TPA1_YEAST - dbPTM
TPA1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TPA1_YEAST
UniProt AC P40032
Protein Name Prolyl 3,4-dihydroxylase TPA1 {ECO:0000303|PubMed:16809762}
Gene Name TPA1 {ECO:0000303|PubMed:16809762}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 644
Subcellular Localization Nucleus .
Protein Description Prolyl 3,4-dihydroxylase that catalyzes 3,4-dihydroxylation of 'Pro-64' of small ribosomal subunit uS12 (RPS23A and RPS23B), thereby regulating protein translation termination efficiency. Part of a messenger ribonucleoprotein (mRNP) complex at the 3'-UTR of mRNAs. It associates specifically with components of the translation termination complex and is involved in both translation termination and in regulation of normal mRNA decay through translation termination-coupled poly(A) shortening..
Protein Sequence MKRKTAEVKGEKERNSKQISLEEDKIKGMFNPKIWDKTFQDGLKKEIEDSQPYNWGTIHELVNDDLLRAVRKEIETEIHFTKKETDIYRVNQSGDLANLSGLDWDDLSRLPNLFKLRQILYSKQYRDFFGYVTKAGKLSGSKTDMSINTYTKGCHLLTHDDVIGSRRISFILYLPDPDRKWKSHYGGGLRLFPSILPNVPHSDPSAKLVPQFNQIAFFKVLPGFSFHDVEEVKVDKHRLSIQGWYHIPQVGEEGYIPGEEEAWVRNNTSTLAQIESNVLEDFEFPKDERNILSFHEVKHFEKMLKGDAGAKTDNTPKESMTSVISDSVKLSEAEFTYLSQYISPEHLSSKGIEKLQKQFVENSSLQIESFLNDDKSELLKKVIKQKELEQECPYHSKDVKAPWKTAIPPHKARYLYIDGKEYRNFQTEADILEALNNNDLPNFQFTKDAIKIISDASGNSRENNFDAELALIDLAVFHKSTIFKKYLALLTSLCPVSEQILIRRFRPGMDFTLATKCRFNELLKSNPDIIDAVLEGTLCLTPSAGWESGELGGYELYMMDDDEDNKQYLKEDVEDASVYRADDSGDSVLINDPPAWNTFNLVLRDESVLEFVKYVSWSAKSSRWDVKMKWDVKSCDEDGQEDEA
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
9AcetylationKRKTAEVKGEKERNS
CCCCCCCCCHHHHCC		53.5125381059
17AcetylationGEKERNSKQISLEED
CHHHHCCCCCCCCHH		56.0224489116
20PhosphorylationERNSKQISLEEDKIK
HHCCCCCCCCHHHHC		27.5128889911
25AcetylationQISLEEDKIKGMFNP
CCCCCHHHHCCCCCH		49.9924489116
33AcetylationIKGMFNPKIWDKTFQ
HCCCCCHHHHHHHHH		58.4924489116
37AcetylationFNPKIWDKTFQDGLK
CCHHHHHHHHHHHHH		35.9224489116
44UbiquitinationKTFQDGLKKEIEDSQ
HHHHHHHHHHHCCCC		54.6223749301
115AcetylationSRLPNLFKLRQILYS
HCCCCHHHHHHHHHC		46.0224489116
134AcetylationDFFGYVTKAGKLSGS
HHHCHHCCCCCCCCC		45.1324489116
142UbiquitinationAGKLSGSKTDMSINT
CCCCCCCCCCCEEEC		52.6623749301
268PhosphorylationEAWVRNNTSTLAQIE
CHHHHCCCCCHHHHH		27.0022369663
269PhosphorylationAWVRNNTSTLAQIES
HHHHCCCCCHHHHHH		24.4422369663
270PhosphorylationWVRNNTSTLAQIESN
HHHCCCCCHHHHHHH		24.8722369663
276PhosphorylationSTLAQIESNVLEDFE
CCHHHHHHHCCCCCC		33.5922369663
293PhosphorylationKDERNILSFHEVKHF
CCCCCEECHHHHHHH		22.2922369663
298AcetylationILSFHEVKHFEKMLK
EECHHHHHHHHHHHC		39.3224489116
312PhosphorylationKGDAGAKTDNTPKES
CCCCCCCCCCCCHHH		33.6728889911
315PhosphorylationAGAKTDNTPKESMTS
CCCCCCCCCHHHHHH		38.2523749301
317AcetylationAKTDNTPKESMTSVI
CCCCCCCHHHHHHHH		61.4522865919
319PhosphorylationTDNTPKESMTSVISD
CCCCCHHHHHHHHCC		33.2222369663
321PhosphorylationNTPKESMTSVISDSV
CCCHHHHHHHHCCCC		29.1722369663
322PhosphorylationTPKESMTSVISDSVK
CCHHHHHHHHCCCCC		14.6022369663
325PhosphorylationESMTSVISDSVKLSE
HHHHHHHCCCCCCCH		22.9822369663
327PhosphorylationMTSVISDSVKLSEAE
HHHHHCCCCCCCHHH		17.8622369663
420AcetylationRYLYIDGKEYRNFQT
EEEEECCEECCCCCC		48.0724489116
420SuccinylationRYLYIDGKEYRNFQT
EEEEECCEECCCCCC		48.0723954790
512PhosphorylationFRPGMDFTLATKCRF
CCCCCCCCHHHHHHH		15.9527017623
577PhosphorylationKEDVEDASVYRADDS
HHHHHHCCEEECCCC		31.8122890988
579PhosphorylationDVEDASVYRADDSGD
HHHHCCEEECCCCCC		9.5122890988
607PhosphorylationNLVLRDESVLEFVKY
EEEECCHHHHHHHHH		35.9720630870
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 TPA1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TPA1_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 TPA1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TPA1_YEASTTPA1physical
14759368
EF3A_YEASTYEF3physical
14759368
RV167_YEASTRVS167physical
16554755
EF3A_YEASTYEF3physical
16554755
CORO_YEASTCRN1physical
16554755
RLM1_YEASTRLM1physical
16554755
PABP_YEASTPAB1physical
16809762
RV161_YEASTRVS161genetic
17314980
MTC4_YEASTMTC4genetic
17314980
UMP1_YEASTUMP1genetic
17314980
GYP7_YEASTGYP7genetic
20093466
MGMT_YEASTMGT1genetic
20093466
RL35A_YEASTRPL35Agenetic
20093466
RL35B_YEASTRPL35Agenetic
20093466
ARF2_YEASTARF2genetic
20093466
YD249_YEASTYDR249Cgenetic
20093466
PEX10_YEASTPEX10genetic
20093466
SUM1_YEASTSUM1genetic
20093466
RTF1_YEASTRTF1genetic
20093466
CGR1_YEASTCGR1genetic
20093466
YG34_YEASTYGR122Wgenetic
20093466
ECM3_YEASTECM3genetic
20093466
YO093_YEASTYOR093Cgenetic
20093466
FABD_YEASTMCT1genetic
20093466
TPO4_YEASTTPO4genetic
20093466
RDL2_YEASTRDL2genetic
20093466
SNU66_YEASTSNU66genetic
20093466
YP247_YEASTYPL247Cgenetic
20093466
RBD2_YEASTRBD2genetic
20093466
PRM3_YEASTPRM3genetic
20093466
YP107_YEASTYPL107Wgenetic
20093466
AAD16_YEASTYPL088Wgenetic
20093466
SRL4_YEASTSRL4genetic
20093466
YP174_YEASTYPR174Cgenetic
20093466
AQY1_YEASTAQY1genetic
20093466
MAG_YEASTMAG1genetic
25381260
DPOZ_YEASTREV3genetic
25381260
GYP7_YEASTGYP7genetic
27708008
MKS1_YEASTMKS1genetic
27708008
NCBP2_YEASTCBC2genetic
27708008
RL35A_YEASTRPL35Agenetic
27708008
RL35B_YEASTRPL35Agenetic
27708008
MGMT_YEASTMGT1genetic
27708008
SPO71_YEASTSPO71genetic
27708008
YD249_YEASTYDR249Cgenetic
27708008
PEX10_YEASTPEX10genetic
27708008
CGR1_YEASTCGR1genetic
27708008
ASK10_YEASTASK10genetic
27708008
RL16A_YEASTRPL16Agenetic
27708008
DAL81_YEASTDAL81genetic
27708008
LHS1_YEASTLHS1genetic
27708008
LST4_YEASTLST4genetic
27708008
YKS7_YEASTFAT3genetic
27708008
PUF3_YEASTPUF3genetic
27708008
ENV10_YEASTENV10genetic
27708008
YPT7_YEASTYPT7genetic
27708008
GTR1_YEASTGTR1genetic
27708008
IOC4_YEASTIOC4genetic
27708008
SAM37_YEASTSAM37genetic
27708008
GBLP_YEASTASC1genetic
27708008
SCS7_YEASTSCS7genetic
27708008
PUB1_YEASTPUB1genetic
27708008
ARK1_YEASTARK1genetic
27708008
SIW14_YEASTSIW14genetic
27708008
BRE5_YEASTBRE5genetic
27708008
YO093_YEASTYOR093Cgenetic
27708008
FABD_YEASTMCT1genetic
27708008
CHL1_YEASTCHL1genetic
27708008
SRL4_YEASTSRL4genetic
27708008
AAD16_YEASTYPL088Wgenetic
27708008
YP107_YEASTYPL107Wgenetic
27708008
YP247_YEASTYPL247Cgenetic
27708008
YP174_YEASTYPR174Cgenetic
27708008
AQY1_YEASTAQY1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TPA1_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-293; SER-577 ANDSER-607, AND MASS SPECTROMETRY.

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