PRPKB_MOUSE
ID PRPKB_MOUSE Reviewed; 244 AA.
AC Q99PW4; Q91W37; Q9CZ32;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=EKC/KEOPS complex subunit Tp53rkb {ECO:0000305};
DE EC=3.6.-.- {ECO:0000250|UniProtKB:Q9UYB9};
DE AltName: Full=Atypical serine/threonine protein kinase Tp53rk {ECO:0000250|UniProtKB:Q96S44};
DE AltName: Full=EKC/KEOPS complex subunit Tp53rk {ECO:0000305};
DE AltName: Full=Nori-2 {ECO:0000312|MGI:MGI:1914050};
DE AltName: Full=TP53-regulating kinase {ECO:0000250|UniProtKB:Q96S44};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q96S44};
DE AltName: Full=p53-related protein kinase {ECO:0000303|PubMed:11546806};
GN Name=Tp53rkb {ECO:0000305};
GN Synonyms=Prpk {ECO:0000312|MGI:MGI:1914050},
GN Tp53rk {ECO:0000312|MGI:MGI:1914050},
GN Trp53rk {ECO:0000312|MGI:MGI:1914050},
GN Trp53rkb {ECO:0000312|MGI:MGI:1914050};
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 [MRNA].
RC TISSUE=Fetus;
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 [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Salivary gland;
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 -!- 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. The complex
CC is probably involved in the transfer of the threonylcarbamoyl moiety of
CC threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. TP53RK has
CC ATPase activity in the context of the EKC/KEOPS complex and likely
CC plays a supporting role to the catalytic subunit OSGEP (By similarity).
CC Atypical protein kinase that phosphorylates 'Ser-15' of p53/TP53
CC protein and may therefore participate in its activation (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:P53323,
CC ECO:0000250|UniProtKB:Q96S44, ECO:0000250|UniProtKB:Q9UYB9}.
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:0000250|UniProtKB:Q96S44};
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:0000250|UniProtKB:Q96S44};
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:0000250|UniProtKB:Q96S44}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96S44}.
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. BUD32 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK013049; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB028045; BAB21614.1; -; mRNA.
DR EMBL; AK013049; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC017155; AAH17155.1; -; mRNA.
DR CCDS; CCDS17090.1; -.
DR AlphaFoldDB; Q99PW4; -.
DR SMR; Q99PW4; -.
DR BioGRID; 218081; 1.
DR STRING; 10090.ENSMUSP00000115353; -.
DR iPTMnet; Q99PW4; -.
DR PhosphoSitePlus; Q99PW4; -.
DR EPD; Q99PW4; -.
DR MaxQB; Q99PW4; -.
DR PaxDb; Q99PW4; -.
DR PRIDE; Q99PW4; -.
DR MGI; MGI:1914050; Trp53rkb.
DR eggNOG; KOG3087; Eukaryota.
DR InParanoid; Q99PW4; -.
DR PhylomeDB; Q99PW4; -.
DR BRENDA; 2.7.11.1; 3474.
DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
DR ChiTaRS; Prpf4b; mouse.
DR PRO; PR:Q99PW4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q99PW4; protein.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0000408; C:EKC/KEOPS complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS: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; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:HGNC.
DR GO; GO:0006468; P:protein phosphorylation; ISS:HGNC.
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 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 2: Evidence at transcript level;
KW ATP-binding; Hydrolase; Kinase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; tRNA processing.
FT CHAIN 1..244
FT /note="EKC/KEOPS complex subunit Tp53rkb"
FT /id="PRO_0000088191"
FT DOMAIN 24..244
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 69..86
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 153
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 30..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96S44"
FT CONFLICT 4
FT /note="T -> V (in Ref. 3; AAH17155)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="A -> V (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 220..221
FT /note="SK -> TQ (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 244 AA; 27394 MW; F79AE39073011C5C CRC64;
MAGTSSEAEA EALAAARERS RLFLSGLELV QQGAEARVFR GRFQGRAAVV KHRFPKSYRH
PELEARLGRR RTVQEARALL RCRRAGIAAP VVFFVDYASN CLYMEEIEDS VTVRDYIQST
METEKDPQCL LDLARRMGQV LAGMHDQDLI HGDLTTSNML LRRPLAQLHI VLIDFGLSFV
SGLPEDKGVD LYVLEKAFLS THPHTETAFE AFLKSYGASS KKSSPVLKKL DEVRLRGRKR
SMVG
