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KTI12_MOUSE
ID   KTI12_MOUSE             Reviewed;         351 AA.
AC   Q9D1R2; Q3UG06;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Protein KTI12 homolog;
GN   Name=Kti12;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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   [4]
RP   IDENTIFICATION BY 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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of electron
RT   capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-156, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
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   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-143, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
CC   -!- SIMILARITY: Belongs to the KTI12 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE28403.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK003197; BAB22635.1; -; mRNA.
DR   EMBL; AK148185; BAE28403.1; ALT_INIT; mRNA.
DR   EMBL; AK156755; BAE33838.1; -; mRNA.
DR   EMBL; AL607070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC021493; AAH21493.1; -; mRNA.
DR   CCDS; CCDS18458.1; -.
DR   RefSeq; NP_083847.1; NM_029571.2.
DR   AlphaFoldDB; Q9D1R2; -.
DR   SMR; Q9D1R2; -.
DR   STRING; 10090.ENSMUSP00000099799; -.
DR   iPTMnet; Q9D1R2; -.
DR   PhosphoSitePlus; Q9D1R2; -.
DR   EPD; Q9D1R2; -.
DR   jPOST; Q9D1R2; -.
DR   MaxQB; Q9D1R2; -.
DR   PaxDb; Q9D1R2; -.
DR   PeptideAtlas; Q9D1R2; -.
DR   PRIDE; Q9D1R2; -.
DR   ProteomicsDB; 265032; -.
DR   DNASU; 100087; -.
DR   Ensembl; ENSMUST00000102738; ENSMUSP00000099799; ENSMUSG00000073775.
DR   GeneID; 100087; -.
DR   KEGG; mmu:100087; -.
DR   UCSC; uc008ubt.1; mouse.
DR   CTD; 112970; -.
DR   MGI; MGI:1923547; Kti12.
DR   VEuPathDB; HostDB:ENSMUSG00000073775; -.
DR   eggNOG; KOG3062; Eukaryota.
DR   GeneTree; ENSGT00390000002443; -.
DR   HOGENOM; CLU_027147_0_0_1; -.
DR   InParanoid; Q9D1R2; -.
DR   OMA; LYCEAKA; -.
DR   OrthoDB; 1300128at2759; -.
DR   PhylomeDB; Q9D1R2; -.
DR   TreeFam; TF312974; -.
DR   BioGRID-ORCS; 100087; 21 hits in 75 CRISPR screens.
DR   PRO; PR:Q9D1R2; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q9D1R2; protein.
DR   Bgee; ENSMUSG00000073775; Expressed in interventricular septum and 246 other tissues.
DR   Genevisible; Q9D1R2; MM.
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..351
FT                   /note="Protein KTI12 homolog"
FT                   /id="PRO_0000285687"
FT   REGION          177..197
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:0007744|PubMed:23806337"
FT   MOD_RES         156
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         157
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19131326"
FT   MOD_RES         198
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96EK9"
SQ   SEQUENCE   351 AA;  38445 MW;  DF535CD2FC839FED CRC64;
     MPLVVVCGLP SSGKSQRTEE LRRALASEGR AVYVVDDASV LGAQDPTVYG DSAGEKALRA
     ALRAAVERRL SRQDVVILDS VNYIKGFRYE LYCLARAART PLCLLYCVRP NWPSRELREA
     SASENRDLAV SVSWRPRAET GGKSQAAGAV EEQRATSPVA NGGVLAAVSK ELDPEEILPS
     NPSAVMTPGS EKSAEPASCA FPPEVLESLA LRFESPDSRN RWDRPLFTVV GLEEPLPLAE
     IRSALFENRA PPPHQSTQSQ PLASGSFLHQ LDQATSQVLT AVMEAQKSAV PGDFLKLPGT
     TEPLRFTRPL TLAELSRLRR QFISYTKMHP NNENLPQLAN MFLQYLNQSL H
 
 
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