ID   MK67I_MOUSE             Reviewed;         317 AA.
AC   Q91VE6; Q8BMV9; Q8BVL4;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   24-JAN-2024, entry version 163.
DE   RecName: Full=MKI67 FHA domain-interacting nucleolar phosphoprotein;
DE   AltName: Full=Nucleolar protein interacting with the FHA domain of pKI-67;
DE            Short=mNIFK;
GN   Name=Nifk; Synonyms=Mki67ip;
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] (ISOFORM 1).
RC   TISSUE=Ascitic tumor;
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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   STRAIN=NMRI; TISSUE=Skeletal muscle;
RX   PubMed=12798774; DOI=10.1016/s1065-6995(03)00038-6;
RA   Magnusson C., Norrby M., Libelius R., Tagerud S.;
RT   "The nifk gene is widely expressed in mouse tissues and is up-regulated in
RT   denervated hind limb muscle.";
RL   Cell Biol. Int. 27:469-475(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 1-125 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Thymus;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Olfactory epithelium;
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-257 AND THR-261, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   CITRULLINATION AT ARG-203.
RX   PubMed=24463520; DOI=10.1038/nature12942;
RA   Christophorou M.A., Castelo-Branco G., Halley-Stott R.P., Oliveira C.S.,
RA   Loos R., Radzisheuskaya A., Mowen K.A., Bertone P., Silva J.C.,
RA   Zernicka-Goetz M., Nielsen M.L., Gurdon J.B., Kouzarides T.;
RT   "Citrullination regulates pluripotency and histone H1 binding to
RT   chromatin.";
RL   Nature 507:104-108(2014).
CC   -!- SUBUNIT: Binds to the FHA domain of MKI67; this interaction is enhanced
CC       in mitosis. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Chromosome {ECO:0000250}.
CC       Note=Localizes to mitotic chromosomes in conjunction with MKI67.
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q91VE6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q91VE6-2; Sequence=VSP_014634;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, heart, hind limb muscles,
CC       intestine, liver, skin and spleen. {ECO:0000269|PubMed:12798774}.
CC   -!- PTM: Phosphorylated. {ECO:0000250}.
CC   -!- PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}.
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DR   EMBL; AB056870; BAB61920.1; -; mRNA.
DR   EMBL; AY030275; AAK38160.1; -; mRNA.
DR   EMBL; AK019209; BAC25583.2; -; mRNA.
DR   EMBL; AK077770; BAC36999.1; -; mRNA.
DR   EMBL; BC058559; AAH58559.1; -; mRNA.
DR   CCDS; CCDS15222.1; -. [Q91VE6-1]
DR   RefSeq; NP_080748.3; NM_026472.4. [Q91VE6-1]
DR   AlphaFoldDB; Q91VE6; -.
DR   SMR; Q91VE6; -.
DR   BioGRID; 212560; 6.
DR   CORUM; Q91VE6; -.
DR   IntAct; Q91VE6; 2.
DR   STRING; 10090.ENSMUSP00000027626; -.
DR   GlyGen; Q91VE6; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q91VE6; -.
DR   PhosphoSitePlus; Q91VE6; -.
DR   EPD; Q91VE6; -.
DR   jPOST; Q91VE6; -.
DR   MaxQB; Q91VE6; -.
DR   PaxDb; 10090-ENSMUSP00000027626; -.
DR   PeptideAtlas; Q91VE6; -.
DR   ProteomicsDB; 295676; -. [Q91VE6-1]
DR   ProteomicsDB; 295677; -. [Q91VE6-2]
DR   Pumba; Q91VE6; -.
DR   Antibodypedia; 4205; 475 antibodies from 34 providers.
DR   DNASU; 67949; -.
DR   Ensembl; ENSMUST00000027626.13; ENSMUSP00000027626.7; ENSMUSG00000026377.13. [Q91VE6-1]
DR   Ensembl; ENSMUST00000112688.10; ENSMUSP00000108308.4; ENSMUSG00000026377.13. [Q91VE6-2]
DR   GeneID; 67949; -.
DR   KEGG; mmu:67949; -.
DR   UCSC; uc007cic.2; mouse. [Q91VE6-1]
DR   UCSC; uc011wql.1; mouse. [Q91VE6-2]
DR   AGR; MGI:1915199; -.
DR   CTD; 84365; -.
DR   MGI; MGI:1915199; Nifk.
DR   VEuPathDB; HostDB:ENSMUSG00000026377; -.
DR   eggNOG; KOG4208; Eukaryota.
DR   GeneTree; ENSGT00390000011515; -.
DR   HOGENOM; CLU_025741_1_0_1; -.
DR   InParanoid; Q91VE6; -.
DR   OMA; RKSMVVD; -.
DR   OrthoDB; 12519at2759; -.
DR   PhylomeDB; Q91VE6; -.
DR   TreeFam; TF315137; -.
DR   BioGRID-ORCS; 67949; 27 hits in 79 CRISPR screens.
DR   ChiTaRS; Nifk; mouse.
DR   PRO; PR:Q91VE6; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q91VE6; Protein.
DR   Bgee; ENSMUSG00000026377; Expressed in primitive streak and 257 other cell types or tissues.
DR   ExpressionAtlas; Q91VE6; baseline and differential.
DR   GO; GO:0005694; C:chromosome; ISO:MGI.
DR   GO; GO:0000794; C:condensed nuclear chromosome; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0003723; F:RNA binding; ISO:MGI.
DR   GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   CDD; cd12307; RRM_NIFK_like; 1.
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   PANTHER; PTHR46754; MKI67 FHA DOMAIN-INTERACTING NUCLEOLAR PHOSPHOPROTEIN; 1.
DR   PANTHER; PTHR46754:SF1; MKI67 FHA DOMAIN-INTERACTING NUCLEOLAR PHOSPHOPROTEIN; 1.
DR   Pfam; PF12196; hNIFK_binding; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   Genevisible; Q91VE6; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Chromosome; Citrullination;
KW   Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW   RNA-binding; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT   CHAIN           2..317
FT                   /note="MKI67 FHA domain-interacting nucleolar
FT                   phosphoprotein"
FT                   /id="PRO_0000081630"
FT   DOMAIN          47..125
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          203..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..238
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..288
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT   MOD_RES         116
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT   MOD_RES         203
FT                   /note="Citrulline"
FT                   /evidence="ECO:0000269|PubMed:24463520"
FT   MOD_RES         219
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT   MOD_RES         253
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT   MOD_RES         257
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         261
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         267
FT                   /note="Omega-N-methylated arginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT   MOD_RES         268
FT                   /note="Omega-N-methylated arginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT   MOD_RES         270
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355"
FT   MOD_RES         301
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT   CROSSLNK        40
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT   CROSSLNK        181
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT   CROSSLNK        194
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT   CROSSLNK        293
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT   CROSSLNK        293
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT   VAR_SEQ         36..83
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_014634"
FT   CONFLICT        18
FT                   /note="E -> G (in Ref. 3; BAC36999)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   317 AA;  36265 MW;  08CC82E54EA2D580 CRC64;
     MAGLAGPAKP SLALNPQEDS QFEKALTQIQ GRTKKPQQKK KEKLNRGVVY LGHLPSTLSE
     SHIYNYCAQF GDISRFRLSR SKRTGNSKGY AFVEFESEDV AKIVAETMDN YLFGERLLSC
     KFMPRKKVHK DLFSQRNALF HRPSFPAVKR YNRKRGHLQM LKMEYRFKKK EKLLRKKLAA
     KGIDYSFPSL VLPKPKNIAV AHRDSEGNQV LPDQKEGLSG EPRRKEKMMK EDISNNIPKK
     RKRSRRKKSS VDSQGPTPVC TPTFLERRKS QVMEVGGDKD DEIILKLPVP PVKEDTQKTP
     TSASPGGKRP RKRKSKQ
//