P52K_MOUSE
ID P52K_MOUSE Reviewed; 758 AA.
AC Q9CUX1; Q80Y58;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=52 kDa repressor of the inhibitor of the protein kinase;
DE Short=p52rIPK;
DE AltName: Full=58 kDa interferon-induced protein kinase-interacting protein;
DE Short=p58IPK-interacting protein;
DE AltName: Full=THAP domain-containing protein 0;
DE AltName: Full=THAP domain-containing protein 12 {ECO:0000250|UniProtKB:O43422};
GN Name=Thap12 {ECO:0000250|UniProtKB:O43422};
GN Synonyms=Prkrir {ECO:0000312|MGI:MGI:1920231}, Thap0;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-652.
RC STRAIN=C57BL/6J; TISSUE=Hippocampus;
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).
CC -!- FUNCTION: Upstream regulator of interferon-induced serine/threonine
CC protein kinase R (PKR). May block the PKR-inhibitory function of
CC DNAJC3, resulting in restoration of kinase activity and suppression of
CC cell growth. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with DNAJC3, probably sequestring it. {ECO:0000250}.
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DR EMBL; BC049103; AAH49103.1; -; mRNA.
DR EMBL; AK013663; BAB28945.1; -; mRNA.
DR CCDS; CCDS21474.1; -.
DR RefSeq; NP_082686.1; NM_028410.1.
DR RefSeq; XP_011240217.1; XM_011241915.2.
DR AlphaFoldDB; Q9CUX1; -.
DR SMR; Q9CUX1; -.
DR BioGRID; 215689; 3.
DR STRING; 10090.ENSMUSP00000033009; -.
DR iPTMnet; Q9CUX1; -.
DR PhosphoSitePlus; Q9CUX1; -.
DR EPD; Q9CUX1; -.
DR MaxQB; Q9CUX1; -.
DR PaxDb; Q9CUX1; -.
DR PeptideAtlas; Q9CUX1; -.
DR PRIDE; Q9CUX1; -.
DR ProteomicsDB; 287754; -.
DR Antibodypedia; 2160; 168 antibodies from 22 providers.
DR DNASU; 72981; -.
DR Ensembl; ENSMUST00000033009; ENSMUSP00000033009; ENSMUSG00000030753.
DR GeneID; 72981; -.
DR KEGG; mmu:72981; -.
DR UCSC; uc009ikt.1; mouse.
DR CTD; 5612; -.
DR MGI; MGI:1920231; Thap12.
DR VEuPathDB; HostDB:ENSMUSG00000030753; -.
DR eggNOG; ENOG502QU3U; Eukaryota.
DR GeneTree; ENSGT00530000063516; -.
DR HOGENOM; CLU_023409_0_0_1; -.
DR InParanoid; Q9CUX1; -.
DR OMA; SCALNIW; -.
DR OrthoDB; 537563at2759; -.
DR PhylomeDB; Q9CUX1; -.
DR TreeFam; TF330114; -.
DR BioGRID-ORCS; 72981; 29 hits in 76 CRISPR screens.
DR ChiTaRS; Prkrir; mouse.
DR PRO; PR:Q9CUX1; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9CUX1; protein.
DR Bgee; ENSMUSG00000030753; Expressed in triceps brachii and 263 other tissues.
DR ExpressionAtlas; Q9CUX1; baseline and differential.
DR Genevisible; Q9CUX1; MM.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR InterPro; IPR025398; DUF4371.
DR InterPro; IPR008906; HATC_C_dom.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR006612; THAP_Znf.
DR Pfam; PF05699; Dimer_Tnp_hAT; 1.
DR Pfam; PF14291; DUF4371; 1.
DR Pfam; PF05485; THAP; 1.
DR SMART; SM00692; DM3; 1.
DR SMART; SM00980; THAP; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS50950; ZF_THAP; 1.
PE 2: Evidence at transcript level;
KW DNA-binding; Metal-binding; Phosphoprotein; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..758
FT /note="52 kDa repressor of the inhibitor of the protein
FT kinase"
FT /id="PRO_0000068635"
FT ZN_FING 1..86
FT /note="THAP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00309"
FT REGION 116..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43422"
SQ SEQUENCE 758 AA; 87021 MW; 0BEDA3FAF680CE1F CRC64;
MPNFCAAPNC TRKSTQSDLA FFRFPRDPAR CQKWVENCRR ADLEDKTPDQ LNKHYRLCAK
HFETSMICRT SPYRTVLRDN AIPTIFDLTS HLNNPHSRHR KRIKELSEDE IRTLKQKKIE
ETSEQEQETN TNAQNPSAEA VNQQDANVLP LTLEEKENKE YLKSLFEILV LMGKQNIPLD
GHEADEVPEG LFAPDNFQAL LECRINSGEE VLRKRFEATA VNTLFCSKTQ QRHMLEICES
CIREETLREV RDSHFFSIIT DDVVDIAGEE HLPVLVRFVD DAHNLREEFV GFLPYEADAE
ILAVKFHTTI TEKWGLNMEY CRGQAYIVSS GFSSKMKVVA SRLLEKYPQA VYTLCSSCAL
NAWLAKSVPV IGVSVALGTI EEVCSFFHRS PQLLLELDSV ISVLFQNSEE RAKELKEICH
SQWTGRHDAF EILVDLLQAL VLCLDGIINS DTNVRWNNYI AGRAFVLCSA VTDFDFIVTI
VVLKNVLSFT RAFGKNLQGQ TSDVFFAASS LTAVLHSLNE VMENIEVYHE FWFEEATNLA
TKLDIQMKLP GKFRRAQQGN LESQLTSESY YKDTLSVPTV EHIIQELKDI FSEQHLKALK
CLSLVPSVMG QLKFNTSEEH HADMYRSDLP NPDTLSAELH CWRIKWKHRG KDIELPSTIY
EALHLPDIKF FPNVYALLKV LCILPVMKVE NERYENGRKR LKAYLRNTLT DQRSSNLALL
NINFDIKHDL DLMVDTYIKL YTNKSELPTI NSETIENT
