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-MAR-2024, entry version 237. 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; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 52-61; 78-83 AND RP 128-136. RX 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 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 a RT ubiquitously expressed subfamily of related but distinct proteins encoded RT by genes mapping to different chromosomes."; RL J. Biol. Chem. 270:28780-28789(1995). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., 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., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., 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 project: RT 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 MET-2, RP AND IDENTIFICATION BY 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., Golemis E.A.; RT "Evidence that Dim1 associates with proteins involved in pre-mRNA splicing, RT and delineation of residues essential for Dim1 interactions with hnRNP F RT and Npw38/PQBP-1."; RL Gene 257:33-43(2000). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPLICEOSOMAL RP 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 IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [12] 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 [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [14] RP INTERACTION WITH AGO1 AND AGO2. RX PubMed=17932509; DOI=10.1038/sj.embor.7401088; RA Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M., RA Urlaub H., Meister G.; RT "Proteomic and functional analysis of Argonaute-containing mRNA-protein RT complexes in human cells."; RL EMBO Rep. 8:1052-1060(2007). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND MET-2, CLEAVAGE OF RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [19] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-224, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., 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 [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND SER-187, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). 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., Buerckstuemmer T., RA 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [23] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [24] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND MET-2, CLEAVAGE OF RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104; SER-107; SER-193; RP THR-215 AND SER-265, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [27] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-200, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [28] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [29] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-87; LYS-167; LYS-185; LYS-200 AND RP LYS-224, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [30] RP STRUCTURE BY NMR OF 1-102; 103-194 AND 277-381 IN COMPLEX WITH BCL-X RNA, RP 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 human RT hnRNP F and interaction studies with Bcl-x G-tract RNA: a novel mode of RNA RT recognition."; RL Nucleic Acids Res. 34:3634-3645(2006). RN [31] 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 quasi- RT 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 events CC that pre-mRNAs undergo before becoming functional, translatable mRNAs CC in the cytoplasm. Plays a role in the regulation of alternative CC splicing events. Binds G-rich sequences in pre-mRNAs and keeps target CC RNA in an unfolded state. {ECO:0000269|PubMed:20526337}. CC -!- SUBUNIT: Identified in the spliceosome C complex. Interacts with AGO1, CC AGO2, TBP and TXNL4/DIM1. {ECO:0000269|PubMed:11054566, CC ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:16885237, CC ECO:0000269|PubMed:17932509}. CC -!- INTERACTION: CC P52597; Q53H80: AKIRIN2; NbExp=3; IntAct=EBI-352986, EBI-742928; CC P52597; P41238: APOBEC1; NbExp=3; IntAct=EBI-352986, EBI-12819523; CC P52597; Q86V38: ATN1; NbExp=3; IntAct=EBI-352986, EBI-11954292; CC P52597; Q9Y6H3: ATP23; NbExp=3; IntAct=EBI-352986, EBI-12811889; CC P52597; Q9BXC9: BBS2; NbExp=3; IntAct=EBI-352986, EBI-748297; CC P52597; Q5SWW7: C10orf55; NbExp=3; IntAct=EBI-352986, EBI-12809220; CC P52597; Q6P1W5: C1orf94; NbExp=6; IntAct=EBI-352986, EBI-946029; CC P52597; Q8N684-3: CPSF7; NbExp=3; IntAct=EBI-352986, EBI-11523759; CC P52597; Q86Y13: DZIP3; NbExp=6; IntAct=EBI-352986, EBI-948630; CC P52597; Q9NRA8: EIF4ENIF1; NbExp=3; IntAct=EBI-352986, EBI-301024; CC P52597; Q9NVL1-2: FAM86C1P; NbExp=3; IntAct=EBI-352986, EBI-12845222; CC P52597; A0A024R5S0: hCG_2003792; NbExp=3; IntAct=EBI-352986, EBI-10188461; CC P52597; P31943: HNRNPH1; NbExp=3; IntAct=EBI-352986, EBI-351590; CC P52597; P52272: HNRNPM; NbExp=6; IntAct=EBI-352986, EBI-486809; CC P52597; Q9BUJ2: HNRNPUL1; NbExp=5; IntAct=EBI-352986, EBI-1018153; CC P52597; Q96LI6: HSFY2; NbExp=3; IntAct=EBI-352986, EBI-3957665; CC P52597; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-352986, EBI-747204; CC P52597; Q0VD86: INCA1; NbExp=3; IntAct=EBI-352986, EBI-6509505; CC P52597; Q6IPM2: IQCE; NbExp=3; IntAct=EBI-352986, EBI-3893098; CC P52597; Q92993: KAT5; NbExp=3; IntAct=EBI-352986, EBI-399080; CC P52597; Q13351: KLF1; NbExp=3; IntAct=EBI-352986, EBI-8284732; CC P52597; Q9UIH9: KLF15; NbExp=3; IntAct=EBI-352986, EBI-2796400; CC P52597; Q5T749: KPRP; NbExp=3; IntAct=EBI-352986, EBI-10981970; CC P52597; O95678: KRT75; NbExp=3; IntAct=EBI-352986, EBI-2949715; CC P52597; Q8IUC3: KRTAP7-1; NbExp=3; IntAct=EBI-352986, EBI-18394498; CC P52597; Q14847-2: LASP1; NbExp=3; IntAct=EBI-352986, EBI-9088686; CC P52597; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-352986, EBI-11742507; CC P52597; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-352986, EBI-739832; CC P52597; Q9NRX2: MRPL17; NbExp=3; IntAct=EBI-352986, EBI-7825154; CC P52597; O43347: MSI1; NbExp=3; IntAct=EBI-352986, EBI-726515; CC P52597; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-352986, EBI-10271199; CC P52597; Q9BRJ7: NUDT16L1; NbExp=3; IntAct=EBI-352986, EBI-2949792; CC P52597; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-352986, EBI-11022007; CC P52597; Q9NR12: PDLIM7; NbExp=5; IntAct=EBI-352986, EBI-350517; CC P52597; P62937-2: PPIA; NbExp=3; IntAct=EBI-352986, EBI-25884072; CC P52597; P17252: PRKCA; NbExp=3; IntAct=EBI-352986, EBI-1383528; CC P52597; O75360: PROP1; NbExp=3; IntAct=EBI-352986, EBI-9027467; CC P52597; B1ATL7: PRR32; NbExp=3; IntAct=EBI-352986, EBI-18587059; CC P52597; Q9NV39: PRR34; NbExp=3; IntAct=EBI-352986, EBI-11959565; CC P52597; O43251: RBFOX2; NbExp=4; IntAct=EBI-352986, EBI-746056; CC P52597; O43251-10: RBFOX2; NbExp=3; IntAct=EBI-352986, EBI-11963050; CC P52597; Q04864-2: REL; NbExp=3; IntAct=EBI-352986, EBI-10829018; CC P52597; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-352986, EBI-6257312; CC P52597; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-352986, EBI-9090795; CC P52597; Q8ND83: SLAIN1; NbExp=3; IntAct=EBI-352986, EBI-10269374; CC P52597; Q53HV7-2: SMUG1; NbExp=3; IntAct=EBI-352986, EBI-12275818; CC P52597; O60504: SORBS3; NbExp=3; IntAct=EBI-352986, EBI-741237; CC P52597; Q6RVD6: SPATA8; NbExp=3; IntAct=EBI-352986, EBI-8635958; CC P52597; Q96A09: TENT5B; NbExp=3; IntAct=EBI-352986, EBI-752030; CC P52597; Q92734: TFG; NbExp=3; IntAct=EBI-352986, EBI-357061; CC P52597; Q96PF1: TGM7; NbExp=3; IntAct=EBI-352986, EBI-12029034; CC P52597; Q08117: TLE5; NbExp=3; IntAct=EBI-352986, EBI-717810; CC P52597; Q08117-2: TLE5; NbExp=3; IntAct=EBI-352986, EBI-11741437; CC P52597; Q96RU7: TRIB3; NbExp=3; IntAct=EBI-352986, EBI-492476; CC P52597; Q14142: TRIM14; NbExp=3; IntAct=EBI-352986, EBI-2820256; CC P52597; Q9H9P5-5: UNKL; NbExp=3; IntAct=EBI-352986, EBI-12817837; CC P52597; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-352986, EBI-11975223; CC P52597; Q99990: VGLL1; NbExp=3; IntAct=EBI-352986, EBI-11983165; CC P52597; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-352986, EBI-2559305; CC P52597; P61981: YWHAG; NbExp=3; IntAct=EBI-352986, EBI-359832; CC P52597; A0A0C4DGF1: ZBTB32; NbExp=3; IntAct=EBI-352986, EBI-10188476; CC P52597; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-352986, EBI-745520; CC P52597; Q96H86: ZNF764; NbExp=3; IntAct=EBI-352986, EBI-745775; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm. CC -!- TISSUE SPECIFICITY: Expressed ubiquitously. CC -!- DOMAIN: The N-terminal RRM domains are responsible for recognizing the CC G-tract of BCL-X RNA. CC -!- PTM: Sumoylated. {ECO:0000269|PubMed:15161980}. 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; -; NOT_ANNOTATED_CDS; 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 CCDS; CCDS7204.1; -. 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 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 PDB; 3TFY; X-ray; 2.75 A; D/E/F=2-10. DR PDBsum; 2HGL; -. DR PDBsum; 2HGM; -. DR PDBsum; 2HGN; -. DR PDBsum; 2KFY; -. DR PDBsum; 2KG0; -. DR PDBsum; 2KG1; -. DR PDBsum; 3TFY; -. DR AlphaFoldDB; P52597; -. DR SMR; P52597; -. DR BioGRID; 109426; 564. DR CORUM; P52597; -. DR DIP; DIP-33145N; -. DR IntAct; P52597; 189. DR MINT; P52597; -. DR STRING; 9606.ENSP00000400433; -. DR ChEMBL; CHEMBL4523238; -. DR DrugBank; DB12695; Phenethyl Isothiocyanate. DR GlyCosmos; P52597; 1 site, 1 glycan. DR GlyGen; P52597; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P52597; -. DR MetOSite; P52597; -. DR PhosphoSitePlus; P52597; -. DR SwissPalm; P52597; -. DR BioMuta; HNRNPF; -. DR DMDM; 1710628; -. DR OGP; P52597; -. DR EPD; P52597; -. DR jPOST; P52597; -. DR MassIVE; P52597; -. DR MaxQB; P52597; -. DR PaxDb; 9606-ENSP00000400433; -. DR PeptideAtlas; P52597; -. DR PRIDE; P52597; -. DR ProteomicsDB; 56497; -. DR Pumba; P52597; -. DR Antibodypedia; 13432; 401 antibodies from 33 providers. DR DNASU; 3185; -. DR Ensembl; ENST00000337970.7; ENSP00000338477.3; ENSG00000169813.17. DR Ensembl; ENST00000356053.7; ENSP00000348345.3; ENSG00000169813.17. DR Ensembl; ENST00000357065.8; ENSP00000349573.4; ENSG00000169813.17. DR Ensembl; ENST00000443950.6; ENSP00000400433.2; ENSG00000169813.17. DR Ensembl; ENST00000544000.5; ENSP00000438061.1; ENSG00000169813.17. DR Ensembl; ENST00000682386.1; ENSP00000507787.1; ENSG00000169813.17. DR GeneID; 3185; -. DR KEGG; hsa:3185; -. DR MANE-Select; ENST00000682386.1; ENSP00000507787.1; NM_001098204.2; NP_001091674.1. DR UCSC; uc001jar.2; human. DR AGR; HGNC:5039; -. DR CTD; 3185; -. DR DisGeNET; 3185; -. DR GeneCards; HNRNPF; -. DR HGNC; HGNC:5039; HNRNPF. DR HPA; ENSG00000169813; Low tissue specificity. DR MIM; 601037; gene. DR neXtProt; NX_P52597; -. DR OpenTargets; ENSG00000169813; -. DR PharmGKB; PA162391271; -. DR VEuPathDB; HostDB:ENSG00000169813; -. DR eggNOG; KOG4211; Eukaryota. DR GeneTree; ENSGT00940000157838; -. DR HOGENOM; CLU_032003_1_0_1; -. DR InParanoid; P52597; -. DR OMA; SANEQHI; -. DR OrthoDB; 314723at2759; -. DR PhylomeDB; P52597; -. DR TreeFam; TF316157; -. DR PathwayCommons; P52597; -. DR Reactome; R-HSA-6803529; FGFR2 alternative splicing. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA. DR Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation. DR SignaLink; P52597; -. DR BioGRID-ORCS; 3185; 137 hits in 1170 CRISPR screens. DR ChiTaRS; HNRNPF; human. DR EvolutionaryTrace; P52597; -. DR GeneWiki; HNRPF; -. DR GenomeRNAi; 3185; -. DR Pharos; P52597; Tbio. DR PRO; PR:P52597; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; P52597; Protein. DR Bgee; ENSG00000169813; Expressed in ventricular zone and 198 other cell types or tissues. DR ExpressionAtlas; P52597; baseline and differential. DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; TAS:ProtInc. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central. DR GO; GO:0045202; C:synapse; IEA:Ensembl. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB. DR GO; GO:0043484; P:regulation of RNA splicing; IDA:UniProtKB. DR GO; GO:0006396; P:RNA processing; TAS:ProtInc. DR CDD; cd12729; RRM1_hnRNPH_hnRNPH2_hnRNPF; 1. DR CDD; cd12731; RRM2_hnRNPH_hnRNPH2_hnRNPF; 1. DR CDD; cd12506; RRM3_hnRNPH_CRSF1_like; 1. DR DisProt; DP01736; -. DR Gene3D; 3.30.70.330; -; 3. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR000504; RRM_dom. DR InterPro; IPR012996; Znf_CHHC. DR PANTHER; PTHR13976:SF32; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN F; 1. DR PANTHER; PTHR13976; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN-RELATED; 1. DR Pfam; PF00076; RRM_1; 2. DR Pfam; PF08080; zf-RNPHF; 1. DR SMART; SM00360; RRM; 3. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 3. DR PROSITE; PS50102; RRM; 2. DR Genevisible; P52597; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Direct protein sequencing; Isopeptide bond; KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Ribonucleoprotein; RNA-binding; Spliceosome; KW Ubl conjugation. FT CHAIN 1..415 FT /note="Heterogeneous nuclear ribonucleoprotein F" FT /id="PRO_0000367114" FT INIT_MET 1 FT /note="Removed; alternate" FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT CHAIN 2..415 FT /note="Heterogeneous nuclear ribonucleoprotein F, N- FT terminally processed" FT /id="PRO_0000081852" FT DOMAIN 13..85 FT /note="RRM 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 111..188 FT /note="RRM 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 289..366 FT /note="RRM 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT REGION 81..86 FT /note="Interaction with RNA" FT REGION 179..184 FT /note="Interaction with RNA" FT REGION 355..360 FT /note="Interaction with RNA" FT SITE 16 FT /note="Interaction with RNA" FT SITE 20 FT /note="Interaction with RNA" FT SITE 52 FT /note="Interaction with RNA" FT SITE 75 FT /note="Interaction with RNA" FT SITE 116 FT /note="Interaction with RNA" FT SITE 120 FT /note="Interaction with RNA" FT SITE 150 FT /note="Interaction with RNA" FT SITE 173 FT /note="Interaction with RNA" FT SITE 294 FT /note="Interaction with RNA" FT SITE 298 FT /note="Interaction with RNA" FT SITE 326 FT /note="Interaction with RNA" FT SITE 349 FT /note="Interaction with RNA" FT MOD_RES 1 FT /note="N-acetylmethionine; in Heterogeneous nuclear FT ribonucleoprotein F; alternate" FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22814378" FT MOD_RES 2 FT /note="N-acetylmethionine; in Heterogeneous nuclear FT ribonucleoprotein F, N-terminally processed" FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT MOD_RES 104 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19369195, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 107 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 161 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332" FT MOD_RES 187 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 193 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 195 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q794E4" FT MOD_RES 200 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9Z2X1" FT MOD_RES 215 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 224 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 265 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 72 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000269|PubMed:15161980" FT CROSSLNK 87 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 167 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 185 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 200 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 224 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 87 FT /note="K -> R (in dbSNP:rs17851426)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_027999" FT MUTAGEN 20 FT /note="W->A: Loss of RNA-binding." FT /evidence="ECO:0000269|PubMed:20526337" FT MUTAGEN 84 FT /note="E->A: Loss of RNA-binding." FT /evidence="ECO:0000269|PubMed:20526337" FT MUTAGEN 116 FT /note="R->A: Decreases affinity for RNA oligonucleotide FT 100-fold." FT /evidence="ECO:0000269|PubMed:20526337" FT MUTAGEN 120 FT /note="F->A: Little disruption of binding RNA. Decreases FT affinity for RNA oligonucleotide 100-fold. Abrogates FT RNA-binding; when associated with A-180." FT /evidence="ECO:0000269|PubMed:16885237, FT ECO:0000269|PubMed:20526337" FT MUTAGEN 150 FT /note="K->A: No effect on affinity for RNA FT oligonucleotide." FT /evidence="ECO:0000269|PubMed:20526337" FT MUTAGEN 156 FT /note="F->A: Drastically effects folding of RRM2." FT /evidence="ECO:0000269|PubMed:16885237" FT MUTAGEN 173 FT /note="K->A: Minimal effect on affinity for RNA FT oligonucleotide." FT /evidence="ECO:0000269|PubMed:20526337" FT MUTAGEN 178 FT /note="H->A: Little disruption of binding RNA." FT /evidence="ECO:0000269|PubMed:16885237" FT MUTAGEN 179 FT /note="R->A: Decreases affinity for RNA oligonucleotide FT 100-fold." FT /evidence="ECO:0000269|PubMed:20526337" FT MUTAGEN 180 FT /note="Y->A: Decreases affinity for RNA oligonucleotide FT 10-fold. Abrogates RNA-binding; when associated with FT A-120." FT /evidence="ECO:0000269|PubMed:16885237, FT ECO:0000269|PubMed:20526337" FT MUTAGEN 182 FT /note="E->A: Decreases affinity for RNA oligonucleotide FT 100-fold." FT /evidence="ECO:0000269|PubMed:20526337" FT MUTAGEN 184 FT /note="F->A: Minimal effect on affinity for RNA FT oligonucleotide." FT /evidence="ECO:0000269|PubMed:20526337" FT STRAND 12..17 FT /evidence="ECO:0007829|PDB:2HGL" FT HELIX 24..30 FT /evidence="ECO:0007829|PDB:2HGL" FT TURN 31..33 FT /evidence="ECO:0007829|PDB:2HGL" FT STRAND 37..40 FT /evidence="ECO:0007829|PDB:2HGL" FT STRAND 43..47 FT /evidence="ECO:0007829|PDB:2HGL" FT STRAND 49..51 FT /evidence="ECO:0007829|PDB:2HGL" FT STRAND 53..60 FT /evidence="ECO:0007829|PDB:2HGL" FT HELIX 64..71 FT /evidence="ECO:0007829|PDB:2HGL" FT TURN 72..74 FT /evidence="ECO:0007829|PDB:2HGL" FT STRAND 75..87 FT /evidence="ECO:0007829|PDB:2HGL" FT HELIX 90..97 FT /evidence="ECO:0007829|PDB:2HGL" FT STRAND 107..109 FT /evidence="ECO:0007829|PDB:2HGM" FT STRAND 112..116 FT /evidence="ECO:0007829|PDB:2HGM" FT HELIX 124..130 FT /evidence="ECO:0007829|PDB:2HGM" FT TURN 131..133 FT /evidence="ECO:0007829|PDB:2HGM" FT STRAND 136..142 FT /evidence="ECO:0007829|PDB:2HGM" FT STRAND 147..151 FT /evidence="ECO:0007829|PDB:2HGM" FT STRAND 153..161 FT /evidence="ECO:0007829|PDB:2HGM" FT HELIX 164..169 FT /evidence="ECO:0007829|PDB:2HGM" FT TURN 170..173 FT /evidence="ECO:0007829|PDB:2HGM" FT STRAND 175..180 FT /evidence="ECO:0007829|PDB:2KG0" FT STRAND 184..186 FT /evidence="ECO:0007829|PDB:2HGM" FT HELIX 188..191 FT /evidence="ECO:0007829|PDB:2HGM" FT STRAND 284..294 FT /evidence="ECO:0007829|PDB:2KG1" FT HELIX 302..309 FT /evidence="ECO:0007829|PDB:2HGN" FT STRAND 315..318 FT /evidence="ECO:0007829|PDB:2HGN" FT STRAND 322..325 FT /evidence="ECO:0007829|PDB:2HGN" FT STRAND 332..334 FT /evidence="ECO:0007829|PDB:2HGN" FT HELIX 337..344 FT /evidence="ECO:0007829|PDB:2HGN" FT STRAND 351..354 FT /evidence="ECO:0007829|PDB:2HGN" FT STRAND 358..362 FT /evidence="ECO:0007829|PDB:2KG1" FT STRAND 368..371 FT /evidence="ECO:0007829|PDB:2KG1" FT STRAND 377..379 FT /evidence="ECO:0007829|PDB:2KG1" 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 //