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Heterogeneous nuclear ribonucleoprotein F (hnRNP F) (Nucleolin-like protein mcs94-1) [Cleaved into: Heterogeneous nuclear ribonucleoprotein F, N-terminally processed]

 HNRPF_HUMAN             Reviewed;         415 AA.
P52597; B3KM84; Q5T0N2; Q96AU2;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 196.
RecName: Full=Heterogeneous nuclear ribonucleoprotein F;
Short=hnRNP F;
AltName: Full=Nucleolin-like protein mcs94-1;
Contains:
RecName: Full=Heterogeneous nuclear ribonucleoprotein F, N-terminally processed;
Name=HNRNPF; Synonyms=HNRPF;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 52-61; 78-83 AND
128-136.
PubMed=7512260; DOI=10.1093/nar/22.6.1059;
Matunis M.J., Xing J., Dreyfuss G.;
"The hnRNP F protein: unique primary structure, nucleic acid-binding
properties, and subcellular localization.";
Nucleic Acids Res. 22:1059-1067(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=7499401; DOI=10.1074/jbc.270.48.28780;
Honore B., Rasmussen H.H., Vorum H., Dejgaard K., Liu X., Gromov P.,
Madsen P., Gesser B., Tommerup N., Celis J.E.;
"Heterogeneous nuclear ribonucleoproteins H, H', and F are members of
a ubiquitously expressed subfamily of related but distinct proteins
encoded by genes mapping to different chromosomes.";
J. Biol. Chem. 270:28780-28789(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1351868; DOI=10.1016/0888-7543(92)90251-M;
McDonald H., Smailus D., Jenkins H., Adams K., Simpson N.E.,
Goodfellow P.J.;
"Identification and characterization of a gene at D10S94 in the MEN2A
region.";
Genomics 13:344-348(1992).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-87.
TISSUE=Bone marrow, Lung, Ovary, Placenta, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 1-14; 53-68; 82-87; 99-114; 151-167; 180-185 AND
300-347, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1 AND
MET-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=B-cell lymphoma, and Colon carcinoma;
Bienvenut W.V., Zebisch A., Kolch W.;
Submitted (OCT-2008) to UniProtKB.
[9]
INTERACTION WITH TXNL4.
PubMed=11054566; DOI=10.1016/S0378-1119(00)00372-3;
Zhang Y.-Z., Lindblom T., Chang A., Sudol M., Sluder A.E.,
Golemis E.A.;
"Evidence that Dim1 associates with proteins involved in pre-mRNA
splicing, and delineation of residues essential for Dim1 interactions
with hnRNP F and Npw38/PQBP-1.";
Gene 257:33-43(2000).
[10]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
SPLICEOSOMAL C COMPLEX.
PubMed=11991638; DOI=10.1017/S1355838202021088;
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
"Purification and characterization of native spliceosomes suitable for
three-dimensional structural analysis.";
RNA 8:426-439(2002).
[11]
SUMOYLATION AT LYS-72.
PubMed=15161980; DOI=10.1073/pnas.0402889101;
Li T., Evdokimov E., Shen R.F., Chao C.C., Tekle E., Wang T.,
Stadtman E.R., Yang D.C., Chock P.B.;
"Sumoylation of heterogeneous nuclear ribonucleoproteins, zinc finger
proteins, and nuclear pore complex proteins: a proteomic analysis.";
Proc. Natl. Acad. Sci. U.S.A. 101:8551-8556(2004).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[13]
INTERACTION WITH AGO1 AND AGO2.
PubMed=17932509; DOI=10.1038/sj.embor.7401088;
Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M.,
Urlaub H., Meister G.;
"Proteomic and functional analysis of Argonaute-containing mRNA-
protein complexes in human cells.";
EMBO Rep. 8:1052-1060(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND MET-2, CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-224, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND SER-187, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[23]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND MET-2, CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104; SER-107; SER-193;
THR-215 AND SER-265, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[26]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-200, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[28]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-87; LYS-167; LYS-185;
LYS-200 AND LYS-224, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[29]
STRUCTURE BY NMR OF 1-102; 103-194 AND 277-381 IN COMPLEX WITH BCL-X
RNA, AND MUTAGENESIS OF PHE-120; PHE-156; HIS-178 AND TYR-180.
PubMed=16885237; DOI=10.1093/nar/gkl488;
Dominguez C., Allain F.H.;
"NMR structure of the three quasi RNA recognition motifs (qRRMs) of
human hnRNP F and interaction studies with Bcl-x G-tract RNA: a novel
mode of RNA recognition.";
Nucleic Acids Res. 34:3634-3645(2006).
[30]
STRUCTURE BY NMR OF 1-194 AND 277-381 IN COMPLEXES WITH AGGGAU RNA
OLIGONUCLEOTIDE, FUNCTION, AND MUTAGENESIS OF TRP-20; GLU-84; ARG-116;
PHE-120; LYS-150; LYS-173; ARG-179; TYR-180; GLU-182 AND PHE-184.
PubMed=20526337; DOI=10.1038/nsmb.1814;
Dominguez C., Fisette J.F., Chabot B., Allain F.H.;
"Structural basis of G-tract recognition and encaging by hnRNP F
quasi-RRMs.";
Nat. Struct. Mol. Biol. 17:853-861(2010).
-!- FUNCTION: Component of the heterogeneous nuclear ribonucleoprotein
(hnRNP) complexes which provide the substrate for the processing
events that pre-mRNAs undergo before becoming functional,
translatable mRNAs in the cytoplasm. Plays a role in the
regulation of alternative splicing events. Binds G-rich sequences
in pre-mRNAs and keeps target RNA in an unfolded state.
{ECO:0000269|PubMed:20526337}.
-!- SUBUNIT: Identified in the spliceosome C complex. Interacts with
AGO1, AGO2, TBP and TXNL4/DIM1. {ECO:0000269|PubMed:11054566,
ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:16885237,
ECO:0000269|PubMed:17932509}.
-!- INTERACTION:
Q08117:AES; NbExp=3; IntAct=EBI-352986, EBI-717810;
Q6P1W5:C1orf94; NbExp=5; IntAct=EBI-352986, EBI-946029;
Q86Y13:DZIP3; NbExp=5; IntAct=EBI-352986, EBI-948630;
Q9NRA8:EIF4ENIF1; NbExp=3; IntAct=EBI-352986, EBI-301024;
P52272:HNRNPM; NbExp=7; IntAct=EBI-352986, EBI-486809;
Q9BUJ2:HNRNPUL1; NbExp=4; IntAct=EBI-352986, EBI-1018153;
Q96LI6:HSFY2; NbExp=3; IntAct=EBI-352986, EBI-3957665;
Q9UKT9:IKZF3; NbExp=3; IntAct=EBI-352986, EBI-747204;
Q9UIH9:KLF15; NbExp=4; IntAct=EBI-352986, EBI-2796400;
Q9HBE1-4:PATZ1; NbExp=4; IntAct=EBI-352986, EBI-11022007;
O43251:RBFOX2; NbExp=4; IntAct=EBI-352986, EBI-746056;
O60504:SORBS3; NbExp=4; IntAct=EBI-352986, EBI-741237;
Q92734:TFG; NbExp=3; IntAct=EBI-352986, EBI-357061;
-!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm.
-!- TISSUE SPECIFICITY: Expressed ubiquitously.
-!- DOMAIN: The N-terminal RRM domains are responsible for recognizing
the G-tract of BCL-X RNA.
-!- PTM: Sumoylated. {ECO:0000269|PubMed:15161980}.
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EMBL; L28010; AAC37584.1; -; mRNA.
EMBL; AL512654; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AK001364; BAG50896.1; -; mRNA.
EMBL; CH471160; EAW86595.1; -; Genomic_DNA.
EMBL; BC001432; AAH01432.1; -; mRNA.
EMBL; BC004254; AAH04254.1; -; mRNA.
EMBL; BC015580; AAH15580.1; -; mRNA.
EMBL; BC016736; AAH16736.1; -; mRNA.
EMBL; BC106008; AAI06009.1; -; mRNA.
CCDS; CCDS7204.1; -.
PIR; S43484; S43484.
RefSeq; NP_001091674.1; NM_001098204.1.
RefSeq; NP_001091675.1; NM_001098205.1.
RefSeq; NP_001091676.1; NM_001098206.1.
RefSeq; NP_001091677.1; NM_001098207.1.
RefSeq; NP_001091678.1; NM_001098208.1.
RefSeq; NP_004957.1; NM_004966.3.
UniGene; Hs.712955; -.
UniGene; Hs.808; -.
PDB; 2HGL; NMR; -; A=1-102.
PDB; 2HGM; NMR; -; A=103-194.
PDB; 2HGN; NMR; -; A=277-381.
PDB; 2KFY; NMR; -; A=1-102.
PDB; 2KG0; NMR; -; A=103-194.
PDB; 2KG1; NMR; -; A=277-381.
PDB; 3TFY; X-ray; 2.75 A; D/E/F=2-10.
PDBsum; 2HGL; -.
PDBsum; 2HGM; -.
PDBsum; 2HGN; -.
PDBsum; 2KFY; -.
PDBsum; 2KG0; -.
PDBsum; 2KG1; -.
PDBsum; 3TFY; -.
ProteinModelPortal; P52597; -.
SMR; P52597; -.
BioGrid; 109426; 180.
CORUM; P52597; -.
DIP; DIP-33145N; -.
IntAct; P52597; 120.
MINT; MINT-1157890; -.
STRING; 9606.ENSP00000338477; -.
iPTMnet; P52597; -.
PhosphoSitePlus; P52597; -.
SwissPalm; P52597; -.
BioMuta; HNRNPF; -.
DMDM; 1710628; -.
OGP; P52597; -.
EPD; P52597; -.
MaxQB; P52597; -.
PaxDb; P52597; -.
PeptideAtlas; P52597; -.
PRIDE; P52597; -.
DNASU; 3185; -.
Ensembl; ENST00000337970; ENSP00000338477; ENSG00000169813.
Ensembl; ENST00000356053; ENSP00000348345; ENSG00000169813.
Ensembl; ENST00000357065; ENSP00000349573; ENSG00000169813.
Ensembl; ENST00000443950; ENSP00000400433; ENSG00000169813.
Ensembl; ENST00000544000; ENSP00000438061; ENSG00000169813.
GeneID; 3185; -.
KEGG; hsa:3185; -.
UCSC; uc001jar.2; human.
CTD; 3185; -.
DisGeNET; 3185; -.
EuPathDB; HostDB:ENSG00000169813.16; -.
GeneCards; HNRNPF; -.
HGNC; HGNC:5039; HNRNPF.
HPA; HPA016884; -.
HPA; HPA069667; -.
MIM; 601037; gene.
neXtProt; NX_P52597; -.
OpenTargets; ENSG00000169813; -.
PharmGKB; PA162391271; -.
eggNOG; KOG4211; Eukaryota.
eggNOG; ENOG410Z6M0; LUCA.
GeneTree; ENSGT00760000119102; -.
HOGENOM; HOG000220896; -.
HOVERGEN; HBG055557; -.
InParanoid; P52597; -.
KO; K12898; -.
OMA; FLSECKI; -.
OrthoDB; EOG091G0CTJ; -.
PhylomeDB; P52597; -.
TreeFam; TF316157; -.
Reactome; R-HSA-6803529; FGFR2 alternative splicing.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
ChiTaRS; HNRNPF; human.
EvolutionaryTrace; P52597; -.
GeneWiki; HNRPF; -.
GenomeRNAi; 3185; -.
PRO; PR:P52597; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000169813; -.
CleanEx; HS_HNRNPF; -.
ExpressionAtlas; P52597; baseline and differential.
Genevisible; P52597; HS.
GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
GO; GO:0017025; F:TBP-class protein binding; IEA:Ensembl.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0035722; P:interleukin-12-mediated signaling pathway; TAS:Reactome.
GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
GO; GO:0043484; P:regulation of RNA splicing; IDA:UniProtKB.
GO; GO:0016070; P:RNA metabolic process; TAS:Reactome.
GO; GO:0006396; P:RNA processing; TAS:ProtInc.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
InterPro; IPR012996; Znf_CHHC.
Pfam; PF00076; RRM_1; 2.
Pfam; PF08080; zf-RNPHF; 1.
SMART; SM00360; RRM; 3.
SUPFAM; SSF54928; SSF54928; 3.
PROSITE; PS50102; RRM; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; Isopeptide bond; mRNA processing;
mRNA splicing; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
Spliceosome; Ubl conjugation.
CHAIN 1 415 Heterogeneous nuclear ribonucleoprotein
F.
/FTId=PRO_0000367114.
INIT_MET 1 1 Removed; alternate.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.8}.
CHAIN 2 415 Heterogeneous nuclear ribonucleoprotein
F, N-terminally processed.
/FTId=PRO_0000081852.
DOMAIN 13 85 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 111 188 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 289 366 RRM 3. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
REGION 81 86 Interaction with RNA.
REGION 179 184 Interaction with RNA.
REGION 355 360 Interaction with RNA.
SITE 16 16 Interaction with RNA.
SITE 20 20 Interaction with RNA.
SITE 52 52 Interaction with RNA.
SITE 75 75 Interaction with RNA.
SITE 116 116 Interaction with RNA.
SITE 120 120 Interaction with RNA.
SITE 150 150 Interaction with RNA.
SITE 173 173 Interaction with RNA.
SITE 294 294 Interaction with RNA.
SITE 298 298 Interaction with RNA.
SITE 326 326 Interaction with RNA.
SITE 349 349 Interaction with RNA.
MOD_RES 1 1 N-acetylmethionine; in Heterogeneous
nuclear ribonucleoprotein F; alternate.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.8}.
MOD_RES 2 2 N-acetylmethionine; in Heterogeneous
nuclear ribonucleoprotein F, N-terminally
processed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.8}.
MOD_RES 104 104 Phosphoserine.
{ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 107 107 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 161 161 Phosphoserine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 187 187 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 193 193 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 195 195 Phosphoserine.
{ECO:0000250|UniProtKB:Q794E4}.
MOD_RES 200 200 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q9Z2X1}.
MOD_RES 215 215 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 224 224 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 265 265 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 72 72 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:15161980}.
CROSSLNK 87 87 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 167 167 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 185 185 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 200 200 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 224 224 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
VARIANT 87 87 K -> R (in dbSNP:rs17851426).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_027999.
MUTAGEN 20 20 W->A: Loss of RNA-binding.
{ECO:0000269|PubMed:20526337}.
MUTAGEN 84 84 E->A: Loss of RNA-binding.
{ECO:0000269|PubMed:20526337}.
MUTAGEN 116 116 R->A: Decreases affinity for RNA
oligonucleotide 100-fold.
{ECO:0000269|PubMed:20526337}.
MUTAGEN 120 120 F->A: Little disruption of binding RNA.
Decreases affinity for RNA
oligonucleotide 100-fold. Abrogates RNA-
binding; when associated with A-180.
{ECO:0000269|PubMed:16885237,
ECO:0000269|PubMed:20526337}.
MUTAGEN 150 150 K->A: No effect on affinity for RNA
oligonucleotide.
{ECO:0000269|PubMed:20526337}.
MUTAGEN 156 156 F->A: Drastically effects folding of
RRM2. {ECO:0000269|PubMed:16885237}.
MUTAGEN 173 173 K->A: Minimal effect on affinity for RNA
oligonucleotide.
{ECO:0000269|PubMed:20526337}.
MUTAGEN 178 178 H->A: Little disruption of binding RNA.
{ECO:0000269|PubMed:16885237}.
MUTAGEN 179 179 R->A: Decreases affinity for RNA
oligonucleotide 100-fold.
{ECO:0000269|PubMed:20526337}.
MUTAGEN 180 180 Y->A: Decreases affinity for RNA
oligonucleotide 10-fold. Abrogates RNA-
binding; when associated with A-120.
{ECO:0000269|PubMed:16885237,
ECO:0000269|PubMed:20526337}.
MUTAGEN 182 182 E->A: Decreases affinity for RNA
oligonucleotide 100-fold.
{ECO:0000269|PubMed:20526337}.
MUTAGEN 184 184 F->A: Minimal effect on affinity for RNA
oligonucleotide.
{ECO:0000269|PubMed:20526337}.
STRAND 12 17 {ECO:0000244|PDB:2HGL}.
HELIX 24 30 {ECO:0000244|PDB:2HGL}.
TURN 31 33 {ECO:0000244|PDB:2HGL}.
STRAND 37 40 {ECO:0000244|PDB:2HGL}.
STRAND 43 47 {ECO:0000244|PDB:2HGL}.
STRAND 49 51 {ECO:0000244|PDB:2HGL}.
STRAND 53 60 {ECO:0000244|PDB:2HGL}.
HELIX 64 71 {ECO:0000244|PDB:2HGL}.
TURN 72 74 {ECO:0000244|PDB:2HGL}.
STRAND 75 87 {ECO:0000244|PDB:2HGL}.
HELIX 90 97 {ECO:0000244|PDB:2HGL}.
STRAND 107 109 {ECO:0000244|PDB:2HGM}.
STRAND 112 116 {ECO:0000244|PDB:2HGM}.
HELIX 124 130 {ECO:0000244|PDB:2HGM}.
TURN 131 133 {ECO:0000244|PDB:2HGM}.
STRAND 136 142 {ECO:0000244|PDB:2HGM}.
STRAND 147 151 {ECO:0000244|PDB:2HGM}.
STRAND 153 161 {ECO:0000244|PDB:2HGM}.
HELIX 164 169 {ECO:0000244|PDB:2HGM}.
TURN 170 173 {ECO:0000244|PDB:2HGM}.
STRAND 175 180 {ECO:0000244|PDB:2KG0}.
STRAND 184 186 {ECO:0000244|PDB:2HGM}.
HELIX 188 191 {ECO:0000244|PDB:2HGM}.
STRAND 284 294 {ECO:0000244|PDB:2KG1}.
HELIX 302 309 {ECO:0000244|PDB:2HGN}.
STRAND 315 318 {ECO:0000244|PDB:2HGN}.
STRAND 322 325 {ECO:0000244|PDB:2HGN}.
STRAND 332 334 {ECO:0000244|PDB:2HGN}.
HELIX 337 344 {ECO:0000244|PDB:2HGN}.
STRAND 351 354 {ECO:0000244|PDB:2HGN}.
STRAND 358 362 {ECO:0000244|PDB:2KG1}.
STRAND 368 371 {ECO:0000244|PDB:2KG1}.
STRAND 377 379 {ECO:0000244|PDB:2KG1}.
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


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