ID T22D3_HUMAN Reviewed; 134 AA. AC Q99576; Q5H9S3; Q5JRI9; Q5JRJ2; Q6FIH6; Q8NAI1; Q8WVB9; Q9UBN5; Q9UG13; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 2. DT 24-JAN-2024, entry version 203. DE RecName: Full=TSC22 domain family protein 3 {ECO:0000312|HGNC:HGNC:3051}; DE AltName: Full=DSIP-immunoreactive peptide {ECO:0000303|PubMed:8982256}; DE Short=Protein DIP {ECO:0000303|PubMed:8982256}; DE Short=hDIP {ECO:0000303|PubMed:8982256}; DE AltName: Full=Delta sleep-inducing peptide immunoreactor; DE AltName: Full=Glucocorticoid-induced leucine zipper protein {ECO:0000303|PubMed:11313722}; DE Short=GILZ {ECO:0000303|PubMed:11313722}; DE AltName: Full=TSC-22-like protein; DE AltName: Full=TSC-22-related protein; DE Short=TSC-22R; GN Name=TSC22D3 {ECO:0000312|HGNC:HGNC:3051}; GN Synonyms=DSIPI {ECO:0000312|HGNC:HGNC:3051}, GILZ GN {ECO:0000303|PubMed:11313722}; 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 4). RC TISSUE=Fetal brain; RX PubMed=8982256; DOI=10.1016/s0167-4781(96)00177-7; RA Vogel P., Maegert H.-J., Cieslak A., Adermann K., Forssmann W.-G.; RT "hDIP -- a potential transcriptional regulator related to murine TSC-22 and RT Drosophila shortsighted (shs) -- is expressed in a large number of human RT tissues."; RL Biochim. Biophys. Acta 1309:200-204(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=T-cell; RX PubMed=11313722; DOI=10.1038/sj.cdd.4400798; RA Cannarile L., Zollo O., D'Adamio F., Ayroldi E., Marchetti C., Tabilio A., RA Bruscoli S., Riccardi C.; RT "Cloning, chromosomal assignment and tissue distribution of human GILZ, a RT glucocorticoid hormone-induced gene."; RL Cell Death Differ. 8:201-203(2001). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Iris; RA Wistow G.J.; RT "Full-length sequence of ocular cDNA clones."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Okada T.; RT "Human GILZ."; RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Hair follicle dermal papilla; RA Kim M.K., Kim Y.H., Suh J.M., Lee H.M., Chung H.J., Sohn M.Y., Hwang S.Y., RA Im S.U., Jung E.J., Kim J.C.; RT "A catalogue of genes in the human dermal papilla cells as identified by RT expressed sequence tags."; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Fetal kidney; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Prostate, and Pulmonary artery; 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 1). RC TISSUE=Adipose tissue; 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 [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton 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 [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Colon, and Melanoma; 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 [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-134. 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 [13] RP FUNCTION, AND INTERACTION WITH NFKB1. RX PubMed=11468175; DOI=10.1182/blood.v98.3.743; RA Ayroldi E., Migliorati G., Bruscoli S., Marchetti C., Zollo O., RA Cannarile L., D'Adamio F., Riccardi C.; RT "Modulation of T-cell activation by the glucocorticoid-induced leucine RT zipper factor via inhibition of nuclear factor kappa B."; RL Blood 98:743-753(2001). RN [14] RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND INTERACTION WITH NFKB1. RX PubMed=12393603; DOI=10.1182/blood-2002-02-0538; RA Berrebi D., Bruscoli S., Cohen N., Foussat A., Migliorati G., RA Bouchet-Delbos L., Maillot M.-C., Portier A., Couderc J., Galanaud P., RA Peuchmaur M., Riccardi C., Emilie D.; RT "Synthesis of glucocorticoid-induced leucine zipper (GILZ) by macrophages: RT an anti-inflammatory and immunosuppressive mechanism shared by RT glucocorticoids and IL-10."; RL Blood 101:729-738(2003). RN [15] RP FUNCTION, AND INDUCTION. RX PubMed=15031210; DOI=10.1182/blood-2003-12-4295; RA Asselin-Labat M.-L., David M., Biola-Vidamment A., Lecoeuche D., RA Zennaro M.-C., Bertoglio J., Pallardy M.; RT "GILZ, a new target for the transcription factor FoxO3, protects T RT lymphocytes from interleukin-2 withdrawal-induced apoptosis."; RL Blood 104:215-223(2004). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND SER-73 (ISOFORM 2), RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; 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). RN [20] RP TISSUE SPECIFICITY, AND INDUCTION BY IL2 DEPRIVATION. 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). CC -!- FUNCTION: Protects T-cells from IL2 deprivation-induced apoptosis CC through the inhibition of FOXO3A transcriptional activity that leads to CC the down-regulation of the pro-apoptotic factor BCL2L11 CC (PubMed:15031210). In macrophages, plays a role in the anti- CC inflammatory and immunosuppressive effects of glucocorticoids and IL10 CC (PubMed:12393603). In T-cells, inhibits anti-CD3-induced NFKB1 nuclear CC translocation and thereby NFKB1 DNA-binding activities CC (PubMed:11468175). In vitro, suppresses AP-1 transcription factor CC complex DNA-binding activities (By similarity). CC {ECO:0000250|UniProtKB:Q9Z2S7, ECO:0000269|PubMed:11468175, CC ECO:0000269|PubMed:12393603, ECO:0000269|PubMed:15031210}. CC -!- FUNCTION: [Isoform 1]: Inhibits myogenic differentiation and mediates CC anti-myogenic effects of glucocorticoids by binding and regulating CC MYOD1 and HDAC1 transcriptional activity resulting in reduced CC expression of MYOG. {ECO:0000250|UniProtKB:Q9Z2S7}. CC -!- SUBUNIT: Can form homodimers, however it is likely to function as a CC monomer (By similarity). Interacts with NFKB1 (PubMed:11468175, CC PubMed:12393603). Interacts (via N-terminus) with JUN and FOS; these CC interactions inhibit the binding of active AP1 to its target DNA (By CC similarity). {ECO:0000250|UniProtKB:Q9Z2S7, CC ECO:0000269|PubMed:11468175, ECO:0000269|PubMed:12393603}. CC -!- SUBUNIT: [Isoform 1]: Interacts with MYOD1 (By similarity). Interacts CC with HDAC1; this interaction affects HDAC1 activity on MYOG promoter CC and thus inhibits MYOD1 transcriptional activity (By similarity). CC {ECO:0000250|UniProtKB:Q9Z2S7}. CC -!- INTERACTION: CC Q99576; Q9Y6D9: MAD1L1; NbExp=3; IntAct=EBI-750174, EBI-742610; CC Q99576; Q04864-2: REL; NbExp=3; IntAct=EBI-750174, EBI-10829018; CC Q99576-3; Q0VDD7: BRME1; NbExp=3; IntAct=EBI-10294415, EBI-741210; CC Q99576-3; Q9Y6D9: MAD1L1; NbExp=3; IntAct=EBI-10294415, EBI-742610; CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm CC {ECO:0000250|UniProtKB:Q9Z2S7}. Nucleus {ECO:0000250|UniProtKB:Q9Z2S7}. CC Note=Localization depends on differentiation status of myoblasts (By CC similarity). In undifferentiated myoblasts; localizes to the cytoplasm, CC but in differentiating myoblast; localizes to the nucleus (By CC similarity). {ECO:0000250|UniProtKB:Q9Z2S7}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q99576-1; Sequence=Displayed; CC Name=2; CC IsoId=Q99576-3; Sequence=VSP_012689; CC Name=4; CC IsoId=Q99576-5; Sequence=VSP_061579; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, including in the fetal CC brain and liver (PubMed:26752201). Expressed in brain, lung, spleen and CC skeletal muscle (PubMed:11313722, PubMed:12393603). Lower levels CC detected in heart and kidney (PubMed:11313722, PubMed:12393603). Not CC detected in the pancreas (PubMed:11313722). In non-lymphoid tissues, in CC the absence of inflammation, the major source of constitutive CC expression is the macrophage lineage (PubMed:12393603). Also expressed CC in cells from different hemopoietic cell lineages, including bone CC marrow cells, CD34+ stem cells, mature B- and T-cells, monocytes and CC granulocytes (PubMed:11313722). Down-regulated in activated macrophages CC from inflammatory lesions of delayed-type hypersensitivity (DTH) CC reactions, such as in tuberculosis and in Crohn disease, whereas in CC Burkitt lymphoma, persists in macrophages involved in the phagocytosis CC of apoptotic malignant cells (PubMed:12393603). CC {ECO:0000269|PubMed:11313722, ECO:0000269|PubMed:12393603, CC ECO:0000269|PubMed:26752201}. CC -!- INDUCTION: Induced in T-lymphocytes by IL2 deprivation. CC {ECO:0000269|PubMed:26752201}. CC -!- DOMAIN: The leucine-zipper is involved in homodimerization. CC {ECO:0000250|UniProtKB:Q9Z2S7}. CC -!- SIMILARITY: Belongs to the TSC-22/Dip/Bun family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAB53669.1; Type=Frameshift; 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; Z50781; CAA90644.1; -; mRNA. DR EMBL; AF228339; AAG12456.1; -; mRNA. DR EMBL; AF183393; AAD56234.1; -; mRNA. DR EMBL; AB025432; BAB18680.1; -; mRNA. DR EMBL; AF153603; AAD41085.1; -; mRNA. DR EMBL; AL110191; CAB53669.1; ALT_FRAME; mRNA. DR EMBL; AK092645; BAC03934.1; -; mRNA. DR EMBL; AK092669; BAG52587.1; -; mRNA. DR EMBL; AL590423; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF459299; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471120; EAX02704.1; -; Genomic_DNA. DR EMBL; CH471120; EAX02705.1; -; Genomic_DNA. DR EMBL; CH471120; EAX02706.1; -; Genomic_DNA. DR EMBL; CR933650; CAI45951.1; -; mRNA. DR EMBL; BC018148; AAH18148.3; -; mRNA. DR EMBL; BC072446; AAH72446.1; -; mRNA. DR EMBL; CR533450; CAG38481.1; -; mRNA. DR CCDS; CCDS14530.1; -. [Q99576-3] DR CCDS; CCDS14531.1; -. [Q99576-1] DR CCDS; CCDS35365.1; -. [Q99576-5] DR PIR; T14749; T14749. DR RefSeq; NP_001015881.1; NM_001015881.1. [Q99576-5] DR RefSeq; NP_001305397.1; NM_001318468.1. [Q99576-3] DR RefSeq; NP_001305399.1; NM_001318470.1. [Q99576-3] DR RefSeq; NP_004080.2; NM_004089.3. [Q99576-1] DR RefSeq; NP_932174.1; NM_198057.2. [Q99576-3] DR RefSeq; XP_005262156.1; XM_005262099.1. DR RefSeq; XP_005262157.1; XM_005262100.1. DR RefSeq; XP_005262159.1; XM_005262102.1. DR RefSeq; XP_005262160.1; XM_005262103.3. DR RefSeq; XP_011529186.1; XM_011530884.1. DR RefSeq; XP_016884824.1; XM_017029335.1. DR AlphaFoldDB; Q99576; -. DR SMR; Q99576; -. DR BioGRID; 108165; 64. DR IntAct; Q99576; 24. DR STRING; 9606.ENSP00000361458; -. DR BindingDB; Q99576; -. DR iPTMnet; Q99576; -. DR PhosphoSitePlus; Q99576; -. DR BioMuta; TSC22D3; -. DR DMDM; 14195584; -. DR EPD; Q99576; -. DR jPOST; Q99576; -. DR MassIVE; Q99576; -. DR MaxQB; Q99576; -. DR PaxDb; 9606-ENSP00000361458; -. DR PeptideAtlas; Q99576; -. DR ProteomicsDB; 63095; -. DR ProteomicsDB; 78335; -. [Q99576-1] DR ProteomicsDB; 78336; -. [Q99576-3] DR Pumba; Q99576; -. DR Antibodypedia; 29322; 492 antibodies from 32 providers. DR DNASU; 1831; -. DR Ensembl; ENST00000315660.8; ENSP00000314655.4; ENSG00000157514.18. [Q99576-3] DR Ensembl; ENST00000372383.9; ENSP00000361458.4; ENSG00000157514.18. [Q99576-3] DR Ensembl; ENST00000372384.6; ENSP00000361459.2; ENSG00000157514.18. [Q99576-3] DR Ensembl; ENST00000372390.8; ENSP00000361466.4; ENSG00000157514.18. [Q99576-5] DR Ensembl; ENST00000372397.6; ENSP00000361474.2; ENSG00000157514.18. [Q99576-1] DR Ensembl; ENST00000506081.5; ENSP00000427427.1; ENSG00000157514.18. [Q99576-3] DR GeneID; 1831; -. DR KEGG; hsa:1831; -. DR MANE-Select; ENST00000372383.9; ENSP00000361458.4; NM_198057.3; NP_932174.1. [Q99576-3] DR UCSC; uc004eng.4; human. [Q99576-1] DR AGR; HGNC:3051; -. DR CTD; 1831; -. DR DisGeNET; 1831; -. DR GeneCards; TSC22D3; -. DR HGNC; HGNC:3051; TSC22D3. DR HPA; ENSG00000157514; Low tissue specificity. DR MIM; 300506; gene. DR neXtProt; NX_Q99576; -. DR OpenTargets; ENSG00000157514; -. DR PharmGKB; PA27504; -. DR VEuPathDB; HostDB:ENSG00000157514; -. DR eggNOG; KOG4797; Eukaryota. DR GeneTree; ENSGT00940000156656; -. DR HOGENOM; CLU_148757_0_0_1; -. DR InParanoid; Q99576; -. DR OMA; MNAEMYQ; -. DR OrthoDB; 2965073at2759; -. DR PhylomeDB; Q99576; -. DR TreeFam; TF329224; -. DR PathwayCommons; Q99576; -. DR Reactome; R-HSA-2672351; Stimuli-sensing channels. DR SignaLink; Q99576; -. DR SIGNOR; Q99576; -. DR BioGRID-ORCS; 1831; 18 hits in 797 CRISPR screens. DR ChiTaRS; TSC22D3; human. DR GeneWiki; TSC22D3; -. DR GenomeRNAi; 1831; -. DR Pharos; Q99576; Tbio. DR PRO; PR:Q99576; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q99576; Protein. DR Bgee; ENSG00000157514; Expressed in right lung and 215 other cell types or tissues. DR ExpressionAtlas; Q99576; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0070236; P:negative regulation of activation-induced cell death of T cells; IBA:GO_Central. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro. DR GO; GO:0006970; P:response to osmotic stress; IEA:Ensembl. DR CDD; cd21940; ZIP_TSC22D3; 1. DR Gene3D; 1.20.5.490; Single helix bin; 1. DR InterPro; IPR000580; TSC22/Bun. DR InterPro; IPR047862; TSC22/BUN_CS. DR PANTHER; PTHR12348; TSC22; 1. DR PANTHER; PTHR12348:SF24; TSC22 DOMAIN FAMILY PROTEIN 3; 1. DR Pfam; PF01166; TSC22; 1. DR SUPFAM; SSF58026; Delta-sleep-inducing peptide immunoreactive peptide; 1. DR PROSITE; PS01289; TSC22; 1. DR Genevisible; Q99576; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein; KW Reference proteome. FT CHAIN 1..134 FT /note="TSC22 domain family protein 3" FT /id="PRO_0000219370" FT REGION 1..60 FT /note="AP1-binding" FT /evidence="ECO:0000250" FT REGION 76..97 FT /note="Leucine-zipper" FT REGION 108..134 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 102 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..57 FT /note="Missing (in isoform 4)" FT /id="VSP_061579" FT VAR_SEQ 1..40 FT /note="MNTEMYQTPMEVAVYQLHNFSISFFSSLLGGDVVSVKLDN -> MAQSKLDC FT RSPVGLDCCNCCLDLAHRSGLQRGSSGENNNPGSPTVSNFRQLQEKLVFENLNTDKLNS FT IMRQDSLEPVLRDPCYLINEGICNRNIDQTMLSILLFFH (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_012689" FT CONFLICT 54 FT /note="I -> F (in Ref. 1; CAA90644)" FT /evidence="ECO:0000305" FT MOD_RES Q99576-3:42 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES Q99576-3:73 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" SQ SEQUENCE 134 AA; 14810 MW; 77B1024969FA8687 CRC64; MNTEMYQTPM EVAVYQLHNF SISFFSSLLG GDVVSVKLDN SASGASVVAI DNKIEQAMDL VKNHLMYAVR EEVEILKEQI RELVEKNSQL ERENTLLKTL ASPEQLEKFQ SCLSPEEPAP ESPQVPEAPG GSAV //