MK67I_MOUSE
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 03-AUG-2022, entry version 155.
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 iPTMnet; Q91VE6; -.
DR PhosphoSitePlus; Q91VE6; -.
DR EPD; Q91VE6; -.
DR jPOST; Q91VE6; -.
DR MaxQB; Q91VE6; -.
DR PaxDb; Q91VE6; -.
DR PeptideAtlas; Q91VE6; -.
DR PRIDE; Q91VE6; -.
DR ProteomicsDB; 295676; -. [Q91VE6-1]
DR ProteomicsDB; 295677; -. [Q91VE6-2]
DR Antibodypedia; 4205; 409 antibodies from 34 providers.
DR DNASU; 67949; -.
DR Ensembl; ENSMUST00000027626; ENSMUSP00000027626; ENSMUSG00000026377. [Q91VE6-1]
DR Ensembl; ENSMUST00000112688; ENSMUSP00000108308; ENSMUSG00000026377. [Q91VE6-2]
DR GeneID; 67949; -.
DR KEGG; mmu:67949; -.
DR UCSC; uc007cic.2; mouse. [Q91VE6-1]
DR UCSC; uc011wql.1; mouse. [Q91VE6-2]
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; GSQRMFR; -.
DR OrthoDB; 1513142at2759; -.
DR PhylomeDB; Q91VE6; -.
DR TreeFam; TF315137; -.
DR BioGRID-ORCS; 67949; 27 hits in 74 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 253 other tissues.
DR ExpressionAtlas; Q91VE6; baseline and differential.
DR Genevisible; Q91VE6; MM.
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 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 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
