ID   KTI12_RAT               Reviewed;         350 AA.
AC   Q5I0L7;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Protein KTI12 homolog;
GN   Name=Kti12;
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=Spleen;
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   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- SIMILARITY: Belongs to the KTI12 family. {ECO:0000305}.
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DR   EMBL; BC088196; AAH88196.1; -; mRNA.
DR   RefSeq; NP_001037753.1; NM_001044288.1.
DR   AlphaFoldDB; Q5I0L7; -.
DR   SMR; Q5I0L7; -.
DR   iPTMnet; Q5I0L7; -.
DR   PhosphoSitePlus; Q5I0L7; -.
DR   PRIDE; Q5I0L7; -.
DR   GeneID; 685656; -.
DR   KEGG; rno:685656; -.
DR   UCSC; RGD:1591357; rat.
DR   CTD; 112970; -.
DR   RGD; 1591357; Kti12.
DR   InParanoid; Q5I0L7; -.
DR   OrthoDB; 1300128at2759; -.
DR   PhylomeDB; Q5I0L7; -.
DR   PRO; PR:Q5I0L7; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR045106; Kti12.
DR   InterPro; IPR013641; KTI12/PSTK.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR12435; PTHR12435; 1.
DR   Pfam; PF08433; KTI12; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..350
FT                   /note="Protein KTI12 homolog"
FT                   /id="PRO_0000285688"
FT   REGION          161..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         8..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         143
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D1R2"
FT   MOD_RES         156
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   350 AA;  38358 MW;  77049BD3E762628F CRC64;
     MPLVVVCGLP SSGKSRRTEE LRRALTGEGR SVYVVDDASV LGAQDSTVYG DSAGEKALRA
     ALRAAVERRL SRQDVVILDS MNYIKGFRYE LYCLARAVRT PLCLVYCIRP GWPSRGLPVP
     GACESSDPAV SVSWRPRADY GEKTQAVGAV EQRAISPLAN GGVPTAVPKE LDPKDILPSN
     PPAVMTPESE KSAEPAPCAF PPELLESLAL RFEAPDSRNR WDRPLFTVVG LEEPLPLAEI
     RSALFENRAP PPHQSTQSQP LASGSFLHQL DQATSQVLTA VMEAQKSAVP GDLLTLPGTT
     EHLRFTRPLT LAELSRLRRQ FISYTKMHPN NENLPQLANM FLQYLNQSLH