SKI2_YEAST - dbPTM
SKI2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SKI2_YEAST
UniProt AC P35207
Protein Name Antiviral helicase SKI2
Gene Name SKI2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1287
Subcellular Localization Cytoplasm .
Protein Description RNA helicase component of the SKI complex involved in 3'-mRNA degradation pathway. Represses dsRNA virus propagation by specifically blocking translation of viral mRNAs, perhaps recognizing the absence of CAP or poly(A). Essential for cell growth only in the presence of M1 replicon..
Protein Sequence MSEGFSSSSIQELYQSLKEITNNADVELFEDRITKLDFESTDEPKHANDIIKDRFLRPSNALPWSLLDMVQDVPHTSSPEDCSGKLDYKELLKVPDPINRTSYQFKRTGLEGKISGYKEEVDLKEVANANASNSLSITRSINHNQNSVRGSTAQLPFTPGGIPMKSVKTDSEQNGSSTMANATKLLHKDGQGLFDIPEGMNRGIKPMDSPAENEDQNGQFKELKQLNEIDNELDIRIEANEAKLKEEEKSAKSISEEIMEEATEETTADNADDAEIDELLPIGIDFGRTKPVSKSVPVKKEWAHVVDLNHKIENFDELIPNPARSWPFELDTFQKEAVYHLEQGDSVFVAAHTSAGKTVVAEYAIAMAHRNMTKTIYTSPIKALSNQKFRDFKETFDDVNIGLITGDVQINPDANCLIMTTEILRSMLYRGADLIRDVEFVIFDEVHYVNDQDRGVVWEEVIIMLPQHVKFILLSATVPNTYEFANWIGRTKQKNIYVISTPKRPVPLEINIWAKKELIPVINQNSEFLEANFRKHKEILNGESAKGAPSKTDNGRGGSTARGGRGGSNTRDGRGGRGNSTRGGANRGGSRGAGAIGSNKRKFFTQDGPSKKTWPEIVNYLRKRELLPMVVFVFSKKRCEEYADWLEGINFCNNKEKSQIHMFIEKSITRLKKEDRDLPQILKTRSLLERGIAVHHGGLLPIVKELIEILFSKGFIKVLFATETFAMGLNLPTRTVIFSSIRKHDGNGLRELTPGEFTQMAGRAGRRGLDSTGTVIVMAYNSPLSIATFKEVTMGVPTRLQSQFRLTYNMILNLLRIEALRVEEMIKYSFSENAKETLQPEHEKQIKVLQEELQTIEYKSCEICDNDIEKFLELMLAYKEATVNLMQEMVKSPSILHILKEGRLVAFRDPNDCLKLGFVFKVSLKDAVCVIMTFTKPYKLPNGEPNHLIYFPKADGYRRRNFPKFQKTDFYMEEVPVTAIEVITKRKFAAPLGKVIKKDVAALNEFNAETNNILDGKTLKEAINIEKQGLKIHQILLDRTNIRDEIFKLKSIKCPNLSQHIVPKFKAHVIKKKIEELYHLMSDQNLSLLPDYEKRLAVLKDTEFIDQNHNVLLKGRVACEINSGYELVLTELILDNFLGSFEPEEIVALLSVFVYEGKTREEEPPIVTPRLAKGKQRIEEIYKKMLCVFNTHQIPLTQDEAEFLDRKRFAMMNVVYEWARGLSFKEIMEMSPEAEGTVVRVITWLDEICREVKTASIIIGNSTLHMKMSRAQELIKRDIVFAASLYL
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
2Phosphorylation------MSEGFSSSS
------CCCCCCHHH		58.7030377154
8PhosphorylationMSEGFSSSSIQELYQ
CCCCCCHHHHHHHHH		30.2030377154
9PhosphorylationSEGFSSSSIQELYQS
CCCCCHHHHHHHHHH		30.1830377154
14PhosphorylationSSSIQELYQSLKEIT
HHHHHHHHHHHHHHH		8.7028132839
16PhosphorylationSIQELYQSLKEITNN
HHHHHHHHHHHHHCC		28.0530377154
93AcetylationLDYKELLKVPDPINR
CCHHHHHCCCCCCCC		65.4324489116
147PhosphorylationSINHNQNSVRGSTAQ
EEECCCCCCCCCCCC		11.9228889911
151PhosphorylationNQNSVRGSTAQLPFT
CCCCCCCCCCCCCCC		15.2527017623
166PhosphorylationPGGIPMKSVKTDSEQ
CCCCCCCCCCCCCCC		23.6929734811
168UbiquitinationGIPMKSVKTDSEQNG
CCCCCCCCCCCCCCC		54.4223749301
169PhosphorylationIPMKSVKTDSEQNGS
CCCCCCCCCCCCCCC		42.4720377248
171PhosphorylationMKSVKTDSEQNGSST
CCCCCCCCCCCCCCH		46.4420377248
176PhosphorylationTDSEQNGSSTMANAT
CCCCCCCCCHHHHHH		30.1320377248
209PhosphorylationRGIKPMDSPAENEDQ
CCCCCCCCCCCCCCC		21.5422369663
253PhosphorylationEEEKSAKSISEEIME
HHHHHHHHHHHHHHH		30.9421440633
373PhosphorylationAMAHRNMTKTIYTSP
HHHHHCCCCEEECCH		28.6928889911
375PhosphorylationAHRNMTKTIYTSPIK
HHHCCCCEEECCHHH		15.2830377154
377PhosphorylationRNMTKTIYTSPIKAL
HCCCCEEECCHHHHH		13.3428889911
378PhosphorylationNMTKTIYTSPIKALS
CCCCEEECCHHHHHC		24.9528889911
379PhosphorylationMTKTIYTSPIKALSN
CCCEEECCHHHHHCC		13.9930377154
620PhosphorylationTWPEIVNYLRKRELL
CHHHHHHHHHHHCCC		9.2919823750
666UbiquitinationQIHMFIEKSITRLKK
HHHHHHHHHHHHHHH		42.2024961812
722PhosphorylationFIKVLFATETFAMGL
HHHHHCCCCHHHCCC		28.3719779198
724PhosphorylationKVLFATETFAMGLNL
HHHCCCCHHHCCCCC		16.6119779198
798PhosphorylationEVTMGVPTRLQSQFR
EECCCCCCHHHHHHH		41.4219779198
802PhosphorylationGVPTRLQSQFRLTYN
CCCCHHHHHHHHHHH		35.5619779198
900AcetylationPSILHILKEGRLVAF
CCHHHHHHCCCEEEE		58.4824489116
953AcetylationNHLIYFPKADGYRRR
CCEEEECCCCCCCCC		49.5724489116
968PhosphorylationNFPKFQKTDFYMEEV
CCCCCCCCCCCCCCC		22.1327017623
971PhosphorylationKFQKTDFYMEEVPVT
CCCCCCCCCCCCCCE		13.3627017623
984PhosphorylationVTAIEVITKRKFAAP
CEEEEHHHCCCCCCC		29.9427017623
1017AcetylationTNNILDGKTLKEAIN
CCCCCCCCHHHHHHC		50.8024489116
1027AcetylationKEAINIEKQGLKIHQ
HHHHCHHHCCCEEEH		45.9624489116
1100AcetylationEKRLAVLKDTEFIDQ
HHHHHHHCCCCEECC		56.8824489116
1184UbiquitinationRIEEIYKKMLCVFNT
HHHHHHHHHHHHHCC		21.8222106047
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 SKI2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SKI2_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 SKI2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SKI3_YEASTSKI3physical
10744028
SKI8_YEASTSKI8physical
10744028
RRP41_YEASTSKI6genetic
10922069
SLH1_YEASTSLH1genetic
10922069
DXO_YEASTRAI1genetic
10805743
XRN2_YEASTRAT1genetic
9315672
DCP1_YEASTDCP1genetic
9482746
FBRL_YEASTNOP1physical
16554755
YRA1_YEASTYRA1physical
16554755
SNU13_YEASTSNU13physical
16554755
XRN1_YEASTXRN1physical
16554755
YKC3_YEASTYKL023Wphysical
16554755
STM1_YEASTSTM1physical
16554755
CBF5_YEASTCBF5physical
16554755
SKI3_YEASTSKI3physical
16554755
IMDH4_YEASTIMD4physical
16554755
HAS1_YEASTHAS1physical
16554755
SKI3_YEASTSKI3physical
16429126
SKI8_YEASTSKI8physical
16429126
RL4B_YEASTRPL4Bphysical
16429126
XRN1_YEASTXRN1genetic
17314980
LSM1_YEASTLSM1genetic
17314980
SLX5_YEASTSLX5genetic
17314980
COPE_YEASTSEC28genetic
17314980
DOA1_YEASTDOA1genetic
17314980
LSM6_YEASTLSM6genetic
17314980
UBP6_YEASTUBP6genetic
17314980
PAT1_YEASTPAT1genetic
17314980
CTF8_YEASTCTF8genetic
17314980
PFD1_YEASTPFD1genetic
17314980
ARO1_YEASTARO1genetic
17314980
PFD2_YEASTGIM4genetic
17314980
PFD6_YEASTYKE2genetic
17314980
SKI8_YEASTSKI8genetic
17314980
SKI3_YEASTSKI3physical
18042677
SKI8_YEASTSKI8physical
18042677
PAT1_YEASTPAT1genetic
19061648
UBI4P_YEASTUBI4genetic
19061648
LSM3_YEASTLSM3genetic
19061648
SLX5_YEASTSLX5genetic
19061648
NOP3_YEASTNPL3genetic
19061648
RS6A_YEASTRPS6Bgenetic
19061648
RS6B_YEASTRPS6Bgenetic
19061648
XRN1_YEASTXRN1genetic
19061648
LSM1_YEASTLSM1genetic
19061648
DOA1_YEASTDOA1genetic
19061648
SN309_YEASTSNT309genetic
19061648
RRP7_YEASTRRP7genetic
19061648
PFD6_YEASTYKE2genetic
19061648
LRS4_YEASTLRS4genetic
19061648
POP8_YEASTPOP8genetic
19061648
POP6_YEASTPOP6genetic
19061648
NU120_YEASTNUP120genetic
19061648
PML39_YEASTPML39genetic
19061648
RNA14_YEASTRNA14genetic
19061648
KA120_YEASTKAP120genetic
19061648
SYNC_YEASTDED81genetic
19061648
IF2G_YEASTGCD11genetic
19061648
LCP5_YEASTLCP5genetic
19061648
LSM1_YEASTLSM1genetic
18719247
HSP72_YEASTSSA2physical
19536198
HSP71_YEASTSSA1physical
19536198
SSB1_YEASTSSB1physical
19536198
KC11_YEASTYCK1genetic
19547744
CYPD_YEASTCPR5genetic
19547744
YMC2_YEASTYMC2genetic
20093466
PAT1_YEASTPAT1genetic
20093466
HBT1_YEASTHBT1genetic
20093466
RLA1_YEASTRPP1Agenetic
20093466
RPN4_YEASTRPN4genetic
20093466
GCN20_YEASTGCN20genetic
20093466
GCN1_YEASTGCN1genetic
20093466
XRN1_YEASTXRN1genetic
20093466
CUE3_YEASTCUE3genetic
20093466
TFS2_YEASTDST1genetic
20093466
PEF1_YEASTPEF1genetic
20093466
CHO2_YEASTCHO2genetic
20093466
WSS1_YEASTWSS1genetic
20093466
NUC1_YEASTNUC1genetic
20093466
LSM1_YEASTLSM1genetic
20093466
UBX6_YEASTUBX6genetic
20093466
CYP7_YEASTCPR7genetic
20093466
DHOM_YEASTHOM6genetic
20093466
BCH2_YEASTBCH2genetic
20093466
METK1_YEASTSAM1genetic
20093466
GBLP_YEASTASC1genetic
20093466
MET22_YEASTMET22genetic
20093466
SHE4_YEASTSHE4genetic
20093466
COQ7_YEASTCAT5genetic
20093466
ISW2_YEASTISW2genetic
20093466
SRS2_YEASTSRS2genetic
21459050
SPR3_YEASTSPR3physical
22875988
TCPZ_YEASTCCT6genetic
27708008
MOB2_YEASTMOB2genetic
27708008
UME6_YEASTUME6genetic
27708008
CDK1_YEASTCDC28genetic
27708008
RPN6_YEASTRPN6genetic
27708008
SNU23_YEASTSNU23genetic
27708008
RRP42_YEASTRRP42genetic
27708008
TFB1_YEASTTFB1genetic
27708008
RPB7_YEASTRPB7genetic
27708008
PSB3_YEASTPUP3genetic
27708008
RSP5_YEASTRSP5genetic
27708008
ACT_YEASTACT1genetic
27708008
RPN11_YEASTRPN11genetic
27708008
PSB7_YEASTPRE4genetic
27708008
PRS8_YEASTRPT6genetic
27708008
SWC4_YEASTSWC4genetic
27708008
RRP4_YEASTRRP4genetic
27708008
STS1_YEASTSTS1genetic
27708008
MTR4_YEASTMTR4genetic
27708008
SDO1_YEASTSDO1genetic
27708008
MED14_YEASTRGR1genetic
27708008
IMB1_YEASTKAP95genetic
27708008
PSA7_YEASTPRE10genetic
27708008
BUR1_YEASTSGV1genetic
27708008
PAT1_YEASTPAT1genetic
27708008
RLA1_YEASTRPP1Agenetic
27708008
VMS1_YEASTVMS1genetic
27708008
OCA6_YEASTOCA6genetic
27708008
RLA4_YEASTRPP2Bgenetic
27708008
XRN1_YEASTXRN1genetic
27708008
MTC1_YEASTMTC1genetic
27708008
LSM1_YEASTLSM1genetic
27708008
NUC1_YEASTNUC1genetic
27708008
DHOM_YEASTHOM6genetic
27708008
BCH2_YEASTBCH2genetic
27708008
UBX2_YEASTUBX2genetic
27708008
GBLP_YEASTASC1genetic
27708008
MET22_YEASTMET22genetic
27708008
RS10A_YEASTRPS10Agenetic
27708008
RS3_YEASTRPS3physical
27980209
RS10A_YEASTRPS10Aphysical
27980209
RS20_YEASTRPS20physical
27980209
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SKI2_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-209, AND MASSSPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, 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-209, AND MASSSPECTROMETRY.

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