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P36102 (PAN3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
PAB-dependent poly(A)-specific ribonuclease subunit PAN3
Alternative name(s):
PAB1P-dependent poly(A)-nuclease
PAN deadenylation complex subunit 3
Gene names
Name:PAN3
Synonyms:ECM35
Ordered Locus Names:YKL025C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length679 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 when the poly(A) stretch is bound by poly(A)-binding protein PAB1, which 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 PAB1. PAN cooperates with protein kinase DUN1 in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress. Ref.1 Ref.4 Ref.5 Ref.6 Ref.10

Subunit structure

Homodimer. Interacts with the catalytic subunit PAN2 to form the poly(A)-nuclease (PAN) deadenylation complex. Interacts (via PAM-2 motif) with poly(A)-binding protein PAB1 (via PABC domain), conferring substrate-specificity of the enzyme complex. Ref.1 Ref.6 Ref.9 Ref.12

Subcellular location

Cytoplasm Ref.7 Ref.10.

Domain

The protein kinase domain is predicted to be catalytically inactive. However it still binds ATP and ATP-binding is required for mRNA degradation By similarity. HAMAP-Rule MF_03181

Post-translational modification

Phosphorylated by the cyclin-CDK complex PCL1-PHO85. Ref.11

Miscellaneous

Present with 1600 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the protein kinase superfamily. PAN3 family.

Contains 1 C3H1-type zinc finger.

Contains 1 protein kinase domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PAB1P041475EBI-12895,EBI-12823
PAN2P530103EBI-12895,EBI-12887

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 679679PAB-dependent poly(A)-specific ribonuclease subunit PAN3 HAMAP-Rule MF_03181
PRO_0000058223

Regions

Domain299 – 549251Protein kinase
Zinc finger8 – 3730C3H1-type HAMAP-Rule MF_03181
Nucleotide binding305 – 3139ATP By similarity
Nucleotide binding376 – 3816ATP By similarity
Region560 – 679120Interaction with PAN2 HAMAP-Rule MF_03181
Motif143 – 16321PABPC1-interacting motif-2 (PAM-2) HAMAP-Rule MF_03181
Compositional bias114 – 20188Asn-rich HAMAP-Rule MF_03181

Sites

Binding site3251ATP By similarity

Amino acid modifications

Modified residue571Phosphothreonine Ref.13
Modified residue2521Phosphoserine Ref.13

Experimental info

Mutagenesis1561F → A: Significantly decreases interaction with PAN1. Ref.12

Sequences

Sequence LengthMass (Da)Tools
P36102 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: DE03E15BF4A5DA7C

FASTA67976,455
        10         20         30         40         50         60 
MDKINPDWAK DIPCRNITIY GYCKKEKEGC PFKHSDNTTA TTINDVPPPI DVGEATTPTM 

        70         80         90        100        110        120 
TSVPKFNAKV SASFTPMTVG SDSLTTVTNT TSAATNATGN IAMAATSATA STVNPMINPI 

       130        140        150        160        170        180 
VNSSLVNNNN NNSNISISIP TTASSSNYDP FNAPIFTPSS TSSIHTNANA HSFPFPSIAN 

       190        200        210        220        230        240 
SGGININATD DNSNNMSMAN NVPPPMQPPP IESSNLKYPR IYPPPHSLLQ YHLYAPEQPS 

       250        260        270        280        290        300 
SLKSLLKPNE RSADQLFIPN NIREDLTKKN LSILQVFPSS GKVIPSIVQD YFNLVPLNFN 

       310        320        330        340        350        360 
NNDFLNKTTL FKVFSNYDGK AYVLKRLPNI DKSMNPNKIS KIYQIWSKIN CTNLIKFRDI 

       370        380        390        400        410        420 
FQTTKFGDLS ICLVFDYYPN SLSLYDYHFV NFPKFPITNN YLWIYLVQLT NVINSIHSQN 

       430        440        450        460        470        480 
LSIGNTLNWR KVLITGDPGR IKLSHCNFMD LLFNDDTDTV VSSGGSTIEG QQQLDYKYLG 

       490        500        510        520        530        540 
ELLFNLSINI ENSNNNTAPK EYRLEEITPQ SIDDMRQIDD KFKDVLKYLI SDNGDSKKSI 

       550        560        570        580        590        600 
HDLTSHFYDK MFMVLESSQT YTEYMESVLS RELENGRLFR LVNKLNCIFG RIESRIDINW 

       610        620        630        640        650        660 
SESGTKFPII LFYDYVFHQV DSNGKPIMDL THVLRCLNKL DAGIQEKLML VTPDELNCII 

       670 
ISYKELKDLI ESTFRSITQ 

« Hide

References

« Hide 'large scale' references
[1]"PAN3 encodes a subunit of the Pab1p-dependent poly(A) nuclease in Saccharomyces cerevisiae."
Brown C.E., Tarun S.Z. Jr., Boeck R., Sachs A.B.
Mol. Cell. Biol. 16:5744-5753(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 443-453 AND 517-524, FUNCTION, INTERACTION WITH PAN2.
[2]"Complete DNA sequence of yeast chromosome XI."
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. expand/collapse author list , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"3'-UTR-dependent deadenylation by the yeast poly(A) nuclease."
Lowell J.E., Rudner D.Z., Sachs A.B.
Genes Dev. 6:2088-2099(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Poly(A) tail length control in Saccharomyces cerevisiae occurs by message-specific deadenylation."
Brown C.E., Sachs A.B.
Mol. Cell. Biol. 18:6548-6559(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Posttranscriptional regulation of the RAD5 DNA repair gene by the Dun1 kinase and the Pan2-Pan3 poly(A)-nuclease complex contributes to survival of replication blocks."
Hammet A., Pike B.L., Heierhorst J.
J. Biol. Chem. 277:22469-22474(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DUN1.
[7]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]"Positive and negative regulation of poly(A) nuclease."
Mangus D.A., Evans M.C., Agrin N.S., Smith M.M., Gongidi P., Jacobson A.
Mol. Cell. Biol. 24:5521-5533(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PAN2 AND PAB1.
[10]"Yeast mRNA poly(A) tail length control can be reconstituted in vitro in the absence of Pab1p-dependent poly(A) nuclease activity."
Dheur S., Nykamp K.R., Viphakone N., Swanson M.S., Minvielle-Sebastia L.
J. Biol. Chem. 280:24532-24538(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]"Combining chemical genetics and proteomics to identify protein kinase substrates."
Dephoure N., Howson R.W., Blethrow J.D., Shokat K.M., O'Shea E.K.
Proc. Natl. Acad. Sci. U.S.A. 102:17940-17945(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY PCL1-PHO85.
[12]"Poly(A) nuclease interacts with the C-terminal domain of polyadenylate-binding protein domain from poly(A)-binding protein."
Siddiqui N., Mangus D.A., Chang T.C., Palermino J.M., Shyu A.B., Gehring K.
J. Biol. Chem. 282:25067-25075(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PAB1, MUTAGENESIS OF PHE-156.
[13]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57 AND SER-252, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z28025 Genomic DNA. Translation: CAA81860.1.
BK006944 Genomic DNA. Translation: DAA09129.1.
PIRS37842.
RefSeqNP_012900.1. NM_001179591.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4CYKNMR-A1-41[»]
ProteinModelPortalP36102.
SMRP36102. Positions 259-674.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34106. 52 interactions.
DIPDIP-3987N.
IntActP36102. 8 interactions.
MINTMINT-480456.
STRING4932.YKL025C.

Proteomic databases

MaxQBP36102.
PaxDbP36102.
PeptideAtlasP36102.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYKL025C; YKL025C; YKL025C.
GeneID853843.
KEGGsce:YKL025C.

Organism-specific databases

CYGDYKL025c.
SGDS000001508. PAN3.

Phylogenomic databases

eggNOGNOG260889.
GeneTreeENSGT00390000001504.
HOGENOMHOG000007619.
KOK12572.
OMAGPHSQNT.
OrthoDBEOG7XM36Z.

Enzyme and pathway databases

BioCycYEAST:G3O-31832-MONOMER.

Gene expression databases

GenevestigatorP36102.

Family and domain databases

HAMAPMF_03181. PAN3.
InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR000571. Znf_CCCH.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS50103. ZF_C3H1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio975058.

Entry information

Entry namePAN3_YEAST
AccessionPrimary (citable) accession number: P36102
Secondary accession number(s): D6VXQ9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: July 9, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XI

Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references