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Protein

PAN2-PAN3 deadenylation complex catalytic subunit PAN2

Gene

PAN2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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.UniRule annotation9 Publications

Miscellaneous

Present with 1510 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

a divalent metal cationUniRule annotation1 PublicationNote: Binds 2 metal cations per subunit in the catalytic exonuclease domain.UniRule annotation1 Publication

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Positively regulated by the regulatory subunit PAN3. Negatively regulated by PAB1-binding protein PBP1. Inhibited under stress conditions. Inhibition of deadenylation under stress increases mRNA stability, which may be a mechanism to retain the majority of the cytoplasmic pool of mRNAs for later reuse and recovery from stress.UniRule annotation3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi660ZincCombined sources1 Publication1
Metal bindingi662Zinc; via pros nitrogenCombined sources1 Publication1
Metal bindingi713ZincCombined sources1 Publication1
Metal bindingi716ZincCombined sources1 Publication1
Metal bindingi910Divalent metal cation; catalyticUniRule annotationBy similarity1 Publication1
Metal bindingi912Divalent metal cation; catalyticUniRule annotationBy similarity1 Publication1
Metal bindingi1020Divalent metal cation; catalyticUniRule annotationBy similarity1
Metal bindingi1071Divalent metal cation; catalyticUniRule annotationBy similarity1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

  • mRNA processing Source: UniProtKB-KW
  • nuclear-transcribed mRNA poly(A) tail shortening Source: SGD
  • postreplication repair Source: SGD

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionExonuclease, Hydrolase, Nuclease
Biological processmRNA processing
LigandMetal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-30594-MONOMER

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
PAN2-PAN3 deadenylation complex catalytic subunit PAN2UniRule annotationCurated (EC:3.1.13.4UniRule annotation)
Alternative name(s):
PAB1P-dependent poly(A)-specific ribonucleaseUniRule annotation
Poly(A)-nuclease deadenylation complex subunit 2UniRule annotation
Short name:
PAN deadenylation complex subunit 2UniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PAN2UniRule annotation
Ordered Locus Names:YGL094C
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome VII

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000003062 PAN2

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi912E → A: Abolishes nuclease activity. 1 Publication1
Mutagenesisi1020D → A: Abolishes nuclease activity. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000582221 – 1115PAN2-PAN3 deadenylation complex catalytic subunit PAN2Add BLAST1115

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P53010

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P53010

PRoteomics IDEntifications database

More...
PRIDEi
P53010

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P53010

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Forms a heterotrimer with an asymmetric homodimer of the regulatory subunit PAN3 to form the poly(A)-nuclease (PAN) deadenylation complex.UniRule annotation4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
PAN3P361029EBI-12887,EBI-12895

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
33157, 128 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-3294 PAN complex

Database of interacting proteins

More...
DIPi
DIP-2466N

Protein interaction database and analysis system

More...
IntActi
P53010, 6 interactors

Molecular INTeraction database

More...
MINTi
P53010

STRING: functional protein association networks

More...
STRINGi
4932.YGL094C

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11115
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P53010

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P53010

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati27 – 66WD 1UniRule annotationAdd BLAST40
Repeati112 – 153WD 2UniRule annotationAdd BLAST42
Repeati155 – 194WD 3UniRule annotationAdd BLAST40
Repeati197 – 236WD 4UniRule annotationAdd BLAST40
Repeati295 – 334WD 5UniRule annotationAdd BLAST40
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini474 – 855USPUniRule annotation1 PublicationAdd BLAST382
Domaini907 – 1079ExonucleaseUniRule annotationAdd BLAST173

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni337 – 473LinkerUniRule annotation1 PublicationAdd BLAST137

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Contains a pseudo-UCH domain. This ubiquitin C-terminal hydrolase (UCH)-like or ubiquitin specific protease (USP)-like domain is predicted to be catalytically inactive because it lacks the active site catalytic triad characteristic of thiol proteases, with residues at the equivalent structural positions that are incompatible with catalysis, and it cannot bind ubiquitin. It functions as a structural scaffold for intra- and intermolecular interactions in the complex.UniRule annotation1 Publication
The linker, or PAN3 interaction domain (PID), between the WD40 repeats and the pseudo-UCH domain mediates interaction with PAN3.UniRule annotation1 Publication

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase C19 family. PAN2 subfamily.UniRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000013978

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000230585

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P53010

KEGG Orthology (KO)

More...
KOi
K12571

Identification of Orthologs from Complete Genome Data

More...
OMAi
EEPHLYM

Database of Orthologous Groups

More...
OrthoDBi
EOG092C0KHR

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.130.10.10, 1 hit
3.30.420.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_03182 PAN2, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013520 Exonuclease_RNaseT/DNA_pol3
IPR030843 PAN2
IPR028881 PAN2_dom
IPR038765 Papain_like_cys_pep_sf
IPR011047 Quinoprotein_ADH-like_supfam
IPR012337 RNaseH-like_sf
IPR036397 RNaseH_sf
IPR028889 USP_dom
IPR015943 WD40/YVTN_repeat-like_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00929 RNase_T, 1 hit
PF13423 UCH_1, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00479 EXOIII, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50998 SSF50998, 1 hit
SSF53098 SSF53098, 1 hit
SSF54001 SSF54001, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50235 USP_3, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P53010-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNNWQHFFNN PVDLSEHLKK PYFRFDNRDK EITAISFDEK ANLIWSGDSY
60 70 80 90 100
GCISSYDPTF QLYTRYRGHI GGNSVKDILS HRDGILSISE DSLHFANRRG
110 120 130 140 150
VTKLNLTSID IAAFSELNTM CYSPHSLKNN IYCGGDNTNW GIASIDLNRG
160 170 180 190 200
CLDSLLNYSS KVKLMCSNNK VLSIGRQTGT VDLLDPTSNR TIKSFNAHSA
210 220 230 240 250
SISAMDLRDN TLVTVGKSKR FYNLYADPFV NVYDLRTMRQ LPPVSFSKGT
260 270 280 290 300
TMGSGGADFV QLHPLLPTVM IVASSSGSFD FIDLSNPTLR TQYVHPCQSI
310 320 330 340 350
KKLCLSPNGD VLGILEADNH LDTWRRSSNN MGMFTNTPEM LAYPDYFNDI
360 370 380 390 400
TSDGPISVDD ETYPLSSVGM PYYLDKLLSA WPPVVFKSEG TIPQLTGKSP
410 420 430 440 450
LPSSGKLKSN LAVISSQNEK LSTQEFPLLR YDRTKYGMRN AIPDYVCLRD
460 470 480 490 500
IRKQITSGLE TSDIQTYTSI NKYEVPPAYS RLPLTSGRFG TDNFDFTPFN
510 520 530 540 550
NTEYSGLDPD VDNHYTNAII QLYRFIPEMF NFVVGCLKDE NFETTLLTDL
560 570 580 590 600
GYLFDMMERS HGKICSSSNF QASLKSLTDK RQLENGEPQE HLEEYLESLC
610 620 630 640 650
IRESIEDFNS SESIKRNMPQ KFNRFLLSQL IKEEAQTVNH NITLNQCFGL
660 670 680 690 700
ETEIRTECSC DHYDTTVKLL PSLSISGINK TVIKQLNKKS NGQNILPYIE
710 720 730 740 750
YAMKNVTQKN SICPTCGKTE TITQECTVKN LPSVLSLELS LLDTEFSNIR
760 770 780 790 800
SSKNWLTSEF YGSIIKNKAV LRSTASELKG TSHIFKYELN GYVAKITDNN
810 820 830 840 850
NETRLVTYVK KYNPKENCFK WLMFNDYLVV EITEEEALKM TYPWKTPEII
860 870 880 890 900
IYCDAEELRK PFFSVDTYSI NYDILFRDYF ANGIRDTARR EYKLLTHDEA
910 920 930 940 950
PKSGTLVAID AEFVSLQSEL CEIDHQGIRS IIRPKRTALA RISIIRGEEG
960 970 980 990 1000
ELYGVPFVDD YVVNTNHIED YLTRYSGILP GDLDPEKSTK RLVRRNVVYR
1010 1020 1030 1040 1050
KVWLLMQLGC VFVGHGLNND FKHININVPR NQIRDTAIYF LQGKRYLSLR
1060 1070 1080 1090 1100
YLAYVLLGMN IQEGNHDSIE DAHTALILYK KYLHLKEKAI FEKVLNSVYE
1110
EGRAHNFKVP ETSKG
Length:1,115
Mass (Da):127,039
Last modified:October 1, 1996 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4F91B737F761AE5A
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U39204 Genomic DNA Translation: AAC49152.1
Z72616 Genomic DNA Translation: CAA96800.1
BK006941 Genomic DNA Translation: DAA08012.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S64101

NCBI Reference Sequences

More...
RefSeqi
NP_011421.1, NM_001180959.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YGL094C_mRNA; YGL094C_mRNA; YGL094C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
852786

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YGL094C

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39204 Genomic DNA Translation: AAC49152.1
Z72616 Genomic DNA Translation: CAA96800.1
BK006941 Genomic DNA Translation: DAA08012.1
PIRiS64101
RefSeqiNP_011421.1, NM_001180959.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4Q8GX-ray2.10A/B416-870[»]
4Q8HX-ray3.10A460-1115[»]
4XR7X-ray3.80A/D/G/J340-1115[»]
ProteinModelPortaliP53010
SMRiP53010
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33157, 128 interactors
ComplexPortaliCPX-3294 PAN complex
DIPiDIP-2466N
IntActiP53010, 6 interactors
MINTiP53010
STRINGi4932.YGL094C

PTM databases

iPTMnetiP53010

Proteomic databases

MaxQBiP53010
PaxDbiP53010
PRIDEiP53010

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL094C_mRNA; YGL094C_mRNA; YGL094C
GeneIDi852786
KEGGisce:YGL094C

Organism-specific databases

SGDiS000003062 PAN2

Phylogenomic databases

GeneTreeiENSGT00390000013978
HOGENOMiHOG000230585
InParanoidiP53010
KOiK12571
OMAiEEPHLYM
OrthoDBiEOG092C0KHR

Enzyme and pathway databases

BioCyciYEAST:G3O-30594-MONOMER

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P53010

Family and domain databases

Gene3Di2.130.10.10, 1 hit
3.30.420.10, 1 hit
HAMAPiMF_03182 PAN2, 1 hit
InterProiView protein in InterPro
IPR013520 Exonuclease_RNaseT/DNA_pol3
IPR030843 PAN2
IPR028881 PAN2_dom
IPR038765 Papain_like_cys_pep_sf
IPR011047 Quinoprotein_ADH-like_supfam
IPR012337 RNaseH-like_sf
IPR036397 RNaseH_sf
IPR028889 USP_dom
IPR015943 WD40/YVTN_repeat-like_dom_sf
PfamiView protein in Pfam
PF00929 RNase_T, 1 hit
PF13423 UCH_1, 1 hit
SMARTiView protein in SMART
SM00479 EXOIII, 1 hit
SUPFAMiSSF50998 SSF50998, 1 hit
SSF53098 SSF53098, 1 hit
SSF54001 SSF54001, 1 hit
PROSITEiView protein in PROSITE
PS50235 USP_3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPAN2_YEAST
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P53010
Secondary accession number(s): D6VU51
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: December 5, 2018
This is version 172 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

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