ID NUFP1_HUMAN Reviewed; 495 AA. AC Q9UHK0; Q8WVM5; Q96SG1; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-2007, sequence version 2. DT 10-JUN-2026, entry version 187. DE RecName: Full=FMR1-interacting protein NUFIP1 {ECO:0000305|PubMed:10556305}; DE AltName: Full=Nuclear FMR1-interacting protein 1 {ECO:0000312|HGNC:HGNC:8057}; DE AltName: Full=Nuclear FMRP-interacting protein 1; GN Name=NUFIP1 {ECO:0000312|HGNC:HGNC:8057}; 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], VARIANT ARG-36, FUNCTION, SUBCELLULAR LOCATION, RP TISSUE 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 GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 163-495. RC TISSUE=Duodenum; 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 [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338; SER-340 AND SER-342, AND RP IDENTIFICATION BY 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 [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338; SER-340 AND SER-342, 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 [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338; SER-340 AND SER-342, 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338; SER-340 AND SER-342, 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 [8] 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403, AND IDENTIFICATION BY RP 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 [10] RP INTERACTION WITH ZNHIT3. RX PubMed=28335020; DOI=10.1093/brain/awx040; RA Anttonen A.K., Laari A., Kousi M., Yang Y.J., Jaeaeskelaeinen T., Somer M., RA Siintola E., Jakkula E., Muona M., Tegelberg S., Loennqvist T., Pihko H., RA Valanne L., Paetau A., Lun M.P., Haestbacka J., Kopra O., Joensuu T., RA Katsanis N., Lehtinen M.K., Palvimo J.J., Lehesjoki A.E.; RT "ZNHIT3 is defective in PEHO syndrome, a severe encephalopathy with RT cerebellar granule neuron loss."; RL Brain 140:1267-1279(2017). RN [11] RP INTERACTION WITH NOP2; NOP56 AND RUVBL1. RX PubMed=36161484; DOI=10.1093/nar/gkac817; RA Liao H., Gaur A., McConie H., Shekar A., Wang K., Chang J.T., Breton G., RA Denicourt C.; RT "Human NOP2/NSUN1 regulates ribosome biogenesis through non-catalytic RT complex formation with box C/D snoRNPs."; RL Nucleic Acids Res. 50:10695-10716(2022). CC -!- FUNCTION: Binds RNA. {ECO:0000269|PubMed:10556305}. CC -!- SUBUNIT: Interacts with FMR1 (PubMed:10556305). Interacts with ZNHIT3 CC (PubMed:28335020). Interacts with NOP2, NOP56 and RUVBL1 CC (PubMed:36161484). {ECO:0000269|PubMed:10556305, CC ECO:0000269|PubMed:28335020, ECO:0000269|PubMed:36161484}. CC -!- INTERACTION: CC Q9UHK0; Q9Y2X3: NOP58; NbExp=3; IntAct=EBI-2563549, EBI-395469; CC Q9UHK0; P55769: SNU13; NbExp=2; IntAct=EBI-2563549, EBI-712228; CC Q9UHK0; Q15649: ZNHIT3; NbExp=10; IntAct=EBI-2563549, EBI-2563564; CC Q9UHK0; Q9NWK9: ZNHIT6; NbExp=3; IntAct=EBI-2563549, EBI-2563515; CC Q9UHK0; P60122: Ruvbl1; Xeno; NbExp=2; IntAct=EBI-2563549, EBI-1634999; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10556305}. CC Note=Distributed in the nucleus in a dot-like pattern. CC -!- TISSUE SPECIFICITY: Expressed in spleen, thymus, prostate, testis, CC ovary, small intestine, colon, peripheral blood leukocyte, heart, CC brain, placenta, lung, liver, skeletal muscle, kidney, and pancreas. CC {ECO:0000269|PubMed:10556305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH17745.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF159548; AAF15315.1; -; mRNA. DR EMBL; AL354816; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL359706; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC017745; AAH17745.1; ALT_INIT; mRNA. DR CCDS; CCDS9393.1; -. DR RefSeq; NP_036477.2; NM_012345.3. DR PDB; 5L85; NMR; -; B=462-495. DR PDBsum; 5L85; -. DR AlphaFoldDB; Q9UHK0; -. DR SMR; Q9UHK0; -. DR BioGRID; 117807; 145. DR CORUM; Q9UHK0; -. DR DIP; DIP-41010N; -. DR FunCoup; Q9UHK0; 2712. DR IntAct; Q9UHK0; 122. DR MINT; Q9UHK0; -. DR STRING; 9606.ENSP00000368459; -. DR GlyGen; Q9UHK0; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9UHK0; -. DR PhosphoSitePlus; Q9UHK0; -. DR BioMuta; NUFIP1; -. DR DMDM; 134047852; -. DR jPOST; Q9UHK0; -. DR MassIVE; Q9UHK0; -. DR PaxDb; 9606-ENSP00000368459; -. DR PeptideAtlas; Q9UHK0; -. DR ProteomicsDB; 84368; -. DR Pumba; Q9UHK0; -. DR Antibodypedia; 23576; 96 antibodies from 28 providers. DR DNASU; 26747; -. DR Ensembl; ENST00000379161.5; ENSP00000368459.4; ENSG00000083635.8. DR GeneID; 26747; -. DR KEGG; hsa:26747; -. DR MANE-Select; ENST00000379161.5; ENSP00000368459.4; NM_012345.3; NP_036477.2. DR UCSC; uc001uzp.3; human. DR AGR; HGNC:8057; -. DR ClinPGx; PA31843; -. DR CTD; 26747; -. DR DisGeNET; 26747; -. DR GeneCards; NUFIP1; -. DR HGNC; HGNC:8057; NUFIP1. DR HPA; ENSG00000083635; Low tissue specificity. DR MIM; 604354; gene. DR OpenTargets; ENSG00000083635; -. DR VEuPathDB; HostDB:ENSG00000083635; -. DR eggNOG; ENOG502QPTB; Eukaryota. DR GeneTree; ENSGT00390000003758; -. DR HOGENOM; CLU_038059_0_0_1; -. DR InParanoid; Q9UHK0; -. DR OMA; WMFWAML; -. DR OrthoDB; 273070at2759; -. DR PAN-GO; Q9UHK0; 3 GO annotations based on evolutionary models. DR PhylomeDB; Q9UHK0; -. DR PathwayCommons; Q9UHK0; -. DR SignaLink; Q9UHK0; -. DR Agora; ENSG00000083635; -. DR BioGRID-ORCS; 26747; 357 hits in 1157 CRISPR screens. DR ChiTaRS; NUFIP1; human. DR GeneWiki; NUFIP1; -. DR GenomeRNAi; 26747; -. DR Pharos; Q9UHK0; Tbio. DR PRO; PR:Q9UHK0; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; Q9UHK0; protein. DR Bgee; ENSG00000083635; Expressed in endothelial cell and 151 other cell types or tissues. DR GO; GO:0016363; C:nuclear matrix; IDA:HGNC-UCL. DR GO; GO:0005730; C:nucleolus; IDA:HGNC-UCL. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005726; C:perichromatin fibrils; IDA:HGNC-UCL. DR GO; GO:0070761; C:pre-snoRNP complex; IDA:BHF-UCL. DR GO; GO:0048786; C:presynaptic active zone; ISS:HGNC. DR GO; GO:0032991; C:protein-containing complex; IDA:BHF-UCL. DR GO; GO:0008023; C:transcription elongation factor complex; IDA:HGNC-UCL. DR GO; GO:0051117; F:ATPase binding; IPI:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:BHF-UCL. DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:BHF-UCL. DR GO; GO:0003723; F:RNA binding; IDA:HGNC-UCL. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0000492; P:box C/D snoRNP assembly; IMP:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:HGNC-UCL. DR GO; GO:0006396; P:RNA processing; TAS:ProtInc. DR DisProt; DP03731; -. DR InterPro; IPR039136; NUFIP1-like. DR InterPro; IPR019496; NUFIP1_cons_dom. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR13309:SF1; FMR1-INTERACTING PROTEIN NUFIP1; 1. DR PANTHER; PTHR13309; NUCLEAR FRAGILE X MENTAL RETARDATION PROTEIN INTERACTING PROTEIN 1; 1. DR Pfam; PF10453; NUFIP1; 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 3D-structure; Metal-binding; Nucleus; Phosphoprotein; KW Proteomics identification; Reference proteome; RNA-binding; Zinc; KW Zinc-finger. FT CHAIN 1..495 FT /note="FMR1-interacting protein NUFIP1" FT /id="PRO_0000245518" FT ZN_FING 174..196 FT /note="C2H2-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 1..108 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 277..357 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 413..435 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 243..260 FT /note="Bipartite nuclear localization signal" FT COMPBIAS 98..108 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 416..431 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 338 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 340 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 342 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 403 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT VARIANT 36 FT /note="S -> R (in dbSNP:rs1140993)" FT /evidence="ECO:0000269|PubMed:10556305" FT /id="VAR_026978" FT HELIX 463..477 FT /evidence="ECO:0007829|PDB:5L85" FT HELIX 478..482 FT /evidence="ECO:0007829|PDB:5L85" SQ SEQUENCE 495 AA; 56300 MW; 318418FB08071001 CRC64; MAEPTSDFET PIGWHASPEL TPTLGPLSDT APPRDSWMFW AMLPPPPPPL TSSLPAAGSK PSSESQPPME AQSLPGAPPP FDAQILPGAQ PPFDAQSPLD SQPQPSGQPW NFHASTSWYW RQSSDRFPRH QKSFNPAVKN SYYPRKYDAK FTDFSLPPSR KQKKKKRKEP VFHFFCDTCD RGFKNQEKYD KHMSEHTKCP ELDCSFTAHE KIVQFHWRNM HAPGMKKIKL DTPEEIARWR EERRKNYPTL ANIERKKKLK LEKEKRGAVL TTTQYGKMKG MSRHSQMAKI RSPGKNHKWK NDNSRQRAVT GSGSHLCDLK LEGPPEANAD PLGVLINSDS ESDKEEKPQH SVIPKEVTPA LCSLMSSYGS LSGSESEPEE TPIKTEADVL AENQVLDSSA PKSPSQDVKA TVRNFSEAKS ENRKKSFEKT NPKRKKDYHN YQTLFEPRTH HPYLLEMLLA PDIRHERNVI LQCVRYIIKK DFFGLDTNSA KSKDV //