THO2_YEAST - dbPTM
THO2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID THO2_YEAST
UniProt AC P53552
Protein Name THO complex subunit 2
Gene Name THO2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1597
Subcellular Localization Nucleus .
Protein Description Component the THO subcomplex of the TREX complex, which operates in coupling transcription elongation to mRNA export. The THO complex is recruited to transcribed genes and moves along the gene with the elongating polymerase during transcription. THO is important for stabilizing nascent RNA in the RNA polymerase II elongation complex by preventing formation of DNA:RNA hybrids behind the elongating polymerase. It functions in cotranscriptional formation of an export-competent messenger ribonucleoprotein particle (mRNP) by facilitating the loading of ATP-dependent RNA helicase SUB2 and the mRNA export factor YRA1 along the nascent mRNA..
Protein Sequence MAEQTLLSKLNALSQKVIPPASPSQASILTEEVIRNWPERSKTLCSDFTALESNDEKEDWLRTLFIELFDFINKNDENSPLKLSDVASFTNELVNHERQVSQASIVGKMFIAVSSTVPNINDLTTISLCKLIPSLHEELFKFSWISSKLLNKEQTTLLRHLLKKSKYELKKYNLLVENSVGYGQLVALLILAYYDPDNFSKVSAYLKEIYHIMGKYSLDSIRTLDVILNVSSQFITEGYKFFIALLRKSDSWPSSHVANNSNYSSLNEGGNMIAANIISFNLSQYNEEVDKENYERYMDMCCILLKNGFVNFYSIWDNVKPEMEFLQEYIQNLETELEEESTKGVENPLAMAAALSTENETDEDNALVVNDDVNMKDKISEETNADIESKGKQKTQQDILLFGKIKLLERLLIHGCVIPVIHVLKQYPKVLYVSESLSRYLGRVFEYLLNPLYTSMTSSGESKDMATALMITRIDNGILAHKPRLIHKYKTHEPFESLELNSSYVFYYSEWNSNLTPFASVNDLFENSHIYLSIIGPYLGRIPTLLSKISRIGVADIQKNHGSESLHVTIDKWIDYVRKFIFPATSLLQNNPIATSEVYELMKFFPFEKRYFIYNEMMTKLSQDILPLKVSFNKAEREAKSILKALSIDTIAKESRRFAKLISTNPLASLVPAVKQIENYDKVSELVVYTTKYFNDFAYDVLQFVLLLRLTYNRPAVQFDGVNQAMWVQRLSIFIAGLAKNCPNMDISNIITYILKTLHNGNIIAVSILKELIITVGGIRDLNEVNMKQLLMLNSGSPLKQYARHLIYDFRDDNSVISSRLTSFFTDQSAISEIILLLYTLNLKANTQNSHYKILSTRCDEMNTLLWSFIELIKHCLKGKAFEENVLPFVELNNRFHLSTPWTFHIWRDYLDNQLNSNENFSIDELIEGAEFSDVDLTKISKDLFTTFWRLSLYDIHFDKSLYDERKNALSGENTGHMSNRKKHLIQNQIKDILVTGISHQRAFKKTSEFISEKSNVWNKDCGEDQIKIFLQNCVVPRVLFSPSDALFSSFFIFMAFRTENLMSILNTCITSNILKTLLFCCTSSEAGNLGLFFTDVLKKLEKMRLNGDFNDQASRKLYEWHSVITEQVIDLLSEKNYMSIRNGIEFMKHVTSVFPVVKAHIQLVYTTLEENLINEEREDIKLPSSALIGHLKARLKDALELDEFCTLTEEEAEQKRIREMELEEIKNYETACQNEQKQVALRKQLELNKSQRLQNDPPKSVASGSAGLNSKDRYTYSRNEPVIPTKPSSSQWSYSKVTRHVDDINHYLATNHLQKAISLVENDDETRNLRKLSKQNMPIFDFRNSTLEIFERYFRTLIQNPQNPDFAEKIDSLKRYIKNISREPYPDTTSSYSEAAAPEYTKRSSRYSGNAGGKDGYGSSNYRGPSNDRSAPKNIKPISSYAHKRSELPTRPSKSKTYNDRSRALRPTGPDRGDGFDQRDNRLREEYKKNSSQRSQLRFPEKPFQEGKDSSKANPYQASSYKRDSPSENEEKPNKRFKKDETIRNKFQTQDYRNTRDSGAAHRANENQRYNGNRKSNTQALPQGPKGGNYVSRYQR
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
22PhosphorylationQKVIPPASPSQASIL
CCCCCCCCHHHHHHH		30.7525752575
24PhosphorylationVIPPASPSQASILTE
CCCCCCHHHHHHHCH		35.5625752575
27PhosphorylationPASPSQASILTEEVI
CCCHHHHHHHCHHHH		15.5325752575
30PhosphorylationPSQASILTEEVIRNW
HHHHHHHCHHHHHHC		28.5629688323
57UbiquitinationALESNDEKEDWLRTL
CCCCCCHHHHHHHHH		64.9323749301
101PhosphorylationVNHERQVSQASIVGK
HCCHHHHHHHHHHHH		16.2230377154
148AcetylationKFSWISSKLLNKEQT
HHHHHHHHHCCHHHH		50.6424489116
152AcetylationISSKLLNKEQTTLLR
HHHHHCCHHHHHHHH		51.6924489116
361PhosphorylationALSTENETDEDNALV
HHCCCCCCCCCCCEE		57.1621440633
647PhosphorylationKSILKALSIDTIAKE
HHHHHHHCHHHHHHH		24.2319795423
650PhosphorylationLKALSIDTIAKESRR
HHHHCHHHHHHHHHH		22.5919795423
675UbiquitinationASLVPAVKQIENYDK
HHHHHHHHHHCCCCC		47.8924961812
800UbiquitinationLNSGSPLKQYARHLI
HCCCCHHHHHHHHHH		44.6524961812
996PhosphorylationQIKDILVTGISHQRA
HHHHHHHHCCCHHHH		25.9227017623
1319PhosphorylationNHLQKAISLVENDDE
HCHHHHHHHHCCCHH		31.0830377154
1390PhosphorylationREPYPDTTSSYSEAA
CCCCCCCCCCCCCCC		24.0530377154
1392PhosphorylationPYPDTTSSYSEAAAP
CCCCCCCCCCCCCCC		30.5028889911
1415AcetylationYSGNAGGKDGYGSSN
CCCCCCCCCCCCCCC		47.2424489116
1427PhosphorylationSSNYRGPSNDRSAPK
CCCCCCCCCCCCCCC		54.9421440633
1445AcetylationPISSYAHKRSELPTR
CCCHHCCCCCCCCCC		49.8225381059
1526PhosphorylationASSYKRDSPSENEEK
CCCCCCCCCCCCCCC		34.0721440633
1528PhosphorylationSYKRDSPSENEEKPN
CCCCCCCCCCCCCCC		57.9428889911
1539AcetylationEKPNKRFKKDETIRN
CCCCCCCCCCHHHHH		64.4525381059
1547AcetylationKDETIRNKFQTQDYR
CCHHHHHHHHCCCCC		29.0624489116
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 THO2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of THO2_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 THO2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HPR1_YEASTHPR1physical
14759368
MFT1_YEASTMFT1physical
14759368
THO2_YEASTTHO2physical
14759368
THP2_YEASTTHP2physical
14759368
TEX1_YEASTTEX1physical
14759368
IMB1_YEASTKAP95physical
14759368
IMA1_YEASTSRP1physical
14759368
HPR1_YEASTHPR1physical
12093753
MFT1_YEASTMFT1physical
12093753
THP2_YEASTTHP2physical
12093753
SUB2_YEASTSUB2physical
11979277
HPR1_YEASTHPR1physical
11979277
MFT1_YEASTMFT1physical
11979277
THP2_YEASTTHP2physical
11979277
YRA1_YEASTYRA1physical
11979277
TEX1_YEASTTEX1physical
11979277
HPR1_YEASTHPR1physical
11060033
RAD16_YEASTRAD16genetic
12000839
RAD7_YEASTRAD7genetic
12000839
YRA1_YEASTYRA1physical
16554755
IMB1_YEASTKAP95physical
16554755
IMA1_YEASTSRP1physical
16554755
TEX1_YEASTTEX1physical
16554755
HXKB_YEASTHXK2physical
16554755
HPR1_YEASTHPR1physical
16429126
MFT1_YEASTMFT1physical
16429126
TEX1_YEASTTEX1physical
16429126
PSP1_YEASTPSP1genetic
17314980
PFD3_YEASTPAC10genetic
17314980
HS104_YEASTHSP104physical
19536198
PCF11_YEASTPCF11genetic
18614048
RNA14_YEASTRNA14genetic
18614048
RNA15_YEASTRNA15genetic
18614048
FIP1_YEASTFIP1genetic
18614048
CTK1_YEASTCTK1genetic
18614048
PAP_YEASTPAP1genetic
18614048
UBP3_YEASTUBP3genetic
18614048
BRE5_YEASTBRE5genetic
18614048
SUB2_YEASTSUB2genetic
12034490
MED3_YEASTPGD1genetic
18682986
SRS2_YEASTSRS2genetic
21459050
HPR1_YEASTHPR1physical
22314234
MFT1_YEASTMFT1physical
22314234
THP2_YEASTTHP2physical
22314234
TEX1_YEASTTEX1physical
22314234
HPR1_YEASTHPR1genetic
22448247
RIF2_YEASTRIF2genetic
22448247
RIF1_YEASTRIF1genetic
22448247
SUB2_YEASTSUB2genetic
22448247
THO2_YEASTTHO2physical
24244187
HPR1_YEASTHPR1physical
24244187
MFT1_YEASTMFT1physical
24244187
HRB1_YEASTHRB1physical
24244187
SUB2_YEASTSUB2physical
24244187
GPB2_YEASTGPB2physical
24244187
THP2_YEASTTHP2physical
24244187
TEX1_YEASTTEX1physical
24244187
YRA1_YEASTYRA1genetic
24244187
HPR1_YEASTHPR1physical
24500206
UAF30_YEASTUAF30genetic
26663077
RRN3_YEASTRRN3genetic
26663077
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of THO2_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-22; SER-24 AND SER-1392,AND MASS SPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND MASSSPECTROMETRY.

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