PEP5/YMR231W Protein Information Help

Standard Name Pep5p 1
Systematic Name Ymr231wp
Alias End1p 2 , Vam1p , Vpl9p 3 , Vps11p 3, 4 , Vpt11p 4
ORF Classification Verified
Description Histone E3 ligase, component of CORVET tethering complex; peripheral vacuolar membrane protein required for protein trafficking and vacuole biogenesis; interacts with Pep7p; involved in ubiquitylation and degradation of excess histones (5, 6, 7, 8)
Name Description carboxyPEPtidase Y-deficient 9
Experimental Data
Molecules/cell 1200 10
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 1,029
Molecular Weight (Da) 117,476
Isoelectric Point (pI) 5.67

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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 Pep5p (InterPro)
Physical Interactions There are 102 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI0000052FFA | P12868
MIPS: YMR231W
NCBI: 129788 | 3680 | 6323887 | 666102 | 887612 | NP_013958.1
GenBank/EMBL/DDBJ: DAA10131.1 | X15355 | X54466 | Z49939
Amino Acid Sequence (or in FASTA format)
       1  MSLSSWRQFQ LFENIPIRDP NFGGDSLLYS DPTLCAATIV DPQTLIIAVN
      51  SNIIKVVKLN QSQVIHEFQS FPHDFQITFL KVINGEFLVA LAESIGKPSL
     101  IRVYKLEKLP NREQLYHSQV ELKNGNNTYP ISVVSISNDL SCIVVGFING
     151  KIILIRGDIS RDRGSQQRII YEDPSKEPIT ALFLNNDATA CFAATTSRIL
     201  LFNTTGRNRG RPSLVLNSKN GLDLNCGSFN PATNEFICCL SNFIEFFSSS
     251  GKKHQFAFDL SLRKRIFCVD KDHILIVTEE TGVPTTSISV NELSPTIINR
     301  IFIIDAKNKI ISLNFVVSSA IIDIFSTSQS GKNITYLLTS EGVMHRITPK
     351  SLENQINIII QKELYPFALQ LAKQHSLSPL DVQEIHKKYG DYLFKKGLRK
     401  EATDQYIQCL DVVETSEIIS KFGVKEVPDP ESMRNLADYL WSLIKNSISQ
     451  RDHVTLLLIV LIKLKDVEGI DTFIQHFDRK GIWNEGVVMD DMDDVTFFYS
     501  DNDFFDLDLI LELMKESDFK RLSYRLAKKY SKDSLIIVDI LLNLLHNPVK
     551  AIKYIKSLPI DETLRCLVTY SKKLLEESPN ETNALLIEVF TGKFKPSTFE
     601  VDLDRRDTTG DFSENIRTVF YSYKTFFNYM NSNGTSDAMS ESSEASHEHE
     651  EPTYHPPKPS IVFSSFVTKP FEFVVFLEAC LACYQQYEGF DEDRQVILTT
     701  LYDLYLNLAQ NDVPERIDDW RSRATGVLRE SNKLVYSAAS NNTSKRVDNS
     751  IMLLISHMDQ SSASAKDKTK IDIASFANDN PEMDLLSTFR AMTLNEEPST
     801  CLKFLEKYGT EEPKLLQVAL SYFVSNKLIF KEMGGNEVLK EKVLRPIIEG
     851  ERMPLLDIIK ALSRTNVAHF GLIQDIIIDH VKTEDTEIKR NEKLIESYDK
     901  ELKEKNKKLK NTINSDQPLH VPLKNQTCFM CRLTLDIPVV FFKCGHIYHQ
     951  HCLNEEEDTL ESERKLFKCP KCLVDLETSN KLFEAQHEVV EKNDLLNFAL
    1001  NSEEGSRDRF KVITEFLGRG AISYSDITI*                      

external links for Pep5p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily YPL+
Ashbya (AGD) BOND GPMdb (Mass Spec.) YeastGFP
Aspergillus (AspGD) BioPIXIE MIPS YeastRC Public Image Repository
Candida (CGD) CYC2008 (complexes) Pfam domains
Candida (CandidaDB) Complexome YeastRC Structure Prediction (Seattle)
YGOB DIP

YOGY GeneMANIA

References cited on this page View Complete Literature Guide for Pep5p
1) Woolford, C., et al.  (1989) Personal Communication, Mortimer Map Edition 10
2) Chvatchko Y, et al.  (1986) Two yeast mutants defective in endocytosis are defective in pheromone response. Cell 46(3):355-64
3) Rothman JH, et al.  (1989) Characterization of genes required for protein sorting and vacuolar function in the yeast Saccharomyces cerevisiae. EMBO J 8(7):2057-65
4) Robinson JS, et al.  (1988) Protein sorting in Saccharomyces cerevisiae: isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases. Mol Cell Biol 8(11):4936-48
5) Srivastava A, et al.  (2000) Pep3p/Pep5p complex: a putative docking factor at multiple steps of vesicular transport to the vacuole of Saccharomyces cerevisiae. Genetics 156(1):105-22
6) Dulic V and Riezman H  (1989) Characterization of the END1 gene required for vacuole biogenesis and gluconeogenic growth of budding yeast. EMBO J 8(5):1349-59
7) Peplowska K, et al.  (2007) The CORVET Tethering Complex Interacts with the Yeast Rab5 Homolog Vps21 and Is Involved in Endo-Lysosomal Biogenesis. Dev Cell 12(5):739-50
8) Singh RK, et al.  (2012) Novel E3 Ubiquitin Ligases That Regulate Histone Protein Levels in the Budding Yeast Saccharomyces cerevisiae. PLoS One 7(5):e36295
9) Jones EW  (1977) Proteinase mutants of Saccharomyces cerevisiae. Genetics 85(1):23-33
10) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41