SUB2/YDL084W Protein Information

Standard Name	Sub2p
Systematic Name	Ydl084wp
ORF Classification	Verified
Description	Component of the TREX complex required for nuclear mRNA export; member of the DEAD-box RNA helicase superfamily and is involved in early and late steps of spliceosome assembly; homolog of the human splicing factor hUAP56; relocalizes from nucleus to cytoplasm upon DNA replication stress (1, 2, 3, 4, 5)
Name Description	SUppressor of Brr1-1

Experimental Data
Molecules/cell	51700 6

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	446
Molecular Weight (Da)	50,309
Isoelectric Point (pI)	5.29

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 Sub2p (InterPro)
Physical Interactions	There are 99 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI000013617A \| Q07478 MIPS: YDL084W NCBI: 1431108 \| 2500534 \| 51013265 \| 6320119 \| NP_010199.1 GenBank/EMBL/DDBJ: DAA11775.1 \| AY692907 \| Z74132
External Classifications	EC: 3.6.1.- [Hydrolases acting on acid anhydrides in phosphorous-containing anhydrides]

Amino Acid Sequence (or in FASTA format)
1 MSHEGEEDLL EYSDNEQEIQ IDASKAAEAG ETGAATSATE GDNNNNTAAG 51 DKKGSYVGIH STGFKDFLLK PELSRAIIDC GFEHPSEVQQ HTIPQSIHGT 101 DVLCQAKSGL GKTAVFVLST LQQLDPVPGE VAVVVICNAR ELAYQIRNEY 151 LRFSKYMPDV KTAVFYGGTP ISKDAELLKN KDTAPHIVVA TPGRLKALVR 201 EKYIDLSHVK NFVIDECDKV LEELDMRRDV QEIFRATPRD KQVMMFSATL 251 SQEIRPICRR FLQNPLEIFV DDEAKLTLHG LQQYYIKLEE REKNRKLAQL 301 LDDLEFNQVI IFVKSTTRAN ELTKLLNASN FPAITVHGHM KQEERIARYK 351 AFKDFEKRIC VSTDVFGRGI DIERINLAIN YDLTNEADQY LHRVGRAGRF 401 GTKGLAISFV SSKEDEEVLA KIQERFDVKI AEFPEEGIDP STYLNN*

Amino Acid Sequence (or in FASTA format)

       1  MSHEGEEDLL EYSDNEQEIQ IDASKAAEAG ETGAATSATE GDNNNNTAAG
      51  DKKGSYVGIH STGFKDFLLK PELSRAIIDC GFEHPSEVQQ HTIPQSIHGT
     101  DVLCQAKSGL GKTAVFVLST LQQLDPVPGE VAVVVICNAR ELAYQIRNEY
     151  LRFSKYMPDV KTAVFYGGTP ISKDAELLKN KDTAPHIVVA TPGRLKALVR
     201  EKYIDLSHVK NFVIDECDKV LEELDMRRDV QEIFRATPRD KQVMMFSATL
     251  SQEIRPICRR FLQNPLEIFV DDEAKLTLHG LQQYYIKLEE REKNRKLAQL
     301  LDDLEFNQVI IFVKSTTRAN ELTKLLNASN FPAITVHGHM KQEERIARYK
     351  AFKDFEKRIC VSTDVFGRGI DIERINLAIN YDLTNEADQY LHRVGRAGRF
     401  GTKGLAISFV SSKEDEEVLA KIQERFDVKI AEFPEEGIDP STYLNN*

external links for Sub2p

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 Sub2p

1)	Fan HY, et al. (2001) High-copy-number expression of Sub2p, a member of the RNA helicase superfamily, suppresses hpr1-mediated genomic instability. Mol Cell Biol 21(16):5459-70
2)	Jensen TH, et al. (2001) The DECD box putative ATPase Sub2p is an early mRNA export factor. Curr Biol 11(21):1711-5
3)	Strasser K and Hurt E (2001) Splicing factor Sub2p is required for nuclear mRNA export through its interaction with Yra1p. Nature 413(6856):648-52
4)	Strasser K, et al. (2002) TREX is a conserved complex coupling transcription with messenger RNA export. Nature 417(6886):304-8
5)	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
6)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41