PAN3_YEAST - dbPTM
PAN3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PAN3_YEAST
UniProt AC P36102
Protein Name PAN2-PAN3 deadenylation complex subunit PAN3 {ECO:0000255|HAMAP-Rule:MF_03181, ECO:0000305}
Gene Name PAN3 {ECO:0000255|HAMAP-Rule:MF_03181}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 679
Subcellular Localization Cytoplasm .
Protein Description Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping by DCP1-DCP2 and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails, trimming the tails from their synthesized length to the slightly shorter, apparently messenger-specific length found on newly exported mRNAs. PAN3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its interaction with RNA and with PAB1. PAN cooperates with protein kinase DUN1 in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress..
Protein Sequence MDKINPDWAKDIPCRNITIYGYCKKEKEGCPFKHSDNTTATTINDVPPPIDVGEATTPTMTSVPKFNAKVSASFTPMTVGSDSLTTVTNTTSAATNATGNIAMAATSATASTVNPMINPIVNSSLVNNNNNNSNISISIPTTASSSNYDPFNAPIFTPSSTSSIHTNANAHSFPFPSIANSGGININATDDNSNNMSMANNVPPPMQPPPIESSNLKYPRIYPPPHSLLQYHLYAPEQPSSLKSLLKPNERSADQLFIPNNIREDLTKKNLSILQVFPSSGKVIPSIVQDYFNLVPLNFNNNDFLNKTTLFKVFSNYDGKAYVLKRLPNIDKSMNPNKISKIYQIWSKINCTNLIKFRDIFQTTKFGDLSICLVFDYYPNSLSLYDYHFVNFPKFPITNNYLWIYLVQLTNVINSIHSQNLSIGNTLNWRKVLITGDPGRIKLSHCNFMDLLFNDDTDTVVSSGGSTIEGQQQLDYKYLGELLFNLSINIENSNNNTAPKEYRLEEITPQSIDDMRQIDDKFKDVLKYLISDNGDSKKSIHDLTSHFYDKMFMVLESSQTYTEYMESVLSRELENGRLFRLVNKLNCIFGRIESRIDINWSESGTKFPIILFYDYVFHQVDSNGKPIMDLTHVLRCLNKLDAGIQEKLMLVTPDELNCIIISYKELKDLIESTFRSITQ
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
35PhosphorylationEGCPFKHSDNTTATT
CCCCCCCCCCCCCEE		32.9022369663
38PhosphorylationPFKHSDNTTATTIND
CCCCCCCCCCEECCC		23.8522369663
39PhosphorylationFKHSDNTTATTINDV
CCCCCCCCCEECCCC		28.4122369663
41PhosphorylationHSDNTTATTINDVPP
CCCCCCCEECCCCCC		26.5622369663
42PhosphorylationSDNTTATTINDVPPP
CCCCCCEECCCCCCC		18.4722369663
56PhosphorylationPIDVGEATTPTMTSV
CCCCCCCCCCCCCCC		29.0722369663
57PhosphorylationIDVGEATTPTMTSVP
CCCCCCCCCCCCCCC		24.6622369663
59PhosphorylationVGEATTPTMTSVPKF
CCCCCCCCCCCCCCC		30.8722369663
61PhosphorylationEATTPTMTSVPKFNA
CCCCCCCCCCCCCCC		29.1122369663
62PhosphorylationATTPTMTSVPKFNAK
CCCCCCCCCCCCCCE		26.1222369663
222PhosphorylationNLKYPRIYPPPHSLL
CCCCCCCCCCCCCCE		15.8027017623
227PhosphorylationRIYPPPHSLLQYHLY
CCCCCCCCCEEEEEE		36.2327017623
231PhosphorylationPPHSLLQYHLYAPEQ
CCCCCEEEEEECCCC		8.1827017623
234PhosphorylationSLLQYHLYAPEQPSS
CCEEEEEECCCCCCH		13.5427017623
240PhosphorylationLYAPEQPSSLKSLLK
EECCCCCCHHHHHCC		48.2527017623
252PhosphorylationLLKPNERSADQLFIP
HCCCCCCCHHHCCCC		29.9817595167
333PhosphorylationRLPNIDKSMNPNKIS
ECCCCCCCCCHHHHH		21.7519823750
340PhosphorylationSMNPNKISKIYQIWS
CCCHHHHHHHHHHHH		18.0128889911
343PhosphorylationPNKISKIYQIWSKIN
HHHHHHHHHHHHHCC		9.5519823750
347PhosphorylationSKIYQIWSKINCTNL
HHHHHHHHHCCCCCC		25.8619823750
603PhosphorylationIDINWSESGTKFPII
CEEECCCCCCCCEEE		46.3728889911
605PhosphorylationINWSESGTKFPIILF
EECCCCCCCCEEEEE		38.5028889911
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 PAN3_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PAN3_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 PAN3_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PAN2_YEASTPAN2physical
8816488
PAN3_YEASTPAN3physical
15169912
IF2M_YEASTIFM1genetic
19061648
PABP_YEASTPAB1genetic
19061648
IF2A_YEASTSUI2genetic
19061648
LTV1_YEASTLTV1genetic
19061648
SAC3_YEASTSAC3genetic
19547744
PFD3_YEASTPAC10genetic
18931302
PFD2_YEASTGIM4genetic
18931302
ATC1_YEASTPMR1genetic
18931302
MNN10_YEASTMNN10genetic
18931302
EMP24_YEASTEMP24genetic
18931302
CSF1_YEASTCSF1genetic
27708008
TSR2_YEASTTSR2genetic
27708008
FAL1_YEASTFAL1genetic
27708008
SCC2_YEASTSCC2genetic
27708008
CDC1_YEASTCDC1genetic
27708008
TCPZ_YEASTCCT6genetic
27708008
STE50_YEASTSTE50genetic
27708008
SNT1_YEASTSNT1genetic
27708008
RPA14_YEASTRPA14genetic
27708008
EF2_YEASTEFT2genetic
27708008
SXM1_YEASTSXM1genetic
27708008
MRM2_YEASTMRM2genetic
27708008
YG1D_YEASTYGR021Wgenetic
27708008
PFD3_YEASTPAC10genetic
27708008
TBP7_YEASTYTA7genetic
27708008
YOR1_YEASTYOR1genetic
27708008
SODM_YEASTSOD2genetic
27708008
ARP1_YEASTARP1genetic
27708008
WSS1_YEASTWSS1genetic
27708008
YJB6_YEASTYJL016Wgenetic
27708008
RL17B_YEASTRPL17Bgenetic
27708008
CBF1_YEASTCBF1genetic
27708008
DNM1_YEASTDNM1genetic
27708008
BPT1_YEASTBPT1genetic
27708008
RAD5_YEASTRAD5genetic
27708008
ERG3_YEASTERG3genetic
27708008
MMR1_YEASTMMR1genetic
27708008
PFD6_YEASTYKE2genetic
27708008
TOP3_YEASTTOP3genetic
27708008
ERG6_YEASTERG6genetic
27708008
TBA3_YEASTTUB3genetic
27708008
NGL2_YEASTNGL2genetic
27708008
CYB5_YEASTCYB5genetic
27708008
PFD4_YEASTGIM3genetic
27708008
IZH2_YEASTIZH2genetic
27708008
INO4_YEASTINO4genetic
27708008
BUB3_YEASTBUB3genetic
27708008
TBCA_YEASTRBL2genetic
27708008
CIN1_YEASTCIN1genetic
27708008
RAD1_YEASTRAD1genetic
27708008
GGPPS_YEASTBTS1genetic
27708008
SET6_YEASTSET6genetic
27708008
TBCC_YEASTCIN2genetic
27708008
CTF4_YEASTCTF4genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PAN3_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 THR-57; THR-59; SER-252 ANDSER-347, AND MASS SPECTROMETRY.
"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 THR-39; THR-61 AND SER-62,AND MASS SPECTROMETRY.
"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 THR-57, AND MASSSPECTROMETRY.

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