DBP2/YNL112W Protein Information

Standard Name	Dbp2p
Systematic Name	Ynl112wp
ORF Classification	Verified
Description	ATP-dependent RNA helicase of the DEAD-box protein family; has a strong preference for dsRNA; involved mRNA decay and rRNA processing; may be involved in suppression of transcription from cryptic initiation sites (1, 2)
Name Description	Dead Box Protein

Experimental Data
Molecules/cell	33100 3

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	546
Molecular Weight (Da)	60,999
Isoelectric Point (pI)	9.34

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Dbp2p (InterPro)
Physical Interactions	There are 88 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI000004F95D \| P24783 MIPS: YNL112W NCBI: 118284 \| 1183961 \| 1302034 \| 398364809 \| 5272 \| NP_014287.3 GenBank/EMBL/DDBJ: DAA10435.1 \| M64991 \| X52649 \| Z69382 \| Z71388
External Classifications	EC: 3.6.1.- [Hydrolases acting on acid anhydrides in phosphorous-containing anhydrides]

Amino Acid Sequence (or in FASTA format)
1 MTYGGRDQQY NKTNYKSRGG DFRGGRNSDR NSYNDRPQGG NYRGGFGGRS 51 NYNQPQELIK PNWDEELPKL PTFEKNFYVE HESVRDRSDS EIAQFRKENE 101 MTISGHDIPK PITTFDEAGF PDYVLNEVKA EGFDKPTGIQ CQGWPMALSG 151 RDMVGIAATG SGKTLSYCLP GIVHINAQPL LAPGDGPIVL VLAPTRELAV 201 QIQTECSKFG HSSRIRNTCV YGGVPKSQQI RDLSRGSEIV IATPGRLIDM 251 LEIGKTNLKR VTYLVLDEAD RMLDMGFEPQ IRKIVDQIRP DRQTLMWSAT 301 WPKEVKQLAA DYLNDPIQVQ VGSLELSASH NITQIVEVVS DFEKRDRLNK 351 YLETASQDNE YKTLIFASTK RMCDDITKYL REDGWPALAI HGDKDQRERD 401 WVLQEFRNGR SPIMVATDVA ARGIDVKGIN YVINYDMPGN IEDYVHRIGR 451 TGRAGATGTA ISFFTEQNKG LGAKLISIMR EANQNIPPEL LKYDRRSYGG 501 GHPRYGGGRG GRGGYGRRGG YGGGRGGYGG NRQRDGGWGN RGRSNY*

Amino Acid Sequence (or in FASTA format)

       1  MTYGGRDQQY NKTNYKSRGG DFRGGRNSDR NSYNDRPQGG NYRGGFGGRS
      51  NYNQPQELIK PNWDEELPKL PTFEKNFYVE HESVRDRSDS EIAQFRKENE
     101  MTISGHDIPK PITTFDEAGF PDYVLNEVKA EGFDKPTGIQ CQGWPMALSG
     151  RDMVGIAATG SGKTLSYCLP GIVHINAQPL LAPGDGPIVL VLAPTRELAV
     201  QIQTECSKFG HSSRIRNTCV YGGVPKSQQI RDLSRGSEIV IATPGRLIDM
     251  LEIGKTNLKR VTYLVLDEAD RMLDMGFEPQ IRKIVDQIRP DRQTLMWSAT
     301  WPKEVKQLAA DYLNDPIQVQ VGSLELSASH NITQIVEVVS DFEKRDRLNK
     351  YLETASQDNE YKTLIFASTK RMCDDITKYL REDGWPALAI HGDKDQRERD
     401  WVLQEFRNGR SPIMVATDVA ARGIDVKGIN YVINYDMPGN IEDYVHRIGR
     451  TGRAGATGTA ISFFTEQNKG LGAKLISIMR EANQNIPPEL LKYDRRSYGG
     501  GHPRYGGGRG GRGGYGRRGG YGGGRGGYGG NRQRDGGWGN RGRSNY*

external links for Dbp2p

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

References cited on this page View Complete Literature Guide for Dbp2p

1)	Bond AT, et al. (2001) Absence of Dbp2p alters both nonsense-mediated mRNA decay and rRNA processing. Mol Cell Biol 21(21):7366-79
2)	Cloutier SC, et al. (2012) The DEAD-box RNA helicase Dbp2 connects RNA quality control with repression of aberrant transcription. J Biol Chem 287(31):26155-66
3)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41