NUFP2_HUMAN
ID NUFP2_HUMAN Reviewed; 695 AA.
AC Q7Z417; A1L3A6; A1L3A7; Q9P2M5;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=FMR1-interacting protein NUFIP2 {ECO:0000305|PubMed:12837692};
DE AltName: Full=82 kDa FMRP-interacting protein;
DE Short=82-FIP;
DE AltName: Full=Cell proliferation-inducing gene 1 protein;
DE AltName: Full=FMRP-interacting protein 2;
DE AltName: Full=Nuclear FMR1-interacting protein 2 {ECO:0000312|HGNC:HGNC:17634};
GN Name=NUFIP2 {ECO:0000312|HGNC:HGNC:17634}; Synonyms=KIAA1321;
GN ORFNames=PIG1;
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), PROTEIN SEQUENCE OF 74-92 AND
RP 593-609, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP FMR1.
RX PubMed=12837692; DOI=10.1093/hmg/ddg181;
RA Bardoni B., Castets M., Huot M.-E., Schenck A., Adinolfi S., Corbin F.,
RA Pastore A., Khandjian E.W., Mandel J.-L.;
RT "82-FIP, a novel FMRP (fragile X mental retardation protein) interacting
RT protein, shows a cell cycle-dependent intracellular localization.";
RL Hum. Mol. Genet. 12:1689-1698(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kim J.W.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
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] (ISOFORMS 1 AND 2).
RC TISSUE=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 92-104; 110-136; 233-269; 331-351; 369-397; 531-563;
RP 571-639; 650-659; 668-677 AND 683-695, PHOSPHORYLATION AT SER-629, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-652, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-652, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212 AND THR-220, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-87, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [13]
RP IDENTIFICATION BY 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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-652, AND IDENTIFICATION BY
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112; SER-113; SER-212;
RP SER-214; TYR-218; THR-219; THR-220; SER-572; SER-629; SER-637; SER-652 AND
RP SER-692, AND 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 [17]
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-652, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212; SER-376; SER-572;
RP SER-629 AND SER-637, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-87; SER-112; SER-212;
RP THR-571; SER-572; SER-629; THR-633; SER-652 AND SER-692, AND IDENTIFICATION
RP 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-112; SER-212; SER-572;
RP SER-629; SER-652; SER-655 AND SER-692, AND IDENTIFICATION BY MASS
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112; SER-212; SER-214;
RP SER-572; SER-592; SER-608; SER-629; SER-652 AND SER-692, AND IDENTIFICATION
RP 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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-629, 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 [25]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-291, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [26]
RP INTERACTION WITH DDX6, AND SUBCELLULAR LOCATION.
RX PubMed=26184334; DOI=10.3390/biom5031441;
RA Bish R., Cuevas-Polo N., Cheng Z., Hambardzumyan D., Munschauer M.,
RA Landthaler M., Vogel C.;
RT "Comprehensive protein interactome analysis of a key RNA helicase:
RT detection of novel stress granule proteins.";
RL Biomolecules 5:1441-1466(2015).
RN [27]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-146 AND LYS-307, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [28]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-78; LYS-109; LYS-136; LYS-146;
RP LYS-157; LYS-171; LYS-262; LYS-281; LYS-293 AND LYS-307, AND IDENTIFICATION
RP 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).
CC -!- FUNCTION: Binds RNA. {ECO:0000269|PubMed:12837692}.
CC -!- SUBUNIT: Interacts with FMR1 (via N-terminus). Interacts with DDX6
CC (PubMed:26184334). {ECO:0000269|PubMed:12837692,
CC ECO:0000269|PubMed:26184334}.
CC -!- INTERACTION:
CC Q7Z417; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-1210753, EBI-10173507;
CC Q7Z417; A2BDD9: AMOT; NbExp=3; IntAct=EBI-1210753, EBI-17286414;
CC Q7Z417; P49747: COMP; NbExp=3; IntAct=EBI-1210753, EBI-2531022;
CC Q7Z417; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-1210753, EBI-3867333;
CC Q7Z417; G5E9A7: DMWD; NbExp=3; IntAct=EBI-1210753, EBI-10976677;
CC Q7Z417; O95967: EFEMP2; NbExp=6; IntAct=EBI-1210753, EBI-743414;
CC Q7Z417; Q9NQ30: ESM1; NbExp=3; IntAct=EBI-1210753, EBI-12260294;
CC Q7Z417; Q9UBX5: FBLN5; NbExp=4; IntAct=EBI-1210753, EBI-947897;
CC Q7Z417; Q5TD97: FHL5; NbExp=3; IntAct=EBI-1210753, EBI-750641;
CC Q7Z417; Q9BTY2: FUCA2; NbExp=3; IntAct=EBI-1210753, EBI-9050116;
CC Q7Z417; Q9UN86-2: G3BP2; NbExp=4; IntAct=EBI-1210753, EBI-11035716;
CC Q7Z417; P28799: GRN; NbExp=10; IntAct=EBI-1210753, EBI-747754;
CC Q7Z417; P42858: HTT; NbExp=6; IntAct=EBI-1210753, EBI-466029;
CC Q7Z417; O60333-2: KIF1B; NbExp=3; IntAct=EBI-1210753, EBI-10975473;
CC Q7Z417; Q5T749: KPRP; NbExp=5; IntAct=EBI-1210753, EBI-10981970;
CC Q7Z417; Q15323: KRT31; NbExp=3; IntAct=EBI-1210753, EBI-948001;
CC Q7Z417; O76014: KRT37; NbExp=3; IntAct=EBI-1210753, EBI-1045716;
CC Q7Z417; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-1210753, EBI-11749135;
CC Q7Z417; Q9BYS1: KRTAP1-5; NbExp=5; IntAct=EBI-1210753, EBI-11741292;
CC Q7Z417; P60370: KRTAP10-5; NbExp=6; IntAct=EBI-1210753, EBI-10172150;
CC Q7Z417; P60409: KRTAP10-7; NbExp=6; IntAct=EBI-1210753, EBI-10172290;
CC Q7Z417; P60410: KRTAP10-8; NbExp=6; IntAct=EBI-1210753, EBI-10171774;
CC Q7Z417; P60411: KRTAP10-9; NbExp=8; IntAct=EBI-1210753, EBI-10172052;
CC Q7Z417; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-1210753, EBI-1052037;
CC Q7Z417; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-1210753, EBI-11953334;
CC Q7Z417; Q9BYR9: KRTAP2-4; NbExp=3; IntAct=EBI-1210753, EBI-14065470;
CC Q7Z417; Q9BYR7: KRTAP3-2; NbExp=6; IntAct=EBI-1210753, EBI-751260;
CC Q7Z417; Q9BYR6: KRTAP3-3; NbExp=3; IntAct=EBI-1210753, EBI-3957694;
CC Q7Z417; A0A087WY89: KRTAP4-1; NbExp=3; IntAct=EBI-1210753, EBI-11957260;
CC Q7Z417; Q9BYQ6: KRTAP4-11; NbExp=6; IntAct=EBI-1210753, EBI-10302392;
CC Q7Z417; Q9BQ66: KRTAP4-12; NbExp=8; IntAct=EBI-1210753, EBI-739863;
CC Q7Z417; Q9BYR5: KRTAP4-2; NbExp=6; IntAct=EBI-1210753, EBI-10172511;
CC Q7Z417; Q9BYR3: KRTAP4-4; NbExp=3; IntAct=EBI-1210753, EBI-11958132;
CC Q7Z417; Q9BYR2: KRTAP4-5; NbExp=3; IntAct=EBI-1210753, EBI-11993254;
CC Q7Z417; Q6L8G4: KRTAP5-11; NbExp=3; IntAct=EBI-1210753, EBI-11993296;
CC Q7Z417; Q701N4: KRTAP5-2; NbExp=3; IntAct=EBI-1210753, EBI-11958178;
CC Q7Z417; Q6L8H2: KRTAP5-3; NbExp=3; IntAct=EBI-1210753, EBI-11974251;
CC Q7Z417; Q6L8H1: KRTAP5-4; NbExp=3; IntAct=EBI-1210753, EBI-11963072;
CC Q7Z417; Q6L8G9: KRTAP5-6; NbExp=6; IntAct=EBI-1210753, EBI-10250562;
CC Q7Z417; P26371: KRTAP5-9; NbExp=5; IntAct=EBI-1210753, EBI-3958099;
CC Q7Z417; Q9BYQ4: KRTAP9-2; NbExp=6; IntAct=EBI-1210753, EBI-1044640;
CC Q7Z417; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-1210753, EBI-1043191;
CC Q7Z417; Q9BYQ2: KRTAP9-4; NbExp=3; IntAct=EBI-1210753, EBI-10185730;
CC Q7Z417; Q9BYQ0: KRTAP9-8; NbExp=3; IntAct=EBI-1210753, EBI-11958364;
CC Q7Z417; Q5T7P3: LCE1B; NbExp=3; IntAct=EBI-1210753, EBI-10245913;
CC Q7Z417; Q5TA81: LCE2C; NbExp=3; IntAct=EBI-1210753, EBI-11973993;
CC Q7Z417; Q5TA82: LCE2D; NbExp=3; IntAct=EBI-1210753, EBI-10246750;
CC Q7Z417; Q9UHV8: LGALS13; NbExp=3; IntAct=EBI-1210753, EBI-3957707;
CC Q7Z417; Q99750: MDFI; NbExp=3; IntAct=EBI-1210753, EBI-724076;
CC Q7Z417; A6BM72: MEGF11; NbExp=3; IntAct=EBI-1210753, EBI-947743;
CC Q7Z417; P07196: NEFL; NbExp=3; IntAct=EBI-1210753, EBI-475646;
CC Q7Z417; Q99435: NELL2; NbExp=2; IntAct=EBI-1210753, EBI-946274;
CC Q7Z417; Q92824: PCSK5; NbExp=3; IntAct=EBI-1210753, EBI-751290;
CC Q7Z417; Q92824-2: PCSK5; NbExp=3; IntAct=EBI-1210753, EBI-11956269;
CC Q7Z417; Q5VY43: PEAR1; NbExp=3; IntAct=EBI-1210753, EBI-1249608;
CC Q7Z417; O15162: PLSCR1; NbExp=2; IntAct=EBI-1210753, EBI-740019;
CC Q7Z417; P30044: PRDX5; NbExp=3; IntAct=EBI-1210753, EBI-722161;
CC Q7Z417; Q9UGC6: RGS17; NbExp=3; IntAct=EBI-1210753, EBI-3918154;
CC Q7Z417; P49795: RGS19; NbExp=3; IntAct=EBI-1210753, EBI-874907;
CC Q7Z417; O76081-6: RGS20; NbExp=3; IntAct=EBI-1210753, EBI-10178530;
CC Q7Z417; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-1210753, EBI-5235340;
CC Q7Z417; Q13077: TRAF1; NbExp=3; IntAct=EBI-1210753, EBI-359224;
CC Q7Z417; O76024: WFS1; NbExp=3; IntAct=EBI-1210753, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12837692,
CC ECO:0000269|PubMed:26184334}. Cytoplasm {ECO:0000269|PubMed:12837692,
CC ECO:0000269|PubMed:26184334}. Cytoplasm, Stress granule
CC {ECO:0000269|PubMed:26184334}. Note=Distribution is cell cycle-
CC modulated, being cytoplasmic in the G2/M phase and accumulating in
CC nucleus during the G1 phase (PubMed:12837692).
CC {ECO:0000269|PubMed:12837692, ECO:0000269|PubMed:26184334}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7Z417-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z417-2; Sequence=VSP_056177;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92559.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ493465; CAD38278.1; -; mRNA.
DR EMBL; AY232289; AAP69984.1; -; mRNA.
DR EMBL; AB037742; BAA92559.1; ALT_INIT; mRNA.
DR EMBL; AK297732; BAG60082.1; -; mRNA.
DR EMBL; AK293075; BAF85764.1; -; mRNA.
DR EMBL; AC005412; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471159; EAW51186.1; -; Genomic_DNA.
DR EMBL; CH471159; EAW51187.1; -; Genomic_DNA.
DR EMBL; BC129989; AAI29990.1; -; mRNA.
DR EMBL; BC129990; AAI29991.1; -; mRNA.
DR EMBL; BC108307; AAI08308.1; -; mRNA.
DR CCDS; CCDS32600.1; -. [Q7Z417-1]
DR RefSeq; NP_065823.1; NM_020772.2. [Q7Z417-1]
DR AlphaFoldDB; Q7Z417; -.
DR SASBDB; Q7Z417; -.
DR BioGRID; 121591; 312.
DR CORUM; Q7Z417; -.
DR DIP; DIP-29023N; -.
DR IntAct; Q7Z417; 127.
DR MINT; Q7Z417; -.
DR STRING; 9606.ENSP00000225388; -.
DR GlyGen; Q7Z417; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q7Z417; -.
DR MetOSite; Q7Z417; -.
DR PhosphoSitePlus; Q7Z417; -.
DR SwissPalm; Q7Z417; -.
DR BioMuta; NUFIP2; -.
DR DMDM; 74713454; -.
DR CPTAC; CPTAC-985; -.
DR EPD; Q7Z417; -.
DR jPOST; Q7Z417; -.
DR MassIVE; Q7Z417; -.
DR MaxQB; Q7Z417; -.
DR PaxDb; Q7Z417; -.
DR PeptideAtlas; Q7Z417; -.
DR PRIDE; Q7Z417; -.
DR ProteomicsDB; 69128; -. [Q7Z417-1]
DR Antibodypedia; 2837; 97 antibodies from 23 providers.
DR DNASU; 57532; -.
DR Ensembl; ENST00000225388.9; ENSP00000225388.3; ENSG00000108256.9. [Q7Z417-1]
DR Ensembl; ENST00000579665.1; ENSP00000463450.1; ENSG00000108256.9. [Q7Z417-2]
DR GeneID; 57532; -.
DR KEGG; hsa:57532; -.
DR MANE-Select; ENST00000225388.9; ENSP00000225388.3; NM_020772.3; NP_065823.1.
DR UCSC; uc002hdx.5; human. [Q7Z417-1]
DR CTD; 57532; -.
DR DisGeNET; 57532; -.
DR GeneCards; NUFIP2; -.
DR HGNC; HGNC:17634; NUFIP2.
DR HPA; ENSG00000108256; Tissue enhanced (bone).
DR MIM; 609356; gene.
DR neXtProt; NX_Q7Z417; -.
DR OpenTargets; ENSG00000108256; -.
DR PharmGKB; PA143485564; -.
DR VEuPathDB; HostDB:ENSG00000108256; -.
DR eggNOG; ENOG502QPMD; Eukaryota.
DR GeneTree; ENSGT00440000038328; -.
DR HOGENOM; CLU_020745_0_0_1; -.
DR InParanoid; Q7Z417; -.
DR OMA; NEQKGNR; -.
DR OrthoDB; 331657at2759; -.
DR PhylomeDB; Q7Z417; -.
DR TreeFam; TF332832; -.
DR PathwayCommons; Q7Z417; -.
DR SignaLink; Q7Z417; -.
DR BioGRID-ORCS; 57532; 39 hits in 1086 CRISPR screens.
DR ChiTaRS; NUFIP2; human.
DR GeneWiki; NUFIP2; -.
DR GenomeRNAi; 57532; -.
DR Pharos; Q7Z417; Tbio.
DR PRO; PR:Q7Z417; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q7Z417; protein.
DR Bgee; ENSG00000108256; Expressed in kidney epithelium and 194 other tissues.
DR Genevisible; Q7Z417; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042788; C:polysomal ribosome; IDA:HGNC-UCL.
DR GO; GO:0003723; F:RNA binding; IDA:HGNC-UCL.
DR InterPro; IPR032747; NUFIP2.
DR PANTHER; PTHR28333; PTHR28333; 1.
DR Pfam; PF15293; NUFIP2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; Ubl conjugation.
FT CHAIN 1..695
FT /note="FMR1-interacting protein NUFIP2"
FT /id="PRO_0000245521"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..55
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 87
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 218
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 219
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 220
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 291
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 571
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 572
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 592
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 629
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 633
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 637
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 652
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 692
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 78
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 109
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 136
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 146
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 157
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 171
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 262
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 281
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 293
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 307
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 93..667
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_056177"
SQ SEQUENCE 695 AA; 76121 MW; BB5C94131F5B5426 CRC64;
MEEKPGQPQP QHHHSHHHPH HHPQQQQQQP HHHHHYYFYN HSHNHHHHHH HQQPHQYLQH
GAEGSPKAQP KPLKHEQKHT LQQHQETPKK KTGYGELNGN AGEREISLKN LSSDEATNPI
SRVLNGNQQV VDTSLKQTVK ANTFGKAGIK TKNFIQKNSM DKKNGKSYEN KSGENQSVDK
SDTIPIPNGV VTNNSGYITN GYMGKGADND GSGSESGYTT PKKRKARRNS AKGCENLNIV
QDKIMQQETS VPTLKQGLET FKPDYSEQKG NRVDGSKPIW KYETGPGGTS RGKPAVGDML
RKSSDSKPGV SSKKFDDRPK GKHASAVASK EDSWTLFKPP PVFPVDNSSA KIVPKISYAS
KVKENLNKTI QNSSVSPTSS SSSSSSTGET QTQSSSRLSQ VPMSALKSVT SANFSNGPVL
AGTDGNVYPP GGQPLLTTAA NTLTPISSGT DSVLQDMSLT SAAVEQIKTS LFIYPSNMQT
MLLSTAQVDL PSQTDQQNLG DIFQNQWGLS FINEPSAGPE TVTGKSSEHK VMEVTFQGEY
PATLVSQGAE IIPSGTEHPV FPKAYELEKR TSPQVLGSIL KSGTTSESGA LSLEPSHIGD
LQKADTSSQG ALVFLSKDYE IESQNPLASP TNTLLGSAKE QRYQRGLERN DSWGSFDLRA
AIVYHTKEME SIWNLQKQDP KRIITYNEAM DSPDQ
