T22D3_HUMAN
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 03-AUG-2022, entry version 195.
DE RecName: Full=TSC22 domain family protein 3 {ECO:0000305};
DE AltName: Full=DSIP-immunoreactive peptide;
DE Short=Protein DIP;
DE Short=hDIP;
DE AltName: Full=Delta sleep-inducing peptide immunoreactor;
DE AltName: Full=Glucocorticoid-induced leucine zipper protein;
DE Short=GILZ;
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}; Synonyms=DSIPI, GILZ;
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 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 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).
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. In
CC macrophages, plays a role in the anti-inflammatory and
CC immunosuppressive effects of glucocorticoids and IL10. In T-cells,
CC inhibits anti-CD3-induced NFKB1 nuclear translocation. In vitro,
CC suppresses AP1 and NFKB1 DNA-binding activities (By similarity).
CC Isoform 1 inhibits myogenic differentiation and mediates anti-myogenic
CC effects of glucocorticoids by binding and regulating MYOD1 and HDAC1
CC transcriptional activity resulting in reduced expression of MYOG (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:15031210}.
CC -!- SUBUNIT: Can form homodimers, however it is likely to function as a
CC monomer. Interacts with AP1 (By similarity). Interacts with NFKB1.
CC Isoform 1 interacts with MYOD1 (By similarity). Isoform 1 interacts
CC with HDAC1; this interaction affects HDAC1 activity on MYOG promoter
CC and thus inhibits MYOD1 transcriptional activity (By similarity).
CC {ECO:0000250}.
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 {ECO:0000250}. Nucleus
CC {ECO:0000250}. Note=Localization depends on differentiation status of
CC myoblasts. In undifferentiated myoblasts, isoform 1 localizes to the
CC cytoplasm, but in differentiating myoblasts, isoform 1 is localized to
CC the nucleus (By similarity). {ECO:0000250}.
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: Expressed in brain, lung, spleen and skeletal
CC muscle. Lower levels detected in heart and kidney. Not detected in the
CC pancreas. In non-lymphoid tissues, in the absence of inflammation, the
CC major source of constitutive expression is the macrophage lineage. Also
CC expressed in cells from different hemopoietic cell lineages, including
CC bone marrow cells, CD34+ stem cells, mature B- and T-cells, monocytes
CC and granulocytes. Down-regulated in activated macrophages from
CC inflammatory lesions of delayed-type hypersensitivity (DTH) reactions,
CC such as in tuberculosis and in Crohn disease, whereas in Burkitt
CC lymphoma, persists in macrophages involved in the phagocytosis of
CC apoptotic malignant cells. {ECO:0000269|PubMed:11313722,
CC ECO:0000269|PubMed:12393603}.
CC -!- INDUCTION: By glucocorticoids in lymphoid cells and upon IL4, IL10,
CC IL13 or glucocorticoid treatment in monocyte/macrophage cells.
CC Transiently induced by IL2 deprivation in T-cells. Isoform 1 expression
CC is up-regulated by synthetic glucocorticoid dexamethasone in
CC differentiating myoblasts (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The leucine-zipper is involved in homodimerization.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TSC-22/Dip/Bun family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB53669.1; Type=Frameshift; Evidence={ECO:0000305};
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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 PIR; T14749; T14749.
DR RefSeq; NP_001015881.1; NM_001015881.1.
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. [Q99576-3]
DR RefSeq; XP_005262157.1; XM_005262100.1. [Q99576-3]
DR RefSeq; XP_005262159.1; XM_005262102.1. [Q99576-3]
DR RefSeq; XP_005262160.1; XM_005262103.3. [Q99576-3]
DR RefSeq; XP_011529186.1; XM_011530884.1. [Q99576-3]
DR RefSeq; XP_016884824.1; XM_017029335.1. [Q99576-3]
DR AlphaFoldDB; Q99576; -.
DR SMR; Q99576; -.
DR BioGRID; 108165; 61.
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; Q99576; -.
DR PeptideAtlas; Q99576; -.
DR PRIDE; Q99576; -.
DR ProteomicsDB; 78335; -. [Q99576-1]
DR ProteomicsDB; 78336; -. [Q99576-3]
DR Antibodypedia; 29322; 453 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; 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 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; YQSPMEV; -.
DR OrthoDB; 1602203at2759; -.
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; 16 hits in 721 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 213 other tissues.
DR ExpressionAtlas; Q99576; baseline and differential.
DR Genevisible; Q99576; HS.
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; IEA:Ensembl.
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 InterPro; IPR000580; TSC-22_Dip_Bun.
DR Pfam; PF01166; TSC22; 1.
DR PROSITE; PS01289; TSC22; 1.
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
