PMS1/YNL082W Protein Information Help

Standard Name Pms1p 1
Systematic Name Ynl082wp
ORF Classification Verified
Description ATP-binding protein required for mismatch repair; required for both mitosis and meiosis; functions as a heterodimer with Mlh1p; binds double- and single-stranded DNA via its N-terminal domain, similar to E. coli MutL (1, 2, 3)
Name Description PostMeiotic Segregation 1
Experimental Data
Molecules/cell 521 4
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 873
Molecular Weight (Da) 99,354
Isoelectric Point (pI) 6.25

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Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Pms1p (InterPro)
Physical Interactions There are 33 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI00003596AF | P14242
MIPS: YNL082W
NCBI: 110282983 | 1301977 | 1346737 | 172203 | 19880869 | 19880883 | 19880897 | 19880904 | 19880918 | 19880925 | 2253174 | 290560158 | 398364981 | 451928628 | 451928668 | 71064118 | 791102 | 86161598 | 86161600 | 86161602 | 86161604 | 86161606 | 887629 | NP_014317.4 | NM_001182920.3
GenBank/EMBL/DDBJ: AAA34885.1 | AAM00521.1 | AAM00533.1 | AAM00545.1 | AAM00551.1 | AAM00563.1 | AAM00569.1 | AAZ22526.1 | ABC86932.1 | ABC86933.1 | ABC86934.1 | ABC86935.1 | ABC86936.1 | CAA60176.1 | CAA61428.1 | CAA95956.1 | CAA95957.1 | DAA10463.1 | AF458969 | AF458971 | AF458973 | AF458974 | AF458976 | AF458977 | DQ115393 | DQ356628 | DQ356629 | DQ356630 | DQ356631 | DQ356632 | M29688 | X86470 | X89016 | Z71357 | Z71358
Amino Acid Sequence (or in FASTA format)
       1  MTQIHQINDI DVHRITSGQV ITDLTTAVKE LVDNSIDANA NQIEIIFKDY
      51  GLESIECSDN GDGIDPSNYE FLALKHYTSK IAKFQDVAKV QTLGFRGEAL
     101  SSLCGIAKLS VITTTSPPKA DKLEYDMVGH ITSKTTTSRN KGTTVLVSQL
     151  FHNLPVRQKE FSKTFKRQFT KCLTVIQGYA IINAAIKFSV WNITPKGKKN
     201  LILSTMRNSS MRKNISSVFG AGGMRGLEEV DLVLDLNPFK NRMLGKYTDD
     251  PDFLDLDYKI RVKGYISQNS FGCGRNSKDR QFIYVNKRPV EYSTLLKCCN
     301  EVYKTFNNVQ FPAVFLNLEL PMSLIDVNVT PDKRVILLHN ERAVIDIFKT
     351  TLSDYYNRQE LALPKRMCSQ SEQQAQKRLK TEVFDDRSTT HESDNENYHT
     401  ARSESNQSNH AHFNSTTGVI DKSNGTELTS VMDGNYTNVT DVIGSECEVS
     451  VDSSVVLDEG NSSTPTKKLP SIKTDSQNLS DLNLNNFSNP EFQNITSPDK
     501  ARSLEKVVEE PVYFDIDGEK FQEKAVLSQA DGLVFVDNEC HEHTNDCCHQ
     551  ERRGSTDTEQ DDEADSIYAE IEPVEINVRT PLKNSRKSIS KDNYRSLSDG
     601  LTHRKFEDEI LEYNLSTKNF KEISKNGKQM SSIISKRKSE AQENIIKNKD
     651  ELEDFEQGEK YLTLTVSKND FKKMEVVGQF NLGFIIVTRK VDNKYDLFIV
     701  DQHASDEKYN FETLQAVTVF KSQKLIIPQP VELSVIDELV VLDNLPVFEK
     751  NGFKLKIDEE EEFGSRVKLL SLPTSKQTLF DLGDFNELIH LIKEDGGLRR
     801  DNIRCSKIRS MFAMRACRSS IMIGKPLNKK TMTRVVHNLS ELDKPWNCPH
     851  GRPTMRHLME LRDWSSFSKD YEI*                            

external links for Pms1p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily LoQate
Ashbya (AGD) BOND GPMdb (Mass Spec.) YPL+
Aspergillus (AspGD) CYC2008 (complexes) MIPS YeastGFP
Candida (CGD) Complexome Pfam domains
YGOB DIP YeastRC Structure Prediction (Seattle)
YOGY GeneMANIA


IMP

References cited on this page View Complete Literature Guide for Pms1p
1) Williamson MS, et al.  (1985) Meiotic gene conversion mutants in Saccharomyces cerevisiae. I. Isolation and characterization of pms1-1 and pms1-2. Genetics 110(4):609-46
2) Hall MC, et al.  (2002) Differential ATP binding and intrinsic ATP hydrolysis by amino-terminal domains of the yeast Mlh1 and Pms1 proteins. J Biol Chem 277(5):3673-9
3) Hall MC, et al.  (2003) DNA binding by yeast Mlh1 and Pms1: implications for DNA mismatch repair. Nucleic Acids Res 31(8):2025-34
4) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41