P52K_HUMAN
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 03-AUG-2022, entry version 176.
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; 141.
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; O43422; -.
DR PeptideAtlas; O43422; -.
DR PRIDE; O43422; -.
DR ProteomicsDB; 48933; -. [O43422-1]
DR ProteomicsDB; 48934; -. [O43422-2]
DR Antibodypedia; 2160; 168 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 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 PhylomeDB; O43422; -.
DR TreeFam; TF330114; -.
DR PathwayCommons; O43422; -.
DR SignaLink; O43422; -.
DR SIGNOR; O43422; -.
DR BioGRID-ORCS; 5612; 330 hits in 1101 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 203 other tissues.
DR ExpressionAtlas; O43422; baseline and differential.
DR Genevisible; O43422; HS.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
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 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 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
