PAN2_YEAST - dbPTM
PAN2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PAN2_YEAST
UniProt AC P53010
Protein Name PAN2-PAN3 deadenylation complex catalytic subunit PAN2 {ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000305}
Gene Name PAN2 {ECO:0000255|HAMAP-Rule:MF_03182}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1115
Subcellular Localization Cytoplasm .
Protein Description Catalytic 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. PAN cooperates with protein kinase DUN1 in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress..
Protein Sequence MNNWQHFFNNPVDLSEHLKKPYFRFDNRDKEITAISFDEKANLIWSGDSYGCISSYDPTFQLYTRYRGHIGGNSVKDILSHRDGILSISEDSLHFANRRGVTKLNLTSIDIAAFSELNTMCYSPHSLKNNIYCGGDNTNWGIASIDLNRGCLDSLLNYSSKVKLMCSNNKVLSIGRQTGTVDLLDPTSNRTIKSFNAHSASISAMDLRDNTLVTVGKSKRFYNLYADPFVNVYDLRTMRQLPPVSFSKGTTMGSGGADFVQLHPLLPTVMIVASSSGSFDFIDLSNPTLRTQYVHPCQSIKKLCLSPNGDVLGILEADNHLDTWRRSSNNMGMFTNTPEMLAYPDYFNDITSDGPISVDDETYPLSSVGMPYYLDKLLSAWPPVVFKSEGTIPQLTGKSPLPSSGKLKSNLAVISSQNEKLSTQEFPLLRYDRTKYGMRNAIPDYVCLRDIRKQITSGLETSDIQTYTSINKYEVPPAYSRLPLTSGRFGTDNFDFTPFNNTEYSGLDPDVDNHYTNAIIQLYRFIPEMFNFVVGCLKDENFETTLLTDLGYLFDMMERSHGKICSSSNFQASLKSLTDKRQLENGEPQEHLEEYLESLCIRESIEDFNSSESIKRNMPQKFNRFLLSQLIKEEAQTVNHNITLNQCFGLETEIRTECSCDHYDTTVKLLPSLSISGINKTVIKQLNKKSNGQNILPYIEYAMKNVTQKNSICPTCGKTETITQECTVKNLPSVLSLELSLLDTEFSNIRSSKNWLTSEFYGSIIKNKAVLRSTASELKGTSHIFKYELNGYVAKITDNNNETRLVTYVKKYNPKENCFKWLMFNDYLVVEITEEEALKMTYPWKTPEIIIYCDAEELRKPFFSVDTYSINYDILFRDYFANGIRDTARREYKLLTHDEAPKSGTLVAIDAEFVSLQSELCEIDHQGIRSIIRPKRTALARISIIRGEEGELYGVPFVDDYVVNTNHIEDYLTRYSGILPGDLDPEKSTKRLVRRNVVYRKVWLLMQLGCVFVGHGLNNDFKHININVPRNQIRDTAIYFLQGKRYLSLRYLAYVLLGMNIQEGNHDSIEDAHTALILYKKYLHLKEKAIFEKVLNSVYEEGRAHNFKVPETSKG
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
36PhosphorylationDKEITAISFDEKANL
CCEEEEEEECCCCCE		24.9630377154
178PhosphorylationVLSIGRQTGTVDLLD
EEEEECCCCCCEEEC		33.2027017623
180PhosphorylationSIGRQTGTVDLLDPT
EEECCCCCCEEECCC		17.7727017623
191PhosphorylationLDPTSNRTIKSFNAH
ECCCCCCEEEEECCC		36.6927017623
199PhosphorylationIKSFNAHSASISAMD
EEEECCCCCEEEEEE		22.6923749301
201PhosphorylationSFNAHSASISAMDLR
EECCCCCEEEEEECC		21.7923749301
211PhosphorylationAMDLRDNTLVTVGKS
EEECCCCEEEEECCC		27.2222369663
214PhosphorylationLRDNTLVTVGKSKRF
CCCCEEEEECCCCCC		27.0122369663
323PhosphorylationEADNHLDTWRRSSNN
EECCCHHHCCCCCCC		27.5119779198
396PhosphorylationEGTIPQLTGKSPLPS
CCCCCCCCCCCCCCC		37.0021440633
399PhosphorylationIPQLTGKSPLPSSGK
CCCCCCCCCCCCCCC		32.7721440633
403PhosphorylationTGKSPLPSSGKLKSN
CCCCCCCCCCCCCCC		60.4524961812
404PhosphorylationGKSPLPSSGKLKSNL
CCCCCCCCCCCCCCE		37.7028889911
409PhosphorylationPSSGKLKSNLAVISS
CCCCCCCCCEEEEEC		47.7319779198
415PhosphorylationKSNLAVISSQNEKLS
CCCEEEEECCCCCCC		21.1928889911
416PhosphorylationSNLAVISSQNEKLST
CCEEEEECCCCCCCC		26.3819779198
604PhosphorylationESLCIRESIEDFNSS
HHHHHHHHHHCCCCC		22.7927017623
698PhosphorylationNGQNILPYIEYAMKN
CCCCHHHHHHHHHHH		11.7027017623
701PhosphorylationNILPYIEYAMKNVTQ
CHHHHHHHHHHHCCC		11.4827017623
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 PAN2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PAN2_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 PAN2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PAN3_YEASTPAN3physical
11805826
PAN3_YEASTPAN3physical
8816488
PAN3_YEASTPAN3physical
15169912
PBP1_YEASTPBP1physical
15169912
PAN3_YEASTPAN3physical
16554755
PABP_YEASTPAB1physical
16429126
PAN3_YEASTPAN3physical
16429126
DEF1_YEASTDEF1physical
18467557
PAN3_YEASTPAN3physical
18719252
PAN3_YEASTPAN3physical
20826334
PAN3_YEASTPAN3physical
24880344
CDC27_YEASTCDC27genetic
27708008
SLI15_YEASTSLI15genetic
27708008
APC11_YEASTAPC11genetic
27708008
ARP2_YEASTARP2genetic
27708008
CCA1_YEASTCCA1genetic
27708008
ACT_YEASTACT1genetic
27708008
PDS5_YEASTPDS5genetic
27708008
VTI1_YEASTVTI1genetic
27708008
NOP2_YEASTNOP2genetic
27708008
SEC12_YEASTSEC12genetic
27708008
MGR1_YEASTMGR1genetic
27708008
GPR1_YEASTGPR1genetic
27708008
STP1_YEASTSTP1genetic
27708008
SNF6_YEASTSNF6genetic
27708008
RL14A_YEASTRPL14Agenetic
27708008
CTK1_YEASTCTK1genetic
27708008
BPT1_YEASTBPT1genetic
27708008
MMR1_YEASTMMR1genetic
27708008
EIF3J_YEASTHCR1genetic
27708008
PFD6_YEASTYKE2genetic
27708008
TBA3_YEASTTUB3genetic
27708008
SUB1_YEASTSUB1genetic
27708008
MGR3_YEASTMGR3genetic
27708008
PFD4_YEASTGIM3genetic
27708008
RTG1_YEASTRTG1genetic
27708008
IRA2_YEASTIRA2genetic
27708008
INO4_YEASTINO4genetic
27708008
BUB3_YEASTBUB3genetic
27708008
TBCA_YEASTRBL2genetic
27708008
LIS1_YEASTPAC1genetic
27708008
SMA1_YEASTSMA1genetic
27708008
GGPPS_YEASTBTS1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PAN2_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-404, AND MASSSPECTROMETRY.

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