CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019659
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Remodeling and spacing factor 1 
Protein Synonyms/Alias
 Rsf-1; HBV pX-associated protein 8; Hepatitis B virus X-associated protein; p325 subunit of RSF chromatin-remodeling complex 
Gene Name
 RSF1 
Gene Synonyms/Alias
 HBXAP; XAP8 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
89VTADRWEKYLIKICQubiquitination[1, 2, 3]
136CQFDDNLKFKNIINEacetylation[4]
136CQFDDNLKFKNIINEubiquitination[5]
158LQPIGRDKDGLMYWYubiquitination[2, 5]
189DQDGSSWKCIVRNRNubiquitination[5]
215QIDPVLLKNSSQQDNubiquitination[1, 2, 3, 5, 6]
254QKESEKMKSEEQPMDsumoylation[7]
254QKESEKMKSEEQPMDubiquitination[6]
277VLEETTVKKEKEDEKsumoylation[7]
278LEETTVKKEKEDEKEsumoylation[8]
288EDEKELVKLPVIVKLsumoylation[8]
288EDEKELVKLPVIVKLubiquitination[1, 2, 3, 6]
294VKLPVIVKLEKPLPEsumoylation[7]
297PVIVKLEKPLPENEEubiquitination[6]
309NEEKKIIKEESDSFKsumoylation[7]
381LKNDQQAKIPLKKREubiquitination[2]
411CKSVTPTKEFLKDEIubiquitination[1, 2, 3]
419EFLKDEIKQEEETCKsumoylation[7]
456ERVAPNFKTEPIETKsumoylation[7]
456ERVAPNFKTEPIETKubiquitination[2]
463KTEPIETKFYETKEEubiquitination[1, 2, 3]
498NSVITSMKTGELEKEubiquitination[6]
698IEEPSETKGSMQKSKubiquitination[6]
709QKSKFKYKLVPEEETubiquitination[6]
758KVLEPENKQEKTEKEubiquitination[6]
1039EAIEDDIKEADGGGVubiquitination[6]
1050GGGVGRGKDISTITGacetylation[9]
1050GGGVGRGKDISTITGubiquitination[2]
1061TITGHRGKDISTILDacetylation[9]
1294EEEEEEGKPSRKRLHacetylation[10]
1338PSEQESTKKPYRIESacetylation[11]
1339SEQESTKKPYRIESDacetylation[9, 10, 11, 12]
1378TNGQSPGKAIENLIGacetylation[11]
1386AIENLIGKPTEKSQTacetylation[11, 12, 13]
1390LIGKPTEKSQTPKDNacetylation[10, 11]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [5] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [6] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [7] Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.
 Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, van Dam H, Gnad F, Mann M, Vertegaal AC.
 Mol Cell. 2010 Aug 27;39(4):641-52. [PMID: 20797634]
 [8] A novel proteomics approach to identify SUMOylated proteins and their modification sites in human cells.
 Galisson F, Mahrouche L, Courcelles M, Bonneil E, Meloche S, Chelbi-Alix MK, Thibault P.
 Mol Cell Proteomics. 2011 Feb;10(2):M110.004796. [PMID: 21098080]
 [9] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [10] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [11] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [12] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [13] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330
Functional Description
 Required for assembly of regular nucleosome arrays by the RSF chromatin-remodeling complex. Facilitates transcription of hepatitis B virus (HBV) genes by the pX transcription activator. In case of infection by HBV, together with pX, it represses TNF- alpha induced NF-kappa-B transcription activation. Represses transcription when artificially recruited to chromatin by fusion to a heterogeneous DNA binding domain. 
Sequence Annotation
 DOMAIN 17 84 DDT.
 ZN_FING 891 941 PHD-type.
 MOD_RES 227 227 Phosphoserine.
 MOD_RES 397 397 Phosphoserine.
 MOD_RES 473 473 Phosphoserine.
 MOD_RES 524 524 Phosphoserine.
 MOD_RES 604 604 Phosphoserine.
 MOD_RES 622 622 Phosphoserine.
 MOD_RES 629 629 Phosphoserine.
 MOD_RES 748 748 Phosphoserine.
 MOD_RES 882 882 Phosphoserine.
 MOD_RES 1050 1050 N6-acetyllysine.
 MOD_RES 1096 1096 Phosphoserine.
 MOD_RES 1098 1098 Phosphoserine.
 MOD_RES 1105 1105 Phosphoserine.
 MOD_RES 1221 1221 Phosphoserine.
 MOD_RES 1223 1223 Phosphoserine.
 MOD_RES 1226 1226 Phosphoserine.
 MOD_RES 1258 1258 Phosphoserine.
 MOD_RES 1277 1277 Phosphoserine.
 MOD_RES 1278 1278 Phosphothreonine.
 MOD_RES 1305 1305 Phosphothreonine.
 MOD_RES 1310 1310 Phosphoserine.
 MOD_RES 1325 1325 Phosphoserine.
 MOD_RES 1339 1339 N6-acetyllysine.
 MOD_RES 1345 1345 Phosphoserine.
 MOD_RES 1359 1359 Phosphoserine.
 MOD_RES 1375 1375 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Chromatin regulator; Coiled coil; Complete proteome; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1441 AA 
Protein Sequence
MATAAAAAAV MAPPGCPGSC PNFAVVCSFL ERYGPLLDLP ELPFPELERV LQAPPPDVGN 60
GEVPKELVEL HLKLMRKIGK SVTADRWEKY LIKICQEFNS TWAWEMEKKG YLEMSVECKL 120
ALLKYLCECQ FDDNLKFKNI INEEDADTMR LQPIGRDKDG LMYWYQLDQD HNVRMYIEEQ 180
DDQDGSSWKC IVRNRNELAE TLALLKAQID PVLLKNSSQQ DNSSRESPSL EDEETKKEEE 240
TPKQEEQKES EKMKSEEQPM DLENRSTANV LEETTVKKEK EDEKELVKLP VIVKLEKPLP 300
ENEEKKIIKE ESDSFKENVK PIKVEVKECR ADPKDTKSSM EKPVAQEPER IEFGGNIKSS 360
HEITEKSTEE TEKLKNDQQA KIPLKKREIK LSDDFDSPVK GPLCKSVTPT KEFLKDEIKQ 420
EEETCKRIST ITALGHEGKQ LVNGEVSDER VAPNFKTEPI ETKFYETKEE SYSPSKDRNI 480
ITEGNGTESL NSVITSMKTG ELEKETAPLR KDADSSISVL EIHSQKAQIE EPDPPEMETS 540
LDSSEMAKDL SSKTALSSTE SCTMKGEEKS PKTKKDKRPP ILECLEKLEK SKKTFLDKDA 600
QRLSPIPEEV PKSTLESEKP GSPEAAETSP PSNIIDHCEK LASEKEVVEC QSTSTVGGQS 660
VKKVDLETLK EDSEFTKVEM DNLDNAQTSG IEEPSETKGS MQKSKFKYKL VPEEETTASE 720
NTEITSERQK EGIKLTIRIS SRKKKPDSPP KVLEPENKQE KTEKEEEKTN VGRTLRRSPR 780
ISRPTAKVAE IRDQKADKKR GEGEDEVEEE STALQKTDKK EILKKSEKDT NSKVSKVKPK 840
GKVRWTGSRT RGRWKYSSND ESEGSGSEKS SAASEEEEEK ESEEAILADD DEPCKKCGLP 900
NHPELILLCD SCDSGYHTAC LRPPLMIIPD GEWFCPPCQH KLLCEKLEEQ LQDLDVALKK 960
KERAERRKER LVYVGISIEN IIPPQEPDFS EDQEEKKKDS KKSKANLLER RSTRTRKCIS 1020
YRFDEFDEAI DEAIEDDIKE ADGGGVGRGK DISTITGHRG KDISTILDEE RKENKRPQRA 1080
AAARRKKRRR LNDLDSDSNL DEEESEDEFK ISDGSQDEFV VSDENPDESE EDPPSNDDSD 1140
TDFCSRRLRR HPSRPMRQSR RLRRKTPKKK YSDDDEEEES EENSRDSESD FSDDFSDDFV 1200
ETRRRRSRRN QKRQINYKED SESDGSQKSL RRGKEIRRVH KRRLSSSESE ESYLSKNSED 1260
DELAKESKRS VRKRGRSTDE YSEADEEEEE EEGKPSRKRL HRIETDEEES CDNAHGDANQ 1320
PARDSQPRVL PSEQESTKKP YRIESDEEED FENVGKVGSP LDYSLVDLPS TNGQSPGKAI 1380
ENLIGKPTEK SQTPKDNSTA SASLASNGTS GGQEAGAPEE EEDELLRVTD LVDYVCNSEQ 1440
L 1441 
Gene Ontology
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0031213; C:RSF complex; IPI:UniProtKB.
 GO:0042393; F:histone binding; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0034080; P:CENP-A containing nucleosome assembly at centromere; TAS:Reactome.
 GO:0006352; P:DNA-dependent transcription, initiation; IDA:UniProtKB.
 GO:0043392; P:negative regulation of DNA binding; IDA:UniProtKB.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0016584; P:nucleosome positioning; IDA:UniProtKB.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0050434; P:positive regulation of viral transcription; IDA:UniProtKB. 
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
 PS50827; DDT
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS