NUFP1_MOUSE
ID NUFP1_MOUSE Reviewed; 484 AA.
AC Q9QXX8; Q9CV69;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=FMR1-interacting protein NUFIP1 {ECO:0000305|PubMed:10556305};
DE AltName: Full=Nuclear FMRP-interacting protein 1;
GN Name=Nufip1 {ECO:0000312|MGI:MGI:1351474};
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INTERACTION WITH FMR1.
RX PubMed=10556305; DOI=10.1093/hmg/8.13.2557;
RA Bardoni B., Schenck A., Mandel J.-L.;
RT "A novel RNA-binding nuclear protein that interacts with the fragile X
RT mental retardation (FMR1) protein.";
RL Hum. Mol. Genet. 8:2557-2566(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Olfactory bulb, Spleen, and Tongue;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=B5/EGFP; TISSUE=Trophoblast stem cell;
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).
CC -!- FUNCTION: Binds RNA. {ECO:0000269|PubMed:10556305}.
CC -!- SUBUNIT: Interacts with FMR1 (PubMed:10556305). Interacts with ZNHIT3
CC (By similarity). {ECO:0000250|UniProtKB:Q9UHK0,
CC ECO:0000269|PubMed:10556305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10556305}.
CC Note=Distributed in the nucleus in a dot-like pattern.
CC -!- TISSUE SPECIFICITY: Expressed in the brain; in neurons and not in glial
CC cells. {ECO:0000269|PubMed:10556305}.
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DR EMBL; AK032324; BAC27815.1; -; mRNA.
DR EMBL; AK009260; BAB26177.1; -; mRNA.
DR EMBL; AK156205; BAE33625.1; -; mRNA.
DR EMBL; AF159549; AAF15316.1; -; mRNA.
DR EMBL; BC056192; AAH56192.1; -; mRNA.
DR CCDS; CCDS27284.1; -.
DR RefSeq; NP_038773.1; NM_013745.5.
DR AlphaFoldDB; Q9QXX8; -.
DR SMR; Q9QXX8; -.
DR BioGRID; 205155; 2.
DR IntAct; Q9QXX8; 1.
DR MINT; Q9QXX8; -.
DR STRING; 10090.ENSMUSP00000022586; -.
DR iPTMnet; Q9QXX8; -.
DR PhosphoSitePlus; Q9QXX8; -.
DR EPD; Q9QXX8; -.
DR MaxQB; Q9QXX8; -.
DR PaxDb; Q9QXX8; -.
DR PeptideAtlas; Q9QXX8; -.
DR PRIDE; Q9QXX8; -.
DR ProteomicsDB; 295464; -.
DR Antibodypedia; 23576; 98 antibodies from 28 providers.
DR Ensembl; ENSMUST00000022586; ENSMUSP00000022586; ENSMUSG00000022009.
DR GeneID; 27275; -.
DR KEGG; mmu:27275; -.
DR UCSC; uc007ure.1; mouse.
DR CTD; 26747; -.
DR MGI; MGI:1351474; Nufip1.
DR VEuPathDB; HostDB:ENSMUSG00000022009; -.
DR eggNOG; ENOG502QPTB; Eukaryota.
DR GeneTree; ENSGT00390000003758; -.
DR HOGENOM; CLU_038059_0_0_1; -.
DR InParanoid; Q9QXX8; -.
DR OMA; KNHKWKN; -.
DR OrthoDB; 1394860at2759; -.
DR PhylomeDB; Q9QXX8; -.
DR TreeFam; TF329804; -.
DR BioGRID-ORCS; 27275; 18 hits in 75 CRISPR screens.
DR ChiTaRS; Nufip1; mouse.
DR PRO; PR:Q9QXX8; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9QXX8; protein.
DR Bgee; ENSMUSG00000022009; Expressed in cleaving embryo and 250 other tissues.
DR Genevisible; Q9QXX8; MM.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; ISS:HGNC-UCL.
DR GO; GO:0005730; C:nucleolus; ISS:HGNC-UCL.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005726; C:perichromatin fibrils; ISS:HGNC-UCL.
DR GO; GO:0070761; C:pre-snoRNP complex; ISO:MGI.
DR GO; GO:0048786; C:presynaptic active zone; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0008023; C:transcription elongation factor complex; ISS:HGNC-UCL.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IDA:MGI.
DR GO; GO:0030515; F:snoRNA binding; ISO:MGI.
DR GO; GO:0000492; P:box C/D snoRNP assembly; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:HGNC-UCL.
DR InterPro; IPR039136; NUFIP1-like.
DR InterPro; IPR019496; NUFIP1_cons_dom.
DR InterPro; IPR022755; Znf_C2H2_jaz.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR13309:SF1; PTHR13309:SF1; 1.
DR Pfam; PF10453; NUFIP1; 1.
DR Pfam; PF12171; zf-C2H2_jaz; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW Zinc; Zinc-finger.
FT CHAIN 1..484
FT /note="FMR1-interacting protein NUFIP1"
FT /id="PRO_0000245519"
FT ZN_FING 165..187
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 234..250
FT /note="Bipartite nuclear localization signal"
FT COMPBIAS 10..24
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..294
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHK0"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHK0"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHK0"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHK0"
SQ SEQUENCE 484 AA; 54713 MW; D17E4B099F4EA579 CRC64;
MAEPAPAVWP SAPDLTPAPG TPSEAAPPRD NWVYWAMLPP PPPPLSSPVA GSEQSRKGQP
HVLPQPPSGA LPPFDAQILP AAQPPFDAQA PPDAQSQFSG QQAWNLQAST PWYWGLSPNG
FSTYHTSYQS PVTHSYFPRS HDAKFNLPQN RKQKTKKRKE PVFHFFCDTC DRGFKNQEKY
DTHMSEHTKC PEVDCSFSAH EKIVQFHWRN MHAPGMKKIK LDTPEEIARW REERRKNYPT
LANIERKKKL QLEKAKRGEV LTTTQYGKMK GMSRHSQMAK IRSPGKHHKW RRGGARQRAV
VGLGNHARDS KPEVPSKANV DPLGALIHSD SESDKEEKAQ RTVVPKEVTP ALCSLMSSYG
DVSGSDSEPE EAPIKTEAEV LAENHVLHSS PPKSPKQNVQ TTGRTVSRSK WENQRNGLRK
ISLKRKKSHC HPLFEPRTHH PYLLEMLLAP DIRHERNVIL QCVRYIIKKD FFGLNTDSVK
TEEV
