PRPK_HUMAN
ID PRPK_HUMAN Reviewed; 253 AA.
AC Q96S44; B3KU44; Q3T977; Q5JZ01; Q6NZ60; Q96FM7; Q9NQE6;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=EKC/KEOPS complex subunit TP53RK {ECO:0000305};
DE EC=3.6.-.- {ECO:0000250|UniProtKB:Q9UYB9};
DE AltName: Full=Atypical serine/threonine protein kinase TP53RK {ECO:0000303|PubMed:11546806};
DE AltName: Full=Nori-2 {ECO:0000312|HGNC:HGNC:16197};
DE AltName: Full=TP53-regulating kinase {ECO:0000312|HGNC:HGNC:16197};
DE EC=2.7.11.1 {ECO:0000269|PubMed:11546806};
DE AltName: Full=p53-related protein kinase {ECO:0000303|PubMed:11546806};
GN Name=TP53RK {ECO:0000312|HGNC:HGNC:16197};
GN Synonyms=C20orf64, PRPK {ECO:0000303|Ref.2};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Spleen;
RX PubMed=11546806; DOI=10.1074/jbc.m105669200;
RA Abe Y., Matsumoto S., Wei S., Nezu K., Miyoshi A., Kito K., Ueda N.,
RA Shigemoto K., Hitsumoto Y., Nikawa J., Enomoto Y.;
RT "Cloning and characterization of a p53-related protein kinase expressed in
RT interleukin-2-activated cytotoxic T-cells, epithelial tumor cell lines, and
RT the testes.";
RL J. Biol. Chem. 276:44003-44011(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-25.
RA Abe Y.;
RT "PRPK mutant.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Colon, and Pancreas;
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 [7]
RP INTERACTION WITH TPRKB.
RX PubMed=12659830; DOI=10.1016/s0006-291x(03)00333-4;
RA Miyoshi A., Kito K., Aramoto T., Abe Y., Kobayashi N., Ueda N.;
RT "Identification of CGI-121, a novel PRPK (p53-related protein kinase)-
RT binding protein.";
RL Biochem. Biophys. Res. Commun. 303:399-405(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-135, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34 AND THR-135, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP IDENTIFICATION IN THE EKC/KEOPS COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=22912744; DOI=10.1371/journal.pone.0042822;
RA Costessi A., Mahrour N., Sharma V., Stunnenberg R., Stoel M.A., Tijchon E.,
RA Conaway J.W., Conaway R.C., Stunnenberg H.G.;
RT "The human EKC/KEOPS complex is recruited to Cullin2 ubiquitin ligases by
RT the human tumour antigen PRAME.";
RL PLoS ONE 7:E42822-E42822(2012).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP IDENTIFICATION IN THE EKC/KEOPS COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=27903914; DOI=10.1093/nar/gkw1181;
RA Wan L.C., Maisonneuve P., Szilard R.K., Lambert J.P., Ng T.F., Manczyk N.,
RA Huang H., Laister R., Caudy A.A., Gingras A.C., Durocher D., Sicheri F.;
RT "Proteomic analysis of the human KEOPS complex identifies C14ORF142 as a
RT core subunit homologous to yeast Gon7.";
RL Nucleic Acids Res. 45:805-817(2017).
RN [15]
RP VARIANTS [LARGE SCALE ANALYSIS] GLN-123; ALA-129 AND ALA-145.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
RN [16]
RP INVOLVEMENT IN GAMOS4, VARIANTS GAMOS4 ASP-42; ARG-81 AND LEU-243,
RP IDENTIFICATION IN THE EKC/KEOPS COMPLEX, SUBCELLULAR LOCATION, AND
RP CHARACTERIZATION OF VARIANT GAMOS4 ARG-81.
RX PubMed=28805828; DOI=10.1038/ng.3933;
RA Braun D.A., Rao J., Mollet G., Schapiro D., Daugeron M.C., Tan W.,
RA Gribouval O., Boyer O., Revy P., Jobst-Schwan T., Schmidt J.M.,
RA Lawson J.A., Schanze D., Ashraf S., Ullmann J.F.P., Hoogstraten C.A.,
RA Boddaert N., Collinet B., Martin G., Liger D., Lovric S., Furlano M.,
RA Guerrera I.C., Sanchez-Ferras O., Hu J.F., Boschat A.C., Sanquer S.,
RA Menten B., Vergult S., De Rocker N., Airik M., Hermle T., Shril S.,
RA Widmeier E., Gee H.Y., Choi W.I., Sadowski C.E., Pabst W.L., Warejko J.K.,
RA Daga A., Basta T., Matejas V., Scharmann K., Kienast S.D., Behnam B.,
RA Beeson B., Begtrup A., Bruce M., Ch'ng G.S., Lin S.P., Chang J.H.,
RA Chen C.H., Cho M.T., Gaffney P.M., Gipson P.E., Hsu C.H., Kari J.A.,
RA Ke Y.Y., Kiraly-Borri C., Lai W.M., Lemyre E., Littlejohn R.O., Masri A.,
RA Moghtaderi M., Nakamura K., Ozaltin F., Praet M., Prasad C., Prytula A.,
RA Roeder E.R., Rump P., Schnur R.E., Shiihara T., Sinha M.D., Soliman N.A.,
RA Soulami K., Sweetser D.A., Tsai W.H., Tsai J.D., Topaloglu R., Vester U.,
RA Viskochil D.H., Vatanavicharn N., Waxler J.L., Wierenga K.J., Wolf M.T.F.,
RA Wong S.N., Leidel S.A., Truglio G., Dedon P.C., Poduri A., Mane S.,
RA Lifton R.P., Bouchard M., Kannu P., Chitayat D., Magen D., Callewaert B.,
RA van Tilbeurgh H., Zenker M., Antignac C., Hildebrandt F.;
RT "Mutations in KEOPS-complex genes cause nephrotic syndrome with primary
RT microcephaly.";
RL Nat. Genet. 49:1529-1538(2017).
CC -!- FUNCTION: Component of the EKC/KEOPS complex that is required for the
CC formation of a threonylcarbamoyl group on adenosine at position 37
CC (t(6)A37) in tRNAs that read codons beginning with adenine
CC (PubMed:22912744, PubMed:27903914). The complex is probably involved in
CC the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP
CC (TC-AMP) to the N6 group of A37 (PubMed:22912744, PubMed:27903914).
CC TP53RK has ATPase activity in the context of the EKC/KEOPS complex and
CC likely plays a supporting role to the catalytic subunit OSGEP (By
CC similarity). Atypical protein kinase that phosphorylates 'Ser-15' of
CC p53/TP53 protein and may therefore participate in its activation
CC (PubMed:11546806). {ECO:0000250|UniProtKB:P53323,
CC ECO:0000250|UniProtKB:Q9UYB9, ECO:0000269|PubMed:11546806,
CC ECO:0000305|PubMed:22912744, ECO:0000305|PubMed:27903914}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:11546806};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:11546806};
CC -!- SUBUNIT: Component of the EKC/KEOPS complex composed of at least GON7,
CC TP53RK, TPRKB, OSGEP and LAGE3; the whole complex dimerizes.
CC {ECO:0000269|PubMed:12659830, ECO:0000269|PubMed:22912744,
CC ECO:0000269|PubMed:27903914, ECO:0000269|PubMed:28805828}.
CC -!- INTERACTION:
CC Q96S44; Q13137: CALCOCO2; NbExp=5; IntAct=EBI-739588, EBI-739580;
CC Q96S44; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-739588, EBI-739467;
CC Q96S44; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-739588, EBI-742948;
CC Q96S44; Q9NPF4: OSGEP; NbExp=4; IntAct=EBI-739588, EBI-1056510;
CC Q96S44; Q9Y3C4: TPRKB; NbExp=5; IntAct=EBI-739588, EBI-750123;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28805828}. Nucleus
CC {ECO:0000269|PubMed:22912744, ECO:0000269|PubMed:27903914,
CC ECO:0000269|PubMed:28805828}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis. Weakly expressed in
CC heart kidney and spleen. {ECO:0000269|PubMed:11546806}.
CC -!- DOMAIN: This protein is considered an atypical serine/threonine kinase,
CC because it lacks the conventional structural elements necessary for the
CC substrate recognition as well as a lysine residue that in all other
CC serine/threonine kinases participates in the catalytic event. TP53RK
CC has protein kinase activity in vitro, but in the context of the
CC EKC/KEOPS complex, the catalytic subunit OSGEP switches the activity of
CC TP53RK from kinase into ATPase (By similarity).
CC {ECO:0000250|UniProtKB:P53323, ECO:0000250|UniProtKB:Q9UYB9}.
CC -!- DISEASE: Galloway-Mowat syndrome 4 (GAMOS4) [MIM:617730]: A form of
CC Galloway-Mowat syndrome, a severe renal-neurological disease
CC characterized by early-onset nephrotic syndrome associated with
CC microcephaly, central nervous system abnormalities, developmental
CC delays, and a propensity for seizures. Brain anomalies include gyration
CC defects ranging from lissencephaly to pachygyria and polymicrogyria,
CC and cerebellar hypoplasia. Most patients show facial dysmorphism
CC characterized by a small, narrow forehead, large/floppy ears, deep-set
CC eyes, hypertelorism and micrognathia. Additional variable features are
CC visual impairment and arachnodactyly. Most patients die in early
CC childhood. {ECO:0000269|PubMed:28805828}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. BUD32 family.
CC {ECO:0000305}.
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DR EMBL; AB017505; BAB61875.2; -; mRNA.
DR EMBL; AB065434; BAB62041.1; -; mRNA.
DR EMBL; AK096502; BAG53306.1; -; mRNA.
DR EMBL; AL031055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75727.1; -; Genomic_DNA.
DR EMBL; BC009727; AAH09727.1; -; mRNA.
DR EMBL; BC010637; AAH10637.1; -; mRNA.
DR EMBL; BC066309; AAH66309.1; -; mRNA.
DR CCDS; CCDS13401.1; -.
DR RefSeq; NP_291028.3; NM_033550.3.
DR PDB; 6WQX; X-ray; 2.53 A; C/D=1-253.
DR PDBsum; 6WQX; -.
DR AlphaFoldDB; Q96S44; -.
DR SMR; Q96S44; -.
DR BioGRID; 125211; 71.
DR CORUM; Q96S44; -.
DR IntAct; Q96S44; 28.
DR STRING; 9606.ENSP00000361186; -.
DR ChEMBL; CHEMBL1938223; -.
DR GlyGen; Q96S44; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96S44; -.
DR PhosphoSitePlus; Q96S44; -.
DR BioMuta; TP53RK; -.
DR DMDM; 26398348; -.
DR EPD; Q96S44; -.
DR jPOST; Q96S44; -.
DR MassIVE; Q96S44; -.
DR MaxQB; Q96S44; -.
DR PaxDb; Q96S44; -.
DR PeptideAtlas; Q96S44; -.
DR PRIDE; Q96S44; -.
DR ProteomicsDB; 78064; -.
DR Antibodypedia; 2100; 306 antibodies from 25 providers.
DR DNASU; 112858; -.
DR Ensembl; ENST00000372114.4; ENSP00000361186.3; ENSG00000172315.6.
DR GeneID; 112858; -.
DR KEGG; hsa:112858; -.
DR MANE-Select; ENST00000372114.4; ENSP00000361186.3; NM_033550.4; NP_291028.3.
DR UCSC; uc002xsk.4; human.
DR CTD; 112858; -.
DR DisGeNET; 112858; -.
DR GeneCards; TP53RK; -.
DR HGNC; HGNC:16197; TP53RK.
DR HPA; ENSG00000172315; Low tissue specificity.
DR MalaCards; TP53RK; -.
DR MIM; 608679; gene.
DR MIM; 617730; phenotype.
DR neXtProt; NX_Q96S44; -.
DR OpenTargets; ENSG00000172315; -.
DR Orphanet; 2065; Galloway-Mowat syndrome.
DR PharmGKB; PA25774; -.
DR VEuPathDB; HostDB:ENSG00000172315; -.
DR eggNOG; KOG3087; Eukaryota.
DR GeneTree; ENSGT00390000012914; -.
DR HOGENOM; CLU_063953_0_0_1; -.
DR InParanoid; Q96S44; -.
DR OMA; HKLYMEY; -.
DR OrthoDB; 1425238at2759; -.
DR PhylomeDB; Q96S44; -.
DR TreeFam; TF325502; -.
DR BRENDA; 2.7.11.1; 2681.
DR PathwayCommons; Q96S44; -.
DR Reactome; R-HSA-6782315; tRNA modification in the nucleus and cytosol.
DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR SignaLink; Q96S44; -.
DR SIGNOR; Q96S44; -.
DR BioGRID-ORCS; 112858; 642 hits in 1047 CRISPR screens.
DR ChiTaRS; TP53RK; human.
DR GeneWiki; TP53RK; -.
DR GenomeRNAi; 112858; -.
DR Pharos; Q96S44; Tbio.
DR PRO; PR:Q96S44; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q96S44; protein.
DR Bgee; ENSG00000172315; Expressed in ventricular zone and 157 other tissues.
DR ExpressionAtlas; Q96S44; baseline and differential.
DR Genevisible; Q96S44; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0000408; C:EKC/KEOPS complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0002039; F:p53 binding; IDA:HGNC-UCL.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0070525; P:tRNA threonylcarbamoyladenosine metabolic process; IBA:GO_Central.
DR InterPro; IPR022495; Bud32.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR PANTHER; PTHR12209; PTHR12209; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR TIGRFAMs; TIGR03724; arch_bud32; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Disease variant; Epilepsy; Hydrolase;
KW Intellectual disability; Kinase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; tRNA processing.
FT CHAIN 1..253
FT /note="EKC/KEOPS complex subunit TP53RK"
FT /id="PRO_0000088190"
FT DOMAIN 33..253
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 78..95
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 162
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 39..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 135
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195"
FT VARIANT 25
FT /note="A -> T"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_014427"
FT VARIANT 42
FT /note="G -> D (in GAMOS4; dbSNP:rs773814837)"
FT /evidence="ECO:0000269|PubMed:28805828"
FT /id="VAR_080371"
FT VARIANT 81
FT /note="T -> R (in GAMOS4; abolished interaction with TPRKB;
FT dbSNP:rs1432218739)"
FT /evidence="ECO:0000269|PubMed:28805828"
FT /id="VAR_080372"
FT VARIANT 123
FT /note="R -> Q (in dbSNP:rs34983477)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041881"
FT VARIANT 129
FT /note="T -> A (in dbSNP:rs11550540)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_030870"
FT VARIANT 145
FT /note="T -> A (in dbSNP:rs56008408)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041882"
FT VARIANT 243
FT /note="R -> L (in GAMOS4; dbSNP:rs776588426)"
FT /evidence="ECO:0000269|PubMed:28805828"
FT /id="VAR_080373"
FT CONFLICT 51
FT /note="R -> H (in Ref. 6; AAH66309)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="R -> L (in Ref. 6; AAH10637)"
FT /evidence="ECO:0000305"
FT HELIX 19..33
FT /evidence="ECO:0007829|PDB:6WQX"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:6WQX"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:6WQX"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:6WQX"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:6WQX"
FT HELIX 70..93
FT /evidence="ECO:0007829|PDB:6WQX"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:6WQX"
FT TURN 106..109
FT /evidence="ECO:0007829|PDB:6WQX"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:6WQX"
FT HELIX 122..132
FT /evidence="ECO:0007829|PDB:6WQX"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:6WQX"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:6WQX"
FT HELIX 140..155
FT /evidence="ECO:0007829|PDB:6WQX"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:6WQX"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:6WQX"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:6WQX"
FT HELIX 193..210
FT /evidence="ECO:0007829|PDB:6WQX"
FT HELIX 215..228
FT /evidence="ECO:0007829|PDB:6WQX"
FT HELIX 232..245
FT /evidence="ECO:0007829|PDB:6WQX"
SQ SEQUENCE 253 AA; 28160 MW; 8B081DED6D2DC034 CRC64;
MAAARATTPA DGEEPAPEAE ALAAARERSS RFLSGLELVK QGAEARVFRG RFQGRAAVIK
HRFPKGYRHP ALEARLGRRR TVQEARALLR CRRAGISAPV VFFVDYASNC LYMEEIEGSV
TVRDYIQSTM ETEKTPQGLS NLAKTIGQVL ARMHDEDLIH GDLTTSNMLL KPPLEQLNIV
LIDFGLSFIS ALPEDKGVDL YVLEKAFLST HPNTETVFEA FLKSYSTSSK KARPVLKKLD
EVRLRGRKRS MVG
