RRD1/YIL153W Protein Information

Standard Name	Rrd1p 1
Systematic Name	Yil153wp
Alias	Ypa1p
ORF Classification	Verified
Description	Peptidyl-prolyl cis/trans-isomerase; activator of the phosphotyrosyl phosphatase activity of PP2A; involved in G1 phase progression, microtubule dynamics, bud morphogenesis and DNA repair; required for rapid reduction of Sgs1p levels in response to rapamycin; subunit of the Tap42p-Sit4p-Rrd1p complex; protein increases in abundance and relative distribution to the nucleus increases upon DNA replication stress (1, 10, 11, 2, 3, 4, 5, 6, 7, 8, 9)
Name Description	Resistant to Rapamycin Deletion 1

Experimental Data
Molecules/cell	4590 12

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	393
Molecular Weight (Da)	45,082
Isoelectric Point (pI)	6.83

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 Rrd1p (InterPro)
Physical Interactions	There are 30 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI000013B45A \| P40454 MIPS: YIL153W NCBI: 114794836 \| 114794837 \| 114794838 \| 114794839 \| 114794840 \| 114794841 \| 557770 \| 6322038 \| 731885 \| NP_012113.1 GenBank/EMBL/DDBJ: DAA08400.1 \| Z38059
External Classifications	EC: 5.2.1.8 [Peptidylprolyl isomerase]

Amino Acid Sequence (or in FASTA format)
1 MSLDRVDWPH ATFSTPVKRI FDTQTTLDFQ SSLAIHRIKY HLHKYTTLIS 51 HCSDPDPHAT ASSIAMVNGL MGVLDKLAHL IDETPPLPGP RRYGNLACRE 101 WHHKLDERLP QWLQEMLPSE YHEVVPELQY YLGNSFGSST RLDYGTGHEL 151 SFMATVAALD MLGMFPHMRG ADVFLLFNKY YTIMRRLILT YTLEPAGSHG 201 VWGLDDHFHL VYILGSSQWQ LLDAQAPLQP REILDKSLVR EYKDTNFYCQ 251 GINFINEVKM GPFEEHSPIL YDIAVTVPRW SKVCKGLLKM YSVEVLKKFP 301 VVQHFWFGTG FFPWVNIQNG TDLPVFEEKE EESIEQANAG SPGREQTSTR 351 FPTSTSMPPP GVPPSGNNIN YLLSHQNQSH RNQTSFSRDR LRR*

Amino Acid Sequence (or in FASTA format)

       1  MSLDRVDWPH ATFSTPVKRI FDTQTTLDFQ SSLAIHRIKY HLHKYTTLIS
      51  HCSDPDPHAT ASSIAMVNGL MGVLDKLAHL IDETPPLPGP RRYGNLACRE
     101  WHHKLDERLP QWLQEMLPSE YHEVVPELQY YLGNSFGSST RLDYGTGHEL
     151  SFMATVAALD MLGMFPHMRG ADVFLLFNKY YTIMRRLILT YTLEPAGSHG
     201  VWGLDDHFHL VYILGSSQWQ LLDAQAPLQP REILDKSLVR EYKDTNFYCQ
     251  GINFINEVKM GPFEEHSPIL YDIAVTVPRW SKVCKGLLKM YSVEVLKKFP
     301  VVQHFWFGTG FFPWVNIQNG TDLPVFEEKE EESIEQANAG SPGREQTSTR
     351  FPTSTSMPPP GVPPSGNNIN YLLSHQNQSH RNQTSFSRDR LRR*

external links for Rrd1p

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 Rrd1p

1)	Rempola B, et al. (2000) Functional analysis of RRD1 (YIL153w) and RRD2 (YPL152w), which encode two putative activators of the phosphotyrosyl phosphatase activity of PP2A in Saccharomyces cerevisiae. Mol Gen Genet 262(6):1081-92
2)	Van Hoof C, et al. (2000) The Saccharomyces cerevisiae homologue YPA1 of the mammalian phosphotyrosyl phosphatase activator of protein phosphatase 2A controls progression through the G1 phase of the yeast cell cycle. J Mol Biol 302(1):103-20
3)	Mitchell DA and Sprague GF Jr (2001) The phosphotyrosyl phosphatase activator, Ncs1p (Rrd1p), functions with Cla4p to regulate the G(2)/M transition in Saccharomyces cerevisiae. Mol Cell Biol 21(2):488-500
4)	Van Hoof C, et al. (2001) The Saccharomyces cerevisiae phosphotyrosyl phosphatase activator proteins are required for a subset of the functions disrupted by protein phosphatase 2A mutations. Exp Cell Res 264(2):372-87
5)	Van Hoof C, et al. (1998) Functional analysis of conserved domains in the phosphotyrosyl phosphatase activator. Molecular cloning of the homologues from Drosophila melanogaster and Saccharomyces cerevisiae. Biochemistry 37(37):12899-908
6)	Zheng Y and Jiang Y (2005) The yeast phosphotyrosyl phosphatase activator is part of the Tap42-phosphatase complexes. Mol Biol Cell 16(4):2119-27
7)	Douville J, et al. (2004) The yeast phosphotyrosyl phosphatase activator protein, yPtpa1/Rrd1, interacts with Sit4 phosphatase to mediate resistance to 4-nitroquinoline-1-oxide and UVA. Curr Genet 46(2):72-81
8)	Fellner T, et al. (2003) A novel and essential mechanism determining specificity and activity of protein phosphatase 2A (PP2A) in vivo. Genes Dev 17(17):2138-50
9)	Jordens J, et al. (2006) The protein phosphatase 2A phosphatase activator is a novel peptidyl-prolyl cis/trans-isomerase. J Biol Chem 281(10):6349-57
10)	Marrakchi R, et al. (2011) The isomerase Rrd1 mediates rapid loss of the Sgs1 helicase in response to rapamycin. Biochem Cell Biol 89(3):332-40
11)	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
12)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41