ECM29/YHL030W Protein Information Help

Standard Name Ecm29p 1
Systematic Name Yhl030wp
ORF Classification Verified
Description Scaffold protein; assists in association of the proteasome core particle with the regulatory particle; degraded by the mature proteasome after assembly; contains HEAT-like repeats; protein increases in abundance and relocalizes from nucleus to cytoplasm upon DNA replication stress (2, 3, 4)
Name Description ExtraCellular Mutant 1
Experimental Data
Molecules/cell 2950 5
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 1,868
Molecular Weight (Da) 210,429
Isoelectric Point (pI) 6.5

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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 Ecm29p (InterPro)
Physical Interactions There are 240 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI0000052F28 | P38737
MIPS: YHL030W
NCBI: 2289859 | 6321757 | 731610 | NP_011833.1
GenBank/EMBL/DDBJ: DAA06655.1 | U11583
Amino Acid Sequence (or in FASTA format)
       1  MSISSDEAKE KQLVEKAELR LAIADSPQKF ETNLQTFLPP LLLKLASPHA
      51  SVRTAVFSAL KNLISRINTL PQVQLPVRAL IVQAKEPNLA AQQDSTNVRL
     101  YSLLLASKGI DRLSLQDRQQ LLPLVVSNIS CLTGTVAARM FHILLKLILE
     151  WVAPQESSHE QEEFVQFLQL DNDGFSFLMR QFTRFFLLVP SKQVQVSQQP
     201  LSRGYTCPGL SLTDVAFFTY DAGVTFNKEQ LNKFKKAIFQ FVCRGMAATQ
     251  TIEQSPRMIE LMEFLCVVST DSTNLSDDAA QFMKRFPMPY ENEEFITFLQ
     301  TLYIGNTANG RPPVKAILQE KILSILNRSH FATTKAECIS LICSIGLHSS
     351  EYKLRSLTLS FIRHVAKLNY KNLNPASSSP SSTDFSTCIV SLIRNNLHAE
     401  GWPKLQLGPQ TPAFNTAILQ RQLQYETLGD ILKRDFELVS DLSYIEFLFE
     451  SLKNDLPQFR SSIQESLLSL VGHLSILPQQ SKLKLKNLLR KNLSIDEQQR
     501  EDNNDAVNSI MALKFVSIKF TNAAFPFHDP EARLFNIWGT VRTNRFDIIE
     551  ESFKGLQPFW FRVNNASINT SATVKTSDLL GSHLSETEFP PFREFLQVLI
     601  DQLDSEAASI TRKSLNNAVR FSKQCLISNA IYGKKTMVIQ DEDWSVRIDK
     651  ALELDDTVVS RVNEMVQGMN DDIFIRYLTL LSNEFTATNS KGEQIAIFPY
     701  QDPIFGSVLL TLLNFVSNNV LRRLEILVPD LYHLVIMKFQ SLSDNDLAVC
     751  ATIIGIISTA IADSTHVKRI TKIAQSQTMA ETYVASYVVP RLYLKDQTNH
     801  IESDSILNLL NILTTHLSHP GTNKDMILKL VCQVTKFGLL LQVSAQERKD
     851  FLKKVMDTIQ DKLINDVTAI QTWSYLSLYS TDLENSSLFQ EKLLETNVSK
     901  QNDFLFSVGE SLSVVAGKWS SKYLIKQIDI PNFNVEIMQQ KFPATNVTTI
     951  LDEIFSGCDS TKPSLRKASC IWLLSYIQYL GHLPEVSSKC NDIHLRFMRF
    1001  LADRDEFIQD SAARGLSLVY EIGGSDLKES MVKGLLKSFT ESTAGSASTS
    1051  ATGISGSVSE ETELFEPGVL NTGDGSISTY KDILNLASEV GDPALVYKFM
    1101  SLAKSSALWS SRKGIAFGLG AIMSKSSLEE LLLKDQQTAK KLIPKLYRYR
    1151  FDPFQAVSRS MTDIWNTLIP ESSLTISLYF NDILDELLCG MANKEWRVRE
    1201  ASTSALLQLI QSQPQEKFSE KMLKIWTMAF RTMDDIKDSV REVGTKFTTV
    1251  LAKILARSID VEKGVNPTKS KEILDNILPF LWGPHGLNSD AEEVRNFALT
    1301  TLIDLVKHSP GAIKPFTPKL IYDFITLFSS IEPQVINYLA LNAANYNIDA
    1351  NVIDTQRKNG VTNSPLFQTI EKLINNSDDC MMEEIINVVI KASRKSVGLP
    1401  SKVASSLVII ILVKRYSIEM KPYSGKLLKV CLTMFEDRNE SVNIAFAISM
    1451  GYLFKVSALD KCIKYSEKLI TKYFEPTSTE NNKKVVGTAI DSILNYAKSE
    1501  FDNVASVFMP LIFIACNDED KDLETLYNKI WTEASSSGAG TVKLYLPEIL
    1551  NVLCVNIKSN DFSIRKTCAK SVIQLCGGIN DSIPYPQIVK LFDISREALS
    1601  GRSWDGKEHI VAALVSLTEK FSQTVADNND LQESINHVMY TEVSRKSMKY
    1651  VKKILPLYAR YINVNPQEET ITFLIEKAKE MIRLLGSESD DSEGSIKQTS
    1701  DESTIKRIKP NTEITQKSSK ENIENEEYVI NLLKVSVDIC NNSKSRYPMN
    1751  LLEFIIDEIA YLFHNDRIIH TWRTQLAASE IGISIVGRFS TISSADFIQN
    1801  VGRLWDQTFP INCNKETIEN VKLQMIKFGG LIIQKIPSLQ NNIEENLRLL
    1851  NSIDSTSRIE LELKNIGL*                                  

external links for Ecm29p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily Organelle DB
Ashbya (AGD) BOND GPMdb (Mass Spec.) YPL+
Aspergillus (AspGD) BioPIXIE MIPS YeastGFP
Candida (CGD) CYC2008 (complexes) Pfam domains YeastRC Public Image Repository
Candida (CandidaDB) Complexome YeastRC Structure Prediction (Seattle)
YGOB DIP

YOGY GeneMANIA

References cited on this page View Complete Literature Guide for Ecm29p
1) Lussier M, et al.  (1997) Large scale identification of genes involved in cell surface biosynthesis and architecture in Saccharomyces cerevisiae. Genetics 147(2):435-50
2) Leggett DS, et al.  (2002) Multiple associated proteins regulate proteasome structure and function. Mol Cell 10(3):495-507
3) Lehmann A, et al.  (2010) Ecm29 fulfils quality control functions in proteasome assembly. Mol Cell 38(6):879-88
4) Tkach JM, et al.  (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
5) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41