CTU2_YEAST - dbPTM
CTU2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CTU2_YEAST
UniProt AC P53923
Protein Name Cytoplasmic tRNA 2-thiolation protein 2 {ECO:0000255|HAMAP-Rule:MF_03054}
Gene Name NCS2 {ECO:0000255|HAMAP-Rule:MF_03054}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 493
Subcellular Localization Cytoplasm .
Protein Description Plays a central role in 2-thiolation of mcm(5)S(2)U 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 mcm(5) 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..
Protein Sequence MECQRCPASARNPATVESRKEKFCDECFIKFVSTKQRKQMMKDEYFRNLFKVIYPFEKEGSVSKILLPLSHSDSGSLVMLDIVHDLLLEQTKQHNNRTGFTVDVLTVFTEENVSVIKERMESLINEKMSQLNKISNIFNVHFIDVNEFFNNASEVSTFIIDNENFEIFSKSKSVDDSNILTLKEILGKYCLNNSSRSDLISIIKTQLIKHFAYENGYNAIMWGHSMTKLSEVIISLVVKGKGSQIATFLDSESFDTLNNKPCKYKNLYPMKDLLSVEIESFLQIRNLAQFLINVEETNVKPNCLIARKSLPSLGQQKLVKNMTINEITNKYFQDIQNDYSNIISTVLRTADKLTQPKSSMAKPSQCQICQSKIYTNPSNWLNRITVTSPYPVETTEEKYLFKQWQDSKLGQSHTHYVELLNEIKQGASNSLDVEDGDVKLCYGCLILLNTSIKDKNLVWPKVDTMDITANATNKNKELSQILDQFEINSDGEE
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
177PhosphorylationKSKSVDDSNILTLKE
CCCCCCCCCCEEHHH		22.7028889911
181PhosphorylationVDDSNILTLKEILGK
CCCCCCEEHHHHHHH		31.8027017623
275PhosphorylationYPMKDLLSVEIESFL
CCHHHHHHCCHHHHH		25.6330377154
309PhosphorylationNCLIARKSLPSLGQQ
CEEEEECCCCCCCCH		39.7025752575
312PhosphorylationIARKSLPSLGQQKLV
EEECCCCCCCCHHHH		50.8828889911
362UbiquitinationQPKSSMAKPSQCQIC
CCCCCCCCHHHCCCC		36.2423749301
388PhosphorylationLNRITVTSPYPVETT
CCCEEECCCCCCCCC		20.3527214570
394PhosphorylationTSPYPVETTEEKYLF
CCCCCCCCCCHHHHH		39.4827017623
398AcetylationPVETTEEKYLFKQWQ
CCCCCCHHHHHHHHH		40.8124489116
468PhosphorylationKVDTMDITANATNKN
CCCCEEECCCCCCCC		15.0327017623
479PhosphorylationTNKNKELSQILDQFE
CCCCHHHHHHHHHHC		19.1019823750
489PhosphorylationLDQFEINSDGEE---
HHHHCCCCCCCC---		53.2917330950
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of CTU2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CTU2_YEAST !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CTU2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
URM1_YEASTURM1physical
19145231
CTU1_YEASTNCS6physical
19145231
UBA4_YEASTUBA4physical
19145231
THTR_YEASTTUM1physical
19145231
DUG2_YEASTDUG2physical
20826334
CDC37_YEASTCDC37genetic
27708008
NIP7_YEASTNIP7genetic
27708008
DPOA2_YEASTPOL12genetic
27708008
EIF3A_YEASTRPG1genetic
27708008
DPOD_YEASTPOL3genetic
27708008
CDC53_YEASTCDC53genetic
27708008
NOP14_YEASTNOP14genetic
27708008
FAL1_YEASTFAL1genetic
27708008
DBF4_YEASTDBF4genetic
27708008
UBC3_YEASTCDC34genetic
27708008
RRP1_YEASTRRP1genetic
27708008
TRS23_YEASTTRS23genetic
27708008
TFB1_YEASTTFB1genetic
27708008
SMT3_YEASTSMT3genetic
27708008
TSC11_YEASTTSC11genetic
27708008
PSB3_YEASTPUP3genetic
27708008
GDI1_YEASTGDI1genetic
27708008
COG3_YEASTCOG3genetic
27708008
CDC4_YEASTCDC4genetic
27708008
ACT_YEASTACT1genetic
27708008
SAD1_YEASTSAD1genetic
27708008
PSB7_YEASTPRE4genetic
27708008
SLD3_YEASTSLD3genetic
27708008
SMD1_YEASTSMD1genetic
27708008
ESP1_YEASTESP1genetic
27708008
CP51_YEASTERG11genetic
27708008
SAM35_YEASTSAM35genetic
27708008
IPI1_YEASTIPI1genetic
27708008
SHQ1_YEASTSHQ1genetic
27708008
MOB1_YEASTMOB1genetic
27708008
MCM10_YEASTMCM10genetic
27708008
PRI1_YEASTPRI1genetic
27708008
RRN7_YEASTRRN7genetic
27708008
TIM16_YEASTPAM16genetic
27708008
CDC6_YEASTCDC6genetic
27708008
DPOD2_YEASTPOL31genetic
27708008
RFC2_YEASTRFC2genetic
27708008
YJ9I_YEASTYJR141Wgenetic
27708008
PRI2_YEASTPRI2genetic
27708008
NOC3_YEASTNOC3genetic
27708008
SSL1_YEASTSSL1genetic
27708008
SED5_YEASTSED5genetic
27708008
CDC45_YEASTCDC45genetic
27708008
CFT2_YEASTCFT2genetic
27708008
RU1C_YEASTYHC1genetic
27708008
STT4_YEASTSTT4genetic
27708008
SEN1_YEASTSEN1genetic
27708008
ORC1_YEASTORC1genetic
27708008
MCM1_YEASTMCM1genetic
27708008
MED11_YEASTMED11genetic
27708008
SPC24_YEASTSPC24genetic
27708008
CBF3B_YEASTCEP3genetic
27708008
VTI1_YEASTVTI1genetic
27708008
RFC4_YEASTRFC4genetic
27708008
PROF_YEASTPFY1genetic
27708008
DYR_YEASTDFR1genetic
27708008
MYO2_YEASTMYO2genetic
27708008
TBF1_YEASTTBF1genetic
27708008
ASA1_YEASTASA1genetic
27708008
ORC4_YEASTORC4genetic
27708008
SEC23_YEASTSEC23genetic
27708008
MAGAC_HUMANMAGEA12physical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CTU2_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-489, AND MASSSPECTROMETRY.

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