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P14242 (PMS1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 148. 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 mismatch repair protein PMS1
Alternative name(s):
Postmeiotic segregation protein 1
Gene names
Name:PMS1
Ordered Locus Names:YNL082W
ORF Names:N2317
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length873 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for DNA mismatch repair (MMR), correcting base-base mismatches and insertion-deletion loops (IDLs) resulting from DNA replication, DNA damage or from recombination events between non-identical sequences during meiosis. Component of the MutLalpha heterodimer that forms a ternary complex with the MutS heterodimers, which initially recognize the DNA mismatches. This complex is thought to be responsible for directing the downsteam MMR events, including strand discrimination, excision, and resynthesis. Plays a major role in maintaining the genetic stability of simple sequence repeats and in the repair of heteroduplex sites present in meiotic recombination intermediates. Ref.10 Ref.11 Ref.19

Subunit structure

Heterodimer of MLH1 and PMS1, called MutLalpha, which is the major MMR MutL activity correcting base-base mismatches as well as IDLs. The heterodimer binds double strand DNA independently of a mismatch with positive cooperativity and has more than one DNA binding site. Forms a ternary complex with either the MSH2-MSH6 (MutSalpha) or the MSH2-MSH3 heterodimer (MutSbeta), which recognize and bind to mismatch DNA. Ternary complex formation is promoted by ATP binding. Ref.10

Subcellular location

Nucleus Ref.16.

Miscellaneous

Present with 521 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the DNA mismatch repair MutL/HexB family.

Biophysicochemical properties

Kinetic parameters:

KM=1.5 mM for ATP Ref.14

Sequence caution

The sequence AAA34885.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAM00521.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAM00533.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAM00545.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAM00551.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAM00563.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAM00569.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA60176.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA61428.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA95956.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA95957.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MLH1P389207EBI-13561,EBI-11003

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 873873DNA mismatch repair protein PMS1
PRO_0000245571

Regions

Region1 – 357357DNA- and ATP-binding
Region661 – 873213Interaction with MLH1

Amino acid modifications

Modified residue3931Phosphoserine Ref.20
Modified residue5661Phosphoserine Ref.21

Natural variations

Natural variant411N → S in strain: SK1 and YJM421. Ref.2 Ref.3
Natural variant1121I → T in strain: SK1 and YJM421. Ref.2 Ref.3
Natural variant3841F → V in strain: SK1, YJM320, YJM339 and YJM421. Ref.2 Ref.3
Natural variant3921E → V in strain: YJM320. Ref.2
Natural variant4001T → S in strain: SK1, YJM320, YJM339 and YJM421. Ref.2 Ref.3
Natural variant4011A → S in strain: YJM320 and YJM421. Ref.2
Natural variant4161T → TCEGT in strain: SK1, YJM320, YJM339 and YJM421.
Natural variant4581D → Y in strain: EAY1068. Ref.4
Natural variant4751D → N in strain: YJM339. Ref.2
Natural variant5131Y → F in strain: SK1. Ref.3
Natural variant5641A → V in strain: YJM320. Ref.2
Natural variant7681K → R in strain: YJM320. Ref.2
Natural variant8181R → K in strain: SK1 and YJM320; forms a non-functional heterodimer with MHL1 from strain S288c, resulting in an accumulation of mutations in spore progeny of crosses between these strains. Ref.2 Ref.3

Experimental info

Mutagenesis301E → A: Reduces ATPase activity by 62%. Displays 60-fold increase in spontaneous mutation accumulation. Ref.12 Ref.14
Mutagenesis341N → A: Reduces ATPase activity by 84%. Displays 11000-fold increase in spontaneous mutation accumulation. Ref.14
Mutagenesis951F → A: Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. Ref.9
Mutagenesis971G → A: Displays an increase in spontaneous mutation accumulation. Ref.12
Mutagenesis2971K → E: Displays a 60-fold increase in spontaneous mutation accumulation. Ref.18
Mutagenesis8511G → E: Confers a strong defect in the repair of primer strand-specific 1-bp loops during DNA replication, but not during meoitic recombination. Does not impair heterodimer formation. Ref.19
Mutagenesis8571H → R: Confers a strong defect in the repair of primer strand-specific 1-bp loops during DNA replication, but not during meoitic recombination. Does not impair heterodimer formation. Ref.19
Sequence conflict6951Y → S in AAA34885. Ref.1
Sequence conflict8611L → I in AAA34885. Ref.1

Secondary structure

....................................................................................... 873
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14242 [UniParc].

Last modified July 11, 2006. Version 3.
Checksum: 2E0FFBC59B718854

FASTA87399,355
        10         20         30         40         50         60 
MTQIHQINDI DVHRITSGQV ITDLTTAVKE LVDNSIDANA NQIEIIFKDY GLESIECSDN 

        70         80         90        100        110        120 
GDGIDPSNYE FLALKHYTSK IAKFQDVAKV QTLGFRGEAL SSLCGIAKLS VITTTSPPKA 

       130        140        150        160        170        180 
DKLEYDMVGH ITSKTTTSRN KGTTVLVSQL FHNLPVRQKE FSKTFKRQFT KCLTVIQGYA 

       190        200        210        220        230        240 
IINAAIKFSV WNITPKGKKN LILSTMRNSS MRKNISSVFG AGGMRGLEEV DLVLDLNPFK 

       250        260        270        280        290        300 
NRMLGKYTDD PDFLDLDYKI RVKGYISQNS FGCGRNSKDR QFIYVNKRPV EYSTLLKCCN 

       310        320        330        340        350        360 
EVYKTFNNVQ FPAVFLNLEL PMSLIDVNVT PDKRVILLHN ERAVIDIFKT TLSDYYNRQE 

       370        380        390        400        410        420 
LALPKRMCSQ SEQQAQKRLK TEVFDDRSTT HESDNENYHT ARSESNQSNH AHFNSTTGVI 

       430        440        450        460        470        480 
DKSNGTELTS VMDGNYTNVT DVIGSECEVS VDSSVVLDEG NSSTPTKKLP SIKTDSQNLS 

       490        500        510        520        530        540 
DLNLNNFSNP EFQNITSPDK ARSLEKVVEE PVYFDIDGEK FQEKAVLSQA DGLVFVDNEC 

       550        560        570        580        590        600 
HEHTNDCCHQ ERRGSTDTEQ DDEADSIYAE IEPVEINVRT PLKNSRKSIS KDNYRSLSDG 

       610        620        630        640        650        660 
LTHRKFEDEI LEYNLSTKNF KEISKNGKQM SSIISKRKSE AQENIIKNKD ELEDFEQGEK 

       670        680        690        700        710        720 
YLTLTVSKND FKKMEVVGQF NLGFIIVTRK VDNKYDLFIV DQHASDEKYN FETLQAVTVF 

       730        740        750        760        770        780 
KSQKLIIPQP VELSVIDELV VLDNLPVFEK NGFKLKIDEE EEFGSRVKLL SLPTSKQTLF 

       790        800        810        820        830        840 
DLGDFNELIH LIKEDGGLRR DNIRCSKIRS MFAMRACRSS IMIGKPLNKK TMTRVVHNLS 

       850        860        870 
ELDKPWNCPH GRPTMRHLME LRDWSSFSKD YEI 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and nucleotide sequence of DNA mismatch repair gene PMS1 from Saccharomyces cerevisiae: homology of PMS1 to procaryotic MutL and HexB."
Kramer W., Kramer B., Williamson M.S., Fogel S.
J. Bacteriol. 171:5339-5346(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Dissecting the architecture of a quantitative trait locus in yeast."
Steinmetz L.M., Sinha H., Richards D.R., Spiegelman J.I., Oefner P.J., McCusker J.H., Davis R.W.
Nature 416:326-330(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-41; THR-112; VAL-384; VAL-392; SER-400; SER-401; 416-THR--THR-420; ASN-475; VAL-564; ARG-768 AND LYS-818.
Strain: ATCC 200060 / W303, S96, SK1, YJM 339 and YJM 421.
[3]"Quantitative trait loci mapped to single-nucleotide resolution in yeast."
Deutschbauer A.M., Davis R.W.
Nat. Genet. 37:1333-1340(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-41; THR-112; VAL-384; SER-400; 416-THR--THR-420; PHE-513 AND LYS-818.
Strain: SK1.
[4]"Negative epistasis between natural variants of the Saccharomyces cerevisiae MLH1 and PMS1 genes results in a defect in mismatch repair."
Heck J.A., Argueso J.L., Gemici Z., Reeves R.G., Bernard A., Aquadro C.F., Alani E.
Proc. Natl. Acad. Sci. U.S.A. 103:3256-3261(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT TYR-458.
Strain: EAY1066, EAY1068, M2-8, M5-7 and M7-8.
[5]"Sequencing a cosmid clone of Saccharomyces cerevisiae chromosome XIV reveals 12 new open reading frames (ORFs) and an ancient duplication of six ORFs."
Poehlmann R., Philippsen P.
Yeast 12:391-402(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[6]"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.
[7]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[8]"The sequence of a 17,933 bp segment of Saccharomyces cerevisiae chromosome XIV contains the RHO2, TOP2, MKT1 and END3 genes and five new open reading frames."
Soler-Mira A., Saiz J.E., Ballesta J.P.G., Remacha M.A.
Yeast 12:485-491(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-225.
Strain: ATCC 96604 / S288c / FY1679.
[9]"Functional domains of the Saccharomyces cerevisiae Mlh1p and Pms1p DNA mismatch repair proteins and their relevance to human hereditary nonpolyposis colorectal cancer-associated mutations."
Pang Q., Prolla T.A., Liskay R.M.
Mol. Cell. Biol. 17:4465-4473(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MLH1, MUTAGENESIS OF PHE-95.
[10]"ATP-dependent assembly of a ternary complex consisting of a DNA mismatch and the yeast MSH2-MSH6 and MLH1-PMS1 protein complexes."
Habraken Y., Sung P., Prakash L., Prakash S.
J. Biol. Chem. 273:9837-9841(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[11]"Functional specificity of MutL homologs in yeast: evidence for three Mlh1-based heterocomplexes with distinct roles during meiosis in recombination and mismatch correction."
Wang T.-F., Kleckner N., Hunter N.
Proc. Natl. Acad. Sci. U.S.A. 96:13914-13919(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MLH1.
[12]"Functional studies on the candidate ATPase domains of Saccharomyces cerevisiae MutLalpha."
Tran P.T., Liskay R.M.
Mol. Cell. Biol. 20:6390-6398(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MLH1, ATP-BINDING, MUTAGENESIS OF GLU-30 AND GLY-97.
[13]"DNA binding properties of the yeast Msh2-Msh6 and Mlh1-Pms1 heterodimers."
Drotschmann K., Hall M.C., Shcherbakova P.V., Wang H., Erie D.A., Brownewell F.R., Kool E.T., Kunkel T.A.
Biol. Chem. 383:969-975(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING.
[14]"Differential ATP binding and intrinsic ATP hydrolysis by amino-terminal domains of the yeast Mlh1 and Pms1 proteins."
Hall M.C., Shcherbakova P.V., Kunkel T.A.
J. Biol. Chem. 277:3673-3679(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: ATP-BINDING, MUTAGENESIS OF GLU-30 AND ASN-34, BIOPHYSICOCHEMICAL PROPERTIES.
[15]"Sequencing and comparison of yeast species to identify genes and regulatory elements."
Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.
Nature 423:241-254(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
[16]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[17]"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].
[18]"DNA binding by yeast Mlh1 and Pms1: implications for DNA mismatch repair."
Hall M.C., Shcherbakova P.V., Fortune J.M., Borchers C.H., Dial J.M., Tomer K.B., Kunkel T.A.
Nucleic Acids Res. 31:2025-2034(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING, MUTAGENESIS OF LYS-297.
[19]"Novel PMS1 alleles preferentially affect the repair of primer strand loops during DNA replication."
Erdeniz N., Dudley S., Gealy R., Jinks-Robertson S., Liskay R.M.
Mol. Cell. Biol. 25:9221-9231(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLY-851 AND HIS-857.
[20]"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-393, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"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-566, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M29688 Genomic DNA. Translation: AAA34885.1. Different initiation.
AF458969 Genomic DNA. Translation: AAM00521.1. Different initiation.
AF458971 Genomic DNA. Translation: AAM00533.1. Different initiation.
AF458973 Genomic DNA. Translation: AAM00545.1. Different initiation.
AF458974 Genomic DNA. Translation: AAM00551.1. Different initiation.
AF458976 Genomic DNA. Translation: AAM00563.1. Different initiation.
AF458977 Genomic DNA. Translation: AAM00569.1. Different initiation.
DQ115393 Genomic DNA. Translation: AAZ22526.1.
DQ356628 Genomic DNA. Translation: ABC86932.1.
DQ356629 Genomic DNA. Translation: ABC86933.1.
DQ356630 Genomic DNA. Translation: ABC86934.1.
DQ356631 Genomic DNA. Translation: ABC86935.1.
DQ356632 Genomic DNA. Translation: ABC86936.1.
X86470 Genomic DNA. Translation: CAA60176.1. Different initiation.
Z71357 Genomic DNA. Translation: CAA95956.1. Different initiation.
Z71358 Genomic DNA. Translation: CAA95957.1. Different initiation.
X89016 Genomic DNA. Translation: CAA61428.1. Different initiation.
BK006947 Genomic DNA. Translation: DAA10463.1.
PIRS53896.
RefSeqNP_014317.4. NM_001182920.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3H4LX-ray2.50A/B1-365[»]
4E4WX-ray2.50B635-873[»]
4FMNX-ray2.69B635-873[»]
4FMOX-ray3.04B635-873[»]
ProteinModelPortalP14242.
SMRP14242. Positions 6-362, 651-873.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35741. 48 interactions.
DIPDIP-2416N.
IntActP14242. 5 interactions.
MINTMINT-625253.

Proteomic databases

MaxQBP14242.
PaxDbP14242.
PeptideAtlasP14242.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNL082W; YNL082W; YNL082W.
GeneID855642.
KEGGsce:YNL082W.

Organism-specific databases

CYGDYNL082w.
SGDS000005026. PMS1.

Phylogenomic databases

eggNOGCOG0323.
GeneTreeENSGT00530000063289.
KOK10858.
OMAGQFNHGF.
OrthoDBEOG72RN8H.

Enzyme and pathway databases

BioCycYEAST:G3O-33111-MONOMER.

Gene expression databases

GenevestigatorP14242.

Family and domain databases

Gene3D3.30.230.10. 1 hit.
3.30.565.10. 1 hit.
InterProIPR013507. DNA_mismatch_repair_C.
IPR014762. DNA_mismatch_repair_CS.
IPR002099. DNA_mismatch_repair_fam.
IPR003594. HATPase_ATP-bd.
IPR014790. MutL_C.
IPR028831. Pms1/Pms2/PMS2L.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view]
PANTHERPTHR10073:SF9. PTHR10073:SF9. 1 hit.
PfamPF01119. DNA_mis_repair. 1 hit.
PF02518. HATPase_c. 1 hit.
PF08676. MutL_C. 1 hit.
[Graphical view]
SMARTSM00387. HATPase_c. 1 hit.
SM00853. MutL_C. 1 hit.
[Graphical view]
SUPFAMSSF54211. SSF54211. 2 hits.
SSF55874. SSF55874. 1 hit.
TIGRFAMsTIGR00585. mutl. 1 hit.
PROSITEPS00058. DNA_MISMATCH_REPAIR_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP14242.
NextBio979872.
PROP14242.

Entry information

Entry namePMS1_YEAST
AccessionPrimary (citable) accession number: P14242
Secondary accession number(s): D6W197 expand/collapse secondary AC list , Q2I044, Q2I045, Q45TY4, Q8TG48, Q8TG50, Q8TG54, Q8TG57
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: July 11, 2006
Last modified: June 11, 2014
This is version 148 of the entry and version 3 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