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T22D4_MOUSE
ID   T22D4_MOUSE             Reviewed;         387 AA.
AC   Q9EQN3; Q99PD5; Q9D2V9;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=TSC22 domain family protein 4;
DE   AltName: Full=TSC22-related-inducible leucine zipper protein 2;
DE   AltName: Full=Thg-1pit;
GN   Name=Tsc22d4; Synonyms=Thg1pit, Tilz2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND INDUCTION.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=11707329; DOI=10.1016/s0378-1119(01)00715-6;
RA   Fiorenza M.T., Mukhopadhyay M., Westphal H.;
RT   "Expression screening for Lhx3 downstream genes identifies Thg-1pit as a
RT   novel mouse gene involved in pituitary development.";
RL   Gene 278:125-130(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Ershler M.A., Belyavsky A.V., Visser J.W.M.;
RT   "Identification and characterization of a family of leucine zipper genes
RT   related to TSC22.";
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165; THR-183; SER-187;
RP   SER-189; SER-219; THR-223; SER-254; SER-258 AND SER-271, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC   Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Transcriptional repressor. {ECO:0000250}.
CC   -!- SUBUNIT: Forms a homodimer or heterodimer. Can form a heterodimer with
CC       TSC22D1 (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q9EQN3; Q9Z0X1: Aifm1; NbExp=4; IntAct=EBI-7821198, EBI-773597;
CC       Q9EQN3; P62500: Tsc22d1; NbExp=2; IntAct=EBI-7821198, EBI-8296837;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Expression starts at 8.5 dpc and undergoes a
CC       second peak of activation at 12.5 dpc. At 12.5 dpc, expression
CC       encompasses the entire central nervous system, with highest levels in
CC       the dorsal root and trigeminal ganglia. {ECO:0000269|PubMed:11707329}.
CC   -!- INDUCTION: Up-regulated by TGF-beta treatment.
CC       {ECO:0000269|PubMed:11707329}.
CC   -!- SIMILARITY: Belongs to the TSC-22/Dip/Bun family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK02018.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF315352; AAK02018.1; ALT_FRAME; mRNA.
DR   EMBL; AF201286; AAG41219.1; -; mRNA.
DR   EMBL; BC018544; AAH18544.1; -; mRNA.
DR   EMBL; BC023761; AAH23761.1; -; mRNA.
DR   EMBL; BC145721; AAI45722.1; -; mRNA.
DR   EMBL; BC145723; AAI45724.1; -; mRNA.
DR   EMBL; AK018735; BAB31377.1; -; mRNA.
DR   EMBL; AK143608; BAE25460.1; -; mRNA.
DR   EMBL; CH466529; EDL19240.1; -; Genomic_DNA.
DR   CCDS; CCDS19776.1; -.
DR   RefSeq; NP_076399.4; NM_023910.6.
DR   AlphaFoldDB; Q9EQN3; -.
DR   SMR; Q9EQN3; -.
DR   BioGRID; 219663; 3.
DR   IntAct; Q9EQN3; 5.
DR   MINT; Q9EQN3; -.
DR   STRING; 10090.ENSMUSP00000098107; -.
DR   iPTMnet; Q9EQN3; -.
DR   PhosphoSitePlus; Q9EQN3; -.
DR   EPD; Q9EQN3; -.
DR   jPOST; Q9EQN3; -.
DR   MaxQB; Q9EQN3; -.
DR   PaxDb; Q9EQN3; -.
DR   PRIDE; Q9EQN3; -.
DR   ProteomicsDB; 263231; -.
DR   Antibodypedia; 1818; 140 antibodies from 26 providers.
DR   DNASU; 78829; -.
DR   Ensembl; ENSMUST00000100539; ENSMUSP00000098107; ENSMUSG00000029723.
DR   GeneID; 78829; -.
DR   KEGG; mmu:78829; -.
DR   UCSC; uc009adu.2; mouse.
DR   CTD; 402573; -.
DR   MGI; MGI:1926079; Tsc22d4.
DR   VEuPathDB; HostDB:ENSMUSG00000029723; -.
DR   eggNOG; KOG4797; Eukaryota.
DR   GeneTree; ENSGT00940000161400; -.
DR   HOGENOM; CLU_052826_0_0_1; -.
DR   InParanoid; Q9EQN3; -.
DR   OMA; FYFFPDA; -.
DR   TreeFam; TF338725; -.
DR   BioGRID-ORCS; 78829; 2 hits in 74 CRISPR screens.
DR   ChiTaRS; Tsc22d4; mouse.
DR   PRO; PR:Q9EQN3; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q9EQN3; protein.
DR   Bgee; ENSMUSG00000029723; Expressed in granulocyte and 268 other tissues.
DR   ExpressionAtlas; Q9EQN3; baseline and differential.
DR   Genevisible; Q9EQN3; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   GO; GO:0006970; P:response to osmotic stress; IDA:MGI.
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   Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..387
FT                   /note="TSC22 domain family protein 4"
FT                   /id="PRO_0000219375"
FT   REGION          1..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          135..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          336..357
FT                   /note="Leucine-zipper"
FT   REGION          368..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..48
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..212
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         57
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y3Q8"
FT   MOD_RES         62
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y3Q8"
FT   MOD_RES         165
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         183
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         187
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         189
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         219
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         223
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         254
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         258
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         271
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         362
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y3Q8"
FT   CONFLICT        97
FT                   /note="E -> K (in Ref. 1; AAK02018)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        339
FT                   /note="Q -> H (in Ref. 2; AAG41219)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   387 AA;  39979 MW;  D4160FA3AB2DFB90 CRC64;
     MSGGKKKSSF QITSVTTDYE GPGSPGASDS PVPPALAGPP PRLPNGDPNP DPGGRGTPRN
     GSPPPGAPAS RFRVVKLPQG LGEPYRRGRW TCVDVYERDL EPPSFGRLLE GIRGASGGTG
     GRSLDSRLEL ASLGISTPIP QPGLSQGPTS WLRPPPTSPG PQARSFTGGL GQLAGPGKAK
     VETPPLSASP PQQRPPGPGT GDSAQTLPSL RVEVESGGSA AATPPLSRRR DGAVRLRMEL
     VAPAETGKVP PTDSRPNSPA LYFDASLVHK SPDPFGAAAA QSLSLARSML AISGHLDSDD
     DSGSGSLVGI DNKIEQAMDL VKSHLMFAVR EEVEVLKEQI RDLAERNAAL EQENGLLRAL
     ASPEQLAQLP SSGLPRLGPS APNGPSI
 
 
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