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Protein

TP53-regulating kinase

Gene

Tp53rk

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t6A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. TP53RK has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit OSGEP (By similarity). Atypical protein kinase that phosphorylates 'Ser-15' of p53/TP53 protein and may therefore participate in its activation (By similarity).By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei51 – 511ATPPROSITE-ProRule annotation
Active sitei153 – 1531Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi30 – 389ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • hydrolase activity Source: UniProtKB-KW
  • p53 binding Source: MGI
  • protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  • protein phosphorylation Source: UniProtKB
  • tRNA processing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
TP53-regulating kinase (EC:2.7.11.1)
Alternative name(s):
Atypical serine/threonine protein kinase Tp53rk
EKC/KEOPS complex subunit Tp53rk (EC:3.6.-.-)
Nori-2
p53-related protein kinase
Gene namesi
Name:Tp53rk
Synonyms:Prpk, Trp53rk
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1914050. Trp53rk.

Subcellular locationi

GO - Cellular componenti

  • membrane Source: InterPro
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 244244TP53-regulating kinasePRO_0000088191Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ99PW4.
MaxQBiQ99PW4.
PaxDbiQ99PW4.
PRIDEiQ99PW4.

PTM databases

iPTMnetiQ99PW4.
PhosphoSiteiQ99PW4.

Interactioni

Subunit structurei

Component of the EKC/KEOPS complex composed of at least TP53RK, TPRKB, OSGEP and LAGE3; the whole complex dimerizes. Interacts with TPRKB (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000115353.

Structurei

3D structure databases

ProteinModelPortaliQ99PW4.
SMRiQ99PW4. Positions 33-242.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 244221Protein kinasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi69 – 8618Nuclear localization signalSequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3087. Eukaryota.
COG3642. LUCA.
HOGENOMiHOG000226425.
HOVERGENiHBG028367.
InParanoidiQ99PW4.
KOiK08851.
PhylomeDBiQ99PW4.

Family and domain databases

InterProiIPR022495. Bud32.
IPR011009. Kinase-like_dom.
IPR010440. LipoPS_kinase.
IPR000719. Prot_kinase_dom.
IPR008266. Tyr_kinase_AS.
[Graphical view]
PANTHERiPTHR12209. PTHR12209. 1 hit.
PfamiPF06293. Kdo. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
TIGRFAMsiTIGR03724. arch_bud32. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99PW4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGTSSEAEA EALAAARERS RLFLSGLELV QQGAEARVFR GRFQGRAAVV
60 70 80 90 100
KHRFPKSYRH PELEARLGRR RTVQEARALL RCRRAGIAAP VVFFVDYASN
110 120 130 140 150
CLYMEEIEDS VTVRDYIQST METEKDPQCL LDLARRMGQV LAGMHDQDLI
160 170 180 190 200
HGDLTTSNML LRRPLAQLHI VLIDFGLSFV SGLPEDKGVD LYVLEKAFLS
210 220 230 240
THPHTETAFE AFLKSYGASS KKSSPVLKKL DEVRLRGRKR SMVG
Length:244
Mass (Da):27,394
Last modified:June 1, 2001 - v1
Checksum:iF79AE39073011C5C
GO

Sequence cautioni

The sequence AK013049 differs from that shown. Reason: Frameshift at position 102. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41T → V in AAH17155 (PubMed:15489334).Curated
Sequence conflicti208 – 2081A → V (PubMed:16141072).Curated
Sequence conflicti220 – 2212SK → TQ (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB028045 mRNA. Translation: BAB21614.1.
AK013049 mRNA. No translation available.
BC017155 mRNA. Translation: AAH17155.1.
CCDSiCCDS17090.1.
RefSeqiNP_076304.2. NM_023815.4.
UniGeneiMm.330796.

Genome annotation databases

GeneIDi76367.
KEGGimmu:76367.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB028045 mRNA. Translation: BAB21614.1.
AK013049 mRNA. No translation available.
BC017155 mRNA. Translation: AAH17155.1.
CCDSiCCDS17090.1.
RefSeqiNP_076304.2. NM_023815.4.
UniGeneiMm.330796.

3D structure databases

ProteinModelPortaliQ99PW4.
SMRiQ99PW4. Positions 33-242.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000115353.

PTM databases

iPTMnetiQ99PW4.
PhosphoSiteiQ99PW4.

Proteomic databases

EPDiQ99PW4.
MaxQBiQ99PW4.
PaxDbiQ99PW4.
PRIDEiQ99PW4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi76367.
KEGGimmu:76367.

Organism-specific databases

CTDi76367.
MGIiMGI:1914050. Trp53rk.

Phylogenomic databases

eggNOGiKOG3087. Eukaryota.
COG3642. LUCA.
HOGENOMiHOG000226425.
HOVERGENiHBG028367.
InParanoidiQ99PW4.
KOiK08851.
PhylomeDBiQ99PW4.

Enzyme and pathway databases

BRENDAi2.7.11.1. 3474.

Miscellaneous databases

PROiQ99PW4.
SOURCEiSearch...

Family and domain databases

InterProiIPR022495. Bud32.
IPR011009. Kinase-like_dom.
IPR010440. LipoPS_kinase.
IPR000719. Prot_kinase_dom.
IPR008266. Tyr_kinase_AS.
[Graphical view]
PANTHERiPTHR12209. PTHR12209. 1 hit.
PfamiPF06293. Kdo. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
TIGRFAMsiTIGR03724. arch_bud32. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of a p53-related protein kinase expressed in interleukin-2-activated cytotoxic T-cells, epithelial tumor cell lines, and the testes."
    Abe Y., Matsumoto S., Wei S., Nezu K., Miyoshi A., Kito K., Ueda N., Shigemoto K., Hitsumoto Y., Nikawa J., Enomoto Y.
    J. Biol. Chem. 276:44003-44011(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fetus.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Salivary gland.

Entry informationi

Entry nameiPRPK_MOUSE
AccessioniPrimary (citable) accession number: Q99PW4
Secondary accession number(s): Q91W37, Q9CZ32
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

This protein is considered an atypical serine/threonine kinase, because it lacks the conventional structural elements necessary for the substrate recognition as well as a lysine residue that in all other serine/threonine kinases participates in the catalytic event. TP53RK has protein kinase activity in vitro, but in the context of the EKC/KEOPS complex, the catalytic subunit OSGEP switches the activity of TP53RK from kinase into ATPase (By similarity).By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.