ID HNRPF_HUMAN Reviewed; 415 AA. AC P52597; B3KM84; Q5T0N2; Q96AU2; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-JUL-2011, entry version 131. DE RecName: Full=Heterogeneous nuclear ribonucleoprotein F; DE Short=hnRNP F; DE AltName: Full=Nucleolin-like protein mcs94-1; DE Contains: DE RecName: Full=Heterogeneous nuclear ribonucleoprotein F, N-terminally processed; GN Name=HNRNPF; Synonyms=HNRPF; 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], AND PROTEIN SEQUENCE OF 52-61; 78-83 AND RP 128-136. RX MEDLINE=94203790; PubMed=7512260; DOI=10.1093/nar/22.6.1059; RA Matunis M.J., Xing J., Dreyfuss G.; RT "The hnRNP F protein: unique primary structure, nucleic acid-binding RT properties, and subcellular localization."; RL Nucleic Acids Res. 22:1059-1067(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RX MEDLINE=96081943; PubMed=7499401; DOI=10.1074/jbc.270.48.28780; RA Honore B., Rasmussen H.H., Vorum H., Dejgaard K., Liu X., Gromov P., RA Madsen P., Gesser B., Tommerup N., Celis J.E.; RT "Heterogeneous nuclear ribonucleoproteins H, H', and F are members of RT a ubiquitously expressed subfamily of related but distinct proteins RT encoded by genes mapping to different chromosomes."; RL J. Biol. Chem. 270:28780-28789(1995). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=92307667; PubMed=1351868; DOI=10.1016/0888-7543(92)90251-M; RA McDonald H., Smailus D., Jenkins H., Adams K., Simpson N.E., RA Goodfellow P.J.; RT "Identification and characterization of a gene at D10S94 in the MEN2A RT region."; RL Genomics 13:344-348(1992). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-87. RC TISSUE=Bone marrow, Lung, Ovary, Placenta, and Uterus; 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 [8] RP PROTEIN SEQUENCE OF 1-14; 53-68; 82-87; 99-114; 151-167; 180-185 AND RP 300-347, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1 AND RP MET-2, AND MASS SPECTROMETRY. RC TISSUE=B-cell lymphoma, and Colon carcinoma; RA Bienvenut W.V., Zebisch A., Kolch W.; RL Submitted (OCT-2008) to UniProtKB. RN [9] RP INTERACTION WITH TXNL4. RX PubMed=11054566; DOI=10.1016/S0378-1119(00)00372-3; RA Zhang Y.-Z., Lindblom T., Chang A., Sudol M., Sluder A.E., RA Golemis E.A.; RT "Evidence that Dim1 associates with proteins involved in pre-mRNA RT splicing, and delineation of residues essential for Dim1 interactions RT with hnRNP F and Npw38/PQBP-1."; RL Gene 257:33-43(2000). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE RP SPLICEOSOMAL C COMPLEX. RX PubMed=11991638; DOI=10.1017/S1355838202021088; RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.; RT "Purification and characterization of native spliceosomes suitable for RT three-dimensional structural analysis."; RL RNA 8:426-439(2002). RN [11] RP SUMOYLATION AT LYS-72. RX PubMed=15161980; DOI=10.1073/pnas.0402889101; RA Li T., Evdokimov E., Shen R.F., Chao C.C., Tekle E., Wang T., RA Stadtman E.R., Yang D.C., Chock P.B.; RT "Sumoylation of heterogeneous nuclear ribonucleoproteins, zinc finger RT proteins, and nuclear pore complex proteins: a proteomic analysis."; RL Proc. Natl. Acad. Sci. U.S.A. 101:8551-8556(2004). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, AND MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=15302935; DOI=10.1073/pnas.0404720101; RA Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., RA Li J., Cohn M.A., Cantley L.C., Gygi S.P.; RT "Large-scale characterization of HeLa cell nuclear phosphoproteins."; RL Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-246, AND MASS RP SPECTROMETRY. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer RT cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND MASS RP SPECTROMETRY. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, 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). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187 AND SER-310, AND RP MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [18] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND MET-2, AND MASS RP SPECTROMETRY. RC TISSUE=Embryonic kidney; RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND SER-310, AND RP MASS SPECTROMETRY. RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [20] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-87 AND LYS-224, AND MASS RP SPECTROMETRY. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [22] RP STRUCTURE BY NMR OF 1-102; 103-194 AND 277-381 IN COMPLEX WITH BCL-X RP RNA, AND MUTAGENESIS OF PHE-120; PHE-156; HIS-178 AND TYR-180. RX PubMed=16885237; DOI=10.1093/nar/gkl488; RA Dominguez C., Allain F.H.; RT "NMR structure of the three quasi RNA recognition motifs (qRRMs) of RT human hnRNP F and interaction studies with Bcl-x G-tract RNA: a novel RT mode of RNA recognition."; RL Nucleic Acids Res. 34:3634-3645(2006). RN [23] RP STRUCTURE BY NMR OF 1-194 AND 277-381 IN COMPLEXES WITH AGGGAU RNA RP OLIGONUCLEOTIDE, FUNCTION, AND MUTAGENESIS OF TRP-20; GLU-84; ARG-116; RP PHE-120; LYS-150; LYS-173; ARG-179; TYR-180; GLU-182 AND PHE-184. RX PubMed=20526337; DOI=10.1038/nsmb.1814; RA Dominguez C., Fisette J.F., Chabot B., Allain F.H.; RT "Structural basis of G-tract recognition and encaging by hnRNP F RT quasi-RRMs."; RL Nat. Struct. Mol. Biol. 17:853-861(2010). CC -!- FUNCTION: Component of the heterogeneous nuclear ribonucleoprotein CC (hnRNP) complexes which provide the substrate for the processing CC events that pre-mRNAs undergo before becoming functional, CC translatable mRNAs in the cytoplasm. Plays a role in the CC regulation of alternative splicing events. Binds G-rich sequences CC in pre-mRNAs and keeps target RNA in an unfolded state. CC -!- SUBUNIT: Identified in the spliceosome C complex. Interacts with CC TBP and TXNL4/DIM1. CC -!- INTERACTION: CC Q92597:NDRG1; NbExp=1; IntAct=EBI-352986, EBI-716486; CC P50616:TOB1; NbExp=1; IntAct=EBI-352986, EBI-723281; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm. CC -!- TISSUE SPECIFICITY: Expressed ubiquitously. CC -!- DOMAIN: The N-terminal RRM domains are responsible for recognizing CC the G-tract of BCL-X RNA. CC -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. CC -!- PTM: Sumoylated. CC -!- SIMILARITY: Contains 3 RRM (RNA recognition motif) domains. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L28010; AAC37584.1; -; mRNA. DR EMBL; AL512654; CAI17066.1; -; Genomic_DNA. DR EMBL; AK001364; BAG50896.1; -; mRNA. DR EMBL; CH471160; EAW86595.1; -; Genomic_DNA. DR EMBL; BC001432; AAH01432.1; -; mRNA. DR EMBL; BC004254; AAH04254.1; -; mRNA. DR EMBL; BC015580; AAH15580.1; -; mRNA. DR EMBL; BC016736; AAH16736.1; -; mRNA. DR EMBL; BC106008; AAI06009.1; -; mRNA. DR IPI; IPI00003881; -. DR PIR; S43484; S43484. DR RefSeq; NP_001091674.1; NM_001098204.1. DR RefSeq; NP_001091675.1; NM_001098205.1. DR RefSeq; NP_001091676.1; NM_001098206.1. DR RefSeq; NP_001091677.1; NM_001098207.1. DR RefSeq; NP_001091678.1; NM_001098208.1. DR RefSeq; NP_004957.1; NM_004966.3. DR UniGene; Hs.712955; -. DR UniGene; Hs.808; -. DR PDB; 2HGL; NMR; -; A=1-102. DR PDB; 2HGM; NMR; -; A=103-194. DR PDB; 2HGN; NMR; -; A=277-381. DR PDB; 2KFY; NMR; -; A=1-102. DR PDB; 2KG0; NMR; -; A=103-194. DR PDB; 2KG1; NMR; -; A=277-381. DR PDBsum; 2HGL; -. DR PDBsum; 2HGM; -. DR PDBsum; 2HGN; -. DR PDBsum; 2KFY; -. DR PDBsum; 2KG0; -. DR PDBsum; 2KG1; -. DR ProteinModelPortal; P52597; -. DR SMR; P52597; 1-194, 287-367. DR IntAct; P52597; 24. DR MINT; MINT-1157890; -. DR STRING; P52597; -. DR PhosphoSite; P52597; -. DR Aarhus/Ghent-2DPAGE; 6304; IEF. DR Aarhus/Ghent-2DPAGE; 7312; IEF. DR OGP; P52597; -. DR PeptideAtlas; P52597; -. DR PRIDE; P52597; -. DR Ensembl; ENST00000337970; ENSP00000338477; ENSG00000169813. DR Ensembl; ENST00000356053; ENSP00000348345; ENSG00000169813. DR Ensembl; ENST00000357065; ENSP00000349573; ENSG00000169813. DR Ensembl; ENST00000443950; ENSP00000400433; ENSG00000169813. DR GeneID; 3185; -. DR KEGG; hsa:3185; -. DR UCSC; uc001jar.2; human. DR CTD; 3185; -. DR GeneCards; GC10M040407; -. DR H-InvDB; HIX0008779; -. DR HGNC; HGNC:5039; HNRNPF. DR HPA; HPA016884; -. DR MIM; 601037; gene. DR neXtProt; NX_P52597; -. DR PharmGKB; PA162391271; -. DR eggNOG; prNOG11489; -. DR HOGENOM; HBG447282; -. DR HOVERGEN; HBG055557; -. DR InParanoid; P52597; -. DR OMA; SADTAND; -. DR OrthoDB; EOG4CRM03; -. DR PhylomeDB; P52597; -. DR Reactome; REACT_1675; mRNA Processing. DR Reactome; REACT_71; Gene Expression. DR NextBio; 12654; -. DR ArrayExpress; P52597; -. DR Bgee; P52597; -. DR CleanEx; HS_HNRNPF; -. DR Genevestigator; P52597; -. DR GermOnline; ENSG00000169813; Homo sapiens. DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:HPA. DR GO; GO:0030530; C:heterogeneous nuclear ribonucleoprotein complex; TAS:ProtInc. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB. DR GO; GO:0043484; P:regulation of RNA splicing; IDA:UniProtKB. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait. DR InterPro; IPR000504; RRM_dom. DR InterPro; IPR012996; Znf_CHHC. DR Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 3. DR Pfam; PF00076; RRM_1; 2. DR Pfam; PF08080; zf-RNPHF; 1. DR SMART; SM00360; RRM; 3. DR PROSITE; PS50102; RRM; 2. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Complete proteome; KW Direct protein sequencing; Isopeptide bond; mRNA processing; KW mRNA splicing; Nucleus; Phosphoprotein; Polymorphism; Repeat; KW Ribonucleoprotein; RNA-binding; Spliceosome; Ubl conjugation. FT CHAIN 1 415 Heterogeneous nuclear ribonucleoprotein FT F. FT /FTId=PRO_0000367114. FT INIT_MET 1 1 Removed; alternate. FT CHAIN 2 415 Heterogeneous nuclear ribonucleoprotein FT F, N-terminally processed. FT /FTId=PRO_0000081852. FT DOMAIN 13 85 RRM 1. FT DOMAIN 111 188 RRM 2. FT DOMAIN 289 366 RRM 3. FT REGION 81 86 Interaction with RNA. FT REGION 179 184 Interaction with RNA. FT REGION 355 360 Interaction with RNA. FT SITE 16 16 Interaction with RNA. FT SITE 20 20 Interaction with RNA. FT SITE 52 52 Interaction with RNA. FT SITE 75 75 Interaction with RNA. FT SITE 116 116 Interaction with RNA. FT SITE 120 120 Interaction with RNA. FT SITE 150 150 Interaction with RNA. FT SITE 173 173 Interaction with RNA. FT SITE 294 294 Interaction with RNA. FT SITE 298 298 Interaction with RNA. FT SITE 326 326 Interaction with RNA. FT SITE 349 349 Interaction with RNA. FT MOD_RES 1 1 N-acetylmethionine; in Heterogeneous FT nuclear ribonucleoprotein F; alternate. FT MOD_RES 2 2 N-acetylmethionine; in Heterogeneous FT nuclear ribonucleoprotein F, N-terminally FT processed. FT MOD_RES 87 87 N6-acetyllysine. FT MOD_RES 104 104 Phosphoserine. FT MOD_RES 161 161 Phosphoserine. FT MOD_RES 187 187 Phosphoserine. FT MOD_RES 224 224 N6-acetyllysine. FT MOD_RES 246 246 Phosphotyrosine. FT MOD_RES 310 310 Phosphoserine. FT CROSSLNK 72 72 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO). FT VARIANT 87 87 K -> R (in dbSNP:rs17851426). FT /FTId=VAR_027999. FT MUTAGEN 20 20 W->A: Loss of RNA-binding. FT MUTAGEN 84 84 E->A: Loss of RNA-binding. FT MUTAGEN 116 116 R->A: Decreases affinity for RNA FT oligonucleotide 100-fold. FT MUTAGEN 120 120 F->A: Little disruption of binding RNA. FT Decreases affinity for RNA FT oligonucleotide 100-fold. Abrogates RNA- FT binding; when associated with A-180. FT MUTAGEN 150 150 K->A: No effect on affinity for RNA FT oligonucleotide. FT MUTAGEN 156 156 F->A: Drastically effects folding of FT RRM2. FT MUTAGEN 173 173 K->A: Minimal effect on affinity for RNA FT oligonucleotide. FT MUTAGEN 178 178 H->A: Little disruption of binding RNA. FT MUTAGEN 179 179 R->A: Decreases affinity for RNA FT oligonucleotide 100-fold. FT MUTAGEN 180 180 Y->A: Decreases affinity for RNA FT oligonucleotide 10-fold. Abrogates RNA- FT binding; when associated with A-120. FT MUTAGEN 182 182 E->A: Decreases affinity for RNA FT oligonucleotide 100-fold. FT MUTAGEN 184 184 F->A: Minimal effect on affinity for RNA FT oligonucleotide. FT STRAND 107 109 FT STRAND 112 116 FT HELIX 124 130 FT TURN 131 133 FT STRAND 136 142 FT STRAND 147 151 FT STRAND 153 161 FT HELIX 164 169 FT TURN 170 173 FT STRAND 184 186 FT HELIX 188 191 FT HELIX 302 309 FT STRAND 315 318 FT STRAND 322 325 FT STRAND 332 334 FT HELIX 337 344 FT STRAND 351 354 SQ SEQUENCE 415 AA; 45672 MW; D14E170631FB1F31 CRC64; MMLGPEGGEG FVVKLRGLPW SCSVEDVQNF LSDCTIHDGA AGVHFIYTRE GRQSGEAFVE LGSEDDVKMA LKKDRESMGH RYIEVFKSHR TEMDWVLKHS GPNSADSAND GFVRLRGLPF GCTKEEIVQF FSGLEIVPNG ITLPVDPEGK ITGEAFVQFA SQELAEKALG KHKERIGHRY IEVFKSSQEE VRSYSDPPLK FMSVQRPGPY DRPGTARRYI GIVKQAGLER MRPGAYSTGY GGYEEYSGLS DGYGFTTDLF GRDLSYCLSG MYDHRYGDSE FTVQSTTGHC VHMRGLPYKA TENDIYNFFS PLNPVRVHIE IGPDGRVTGE ADVEFATHEE AVAAMSKDRA NMQHRYIELF LNSTTGASNG AYSSQVMQGM GVSAAQATYS GLESQSVSGC YGAGYSGQNS MGGYD //