ID   P52K_HUMAN              Reviewed;         761 AA.
AC   O43422; A8K728; Q17RY9; Q8WTW1; Q9Y3Z4;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   27-MAR-2024, entry version 184.
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=Death-associated protein 4;
DE   AltName: Full=THAP domain-containing protein 0;
DE   AltName: Full=THAP domain-containing protein 12 {ECO:0000312|HGNC:HGNC:9440};
GN   Name=THAP12 {ECO:0000312|HGNC:HGNC:9440};
GN   Synonyms=DAP4, P52RIPK, PRKRIR, THAP0;
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] (ISOFORM SHORT).
RX   PubMed=9447982; DOI=10.1128/mcb.18.2.859;
RA   Gale M.J. Jr., Blakely C.M., Hopkins D.A., Melville M.W., Wambach M.,
RA   Romano P.R., Katze M.G.;
RT   "Regulation of interferon-induced protein kinase PKR: modulation of P58IPK
RT   inhibitory function by a novel protein, P52rIPK.";
RL   Mol. Cell. Biol. 18:859-871(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RA   Barzilay G., Kimchi A.;
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC   TISSUE=Brain, and Prostate;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-761 (ISOFORM LONG).
RC   TISSUE=Brain;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
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., Buerckstuemmer T.,
RA   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 BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-566, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
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.
CC   -!- SUBUNIT: Interacts with DNAJC3, probably sequestring it.
CC   -!- INTERACTION:
CC       O43422; Q8N8K9: KIAA1958; NbExp=3; IntAct=EBI-2828217, EBI-10181113;
CC       O43422; Q13228: SELENBP1; NbExp=3; IntAct=EBI-2828217, EBI-711619;
CC       O43422; O75410: TACC1; NbExp=3; IntAct=EBI-2828217, EBI-624237;
CC       O43422; O75410-7: TACC1; NbExp=3; IntAct=EBI-2828217, EBI-12007872;
CC       O43422; Q8TF50: ZNF526; NbExp=3; IntAct=EBI-2828217, EBI-11035148;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=O43422-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=O43422-2; Sequence=VSP_004355, VSP_004356;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH21992.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAB43226.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF007393; AAC39564.1; -; mRNA.
DR   EMBL; AF081567; AAG01570.1; -; mRNA.
DR   EMBL; AK291843; BAF84532.1; -; mRNA.
DR   EMBL; CH471076; EAW74993.1; -; Genomic_DNA.
DR   EMBL; BC021992; AAH21992.1; ALT_INIT; mRNA.
DR   EMBL; BC117138; AAI17139.1; -; mRNA.
DR   EMBL; BC117140; AAI17141.1; -; mRNA.
DR   EMBL; AL049970; CAB43226.1; ALT_FRAME; mRNA.
DR   CCDS; CCDS8243.1; -. [O43422-1]
DR   RefSeq; NP_004696.2; NM_004705.3. [O43422-1]
DR   AlphaFoldDB; O43422; -.
DR   SMR; O43422; -.
DR   BioGRID; 111598; 146.
DR   IntAct; O43422; 24.
DR   STRING; 9606.ENSP00000260045; -.
DR   iPTMnet; O43422; -.
DR   PhosphoSitePlus; O43422; -.
DR   BioMuta; THAP12; -.
DR   EPD; O43422; -.
DR   jPOST; O43422; -.
DR   MassIVE; O43422; -.
DR   MaxQB; O43422; -.
DR   PaxDb; 9606-ENSP00000260045; -.
DR   PeptideAtlas; O43422; -.
DR   ProteomicsDB; 48933; -. [O43422-1]
DR   ProteomicsDB; 48934; -. [O43422-2]
DR   Pumba; O43422; -.
DR   Antibodypedia; 2160; 192 antibodies from 22 providers.
DR   DNASU; 5612; -.
DR   Ensembl; ENST00000260045.8; ENSP00000260045.3; ENSG00000137492.9. [O43422-1]
DR   GeneID; 5612; -.
DR   KEGG; hsa:5612; -.
DR   MANE-Select; ENST00000260045.8; ENSP00000260045.3; NM_004705.4; NP_004696.2.
DR   UCSC; uc001oxh.2; human. [O43422-1]
DR   AGR; HGNC:9440; -.
DR   CTD; 5612; -.
DR   DisGeNET; 5612; -.
DR   GeneCards; THAP12; -.
DR   HGNC; HGNC:9440; THAP12.
DR   HPA; ENSG00000137492; Low tissue specificity.
DR   MIM; 607374; gene.
DR   neXtProt; NX_O43422; -.
DR   OpenTargets; ENSG00000137492; -.
DR   PharmGKB; PA33781; -.
DR   VEuPathDB; HostDB:ENSG00000137492; -.
DR   eggNOG; ENOG502QU3U; Eukaryota.
DR   GeneTree; ENSGT00530000063516; -.
DR   HOGENOM; CLU_023409_0_0_1; -.
DR   InParanoid; O43422; -.
DR   OMA; SCALNIW; -.
DR   OrthoDB; 3405036at2759; -.
DR   PhylomeDB; O43422; -.
DR   TreeFam; TF330114; -.
DR   PathwayCommons; O43422; -.
DR   SignaLink; O43422; -.
DR   SIGNOR; O43422; -.
DR   BioGRID-ORCS; 5612; 351 hits in 1173 CRISPR screens.
DR   ChiTaRS; THAP12; human.
DR   GeneWiki; PRKRIR; -.
DR   GenomeRNAi; 5612; -.
DR   Pharos; O43422; Tbio.
DR   PRO; PR:O43422; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; O43422; Protein.
DR   Bgee; ENSG00000137492; Expressed in calcaneal tendon and 205 other cell types or tissues.
DR   ExpressionAtlas; O43422; baseline and differential.
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   GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   InterPro; IPR025398; DUF4371.
DR   InterPro; IPR008906; HATC_C_dom.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR006612; THAP_Znf.
DR   PANTHER; PTHR46289:SF16; 52 KDA REPRESSOR OF THE INHIBITOR OF THE PROTEIN KINASE; 1.
DR   PANTHER; PTHR46289; 52 KDA REPRESSOR OF THE INHIBITOR OF THE PROTEIN KINASE-LIKE PROTEIN-RELATED; 1.
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; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS50950; ZF_THAP; 1.
DR   Genevisible; O43422; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; DNA-binding; Metal-binding; Phosphoprotein;
KW   Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..761
FT                   /note="52 kDa repressor of the inhibitor of the protein
FT                   kinase"
FT                   /id="PRO_0000068634"
FT   ZN_FING         1..86
FT                   /note="THAP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00309"
FT   REGION          116..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..131
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         566
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         489..492
FT                   /note="VLSF -> EIKI (in isoform Short)"
FT                   /evidence="ECO:0000303|PubMed:9447982"
FT                   /id="VSP_004355"
FT   VAR_SEQ         493..761
FT                   /note="Missing (in isoform Short)"
FT                   /evidence="ECO:0000303|PubMed:9447982"
FT                   /id="VSP_004356"
FT   CONFLICT        157
FT                   /note="L -> W (in Ref. 6)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        738
FT                   /note="D -> V (in Ref. 6)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        754
FT                   /note="N -> K (in Ref. 6)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   761 AA;  87704 MW;  88809CFE52399C13 CRC64;
     MPNFCAAPNC TRKSTQSDLA FFRFPRDPAR CQKWVENCRR ADLEDKTPDQ LNKHYRLCAK
     HFETSMICRT SPYRTVLRDN AIPTIFDLTS HLNNPHSRHR KRIKELSEDE IRTLKQKKID
     ETSEQEQKHK ETNNSNAQNP SEEEGEGQDE DILPLTLEEK ENKEYLKSLF EILILMGKQN
     IPLDGHEADE IPEGLFTPDN FQALLECRIN SGEEVLRKRF ETTAVNTLFC SKTQQRQMLE
     ICESCIREET LREVRDSHFF SIITDDVVDI AGEEHLPVLV RFVDESHNLR EEFIGFLPYE
     ADAEILAVKF HTMITEKWGL NMEYCRGQAY IVSSGFSSKM KVVASRLLEK YPQAIYTLCS
     SCALNMWLAK SVPVMGVSVA LGTIEEVCSF FHRSPQLLLE LDNVISVLFQ NSKERGKELK
     EICHSQWTGR HDAFEILVEL LQALVLCLDG INSDTNIRWN NYIAGRAFVL CSAVSDFDFI
     VTIVVLKNVL SFTRAFGKNL QGQTSDVFFA AGSLTAVLHS LNEVMENIEV YHEFWFEEAT
     NLATKLDIQM KLPGKFRRAH QGNLESQLTS ESYYKETLSV PTVEHIIQEL KDIFSEQHLK
     ALKCLSLVPS VMGQLKFNTS EEHHADMYRS DLPNPDTLSA ELHCWRIKWK HRGKDIELPS
     TIYEALHLPD IKFFPNVYAL LKVLCILPVM KVENERYENG RKRLKAYLRN TLTDQRSSNL
     ALLNINFDIK HDLDLMVDTY IKLYTSKSEL PTDNSETVEN T
//