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TSC22 domain family protein 3 (DSIP-immunoreactive peptide) (Protein DIP) (hDIP) (Delta sleep-inducing peptide immunoreactor) (Glucocorticoid-induced leucine zipper protein) (GILZ) (TSC-22-like protein) (TSC-22-related protein) (TSC-22R)

 T22D3_HUMAN             Reviewed;         134 AA.
Q99576; Q5H9S3; Q5JRI9; Q6FIH6; Q8NAI1; Q8WVB9; Q9UBN5; Q9UG13;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 2.
27-SEP-2017, entry version 162.
RecName: Full=TSC22 domain family protein 3;
AltName: Full=DSIP-immunoreactive peptide;
Short=Protein DIP;
Short=hDIP;
AltName: Full=Delta sleep-inducing peptide immunoreactor;
AltName: Full=Glucocorticoid-induced leucine zipper protein;
Short=GILZ;
AltName: Full=TSC-22-like protein;
AltName: Full=TSC-22-related protein;
Short=TSC-22R;
Name=TSC22D3; Synonyms=DSIPI, GILZ;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Fetal brain;
PubMed=8982256; DOI=10.1016/S0167-4781(96)00177-7;
Vogel P., Maegert H.-J., Cieslak A., Adermann K., Forssmann W.-G.;
"hDIP -- a potential transcriptional regulator related to murine TSC-
22 and Drosophila shortsighted (shs) -- is expressed in a large number
of human tissues.";
Biochim. Biophys. Acta 1309:200-204(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=T-cell;
PubMed=11313722; DOI=10.1038/sj.cdd.4400798;
Cannarile L., Zollo O., D'Adamio F., Ayroldi E., Marchetti C.,
Tabilio A., Bruscoli S., Riccardi C.;
"Cloning, chromosomal assignment and tissue distribution of human
GILZ, a glucocorticoid hormone-induced gene.";
Cell Death Differ. 8:201-203(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Iris;
Wistow G.J.;
"Full-length sequence of ocular cDNA clones.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Okada T.;
"Human GILZ.";
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Hair follicle dermal papilla;
Kim M.K., Kim Y.H., Suh J.M., Lee H.M., Chung H.J., Sohn M.Y.,
Hwang S.Y., Im S.U., Jung E.J., Kim J.C.;
"A catalogue of genes in the human dermal papilla cells as identified
by expressed sequence tags.";
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Fetal kidney;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Prostate, and Pulmonary artery;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Adipose tissue;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 12-122 (ISOFORM 3).
TISSUE=Colon, and Melanoma;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-134.
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[13]
INTERACTION WITH NFKB1.
PubMed=11468175; DOI=10.1182/blood.V98.3.743;
Ayroldi E., Migliorati G., Bruscoli S., Marchetti C., Zollo O.,
Cannarile L., D'Adamio F., Riccardi C.;
"Modulation of T-cell activation by the glucocorticoid-induced leucine
zipper factor via inhibition of nuclear factor kappa B.";
Blood 98:743-753(2001).
[14]
TISSUE SPECIFICITY, INDUCTION, AND INTERACTION WITH NFKB1.
PubMed=12393603; DOI=10.1182/blood-2002-02-0538;
Berrebi D., Bruscoli S., Cohen N., Foussat A., Migliorati G.,
Bouchet-Delbos L., Maillot M.-C., Portier A., Couderc J., Galanaud P.,
Peuchmaur M., Riccardi C., Emilie D.;
"Synthesis of glucocorticoid-induced leucine zipper (GILZ) by
macrophages: an anti-inflammatory and immunosuppressive mechanism
shared by glucocorticoids and IL-10.";
Blood 101:729-738(2003).
[15]
FUNCTION, AND INDUCTION.
PubMed=15031210; DOI=10.1182/blood-2003-12-4295;
Asselin-Labat M.-L., David M., Biola-Vidamment A., Lecoeuche D.,
Zennaro M.-C., Bertoglio J., Pallardy M.;
"GILZ, a new target for the transcription factor FoxO3, protects T
lymphocytes from interleukin-2 withdrawal-induced apoptosis.";
Blood 104:215-223(2004).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND SER-73 (ISOFORM
2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: Protects T-cells from IL2 deprivation-induced apoptosis
through the inhibition of FOXO3A transcriptional activity that
leads to the down-regulation of the pro-apoptotic factor BCL2L11.
In macrophages, plays a role in the anti-inflammatory and
immunosuppressive effects of glucocorticoids and IL10. In T-cells,
inhibits anti-CD3-induced NFKB1 nuclear translocation. In vitro,
suppresses AP1 and NFKB1 DNA-binding activities (By similarity).
Isoform 1 inhibits myogenic differentiation and mediates anti-
myogenic effects of glucocorticoids by binding and regulating
MYOD1 and HDAC1 transcriptional activity resulting in reduced
expression of MYOG (By similarity). {ECO:0000250,
ECO:0000269|PubMed:15031210}.
-!- SUBUNIT: Can form homodimers, however it is likely to function as
a monomer. Interacts with AP1 (By similarity). Interacts with
NFKB1. Isoform 1 interacts with MYOD1 (By similarity). Isoform 1
interacts with HDAC1; this interaction affects HDAC1 activity on
MYOG promoter and thus inhibits MYOD1 transcriptional activity (By
similarity). {ECO:0000250}.
-!- INTERACTION:
Q0VDD7:C19orf57; NbExp=3; IntAct=EBI-10294415, EBI-741210;
Q9Y6D9:MAD1L1; NbExp=3; IntAct=EBI-10294415, EBI-742610;
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}. Note=Localization depends on differentiation status
of myoblasts. In undifferentiated myoblasts, isoform 1 localizes
to the cytoplasm, but in differentiating myoblasts, isoform 1 is
localized to the nucleus (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q99576-1; Sequence=Displayed;
Name=2;
IsoId=Q99576-3; Sequence=VSP_012689;
Note=Contains a phosphoserine at position 42. Contains a
phosphoserine at position 73. {ECO:0000244|PubMed:18669648};
Name=3;
IsoId=Q99576-4; Sequence=VSP_020732;
Note=Incomplete sequence. No experimental confirmation
available.;
-!- TISSUE SPECIFICITY: Expressed in brain, lung, spleen and skeletal
muscle. Lower levels detected in heart and kidney. Not detected in
the pancreas. In non-lymphoid tissues, in the absence of
inflammation, the major source of constitutive expression is the
macrophage lineage. Also expressed in cells from different
hemopoietic cell lineages, including bone marrow cells, CD34+ stem
cells, mature B- and T-cells, monocytes and granulocytes. Down-
regulated in activated macrophages from inflammatory lesions of
delayed-type hypersensitivity (DTH) reactions, such as in
tuberculosis and in Crohn disease, whereas in Burkitt lymphoma,
persists in macrophages involved in the phagocytosis of apoptotic
malignant cells. {ECO:0000269|PubMed:11313722,
ECO:0000269|PubMed:12393603}.
-!- INDUCTION: By glucocorticoids in lymphoid cells and upon IL4,
IL10, IL13 or glucocorticoid treatment in monocyte/macrophage
cells. Transiently induced by IL2 deprivation in T-cells. Isoform
1 expression is up-regulated by synthetic glucocorticoid
dexamethasone in differentiating myoblasts (By similarity).
{ECO:0000250}.
-!- DOMAIN: The leucine-zipper is involved in homodimerization.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the TSC-22/Dip/Bun family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH18148.3; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAA90644.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAB53669.1; Type=Frameshift; Positions=4; Evidence={ECO:0000305};
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EMBL; Z50781; CAA90644.1; ALT_INIT; mRNA.
EMBL; AF228339; AAG12456.1; -; mRNA.
EMBL; AF183393; AAD56234.1; -; mRNA.
EMBL; AB025432; BAB18680.1; -; mRNA.
EMBL; AF153603; AAD41085.1; -; mRNA.
EMBL; AL110191; CAB53669.1; ALT_FRAME; mRNA.
EMBL; AK092645; BAC03934.1; -; mRNA.
EMBL; AK092669; BAG52587.1; -; mRNA.
EMBL; AL590423; CAI41544.1; -; Genomic_DNA.
EMBL; CH471120; EAX02704.1; -; Genomic_DNA.
EMBL; CH471120; EAX02705.1; -; Genomic_DNA.
EMBL; CH471120; EAX02706.1; -; Genomic_DNA.
EMBL; CR933650; CAI45951.1; -; mRNA.
EMBL; BC018148; AAH18148.3; ALT_INIT; mRNA.
EMBL; BC072446; AAH72446.1; -; mRNA.
EMBL; CR533450; CAG38481.1; -; mRNA.
CCDS; CCDS14530.1; -. [Q99576-3]
CCDS; CCDS14531.1; -. [Q99576-1]
PIR; T14749; T14749.
RefSeq; NP_001015881.1; NM_001015881.1.
RefSeq; NP_001305397.1; NM_001318468.1. [Q99576-3]
RefSeq; NP_001305399.1; NM_001318470.1. [Q99576-3]
RefSeq; NP_004080.2; NM_004089.3. [Q99576-1]
RefSeq; NP_932174.1; NM_198057.2. [Q99576-3]
RefSeq; XP_005262156.1; XM_005262099.1. [Q99576-3]
RefSeq; XP_005262157.1; XM_005262100.1. [Q99576-3]
RefSeq; XP_005262159.1; XM_005262102.1. [Q99576-3]
RefSeq; XP_005262160.1; XM_005262103.3. [Q99576-3]
RefSeq; XP_011529186.1; XM_011530884.1. [Q99576-3]
RefSeq; XP_016884824.1; XM_017029335.1. [Q99576-3]
UniGene; Hs.522074; -.
ProteinModelPortal; Q99576; -.
SMR; Q99576; -.
BioGrid; 108165; 46.
IntAct; Q99576; 13.
MINT; MINT-4715756; -.
STRING; 9606.ENSP00000314655; -.
iPTMnet; Q99576; -.
PhosphoSitePlus; Q99576; -.
BioMuta; TSC22D3; -.
DMDM; 14195584; -.
EPD; Q99576; -.
MaxQB; Q99576; -.
PaxDb; Q99576; -.
PeptideAtlas; Q99576; -.
PRIDE; Q99576; -.
DNASU; 1831; -.
Ensembl; ENST00000315660; ENSP00000314655; ENSG00000157514. [Q99576-3]
Ensembl; ENST00000372383; ENSP00000361458; ENSG00000157514. [Q99576-3]
Ensembl; ENST00000372384; ENSP00000361459; ENSG00000157514. [Q99576-3]
Ensembl; ENST00000372397; ENSP00000361474; ENSG00000157514. [Q99576-1]
Ensembl; ENST00000506081; ENSP00000427427; ENSG00000157514. [Q99576-3]
GeneID; 1831; -.
KEGG; hsa:1831; -.
UCSC; uc004eng.4; human. [Q99576-1]
CTD; 1831; -.
DisGeNET; 1831; -.
EuPathDB; HostDB:ENSG00000157514.16; -.
GeneCards; TSC22D3; -.
HGNC; HGNC:3051; TSC22D3.
HPA; HPA001916; -.
MIM; 300506; gene.
neXtProt; NX_Q99576; -.
OpenTargets; ENSG00000157514; -.
PharmGKB; PA27504; -.
eggNOG; ENOG410IRR1; Eukaryota.
eggNOG; ENOG410YAFT; LUCA.
GeneTree; ENSGT00530000063062; -.
HOVERGEN; HBG056226; -.
InParanoid; Q99576; -.
OMA; STEMFAK; -.
OrthoDB; EOG091G06PM; -.
PhylomeDB; Q99576; -.
TreeFam; TF329224; -.
Reactome; R-HSA-2672351; Stimuli-sensing channels.
SIGNOR; Q99576; -.
ChiTaRS; TSC22D3; human.
GeneWiki; TSC22D3; -.
GenomeRNAi; 1831; -.
PRO; PR:Q99576; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000157514; -.
CleanEx; HS_TSC22D3; -.
ExpressionAtlas; Q99576; baseline and differential.
Genevisible; Q99576; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0043426; F:MRF binding; IEA:Ensembl.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; TAS:ProtInc.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
GO; GO:0070236; P:negative regulation of activation-induced cell death of T cells; IBA:GO_Central.
GO; GO:0048642; P:negative regulation of skeletal muscle tissue development; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:ProtInc.
GO; GO:0006970; P:response to osmotic stress; IEA:Ensembl.
InterPro; IPR000580; TSC-22_Dip_Bun.
PANTHER; PTHR12348; PTHR12348; 1.
Pfam; PF01166; TSC22; 1.
ProDom; PD007152; TSC-22_Dip_Bun; 1.
PROSITE; PS01289; TSC22; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Nucleus;
Phosphoprotein; Reference proteome.
CHAIN 1 134 TSC22 domain family protein 3.
/FTId=PRO_0000219370.
REGION 1 60 AP1-binding. {ECO:0000250}.
REGION 76 97 Leucine-zipper.
MOD_RES 102 102 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 41 MNTEMYQTPMEVAVYQLHNFSISFFSSLLGGDVVSVKLDNS
-> GGWPSAVRAWEKAGSLPAEKEFLASFRAG (in
isoform 3). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8982256}.
/FTId=VSP_020732.
VAR_SEQ 1 40 MNTEMYQTPMEVAVYQLHNFSISFFSSLLGGDVVSVKLDN
-> MAQSKLDCRSPVGLDCCNCCLDLAHRSGLQRGSSGENN
NPGSPTVSNFRQLQEKLVFENLNTDKLNSIMRQDSLEPVLR
DPCYLINEGICNRNIDQTMLSILLFFH (in isoform
2). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_012689.
CONFLICT 54 54 I -> F (in Ref. 1; CAA90644).
{ECO:0000305}.
SEQUENCE 134 AA; 14810 MW; 77B1024969FA8687 CRC64;
MNTEMYQTPM EVAVYQLHNF SISFFSSLLG GDVVSVKLDN SASGASVVAI DNKIEQAMDL
VKNHLMYAVR EEVEILKEQI RELVEKNSQL ERENTLLKTL ASPEQLEKFQ SCLSPEEPAP
ESPQVPEAPG GSAV


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