ISW1/YBR245C Protein Information

Standard Name	Isw1p 1
Systematic Name	Ybr245cp
Alias	Sgn2p 2
ORF Classification	Verified
Description	ATPase subunit of imitation-switch (ISWI) class chromatin remodelers; ATPase; forms a complex with Ioc3p (Isw1a), and a complex with Ioc2p and Ioc4p (Isw1b); Isw1a and Isw1b have partially overlapping and distinct roles, Isw1a involved in repression of transcription initiation and Isw1b involved in regulation of transcription elongation; Isw1b recruited to open reading frames by H3K36 methylation and acts with Chd1p to prevent trans-histone exchange over coding regions (1, 3, 4, 5, 6)
Name Description	Imitation SWitch subfamily 1

Experimental Data
Molecules/cell	1500 7

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	1,129
Molecular Weight (Da)	131,101
Isoelectric Point (pI)	6.61

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 Isw1p (InterPro)
Physical Interactions	There are 127 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI0000052F02 \| P38144 MIPS: YBR245C NCBI: 1872131 \| 2506238 \| 329665879 \| 329665881 \| 6319722 \| NP_009804.1 \| NM_001178593.1 GenBank/EMBL/DDBJ: DAA07361.1 \| Z36114
External Classifications	EC: 3.6.1.- [Hydrolases acting on acid anhydrides in phosphorous-containing anhydrides] EC: 3.6.4.-

Amino Acid Sequence (or in FASTA format)
1 MAYMLAIANF HFFKFYTRMR KKHENNSCNE KDKDENLFKI ILAIFLQEKK 51 KYDCISSGSI MTASEEYLEN LKPFQVGLPP HDPESNKKRY LLKDANGKKF 101 DLEGTTKRFE HLLSLSGLFK HFIESKAAKD PKFRQVLDVL EENKANGKGK 151 GKHQDVRRRK TEHEEDAELL KEEDSDDDES IEFQFRESPA YVNGQLRPYQ 201 IQGVNWLVSL HKNKIAGILA DEMGLGKTLQ TISFLGYLRY IEKIPGPFLV 251 IAPKSTLNNW LREINRWTPD VNAFILQGDK EERAELIQKK LLGCDFDVVI 301 ASYEIIIREK SPLKKINWEY IIIDEAHRIK NEESMLSQVL REFTSRNRLL 351 ITGTPLQNNL HELWALLNFL LPDIFSDAQD FDDWFSSEST EEDQDKIVKQ 401 LHTVLQPFLL RRIKSDVETS LLPKKELNLY VGMSSMQKKW YKKILEKDLD 451 AVNGSNGSKE SKTRLLNIMM QLRKCCNHPY LFDGAEPGPP YTTDEHLVYN 501 AAKLQVLDKL LKKLKEEGSR VLIFSQMSRL LDILEDYCYF RNYEYCRIDG 551 STAHEDRIQA IDDYNAPDSK KFVFLLTTRA GGLGINLTSA DVVVLYDSDW 601 NPQADLQAMD RAHRIGQKKQ VKVFRLVTDN SVEEKILERA TQKLRLDQLV 651 IQQNRTSLKK KENKADSKDA LLSMIQHGAA DVFKSGTSTG SAGTPEPGSG 701 EKGDDIDLDE LLLKSENKTK SLNAKYETLG LDDLQKFNQD SAYEWNGQDF 751 KKKIQRDIIS PLLLNPTKRE RKENYSIDNY YKDVLNTGRS STPSHPRMPK 801 PHVFHSHQLQ PPQLKVLYEK ERMWTAKKTG YVPTMDDVKA AYGDISDEEE 851 KKQKLELLKL SVNNSQPLTE EEEKMKADWE SEGFTNWNKL EFRKFITVSG 901 KYGRNSIQAI ARELAPGKTL EEVRAYAKAF WSNIERIEDY EKYLKIIENE 951 EEKIKRVKMQ QEALRRKLSE YKNPFFDLKL KHPPSSNNKR TYSEEEDRFI 1001 LLMLFKYGLD RDDVYELVRD EIRDCPLFEL DFYFRSRTPV ELARRGNTLL 1051 QCLEKEFNAG IVLDDATKDR MKKEDENGKR IREEFADQTA NEKENVDGVE 1101 SKKAKIEDTS NVGTEQLVAE KIPENETTH*

Amino Acid Sequence (or in FASTA format)

       1  MAYMLAIANF HFFKFYTRMR KKHENNSCNE KDKDENLFKI ILAIFLQEKK
      51  KYDCISSGSI MTASEEYLEN LKPFQVGLPP HDPESNKKRY LLKDANGKKF
     101  DLEGTTKRFE HLLSLSGLFK HFIESKAAKD PKFRQVLDVL EENKANGKGK
     151  GKHQDVRRRK TEHEEDAELL KEEDSDDDES IEFQFRESPA YVNGQLRPYQ
     201  IQGVNWLVSL HKNKIAGILA DEMGLGKTLQ TISFLGYLRY IEKIPGPFLV
     251  IAPKSTLNNW LREINRWTPD VNAFILQGDK EERAELIQKK LLGCDFDVVI
     301  ASYEIIIREK SPLKKINWEY IIIDEAHRIK NEESMLSQVL REFTSRNRLL
     351  ITGTPLQNNL HELWALLNFL LPDIFSDAQD FDDWFSSEST EEDQDKIVKQ
     401  LHTVLQPFLL RRIKSDVETS LLPKKELNLY VGMSSMQKKW YKKILEKDLD
     451  AVNGSNGSKE SKTRLLNIMM QLRKCCNHPY LFDGAEPGPP YTTDEHLVYN
     501  AAKLQVLDKL LKKLKEEGSR VLIFSQMSRL LDILEDYCYF RNYEYCRIDG
     551  STAHEDRIQA IDDYNAPDSK KFVFLLTTRA GGLGINLTSA DVVVLYDSDW
     601  NPQADLQAMD RAHRIGQKKQ VKVFRLVTDN SVEEKILERA TQKLRLDQLV
     651  IQQNRTSLKK KENKADSKDA LLSMIQHGAA DVFKSGTSTG SAGTPEPGSG
     701  EKGDDIDLDE LLLKSENKTK SLNAKYETLG LDDLQKFNQD SAYEWNGQDF
     751  KKKIQRDIIS PLLLNPTKRE RKENYSIDNY YKDVLNTGRS STPSHPRMPK
     801  PHVFHSHQLQ PPQLKVLYEK ERMWTAKKTG YVPTMDDVKA AYGDISDEEE
     851  KKQKLELLKL SVNNSQPLTE EEEKMKADWE SEGFTNWNKL EFRKFITVSG
     901  KYGRNSIQAI ARELAPGKTL EEVRAYAKAF WSNIERIEDY EKYLKIIENE
     951  EEKIKRVKMQ QEALRRKLSE YKNPFFDLKL KHPPSSNNKR TYSEEEDRFI
    1001  LLMLFKYGLD RDDVYELVRD EIRDCPLFEL DFYFRSRTPV ELARRGNTLL
    1051  QCLEKEFNAG IVLDDATKDR MKKEDENGKR IREEFADQTA NEKENVDGVE
    1101  SKKAKIEDTS NVGTEQLVAE KIPENETTH*

external links for Isw1p

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

References cited on this page View Complete Literature Guide for Isw1p

1)	Tsukiyama T, et al. (1999) Characterization of the imitation switch subfamily of ATP-dependent chromatin-remodeling factors in Saccharomyces cerevisiae. Genes Dev 13(6):686-97
2)	Entian KD, et al. (1999) Functional analysis of 150 deletion mutants in Saccharomyces cerevisiae by a systematic approach. Mol Gen Genet 262(4-5):683-702
3)	Vary JC Jr, et al. (2003) Yeast Isw1p forms two separable complexes in vivo. Mol Cell Biol 23(1):80-91
4)	Morillon A, et al. (2003) Isw1 chromatin remodeling ATPase coordinates transcription elongation and termination by RNA polymerase II. Cell 115(4):425-35
5)	Mellor J and Morillon A (2004) ISWI complexes in Saccharomyces cerevisiae. Biochim Biophys Acta 1677(1-3):100-12
6)	Smolle M, et al. (2012) Chromatin remodelers Isw1 and Chd1 maintain chromatin structure during transcription by preventing histone exchange. Nat Struct Mol Biol 19(9):884-92
7)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41