FIP1_HUMAN
ID FIP1_HUMAN Reviewed; 594 AA.
AC Q6UN15; B4DIR3; G3XAD6; Q0VGE0; Q499Y4; Q49AU3; Q7Z608; Q8WVN3; Q96F80;
AC Q9H077;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Pre-mRNA 3'-end-processing factor FIP1;
DE Short=hFip1;
DE AltName: Full=FIP1-like 1 protein;
DE AltName: Full=Factor interacting with PAP;
DE AltName: Full=Rearranged in hypereosinophilia;
GN Name=FIP1L1; Synonyms=FIP1, RHE;
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] (ISOFORM 1), FUNCTION IN PRE-MRNA 3'-END
RP PROCESSING, IDENTIFICATION IN THE CPSF COMPLEX, IDENTIFICATION IN A COMPLEX
RP WITH CPSF1 AND PAPOLA, INTERACTION WITH CPSF1; CPSF4; CSTF2; CSTF3 AND
RP PAPOLA, RNA-BINDING, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Testis;
RX PubMed=14749727; DOI=10.1038/sj.emboj.7600070;
RA Kaufmann I., Martin G., Friedlein A., Langen H., Keller W.;
RT "Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements and
RT stimulates poly(A) polymerase.";
RL EMBO J. 23:616-626(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Uterus;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Hippocampus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Brain, Eye, Placenta, and Testis;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-339, DISEASE, AND IDENTIFICATION BY MASS
RP SPECTROMETRY OF THE FIP1L1-PDGFRA FUSION PROTEIN.
RC TISSUE=Eosinophil;
RX PubMed=12808148; DOI=10.1073/pnas.0932698100;
RA Griffin J.H., Leung J., Bruner R.J., Caligiuri M.A., Briesewitz R.;
RT "Discovery of a fusion kinase in EOL-1 cells and idiopathic
RT hypereosinophilic syndrome.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7830-7835(2003).
RN [8]
RP RNA-BINDING.
RX PubMed=15767428; DOI=10.1128/jvi.79.7.4270-4288.2005;
RA Zhao X., Oeberg D., Rush M., Fay J., Lambkin H., Schwartz S.;
RT "A 57-nucleotide upstream early polyadenylation element in human
RT papillomavirus type 16 interacts with hFip1, CstF-64, hnRNP C1/C2, and
RT polypyrimidine tract binding protein.";
RL J. Virol. 79:4270-4288(2005).
RN [9]
RP DISEASE.
RX PubMed=12660384; DOI=10.1056/nejmoa025217;
RA Cools J., DeAngelo D.J., Gotlib J., Stover E.H., Legare R.D., Cortes J.,
RA Kutok J., Clark J., Galinsky I., Griffin J.D., Cross N.C., Tefferi A.,
RA Malone J., Alam R., Schrier S.L., Schmid J., Rose M., Vandenberghe P.,
RA Verhoef G., Boogaerts M., Wlodarska I., Kantarjian H., Marynen P.,
RA Coutre S.E., Stone R., Gilliland D.G.;
RT "A tyrosine kinase created by fusion of the PDGFRA and FIP1L1 genes as a
RT therapeutic target of imatinib in idiopathic hypereosinophilic syndrome.";
RL N. Engl. J. Med. 348:1201-1214(2003).
RN [10]
RP INTERACTION WITH NUDT21/CPSF5.
RX PubMed=15937220; DOI=10.1101/gad.1298605;
RA Venkataraman K., Brown K.M., Gilmartin G.M.;
RT "Analysis of a noncanonical poly(A) site reveals a tripartite mechanism for
RT vertebrate poly(A) site recognition.";
RL Genes Dev. 19:1315-1327(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-426, AND IDENTIFICATION BY
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-500, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492; SER-496 AND SER-500, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [16]
RP IDENTIFICATION BY MASS 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 [17]
RP INTERACTION WITH AHCYL1 AND PAPOLA.
RX PubMed=19224921; DOI=10.1074/jbc.m807136200;
RA Kiefer H., Mizutani A., Iemura S., Natsume T., Ando H., Kuroda Y.,
RA Mikoshiba K.;
RT "Inositol 1,4,5-triphosphate receptor-binding protein released with
RT inositol 1,4,5-triphosphate (IRBIT) associates with components of the mRNA
RT 3' processing machinery in a phosphorylation-dependent manner and inhibits
RT polyadenylation.";
RL J. Biol. Chem. 284:10694-10705(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492; THR-494; SER-496 AND
RP SER-500, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492 AND SER-554, 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492 AND SER-496, AND
RP IDENTIFICATION BY 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492 AND SER-500, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-500 AND SER-554, AND
RP IDENTIFICATION BY 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 [23]
RP INTERACTION WITH CPSF6 AND CPSF7, AND DOMAIN.
RX PubMed=29276085; DOI=10.1016/j.molcel.2017.11.031;
RA Zhu Y., Wang X., Forouzmand E., Jeong J., Qiao F., Sowd G.A.,
RA Engelman A.N., Xie X., Hertel K.J., Shi Y.;
RT "Molecular mechanisms for CFIm-mediated regulation of mRNA alternative
RT polyadenylation.";
RL Mol. Cell 69:62-74(2018).
CC -!- FUNCTION: Component of the cleavage and polyadenylation specificity
CC factor (CPSF) complex that plays a key role in pre-mRNA 3'-end
CC formation, recognizing the AAUAAA signal sequence and interacting with
CC poly(A) polymerase and other factors to bring about cleavage and
CC poly(A) addition. FIP1L1 contributes to poly(A) site recognition and
CC stimulates poly(A) addition. Binds to U-rich RNA sequence elements
CC surrounding the poly(A) site. May act to tether poly(A) polymerase to
CC the CPSF complex. {ECO:0000269|PubMed:14749727}.
CC -!- SUBUNIT: Component of the cleavage and polyadenylation specificity
CC factor (CPSF) complex, composed of CPSF1, CPSF2, CPSF3, CPSF4 and
CC FIP1L1. Found in a complex with CPSF1, FIP1L1 and PAPOLA. Interacts
CC with CPSF1, CPSF4, CSTF2 and CSTF3 (PubMed:14749727). Interacts with
CC AHCYL1 (when phosphorylated); the interaction is direct and associates
CC AHCYL1 with the CPSF complex and RNA (PubMed:19224921). Interacts with
CC NUDT21/CPSF5; this interaction occurs in a RNA sequence-specific manner
CC (PubMed:15937220). Interacts (preferentially via unphosphorylated form
CC and Arg/Glu/Asp-rich domain) with CPSF6 (via Arg/Ser-rich domain); this
CC interaction mediates, at least in part, the interaction between the
CC CFIm and CPSF complexes and may be inhibited by CPSF6 hyper-
CC phosphorylation (PubMed:29276085). Interacts (preferentially via
CC unphosphorylated form and Arg/Asp/Glu-rich domain) with CPSF7 (via
CC Arg/Ser-rich domain); this interaction mediates, at least in part, the
CC interaction between the CFIm and CPSF complexes and may be inhibited by
CC CPSF7 hyper-phosphorylation (PubMed:29276085). Interacts with PAPOLA;
CC the interaction seems to be increased by the interaction with AHCYL1
CC (By similarity). {ECO:0000250|UniProtKB:Q9D824,
CC ECO:0000269|PubMed:14749727, ECO:0000269|PubMed:15937220,
CC ECO:0000269|PubMed:19224921, ECO:0000269|PubMed:29276085}.
CC -!- INTERACTION:
CC Q6UN15; Q08379: GOLGA2; NbExp=3; IntAct=EBI-1021914, EBI-618309;
CC Q6UN15; P41227: NAA10; NbExp=3; IntAct=EBI-1021914, EBI-747693;
CC Q6UN15; Q96E35: ZMYND19; NbExp=3; IntAct=EBI-1021914, EBI-746595;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6UN15-1; Sequence=Displayed;
CC Name=3;
CC IsoId=Q6UN15-3; Sequence=VSP_016728, VSP_016729, VSP_016730;
CC Name=4;
CC IsoId=Q6UN15-4; Sequence=VSP_016728, VSP_016731, VSP_016732;
CC Name=5;
CC IsoId=Q6UN15-5; Sequence=VSP_016728, VSP_046213;
CC -!- DISEASE: Note=A chromosomal aberration involving FIP1L1 is found in
CC some cases of hypereosinophilic syndrome. Interstitial chromosomal
CC deletion del(4)(q12q12) causes the fusion of FIP1L1 and PDGFRA (FIP1L1-
CC PDGFRA). {ECO:0000269|PubMed:12660384, ECO:0000269|PubMed:12808148}.
CC -!- SIMILARITY: Belongs to the FIP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH24016.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=AAH52959.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AY366510; AAQ88277.1; -; mRNA.
DR EMBL; AL136910; CAB66844.1; -; mRNA.
DR EMBL; AK295737; BAG58575.1; -; mRNA.
DR EMBL; AC058822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC095040; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC098587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC098821; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC105384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC110298; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC110792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC124017; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC138607; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC138779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471057; EAX05448.1; -; Genomic_DNA.
DR EMBL; BC011543; AAH11543.1; -; mRNA.
DR EMBL; BC017724; AAH17724.1; -; mRNA.
DR EMBL; BC024016; AAH24016.1; ALT_SEQ; mRNA.
DR EMBL; BC052959; AAH52959.1; ALT_SEQ; mRNA.
DR EMBL; BC110383; AAI10384.1; -; mRNA.
DR EMBL; AY229892; AAP69563.1; ALT_TERM; mRNA.
DR CCDS; CCDS3491.1; -. [Q6UN15-1]
DR CCDS; CCDS47055.1; -. [Q6UN15-5]
DR CCDS; CCDS47056.1; -. [Q6UN15-3]
DR RefSeq; NP_001128409.1; NM_001134937.1. [Q6UN15-5]
DR RefSeq; NP_001128410.1; NM_001134938.1. [Q6UN15-3]
DR RefSeq; NP_112179.2; NM_030917.3. [Q6UN15-1]
DR PDB; 7K95; X-ray; 1.90 A; B/C=159-200.
DR PDBsum; 7K95; -.
DR AlphaFoldDB; Q6UN15; -.
DR SMR; Q6UN15; -.
DR BioGRID; 123545; 178.
DR CORUM; Q6UN15; -.
DR DIP; DIP-42503N; -.
DR IntAct; Q6UN15; 77.
DR MINT; Q6UN15; -.
DR STRING; 9606.ENSP00000336752; -.
DR GlyGen; Q6UN15; 17 sites, 2 O-linked glycans (17 sites).
DR iPTMnet; Q6UN15; -.
DR MetOSite; Q6UN15; -.
DR PhosphoSitePlus; Q6UN15; -.
DR BioMuta; FIP1L1; -.
DR DMDM; 74749365; -.
DR EPD; Q6UN15; -.
DR jPOST; Q6UN15; -.
DR MassIVE; Q6UN15; -.
DR MaxQB; Q6UN15; -.
DR PaxDb; Q6UN15; -.
DR PeptideAtlas; Q6UN15; -.
DR PRIDE; Q6UN15; -.
DR ProteomicsDB; 33719; -.
DR ProteomicsDB; 67417; -. [Q6UN15-1]
DR ProteomicsDB; 67418; -. [Q6UN15-3]
DR ProteomicsDB; 67419; -. [Q6UN15-4]
DR Antibodypedia; 12232; 163 antibodies from 28 providers.
DR DNASU; 81608; -.
DR Ensembl; ENST00000306932.10; ENSP00000302993.6; ENSG00000145216.16. [Q6UN15-3]
DR Ensembl; ENST00000337488.11; ENSP00000336752.6; ENSG00000145216.16. [Q6UN15-1]
DR Ensembl; ENST00000358575.9; ENSP00000351383.5; ENSG00000145216.16. [Q6UN15-5]
DR Ensembl; ENST00000507922.5; ENSP00000425456.1; ENSG00000145216.16. [Q6UN15-4]
DR GeneID; 81608; -.
DR KEGG; hsa:81608; -.
DR MANE-Select; ENST00000337488.11; ENSP00000336752.6; NM_030917.4; NP_112179.2.
DR UCSC; uc003gzx.5; human. [Q6UN15-1]
DR CTD; 81608; -.
DR DisGeNET; 81608; -.
DR GeneCards; FIP1L1; -.
DR HGNC; HGNC:19124; FIP1L1.
DR HPA; ENSG00000145216; Low tissue specificity.
DR MalaCards; FIP1L1; -.
DR MIM; 607685; phenotype.
DR MIM; 607686; gene.
DR neXtProt; NX_Q6UN15; -.
DR OpenTargets; ENSG00000145216; -.
DR Orphanet; 520; Acute promyelocytic leukemia.
DR Orphanet; 168940; Chronic eosinophilic leukemia.
DR Orphanet; 314950; Primary hypereosinophilic syndrome.
DR PharmGKB; PA134875694; -.
DR VEuPathDB; HostDB:ENSG00000145216; -.
DR eggNOG; KOG1049; Eukaryota.
DR GeneTree; ENSGT01050000245006; -.
DR HOGENOM; CLU_035577_0_0_1; -.
DR OMA; YYPRRED; -.
DR OrthoDB; 929913at2759; -.
DR PhylomeDB; Q6UN15; -.
DR TreeFam; TF318610; -.
DR PathwayCommons; Q6UN15; -.
DR Reactome; R-HSA-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72187; mRNA 3'-end processing.
DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-HSA-77595; Processing of Intronless Pre-mRNAs.
DR Reactome; R-HSA-9673766; Signaling by cytosolic PDGFRA and PDGFRB fusion proteins.
DR SignaLink; Q6UN15; -.
DR SIGNOR; Q6UN15; -.
DR BioGRID-ORCS; 81608; 689 hits in 1087 CRISPR screens.
DR ChiTaRS; FIP1L1; human.
DR GeneWiki; FIP1L1; -.
DR GenomeRNAi; 81608; -.
DR Pharos; Q6UN15; Tbio.
DR PRO; PR:Q6UN15; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q6UN15; protein.
DR Bgee; ENSG00000145216; Expressed in tendon of biceps brachii and 198 other tissues.
DR ExpressionAtlas; Q6UN15; baseline and differential.
DR Genevisible; Q6UN15; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IBA:GO_Central.
DR InterPro; IPR007854; Fip1_dom.
DR Pfam; PF05182; Fip1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; mRNA processing; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..594
FT /note="Pre-mRNA 3'-end-processing factor FIP1"
FT /id="PRO_0000215037"
FT REGION 1..356
FT /note="Necessary for stimulating PAPOLA activity"
FT REGION 1..111
FT /note="Sufficient for interaction with PAPOLA"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..243
FT /note="Sufficient for interaction with CPSF4"
FT /evidence="ECO:0000269|PubMed:14749727"
FT REGION 238..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..594
FT /note="Sufficient for interaction with CPSF1 and CSTF3"
FT /evidence="ECO:0000269|PubMed:14749727"
FT REGION 457..490
FT /note="Arg/Asp/Glu-rich domain"
FT /evidence="ECO:0000269|PubMed:29276085"
FT COMPBIAS 238..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..404
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..561
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 339..340
FT /note="Breakpoint for interstitial deletion to form the
FT FIP1L1-PDGFRA fusion protein"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D824"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D824"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D824"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D824"
FT MOD_RES 426
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 494
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 29..43
FT /note="Missing (in isoform 3, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:11230166,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_016728"
FT VAR_SEQ 213..235
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11230166"
FT /id="VSP_016729"
FT VAR_SEQ 272..307
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11230166"
FT /id="VSP_016730"
FT VAR_SEQ 389
FT /note="P -> PPPGIPITVP (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046213"
FT VAR_SEQ 393
FT /note="F -> K (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016731"
FT VAR_SEQ 394..594
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016732"
FT CONFLICT 118
FT /note="V -> I (in Ref. 3; BAG58575)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="G -> R (in Ref. 6; AAH24016/AAH52959)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="K -> R (in Ref. 6; AAH52959)"
FT /evidence="ECO:0000305"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:7K95"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:7K95"
FT HELIX 182..197
FT /evidence="ECO:0007829|PDB:7K95"
SQ SEQUENCE 594 AA; 66526 MW; B391D142419ED061 CRC64;
MSAGEVERLV SELSGGTGGD EEEEWLYGGP WDVHVHSDLA KDLDENEVER PEEENASANP
PSGIEDETAE NGVPKPKVTE TEDDSDSDSD DDEDDVHVTI GDIKTGAPQY GSYGTAPVNL
NIKTGGRVYG TTGTKVKGVD LDAPGSINGV PLLEVDLDSF EDKPWRKPGA DLSDYFNYGF
NEDTWKAYCE KQKRIRMGLE VIPVTSTTNK ITAEDCTMEV TPGAEIQDGR FNLFKVQQGR
TGNSEKETAL PSTKAEFTSP PSLFKTGLPP SRNSTSSQSQ TSTASRKANS SVGKWQDRYG
RAESPDLRRL PGAIDVIGQT ITISRVEGRR RANENSNIQV LSERSATEVD NNFSKPPPFF
PPGAPPTHLP PPPFLPPPPT VSTAPPLIPP PGFPPPPGAP PPSLIPTIES GHSSGYDSRS
ARAFPYGNVA FPHLPGSAPS WPSLVDTSKQ WDYYARREKD RDRERDRDRE RDRDRDRERE
RTRERERERD HSPTPSVFNS DEERYRYREY AERGYERHRA SREKEERHRE RRHREKEETR
HKSSRSNSRR RHESEEGDSH RRHKHKKSKR SKEGKEAGSE PAPEQESTEA TPAE
