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Protein

DNA polymerase alpha catalytic subunit A

Gene

POL1

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 component of DNA polymerase alpha, which in complex with DNA primase (DNA polymerase alpha:primase) constitutes a replicative polymerase. POL1 has a role in promoting telomere replication during interaction with CDC13.1 Publication

Miscellaneous

In eukaryotes there are five DNA polymerases: alpha, beta, gamma, delta, and epsilon which are responsible for different reactions of DNA synthesis.
Present with 1050 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

[4Fe-4S] cluster1 PublicationNote: Binds 1 [4Fe-4S] cluster.1 Publication

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 bindingi1287ZincBy similarity1
Metal bindingi1290ZincBy similarity1
Metal bindingi1314ZincBy similarity1
Metal bindingi1317ZincBy similarity1
Metal bindingi1348Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi1353Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi1367Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi1372Iron-sulfur (4Fe-4S)By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri1287 – 1317CysA-typeAdd BLAST31

<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

<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 functionDNA-binding, DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase
Biological processDNA replication
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-33130-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.7.7 984

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-113501 Inhibition of replication initiation of damaged DNA by RB1/E2F1
R-SCE-174411 Polymerase switching on the C-strand of the telomere
R-SCE-174430 Telomere C-strand synthesis initiation
R-SCE-68952 DNA replication initiation
R-SCE-68962 Activation of the pre-replicative complex
R-SCE-69091 Polymerase switching
R-SCE-69166 Removal of the Flap Intermediate
R-SCE-69183 Processive synthesis on the lagging strand

<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:
DNA polymerase alpha catalytic subunit A (EC:2.7.7.7)
Alternative name(s):
DNA polymerase I subunit A
DNA polymerase alpha:primase complex p180 subunit
Short name:
DNA polymerase-primase complex p180 subunit
Short name:
Pol alpha-primase complex p180 subunit
<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:POL1
Synonyms:CDC17
Ordered Locus Names:YNL102W
ORF Names:N2181
<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 XIV

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000005046 POL1

<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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

<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>Mutagenesisi236D → N: Increase in length of X' and Y' telomeres. No effect on telomere position effect. Reduced interaction with CDC13. 1 Publication1
Mutagenesisi238E → K: Increase in length of X' and Y' telomeres. Reduced interaction with CDC13. 1 Publication1
Mutagenesisi241P → T: Increase in length of X' and Y' telomeres. Reduced interaction with CDC13. 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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<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_00000464402 – 1468DNA polymerase alpha catalytic subunit AAdd BLAST1467

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserineCombined sources1
Modified residuei31PhosphoserineCombined sources1
Modified residuei82PhosphoserineCombined sources1
Modified residuei83PhosphoserineCombined sources1
Modified residuei84PhosphoserineCombined sources1
Modified residuei169PhosphoserineCombined sources1
Modified residuei170PhosphoserineCombined sources1
Modified residuei172PhosphothreonineCombined sources1
Modified residuei240PhosphoserineCombined sources1
Modified residuei274PhosphoserineCombined sources1
Modified residuei309PhosphothreonineCombined sources1
Modified residuei313PhosphothreonineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P13382

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

More...
PaxDbi
P13382

PRoteomics IDEntifications database

More...
PRIDEi
P13382

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P13382

<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

DNA polymerase alpha:primase is a four subunit enzyme complex, which is assembled throughout the cell cycle, and consists of the two DNA polymerase subunits A and B, and the DNA primase large and small subunits. Subunit B binds to subunit A (By similarity). POL1 interacts with CDC13, POB3, SPT16 and MCM10.By similarity4 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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
35721, 703 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-2091 DNA polymerase alpha:primase complex

Database of interacting proteins

More...
DIPi
DIP-2526N

Protein interaction database and analysis system

More...
IntActi
P13382, 16 interactors

Molecular INTeraction database

More...
MINTi
P13382

STRING: functional protein association networks

More...
STRINGi
4932.YNL102W

<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

11468
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
P13382

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

More...
SMRi
P13382

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P13382

<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

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>Regioni1246 – 1381DNA-binding regionSequence analysisAdd BLAST136

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi1348 – 1372CysB motifAdd BLAST25

<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

The CysB motif binds 1 4Fe-4S cluster and is required for the formation of polymerase complexes.By similarity

<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 DNA polymerase type-B family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1287 – 1317CysA-typeAdd BLAST31

Keywords - Domaini

Zinc-finger

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00550000074891

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000163524

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P13382

KEGG Orthology (KO)

More...
KOi
K02320

Identification of Orthologs from Complete Genome Data

More...
OMAi
FPYDFKE

Database of Orthologous Groups

More...
OrthoDBi
EOG092C038B

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.3200.20, 1 hit
3.30.420.10, 1 hit
3.90.1600.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006172 DNA-dir_DNA_pol_B
IPR017964 DNA-dir_DNA_pol_B_CS
IPR006133 DNA-dir_DNA_pol_B_exonuc
IPR006134 DNA-dir_DNA_pol_B_multi_dom
IPR024647 DNA_pol_a_cat_su_N
IPR023211 DNA_pol_palm_dom_sf
IPR038256 Pol_alpha_znc_sf
IPR012337 RNaseH-like_sf
IPR036397 RNaseH_sf
IPR015088 Znf_DNA-dir_DNA_pol_B_alpha

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF12254 DNA_pol_alpha_N, 1 hit
PF00136 DNA_pol_B, 1 hit
PF03104 DNA_pol_B_exo1, 1 hit
PF08996 zf-DNA_Pol, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00106 DNAPOLB

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00486 POLBc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53098 SSF53098, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00116 DNA_POLYMERASE_B, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P13382-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSSKSEKLEK LRKLQAARNG TSIDDYEGDE SDGDRIYDEI DEKEYRARKR
60 70 80 90 100
QELLHDDFVV DDDGVGYVDR GVEEDWREVD NSSSDEDTGN LASKDSKRKK
110 120 130 140 150
NIKREKDHQI TDMLRTQHSK STLLAHAKKS QKKSIPIDNF DDILGEFESG
160 170 180 190 200
EVEKPNILLP SKLRENLNSS PTSEFKSSIK RVNGNDESSH DAGISKKVKI
210 220 230 240 250
DPDSSTDKYL EIESSPLKLQ SRKLRYANDV QDLLDDVENS PVVATKRQNV
260 270 280 290 300
LQDTLLANPP SAQSLADEED DEDSDEDIIL KRRTMRSVTT TRRVNIDSRS
310 320 330 340 350
NPSTSPFVTA PGTPIGIKGL TPSKSLQSNT DVATLAVNVK KEDVVDPETD
360 370 380 390 400
TFQMFWLDYC EVNNTLILFG KVKLKDDNCV SAMVQINGLC RELFFLPREG
410 420 430 440 450
KTPTDIHEEI IPLLMDKYGL DNIRAKPQKM KYSFELPDIP SESDYLKVLL
460 470 480 490 500
PYQTPKSSRD TIPSDLSSDT FYHVFGGNSN IFESFVIQNR IMGPCWLDIK
510 520 530 540 550
GADFNSIRNA SHCAVEVSVD KPQNITPTTT KTMPNLRCLS LSIQTLMNPK
560 570 580 590 600
ENKQEIVSIT LSAYRNISLD SPIPENIKPD DLCTLVRPPQ STSFPLGLAA
610 620 630 640 650
LAKQKLPGRV RLFNNEKAML SCFCAMLKVE DPDVIIGHRL QNVYLDVLAH
660 670 680 690 700
RMHDLNIPTF SSIGRRLRRT WPEKFGRGNS NMNHFFISDI CSGRLICDIA
710 720 730 740 750
NEMGQSLTPK CQSWDLSEMY QVTCEKEHKP LDIDYQNPQY QNDVNSMTMA
760 770 780 790 800
LQENITNCMI SAEVSYRIQL LTLTKQLTNL AGNAWAQTLG GTRAGRNEYI
810 820 830 840 850
LLHEFSRNGF IVPDKEGNRS RAQKQRQNEE NADAPVNSKK AKYQGGLVFE
860 870 880 890 900
PEKGLHKNYV LVMDFNSLYP SIIQEFNICF TTVDRNKEDI DELPSVPPSE
910 920 930 940 950
VDQGVLPRLL ANLVDRRREV KKVMKTETDP HKRVQCDIRQ QALKLTANSM
960 970 980 990 1000
YGCLGYVNSR FYAKPLAMLV TNKGREILMN TRQLAESMNL LVVYGDTDSV
1010 1020 1030 1040 1050
MIDTGCDNYA DAIKIGLGFK RLVNERYRLL EIDIDNVFKK LLLHAKKKYA
1060 1070 1080 1090 1100
ALTVNLDKNG NGTTVLEVKG LDMKRREFCP LSRDVSIHVL NTILSDKDPE
1110 1120 1130 1140 1150
EALQEVYDYL EDIRIKVETN NIRIDKYKIN MKLSKDPKAY PGGKNMPAVQ
1160 1170 1180 1190 1200
VALRMRKAGR VVKAGSVITF VITKQDEIDN AADTPALSVA ERAHALNEVM
1210 1220 1230 1240 1250
IKSNNLIPDP QYYLEKQIFA PVERLLERID SFNVVRLSEA LGLDSKKYFR
1260 1270 1280 1290 1300
REGGNNNGED INNLQPLETT ITDVERFKDT VTLELSCPSC DKRFPFGGIV
1310 1320 1330 1340 1350
SSNYYRVSYN GLQCKHCEQL FTPLQLTSQI EHSIRAHISL YYAGWLQCDD
1360 1370 1380 1390 1400
STCGIVTRQV SVFGKRCLND GCTGVMRYKY SDKQLYNQLL YFDSLFDCEK
1410 1420 1430 1440 1450
NKKQELKPIY LPDDLDYPKE QLTESSIKAL TEQNRELMET GRSVVQKYLN
1460
DCGRRYVDMT SIFDFMLN
Length:1,468
Mass (Da):166,809
Last modified:October 1, 1996 - v2
<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:i50C9032DBE95B5AE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti759 – 760MI → IV in AAA34888 (PubMed:3287376).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti493G → R in temperature sensitive mutant. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
J03268 Genomic DNA Translation: AAA34888.1
Z50161 Genomic DNA Translation: CAA90524.1
Z71378 Genomic DNA Translation: CAA95978.1
Z12126 Genomic DNA Translation: CAA78111.1
BK006947 Genomic DNA Translation: DAA10443.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S58250

NCBI Reference Sequences

More...
RefSeqi
NP_014297.3, NM_001182940.3

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YNL102W_mRNA; YNL102W_mRNA; YNL102W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
855621

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YNL102W

<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
J03268 Genomic DNA Translation: AAA34888.1
Z50161 Genomic DNA Translation: CAA90524.1
Z71378 Genomic DNA Translation: CAA95978.1
Z12126 Genomic DNA Translation: CAA78111.1
BK006947 Genomic DNA Translation: DAA10443.1
PIRiS58250
RefSeqiNP_014297.3, NM_001182940.3

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
3FLOX-ray2.50B/D/F/H1263-1468[»]
3OIQX-ray2.40B215-250[»]
4B08X-ray2.67A349-1258[»]
4C93X-ray2.69D/E137-149[»]
4FVMX-ray2.30A349-1258[»]
4FXDX-ray3.00A/B349-1258[»]
4FYDX-ray3.10A/B349-1258[»]
ProteinModelPortaliP13382
SMRiP13382
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35721, 703 interactors
ComplexPortaliCPX-2091 DNA polymerase alpha:primase complex
DIPiDIP-2526N
IntActiP13382, 16 interactors
MINTiP13382
STRINGi4932.YNL102W

PTM databases

iPTMnetiP13382

Proteomic databases

MaxQBiP13382
PaxDbiP13382
PRIDEiP13382

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL102W_mRNA; YNL102W_mRNA; YNL102W
GeneIDi855621
KEGGisce:YNL102W

Organism-specific databases

SGDiS000005046 POL1

Phylogenomic databases

GeneTreeiENSGT00550000074891
HOGENOMiHOG000163524
InParanoidiP13382
KOiK02320
OMAiFPYDFKE
OrthoDBiEOG092C038B

Enzyme and pathway databases

BioCyciYEAST:G3O-33130-MONOMER
BRENDAi2.7.7.7 984
ReactomeiR-SCE-113501 Inhibition of replication initiation of damaged DNA by RB1/E2F1
R-SCE-174411 Polymerase switching on the C-strand of the telomere
R-SCE-174430 Telomere C-strand synthesis initiation
R-SCE-68952 DNA replication initiation
R-SCE-68962 Activation of the pre-replicative complex
R-SCE-69091 Polymerase switching
R-SCE-69166 Removal of the Flap Intermediate
R-SCE-69183 Processive synthesis on the lagging strand

Miscellaneous databases

EvolutionaryTraceiP13382

Protein Ontology

More...
PROi
PR:P13382

Family and domain databases

Gene3Di1.10.3200.20, 1 hit
3.30.420.10, 1 hit
3.90.1600.10, 1 hit
InterProiView protein in InterPro
IPR006172 DNA-dir_DNA_pol_B
IPR017964 DNA-dir_DNA_pol_B_CS
IPR006133 DNA-dir_DNA_pol_B_exonuc
IPR006134 DNA-dir_DNA_pol_B_multi_dom
IPR024647 DNA_pol_a_cat_su_N
IPR023211 DNA_pol_palm_dom_sf
IPR038256 Pol_alpha_znc_sf
IPR012337 RNaseH-like_sf
IPR036397 RNaseH_sf
IPR015088 Znf_DNA-dir_DNA_pol_B_alpha
PfamiView protein in Pfam
PF12254 DNA_pol_alpha_N, 1 hit
PF00136 DNA_pol_B, 1 hit
PF03104 DNA_pol_B_exo1, 1 hit
PF08996 zf-DNA_Pol, 1 hit
PRINTSiPR00106 DNAPOLB
SMARTiView protein in SMART
SM00486 POLBc, 1 hit
SUPFAMiSSF53098 SSF53098, 1 hit
PROSITEiView protein in PROSITE
PS00116 DNA_POLYMERASE_B, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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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 nameiDPOA_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: P13382
Secondary accession number(s): D6W177
<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: January 1, 1990
Last sequence update: October 1, 1996
Last modified: December 5, 2018
This is version 191 of the entry and version 2 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, Reference proteome

Documents

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