THRSP_HUMAN
ID THRSP_HUMAN Reviewed; 146 AA.
AC Q92748; B2R4W7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Thyroid hormone-inducible hepatic protein;
DE AltName: Full=Spot 14 protein;
DE Short=S14;
DE Short=SPOT14;
GN Name=THRSP;
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 [GENOMIC DNA].
RX PubMed=9003802; DOI=10.1016/s0014-5793(96)01433-0;
RA Grillasca J.-P., Gastaldi M., Khiri H., Dace A., Peyrol N., Reynier P.,
RA Torresani J., Planells R.;
RT "Cloning and initial characterization of human and mouse Spot 14 genes.";
RL FEBS Lett. 401:38-42(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [5]
RP INTERACTION WITH THRB, SUBUNIT, AND FUNCTION.
RX PubMed=17418816; DOI=10.1016/j.bbrc.2007.03.103;
RA Chou W.Y., Cheng Y.S., Ho C.L., Liu S.T., Liu P.Y., Kuo C.C., Chang H.P.,
RA Chen Y.H., Chang G.G., Huang S.M.;
RT "Human spot 14 protein interacts physically and functionally with the
RT thyroid receptor.";
RL Biochem. Biophys. Res. Commun. 357:133-138(2007).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PLAGL1.
RX PubMed=18299245; DOI=10.1016/j.biocel.2008.01.014;
RA Chou W.Y., Ho C.L., Tseng M.L., Liu S.T., Yen L.C., Huang S.M.;
RT "Human Spot 14 protein is a p53-dependent transcriptional coactivator via
RT the recruitment of thyroid receptor and Zac1.";
RL Int. J. Biochem. Cell Biol. 40:1826-1834(2008).
CC -!- FUNCTION: Plays a role in the regulation of lipogenesis, especially in
CC lactating mammary gland. Important for the biosynthesis of
CC triglycerides with medium-length fatty acid chains. May modulate
CC lipogenesis by interacting with MID1IP1 and preventing its interaction
CC with ACACA (By similarity). May function as transcriptional
CC coactivator. May modulate the transcription factor activity of THRB.
CC {ECO:0000250, ECO:0000269|PubMed:17418816,
CC ECO:0000269|PubMed:18299245}.
CC -!- SUBUNIT: Homodimer. Heterodimer with MID1IP1 (By similarity). Interacts
CC with THRB and PLAGL1. {ECO:0000250, ECO:0000269|PubMed:17418816,
CC ECO:0000269|PubMed:18299245}.
CC -!- INTERACTION:
CC Q92748; Q0VD86: INCA1; NbExp=3; IntAct=EBI-1749955, EBI-6509505;
CC Q92748; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-1749955, EBI-11139477;
CC Q92748; Q92748: THRSP; NbExp=4; IntAct=EBI-1749955, EBI-1749955;
CC Q92748; Q9H0C1: ZMYND12; NbExp=3; IntAct=EBI-1749955, EBI-12030590;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18299245}. Cytoplasm
CC {ECO:0000269|PubMed:18299245}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in tissues that synthesize
CC triglycerides.
CC -!- SIMILARITY: Belongs to the SPOT14 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/THRSPID42555ch11q14.html";
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DR EMBL; Y08409; CAA69685.1; -; Genomic_DNA.
DR EMBL; AK311975; BAG34914.1; -; mRNA.
DR EMBL; CH471076; EAW75045.1; -; Genomic_DNA.
DR EMBL; BC031989; AAH31989.1; -; mRNA.
DR CCDS; CCDS8256.1; -.
DR RefSeq; NP_003242.1; NM_003251.3.
DR AlphaFoldDB; Q92748; -.
DR SMR; Q92748; -.
DR BioGRID; 112925; 67.
DR DIP; DIP-40451N; -.
DR IntAct; Q92748; 27.
DR MINT; Q92748; -.
DR STRING; 9606.ENSP00000281030; -.
DR PhosphoSitePlus; Q92748; -.
DR BioMuta; THRSP; -.
DR DMDM; 2842710; -.
DR MassIVE; Q92748; -.
DR PaxDb; Q92748; -.
DR PeptideAtlas; Q92748; -.
DR PRIDE; Q92748; -.
DR ProteomicsDB; 75439; -.
DR Antibodypedia; 31292; 211 antibodies from 31 providers.
DR DNASU; 7069; -.
DR Ensembl; ENST00000281030.2; ENSP00000281030.2; ENSG00000151365.2.
DR GeneID; 7069; -.
DR KEGG; hsa:7069; -.
DR MANE-Select; ENST00000281030.2; ENSP00000281030.2; NM_003251.4; NP_003242.1.
DR UCSC; uc001oyx.4; human.
DR CTD; 7069; -.
DR DisGeNET; 7069; -.
DR GeneCards; THRSP; -.
DR HGNC; HGNC:11800; THRSP.
DR HPA; ENSG00000151365; Tissue enhanced (adipose tissue, liver).
DR MIM; 601926; gene.
DR neXtProt; NX_Q92748; -.
DR OpenTargets; ENSG00000151365; -.
DR PharmGKB; PA36509; -.
DR VEuPathDB; HostDB:ENSG00000151365; -.
DR eggNOG; ENOG502S7IQ; Eukaryota.
DR GeneTree; ENSGT00500000044890; -.
DR HOGENOM; CLU_066079_1_0_1; -.
DR InParanoid; Q92748; -.
DR OMA; MDRYSAT; -.
DR OrthoDB; 1326063at2759; -.
DR PhylomeDB; Q92748; -.
DR TreeFam; TF326826; -.
DR PathwayCommons; Q92748; -.
DR Reactome; R-HSA-200425; Carnitine metabolism.
DR SignaLink; Q92748; -.
DR SIGNOR; Q92748; -.
DR BioGRID-ORCS; 7069; 17 hits in 1075 CRISPR screens.
DR GeneWiki; THRSP; -.
DR GenomeRNAi; 7069; -.
DR Pharos; Q92748; Tbio.
DR PRO; PR:Q92748; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q92748; protein.
DR Bgee; ENSG00000151365; Expressed in upper leg skin and 124 other tissues.
DR Genevisible; Q92748; HS.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
DR GO; GO:0046890; P:regulation of lipid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0010866; P:regulation of triglyceride biosynthetic process; IEA:Ensembl.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR InterPro; IPR009786; Spot_14.
DR PANTHER; PTHR14315; PTHR14315; 1.
DR Pfam; PF07084; Spot_14; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Lipid biosynthesis; Lipid metabolism; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..146
FT /note="Thyroid hormone-inducible hepatic protein"
FT /id="PRO_0000123773"
FT REGION 83..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 146 AA; 16561 MW; 5135FB8EE380DF8F CRC64;
MQVLTKRYPK NCLLTVMDRY AAEVHNMEQV VMIPSLLRDV QLSGPGGQAQ AEAPDLYTYF
TMLKAICVDV DHGLLPREEW QAKVAGSEEN GTAETEEVED ESASGELDLE AQFHLHFSSL
HHILMHLTEK AQEVTRKYQE MTGQVW