ID T22D1_HUMAN Reviewed; 1073 AA. AC Q15714; A0A087X0H8; B3KRL7; B9EGI0; O00666; Q6AHX5; Q6IBU1; Q8NCN1; Q96JS5; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 31-MAY-2011, sequence version 3. DT 27-MAR-2024, entry version 200. DE RecName: Full=TSC22 domain family protein 1 {ECO:0000312|HGNC:HGNC:16826}; DE AltName: Full=Cerebral protein 2 {ECO:0000303|Ref.4}; DE Short=HUCEP-2 {ECO:0000303|Ref.4}; DE AltName: Full=Regulatory protein TSC-22 {ECO:0000250|UniProtKB:P62501}; DE AltName: Full=TGFB-stimulated clone 22 homolog {ECO:0000250|UniProtKB:P62501}; DE AltName: Full=Transforming growth factor beta-1-induced transcript 4 protein {ECO:0000312|HGNC:HGNC:16826}; GN Name=TSC22D1 {ECO:0000312|HGNC:HGNC:16826}; GN Synonyms=KIAA1994, TGFB1I4, TSC22 {ECO:0000312|HGNC:HGNC:16826}; GN ORFNames=hucep-2; 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 2), TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RX PubMed=8651929; DOI=10.1006/bbrc.1996.0825; RA Jay P., Wei J.W., Marsollier C., Taviaux S., Berge-Lefranc J.-L., Berta P.; RT "Cloning of the human homologue of the TGF beta-stimulated clone 22 gene."; RL Biochem. Biophys. Res. Commun. 222:821-826(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND INDUCTION BY TGFB1 RP AND CYTOKINES. RC TISSUE=Kidney; RX PubMed=9022669; DOI=10.1111/j.1432-1033.1996.460rr.x; RA Ohta S., Shimekake Y., Nagata K.; RT "Molecular cloning and characterization of a transcription factor for the RT C-type natriuretic peptide gene promoter."; RL Eur. J. Biochem. 242:460-466(1996). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=9026990; RA Dmitrenko V.V., Garifulin O.M., Shostak E.A., Smikodub A.I., Kavsan V.M.; RT "The characteristics of different types of mRNA expressed in the human RT brain."; RL Cyt. Genet. 30:41-47(1996). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Brain cortex; RA Yazaki M., Takayama K., Matsumoto K., Yoshimoto M.; RT "Hucep-2, a gene which is expressed in the human brain, is a homologue of RT rodent and chicken TSC-22."; RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Kawamata H., Uchida D., Omotehara F., Hino S., Nakashiro K., Miwa Y., RA Begum N., Hoque M.O., Yoshida H., Sato M.; RT "Cloning and characterization of human TSC-22 genomic DNA."; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=12056414; DOI=10.1093/dnares/9.2.47; RA Ohara O., Nagase T., Mitsui G., Kohga H., Kikuno R., Hiraoka S., RA Takahashi Y., Kitajima S., Saga Y., Koseki H.; RT "Characterization of size-fractionated cDNA libraries generated by the in RT vitro recombination-assisted method."; RL DNA Res. 9:47-57(2002). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4). RC TISSUE=Brain cortex, and Lung; 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Fetal 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 [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [11] 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 [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain, Colon, Lung, Ovary, and Testis; 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 [13] RP FUNCTION, SUBUNIT, AND INTERACTION WITH TSC22D4 (ISOFORM 2). RX PubMed=10488076; DOI=10.1074/jbc.274.39.27439; RA Kester H.A., Blanchetot C., den Hertog J., van der Saag P.T., RA van der Burg B.; RT "Transforming growth factor-beta-stimulated clone-22 is a member of a RT family of leucine zipper proteins that can homo- and heterodimerize and has RT transcriptional repressor activity."; RL J. Biol. Chem. 274:27439-27447(1999). RN [14] RP TISSUE SPECIFICITY. RX PubMed=12468551; DOI=10.1074/jbc.m208076200; RA Gupta R.A., Sarraf P., Brockman J.A., Shappell S.B., Raftery L.A., RA Willson T.M., DuBois R.N.; RT "Peroxisome proliferator-activated receptor gamma and transforming growth RT factor-beta pathways inhibit intestinal epithelial cell growth by RT regulating levels of TSC-22."; RL J. Biol. Chem. 278:7431-7438(2003). RN [15] RP FUNCTION, AND INTERACTION WITH SMAD4. RX PubMed=15881652; DOI=10.1007/s11010-005-3456-7; RA Choi S.J., Moon J.H., Ahn Y.W., Ahn J.H., Kim D.U., Han T.H.; RT "Tsc-22 enhances TGF-beta signaling by associating with Smad4 and induces RT erythroid cell differentiation."; RL Mol. Cell. Biochem. 271:23-28(2005). RN [16] RP FUNCTION, AND INTERACTION WITH TPT1. RX PubMed=18325344; DOI=10.1016/j.febslet.2008.01.066; RA Lee J.H., Rho S.B., Park S.Y., Chun T.; RT "Interaction between fortilin and transforming growth factor-beta RT stimulated clone-22 (TSC-22) prevents apoptosis via the destabilization of RT TSC-22."; RL FEBS Lett. 582:1210-1218(2008). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [18] 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 [19] RP INTERACTION WITH TSC22D4. RX PubMed=21448135; DOI=10.1038/emboj.2011.95; RA Hoemig-Hoelzel C., van Doorn R., Vogel C., Germann M., Cecchini M.G., RA Verdegaal E., Peeper D.S.; RT "Antagonistic TSC22D1 variants control BRAF(E600)-induced senescence."; RL EMBO J. 30:1753-1765(2011). RN [20] RP FUNCTION, IDENTIFICATION IN COMPLEX WITH TGFBR1 AND TGFBR2, INTERACTION RP WITH ACVRL1; ACVR1; BMPR1A; ACVR1B; BMPR1B; ACVR2A; BMPR2; SMAD6 AND SMAD7, RP AND SUBCELLULAR LOCATION. RX PubMed=21791611; DOI=10.1128/mcb.05448-11; RA Yan X., Zhang J., Pan L., Wang P., Xue H., Zhang L., Gao X., Zhao X., RA Ning Y., Chen Y.G.; RT "TSC-22 promotes transforming growth factor beta-mediated cardiac RT myofibroblast differentiation by antagonizing Smad7 activity."; RL Mol. Cell. Biol. 31:3700-3709(2011). RN [21] RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=26752201; DOI=10.1002/jcb.25485; RA Pepin A., Espinasse M.A., Latre de Late P., Szely N., Pallardy M., RA Biola-Vidamment A.; RT "TSC-22 Promotes Interleukin-2-Deprivation Induced Apoptosis in T- RT Lymphocytes."; RL J. Cell. Biochem. 117:1855-1868(2016). RN [22] RP INTERACTION WITH H1-2 (ISOFORMS 2 AND 5), INTERACTION WITH GNL3 (ISOFORM RP 2), AND SUBCELLULAR LOCATION (ISOFORMS 1; 2 AND 5). RX PubMed=34681573; DOI=10.3390/ijms222010913; RA Kamimura R., Uchida D., Kanno S.I., Shiraishi R., Hyodo T., Sawatani Y., RA Shimura M., Hasegawa T., Tsubura-Okubo M., Yaguchi E., Komiyama Y., RA Fukumoto C., Izumi S., Fujita A., Wakui T., Kawamata H.; RT "Identification of Binding Proteins for TSC22D1 Family Proteins Using Mass RT Spectrometry."; RL Int. J. Mol. Sci. 22:0-0(2021). CC -!- FUNCTION: Transcriptional repressor (PubMed:10488076). Acts on the C- CC type natriuretic peptide (CNP) promoter (PubMed:9022669). Acts to CC promote CASP3-mediated apoptosis (PubMed:18325344). Positively CC regulates TGF-beta signaling by interacting with SMAD7 which inhibits CC binding of SMAD7 to TGFBR1, preventing recruitment of SMURF ubiquitin CC ligases to TGFBR1 and inhibiting SMURF-mediated ubiquitination and CC degradation of TGFBR1 (PubMed:21791611). Contributes to enhancement of CC TGF-beta signaling by binding to and modulating the transcription CC activator activity of SMAD4 (PubMed:15881652). Promotes TGF-beta- CC induced transcription of COL1A2; via its interaction with TFE3 at E- CC boxes in the gene proximal promoter (By similarity). Plays a role in CC the repression of hematopoietic precursor cell growth (By similarity). CC Promotes IL2 deprivation-induced apoptosis in T-lymphocytes, via CC repression of TSC22D3/GILZ transcription and activation of the caspase CC cascade (PubMed:26752201). {ECO:0000250|UniProtKB:P62500, CC ECO:0000269|PubMed:10488076, ECO:0000269|PubMed:15881652, CC ECO:0000269|PubMed:18325344, ECO:0000269|PubMed:21791611, CC ECO:0000269|PubMed:26752201, ECO:0000269|PubMed:9022669}. CC -!- FUNCTION: [Isoform 1]: May act to negatively regulate TGFB3 signaling CC and thereby inhibit cell death in mammary gland cells. CC {ECO:0000250|UniProtKB:P62500}. CC -!- FUNCTION: [Isoform 2]: Positively regulates cell death in response to CC TGFB3 during mammary gland involution. {ECO:0000250|UniProtKB:P62500}. CC -!- SUBUNIT: Forms homodimers (PubMed:10488076). Forms heterodimers CC (PubMed:10488076). Component of a complex composed of TSC22D1 (via N- CC terminus), TGFBR1 and TGFBR2; the interaction between TSC22D1 and CC TGFBR1 is inhibited by SMAD7 and promoted by TGFB1 (PubMed:21791611). CC Interacts with SMAD7; the interaction requires TGF-beta and the CC interaction is inhibited by TGFBR1 (PubMed:21791611). Interacts with CC TPT1/fortilin; interaction results in the destabilization of TSC22D1 CC protein and prevents TSC22D1-mediated apoptosis (PubMed:18325344). CC Interacts with SMAD4 (via N-terminus) (PubMed:15881652). Interacts with CC ACVRL1/ALK1, ACVR1/ALK2, BMPR1A/ALK3, ACVR1B/ALK4, BMPR1B/ALK6, CC ACVR2A/ACTRII, and BMPR2 (PubMed:21791611). Interacts with SMAD6 CC (PubMed:21791611). Interacts with TFE3; the interaction is enhanced in CC the presence of TGF-beta (By similarity). CC {ECO:0000250|UniProtKB:P62500, ECO:0000269|PubMed:10488076, CC ECO:0000269|PubMed:15881652, ECO:0000269|PubMed:18325344, CC ECO:0000269|PubMed:21791611}. CC -!- SUBUNIT: [Isoform 1]: Forms a heterodimer with TSC22D4/THG1. CC {ECO:0000269|PubMed:21448135}. CC -!- SUBUNIT: [Isoform 2]: Forms a heterodimer with TSC22D4/THG1 CC (PubMed:10488076, PubMed:21448135). Interacts with histone H1-2 CC (PubMed:34681573). Interacts with GNL3 (PubMed:34681573). CC {ECO:0000269|PubMed:10488076, ECO:0000269|PubMed:21448135, CC ECO:0000269|PubMed:34681573}. CC -!- SUBUNIT: [Isoform 5]: Interacts with histone H1-2. CC {ECO:0000269|PubMed:34681573}. CC -!- INTERACTION: CC Q15714; Q96HA8: NTAQ1; NbExp=4; IntAct=EBI-712609, EBI-741158; CC Q15714; P13693: TPT1; NbExp=5; IntAct=EBI-712609, EBI-1783169; CC Q15714-2; P05067: APP; NbExp=3; IntAct=EBI-12034704, EBI-77613; CC Q15714-2; Q9BVP2: GNL3; NbExp=2; IntAct=EBI-12034704, EBI-641642; CC Q15714-2; Q9H8Y8: GORASP2; NbExp=8; IntAct=EBI-12034704, EBI-739467; CC Q15714-2; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-12034704, EBI-741158; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21791611}. Nucleus CC {ECO:0000250|UniProtKB:P62500}. Cell membrane CC {ECO:0000269|PubMed:21791611}; Peripheral membrane protein CC {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm CC {ECO:0000269|PubMed:34681573}. Nucleus {ECO:0000269|PubMed:34681573}. CC Mitochondrion {ECO:0000269|PubMed:34681573}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm CC {ECO:0000269|PubMed:34681573}. Nucleus {ECO:0000269|PubMed:34681573}. CC Mitochondrion {ECO:0000269|PubMed:34681573}. CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm CC {ECO:0000269|PubMed:34681573}. Nucleus {ECO:0000269|PubMed:34681573}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; Synonyms=TSC22D1-1 {ECO:0000303|PubMed:34681573}; CC IsoId=Q15714-1; Sequence=Displayed; CC Name=2; Synonyms=TSC22D1-2 {ECO:0000303|PubMed:34681573}, TSC-22 CC {ECO:0000303|PubMed:34681573}; CC IsoId=Q15714-2; Sequence=VSP_035325, VSP_035326; CC Name=3; CC IsoId=Q15714-3; Sequence=VSP_035324; CC Name=4; CC IsoId=Q15714-4; Sequence=VSP_044939, VSP_044940; CC Name=5; Synonyms=TSC22D1-3 {ECO:0000303|PubMed:34681573}, TSC22(86) CC {ECO:0000303|PubMed:34681573}; CC IsoId=Q15714-5; Sequence=VSP_061917; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in adult tissues CC (PubMed:8651929, PubMed:26752201). Expressed in the postmitotic CC epithelial compartment at the top of intestinal mucosal villi CC (PubMed:12468551). {ECO:0000269|PubMed:12468551, CC ECO:0000269|PubMed:26752201, ECO:0000269|PubMed:8651929}. CC -!- DEVELOPMENTAL STAGE: Expressed in the fetal brain, lung, liver and CC kidney. {ECO:0000269|PubMed:26752201, ECO:0000269|PubMed:8651929}. CC -!- INDUCTION: Induced by cytokines including TGFB1 in aortic endothelial CC cells. {ECO:0000269|PubMed:9022669}. CC -!- SIMILARITY: Belongs to the TSC-22/Dip/Bun family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAC02703.1; Type=Erroneous initiation; Evidence={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; U35048; AAC50566.1; -; mRNA. DR EMBL; D38585; BAA07598.1; -; mRNA. DR EMBL; AJ222700; CAA10951.1; -; mRNA. DR EMBL; D87061; BAB46917.1; -; mRNA. DR EMBL; AF256226; AAG53077.1; -; Genomic_DNA. DR EMBL; AB082525; BAC02703.1; ALT_INIT; mRNA. DR EMBL; AK091854; BAG52429.1; -; mRNA. DR EMBL; AK312345; BAG35266.1; -; mRNA. DR EMBL; CR456711; CAG32992.1; -; mRNA. DR EMBL; CR627459; CAH10539.1; -; mRNA. DR EMBL; AL138960; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL139184; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL356107; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF455773; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471075; EAX08710.1; -; Genomic_DNA. DR EMBL; BC000456; AAH00456.1; -; mRNA. DR EMBL; BC016867; AAH16867.1; -; mRNA. DR EMBL; BC069207; AAH69207.1; -; mRNA. DR EMBL; BC105277; AAI05278.1; -; mRNA. DR EMBL; BC136475; AAI36476.1; -; mRNA. DR EMBL; BC136482; AAI36483.1; -; mRNA. DR EMBL; BC146664; AAI46665.1; -; mRNA. DR EMBL; BC146679; AAI46680.1; -; mRNA. DR CCDS; CCDS31966.1; -. [Q15714-1] DR CCDS; CCDS58291.1; -. [Q15714-4] DR CCDS; CCDS73565.1; -. [Q15714-5] DR CCDS; CCDS9392.1; -. [Q15714-2] DR PIR; JC4813; JC4813. DR RefSeq; NP_001230726.1; NM_001243797.1. [Q15714-5] DR RefSeq; NP_001230727.1; NM_001243798.1. [Q15714-5] DR RefSeq; NP_001230728.1; NM_001243799.1. [Q15714-4] DR RefSeq; NP_006013.1; NM_006022.3. [Q15714-2] DR RefSeq; NP_904358.2; NM_183422.3. [Q15714-1] DR AlphaFoldDB; Q15714; -. DR SMR; Q15714; -. DR BioGRID; 114374; 101. DR IntAct; Q15714; 79. DR MINT; Q15714; -. DR STRING; 9606.ENSP00000397435; -. DR GlyCosmos; Q15714; 3 sites, 1 glycan. DR GlyGen; Q15714; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q15714; -. DR MetOSite; Q15714; -. DR PhosphoSitePlus; Q15714; -. DR BioMuta; TSC22D1; -. DR DMDM; 334302874; -. DR EPD; Q15714; -. DR jPOST; Q15714; -. DR MassIVE; Q15714; -. DR MaxQB; Q15714; -. DR PaxDb; 9606-ENSP00000397435; -. DR PeptideAtlas; Q15714; -. DR ProteomicsDB; 3607; -. DR ProteomicsDB; 60713; -. [Q15714-1] DR ProteomicsDB; 60714; -. [Q15714-2] DR ProteomicsDB; 60715; -. [Q15714-3] DR Pumba; Q15714; -. DR TopDownProteomics; Q15714-3; -. [Q15714-3] DR Antibodypedia; 23553; 527 antibodies from 31 providers. DR DNASU; 8848; -. DR Ensembl; ENST00000261489.7; ENSP00000261489.2; ENSG00000102804.16. [Q15714-2] DR Ensembl; ENST00000458659.3; ENSP00000397435.2; ENSG00000102804.16. [Q15714-1] DR Ensembl; ENST00000611198.4; ENSP00000481585.1; ENSG00000102804.16. [Q15714-5] DR Ensembl; ENST00000622051.1; ENSP00000483407.1; ENSG00000102804.16. [Q15714-5] DR GeneID; 8848; -. DR KEGG; hsa:8848; -. DR MANE-Select; ENST00000458659.3; ENSP00000397435.2; NM_183422.4; NP_904358.2. DR UCSC; uc001uzm.5; human. [Q15714-1] DR AGR; HGNC:16826; -. DR CTD; 8848; -. DR DisGeNET; 8848; -. DR GeneCards; TSC22D1; -. DR HGNC; HGNC:16826; TSC22D1. DR HPA; ENSG00000102804; Low tissue specificity. DR MIM; 607715; gene. DR neXtProt; NX_Q15714; -. DR OpenTargets; ENSG00000102804; -. DR PharmGKB; PA134887618; -. DR VEuPathDB; HostDB:ENSG00000102804; -. DR eggNOG; KOG4797; Eukaryota. DR GeneTree; ENSGT00940000159144; -. DR HOGENOM; CLU_148757_0_0_1; -. DR InParanoid; Q15714; -. DR OMA; EDSGHQQ; -. DR OrthoDB; 2965073at2759; -. DR PhylomeDB; Q15714; -. DR TreeFam; TF318837; -. DR PathwayCommons; Q15714; -. DR SignaLink; Q15714; -. DR SIGNOR; Q15714; -. DR BioGRID-ORCS; 8848; 16 hits in 1179 CRISPR screens. DR ChiTaRS; TSC22D1; human. DR GeneWiki; TSC22D1; -. DR GenomeRNAi; 8848; -. DR Pharos; Q15714; Tbio. DR PRO; PR:Q15714; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; Q15714; Protein. DR Bgee; ENSG00000102804; Expressed in endothelial cell and 219 other cell types or tissues. DR ExpressionAtlas; Q15714; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central. DR GO; GO:1902034; P:negative regulation of hematopoietic stem cell proliferation; ISS:UniProtKB. DR GO; GO:0043069; P:negative regulation of programmed cell death; ISS:UniProtKB. DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central. DR GO; GO:0043068; P:positive regulation of programmed cell death; ISS:UniProtKB. DR GO; GO:1901390; P:positive regulation of transforming growth factor beta activation; IMP:UniProtKB. DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IMP:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro. DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc. DR CDD; cd21938; ZIP_TSC22D1; 1. DR Gene3D; 1.20.5.490; Single helix bin; 1. DR InterPro; IPR000580; TSC22/Bun. DR InterPro; IPR047862; TSC22/BUN_CS. DR PANTHER; PTHR46745; TSC22 DOMAIN FAMILY PROTEIN 1; 1. DR PANTHER; PTHR46745:SF1; TSC22 DOMAIN FAMILY PROTEIN 1; 1. DR Pfam; PF01166; TSC22; 1. DR SUPFAM; SSF58026; Delta-sleep-inducing peptide immunoreactive peptide; 1. DR PROSITE; PS01289; TSC22; 1. DR Genevisible; Q15714; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Cytoplasm; Membrane; Mitochondrion; KW Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription; KW Transcription regulation. FT CHAIN 1..1073 FT /note="TSC22 domain family protein 1" FT /id="PRO_0000219365" FT REGION 1..98 FT /note="Required for interaction with TGFBR1 and promotion FT of TGF-beta signaling" FT /evidence="ECO:0000269|PubMed:21791611" FT REGION 22..110 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 125..205 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 220..288 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 458..486 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 607..628 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 742..766 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1006..1027 FT /note="Leucine-zipper" FT REGION 1037..1073 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 35..59 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 60..84 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 85..99 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 172..188 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 220..238 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 249..288 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 458..483 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 610..624 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 263 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT VAR_SEQ 1..987 FT /note="Missing (in isoform 5)" FT /id="VSP_061917" FT VAR_SEQ 1..921 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8651929, FT ECO:0000303|PubMed:9022669, ECO:0000303|PubMed:9026990, FT ECO:0000303|Ref.4, ECO:0000303|Ref.8" FT /id="VSP_035325" FT VAR_SEQ 1..488 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_035324" FT VAR_SEQ 557..570 FT /note="QQKQGLQPVPLQAT -> LTMKVVLLIVYLCM (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044939" FT VAR_SEQ 571..1073 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044940" FT VAR_SEQ 922..970 FT /note="VGLPQTISGDSGGMSAVSDGSSSSLAASASLFPLKVLPLTTPLVDGEDE -> FT MKSQWCRPVAMDLGVYQLRHFSISFLSSLLGTENASVRLDN (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8651929, FT ECO:0000303|PubMed:9022669, ECO:0000303|PubMed:9026990, FT ECO:0000303|Ref.4, ECO:0000303|Ref.8" FT /id="VSP_035326" FT VARIANT 652 FT /note="P -> S (in dbSNP:rs9525983)" FT /id="VAR_057311" FT CONFLICT 332 FT /note="M -> I (in Ref. 6; BAC02703)" FT /evidence="ECO:0000305" FT CONFLICT 581 FT /note="P -> L (in Ref. 12; CAH10539)" FT /evidence="ECO:0000305" FT CONFLICT 661 FT /note="P -> S (in Ref. 12; CAH10539)" FT /evidence="ECO:0000305" FT CONFLICT Q15714-2:15 FT /note="V -> A (in Ref. 4; BAB46917)" FT /evidence="ECO:0000305" SQ SEQUENCE 1073 AA; 109677 MW; BFA471E36FCD06BD CRC64; MHQPPESTAA AAAAADISAR KMAHPAMFPR RGSGSGSASA LNAAGTGVGS NATSSEDFPP PSLLQPPPPA ASSTSGPQPP PPQSLNLLSQ AQLQAQPLAP GGTQMKKKSG FQITSVTPAQ ISASISSNNS IAEDTESYDD LDESHTEDLS SSEILDVSLS RATDLGEPER SSSEETLNNF QEAETPGAVS PNQPHLPQPH LPHLPQQNVV INGNAHPHHL HHHHQIHHGH HLQHGHHHPS HVAVASASIT GGPPSSPVSR KLSTTGSSDS ITPVAPTSAV SSSGSPASVM TNMRAPSTTG GIGINSVTGT STVNNVNITA VGSFNPNVTS SMLGNVNIST SNIPSAAGVS VGPGVTSGVN VNILSGMGNG TISSSAAVSS VPNAAAGMTG GSVSSQQQQP TVNTSRFRVV KLDSSSEPFK KGRWTCTEFY EKENAVPATE GVLINKVVET VKQNPIEVTS ERESTSGSSV SSSVSTLSHY TESVGSGEMG APTVVVQQQQ QQQQQQQQQP ALQGVTLQQM DFGSTGPQSI PAVSIPQSIS QSQISQVQLQ SQELSYQQKQ GLQPVPLQAT MSAATGIQPS PVNVVGVTSA LGQQPSISSL AQPQLPYSQA APPVQTPLPG APPPQQLQYG QQQPMVSTQM APGHVKSVTQ NPASEYVQQQ PILQTAMSSG QPSSAGVGAG TTVIPVAQPQ GIQLPVQPTA VPAQPAGASV QPVGQAPAAV SAVPTGSQIA NIGQQANIPT AVQQPSTQVP PSVIQQGAPP SSQVVPPAQT GIIHQGVQTS APSLPQQLVI ASQSSLLTVP PQPQGVEPVA QGIVSQQLPA VSSLPSASSI SVTSQVSSTG PSGMPSAPTN LVPPQNIAQT PATQNGNLVQ SVSQPPLIAT NTNLPLAQQI PLSSTQFSAQ SLAQAIGSQI EDARRAAEPS LVGLPQTISG DSGGMSAVSD GSSSSLAASA SLFPLKVLPL TTPLVDGEDE SSSGASVVAI DNKIEQAMDL VKSHLMYAVR EEVEVLKEQI KELIEKNSQL EQENNLLKTL ASPEQLAQFQ AQLQTGSPPA TTQPQGTTQP PAQPASQGSG PTA //