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Protein

TP53-regulating kinase

Gene

TP53RK

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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 similarity1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei60 – 601ATPPROSITE-ProRule annotation
Active sitei162 – 1621Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi39 – 479ATPPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

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. 2681.
ReactomeiR-HSA-6782315. tRNA modification in the nucleus and cytosol.

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:C20orf64, PRPK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:16197. TP53RK.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: GO_Central
  • EKC/KEOPS complex Source: GO_Central
  • membrane Source: InterPro
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25774.

Chemistry

ChEMBLiCHEMBL1938223.

Polymorphism and mutation databases

BioMutaiTP53RK.
DMDMi26398348.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 253253TP53-regulating kinasePRO_0000088190Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei34 – 341PhosphoserineCombined sources
Modified residuei135 – 1351PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ96S44.
MaxQBiQ96S44.
PaxDbiQ96S44.
PeptideAtlasiQ96S44.
PRIDEiQ96S44.

PTM databases

iPTMnetiQ96S44.
PhosphoSiteiQ96S44.

Expressioni

Tissue specificityi

Highly expressed in testis. Weakly expressed in heart kidney and spleen.

Gene expression databases

BgeeiQ96S44.
CleanExiHS_TP53RK.
ExpressionAtlasiQ96S44. baseline and differential.
GenevisibleiQ96S44. HS.

Organism-specific databases

HPAiCAB004688.
HPA015837.

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CALCOCO2Q131374EBI-739588,EBI-739580
MTUS2Q5JR593EBI-739588,EBI-742948
TPRKBQ9Y3C43EBI-739588,EBI-750123

GO - Molecular functioni

  • p53 binding Source: HGNC

Protein-protein interaction databases

BioGridi125211. 52 interactions.
IntActiQ96S44. 15 interactions.
STRINGi9606.ENSP00000361186.

Structurei

3D structure databases

ProteinModelPortaliQ96S44.
SMRiQ96S44. Positions 42-249.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 253221Protein kinasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi78 – 9518Nuclear localization signalSequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3087. Eukaryota.
COG3642. LUCA.
GeneTreeiENSGT00390000012914.
HOVERGENiHBG028367.
InParanoidiQ96S44.
KOiK08851.
OMAiPPLEQLN.
OrthoDBiEOG70CR7K.
PhylomeDBiQ96S44.
TreeFamiTF325502.

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]
SMARTiSM00220. S_TKc. 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.

Q96S44-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAARATTPA DGEEPAPEAE ALAAARERSS RFLSGLELVK QGAEARVFRG
60 70 80 90 100
RFQGRAAVIK HRFPKGYRHP ALEARLGRRR TVQEARALLR CRRAGISAPV
110 120 130 140 150
VFFVDYASNC LYMEEIEGSV TVRDYIQSTM ETEKTPQGLS NLAKTIGQVL
160 170 180 190 200
ARMHDEDLIH GDLTTSNMLL KPPLEQLNIV LIDFGLSFIS ALPEDKGVDL
210 220 230 240 250
YVLEKAFLST HPNTETVFEA FLKSYSTSSK KARPVLKKLD EVRLRGRKRS

MVG
Length:253
Mass (Da):28,160
Last modified:December 6, 2002 - v2
Checksum:i8B081DED6D2DC034
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti51 – 511R → H in AAH66309 (PubMed:15489334).Curated
Sequence conflicti93 – 931R → L in AAH10637 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti25 – 251A → T.1 Publication
VAR_014427
Natural varianti123 – 1231R → Q.1 Publication
Corresponds to variant rs34983477 [ dbSNP | Ensembl ].
VAR_041881
Natural varianti129 – 1291T → A.1 Publication
Corresponds to variant rs11550540 [ dbSNP | Ensembl ].
VAR_030870
Natural varianti145 – 1451T → A.1 Publication
Corresponds to variant rs56008408 [ dbSNP | Ensembl ].
VAR_041882

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017505 mRNA. Translation: BAB61875.2.
AB065434 mRNA. Translation: BAB62041.1.
AK096502 mRNA. Translation: BAG53306.1.
AL031055, AL133520 Genomic DNA. Translation: CAC00561.1.
AL133520, AL031055 Genomic DNA. Translation: CAJ30016.1.
CH471077 Genomic DNA. Translation: EAW75727.1.
BC009727 mRNA. Translation: AAH09727.1.
BC010637 mRNA. Translation: AAH10637.1.
BC066309 mRNA. Translation: AAH66309.1.
CCDSiCCDS13401.1.
RefSeqiNP_291028.3. NM_033550.3.
UniGeneiHs.440263.

Genome annotation databases

EnsembliENST00000372114; ENSP00000361186; ENSG00000172315.
GeneIDi112858.
KEGGihsa:112858.
UCSCiuc002xsk.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017505 mRNA. Translation: BAB61875.2.
AB065434 mRNA. Translation: BAB62041.1.
AK096502 mRNA. Translation: BAG53306.1.
AL031055, AL133520 Genomic DNA. Translation: CAC00561.1.
AL133520, AL031055 Genomic DNA. Translation: CAJ30016.1.
CH471077 Genomic DNA. Translation: EAW75727.1.
BC009727 mRNA. Translation: AAH09727.1.
BC010637 mRNA. Translation: AAH10637.1.
BC066309 mRNA. Translation: AAH66309.1.
CCDSiCCDS13401.1.
RefSeqiNP_291028.3. NM_033550.3.
UniGeneiHs.440263.

3D structure databases

ProteinModelPortaliQ96S44.
SMRiQ96S44. Positions 42-249.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125211. 52 interactions.
IntActiQ96S44. 15 interactions.
STRINGi9606.ENSP00000361186.

Chemistry

ChEMBLiCHEMBL1938223.

PTM databases

iPTMnetiQ96S44.
PhosphoSiteiQ96S44.

Polymorphism and mutation databases

BioMutaiTP53RK.
DMDMi26398348.

Proteomic databases

EPDiQ96S44.
MaxQBiQ96S44.
PaxDbiQ96S44.
PeptideAtlasiQ96S44.
PRIDEiQ96S44.

Protocols and materials databases

DNASUi112858.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000372114; ENSP00000361186; ENSG00000172315.
GeneIDi112858.
KEGGihsa:112858.
UCSCiuc002xsk.4. human.

Organism-specific databases

CTDi112858.
GeneCardsiTP53RK.
HGNCiHGNC:16197. TP53RK.
HPAiCAB004688.
HPA015837.
MIMi608679. gene.
neXtProtiNX_Q96S44.
PharmGKBiPA25774.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3087. Eukaryota.
COG3642. LUCA.
GeneTreeiENSGT00390000012914.
HOVERGENiHBG028367.
InParanoidiQ96S44.
KOiK08851.
OMAiPPLEQLN.
OrthoDBiEOG70CR7K.
PhylomeDBiQ96S44.
TreeFamiTF325502.

Enzyme and pathway databases

BRENDAi2.7.11.1. 2681.
ReactomeiR-HSA-6782315. tRNA modification in the nucleus and cytosol.

Miscellaneous databases

ChiTaRSiTP53RK. human.
GeneWikiiTP53RK.
GenomeRNAii112858.
NextBioi78689.
PROiQ96S44.
SOURCEiSearch...

Gene expression databases

BgeeiQ96S44.
CleanExiHS_TP53RK.
ExpressionAtlasiQ96S44. baseline and differential.
GenevisibleiQ96S44. HS.

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]
SMARTiSM00220. S_TKc. 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], FUNCTION, CHARACTERIZATION.
    Tissue: Spleen.
  2. "PRPK mutant."
    Abe Y.
    Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-25.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Brain, Colon and Pancreas.
  7. "Identification of CGI-121, a novel PRPK (p53-related protein kinase)-binding protein."
    Miyoshi A., Kito K., Aramoto T., Abe Y., Kobayashi N., Ueda N.
    Biochem. Biophys. Res. Commun. 303:399-405(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TPRKB.
  8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-135, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34 AND THR-135, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "The human EKC/KEOPS complex is recruited to Cullin2 ubiquitin ligases by the human tumour antigen PRAME."
    Costessi A., Mahrour N., Sharma V., Stunnenberg R., Stoel M.A., Tijchon E., Conaway J.W., Conaway R.C., Stunnenberg H.G.
    PLoS ONE 7:E42822-E42822(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE EKC/KEOPS COMPLEX, SUBCELLULAR LOCATION.
  13. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-123; ALA-129 AND ALA-145.

Entry informationi

Entry nameiPRPK_HUMAN
AccessioniPrimary (citable) accession number: Q96S44
Secondary accession number(s): B3KU44
, Q3T977, Q5JZ01, Q6NZ60, Q96FM7, Q9NQE6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: December 6, 2002
Last modified: May 11, 2016
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. 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.