Enzyme and pathway databases

UniPathwayiUPA00988.
BioCyciYEAST:G3O-33141-MONOMER.

Miscellaneous databases

PROiP53923.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
HAMAPiMF_03054. CTU2.
InterProiIPR019407. CTU2.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF10288. CTU2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequential elimination of major-effect contributors identifies additional quantitative trait loci conditioning high-temperature growth in yeast."
    Sinha H., David L., Pascon R.C., Clauder-Muenster S., Krishnakumar S., Nguyen M., Shi G., Dean J., Davis R.W., Oefner P.J., McCusker J.H., Steinmetz L.M.
    Genetics 180:1661-1670(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-7; LEU-71; SER-193; SER-409; GLY-428; SER-436 AND ASN-474.
    Strain: ATCC 200060 / W303, S103, SK1, V1-09, YJM 1129, YJM 269, YJM 270, YJM 320, YJM 326, YJM 339, YJM 627 and YJM230.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Urmylation: a ubiquitin-like pathway that functions during invasive growth and budding in yeast."
    Goehring A.S., Rivers D.M., Sprague G.F. Jr.
    Mol. Biol. Cell 14:4329-4341(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Systematic, genome-wide identification of host genes affecting replication of a positive-strand RNA virus."
    Kushner D.B., Lindenbach B.D., Grdzelishvili V.Z., Noueiry A.O., Paul S.M., Ahlquist P.
    Proc. Natl. Acad. Sci. U.S.A. 100:15764-15769(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-489, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  10. "Thio-modification of yeast cytosolic tRNA requires a ubiquitin-related system that resembles bacterial sulfur transfer systems."
    Nakai Y., Nakai M., Hayashi H.
    J. Biol. Chem. 283:27469-27476(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  11. "A genome-wide screen identifies genes required for formation of the wobble nucleoside 5-methoxycarbonylmethyl-2-thiouridine in Saccharomyces cerevisiae."
    Huang B., Lu J., Bystroem A.S.
    RNA 14:2183-2194(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Ubiquitin-related modifier Urm1 acts as a sulphur carrier in thiolation of eukaryotic transfer RNA."
    Leidel S., Pedrioli P.G.A., Bucher T., Brost R., Costanzo M., Schmidt A., Aebersold R., Boone C., Hofmann K., Peter M.
    Nature 458:228-233(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN 2-THIOLATION OF TRNA, INTERACTION WITH NCS6 AND URM1.
  13. "Mechanistic characterization of the sulfur-relay system for eukaryotic 2-thiouridine biogenesis at tRNA wobble positions."
    Noma A., Sakaguchi Y., Suzuki T.
    Nucleic Acids Res. 37:1335-1352(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN 2-THIOLATION OF TRNA.

Entry informationi

Entry nameiCTU2_YEAST
AccessioniPrimary (citable) accession number: P53923
Secondary accession number(s): B0KZR6
, B0KZS5, B0KZU3, B0KZW1, B0L006, D6W163, Q66R25
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2860 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.