MK67I_BOVIN
ID MK67I_BOVIN Reviewed; 296 AA.
AC Q3SZM1;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; BC102791; AAI02792.1; -; mRNA.
DR RefSeq; NP_001029526.1; NM_001034354.2.
DR AlphaFoldDB; Q3SZM1; -.
DR SMR; Q3SZM1; -.
DR STRING; 9913.ENSBTAP00000031516; -.
DR PaxDb; Q3SZM1; -.
DR PRIDE; Q3SZM1; -.
DR Ensembl; ENSBTAT00000031564; ENSBTAP00000031516; ENSBTAG00000019387.
DR GeneID; 509598; -.
DR KEGG; bta:509598; -.
DR CTD; 84365; -.
DR VEuPathDB; HostDB:ENSBTAG00000019387; -.
DR VGNC; VGNC:32076; NIFK.
DR eggNOG; KOG4208; Eukaryota.
DR GeneTree; ENSGT00390000011515; -.
DR HOGENOM; CLU_025741_1_0_1; -.
DR InParanoid; Q3SZM1; -.
DR OMA; GSQRMFR; -.
DR OrthoDB; 1513142at2759; -.
DR TreeFam; TF315137; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000019387; Expressed in oocyte and 104 other tissues.
DR GO; GO:0000794; C:condensed nuclear chromosome; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
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..296
FT /note="MKI67 FHA domain-interacting nucleolar
FT phosphoprotein"
FT /id="PRO_0000247990"
FT DOMAIN 45..123
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..272
FT /note="Interaction with MKI67"
FT /evidence="ECO:0000250"
FT COMPBIAS 18..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..265
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 114
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT MOD_RES 226
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT MOD_RES 237
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT MOD_RES 241
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT MOD_RES 248
FT /note="Omega-N-methylated arginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT CROSSLNK 139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT CROSSLNK 179
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT CROSSLNK 274
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9BYG3"
FT CROSSLNK 274
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9BYG3"
SQ SEQUENCE 296 AA; 34155 MW; 5DEEE503B8D8F7AC CRC64;
MAAFGGPAKP LLSLNPQEDA KFKKEVAQVR RRATKQQEKQ KPTPGVIYVG HLPPTLYETQ
IRAYFSQFGT VTRFRLSRSK KTGNSKGYGF VEFESEDVAK IAAETMNNYL FGERLLKCHF
IPPEKVHEEL FREWHMPFKR PSYPAVKRYN QNRSLVQKLR MEERFKKKEK LLRKRLAKKG
IDYNFPSLVK VLHKNEENAS NTGPQNSRKH QALRKKKKAA SVTPETPEKA VDSQGPTPVC
TPAFLEKRKS EVAKMNDDDK DNEIVFKQPV SGVKEETQET QSPASSKKKR RRKHNQ
