CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-038159
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Protein Rsf1 
Protein Synonyms/Alias
  
Gene Name
 Rsf1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
500EKEAPLGKGIDSSVPacetylation[1]
563EEKAPRSKSENHTPGacetylation[1]
1038GGGVGRGKDISTITGacetylation[1, 2, 3]
1049TITGHRGKDISTILDacetylation[1, 2, 3, 4]
1371AIENLMGKATEKSQTacetylation[3]
Reference
 [1] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [2] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [3] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [4] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Metal-binding; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1426 AA 
Protein Sequence
MAPPGCPGSC PNFAVVCSFL ERYGPLLDLP ELPFPELERV LQAPPPDIGN GEVPKELVEL 60
HLKLMRKIGK SVTADRWEKY LIKICQEFNS TWAWEMEKKG YLEMSVECKL ALLKYLCECQ 120
FDDNLKFKNI INEEDADTMR LQPIGRDKDG LMYWYQLDQD HNVRMYIEEQ DDQDGSSWKC 180
IVRNRNELAE TLALLKAQID PVLLKNSSQQ EDSSRESPTL EDEETKKDEE TPKQEASKEN 240
EKTGADERSV DSGKCSAASA LEEPAVKTEK ADEKELAKLP VIVKLEKPLP ETEEKKIIRE 300
ESDSFKENVK PIKVEAKECR ADPKDLKGSL ERLGSQEPER ADFGSNIKSQ DIIEKSTEET 360
EKLKNDQQAK IPLKKREIKL SDDFDSPVKG PLCKSATPTK EVLKDDIKQE EETCKRVSTI 420
SALSHEGKQL VNGEINDDKV IPNFKTEQME IQLCDTKEDS ASIPAKDGNA CMEGNGTECL 480
NSVITSTKTS ELEKEAPLGK GIDSSVPDIE SLSQKARLEE PGLLNMDMPL EPSEKATDLS 540
LKPTLSATEP CSTKVEEKAP RSKSENHTPG IECLERVEKA KKTSIDKDIQ KLSPIPEEVV 600
RGALESEKSG PCEVAETPLP LSMAGAKEKQ TSEKKDVDCS RGSSESQSLE NASPEILKED 660
SESSREEVAK LDNAQTSGME DTSETKGSVQ KNKFKYKLVS ERNSTASENT EITSERKKEG 720
IKLTIRISSR KKKPDCPPQT VDSESKEEKA GKEEEKASVG RTLRRSPRIS RPTAKVAEIR 780
VQKADKRRAD GEDGVEGEPA SLQTADKKDH LKKAEKDTNS KASKVKPKGK VRWTGSRTRG 840
RWKYSSNDES EGSESDKSSA ALEEEEGKEG EEAVLPDDDE PCKKCGLPNH PELILLCDSC 900
DSGYHTACLR PPLMIIPDGE WFCPPCQHKL LCEKLEEQLQ DLDVALKKKE RAERRKERLV 960
YVGISIENII PPQEPEFSEE QEEKKKDAKK SKANALERRS TRTRKCISYR FDEFDEAIDE 1020
AIEDDIKEAD GGGVGRGKDI STITGHRGKD ISTILDEERK ENKRPQRAAA ARRKKRRRLN 1080
DLDSDSNLDE EESEDEFKIS DGSQDEFVVS DENPDESEEE PPSNEDSDTD FCSRRLRRHP 1140
SRPMRQSRRL RRKTPKKKYS DDDEEEEESE ENSRDSESDF SDDFSDDFVE TRRRRSRRNQ 1200
KRQINYKEDS ESDGSQKSLR RGKEIRRVHK RRLSSSESEE SFMSKNSEDD ELTKESKRSV 1260
RKRGRSTDDY SEADEDDEEE GKPSRKRLHR IETDEESCDN AHGDADQPAR DSQPSALPSE 1320
QESSKKPYRI ESDEEEDFEN KVGSPLDYSL VDLPSTNGQS PGKAIENLMG KATEKSQTPK 1380
DNGTASASLA PNGTSGGQEV GAPEEDEDEL LRVTDLVDYV CNSEQL 1426 
Gene Ontology
 GO:0031213; C:RSF complex; IEA:Compara.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006338; P:chromatin remodeling; IEA:Compara.
 GO:0006352; P:DNA-dependent transcription, initiation; IEA:Compara.
 GO:0043392; P:negative regulation of DNA binding; IEA:Compara.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IEA:Compara.
 GO:0006334; P:nucleosome assembly; IEA:Compara.
 GO:0016584; P:nucleosome positioning; IEA:Compara.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IEA:Compara.
 GO:0050434; P:positive regulation of viral transcription; IEA:Compara. 
Interpro
 IPR019786; Zinc_finger_PHD-type_CS.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF00628; PHD 
SMART
 SM00249; PHD 
PROSITE
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS