CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012010
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Zinc finger protein Rlf 
Protein Synonyms/Alias
 Rearranged L-myc fusion gene protein; Zn-15-related protein 
Gene Name
 RLF 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
191WKNPVLLKILSQQPVubiquitination[1]
704QNNDENAKHYLDMKNubiquitination[2]
839GDIKKSVKLEESATGsumoylation[3]
848EESATGEKQDCINQPubiquitination[2]
1211HKLLDNEKCDHEGPCubiquitination[2]
1224PCSVDRLKGDCSAELubiquitination[4]
1339RTVHQYNKEQLCLEKubiquitination[4]
1470QHVYYRHKDYYDDLFmethylation[5]
1492ERLLRSEKVCQTADTubiquitination[6]
1599VKYGTKIKEEPPSEAsumoylation[3]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [5] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510]
 [6] 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
Functional Description
 May be involved in transcriptional regulation. 
Sequence Annotation
 ZN_FING 582 604 C2H2-type 1.
 ZN_FING 671 696 C2H2-type 2.
 ZN_FING 714 736 C2H2-type 3.
 ZN_FING 742 766 C2H2-type 4.
 ZN_FING 771 795 C2H2-type 5.
 ZN_FING 801 825 C2H2-type 6.
 ZN_FING 954 979 C2H2-type 7.
 ZN_FING 1127 1152 C2H2-type 8.
 ZN_FING 1172 1195 C2H2-type 9.
 ZN_FING 1310 1335 C2H2-type 10.
 ZN_FING 1362 1387 C2H2-type 11.
 ZN_FING 1407 1432 C2H2-type 12.
 ZN_FING 1444 1469 C2H2-type 13.
 ZN_FING 1549 1574 C2H2-type 14.
 MOD_RES 41 41 Phosphoserine.
 MOD_RES 632 632 Phosphoserine.  
Keyword
 Complete proteome; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1914 AA 
Protein Sequence
MADGKGDAAA VAGAGAEAPA VAGAGDGVET ESMVRGHRPV SPAPGASGLR PCLWQLETEL 60
REQEVSEVSS LNYCRSFCQT LLQYASNKNA SEHIVYLLEV YRLAIQSFAS ARPYLTTECE 120
DVLLVLGRLV LSCFELLLSV SESELPCEVW LPFLQSLQES HDALLEFGNN NLQILVHVTK 180
EGVWKNPVLL KILSQQPVET EEVNKLIAQE GPSFLQMRIK HLLKSNCIPQ ATALSKLCAE 240
SKEISNVSSF QQAYITCLCS MLPNEDAIKE IAKVDCKEVL DIICNLESEG QDNTAFVLCT 300
TYLTQQLQTA SVYCSWELTL FWSKLQRRID PSLDTFLERC RQFGVIAKTQ QHLFCLIRVI 360
QTEAQDAGLG VSILLCVRAL QLRSSEDEEM KASVCKTIAC LLPEDLEVRR ACQLTEFLIE 420
PSLDGFNMLE ELYLQPDQKF DEENAPVPNS LRCELLLALK AHWPFDPEFW DWKTLKRHCH 480
QLLGQEASDS DDDLSGYEMS INDTDVLESF LSDYDEGKED KQYRRRDLTD QHKEKRDKKP 540
IGSSERYQRW LQYKFFCLLC KRECIEARIL HHSKMHMEDG IYTCPVCIKK FKRKEMFVPH 600
VMEHVKMPPS RRDRSKKKLL LKGSQKGICP KSPSAIPEQN HSLNDQAKGE SHEYVTFSKL 660
EDCHLQDRDL YPCPGTDCSR VFKQFKYLSV HLKAEHQNND ENAKHYLDMK NRREKCTYCR 720
RHFMSAFHLR EHEQVHCGPQ PYMCVSIDCY ARFGSVNELL NHKQKHDDLR YKCELNGCNI 780
VFSDLGQLYH HEAQHFRDAS YTCNFLGCKK FYYSKIEYQN HLSMHNVENS NGDIKKSVKL 840
EESATGEKQD CINQPHLLNQ TDKSHLPEDL FCAESANSQI DTETAENLKE NSDSNSSDQL 900
SHSSSASMNE ELIDTLDHSE TMQDVLLSNE KVFGPSSLKE KCSSMAVCFD GTKFTCGFDG 960
CGSTYKNARG MQKHLRKVHP YHFKPKKIKT KDLFPSLGNE HNQTTEKLDA EPKPCSDTNS 1020
DSPDEGLDHN IHIKCKREHQ GYSSESSICA SKRPCTEDTM LELLLRLKHL SLKNSITHGS 1080
FSGSLQGYPS SGAKSLQSVS SISDLNFQNQ DENMPSQYLA QLAAKPFFCE LQGCKYEFVT 1140
REALLMHYLK KHNYSKEKVL QLTMFQHRYS PFQCHICQRS FTRKTHLRIH YKNKHQIGSD 1200
RATHKLLDNE KCDHEGPCSV DRLKGDCSAE LGGDPSSNSE KPHCHPKKDE CSSETDLESS 1260
CEETESKTSD ISSPIGSHRE EQEGREGRGS RRTVAKGNLC YILNKYHKPF HCIHKTCNSS 1320
FTNLKGLIRH YRTVHQYNKE QLCLEKDKAR TKRELVKCKK IFACKYKECN KRFLCSKALA 1380
KHCSDSHNLD HIEEPKVLSE AGSAARFSCN QPQCPAVFYT FNKLKHHLME QHNIEGEIHS 1440
DYEIHCDLNG CGQIFTHRSN YSQHVYYRHK DYYDDLFRSQ KVANERLLRS EKVCQTADTQ 1500
GHEHQTTRRS FNAKSKKCGL IKEKKAPISF KTRAEALHMC VEHSEHTQYP CMVQGCLSVV 1560
KLESSIVRHY KRTHQMSSAY LEQQMENLVV CVKYGTKIKE EPPSEADPCI KKEENRSCES 1620
ERTEHSHSPG DSSAPIQNTD CCHSSERDGG QKGCIESSSV FDADTLLYRG TLKCNHSSKT 1680
TSLEQCNIVQ PPPPCKIENS IPNPNGTESG TYFTSFQLPL PRIKESETRQ HSSGQENTVK 1740
NPTHVPKENF RKHSQPRSFD LKTYKPMGFE SSFLKFIQES EEKEDDFDDW EPSEHLTLSN 1800
SSQSSNDLTG NVVANNMVND SEPEVDIPHS SSDSTIHENL TAIPPLIVAE TTTVPSLENL 1860
RVVLDKALTD CGELALKQLH YLRPVVVLER SKFSTPILDL FPTKKTDELC VGSS 1914 
Gene Ontology
 GO:0005634; C:nucleus; IC:UniProtKB.
 GO:0003677; F:DNA binding; NAS:UniProtKB.
 GO:0008270; F:zinc ion binding; TAS:ProtInc.
 GO:0051276; P:chromosome organization; IDA:UniProtKB.
 GO:0015074; P:DNA integration; IDA:UniProtKB.
 GO:0009294; P:DNA mediated transformation; NAS:UniProtKB.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR007087; Znf_C2H2.
 IPR015880; Znf_C2H2-like.
 IPR013087; Znf_C2H2/integrase_DNA-bd. 
Pfam
  
SMART
 SM00355; ZnF_C2H2 
PROSITE
 PS00028; ZINC_FINGER_C2H2_1
 PS50157; ZINC_FINGER_C2H2_2 
PRINTS