THAP5_HUMAN
ID THAP5_HUMAN Reviewed; 395 AA.
AC Q7Z6K1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=THAP domain-containing protein 5;
GN Name=THAP5;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC 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 [3]
RP POSSIBLE FUNCTION IN CELL CYCLE, INTERACTION WITH HTRA2, CLEAVAGE BY HTRA2,
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=19502560; DOI=10.1152/ajpheart.00234.2009;
RA Balakrishnan M.P., Cilenti L., Mashak Z., Popat P., Alnemri E.S.,
RA Zervos A.S.;
RT "THAP5 is a human cardiac-specific inhibitor of cell cycle that is cleaved
RT by the proapoptotic Omi/HtrA2 protease during cell death.";
RL Am. J. Physiol. 297:H643-H653(2009).
RN [4]
RP FUNCTION, DNA-BINDING, SUBCELLULAR LOCATION, AND INDUCTION BY UV AND
RP CISPLATIN.
RX PubMed=21110952; DOI=10.1016/j.bbrc.2010.11.092;
RA Balakrishnan M.P., Cilenti L., Ambivero C., Goto Y., Takata M., Turkson J.,
RA Li X.S., Zervos A.S.;
RT "THAP5 is a DNA-binding transcriptional repressor that is regulated in
RT melanoma cells during DNA damage-induced cell death.";
RL Biochem. Biophys. Res. Commun. 404:195-200(2011).
RN [5]
RP INTERACTION WITH ABRAXAS2, AND TISSUE SPECIFICITY.
RX PubMed=21195082; DOI=10.1016/j.yjmcc.2010.12.015;
RA Cilenti L., Balakrishnan M.P., Wang X.L., Ambivero C., Sterlicchi M.,
RA del Monte F., Ma X.L., Zervos A.S.;
RT "Regulation of Abro1/KIAA0157 during myocardial infarction and cell death
RT reveals a novel cardioprotective mechanism for Lys63-specific
RT deubiquitination.";
RL J. Mol. Cell. Cardiol. 50:652-661(2011).
CC -!- FUNCTION: Has sequence-specific DNA-binding activity and can function
CC as transcriptional repressor (in vitro) (PubMed:21110952). May be a
CC regulator of cell cycle: THAP5 overexpression in human cell lines
CC causes cell cycle arrest at G2/M phase (PubMed:19502560).
CC {ECO:0000269|PubMed:21110952, ECO:0000305|PubMed:19502560}.
CC -!- SUBUNIT: Interacts with HTRA2; under apoptotic conditions
CC (PubMed:19502560). Interacts with ABRAXAS2 (PubMed:21195082).
CC {ECO:0000269|PubMed:19502560, ECO:0000269|PubMed:21195082}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19502560,
CC ECO:0000269|PubMed:21110952}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7Z6K1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z6K1-2; Sequence=VSP_033558;
CC -!- TISSUE SPECIFICITY: Detected in heart (PubMed:19502560,
CC PubMed:21195082). Detected in brain and muscle (at protein level)
CC (PubMed:19502560). Highly expressed in the heart. Also found in brain
CC and skeletal muscle (PubMed:19502560, PubMed:21195082).
CC {ECO:0000269|PubMed:19502560, ECO:0000269|PubMed:21195082}.
CC -!- INDUCTION: Up-regulated both in response to UV light treatment and
CC cisplatin, agents that cause DNA damage (at protein level).
CC {ECO:0000269|PubMed:21110952}.
CC -!- PTM: Cleaved by HTRA2 during apoptosis. {ECO:0000269|PubMed:19502560}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH53634.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAL24383.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH236947; EAL24383.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC053634; AAH53634.1; ALT_INIT; mRNA.
DR CCDS; CCDS34734.2; -. [Q7Z6K1-2]
DR CCDS; CCDS47687.1; -. [Q7Z6K1-1]
DR RefSeq; NP_001123947.1; NM_001130475.2. [Q7Z6K1-1]
DR RefSeq; NP_001274527.1; NM_001287598.1.
DR RefSeq; NP_001274528.1; NM_001287599.1.
DR RefSeq; NP_001274530.1; NM_001287601.1.
DR RefSeq; NP_872335.2; NM_182529.3. [Q7Z6K1-2]
DR AlphaFoldDB; Q7Z6K1; -.
DR SMR; Q7Z6K1; -.
DR BioGRID; 127964; 8.
DR ELM; Q7Z6K1; -.
DR IntAct; Q7Z6K1; 5.
DR MINT; Q7Z6K1; -.
DR STRING; 9606.ENSP00000400500; -.
DR GlyConnect; 2084; 1 N-Linked glycan (1 site).
DR GlyGen; Q7Z6K1; 1 site, 2 N-linked glycans (1 site).
DR iPTMnet; Q7Z6K1; -.
DR PhosphoSitePlus; Q7Z6K1; -.
DR BioMuta; THAP5; -.
DR DMDM; 189029912; -.
DR EPD; Q7Z6K1; -.
DR MassIVE; Q7Z6K1; -.
DR PaxDb; Q7Z6K1; -.
DR PeptideAtlas; Q7Z6K1; -.
DR PRIDE; Q7Z6K1; -.
DR ProteomicsDB; 69431; -. [Q7Z6K1-1]
DR ProteomicsDB; 69432; -. [Q7Z6K1-2]
DR Antibodypedia; 31461; 54 antibodies from 15 providers.
DR DNASU; 168451; -.
DR Ensembl; ENST00000313516.5; ENSP00000322440.5; ENSG00000177683.14. [Q7Z6K1-2]
DR Ensembl; ENST00000415914.4; ENSP00000400500.2; ENSG00000177683.14. [Q7Z6K1-1]
DR GeneID; 168451; -.
DR KEGG; hsa:168451; -.
DR MANE-Select; ENST00000415914.4; ENSP00000400500.2; NM_001130475.3; NP_001123947.1.
DR UCSC; uc003vfl.5; human. [Q7Z6K1-1]
DR CTD; 168451; -.
DR DisGeNET; 168451; -.
DR GeneCards; THAP5; -.
DR HGNC; HGNC:23188; THAP5.
DR HPA; ENSG00000177683; Low tissue specificity.
DR MIM; 612534; gene.
DR neXtProt; NX_Q7Z6K1; -.
DR OpenTargets; ENSG00000177683; -.
DR PharmGKB; PA134905837; -.
DR VEuPathDB; HostDB:ENSG00000177683; -.
DR eggNOG; ENOG502RYVM; Eukaryota.
DR GeneTree; ENSGT00940000162392; -.
DR HOGENOM; CLU_057257_0_0_1; -.
DR InParanoid; Q7Z6K1; -.
DR OMA; NCFTTFE; -.
DR OrthoDB; 1382095at2759; -.
DR PhylomeDB; Q7Z6K1; -.
DR TreeFam; TF335838; -.
DR PathwayCommons; Q7Z6K1; -.
DR SignaLink; Q7Z6K1; -.
DR BioGRID-ORCS; 168451; 227 hits in 1066 CRISPR screens.
DR ChiTaRS; THAP5; human.
DR GenomeRNAi; 168451; -.
DR Pharos; Q7Z6K1; Tdark.
DR PRO; PR:Q7Z6K1; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q7Z6K1; protein.
DR Bgee; ENSG00000177683; Expressed in calcaneal tendon and 196 other tissues.
DR ExpressionAtlas; Q7Z6K1; baseline and differential.
DR Genevisible; Q7Z6K1; HS.
DR GO; GO:0000785; C:chromatin; IDA:ARUK-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0045786; P:negative regulation of cell cycle; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
DR InterPro; IPR006612; THAP_Znf.
DR Pfam; PF05485; THAP; 1.
DR SMART; SM00692; DM3; 1.
DR SMART; SM00980; THAP; 1.
DR PROSITE; PS50950; ZF_THAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Coiled coil; DNA-binding; Metal-binding;
KW Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..395
FT /note="THAP domain-containing protein 5"
FT /id="PRO_0000333817"
FT ZN_FING 1..84
FT /note="THAP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00309"
FT REGION 85..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 348..382
FT /evidence="ECO:0000255"
FT MOTIF 321..324
FT /note="HCFC1-binding motif (HBM)"
FT /evidence="ECO:0000250"
FT COMPBIAS 91..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..42
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033558"
SQ SEQUENCE 395 AA; 45416 MW; 8AA3BE0E30DDB36A CRC64;
MPRYCAAICC KNRRGRNNKD RKLSFYPFPL HDKERLEKWL KNMKRDSWVP SKYQFLCSDH
FTPDSLDIRW GIRYLKQTAV PTIFSLPEDN QGKDPSKKKS QKKNLEDEKE VCPKAKSEES
FVLNETKKNI VNTDVPHQHP ELLHSSSLVK PPAPKTGSIQ NNMLTLNLVK QHTGKPESTL
ETSVNQDTGR GGFHTCFENL NSTTITLTTS NSESIHQSLE TQEVLEVTTS HLANPNFTSN
SMEIKSAQEN PFLFSTINQT VEELNTNKES VIAIFVPAEN SKPSVNSFIS AQKETTEMED
TDIEDSLYKD VDYGTEVLQI EHSYCRQDIN KEHLWQKVSK LHSKITLLEL KEQQTLGRLK
SLEALIRQLK QENWLSEENV KIIENHFTTY EVTMI
