TSSK1_HUMAN
ID TSSK1_HUMAN Reviewed; 367 AA.
AC Q9BXA7; B2R8D9;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Testis-specific serine/threonine-protein kinase 1;
DE Short=TSK-1;
DE Short=TSK1;
DE Short=TSSK-1;
DE Short=Testis-specific kinase 1;
DE EC=2.7.11.1 {ECO:0000269|PubMed:19530700};
DE AltName: Full=Serine/threonine-protein kinase 22A;
GN Name=TSSK1B; Synonyms=SPOGA1, SPOGA4, STK22A, STK22D, TSSK1;
GN ORFNames=FKSG81;
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], TISSUE SPECIFICITY, AND INTERACTION WITH TSSK2.
RX PubMed=15044604; DOI=10.1093/molehr/gah052;
RA Hao Z., Jha K.N., Kim Y.H., Vemuganti S., Westbrook V.A., Chertihin O.,
RA Markgraf K., Flickinger C.J., Coppola M., Herr J.C., Visconti P.E.;
RT "Expression analysis of the human testis-specific serine/threonine kinase
RT (TSSK) homologues. A TSSK member is present in the equatorial segment of
RT human sperm.";
RL Mol. Hum. Reprod. 10:433-444(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION,
RP AUTOPHOSPHORYLATION, PHOSPHORYLATION AT THR-174, AND MUTAGENESIS OF
RP THR-174.
RX PubMed=15733851; DOI=10.1016/j.febslet.2005.01.042;
RA Jaleel M., McBride A., Lizcano J.M., Deak M., Toth R., Morrice N.A.,
RA Alessi D.R.;
RT "Identification of the sucrose non-fermenting related kinase SNRK, as a
RT novel LKB1 substrate.";
RL FEBS Lett. 579:1417-1423(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wang Y.-G., Gong L.;
RT "Molecular cloning and characterization of FKSG81, a novel gene located on
RT human chromosome 5.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hippocampus;
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 PUTATIVE CONTRACEPTIVE TARGET.
RX PubMed=17566264;
RA Xu B., Hao Z., Jha K.N., Digilio L., Urekar C., Kim Y.H., Pulido S.,
RA Flickinger C.J., Herr J.C.;
RT "Validation of a testis specific serine/threonine kinase [TSSK] family and
RT the substrate of TSSK1 & 2, TSKS, as contraceptive targets.";
RL Soc. Reprod. Fertil. Suppl. 63:87-101(2007).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=19530700; DOI=10.1021/jm9002846;
RA Zhang L., Yan Y., Liu Z., Abliz Z., Liu G.;
RT "Identification of peptide substrate and small molecule inhibitors of
RT testis-specific serine/threonine kinase1 (TSSK1) by the developed assays.";
RL J. Med. Chem. 52:4419-4428(2009).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=20729278; DOI=10.1093/molehr/gaq071;
RA Li Y., Sosnik J., Brassard L., Reese M., Spiridonov N.A., Bates T.C.,
RA Johnson G.R., Anguita J., Visconti P.E., Salicioni A.M.;
RT "Expression and localization of five members of the testis-specific serine
RT kinase (Tssk) family in mouse and human sperm and testis.";
RL Mol. Hum. Reprod. 17:42-56(2011).
RN [10]
RP VARIANTS [LARGE SCALE ANALYSIS] THR-50; TYR-83; LEU-233; CYS-237; TRP-288
RP AND GLU-293.
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).
CC -!- FUNCTION: Testis-specific serine/threonine-protein kinase required
CC during spermatid development. Phosphorylates 'Ser-288' of TSKS.
CC Involved in the late stages of spermatogenesis, during the
CC reconstruction of the cytoplasm. During spermatogenesis, required for
CC the transformation of a ring-shaped structure around the base of the
CC flagellum originating from the chromatoid body.
CC {ECO:0000269|PubMed:15733851, ECO:0000269|PubMed:19530700}.
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:19530700};
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:19530700};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q61241};
CC -!- ACTIVITY REGULATION: Kinase activity is specifically inhibited by 2
CC classes of compounds: biphenyl compounds (1,1'-(biphenyl-4,4'-
CC diyl)bis(2,2-dihydroxyethanone)) and 1,2,7-trialky-1H-imidazo[4,5-
CC g]quinoxalin-6-one. Activated by phosphorylation on Thr-174 and
CC potentially by autophosphorylation. {ECO:0000269|PubMed:15733851,
CC ECO:0000269|PubMed:19530700}.
CC -!- SUBUNIT: Interacts with TSSK2. Interacts with HSP90; this interaction
CC stabilizes TSSK1 (By similarity). {ECO:0000250|UniProtKB:Q61241,
CC ECO:0000269|PubMed:15044604}.
CC -!- INTERACTION:
CC Q9BXA7; O43281: EFS; NbExp=3; IntAct=EBI-6423734, EBI-718488;
CC Q9BXA7; O43281-2: EFS; NbExp=3; IntAct=EBI-6423734, EBI-11525448;
CC Q9BXA7; Q4G0N7: FAM229B; NbExp=4; IntAct=EBI-6423734, EBI-18340430;
CC Q9BXA7; O15353: FOXN1; NbExp=4; IntAct=EBI-6423734, EBI-11319000;
CC Q9BXA7; P08238: HSP90AB1; NbExp=2; IntAct=EBI-6423734, EBI-352572;
CC Q9BXA7; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-6423734, EBI-16439278;
CC Q9BXA7; Q9UJT2: TSKS; NbExp=3; IntAct=EBI-6423734, EBI-852101;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle,
CC secretory vesicle, acrosome {ECO:0000250}. Cell projection, cilium,
CC flagellum {ECO:0000250}. Note=In spermatozoa, present in the sperm head
CC and in the flagellum. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Testis-specific. Present in sperm (at protein
CC level). {ECO:0000269|PubMed:15044604, ECO:0000269|PubMed:20729278}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:15733851}.
CC -!- PTM: Ubiquitinated; HSP90 activity negatively regulates ubiquitination
CC and degradation. {ECO:0000250|UniProtKB:Q61241}.
CC -!- MISCELLANEOUS: TSSK1B might be used as a target for male contraception
CC or and intra-vaginal spermicides. {ECO:0000305|PubMed:17566264}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AY028964; AAK27734.1; -; mRNA.
DR EMBL; AF348076; AAK29413.1; -; mRNA.
DR EMBL; AK313332; BAG36136.1; -; mRNA.
DR EMBL; AC010431; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022515; AAH22515.1; -; mRNA.
DR CCDS; CCDS4112.1; -.
DR RefSeq; NP_114417.1; NM_032028.3.
DR AlphaFoldDB; Q9BXA7; -.
DR SMR; Q9BXA7; -.
DR BioGRID; 123825; 47.
DR IntAct; Q9BXA7; 36.
DR STRING; 9606.ENSP00000375081; -.
DR BindingDB; Q9BXA7; -.
DR ChEMBL; CHEMBL6003; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; Q9BXA7; -.
DR GuidetoPHARMACOLOGY; 2257; -.
DR GlyGen; Q9BXA7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BXA7; -.
DR PhosphoSitePlus; Q9BXA7; -.
DR BioMuta; TSSK1B; -.
DR DMDM; 30316282; -.
DR MassIVE; Q9BXA7; -.
DR PaxDb; Q9BXA7; -.
DR PeptideAtlas; Q9BXA7; -.
DR PRIDE; Q9BXA7; -.
DR ProteomicsDB; 79392; -.
DR Antibodypedia; 25396; 47 antibodies from 18 providers.
DR DNASU; 83942; -.
DR Ensembl; ENST00000390666.4; ENSP00000375081.3; ENSG00000212122.4.
DR GeneID; 83942; -.
DR KEGG; hsa:83942; -.
DR MANE-Select; ENST00000390666.4; ENSP00000375081.3; NM_032028.4; NP_114417.1.
DR UCSC; uc003kqm.2; human.
DR CTD; 83942; -.
DR DisGeNET; 83942; -.
DR GeneCards; TSSK1B; -.
DR HGNC; HGNC:14968; TSSK1B.
DR HPA; ENSG00000212122; Tissue enriched (testis).
DR MIM; 610709; gene.
DR neXtProt; NX_Q9BXA7; -.
DR OpenTargets; ENSG00000212122; -.
DR PharmGKB; PA37944; -.
DR VEuPathDB; HostDB:ENSG00000212122; -.
DR eggNOG; KOG0583; Eukaryota.
DR GeneTree; ENSGT00940000163130; -.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q9BXA7; -.
DR OMA; NKFFPRE; -.
DR OrthoDB; 947464at2759; -.
DR PhylomeDB; Q9BXA7; -.
DR TreeFam; TF352374; -.
DR PathwayCommons; Q9BXA7; -.
DR SignaLink; Q9BXA7; -.
DR SIGNOR; Q9BXA7; -.
DR BioGRID-ORCS; 83942; 7 hits in 1093 CRISPR screens.
DR GenomeRNAi; 83942; -.
DR Pharos; Q9BXA7; Tchem.
DR PRO; PR:Q9BXA7; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9BXA7; protein.
DR Bgee; ENSG00000212122; Expressed in right testis and 27 other tissues.
DR ExpressionAtlas; Q9BXA7; baseline and differential.
DR Genevisible; Q9BXA7; HS.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0031514; C:motile cilium; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
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:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0007286; P:spermatid development; ISS:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell projection; Cilium; Cytoplasm; Cytoplasmic vesicle;
KW Developmental protein; Differentiation; Flagellum; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Spermatogenesis; Transferase;
KW Ubl conjugation.
FT CHAIN 1..367
FT /note="Testis-specific serine/threonine-protein kinase 1"
FT /id="PRO_0000086766"
FT DOMAIN 12..272
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 276..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 136
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 18..26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 174
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:15733851"
FT VARIANT 50
FT /note="A -> T (in dbSNP:rs747955728)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041235"
FT VARIANT 83
FT /note="H -> Y (in dbSNP:rs55930004)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041236"
FT VARIANT 233
FT /note="V -> L (in dbSNP:rs55940513)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041237"
FT VARIANT 237
FT /note="R -> C (in dbSNP:rs55738530)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041238"
FT VARIANT 288
FT /note="G -> W (in dbSNP:rs34696815)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041239"
FT VARIANT 293
FT /note="G -> E (in dbSNP:rs11953478)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041240"
FT MUTAGEN 174
FT /note="T->A: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:15733851"
FT MUTAGEN 174
FT /note="T->E: Constitutively active."
FT /evidence="ECO:0000269|PubMed:15733851"
FT CONFLICT 345
FT /note="P -> L (in Ref. 4; BAG36136)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 367 AA; 41618 MW; 1B740988894A1589 CRC64;
MDDAAVLKRR GYLLGINLGE GSYAKVKSAY SERLKFNVAI KIIDRKKAPA DFLEKFLPRE
IEILAMLNHC SIIKTYEIFE TSHGKVYIVM ELAVQGDLLE LIKTRGALHE DEARKKFHQL
SLAIKYCHDL DVVHRDLKCD NLLLDKDFNI KLSDFSFSKR CLRDDSGRMA LSKTFCGSPA
YAAPEVLQGI PYQPKVYDIW SLGVILYIMV CGSMPYDDSN IKKMLRIQKE HRVNFPRSKH
LTGECKDLIY HMLQPDVNRR LHIDEILSHC WMQPKARGSP SVAINKEGES SRGTEPLWTP
EPGSDKKSAT KLEPEGEAQP QAQPETKPEG TAMQMSRQSE ILGFPSKPST METEEGPPQQ
PPETRAQ
