NUFP1_HUMAN
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 03-AUG-2022, entry version 169.
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).
CC -!- FUNCTION: Binds RNA. {ECO:0000269|PubMed:10556305}.
CC -!- SUBUNIT: Interacts with FMR1 (PubMed:10556305). Interacts with ZNHIT3
CC (PubMed:28335020). {ECO:0000269|PubMed:10556305,
CC ECO:0000269|PubMed:28335020}.
CC -!- INTERACTION:
CC Q9UHK0; P55769: SNU13; NbExp=2; IntAct=EBI-2563549, EBI-712228;
CC Q9UHK0; Q15649: ZNHIT3; NbExp=7; IntAct=EBI-2563549, EBI-2563564;
CC Q9UHK0; Q9NWK9: ZNHIT6; NbExp=2; 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};
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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_012345.2.
DR PDB; 5L85; NMR; -; B=462-495.
DR PDBsum; 5L85; -.
DR AlphaFoldDB; Q9UHK0; -.
DR SMR; Q9UHK0; -.
DR BioGRID; 117807; 136.
DR DIP; DIP-41010N; -.
DR IntAct; Q9UHK0; 94.
DR MINT; Q9UHK0; -.
DR STRING; 9606.ENSP00000368459; -.
DR iPTMnet; Q9UHK0; -.
DR PhosphoSitePlus; Q9UHK0; -.
DR BioMuta; NUFIP1; -.
DR DMDM; 134047852; -.
DR EPD; Q9UHK0; -.
DR jPOST; Q9UHK0; -.
DR MassIVE; Q9UHK0; -.
DR MaxQB; Q9UHK0; -.
DR PaxDb; Q9UHK0; -.
DR PeptideAtlas; Q9UHK0; -.
DR PRIDE; Q9UHK0; -.
DR ProteomicsDB; 84368; -.
DR Antibodypedia; 23576; 98 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 CTD; 26747; -.
DR DisGeNET; 26747; -.
DR GeneCards; NUFIP1; -.
DR HGNC; HGNC:8057; NUFIP1.
DR HPA; ENSG00000083635; Low tissue specificity.
DR MIM; 604354; gene.
DR neXtProt; NX_Q9UHK0; -.
DR OpenTargets; ENSG00000083635; -.
DR PharmGKB; PA31843; -.
DR VEuPathDB; HostDB:ENSG00000083635; -.
DR eggNOG; ENOG502QPTB; Eukaryota.
DR GeneTree; ENSGT00390000003758; -.
DR HOGENOM; CLU_038059_0_0_1; -.
DR InParanoid; Q9UHK0; -.
DR OMA; KNHKWKN; -.
DR OrthoDB; 1394860at2759; -.
DR PhylomeDB; Q9UHK0; -.
DR TreeFam; TF329804; -.
DR PathwayCommons; Q9UHK0; -.
DR SignaLink; Q9UHK0; -.
DR BioGRID-ORCS; 26747; 332 hits in 1079 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 149 other tissues.
DR Genevisible; Q9UHK0; HS.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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: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 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 3D-structure; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; Zinc; 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 39..54
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..86
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..435
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..480
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
