CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006856
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ISWI chromatin-remodeling complex ATPase ISW1 
Protein Synonyms/Alias
  
Gene Name
 ISW1 
Gene Synonyms/Alias
 YBR245C; YBR1633 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
14IANFHFFKFYTRMRKmethylation[1]
725KTKSLNAKYETLGLDacetylation[2]
768PLLLNPTKRERKENYacetylation[2]
972RRKLSEYKNPFFDLKacetylation[2]
1105GVESKKAKIEDTSNVacetylation[2]
1121TEQLVAEKIPENETTacetylation[2]
Reference
 [1] Identification of arginine- and lysine-methylation in the proteome of Saccharomyces cerevisiae and its functional implications.
 Pang CN, Gasteiger E, Wilkins MR.
 BMC Genomics. 2010 Feb 5;11:92. [PMID: 20137074]
 [2] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919] 
Functional Description
 Catalytic component of ISW1-type complexes, which act by remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. They are involved in coordinating transcriptional repression, activation and elongation phases. The ISW1A complex represses gene expression at initiation through specific positioning of a promoter proximal dinucleosome. The ISW1B complex acts within coding regions to control the amount of RNA polymerase II released into productive elongation and to coordinate elongation with termination and pre-mRNA processing. 
Sequence Annotation
 DOMAIN 208 373 Helicase ATP-binding.
 DOMAIN 506 657 Helicase C-terminal.
 DOMAIN 882 935 SANT 1.
 DOMAIN 988 1052 SANT 2.
 NP_BIND 221 228 ATP (Potential).
 MOTIF 324 327 DEAH box.
 MOD_RES 694 694 Phosphothreonine.
 MOD_RES 846 846 Phosphoserine.  
Keyword
 3D-structure; ATP-binding; Chromatin regulator; Complete proteome; DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1129 AA 
Protein Sequence
MAYMLAIANF HFFKFYTRMR KKHENNSCNE KDKDENLFKI ILAIFLQEKK KYDCISSGSI 60
MTASEEYLEN LKPFQVGLPP HDPESNKKRY LLKDANGKKF DLEGTTKRFE HLLSLSGLFK 120
HFIESKAAKD PKFRQVLDVL EENKANGKGK GKHQDVRRRK TEHEEDAELL KEEDSDDDES 180
IEFQFRESPA YVNGQLRPYQ IQGVNWLVSL HKNKIAGILA DEMGLGKTLQ TISFLGYLRY 240
IEKIPGPFLV IAPKSTLNNW LREINRWTPD VNAFILQGDK EERAELIQKK LLGCDFDVVI 300
ASYEIIIREK SPLKKINWEY IIIDEAHRIK NEESMLSQVL REFTSRNRLL ITGTPLQNNL 360
HELWALLNFL LPDIFSDAQD FDDWFSSEST EEDQDKIVKQ LHTVLQPFLL RRIKSDVETS 420
LLPKKELNLY VGMSSMQKKW YKKILEKDLD AVNGSNGSKE SKTRLLNIMM QLRKCCNHPY 480
LFDGAEPGPP YTTDEHLVYN AAKLQVLDKL LKKLKEEGSR VLIFSQMSRL LDILEDYCYF 540
RNYEYCRIDG STAHEDRIQA IDDYNAPDSK KFVFLLTTRA GGLGINLTSA DVVVLYDSDW 600
NPQADLQAMD RAHRIGQKKQ VKVFRLVTDN SVEEKILERA TQKLRLDQLV IQQNRTSLKK 660
KENKADSKDA LLSMIQHGAA DVFKSGTSTG SAGTPEPGSG EKGDDIDLDE LLLKSENKTK 720
SLNAKYETLG LDDLQKFNQD SAYEWNGQDF KKKIQRDIIS PLLLNPTKRE RKENYSIDNY 780
YKDVLNTGRS STPSHPRMPK PHVFHSHQLQ PPQLKVLYEK ERMWTAKKTG YVPTMDDVKA 840
AYGDISDEEE KKQKLELLKL SVNNSQPLTE EEEKMKADWE SEGFTNWNKL EFRKFITVSG 900
KYGRNSIQAI ARELAPGKTL EEVRAYAKAF WSNIERIEDY EKYLKIIENE EEKIKRVKMQ 960
QEALRRKLSE YKNPFFDLKL KHPPSSNNKR TYSEEEDRFI LLMLFKYGLD RDDVYELVRD 1020
EIRDCPLFEL DFYFRSRTPV ELARRGNTLL QCLEKEFNAG IVLDDATKDR MKKEDENGKR 1080
IREEFADQTA NEKENVDGVE SKKAKIEDTS NVGTEQLVAE KIPENETTH 1129 
Gene Ontology
 GO:0016587; C:Isw1 complex; IPI:SGD.
 GO:0030874; C:nucleolar chromatin; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
 GO:0031491; F:nucleosome binding; IEA:InterPro.
 GO:0000182; F:rDNA binding; IDA:SGD.
 GO:0006200; P:ATP catabolic process; IDA:GOC.
 GO:0043044; P:ATP-dependent chromatin remodeling; IEA:InterPro.
 GO:0006338; P:chromatin remodeling; IGI:SGD.
 GO:0006354; P:DNA-dependent transcription, elongation; IDA:SGD.
 GO:0070870; P:heterochromatin maintenance involved in chromatin silencing; IMP:SGD.
 GO:0016584; P:nucleosome positioning; IMP:SGD.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:SGD.
 GO:0034401; P:regulation of transcription by chromatin organization; IMP:SGD.
 GO:0001178; P:regulation of transcriptional start site selection at RNA polymerase II promoter; IGI:SGD.
 GO:0006363; P:termination of RNA polymerase I transcription; IGI:SGD.
 GO:0006369; P:termination of RNA polymerase II transcription; IGI:SGD. 
Interpro
 IPR014001; Helicase_ATP-bd.
 IPR001650; Helicase_C.
 IPR009057; Homeodomain-like.
 IPR015194; ISWI_HAND-dom.
 IPR027417; P-loop_NTPase.
 IPR001005; SANT/Myb.
 IPR017884; SANT_dom.
 IPR015195; SLIDE.
 IPR000330; SNF2_N. 
Pfam
 PF09110; HAND
 PF00271; Helicase_C
 PF09111; SLIDE
 PF00176; SNF2_N 
SMART
 SM00487; DEXDc
 SM00490; HELICc
 SM00717; SANT 
PROSITE
 PS00690; DEAH_ATP_HELICASE
 PS51192; HELICASE_ATP_BIND_1
 PS51194; HELICASE_CTER
 PS51293; SANT 
PRINTS