MK67I_RAT
ID MK67I_RAT Reviewed; 271 AA.
AC Q5RJM0;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=MKI67 FHA domain-interacting nucleolar phosphoprotein;
DE AltName: Full=Nucleolar protein interacting with the FHA domain of pKI-67;
GN Name=Nifk; Synonyms=Mki67ip;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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).
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 -!- PTM: Phosphorylated. {ECO:0000250}.
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DR EMBL; BC086585; AAH86585.1; -; mRNA.
DR RefSeq; NP_631925.2; NM_139186.2.
DR AlphaFoldDB; Q5RJM0; -.
DR SMR; Q5RJM0; -.
DR STRING; 10116.ENSRNOP00000058336; -.
DR iPTMnet; Q5RJM0; -.
DR PhosphoSitePlus; Q5RJM0; -.
DR PaxDb; Q5RJM0; -.
DR PRIDE; Q5RJM0; -.
DR GeneID; 246042; -.
DR KEGG; rno:246042; -.
DR CTD; 84365; -.
DR RGD; 708462; Nifk.
DR VEuPathDB; HostDB:ENSRNOG00000025701; -.
DR eggNOG; KOG4208; Eukaryota.
DR HOGENOM; CLU_025741_1_0_1; -.
DR InParanoid; Q5RJM0; -.
DR OMA; GSQRMFR; -.
DR OrthoDB; 1513142at2759; -.
DR PhylomeDB; Q5RJM0; -.
DR TreeFam; TF315137; -.
DR PRO; PR:Q5RJM0; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000025701; Expressed in thymus and 20 other tissues.
DR ExpressionAtlas; Q5RJM0; baseline and differential.
DR Genevisible; Q5RJM0; RN.
DR GO; GO:0000794; C:condensed nuclear chromosome; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; ISO:RGD.
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 2: Evidence at transcript level;
KW Acetylation; Chromosome; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT CHAIN 2..271
FT /note="MKI67 FHA domain-interacting nucleolar
FT phosphoprotein"
FT /id="PRO_0000247991"
FT DOMAIN 44..122
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT MOD_RES 113
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT MOD_RES 213
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT MOD_RES 217
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT MOD_RES 223
FT /note="Omega-N-methylated arginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT MOD_RES 224
FT /note="Omega-N-methylated arginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT CROSSLNK 37
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT CROSSLNK 178
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT CROSSLNK 191
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT CROSSLNK 247
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT CROSSLNK 247
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9BYG3"
SQ SEQUENCE 271 AA; 31351 MW; 14472E53C24EC24E CRC64;
MAEYSGPAKP TLALNPREDS QFEKDLTQIQ RRAKKKKEEK LNSGVVYLGH LPSTLSESHI
YDYCAQFGDI RRFRLSRSKR TGNSRGFAFV EFESEDVAKI VAETMDNYLF GERLLSCKFM
PREKVHKDLF NQCNVPFHPP SFPAVKRYNQ KRGHLQMLKM EYRFKKKEKL LRKKLAKKGI
DYSFPSLVLP KPKKEISSIA NTHGDSEANQ DPTPVCTPTF LERRKSQLME INDDDEIILK
LPVSPVKEDT QKTPAPESSG KKRLRKRKSK Q
