ECM16/YMR128W Protein Information Help

Standard Name Ecm16p 1
Systematic Name Ymr128wp
Alias Dhr1p
ORF Classification Verified
Description Essential DEAH-box ATP-dependent RNA helicase specific to the U3 snoRNP, predominantly nucleolar in distribution, required for 18S rRNA synthesis (2, 3, 4)
Name Description ExtraCellular Mutant 1
Experimental Data
Molecules/cell 2000 5
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 1,267
Molecular Weight (Da) 144,953
Isoelectric Point (pI) 6.28

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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 Ecm16p (InterPro)
Physical Interactions There are 114 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI0000052F3B | Q04217
MIPS: YMR128W
NCBI: 2500542 | 6323776 | 728667 | NP_013847.1
GenBank/EMBL/DDBJ: DAA10025.1 | Z48622
External Classifications EC: 3.6.1.- [Hydrolases acting on acid anhydrides in phosphorous-containing anhydrides]
Amino Acid Sequence (or in FASTA format)
       1  MGTYRKRFNE KARSGHMAKL KELKRIRNKQ FTRQDENDER VENPDSAPAE
      51  SSTTEPNANA EILEPLTEEE KKMKKRKLQE LFTPKESKVS RLKKKRLDKF
     101  IEHQLKREER KTIIGKLQDY KIDTSLLTSS KRLGEGRQTK KEEFKEALSL
     151  ERQGRGNEQT NEILYEEYEP KVWDEYGEGG SSEDDDGEDD FEASFGSMPK
     201  PTDNEEKKSS GFIDHRPAKF GGSGLSFGFS NIKVINKESK TPKKKYNWRQ
     251  RVEMEELKKH GKEDEMDFDT TSEDDDEEED QEEEDKMHPS ENPLEEVESA
     301  DSETGSEKFD QNDVANEFKD WANQEIKKLE GRDQELVTPT LNIDYKPIIR
     351  KEDLDDGLQE AYVPINENST RKAFYVEVSR SDEIQKARIQ LPVFGEEHKI
     401  MEAIHHNDVV IICGETGSGK TTQVPQFLYE AGFGAEDSPD YPGMVGITQP
     451  RRVAAVSMAE RVANELGDHG HKVGYQIRFD STAKEDTKVK FMTDGVLLRE
     501  MMHDFKLTKY SSIIIDEAHE RNINTDILIG MLSRCVRLRA KLHKENPIEH
     551  KKLKLIIMSA TLRVSDFSEN KTLFPIAPPV LQVDARQFPV SIHFNRRTAF
     601  NYTDEAFRKT CKIHQKLPPG AILVFLTGQQ EITHMVKRLR KEFPFKKNSK
     651  YNKDLETPVS KMGINSKTTD LEAEDIDFSV QVIDQDKFKS AIRYEEDEGN
     701  SGNGEDEEDE EEEGFEEVLT EGQTANDPLY VLPLYSLLPT KEQMRVFQKP
     751  PQGSRLCIVA TNVAETSLTI PGVRYVVDSG RSKERKYNES NGVQSFEVGW
     801  VSKASANQRS GRAGRTGPGH CYRLYSSAVF EHDFEQFSKP EILRMPVESI
     851  VLQMKSMAIH NIINFPFPTP PDRVALSKAI QLLQYLGALD NKEMITEDGK
     901  KMSLFPLSPR FSKMLLVSDE KACLPYIVAI VSALSVGDPF INEFELGINE
     951  ISRKPNPDEN LDDKIREHDE STPGMDPELK KELRSKFYKS RSQFSKLDKF
    1001  SDVFRLLSVV SAMDYVPKEQ KEIFMKKNFL RGKLMEEIVK LRKQLMYIIK
    1051  SNTSKENIAV VIRNEDLKSD IPSVIQIKLL KQMICAGFVD HVAVRADVLF
    1101  PDDAKITNRT SIINIPYIPV LATRTPNIED CFVYIHPTSI LNNLGEMPPK
    1151  YMLYYSLHLG GNNKTRMNTL CDIASTPLAN IARKGLLLTY SKPLTGQGLK
    1201  TVNLSPTERY CYVVPRFGST VDNDLKIGWD LNPIAVHQKK QKGQWTVIKF
    1251  ITRKGFQTIT GEEKEKK*                                   

external links for Ecm16p
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
YGOB CYC2008 (complexes) Pfam domains YeastRC Public Image Repository
YOGY Complexome YeastRC Structure Prediction (Seattle)

DIP


GeneMANIA

References cited on this page View Complete Literature Guide for Ecm16p
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) Shiratori A, et al.  (1999) Systematic identification, classification, and characterization of the open reading frames which encode novel helicase-related proteins in Saccharomyces cerevisiae by gene disruption and Northern analysis. Yeast 15(3):219-53
3) Colley A, et al.  (2000) Dhr1p, a putative DEAH-box RNA helicase, is associated with the box C+D snoRNP U3. Mol Cell Biol 20(19):7238-46
4) Dragon F, et al.  (2002) A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA biogenesis. Nature 417(6892):967-70
5) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41