Full text data of TSC22D4
TSC22D4
(THG1, TILZ2)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
TSC22 domain family protein 4 (TSC22-related-inducible leucine zipper protein 2; Tsc-22-like protein THG-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
TSC22 domain family protein 4 (TSC22-related-inducible leucine zipper protein 2; Tsc-22-like protein THG-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9Y3Q8
ID T22D4_HUMAN Reviewed; 395 AA.
AC Q9Y3Q8; A4D2C3; D6W5V9;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 2.
DT 22-JAN-2014, entry version 117.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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
RT and has transcriptional repressor activity.";
RL J. Biol. Chem. 274:27439-27447(1999).
RN [2]
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.,
RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA 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.,
RA Mural R.J., Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; THR-211 AND SER-279,
RP AND MASS SPECTROMETRY.
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; THR-211 AND SER-370,
RP AND MASS SPECTROMETRY.
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49 AND SER-279, AND MASS
RP SPECTROMETRY.
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165; SER-279 AND
RP SER-370, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
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.,
RA Buerckstuemmer T., 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 [10]
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.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Transcriptional repressor.
CC -!- SUBUNIT: Forms a homodimer or heterodimer. Can form a heterodimer
CC with TSC22D1.
CC -!- INTERACTION:
CC O95831:AIFM1; NbExp=2; IntAct=EBI-739485, EBI-356440;
CC Q14145:KEAP1; NbExp=3; IntAct=EBI-739485, EBI-751001;
CC Q15365:PCBP1; NbExp=2; IntAct=EBI-739485, EBI-946095;
CC P84022:SMAD3; NbExp=2; IntAct=EBI-739485, EBI-347161;
CC O75800:ZMYND10; NbExp=2; IntAct=EBI-739485, EBI-747061;
CC -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC -!- SIMILARITY: Belongs to the TSC-22/Dip/Bun family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AJ133115; CAB43491.1; -; mRNA.
DR EMBL; CH236956; EAL23831.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76527.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76528.1; -; 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 RefSeq; NP_112197.1; NM_030935.3.
DR RefSeq; XP_005250672.1; XM_005250615.1.
DR UniGene; Hs.469798; -.
DR ProteinModelPortal; Q9Y3Q8; -.
DR SMR; Q9Y3Q8; 326-379.
DR IntAct; Q9Y3Q8; 39.
DR MINT; MINT-1442100; -.
DR STRING; 9606.ENSP00000300181; -.
DR PhosphoSite; Q9Y3Q8; -.
DR DMDM; 14195254; -.
DR PaxDb; Q9Y3Q8; -.
DR PeptideAtlas; Q9Y3Q8; -.
DR PRIDE; Q9Y3Q8; -.
DR DNASU; 81628; -.
DR Ensembl; ENST00000300181; ENSP00000300181; ENSG00000166925.
DR GeneID; 81628; -.
DR KEGG; hsa:81628; -.
DR UCSC; uc003uva.3; human.
DR CTD; 81628; -.
DR GeneCards; GC07M100060; -.
DR HGNC; HGNC:21696; TSC22D4.
DR HPA; HPA006757; -.
DR MIM; 611914; gene.
DR neXtProt; NX_Q9Y3Q8; -.
DR PharmGKB; PA142670698; -.
DR eggNOG; NOG278953; -.
DR HOGENOM; HOG000253006; -.
DR HOVERGEN; HBG069048; -.
DR InParanoid; Q9Y3Q8; -.
DR OMA; FSLAHSM; -.
DR OrthoDB; EOG7RZ5PT; -.
DR PhylomeDB; Q9Y3Q8; -.
DR GenomeRNAi; 81628; -.
DR NextBio; 72010; -.
DR PRO; PR:Q9Y3Q8; -.
DR ArrayExpress; Q9Y3Q8; -.
DR Bgee; Q9Y3Q8; -.
DR CleanEx; HS_TSC22D4; -.
DR Genevestigator; Q9Y3Q8; -.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; NAS:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IEA:Ensembl.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR InterPro; IPR000580; TSC-22_Dip_Bun.
DR PANTHER; PTHR12348; PTHR12348; 1.
DR Pfam; PF01166; TSC22; 1.
DR ProDom; PD007152; TSC-22_Dip_Bun; 1.
DR PROSITE; PS01289; TSC22; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1 395 TSC22 domain family protein 4.
FT /FTId=PRO_0000219374.
FT REGION 344 365 Leucine-zipper.
FT MOD_RES 49 49 Phosphoserine.
FT MOD_RES 62 62 Phosphoserine.
FT MOD_RES 165 165 Phosphoserine.
FT MOD_RES 211 211 Phosphothreonine.
FT MOD_RES 279 279 Phosphoserine.
FT MOD_RES 370 370 Phosphoserine.
FT VARIANT 329 329 V -> M (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_036284.
FT CONFLICT 355 356 NA -> KR (in Ref. 1; CAB43491).
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
//
ID T22D4_HUMAN Reviewed; 395 AA.
AC Q9Y3Q8; A4D2C3; D6W5V9;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 2.
DT 22-JAN-2014, entry version 117.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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
RT and has transcriptional repressor activity.";
RL J. Biol. Chem. 274:27439-27447(1999).
RN [2]
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.,
RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA 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.,
RA Mural R.J., Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; THR-211 AND SER-279,
RP AND MASS SPECTROMETRY.
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; THR-211 AND SER-370,
RP AND MASS SPECTROMETRY.
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49 AND SER-279, AND MASS
RP SPECTROMETRY.
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165; SER-279 AND
RP SER-370, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
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.,
RA Buerckstuemmer T., 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 [10]
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.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Transcriptional repressor.
CC -!- SUBUNIT: Forms a homodimer or heterodimer. Can form a heterodimer
CC with TSC22D1.
CC -!- INTERACTION:
CC O95831:AIFM1; NbExp=2; IntAct=EBI-739485, EBI-356440;
CC Q14145:KEAP1; NbExp=3; IntAct=EBI-739485, EBI-751001;
CC Q15365:PCBP1; NbExp=2; IntAct=EBI-739485, EBI-946095;
CC P84022:SMAD3; NbExp=2; IntAct=EBI-739485, EBI-347161;
CC O75800:ZMYND10; NbExp=2; IntAct=EBI-739485, EBI-747061;
CC -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC -!- SIMILARITY: Belongs to the TSC-22/Dip/Bun family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AJ133115; CAB43491.1; -; mRNA.
DR EMBL; CH236956; EAL23831.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76527.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76528.1; -; 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 RefSeq; NP_112197.1; NM_030935.3.
DR RefSeq; XP_005250672.1; XM_005250615.1.
DR UniGene; Hs.469798; -.
DR ProteinModelPortal; Q9Y3Q8; -.
DR SMR; Q9Y3Q8; 326-379.
DR IntAct; Q9Y3Q8; 39.
DR MINT; MINT-1442100; -.
DR STRING; 9606.ENSP00000300181; -.
DR PhosphoSite; Q9Y3Q8; -.
DR DMDM; 14195254; -.
DR PaxDb; Q9Y3Q8; -.
DR PeptideAtlas; Q9Y3Q8; -.
DR PRIDE; Q9Y3Q8; -.
DR DNASU; 81628; -.
DR Ensembl; ENST00000300181; ENSP00000300181; ENSG00000166925.
DR GeneID; 81628; -.
DR KEGG; hsa:81628; -.
DR UCSC; uc003uva.3; human.
DR CTD; 81628; -.
DR GeneCards; GC07M100060; -.
DR HGNC; HGNC:21696; TSC22D4.
DR HPA; HPA006757; -.
DR MIM; 611914; gene.
DR neXtProt; NX_Q9Y3Q8; -.
DR PharmGKB; PA142670698; -.
DR eggNOG; NOG278953; -.
DR HOGENOM; HOG000253006; -.
DR HOVERGEN; HBG069048; -.
DR InParanoid; Q9Y3Q8; -.
DR OMA; FSLAHSM; -.
DR OrthoDB; EOG7RZ5PT; -.
DR PhylomeDB; Q9Y3Q8; -.
DR GenomeRNAi; 81628; -.
DR NextBio; 72010; -.
DR PRO; PR:Q9Y3Q8; -.
DR ArrayExpress; Q9Y3Q8; -.
DR Bgee; Q9Y3Q8; -.
DR CleanEx; HS_TSC22D4; -.
DR Genevestigator; Q9Y3Q8; -.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; NAS:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IEA:Ensembl.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR InterPro; IPR000580; TSC-22_Dip_Bun.
DR PANTHER; PTHR12348; PTHR12348; 1.
DR Pfam; PF01166; TSC22; 1.
DR ProDom; PD007152; TSC-22_Dip_Bun; 1.
DR PROSITE; PS01289; TSC22; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1 395 TSC22 domain family protein 4.
FT /FTId=PRO_0000219374.
FT REGION 344 365 Leucine-zipper.
FT MOD_RES 49 49 Phosphoserine.
FT MOD_RES 62 62 Phosphoserine.
FT MOD_RES 165 165 Phosphoserine.
FT MOD_RES 211 211 Phosphothreonine.
FT MOD_RES 279 279 Phosphoserine.
FT MOD_RES 370 370 Phosphoserine.
FT VARIANT 329 329 V -> M (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_036284.
FT CONFLICT 355 356 NA -> KR (in Ref. 1; CAB43491).
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
//
MIM
611914
*RECORD*
*FIELD* NO
611914
*FIELD* TI
*611914 TSC22 DOMAIN FAMILY, MEMBER 4; TSC22D4
;;TSC22 HOMOLOGOUS GENE 1; THG1;;
TSC22-LIKE
read more*FIELD* TX
DESCRIPTION
TSC22D4 is a member of the TSC22 domain family of leucine zipper
transcriptional regulators (see TSC22D3; 300506) (Kester et al., 1999;
Fiorenza et al., 2001).
CLONING
By yeast 2-hybrid screening of a mouse brain cDNA library using TSC22D1
(607715) as bait, followed by database analysis, Kester et al. (1999)
cloned human and mouse TSC22D4, which they called THG1. The deduced
395-amino acid human protein contains a TSC box and leucine zipper
region and has a calculated molecular mass of 41 kD. TSC22D4 shares
similarity with TSC22D1, TSC22D3, KIAA0669, and Drosophila
'shortsighted' shs over the TSC box leucine zipper domain.
Fiorenza et al. (2001) used differential screening by subtractive
hybridization of cDNAs isolated from embryonic day 12.5 wildtype and
Lhx3 (LHX4; 602146) mutant mouse pituitaries to clone mouse Tsc22d4,
which they called Thg-1pit. The 387-amino acid mouse protein shares 79%
amino acid identity with human TSC22D4.
Fiorenza et al. (2001) showed that mouse Tsc22d4 expression in the
pituitary cell line GH3 was induced in response to TGF-beta (TGFB1;
190180). RT-PCR assays detected Tsc22d4 expression during mouse
embryonic development with expression first detected at stage 98.5
followed by a sharp increase during the next 24 hours that coincided
with initiation of Lhx3 expression and preceded formation of the
pituitary rudiment. A second increase in Tsc22d4 expression at embryonic
day 12.5 coincided with development of Rathke's pouch. Tsc22d4
expression was also detected in the entire central nervous system. In
contrast, Tsc22d4 expression in Lhx3 mutant mouse embryos showed an
absence of pituitary expression of Tsc22d4 although expression in the
rest of the brain was no different from wildtype. Fiorenza et al. (2001)
concluded that Tsc22d4 is regulated by Lhx3 during pituitary
organogenesis.
GENE FUNCTION
By yeast 2-hybrid analysis, gel shift assay, and GST pull-down
experiments, Kester et al. (1999) confirmed that TSC22D4 interacts with
TSC22D1 by forming heterodimers. They demonstrated that TSC22D4 has
transcriptional repressor activity.
*FIELD* RF
1. Fiorenza, M. T.; Mukhopadhyay, M.; Westphal, H.: Expression screening
for Lhx3 downstream genes identifies Thg-1pit as a novel mouse gene
involved in pituitary development. Gene 278: 125-130, 2001.
2. Kester, H. A.; Blanchetot, C.; den Hertog, J.; van der Saag, P.
T.; van der Burg, B.: Transforming growth factor-beta-stimulated
clone-22 is a member of a family of leucine zipper proteins that can
homo- and heterodimerize and has transcriptional repressor activity. J.
Biol. Chem. 274: 27439-27447, 1999.
*FIELD* CD
Dorothy S. Reilly: 3/24/2008
*FIELD* ED
wwang: 03/24/2008
*RECORD*
*FIELD* NO
611914
*FIELD* TI
*611914 TSC22 DOMAIN FAMILY, MEMBER 4; TSC22D4
;;TSC22 HOMOLOGOUS GENE 1; THG1;;
TSC22-LIKE
read more*FIELD* TX
DESCRIPTION
TSC22D4 is a member of the TSC22 domain family of leucine zipper
transcriptional regulators (see TSC22D3; 300506) (Kester et al., 1999;
Fiorenza et al., 2001).
CLONING
By yeast 2-hybrid screening of a mouse brain cDNA library using TSC22D1
(607715) as bait, followed by database analysis, Kester et al. (1999)
cloned human and mouse TSC22D4, which they called THG1. The deduced
395-amino acid human protein contains a TSC box and leucine zipper
region and has a calculated molecular mass of 41 kD. TSC22D4 shares
similarity with TSC22D1, TSC22D3, KIAA0669, and Drosophila
'shortsighted' shs over the TSC box leucine zipper domain.
Fiorenza et al. (2001) used differential screening by subtractive
hybridization of cDNAs isolated from embryonic day 12.5 wildtype and
Lhx3 (LHX4; 602146) mutant mouse pituitaries to clone mouse Tsc22d4,
which they called Thg-1pit. The 387-amino acid mouse protein shares 79%
amino acid identity with human TSC22D4.
Fiorenza et al. (2001) showed that mouse Tsc22d4 expression in the
pituitary cell line GH3 was induced in response to TGF-beta (TGFB1;
190180). RT-PCR assays detected Tsc22d4 expression during mouse
embryonic development with expression first detected at stage 98.5
followed by a sharp increase during the next 24 hours that coincided
with initiation of Lhx3 expression and preceded formation of the
pituitary rudiment. A second increase in Tsc22d4 expression at embryonic
day 12.5 coincided with development of Rathke's pouch. Tsc22d4
expression was also detected in the entire central nervous system. In
contrast, Tsc22d4 expression in Lhx3 mutant mouse embryos showed an
absence of pituitary expression of Tsc22d4 although expression in the
rest of the brain was no different from wildtype. Fiorenza et al. (2001)
concluded that Tsc22d4 is regulated by Lhx3 during pituitary
organogenesis.
GENE FUNCTION
By yeast 2-hybrid analysis, gel shift assay, and GST pull-down
experiments, Kester et al. (1999) confirmed that TSC22D4 interacts with
TSC22D1 by forming heterodimers. They demonstrated that TSC22D4 has
transcriptional repressor activity.
*FIELD* RF
1. Fiorenza, M. T.; Mukhopadhyay, M.; Westphal, H.: Expression screening
for Lhx3 downstream genes identifies Thg-1pit as a novel mouse gene
involved in pituitary development. Gene 278: 125-130, 2001.
2. Kester, H. A.; Blanchetot, C.; den Hertog, J.; van der Saag, P.
T.; van der Burg, B.: Transforming growth factor-beta-stimulated
clone-22 is a member of a family of leucine zipper proteins that can
homo- and heterodimerize and has transcriptional repressor activity. J.
Biol. Chem. 274: 27439-27447, 1999.
*FIELD* CD
Dorothy S. Reilly: 3/24/2008
*FIELD* ED
wwang: 03/24/2008