HNRPF_MOUSE
ID HNRPF_MOUSE Reviewed; 415 AA.
AC Q9Z2X1; Q5FWK2; Q8BVU8; Q8K2U9; Q8R0E7;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein F;
DE Short=hnRNP F;
DE Contains:
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein F, N-terminally processed;
GN Name=Hnrnpf; Synonyms=Hnrpf;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, Czech II, and FVB/N;
RC TISSUE=Eye, Fetal brain, Mammary gland, and Mammary tumor;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107 AND SER-187, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-200, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [5]
RP STRUCTURE BY NMR OF 1-105.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RNA binding domain in heterogeneous nuclear
RT ribonucleoprotein F homolog.";
RL Submitted (JUN-2006) to the PDB data bank.
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Identified in the spliceosome C complex. Interacts with AGO1,
CC AGO2, TBP and TXNL4/DIM1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Z2X1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z2X1-2; Sequence=VSP_021004;
CC -!- DOMAIN: The N-terminal RRM domains are responsible for recognizing the
CC G-tract of BCL-X RNA. {ECO:0000250}.
CC -!- PTM: Sumoylated. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH27003.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH29764.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC36361.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK076478; BAC36361.1; ALT_SEQ; mRNA.
DR EMBL; BC018185; AAH18185.1; -; mRNA.
DR EMBL; BC025481; AAH25481.1; -; mRNA.
DR EMBL; BC027003; AAH27003.1; ALT_INIT; mRNA.
DR EMBL; BC029163; AAH29163.1; -; mRNA.
DR EMBL; BC029764; AAH29764.1; ALT_INIT; mRNA.
DR EMBL; BC033483; AAH33483.1; -; mRNA.
DR EMBL; BC089313; AAH89313.1; -; mRNA.
DR CCDS; CCDS20467.1; -. [Q9Z2X1-1]
DR RefSeq; NP_001159899.1; NM_001166427.1. [Q9Z2X1-1]
DR RefSeq; NP_001159900.1; NM_001166428.1. [Q9Z2X1-1]
DR RefSeq; NP_001159901.1; NM_001166429.1. [Q9Z2X1-1]
DR RefSeq; NP_001159902.1; NM_001166430.1. [Q9Z2X1-1]
DR RefSeq; NP_001159903.1; NM_001166431.1. [Q9Z2X1-1]
DR RefSeq; NP_001159904.1; NM_001166432.1. [Q9Z2X1-1]
DR RefSeq; NP_598595.1; NM_133834.2. [Q9Z2X1-1]
DR RefSeq; XP_006506892.1; XM_006506829.3. [Q9Z2X1-1]
DR PDB; 2DB1; NMR; -; A=1-105.
DR PDBsum; 2DB1; -.
DR AlphaFoldDB; Q9Z2X1; -.
DR SMR; Q9Z2X1; -.
DR BioGRID; 221126; 103.
DR CORUM; Q9Z2X1; -.
DR IntAct; Q9Z2X1; 41.
DR MINT; Q9Z2X1; -.
DR STRING; 10090.ENSMUSP00000130023; -.
DR iPTMnet; Q9Z2X1; -.
DR PhosphoSitePlus; Q9Z2X1; -.
DR SwissPalm; Q9Z2X1; -.
DR REPRODUCTION-2DPAGE; Q9Z2X1; -.
DR EPD; Q9Z2X1; -.
DR jPOST; Q9Z2X1; -.
DR MaxQB; Q9Z2X1; -.
DR PaxDb; Q9Z2X1; -.
DR PeptideAtlas; Q9Z2X1; -.
DR PRIDE; Q9Z2X1; -.
DR ProteomicsDB; 269618; -. [Q9Z2X1-1]
DR ProteomicsDB; 269619; -. [Q9Z2X1-2]
DR Antibodypedia; 13432; 357 antibodies from 33 providers.
DR DNASU; 98758; -.
DR Ensembl; ENSMUST00000035493; ENSMUSP00000045048; ENSMUSG00000042079. [Q9Z2X1-1]
DR Ensembl; ENSMUST00000163168; ENSMUSP00000130023; ENSMUSG00000042079. [Q9Z2X1-1]
DR Ensembl; ENSMUST00000167182; ENSMUSP00000126817; ENSMUSG00000042079. [Q9Z2X1-1]
DR Ensembl; ENSMUST00000180020; ENSMUSP00000137632; ENSMUSG00000042079. [Q9Z2X1-1]
DR Ensembl; ENSMUST00000180341; ENSMUSP00000136700; ENSMUSG00000042079. [Q9Z2X1-1]
DR GeneID; 98758; -.
DR KEGG; mmu:98758; -.
DR UCSC; uc009dle.2; mouse. [Q9Z2X1-1]
DR CTD; 3185; -.
DR MGI; MGI:2138741; Hnrnpf.
DR VEuPathDB; HostDB:ENSMUSG00000042079; -.
DR eggNOG; KOG4211; Eukaryota.
DR GeneTree; ENSGT00940000157838; -.
DR HOGENOM; CLU_032003_1_0_1; -.
DR InParanoid; Q9Z2X1; -.
DR OMA; GDACVIF; -.
DR OrthoDB; 603679at2759; -.
DR PhylomeDB; Q9Z2X1; -.
DR TreeFam; TF316157; -.
DR Reactome; R-MMU-6803529; FGFR2 alternative splicing.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR BioGRID-ORCS; 98758; 15 hits in 74 CRISPR screens.
DR ChiTaRS; Hnrnpf; mouse.
DR EvolutionaryTrace; Q9Z2X1; -.
DR PRO; PR:Q9Z2X1; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9Z2X1; protein.
DR Bgee; ENSMUSG00000042079; Expressed in epiblast (generic) and 72 other tissues.
DR ExpressionAtlas; Q9Z2X1; baseline and differential.
DR Genevisible; Q9Z2X1; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003727; F:single-stranded RNA binding; ISS:UniProtKB.
DR GO; GO:0017025; F:TBP-class protein binding; ISO:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0043484; P:regulation of RNA splicing; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
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 Pfam; PF00076; RRM_1; 2.
DR Pfam; PF08080; zf-RNPHF; 1.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 3.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; 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_0000253053"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52597"
FT CHAIN 2..415
FT /note="Heterogeneous nuclear ribonucleoprotein F, N-
FT terminally processed"
FT /id="PRO_0000367116"
FT DOMAIN 11..90
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 /evidence="ECO:0000250"
FT REGION 179..184
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT REGION 355..360
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 16
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 20
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 52
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 75
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 116
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 120
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 150
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 173
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 294
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 298
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 326
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 349
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P52597"
FT MOD_RES 2
FT /note="N-acetylmethionine; in Heterogeneous nuclear
FT ribonucleoprotein F, N-terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P52597"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52597"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52597"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52597"
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:0007744|PubMed:23806337"
FT MOD_RES 215
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P52597"
FT MOD_RES 224
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52597"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52597"
FT CROSSLNK 72
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 87
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52597"
FT CROSSLNK 167
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52597"
FT CROSSLNK 185
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52597"
FT CROSSLNK 200
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P52597"
FT CROSSLNK 224
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P52597"
FT VAR_SEQ 1..22
FT /note="MMLGPEGGEGYVVKLRGLPWSC -> MW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021004"
FT CONFLICT 272
FT /note="Y -> C (in Ref. 2; AAH27003)"
FT /evidence="ECO:0000305"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:2DB1"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:2DB1"
FT HELIX 24..30
FT /evidence="ECO:0007829|PDB:2DB1"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:2DB1"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:2DB1"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:2DB1"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:2DB1"
FT STRAND 53..63
FT /evidence="ECO:0007829|PDB:2DB1"
FT HELIX 64..70
FT /evidence="ECO:0007829|PDB:2DB1"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:2DB1"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:2DB1"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:2DB1"
FT HELIX 90..98
FT /evidence="ECO:0007829|PDB:2DB1"
SQ SEQUENCE 415 AA; 45730 MW; 31E1C9C90A8E051F CRC64;
MMLGPEGGEG YVVKLRGLPW SCSIEDVQNF LSDCTIHDGV AGVHFIYTRE GRQSGEAFVE
LESEDDVKLA LKKDRESMGH RYIEVFKSHR TEMDWVLKHS GPNSADSAND GFVRLRGLPF
GCTKEEIVQF FSGLEIVPNG ITLPVDPEGK ITGEAFVQFA SQELAEKALG KHKERIGHRY
IEVFKSSQEE VRSYSDPPLK FMSVQRPGPY DRPGTARRYI GIVKQAGLDR MRSGAYSAGY
GGYEEYSGLS DGYGFTTDLF GRDLSYCLSG MYDHRYGDSE FTVQSTTGHC VHMRGLPYKA
TENDIYNFFS PLNPVRVHIE IGPDGRVTGE ADVEFATHEE AVAAMSKDRA NMQHRYIELF
LNSTTGASNG AYSSQVMQGM GVSAAQATYS GLESQSVSGC YGAGYSGQNS MGGYD
