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P36102

- PAN3_YEAST

UniProt

P36102 - PAN3_YEAST

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Protein

PAB-dependent poly(A)-specific ribonuclease subunit PAN3

Gene

PAN3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.5 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei325 – 3251ATPUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri8 – 3730C3H1-typeUniRule annotationAdd
BLAST
Nucleotide bindingi305 – 3139ATPUniRule annotation
Nucleotide bindingi376 – 3816ATPUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. protein kinase activity Source: InterPro

GO - Biological processi

  1. DNA repair Source: SGD
  2. mRNA 3'-end processing Source: SGD
  3. postreplication repair Source: SGD
  4. RNA phosphodiester bond hydrolysis, exonucleolytic Source: GOC
Complete GO annotation...

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-31832-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
PAB-dependent poly(A)-specific ribonuclease subunit PAN3UniRule annotation
Alternative name(s):
PAB1P-dependent poly(A)-nucleaseUniRule annotation
PAN deadenylation complex subunit 3UniRule annotation
Gene namesi
Name:PAN3UniRule annotation
Synonyms:ECM35
Ordered Locus Names:YKL025C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XI

Organism-specific databases

CYGDiYKL025c.
SGDiS000001508. PAN3.

Subcellular locationi

Cytoplasm 2 PublicationsUniRule annotation

GO - Cellular componenti

  1. PAN complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi156 – 1561F → A: Significantly decreases interaction with PAN1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 679679PAB-dependent poly(A)-specific ribonuclease subunit PAN3PRO_0000058223Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei57 – 571Phosphothreonine1 Publication
Modified residuei252 – 2521Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated by the cyclin-CDK complex PCL1-PHO85.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP36102.
PaxDbiP36102.
PeptideAtlasiP36102.

Expressioni

Gene expression databases

GenevestigatoriP36102.

Interactioni

Subunit structurei

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.4 PublicationsUniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
PAB1P041475EBI-12895,EBI-12823
PAN2P530103EBI-12895,EBI-12887

Protein-protein interaction databases

BioGridi34106. 54 interactions.
DIPiDIP-3987N.
IntActiP36102. 8 interactions.
MINTiMINT-480456.
STRINGi4932.YKL025C.

Structurei

Secondary structure

1
679
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 94
Helixi15 – 195
Helixi24 – 274

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CYKNMR-A1-41[»]
4Q8JX-ray3.80B/C/E/F/H/I/K/L226-679[»]
ProteinModelPortaliP36102.
SMRiP36102. Positions 1-41, 228-679.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini299 – 549251Protein kinaseUniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni560 – 679120Interaction with PAN2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi143 – 16321PABPC1-interacting motif-2 (PAM-2)Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi114 – 20188Asn-richAdd
BLAST

Domaini

The protein kinase domain is predicted to be catalytically inactive. However it still binds ATP and ATP-binding is required for mRNA degradation.UniRule annotation

Sequence similaritiesi

Belongs to the protein kinase superfamily. PAN3 family.UniRule annotation
Contains 1 C3H1-type zinc finger.UniRule annotation
Contains 1 protein kinase domain.UniRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri8 – 3730C3H1-typeUniRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG260889.
GeneTreeiENSGT00390000001504.
HOGENOMiHOG000007619.
InParanoidiP36102.
KOiK12572.
OMAiGPHSQNT.
OrthoDBiEOG7XM36Z.

Family and domain databases

HAMAPiMF_03181. PAN3.
InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR000571. Znf_CCCH.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS50103. ZF_C3H1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P36102-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDKINPDWAK DIPCRNITIY GYCKKEKEGC PFKHSDNTTA TTINDVPPPI
60 70 80 90 100
DVGEATTPTM TSVPKFNAKV SASFTPMTVG SDSLTTVTNT TSAATNATGN
110 120 130 140 150
IAMAATSATA STVNPMINPI VNSSLVNNNN NNSNISISIP TTASSSNYDP
160 170 180 190 200
FNAPIFTPSS TSSIHTNANA HSFPFPSIAN SGGININATD DNSNNMSMAN
210 220 230 240 250
NVPPPMQPPP IESSNLKYPR IYPPPHSLLQ YHLYAPEQPS SLKSLLKPNE
260 270 280 290 300
RSADQLFIPN NIREDLTKKN LSILQVFPSS GKVIPSIVQD YFNLVPLNFN
310 320 330 340 350
NNDFLNKTTL FKVFSNYDGK AYVLKRLPNI DKSMNPNKIS KIYQIWSKIN
360 370 380 390 400
CTNLIKFRDI FQTTKFGDLS ICLVFDYYPN SLSLYDYHFV NFPKFPITNN
410 420 430 440 450
YLWIYLVQLT NVINSIHSQN LSIGNTLNWR KVLITGDPGR IKLSHCNFMD
460 470 480 490 500
LLFNDDTDTV VSSGGSTIEG QQQLDYKYLG ELLFNLSINI ENSNNNTAPK
510 520 530 540 550
EYRLEEITPQ SIDDMRQIDD KFKDVLKYLI SDNGDSKKSI HDLTSHFYDK
560 570 580 590 600
MFMVLESSQT YTEYMESVLS RELENGRLFR LVNKLNCIFG RIESRIDINW
610 620 630 640 650
SESGTKFPII LFYDYVFHQV DSNGKPIMDL THVLRCLNKL DAGIQEKLML
660 670
VTPDELNCII ISYKELKDLI ESTFRSITQ
Length:679
Mass (Da):76,455
Last modified:June 1, 1994 - v1
Checksum:iDE03E15BF4A5DA7C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z28025 Genomic DNA. Translation: CAA81860.1.
BK006944 Genomic DNA. Translation: DAA09129.1.
PIRiS37842.
RefSeqiNP_012900.1. NM_001179591.1.

Genome annotation databases

EnsemblFungiiYKL025C; YKL025C; YKL025C.
GeneIDi853843.
KEGGisce:YKL025C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z28025 Genomic DNA. Translation: CAA81860.1 .
BK006944 Genomic DNA. Translation: DAA09129.1 .
PIRi S37842.
RefSeqi NP_012900.1. NM_001179591.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4CYK NMR - A 1-41 [» ]
4Q8J X-ray 3.80 B/C/E/F/H/I/K/L 226-679 [» ]
ProteinModelPortali P36102.
SMRi P36102. Positions 1-41, 228-679.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 34106. 54 interactions.
DIPi DIP-3987N.
IntActi P36102. 8 interactions.
MINTi MINT-480456.
STRINGi 4932.YKL025C.

Proteomic databases

MaxQBi P36102.
PaxDbi P36102.
PeptideAtlasi P36102.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YKL025C ; YKL025C ; YKL025C .
GeneIDi 853843.
KEGGi sce:YKL025C.

Organism-specific databases

CYGDi YKL025c.
SGDi S000001508. PAN3.

Phylogenomic databases

eggNOGi NOG260889.
GeneTreei ENSGT00390000001504.
HOGENOMi HOG000007619.
InParanoidi P36102.
KOi K12572.
OMAi GPHSQNT.
OrthoDBi EOG7XM36Z.

Enzyme and pathway databases

BioCyci YEAST:G3O-31832-MONOMER.

Miscellaneous databases

NextBioi 975058.

Gene expression databases

Genevestigatori P36102.

Family and domain databases

HAMAPi MF_03181. PAN3.
InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR000571. Znf_CCCH.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS50103. ZF_C3H1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. 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].

Entry informationi

Entry nameiPAN3_YEAST
AccessioniPrimary (citable) accession number: P36102
Secondary accession number(s): D6VXQ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: October 29, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1600 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

External Data

Dasty 3