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P13382 (DPOA_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 145. 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:
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
Gene names
Name:POL1
Synonyms:CDC17
Ordered Locus Names:YNL102W
ORF Names:N2181
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1468 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalytic component of DNA polymerase alpha, which in complex with DNA primase (DNA polymerase alpha:primase) consitutes a replicative polymerase. POL1 has a role in promoting telomere replication during interaction with CDC13. Ref.9

Catalytic activity

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

Cofactor

Binds 1 4Fe-4S cluster. Ref.16

Subunit structure

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. Ref.7 Ref.8 Ref.9 Ref.11

Subcellular location

Nucleus.

Domain

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

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.

Sequence similarities

Belongs to the DNA polymerase type-B family.

Contains 1 CysA-type zinc finger.

Ontologies

Keywords
   Biological processDNA replication
   Cellular componentNucleus
   DomainZinc-finger
   Ligand4Fe-4S
DNA-binding
Iron
Iron-sulfur
Metal-binding
Zinc
   Molecular functionDNA-directed DNA polymerase
Nucleotidyltransferase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from mutant phenotype PubMed 2651896. Source: SGD

DNA replication initiation

Inferred by curator PubMed 3888995. Source: SGD

DNA synthesis involved in DNA repair

Inferred from mutant phenotype PubMed 10025407PubMed 2651896. Source: SGD

RNA-dependent DNA replication

Inferred from direct assay PubMed 17429354. Source: SGD

lagging strand elongation

Inferred by curator PubMed 3888995. Source: SGD

premeiotic DNA replication

Inferred from mutant phenotype PubMed 2651896. Source: SGD

   Cellular_componentalpha DNA polymerase:primase complex

Inferred from direct assay PubMed 22593576PubMed 3888995. Source: SGD

replication fork

Inferred from direct assay PubMed 15773893. Source: SGD

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA-directed DNA polymerase activity

Inferred from direct assay PubMed 1704371PubMed 3888995PubMed 3907855. Source: SGD

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleoside binding

Inferred from electronic annotation. Source: InterPro

nucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.17
Chain2 – 14681467DNA polymerase alpha catalytic subunit A
PRO_0000046440

Regions

Zinc finger1287 – 131731CysA-type
Region1246 – 1381136DNA-binding region Potential
Motif1348 – 137225CysB motif

Sites

Metal binding12871Zinc By similarity
Metal binding12901Zinc By similarity
Metal binding13141Zinc By similarity
Metal binding13171Zinc By similarity
Metal binding13481Iron-sulfur (4Fe-4S) By similarity
Metal binding13531Iron-sulfur (4Fe-4S) By similarity
Metal binding13671Iron-sulfur (4Fe-4S) By similarity
Metal binding13721Iron-sulfur (4Fe-4S) By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.17
Modified residue311Phosphoserine Ref.14 Ref.15
Modified residue821Phosphoserine Ref.15
Modified residue831Phosphoserine Ref.15
Modified residue841Phosphoserine Ref.15
Modified residue1691Phosphoserine Ref.15
Modified residue1701Phosphoserine Ref.12 Ref.15
Modified residue1721Phosphothreonine Ref.15
Modified residue2401Phosphoserine Ref.14 Ref.15
Modified residue2741Phosphoserine Ref.14 Ref.15
Modified residue3091Phosphothreonine Ref.15
Modified residue3131Phosphothreonine Ref.12 Ref.15

Natural variations

Natural variant4931G → R in temperature sensitive mutant. Ref.1

Experimental info

Mutagenesis2361D → N: Increase in length of X' and Y' telomeres. No effect on telomere position effect. Reduced interaction with CDC13. Ref.9
Mutagenesis2381E → K: Increase in length of X' and Y' telomeres. Reduced interaction with CDC13. Ref.9
Mutagenesis2411P → T: Increase in length of X' and Y' telomeres. Reduced interaction with CDC13. Ref.9
Sequence conflict759 – 7602MI → IV in AAA34888. Ref.1

Secondary structure

.................................................................................................................................................................... 1468
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13382 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 50C9032DBE95B5AE

FASTA1,468166,809
        10         20         30         40         50         60 
MSSKSEKLEK LRKLQAARNG TSIDDYEGDE SDGDRIYDEI DEKEYRARKR QELLHDDFVV 

        70         80         90        100        110        120 
DDDGVGYVDR GVEEDWREVD NSSSDEDTGN LASKDSKRKK NIKREKDHQI TDMLRTQHSK 

       130        140        150        160        170        180 
STLLAHAKKS QKKSIPIDNF DDILGEFESG EVEKPNILLP SKLRENLNSS PTSEFKSSIK 

       190        200        210        220        230        240 
RVNGNDESSH DAGISKKVKI DPDSSTDKYL EIESSPLKLQ SRKLRYANDV QDLLDDVENS 

       250        260        270        280        290        300 
PVVATKRQNV LQDTLLANPP SAQSLADEED DEDSDEDIIL KRRTMRSVTT TRRVNIDSRS 

       310        320        330        340        350        360 
NPSTSPFVTA PGTPIGIKGL TPSKSLQSNT DVATLAVNVK KEDVVDPETD TFQMFWLDYC 

       370        380        390        400        410        420 
EVNNTLILFG KVKLKDDNCV SAMVQINGLC RELFFLPREG KTPTDIHEEI IPLLMDKYGL 

       430        440        450        460        470        480 
DNIRAKPQKM KYSFELPDIP SESDYLKVLL PYQTPKSSRD TIPSDLSSDT FYHVFGGNSN 

       490        500        510        520        530        540 
IFESFVIQNR IMGPCWLDIK GADFNSIRNA SHCAVEVSVD KPQNITPTTT KTMPNLRCLS 

       550        560        570        580        590        600 
LSIQTLMNPK ENKQEIVSIT LSAYRNISLD SPIPENIKPD DLCTLVRPPQ STSFPLGLAA 

       610        620        630        640        650        660 
LAKQKLPGRV RLFNNEKAML SCFCAMLKVE DPDVIIGHRL QNVYLDVLAH RMHDLNIPTF 

       670        680        690        700        710        720 
SSIGRRLRRT WPEKFGRGNS NMNHFFISDI CSGRLICDIA NEMGQSLTPK CQSWDLSEMY 

       730        740        750        760        770        780 
QVTCEKEHKP LDIDYQNPQY QNDVNSMTMA LQENITNCMI SAEVSYRIQL LTLTKQLTNL 

       790        800        810        820        830        840 
AGNAWAQTLG GTRAGRNEYI LLHEFSRNGF IVPDKEGNRS RAQKQRQNEE NADAPVNSKK 

       850        860        870        880        890        900 
AKYQGGLVFE PEKGLHKNYV LVMDFNSLYP SIIQEFNICF TTVDRNKEDI DELPSVPPSE 

       910        920        930        940        950        960 
VDQGVLPRLL ANLVDRRREV KKVMKTETDP HKRVQCDIRQ QALKLTANSM YGCLGYVNSR 

       970        980        990       1000       1010       1020 
FYAKPLAMLV TNKGREILMN TRQLAESMNL LVVYGDTDSV MIDTGCDNYA DAIKIGLGFK 

      1030       1040       1050       1060       1070       1080 
RLVNERYRLL EIDIDNVFKK LLLHAKKKYA ALTVNLDKNG NGTTVLEVKG LDMKRREFCP 

      1090       1100       1110       1120       1130       1140 
LSRDVSIHVL NTILSDKDPE EALQEVYDYL EDIRIKVETN NIRIDKYKIN MKLSKDPKAY 

      1150       1160       1170       1180       1190       1200 
PGGKNMPAVQ VALRMRKAGR VVKAGSVITF VITKQDEIDN AADTPALSVA ERAHALNEVM 

      1210       1220       1230       1240       1250       1260 
IKSNNLIPDP QYYLEKQIFA PVERLLERID SFNVVRLSEA LGLDSKKYFR REGGNNNGED 

      1270       1280       1290       1300       1310       1320 
INNLQPLETT ITDVERFKDT VTLELSCPSC DKRFPFGGIV SSNYYRVSYN GLQCKHCEQL 

      1330       1340       1350       1360       1370       1380 
FTPLQLTSQI EHSIRAHISL YYAGWLQCDD STCGIVTRQV SVFGKRCLND GCTGVMRYKY 

      1390       1400       1410       1420       1430       1440 
SDKQLYNQLL YFDSLFDCEK NKKQELKPIY LPDDLDYPKE QLTESSIKAL TEQNRELMET 

      1450       1460 
GRSVVQKYLN DCGRRYVDMT SIFDFMLN 

« Hide

References

« Hide 'large scale' references
[1]"DNA polymerase I gene of Saccharomyces cerevisiae: nucleotide sequence, mapping of a temperature-sensitive mutation, and protein homology with other DNA polymerases."
Pizzagalli A., Valsasnini P., Plevani P., Lucchini G.
Proc. Natl. Acad. Sci. U.S.A. 85:3772-3776(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-493.
[2]"The sequence of a 21.3 kb DNA fragment from the left arm of yeast chromosome XIV reveals LEU4, MET4, POL1, RAS2, and six new open reading frames."
Saiz J.E., Buitrago M.J., Soler A., del Rey F., Revuelta J.L.
Yeast 12:403-409(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. expand/collapse author list , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"The general amino acid control regulates MET4, which encodes a methionine-pathway-specific transcriptional activator of Saccharomyces cerevisiae."
Mountain H.A., Bystroem A.S., Korch C.
Mol. Microbiol. 7:215-228(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
Strain: ATCC 204508 / S288c.
[6]"The yeast DNA polymerase-primase complex: genes and proteins."
Plevani P., Foiani M., Muzi Falconi M., Pizzagalli A., Santocanale C., Francesconi S., Valsasnini P., Comedini A., Piatti S., Lucchini G.
Biochim. Biophys. Acta 951:268-273(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: COMPOSITION OF THE DNA POLYMERASE ALPHA:PRIMASE COMPLEX.
[7]"Phosphorylation of the DNA polymerase alpha-primase B subunit is dependent on its association with the p180 polypeptide."
Ferrari M., Lucchini G., Plevani P., Foiani M.
J. Biol. Chem. 271:8661-8666(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, IDENTIFICATION IN THE DNA POLYMERASE ALPHA:PRIMASE COMPLEX.
[8]"The Saccharomyces cerevisiae DNA polymerase alpha catalytic subunit interacts with Cdc68/Spt16 and with Pob3, a protein similar to an HMG1-like protein."
Wittmeyer J., Formosa T.
Mol. Cell. Biol. 17:4178-4190(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH POB3 AND SPT16.
[9]"The Saccharomyces telomere-binding protein Cdc13p interacts with both the catalytic subunit of DNA polymerase alpha and the telomerase-associated est1 protein."
Qi H., Zakian V.A.
Genes Dev. 14:1777-1788(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CDC13, MUTAGENESIS OF ASP-236; GLU-238 AND PRO-241.
[10]"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].
[11]"A conserved Hsp10-like domain in Mcm10 is required to stabilize the catalytic subunit of DNA polymerase-alpha in budding yeast."
Ricke R.M., Bielinsky A.-K.
J. Biol. Chem. 281:18414-18425(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MCM10.
[12]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170 AND THR-313, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[13]"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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 SER-31; SER-240 AND SER-274, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-82; SER-83; SER-84; SER-169; SER-170; THR-172; SER-240; SER-274; THR-309 AND THR-313, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Eukaryotic DNA polymerases require an iron-sulfur cluster for the formation of active complexes."
Netz D.J., Stith C.M., Stumpfig M., Kopf G., Vogel D., Genau H.M., Stodola J.L., Lill R., Burgers P.M., Pierik A.J.
Nat. Chem. Biol. 8:125-132(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: COFACTOR, IRON-SULFUR-BINDING.
[17]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS58250.
RefSeqNP_014297.3. NM_001182940.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3FLOX-ray2.50B/D/F/H1263-1468[»]
3OIQX-ray2.40B215-250[»]
4B08X-ray2.67A349-1258[»]
4FVMX-ray2.30A349-1258[»]
4FXDX-ray3.00A/B349-1258[»]
4FYDX-ray3.10A/B349-1258[»]
ProteinModelPortalP13382.
SMRP13382. Positions 216-245, 351-1242, 1273-1452.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35721. 77 interactions.
DIPDIP-2526N.
IntActP13382. 14 interactions.
MINTMINT-421899.
STRING4932.YNL102W.

Proteomic databases

PaxDbP13382.
PeptideAtlasP13382.
PRIDEP13382.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNL102W; YNL102W; YNL102W.
GeneID855621.
KEGGsce:YNL102W.

Organism-specific databases

CYGDYNL102w.
SGDS000005046. POL1.

Phylogenomic databases

eggNOGCOG0417.
GeneTreeENSGT00550000074891.
HOGENOMHOG000163524.
KOK02320.
OMAEKYRDCE.
OrthoDBEOG7380D8.

Enzyme and pathway databases

BioCycYEAST:G3O-33130-MONOMER.

Gene expression databases

GenevestigatorP13382.

Family and domain databases

Gene3D3.30.420.10. 1 hit.
3.90.1600.10. 2 hits.
InterProIPR006172. 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.
IPR004578. DNA-dir_DNA_pol_B_pol2.
IPR024647. DNA_pol_a_cat_su_N.
IPR023211. DNA_pol_palm_dom.
IPR012337. RNaseH-like_dom.
IPR015088. Znf_DNA-dir_DNA_pol_B_alpha.
[Graphical view]
PfamPF12254. 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.
[Graphical view]
PRINTSPR00106. DNAPOLB.
SMARTSM00486. POLBc. 1 hit.
[Graphical view]
SUPFAMSSF53098. SSF53098. 2 hits.
TIGRFAMsTIGR00592. pol2. 1 hit.
PROSITEPS00116. DNA_POLYMERASE_B. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP13382.
NextBio979813.
PROP13382.

Entry information

Entry nameDPOA_YEAST
AccessionPrimary (citable) accession number: P13382
Secondary accession number(s): D6W177
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIV

Yeast (Saccharomyces cerevisiae) chromosome XIV: 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