ID RLF_HUMAN Reviewed; 1914 AA. AC Q13129; Q14CQ1; Q9NU60; DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 29-MAR-2005, sequence version 2. DT 05-OCT-2010, entry version 95. DE RecName: Full=Zinc finger protein Rlf; DE AltName: Full=Rearranged L-myc fusion gene protein; DE AltName: Full=Zn-15-related protein; GN Name=RLF; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=96132723; PubMed=8545128; RA Makela T.P., Hellsten E., Vesa J., Hirvonen H., Palotie A., RA Peltonen L., Alitalo K.; RT "The rearranged L-myc fusion gene (RLF) encodes a Zn-15 related zinc RT finger protein."; RL Oncogene 11:2699-2704(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Cerebellum; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, AND MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, AND MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). CC -!- FUNCTION: May be involved in transcriptional regulation. CC -!- SUBUNIT: Interacts with RIT1 and RIT2 (By similarity). CC -!- INTERACTION: CC P30793:GCH1; NbExp=2; IntAct=EBI-958266, EBI-958183; CC Q92963:RIT1; NbExp=1; IntAct=EBI-958266, EBI-365845; CC P70425:Rit2 (xeno); NbExp=1; IntAct=EBI-958266, EBI-2649620; CC -!- SUBCELLULAR LOCATION: Nucleus (Probable). CC -!- TISSUE SPECIFICITY: Widely expressed in fetal and adult tissues. CC -!- MISCELLANEOUS: In some small cell lung carcinoma (SCLC) cell CC lines, there is an intrachromosomal rearrangements at 1p32 fusing CC the first exon of the RLF gene with L-myc. CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein CC family. CC -!- SIMILARITY: Contains 14 C2H2-type zinc fingers. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U22377; AAC50396.1; -; mRNA. DR EMBL; AL050341; CAB81608.2; -; Genomic_DNA. DR EMBL; AL929567; CAH71081.1; -; Genomic_DNA. DR EMBL; AL050341; CAH71081.1; JOINED; Genomic_DNA. DR EMBL; AL356424; CAH71081.1; JOINED; Genomic_DNA. DR EMBL; AL512599; CAH71081.1; JOINED; Genomic_DNA. DR EMBL; AL512599; CAI11028.1; -; Genomic_DNA. DR EMBL; AL050341; CAI11028.1; JOINED; Genomic_DNA. DR EMBL; AL356424; CAI11028.1; JOINED; Genomic_DNA. DR EMBL; AL929567; CAI11028.1; JOINED; Genomic_DNA. DR EMBL; AL356424; CAI21999.1; -; Genomic_DNA. DR EMBL; AL050341; CAI21999.1; JOINED; Genomic_DNA. DR EMBL; AL512599; CAI21999.1; JOINED; Genomic_DNA. DR EMBL; AL929567; CAI21999.1; JOINED; Genomic_DNA. DR EMBL; BC113666; AAI13667.1; -; mRNA. DR IPI; IPI00018294; -. DR PIR; S21662; S21662. DR RefSeq; NP_036553.2; -. DR UniGene; Hs.205627; -. DR ProteinModelPortal; Q13129; -. DR SMR; Q13129; 579-765, 671-825, 1310-1465. DR IntAct; Q13129; 10. DR MINT; MINT-1192845; -. DR STRING; Q13129; -. DR PhosphoSite; Q13129; -. DR PRIDE; Q13129; -. DR Ensembl; ENST00000372771; ENSP00000361857; ENSG00000117000. DR GeneID; 6018; -. DR KEGG; hsa:6018; -. DR NMPDR; fig|9606.3.peg.928; -. DR UCSC; uc001cfc.2; human. DR CTD; 6018; -. DR GeneCards; GC01P040627; -. DR HGNC; HGNC:10025; RLF. DR MIM; 180610; gene. DR PharmGKB; PA34398; -. DR eggNOG; prNOG17816; -. DR HOGENOM; HBG713137; -. DR HOVERGEN; HBG057472; -. DR InParanoid; Q13129; -. DR OMA; IRHYRTV; -. DR OrthoDB; EOG9K6JQQ; -. DR PhylomeDB; Q13129; -. DR NextBio; 23479; -. DR ArrayExpress; Q13129; -. DR Bgee; Q13129; -. DR CleanEx; HS_RLF; -. DR Genevestigator; Q13129; -. DR GermOnline; ENSG00000117000; Homo sapiens. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0003700; F:transcription factor activity; TAS:ProtInc. DR GO; GO:0008270; F:zinc ion binding; TAS:ProtInc. DR GO; GO:0006350; P:transcription; IEA:UniProtKB-KW. DR InterPro; IPR007087; Znf_C2H2. DR InterPro; IPR015880; Znf_C2H2-like. DR SMART; SM00355; ZnF_C2H2; 15. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 14. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11. PE 1: Evidence at protein level; KW Complete proteome; DNA-binding; Metal-binding; Nucleus; KW Phosphoprotein; Polymorphism; Repeat; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1 1914 Zinc finger protein Rlf. FT /FTId=PRO_0000047325. FT ZN_FING 582 604 C2H2-type 1. FT ZN_FING 671 696 C2H2-type 2. FT ZN_FING 714 736 C2H2-type 3. FT ZN_FING 742 766 C2H2-type 4. FT ZN_FING 771 795 C2H2-type 5. FT ZN_FING 801 825 C2H2-type 6. FT ZN_FING 954 979 C2H2-type 7. FT ZN_FING 1127 1152 C2H2-type 8. FT ZN_FING 1172 1195 C2H2-type 9. FT ZN_FING 1310 1335 C2H2-type 10. FT ZN_FING 1362 1387 C2H2-type 11. FT ZN_FING 1407 1432 C2H2-type 12. FT ZN_FING 1444 1469 C2H2-type 13. FT ZN_FING 1549 1574 C2H2-type 14. FT MOD_RES 41 41 Phosphoserine. FT VARIANT 668 668 R -> K (in dbSNP:rs35189918). FT /FTId=VAR_052739. FT VARIANT 932 932 V -> A (in dbSNP:rs35563960). FT /FTId=VAR_052740. FT VARIANT 957 957 G -> D (in dbSNP:rs35042446). FT /FTId=VAR_052741. FT VARIANT 1629 1629 P -> L (in dbSNP:rs34123123). FT /FTId=VAR_061929. FT VARIANT 1685 1685 Q -> E (in dbSNP:rs34141181). FT /FTId=VAR_061930. FT VARIANT 1784 1784 E -> D (in dbSNP:rs10889205). FT /FTId=VAR_052742. FT CONFLICT 1546 1548 HTQ -> LSL (in Ref. 1; AAC50396). SQ SEQUENCE 1914 AA; 217953 MW; 105C85C645563999 CRC64; MADGKGDAAA VAGAGAEAPA VAGAGDGVET ESMVRGHRPV SPAPGASGLR PCLWQLETEL REQEVSEVSS LNYCRSFCQT LLQYASNKNA SEHIVYLLEV YRLAIQSFAS ARPYLTTECE DVLLVLGRLV LSCFELLLSV SESELPCEVW LPFLQSLQES HDALLEFGNN NLQILVHVTK EGVWKNPVLL KILSQQPVET EEVNKLIAQE GPSFLQMRIK HLLKSNCIPQ ATALSKLCAE SKEISNVSSF QQAYITCLCS MLPNEDAIKE IAKVDCKEVL DIICNLESEG QDNTAFVLCT TYLTQQLQTA SVYCSWELTL FWSKLQRRID PSLDTFLERC RQFGVIAKTQ QHLFCLIRVI QTEAQDAGLG VSILLCVRAL QLRSSEDEEM KASVCKTIAC LLPEDLEVRR ACQLTEFLIE PSLDGFNMLE ELYLQPDQKF DEENAPVPNS LRCELLLALK AHWPFDPEFW DWKTLKRHCH QLLGQEASDS DDDLSGYEMS INDTDVLESF LSDYDEGKED KQYRRRDLTD QHKEKRDKKP IGSSERYQRW LQYKFFCLLC KRECIEARIL HHSKMHMEDG IYTCPVCIKK FKRKEMFVPH VMEHVKMPPS RRDRSKKKLL LKGSQKGICP KSPSAIPEQN HSLNDQAKGE SHEYVTFSKL EDCHLQDRDL YPCPGTDCSR VFKQFKYLSV HLKAEHQNND ENAKHYLDMK NRREKCTYCR RHFMSAFHLR EHEQVHCGPQ PYMCVSIDCY ARFGSVNELL NHKQKHDDLR YKCELNGCNI VFSDLGQLYH HEAQHFRDAS YTCNFLGCKK FYYSKIEYQN HLSMHNVENS NGDIKKSVKL EESATGEKQD CINQPHLLNQ TDKSHLPEDL FCAESANSQI DTETAENLKE NSDSNSSDQL SHSSSASMNE ELIDTLDHSE TMQDVLLSNE KVFGPSSLKE KCSSMAVCFD GTKFTCGFDG CGSTYKNARG MQKHLRKVHP YHFKPKKIKT KDLFPSLGNE HNQTTEKLDA EPKPCSDTNS DSPDEGLDHN IHIKCKREHQ GYSSESSICA SKRPCTEDTM LELLLRLKHL SLKNSITHGS FSGSLQGYPS SGAKSLQSVS SISDLNFQNQ DENMPSQYLA QLAAKPFFCE LQGCKYEFVT REALLMHYLK KHNYSKEKVL QLTMFQHRYS PFQCHICQRS FTRKTHLRIH YKNKHQIGSD RATHKLLDNE KCDHEGPCSV DRLKGDCSAE LGGDPSSNSE KPHCHPKKDE CSSETDLESS CEETESKTSD ISSPIGSHRE EQEGREGRGS RRTVAKGNLC YILNKYHKPF HCIHKTCNSS FTNLKGLIRH YRTVHQYNKE QLCLEKDKAR TKRELVKCKK IFACKYKECN KRFLCSKALA KHCSDSHNLD HIEEPKVLSE AGSAARFSCN QPQCPAVFYT FNKLKHHLME QHNIEGEIHS DYEIHCDLNG CGQIFTHRSN YSQHVYYRHK DYYDDLFRSQ KVANERLLRS EKVCQTADTQ GHEHQTTRRS FNAKSKKCGL IKEKKAPISF KTRAEALHMC VEHSEHTQYP CMVQGCLSVV KLESSIVRHY KRTHQMSSAY LEQQMENLVV CVKYGTKIKE EPPSEADPCI KKEENRSCES ERTEHSHSPG DSSAPIQNTD CCHSSERDGG QKGCIESSSV FDADTLLYRG TLKCNHSSKT TSLEQCNIVQ PPPPCKIENS IPNPNGTESG TYFTSFQLPL PRIKESETRQ HSSGQENTVK NPTHVPKENF RKHSQPRSFD LKTYKPMGFE SSFLKFIQES EEKEDDFDDW EPSEHLTLSN SSQSSNDLTG NVVANNMVND SEPEVDIPHS SSDSTIHENL TAIPPLIVAE TTTVPSLENL RVVLDKALTD CGELALKQLH YLRPVVVLER SKFSTPILDL FPTKKTDELC VGSS //