MK67I_HUMAN
ID MK67I_HUMAN Reviewed; 293 AA.
AC Q9BYG3; A8K788; Q8TB66; Q96ED4;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=MKI67 FHA domain-interacting nucleolar phosphoprotein;
DE AltName: Full=Nucleolar phosphoprotein Nopp34;
DE AltName: Full=Nucleolar protein interacting with the FHA domain of pKI-67;
DE Short=hNIFK;
GN Name=NIFK; Synonyms=MKI67IP, NOPP34;
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], INTERACTION WITH MKI67, MUTAGENESIS OF THR-234
RP AND THR-238, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=11342549; DOI=10.1074/jbc.m102227200;
RA Takagi M., Sueishi M., Saiwaki T., Kametaka A., Yoneda Y.;
RT "A novel nucleolar protein, NIFK, interacts with the forkhead associated
RT domain of Ki-67 antigen in mitosis.";
RL J. Biol. Chem. 276:25386-25391(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-144.
RC TISSUE=Brain, Lung, and Placenta;
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 [6]
RP PROTEIN SEQUENCE OF 2-24; 87-114; 180-192; 227-244 AND 272-284, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [8]
RP PHOSPHORYLATION AT THR-234, AND INTERACTION WITH MKI67.
RX PubMed=14659764; DOI=10.1016/j.jmb.2003.10.032;
RA Li H., Byeon I.-J., Ju Y., Tsai M.-D.;
RT "Structure of human Ki67 FHA domain and its binding to a phosphoprotein
RT fragment from hNIFK reveal unique recognition sites and new views to the
RT structural basis of FHA domain functions.";
RL J. Mol. Biol. 335:371-381(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-223, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-234; THR-238 AND THR-279, 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [12]
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218 AND THR-223, 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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218; THR-223 AND SER-247, 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 [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145; THR-223 AND SER-247, 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 [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-271, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-38; LYS-139; LYS-179; LYS-192 AND
RP LYS-271, AND IDENTIFICATION 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).
RN [20]
RP STRUCTURE BY NMR OF 226-269 IN COMPLEX WITH MKI67, IDENTIFICATION BY MASS
RP SPECTROMETRY, MUTAGENESIS OF SER-230; THR-234; PRO-235; THR-238 AND
RP PRO-239, AND PHOSPHORYLATION AT SER-230; THR-234 AND THR-238.
RX PubMed=16244663; DOI=10.1038/nsmb1008;
RA Byeon I.-J., Li H., Song H., Gronenborn A.M., Tsai M.-D.;
RT "Sequential phosphorylation and multisite interactions characterize
RT specific target recognition by the FHA domain of Ki67.";
RL Nat. Struct. Mol. Biol. 12:987-993(2005).
RN [21]
RP METHYLATION AT ARG-114; ARG-244; ARG-245 AND ARG-284, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=26529540; DOI=10.1021/acs.biochem.5b00995;
RA Lee W.C., Lin W.L., Matsui T., Chen E.S., Wei T.Y., Lin W.H., Hu H.,
RA Zheng Y.G., Tsai M.D., Ho M.C.;
RT "Protein Arginine Methyltransferase 8: Tetrameric Structure and Protein
RT Substrate Specificity.";
RL Biochemistry 54:7514-7523(2015).
CC -!- SUBUNIT: Binds to the FHA domain of MKI67; this interaction is enhanced
CC in mitosis. {ECO:0000269|PubMed:16244663}.
CC -!- INTERACTION:
CC Q9BYG3; P46013: MKI67; NbExp=3; IntAct=EBI-2561019, EBI-876367;
CC Q9BYG3; Q15025: TNIP1; NbExp=3; IntAct=EBI-2561019, EBI-357849;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Chromosome. Note=Localizes to
CC mitotic chromosomes in conjunction with MKI67.
CC -!- PTM: Sequentially phosphorylated on Thr-238, Thr-234 and Ser-230. Thr-
CC 234 is phosphorylated only when Thr-238 is phosphorylated. Likewise,
CC phosphorylation at Ser-230 requires that Thr-234 and Thr-238 are
CC phosphorylated. Phosphorylation enhances MKI67 binding.
CC {ECO:0000269|PubMed:11342549, ECO:0000269|PubMed:14659764,
CC ECO:0000269|PubMed:16244663}.
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DR EMBL; AB044971; BAB41210.1; -; mRNA.
DR EMBL; AK291903; BAF84592.1; -; mRNA.
DR EMBL; AC018737; AAY14830.1; -; Genomic_DNA.
DR EMBL; CH471103; EAW95261.1; -; Genomic_DNA.
DR EMBL; BC012457; AAH12457.1; -; mRNA.
DR EMBL; BC022990; AAH22990.1; -; mRNA.
DR EMBL; BC024238; AAH24238.1; -; mRNA.
DR CCDS; CCDS2135.1; -.
DR RefSeq; NP_115766.3; NM_032390.4.
DR PDB; 2AFF; NMR; -; B=226-269.
DR PDBsum; 2AFF; -.
DR AlphaFoldDB; Q9BYG3; -.
DR BMRB; Q9BYG3; -.
DR SMR; Q9BYG3; -.
DR BioGRID; 124066; 406.
DR DIP; DIP-28134N; -.
DR IntAct; Q9BYG3; 96.
DR MINT; Q9BYG3; -.
DR STRING; 9606.ENSP00000285814; -.
DR ChEMBL; CHEMBL4523443; -.
DR GlyGen; Q9BYG3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BYG3; -.
DR PhosphoSitePlus; Q9BYG3; -.
DR BioMuta; NIFK; -.
DR DMDM; 71151919; -.
DR SWISS-2DPAGE; Q9BYG3; -.
DR EPD; Q9BYG3; -.
DR jPOST; Q9BYG3; -.
DR MassIVE; Q9BYG3; -.
DR MaxQB; Q9BYG3; -.
DR PaxDb; Q9BYG3; -.
DR PeptideAtlas; Q9BYG3; -.
DR PRIDE; Q9BYG3; -.
DR ProteomicsDB; 79637; -.
DR Antibodypedia; 4205; 409 antibodies from 34 providers.
DR DNASU; 84365; -.
DR Ensembl; ENST00000285814.9; ENSP00000285814.4; ENSG00000155438.12.
DR GeneID; 84365; -.
DR KEGG; hsa:84365; -.
DR MANE-Select; ENST00000285814.9; ENSP00000285814.4; NM_032390.5; NP_115766.3.
DR UCSC; uc002tnk.4; human.
DR CTD; 84365; -.
DR DisGeNET; 84365; -.
DR GeneCards; NIFK; -.
DR HGNC; HGNC:17838; NIFK.
DR HPA; ENSG00000155438; Low tissue specificity.
DR MIM; 611970; gene.
DR neXtProt; NX_Q9BYG3; -.
DR OpenTargets; ENSG00000155438; -.
DR PharmGKB; PA38470; -.
DR VEuPathDB; HostDB:ENSG00000155438; -.
DR eggNOG; KOG4208; Eukaryota.
DR GeneTree; ENSGT00390000011515; -.
DR HOGENOM; CLU_025741_1_0_1; -.
DR InParanoid; Q9BYG3; -.
DR OMA; GSQRMFR; -.
DR OrthoDB; 1513142at2759; -.
DR PhylomeDB; Q9BYG3; -.
DR TreeFam; TF315137; -.
DR PathwayCommons; Q9BYG3; -.
DR SignaLink; Q9BYG3; -.
DR SIGNOR; Q9BYG3; -.
DR BioGRID-ORCS; 84365; 766 hits in 1025 CRISPR screens.
DR ChiTaRS; NIFK; human.
DR EvolutionaryTrace; Q9BYG3; -.
DR GeneWiki; MKI67IP; -.
DR GenomeRNAi; 84365; -.
DR Pharos; Q9BYG3; Tbio.
DR PRO; PR:Q9BYG3; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9BYG3; protein.
DR Bgee; ENSG00000155438; Expressed in calcaneal tendon and 189 other tissues.
DR ExpressionAtlas; Q9BYG3; baseline and differential.
DR Genevisible; Q9BYG3; HS.
DR GO; GO:0005694; C:chromosome; IDA:HPA.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0065003; P:protein-containing complex assembly; NAS:UniProtKB.
DR GO; GO:0016072; P:rRNA metabolic process; NAS:UniProtKB.
DR GO; GO:0009303; P:rRNA transcription; NAS:UniProtKB.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR021043; NIFK_FHA_Ki67-binding.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF12196; hNIFK_binding; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromosome; Direct protein sequencing;
KW Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..293
FT /note="MKI67 FHA domain-interacting nucleolar
FT phosphoprotein"
FT /id="PRO_0000081629"
FT DOMAIN 45..123
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 197..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..269
FT /note="Interaction with MKI67"
FT REGION 271..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 114
FT /note="Omega-N-methylarginine; by PRMT1 and PRMT8"
FT /evidence="ECO:0000269|PubMed:26529540"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 223
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16244663"
FT MOD_RES 234
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:14659764,
FT ECO:0000269|PubMed:16244663, ECO:0007744|PubMed:18669648"
FT MOD_RES 238
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:16244663,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 244
FT /note="Omega-N-methylated arginine; by PRMT1 and PRMT8"
FT /evidence="ECO:0000269|PubMed:26529540"
FT MOD_RES 245
FT /note="Omega-N-methylated arginine; by PRMT1 and PRMT8"
FT /evidence="ECO:0000269|PubMed:26529540"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 279
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 284
FT /note="Omega-N-methylarginine; by PRMT1 and PRMT8"
FT /evidence="ECO:0000269|PubMed:26529540"
FT CROSSLNK 38
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 179
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 192
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 271
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 271
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 144
FT /note="P -> Q (in dbSNP:rs17852212)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027182"
FT MUTAGEN 230
FT /note="S->A: Loss of phosphorylation site."
FT /evidence="ECO:0000269|PubMed:16244663"
FT MUTAGEN 234
FT /note="T->A: Loss of phosphorylation site. Abrogates
FT interaction with MKI67."
FT /evidence="ECO:0000269|PubMed:11342549,
FT ECO:0000269|PubMed:16244663"
FT MUTAGEN 235
FT /note="P->A: Reduces phosphorylation at T-234."
FT /evidence="ECO:0000269|PubMed:16244663"
FT MUTAGEN 238
FT /note="T->A: Loss of phosphorylation site. Abrogates
FT interaction with MKI67."
FT /evidence="ECO:0000269|PubMed:11342549,
FT ECO:0000269|PubMed:16244663"
FT MUTAGEN 239
FT /note="P->A: Reduces phosphorylation at T-234 and T-238."
FT /evidence="ECO:0000269|PubMed:16244663"
FT HELIX 239..251
FT /evidence="ECO:0007829|PDB:2AFF"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:2AFF"
FT STRAND 260..265
FT /evidence="ECO:0007829|PDB:2AFF"
SQ SEQUENCE 293 AA; 34222 MW; 9D288ECF2B4CE119 CRC64;
MATFSGPAGP ILSLNPQEDV EFQKEVAQVR KRITQRKKQE QLTPGVVYVR HLPNLLDETQ
IFSYFSQFGT VTRFRLSRSK RTGNSKGYAF VEFESEDVAK IVAETMNNYL FGERLLECHF
MPPEKVHKEL FKDWNIPFKQ PSYPSVKRYN RNRTLTQKLR MEERFKKKER LLRKKLAKKG
IDYDFPSLIL QKTESISKTN RQTSTKGQVL RKKKKKVSGT LDTPEKTVDS QGPTPVCTPT
FLERRKSQVA ELNDDDKDDE IVFKQPISCV KEEIQETQTP THSRKKRRRS SNQ
