THA11_HUMAN
ID THA11_HUMAN Reviewed; 314 AA.
AC Q96EK4; A4UCT5; A8K002; O94795;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=THAP domain-containing protein 11;
GN Name=THAP11; ORFNames=HRIHFB2206;
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 MRNA].
RC TISSUE=Neuroblastoma;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 44-197.
RA Santana-Roman H., Curiel-Quesada E., Tapia-Ramirez J.;
RT "Searching for interaction partners of the transcription factor REST/NRSF
RT by two-hybrid screening.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 226-313, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Brain;
RX PubMed=9853615; DOI=10.1038/4315;
RA Ueki N., Oda T., Kondo M., Yano K., Noguchi T., Muramatsu M.-A.;
RT "Selection system for genes encoding nuclear-targeted proteins.";
RL Nat. Biotechnol. 16:1338-1342(1998).
RN [5]
RP TRIPLET REPEAT EXPANSION.
RX PubMed=15368101; DOI=10.1007/s10038-004-0194-8;
RA Pandey N., Mittal U., Srivastava A.K., Mukerji M.;
RT "SMARCA2 and THAP11: potential candidates for polyglutamine disorders as
RT evidenced from polymorphism and protein-folding simulation studies.";
RL J. Hum. Genet. 49:596-602(2004).
RN [6]
RP STRUCTURE BY NMR OF 1-81 IN COMPLEX WITH ZINC ION, AND DNA-BINDING.
RX PubMed=23306615; DOI=10.1007/s10858-012-9699-1;
RA Gervais V., Campagne S., Durand J., Muller I., Milon A.;
RT "NMR studies of a new family of DNA binding proteins: the THAP proteins.";
RL J. Biomol. NMR 56:3-15(2013).
CC -!- FUNCTION: Transcriptional repressor that plays a central role for
CC embryogenesis and the pluripotency of embryonic stem (ES) cells.
CC Sequence-specific DNA-binding factor that represses gene expression in
CC pluripotent ES cells by directly binding to key genetic loci and
CC recruiting epigenetic modifiers (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via coiled coil domain) with HCFC1. {ECO:0000250}.
CC -!- INTERACTION:
CC Q96EK4; Q13363: CTBP1; NbExp=3; IntAct=EBI-1790529, EBI-908846;
CC Q96EK4; P51610: HCFC1; NbExp=2; IntAct=EBI-1790529, EBI-396176;
CC Q96EK4; Q15365: PCBP1; NbExp=4; IntAct=EBI-1790529, EBI-946095;
CC Q96EK4; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-1790529, EBI-2799833;
CC Q96EK4; P70677: Casp3; Xeno; NbExp=2; IntAct=EBI-1790529, EBI-1790419;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9853615}. Cytoplasm
CC {ECO:0000250}. Note=May be regulated by shuttling of the protein
CC between the cytoplasm and nucleus. {ECO:0000250}.
CC -!- POLYMORPHISM: The length of the poly-Gln region is variable in the
CC population. {ECO:0000269|PubMed:15368101}.
CC -!- SIMILARITY: Belongs to the THAP11 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK289367; BAF82056.1; -; mRNA.
DR EMBL; BC012182; AAH12182.1; -; mRNA.
DR EMBL; EF036502; ABO65088.1; -; mRNA.
DR EMBL; AB015338; BAA34796.1; -; mRNA.
DR CCDS; CCDS10847.1; -.
DR RefSeq; NP_065190.2; NM_020457.2.
DR PDB; 2LAU; NMR; -; A=2-80.
DR PDB; 5AJS; X-ray; 2.30 A; A/B/C/D=247-314.
DR PDBsum; 2LAU; -.
DR PDBsum; 5AJS; -.
DR AlphaFoldDB; Q96EK4; -.
DR BMRB; Q96EK4; -.
DR SMR; Q96EK4; -.
DR BioGRID; 121453; 121.
DR CORUM; Q96EK4; -.
DR DIP; DIP-46732N; -.
DR IntAct; Q96EK4; 58.
DR MINT; Q96EK4; -.
DR STRING; 9606.ENSP00000304689; -.
DR CarbonylDB; Q96EK4; -.
DR GlyGen; Q96EK4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96EK4; -.
DR PhosphoSitePlus; Q96EK4; -.
DR BioMuta; THAP11; -.
DR DMDM; 209572685; -.
DR EPD; Q96EK4; -.
DR jPOST; Q96EK4; -.
DR MassIVE; Q96EK4; -.
DR MaxQB; Q96EK4; -.
DR PaxDb; Q96EK4; -.
DR PeptideAtlas; Q96EK4; -.
DR PRIDE; Q96EK4; -.
DR ProteomicsDB; 76416; -.
DR Antibodypedia; 29649; 286 antibodies from 34 providers.
DR DNASU; 57215; -.
DR Ensembl; ENST00000303596.3; ENSP00000304689.1; ENSG00000168286.3.
DR GeneID; 57215; -.
DR KEGG; hsa:57215; -.
DR MANE-Select; ENST00000303596.3; ENSP00000304689.1; NM_020457.3; NP_065190.2.
DR UCSC; uc002euo.4; human.
DR CTD; 57215; -.
DR DisGeNET; 57215; -.
DR GeneCards; THAP11; -.
DR GeneReviews; THAP11; -.
DR HGNC; HGNC:23194; THAP11.
DR HPA; ENSG00000168286; Low tissue specificity.
DR MalaCards; THAP11; -.
DR MIM; 609119; gene.
DR neXtProt; NX_Q96EK4; -.
DR OpenTargets; ENSG00000168286; -.
DR PharmGKB; PA134979842; -.
DR VEuPathDB; HostDB:ENSG00000168286; -.
DR eggNOG; ENOG502QQ1Z; Eukaryota.
DR GeneTree; ENSGT00390000006585; -.
DR HOGENOM; CLU_090879_1_0_1; -.
DR InParanoid; Q96EK4; -.
DR OMA; NSHRDKD; -.
DR OrthoDB; 1177412at2759; -.
DR PhylomeDB; Q96EK4; -.
DR TreeFam; TF331359; -.
DR PathwayCommons; Q96EK4; -.
DR SignaLink; Q96EK4; -.
DR BioGRID-ORCS; 57215; 407 hits in 1114 CRISPR screens.
DR GenomeRNAi; 57215; -.
DR Pharos; Q96EK4; Tbio.
DR PRO; PR:Q96EK4; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q96EK4; protein.
DR Bgee; ENSG00000168286; Expressed in amniotic fluid and 204 other tissues.
DR Genevisible; Q96EK4; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0022900; P:electron transport chain; IEA:Ensembl.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR GO; GO:2000825; P:positive regulation of androgen receptor activity; IEA:Ensembl.
DR GO; GO:1903108; P:regulation of mitochondrial transcription; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 3D-structure; Coiled coil; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Triplet repeat expansion; Zinc; Zinc-finger.
FT CHAIN 1..314
FT /note="THAP domain-containing protein 11"
FT /id="PRO_0000068653"
FT ZN_FING 1..80
FT /note="THAP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00309"
FT REGION 85..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 255..305
FT /evidence="ECO:0000255"
FT MOTIF 243..246
FT /note="HCFC1-binding motif (HBM)"
FT /evidence="ECO:0000250"
FT CONFLICT 132
FT /note="Missing (in Ref. 2; AAH12182)"
FT /evidence="ECO:0000305"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:2LAU"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:2LAU"
FT HELIX 30..40
FT /evidence="ECO:0007829|PDB:2LAU"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:2LAU"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:2LAU"
FT HELIX 254..312
FT /evidence="ECO:0007829|PDB:5AJS"
SQ SEQUENCE 314 AA; 34455 MW; 25235D20CB54D8C2 CRC64;
MPGFTCCVPG CYNNSHRDKA LHFYTFPKDA ELRRLWLKNV SRAGVSGCFS TFQPTTGHRL
CSVHFQGGRK TYTVRVPTIF PLRGVNERKV ARRPAGAAAA RRRQQQQQQQ QQQQQQQQQQ
QQQQQQQQQQ QQSSPSASTA QTAQLQPNLV SASAAVLLTL QATVDSSQAP GSVQPAPITP
TGEDVKPIDL TVQVEFAAAE GAAAAAAASE LQAATAGLEA AECPMGPQLV VVGEEGFPDT
GSDHSYSLSS GTTEEELLRK LNEQRDILAL MEVKMKEMKG SIRHLRLTEA KLREELREKD
RLLAMAVIRK KHGM
