T22D4_HUMAN
ID T22D4_HUMAN Reviewed; 395 AA.
AC Q9Y3Q8; A4D2C3; A8MWR6; D6W5V9;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=TSC22 domain family protein 4;
DE AltName: Full=TSC22-related-inducible leucine zipper protein 2;
DE AltName: Full=Tsc-22-like protein THG-1;
GN Name=TSC22D4; Synonyms=THG1, TILZ2;
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 1).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix, Lung, and 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; THR-211 AND SER-279, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; THR-211 AND SER-370, AND
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49 AND SER-279, AND
RP IDENTIFICATION BY 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165; SER-279 AND SER-370, AND
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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; THR-57; SER-62; SER-165;
RP SER-190; SER-225; THR-229; SER-279 AND SER-370, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-229 AND SER-279, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP VARIANT [LARGE SCALE ANALYSIS] MET-329.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Transcriptional repressor.
CC -!- SUBUNIT: Forms a homodimer or heterodimer. Can form a heterodimer with
CC TSC22D1.
CC -!- INTERACTION:
CC Q9Y3Q8; O95831: AIFM1; NbExp=2; IntAct=EBI-739485, EBI-356440;
CC Q9Y3Q8; Q96GX9: APIP; NbExp=3; IntAct=EBI-739485, EBI-359248;
CC Q9Y3Q8; Q9BRR9: ARHGAP9; NbExp=3; IntAct=EBI-739485, EBI-750254;
CC Q9Y3Q8; Q9HC52: CBX8; NbExp=3; IntAct=EBI-739485, EBI-712912;
CC Q9Y3Q8; Q8IYE0-2: CCDC146; NbExp=3; IntAct=EBI-739485, EBI-10247802;
CC Q9Y3Q8; Q9UJX2: CDC23; NbExp=4; IntAct=EBI-739485, EBI-396137;
CC Q9Y3Q8; P28329-3: CHAT; NbExp=3; IntAct=EBI-739485, EBI-25837549;
CC Q9Y3Q8; Q9UBT7: CTNNAL1; NbExp=3; IntAct=EBI-739485, EBI-514206;
CC Q9Y3Q8; P22607: FGFR3; NbExp=3; IntAct=EBI-739485, EBI-348399;
CC Q9Y3Q8; P28799: GRN; NbExp=3; IntAct=EBI-739485, EBI-747754;
CC Q9Y3Q8; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-739485, EBI-14103818;
CC Q9Y3Q8; P04792: HSPB1; NbExp=3; IntAct=EBI-739485, EBI-352682;
CC Q9Y3Q8; Q14145: KEAP1; NbExp=3; IntAct=EBI-739485, EBI-751001;
CC Q9Y3Q8; O60333-2: KIF1B; NbExp=3; IntAct=EBI-739485, EBI-10975473;
CC Q9Y3Q8; P25800: LMO1; NbExp=3; IntAct=EBI-739485, EBI-8639312;
CC Q9Y3Q8; P25791: LMO2; NbExp=3; IntAct=EBI-739485, EBI-739696;
CC Q9Y3Q8; Q13257: MAD2L1; NbExp=5; IntAct=EBI-739485, EBI-78203;
CC Q9Y3Q8; Q8WY64: MYLIP; NbExp=3; IntAct=EBI-739485, EBI-6952711;
CC Q9Y3Q8; Q9UHY1: NRBP1; NbExp=7; IntAct=EBI-739485, EBI-749731;
CC Q9Y3Q8; D3DWK9: NRBP2; NbExp=3; IntAct=EBI-739485, EBI-10176870;
CC Q9Y3Q8; Q15365: PCBP1; NbExp=2; IntAct=EBI-739485, EBI-946095;
CC Q9Y3Q8; O14917: PCDH17; NbExp=3; IntAct=EBI-739485, EBI-947061;
CC Q9Y3Q8; Q9NWS0: PIH1D1; NbExp=4; IntAct=EBI-739485, EBI-357318;
CC Q9Y3Q8; Q13526: PIN1; NbExp=7; IntAct=EBI-739485, EBI-714158;
CC Q9Y3Q8; O15160: POLR1C; NbExp=6; IntAct=EBI-739485, EBI-1055079;
CC Q9Y3Q8; O60437: PPL; NbExp=3; IntAct=EBI-739485, EBI-368321;
CC Q9Y3Q8; Q13131: PRKAA1; NbExp=3; IntAct=EBI-739485, EBI-1181405;
CC Q9Y3Q8; P54646: PRKAA2; NbExp=3; IntAct=EBI-739485, EBI-1383852;
CC Q9Y3Q8; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-739485, EBI-396669;
CC Q9Y3Q8; P84022: SMAD3; NbExp=2; IntAct=EBI-739485, EBI-347161;
CC Q9Y3Q8; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-739485, EBI-741480;
CC Q9Y3Q8; P61758: VBP1; NbExp=3; IntAct=EBI-739485, EBI-357430;
CC Q9Y3Q8; O76024: WFS1; NbExp=3; IntAct=EBI-739485, EBI-720609;
CC Q9Y3Q8; O43167: ZBTB24; NbExp=6; IntAct=EBI-739485, EBI-744471;
CC Q9Y3Q8; O75800: ZMYND10; NbExp=5; IntAct=EBI-739485, EBI-747061;
CC Q9Y3Q8; Q9Y649; NbExp=3; IntAct=EBI-739485, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y3Q8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y3Q8-2; Sequence=VSP_056245;
CC -!- SIMILARITY: Belongs to the TSC-22/Dip/Bun family. {ECO:0000305}.
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DR EMBL; AJ133115; CAB43491.1; -; mRNA.
DR EMBL; AK297702; BAG60060.1; -; mRNA.
DR EMBL; AC092849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236956; EAL23831.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76527.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76528.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76529.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76531.1; -; Genomic_DNA.
DR EMBL; BC001486; AAH01486.1; -; mRNA.
DR EMBL; BC001966; AAH01966.1; -; mRNA.
DR EMBL; BC002972; AAH02972.1; -; mRNA.
DR EMBL; BC010406; AAH10406.1; -; mRNA.
DR CCDS; CCDS5695.1; -. [Q9Y3Q8-1]
DR RefSeq; NP_001289972.1; NM_001303043.1. [Q9Y3Q8-1]
DR RefSeq; NP_112197.1; NM_030935.4. [Q9Y3Q8-1]
DR AlphaFoldDB; Q9Y3Q8; -.
DR SMR; Q9Y3Q8; -.
DR BioGRID; 123563; 121.
DR IntAct; Q9Y3Q8; 94.
DR MINT; Q9Y3Q8; -.
DR STRING; 9606.ENSP00000300181; -.
DR iPTMnet; Q9Y3Q8; -.
DR PhosphoSitePlus; Q9Y3Q8; -.
DR BioMuta; TSC22D4; -.
DR DMDM; 14195254; -.
DR EPD; Q9Y3Q8; -.
DR jPOST; Q9Y3Q8; -.
DR MassIVE; Q9Y3Q8; -.
DR MaxQB; Q9Y3Q8; -.
DR PaxDb; Q9Y3Q8; -.
DR PeptideAtlas; Q9Y3Q8; -.
DR PRIDE; Q9Y3Q8; -.
DR ProteomicsDB; 2262; -.
DR ProteomicsDB; 86064; -. [Q9Y3Q8-1]
DR ABCD; Q9Y3Q8; 7 sequenced antibodies.
DR Antibodypedia; 1818; 140 antibodies from 26 providers.
DR DNASU; 81628; -.
DR Ensembl; ENST00000300181.7; ENSP00000300181.2; ENSG00000166925.9. [Q9Y3Q8-1]
DR Ensembl; ENST00000393991.5; ENSP00000377560.1; ENSG00000166925.9. [Q9Y3Q8-2]
DR GeneID; 81628; -.
DR KEGG; hsa:81628; -.
DR MANE-Select; ENST00000300181.7; ENSP00000300181.2; NM_030935.5; NP_112197.1.
DR UCSC; uc003uva.3; human. [Q9Y3Q8-1]
DR CTD; 81628; -.
DR DisGeNET; 81628; -.
DR GeneCards; TSC22D4; -.
DR HGNC; HGNC:21696; TSC22D4.
DR HPA; ENSG00000166925; Tissue enhanced (brain).
DR MIM; 611914; gene.
DR neXtProt; NX_Q9Y3Q8; -.
DR OpenTargets; ENSG00000166925; -.
DR PharmGKB; PA142670698; -.
DR VEuPathDB; HostDB:ENSG00000166925; -.
DR eggNOG; KOG4797; Eukaryota.
DR GeneTree; ENSGT00940000161400; -.
DR HOGENOM; CLU_052826_0_0_1; -.
DR InParanoid; Q9Y3Q8; -.
DR OMA; FYFFPDA; -.
DR PhylomeDB; Q9Y3Q8; -.
DR TreeFam; TF338725; -.
DR PathwayCommons; Q9Y3Q8; -.
DR SignaLink; Q9Y3Q8; -.
DR BioGRID-ORCS; 81628; 16 hits in 1103 CRISPR screens.
DR ChiTaRS; TSC22D4; human.
DR GenomeRNAi; 81628; -.
DR Pharos; Q9Y3Q8; Tbio.
DR PRO; PR:Q9Y3Q8; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9Y3Q8; protein.
DR Bgee; ENSG00000166925; Expressed in C1 segment of cervical spinal cord and 179 other tissues.
DR ExpressionAtlas; Q9Y3Q8; baseline and differential.
DR Genevisible; Q9Y3Q8; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR GO; GO:0006970; P:response to osmotic stress; IBA:GO_Central.
DR InterPro; IPR000580; TSC-22_Dip_Bun.
DR InterPro; IPR042553; TSC22D4.
DR PANTHER; PTHR47610; PTHR47610; 1.
DR Pfam; PF01166; TSC22; 1.
DR PROSITE; PS01289; TSC22; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..395
FT /note="TSC22 domain family protein 4"
FT /id="PRO_0000219374"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..365
FT /note="Leucine-zipper"
FT REGION 376..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..48
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 57
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQN3"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQN3"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 211
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 229
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQN3"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQN3"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..239
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056245"
FT VARIANT 329
FT /note="V -> M (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036284"
FT CONFLICT 355..356
FT /note="NA -> KR (in Ref. 1; CAB43491)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 395 AA; 41026 MW; DA08B5617C9BB151 CRC64;
MSGGKKKSSF QITSVTTDYE GPGSPGASDP PTPQPPTGPP PRLPNGEPSP DPGGKGTPRN
GSPPPGAPSS RFRVVKLPHG LGEPYRRGRW TCVDVYERDL EPHSFGGLLE GIRGASGGAG
GRSLDSRLEL ASLGLGAPTP PSGLSQGPTS WLRPPPTSPG PQARSFTGGL GQLVVPSKAK
AEKPPLSASS PQQRPPEPET GESAGTSRAA TPLPSLRVEA EAGGSGARTP PLSRRKAVDM
RLRMELGAPE EMGQVPPLDS RPSSPALYFT HDASLVHKSP DPFGAVAAQK FSLAHSMLAI
SGHLDSDDDS GSGSLVGIDN KIEQAMDLVK SHLMFAVREE VEVLKEQIRE LAERNAALEQ
ENGLLRALAS PEQLAQLPSS GVPRLGPPAP NGPSV
