Full text data of TPRKB
TPRKB
[Confidence: low (only semi-automatic identification from reviews)]
EKC/KEOPS complex subunit TPRKB (PRPK-binding protein; TP53RK-binding protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
EKC/KEOPS complex subunit TPRKB (PRPK-binding protein; TP53RK-binding protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9Y3C4
ID TPRKB_HUMAN Reviewed; 175 AA.
AC Q9Y3C4; D6W5H6; Q8IWR6; Q8IWR7; Q9H3K4;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 88.
DE RecName: Full=EKC/KEOPS complex subunit TPRKB;
DE AltName: Full=PRPK-binding protein;
DE AltName: Full=TP53RK-binding protein;
GN Name=TPRKB; ORFNames=CGI-121, My019;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), SUBCELLULAR
RP LOCATION, INTERACTION WITH TP53RK, AND TISSUE SPECIFICITY.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RA Mao Y.M., Xie Y., Mu Z.M., Li Y., Huang Y.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, AND MASS
RP SPECTROMETRY.
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 [7]
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.,
RA Buerckstuemmer T., 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 [8]
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.,
RA Tijchon E., Conaway J.W., Conaway R.C., Stunnenberg H.G.;
RT "The human EKC/KEOPS complex is recruited to Cullin2 ubiquitin ligases
RT by the human tumour antigen PRAME.";
RL PLoS ONE 7:E42822-E42822(2012).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS).
RX PubMed=18951093; DOI=10.1016/j.molcel.2008.10.002;
RA Mao D.Y., Neculai D., Downey M., Orlicky S., Haffani Y.Z.,
RA Ceccarelli D.F., Ho J.S., Szilard R.K., Zhang W., Ho C.S., Wan L.,
RA Fares C., Rumpel S., Kurinov I., Arrowsmith C.H., Durocher D.,
RA Sicheri F.;
RT "Atomic structure of the KEOPS complex: an ancient protein kinase-
RT containing molecular machine.";
RL Mol. Cell 32:259-275(2008).
CC -!- FUNCTION: Component of the EKC/KEOPS complex that is required for
CC the formation of a threonylcarbamoyl group on adenosine at
CC position 37 (t(6)A37) in tRNAs that read codons beginning with
CC adenine. The complex is probably involved in the transfer of the
CC threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the
CC N6 group of A37. TPRKB acts as an allosteric effector that
CC regulates the t(6)A activity of the complex. TPRKB is not required
CC for tRNA modification (By similarity).
CC -!- SUBUNIT: Component of the EKC/KEOPS complex composed of at least
CC TP53RK, TPRKB, OSGEP and LAGE3; the whole complex dimerizes.
CC Interacts with TP53RK/PRPK.
CC -!- INTERACTION:
CC Q96S44:TP53RK; NbExp=3; IntAct=EBI-750123, EBI-739588;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y3C4-1; Sequence=Displayed;
CC Name=2; Synonyms=S1;
CC IsoId=Q9Y3C4-2; Sequence=VSP_023414;
CC Name=3; Synonyms=L1;
CC IsoId=Q9Y3C4-3; Sequence=VSP_023415;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the CGI121/TPRKB family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AY157986; AAN76356.1; -; mRNA.
DR EMBL; AY157987; AAN76357.1; -; mRNA.
DR EMBL; AF060921; AAG43133.1; -; mRNA.
DR EMBL; AF151879; AAD34116.1; -; mRNA.
DR EMBL; CH471053; EAW99720.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99722.1; -; Genomic_DNA.
DR EMBL; BC029492; AAH29492.1; -; mRNA.
DR RefSeq; NP_057142.1; NM_016058.2.
DR RefSeq; XP_005264400.1; XM_005264343.1.
DR RefSeq; XP_005264402.1; XM_005264345.1.
DR RefSeq; XP_005264404.1; XM_005264347.1.
DR UniGene; Hs.157401; -.
DR PDB; 3ENP; X-ray; 2.48 A; A/B=1-175.
DR PDBsum; 3ENP; -.
DR ProteinModelPortal; Q9Y3C4; -.
DR SMR; Q9Y3C4; 1-172.
DR IntAct; Q9Y3C4; 1.
DR MINT; MINT-1451673; -.
DR STRING; 9606.ENSP00000272424; -.
DR PhosphoSite; Q9Y3C4; -.
DR DMDM; 74735252; -.
DR PaxDb; Q9Y3C4; -.
DR PRIDE; Q9Y3C4; -.
DR DNASU; 51002; -.
DR Ensembl; ENST00000272424; ENSP00000272424; ENSG00000144034.
DR Ensembl; ENST00000318190; ENSP00000325398; ENSG00000144034.
DR Ensembl; ENST00000409716; ENSP00000386936; ENSG00000144034.
DR GeneID; 51002; -.
DR KEGG; hsa:51002; -.
DR UCSC; uc002sjn.2; human.
DR CTD; 51002; -.
DR GeneCards; GC02M073955; -.
DR HGNC; HGNC:24259; TPRKB.
DR HPA; HPA035712; -.
DR MIM; 608680; gene.
DR neXtProt; NX_Q9Y3C4; -.
DR PharmGKB; PA143485660; -.
DR eggNOG; NOG325471; -.
DR HOGENOM; HOG000272647; -.
DR HOVERGEN; HBG056797; -.
DR KO; K15901; -.
DR OMA; LQPDPYD; -.
DR OrthoDB; EOG7SV0XG; -.
DR ChiTaRS; TPRKB; human.
DR EvolutionaryTrace; Q9Y3C4; -.
DR GenomeRNAi; 51002; -.
DR NextBio; 53460; -.
DR PRO; PR:Q9Y3C4; -.
DR Bgee; Q9Y3C4; -.
DR CleanEx; HS_TPRKB; -.
DR Genevestigator; Q9Y3C4; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030163; P:protein catabolic process; NAS:UniProtKB.
DR InterPro; IPR013926; CGI121/TPRKB.
DR PANTHER; PTHR15840; PTHR15840; 1.
DR Pfam; PF08617; CGI-121; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
KW Nucleus; Phosphoprotein; Reference proteome; tRNA processing.
FT CHAIN 1 175 EKC/KEOPS complex subunit TPRKB.
FT /FTId=PRO_0000279220.
FT MOD_RES 132 132 Phosphoserine.
FT VAR_SEQ 15 47 Missing (in isoform 2).
FT /FTId=VSP_023414.
FT VAR_SEQ 47 47 V -> VFHSCCPGWSAMARSWLTATSASRVQAIVLPQPPEL
FT LGLQ (in isoform 3).
FT /FTId=VSP_023415.
FT CONFLICT 147 147 K -> R (in Ref. 2; AAG43133).
FT STRAND 3 6
FT STRAND 14 22
FT HELIX 26 35
FT STRAND 40 43
FT HELIX 45 47
FT HELIX 51 65
FT TURN 66 68
FT STRAND 71 74
FT HELIX 75 83
FT STRAND 85 87
FT HELIX 89 96
FT STRAND 103 111
FT HELIX 120 123
FT STRAND 126 131
FT HELIX 133 138
FT HELIX 142 149
FT HELIX 158 171
SQ SEQUENCE 175 AA; 19661 MW; FB13C0923148C157 CRC64;
MQLTHQLDLF PECRVTLLLF KDVKNAGDLR RKAMEGTIDG SLINPTVIVD PFQILVAANK
AVHLYKLGKM KTRTLSTEII FNLSPNNNIS EALKKFGISA NDTSILIVYI EEGEKQINQE
YLISQVEGHQ VSLKNLPEIM NITEVKKIYK LSSQEESIGT LLDAIICRMS TKDVL
//
ID TPRKB_HUMAN Reviewed; 175 AA.
AC Q9Y3C4; D6W5H6; Q8IWR6; Q8IWR7; Q9H3K4;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 88.
DE RecName: Full=EKC/KEOPS complex subunit TPRKB;
DE AltName: Full=PRPK-binding protein;
DE AltName: Full=TP53RK-binding protein;
GN Name=TPRKB; ORFNames=CGI-121, My019;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), SUBCELLULAR
RP LOCATION, INTERACTION WITH TP53RK, AND TISSUE SPECIFICITY.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RA Mao Y.M., Xie Y., Mu Z.M., Li Y., Huang Y.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, AND MASS
RP SPECTROMETRY.
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 [7]
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.,
RA Buerckstuemmer T., 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 [8]
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.,
RA Tijchon E., Conaway J.W., Conaway R.C., Stunnenberg H.G.;
RT "The human EKC/KEOPS complex is recruited to Cullin2 ubiquitin ligases
RT by the human tumour antigen PRAME.";
RL PLoS ONE 7:E42822-E42822(2012).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS).
RX PubMed=18951093; DOI=10.1016/j.molcel.2008.10.002;
RA Mao D.Y., Neculai D., Downey M., Orlicky S., Haffani Y.Z.,
RA Ceccarelli D.F., Ho J.S., Szilard R.K., Zhang W., Ho C.S., Wan L.,
RA Fares C., Rumpel S., Kurinov I., Arrowsmith C.H., Durocher D.,
RA Sicheri F.;
RT "Atomic structure of the KEOPS complex: an ancient protein kinase-
RT containing molecular machine.";
RL Mol. Cell 32:259-275(2008).
CC -!- FUNCTION: Component of the EKC/KEOPS complex that is required for
CC the formation of a threonylcarbamoyl group on adenosine at
CC position 37 (t(6)A37) in tRNAs that read codons beginning with
CC adenine. The complex is probably involved in the transfer of the
CC threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the
CC N6 group of A37. TPRKB acts as an allosteric effector that
CC regulates the t(6)A activity of the complex. TPRKB is not required
CC for tRNA modification (By similarity).
CC -!- SUBUNIT: Component of the EKC/KEOPS complex composed of at least
CC TP53RK, TPRKB, OSGEP and LAGE3; the whole complex dimerizes.
CC Interacts with TP53RK/PRPK.
CC -!- INTERACTION:
CC Q96S44:TP53RK; NbExp=3; IntAct=EBI-750123, EBI-739588;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y3C4-1; Sequence=Displayed;
CC Name=2; Synonyms=S1;
CC IsoId=Q9Y3C4-2; Sequence=VSP_023414;
CC Name=3; Synonyms=L1;
CC IsoId=Q9Y3C4-3; Sequence=VSP_023415;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the CGI121/TPRKB family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AY157986; AAN76356.1; -; mRNA.
DR EMBL; AY157987; AAN76357.1; -; mRNA.
DR EMBL; AF060921; AAG43133.1; -; mRNA.
DR EMBL; AF151879; AAD34116.1; -; mRNA.
DR EMBL; CH471053; EAW99720.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99722.1; -; Genomic_DNA.
DR EMBL; BC029492; AAH29492.1; -; mRNA.
DR RefSeq; NP_057142.1; NM_016058.2.
DR RefSeq; XP_005264400.1; XM_005264343.1.
DR RefSeq; XP_005264402.1; XM_005264345.1.
DR RefSeq; XP_005264404.1; XM_005264347.1.
DR UniGene; Hs.157401; -.
DR PDB; 3ENP; X-ray; 2.48 A; A/B=1-175.
DR PDBsum; 3ENP; -.
DR ProteinModelPortal; Q9Y3C4; -.
DR SMR; Q9Y3C4; 1-172.
DR IntAct; Q9Y3C4; 1.
DR MINT; MINT-1451673; -.
DR STRING; 9606.ENSP00000272424; -.
DR PhosphoSite; Q9Y3C4; -.
DR DMDM; 74735252; -.
DR PaxDb; Q9Y3C4; -.
DR PRIDE; Q9Y3C4; -.
DR DNASU; 51002; -.
DR Ensembl; ENST00000272424; ENSP00000272424; ENSG00000144034.
DR Ensembl; ENST00000318190; ENSP00000325398; ENSG00000144034.
DR Ensembl; ENST00000409716; ENSP00000386936; ENSG00000144034.
DR GeneID; 51002; -.
DR KEGG; hsa:51002; -.
DR UCSC; uc002sjn.2; human.
DR CTD; 51002; -.
DR GeneCards; GC02M073955; -.
DR HGNC; HGNC:24259; TPRKB.
DR HPA; HPA035712; -.
DR MIM; 608680; gene.
DR neXtProt; NX_Q9Y3C4; -.
DR PharmGKB; PA143485660; -.
DR eggNOG; NOG325471; -.
DR HOGENOM; HOG000272647; -.
DR HOVERGEN; HBG056797; -.
DR KO; K15901; -.
DR OMA; LQPDPYD; -.
DR OrthoDB; EOG7SV0XG; -.
DR ChiTaRS; TPRKB; human.
DR EvolutionaryTrace; Q9Y3C4; -.
DR GenomeRNAi; 51002; -.
DR NextBio; 53460; -.
DR PRO; PR:Q9Y3C4; -.
DR Bgee; Q9Y3C4; -.
DR CleanEx; HS_TPRKB; -.
DR Genevestigator; Q9Y3C4; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030163; P:protein catabolic process; NAS:UniProtKB.
DR InterPro; IPR013926; CGI121/TPRKB.
DR PANTHER; PTHR15840; PTHR15840; 1.
DR Pfam; PF08617; CGI-121; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
KW Nucleus; Phosphoprotein; Reference proteome; tRNA processing.
FT CHAIN 1 175 EKC/KEOPS complex subunit TPRKB.
FT /FTId=PRO_0000279220.
FT MOD_RES 132 132 Phosphoserine.
FT VAR_SEQ 15 47 Missing (in isoform 2).
FT /FTId=VSP_023414.
FT VAR_SEQ 47 47 V -> VFHSCCPGWSAMARSWLTATSASRVQAIVLPQPPEL
FT LGLQ (in isoform 3).
FT /FTId=VSP_023415.
FT CONFLICT 147 147 K -> R (in Ref. 2; AAG43133).
FT STRAND 3 6
FT STRAND 14 22
FT HELIX 26 35
FT STRAND 40 43
FT HELIX 45 47
FT HELIX 51 65
FT TURN 66 68
FT STRAND 71 74
FT HELIX 75 83
FT STRAND 85 87
FT HELIX 89 96
FT STRAND 103 111
FT HELIX 120 123
FT STRAND 126 131
FT HELIX 133 138
FT HELIX 142 149
FT HELIX 158 171
SQ SEQUENCE 175 AA; 19661 MW; FB13C0923148C157 CRC64;
MQLTHQLDLF PECRVTLLLF KDVKNAGDLR RKAMEGTIDG SLINPTVIVD PFQILVAANK
AVHLYKLGKM KTRTLSTEII FNLSPNNNIS EALKKFGISA NDTSILIVYI EEGEKQINQE
YLISQVEGHQ VSLKNLPEIM NITEVKKIYK LSSQEESIGT LLDAIICRMS TKDVL
//
MIM
608680
*RECORD*
*FIELD* NO
608680
*FIELD* TI
*608680 PRPK-BINDING PROTEIN
;;CGI-121
*FIELD* TX
CLONING
Using PRPK (608679) as bait in a yeast 2-hybrid screen of a testis cDNA
read morelibrary, followed by 5-prime RACE, Miyoshi et al. (2003) cloned CGI-121.
The deduced 175-amino acid protein has a calculated molecular mass of
19.7 kD. CGI-121 shares 85% amino acid identity with mouse Cgi-121 and
34% amino acid identity with the yeast homolog. Miyoshi et al. (2003)
also identified 2 alternatively spliced variants, which they designated
CGI-121-L1 and CGI-121-S1. CGI-121-L1 encodes a deduced 214-amino acid
protein with a calculated molecular mass of 23.9 kD, and CGI-121-S1
encodes a deduced 142-amino acid protein with a calculated molecular
mass of 16.1 kD. Western blot analysis detected a single CGI-121 protein
with an apparent molecular mass of 20 kD. Immunofluorescent microscopy
detected endogenous CGI-121 distributed in both the nucleus and the
cytosol.
GENE FUNCTION
By coimmunoprecipitation of transiently transfected embryonic kidney
cells, and by in vitro binding assay, Miyoshi et al. (2003) confirmed
the interaction between CGI-121 and PRPK. Neither CGI-121 nor PRPK
formed homodimers in vivo or in vitro. Coprecipitation of p53 (191170)
with PRPK was inhibited by adding recombinant CGI-121 in vitro,
suggesting that CGI-121 may inhibit the PRPK-p53 interaction.
GENE STRUCTURE
Miyoshi et al. (2003) determined that the CGI-121 gene contains at least
6 exons and spans 7.4 kb. Exon 1 is noncoding.
MAPPING
By FISH, Miyoshi et al. (2003) mapped the CGI-121 gene to chromosome
2p13-p12.
*FIELD* RF
1. Miyoshi, A.; Kito, K.; Aramoto, T.; Abe, Y.; Kobayashi, N.; Ueda,
N.: Identification of CGI-121, a novel PRPK (p53-related protein
kinase)-binding protein. Biochem. Biophys. Res. Commun. 303: 399-405,
2003.
*FIELD* CD
Patricia A. Hartz: 5/21/2004
*FIELD* ED
mgross: 05/21/2004
*RECORD*
*FIELD* NO
608680
*FIELD* TI
*608680 PRPK-BINDING PROTEIN
;;CGI-121
*FIELD* TX
CLONING
Using PRPK (608679) as bait in a yeast 2-hybrid screen of a testis cDNA
read morelibrary, followed by 5-prime RACE, Miyoshi et al. (2003) cloned CGI-121.
The deduced 175-amino acid protein has a calculated molecular mass of
19.7 kD. CGI-121 shares 85% amino acid identity with mouse Cgi-121 and
34% amino acid identity with the yeast homolog. Miyoshi et al. (2003)
also identified 2 alternatively spliced variants, which they designated
CGI-121-L1 and CGI-121-S1. CGI-121-L1 encodes a deduced 214-amino acid
protein with a calculated molecular mass of 23.9 kD, and CGI-121-S1
encodes a deduced 142-amino acid protein with a calculated molecular
mass of 16.1 kD. Western blot analysis detected a single CGI-121 protein
with an apparent molecular mass of 20 kD. Immunofluorescent microscopy
detected endogenous CGI-121 distributed in both the nucleus and the
cytosol.
GENE FUNCTION
By coimmunoprecipitation of transiently transfected embryonic kidney
cells, and by in vitro binding assay, Miyoshi et al. (2003) confirmed
the interaction between CGI-121 and PRPK. Neither CGI-121 nor PRPK
formed homodimers in vivo or in vitro. Coprecipitation of p53 (191170)
with PRPK was inhibited by adding recombinant CGI-121 in vitro,
suggesting that CGI-121 may inhibit the PRPK-p53 interaction.
GENE STRUCTURE
Miyoshi et al. (2003) determined that the CGI-121 gene contains at least
6 exons and spans 7.4 kb. Exon 1 is noncoding.
MAPPING
By FISH, Miyoshi et al. (2003) mapped the CGI-121 gene to chromosome
2p13-p12.
*FIELD* RF
1. Miyoshi, A.; Kito, K.; Aramoto, T.; Abe, Y.; Kobayashi, N.; Ueda,
N.: Identification of CGI-121, a novel PRPK (p53-related protein
kinase)-binding protein. Biochem. Biophys. Res. Commun. 303: 399-405,
2003.
*FIELD* CD
Patricia A. Hartz: 5/21/2004
*FIELD* ED
mgross: 05/21/2004