TSH2_MOUSE
ID TSH2_MOUSE Reviewed; 1030 AA.
AC Q68FE9; Q5DTF1; Q6AXH5; Q9JL71;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Teashirt homolog 2;
DE AltName: Full=SDCCAG33-like protein;
DE AltName: Full=Zinc finger protein 218;
GN Name=Tshz2; Synonyms=Kiaa4248, Sdccag33l, Tsh2, Zfp218, Znf218;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 13-1030, AND FUNCTION.
RX PubMed=10704881; DOI=10.1016/s0925-4773(99)00318-4;
RA Caubit X., Core N., Boned A., Kerridge S., Djabali M., Fasano L.;
RT "Vertebrate orthologues of the Drosophila region-specific patterning gene
RT teashirt.";
RL Mech. Dev. 91:445-448(2000).
RN [4]
RP POSSIBLE FUNCTION.
RX PubMed=14973285; DOI=10.1242/dev.00977;
RA Manfroid I., Caubit X., Kerridge S., Fasano L.;
RT "Three putative murine Teashirt orthologues specify trunk structures in
RT Drosophila in the same way as the Drosophila teashirt gene.";
RL Development 131:1065-1073(2004).
RN [5]
RP INTERACTION WITH APBB1.
RX PubMed=19343227; DOI=10.1371/journal.pone.0005071;
RA Kajiwara Y., Akram A., Katsel P., Haroutunian V., Schmeidler J.,
RA Beecham G., Haines J.L., Pericak-Vance M.A., Buxbaum J.D.;
RT "FE65 binds Teashirt, inhibiting expression of the primate-specific
RT caspase-4.";
RL PLoS ONE 4:E5071-E5071(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-976, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Spleen;
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).
RN [7]
RP DEVELOPMENTAL STAGE.
RX PubMed=19745106; DOI=10.1093/ndt/gfp453;
RA Jenkins D., Caubit X., Dimovski A., Matevska N., Lye C.M., Cabuk F.,
RA Gucev Z., Tasic V., Fasano L., Woolf A.S.;
RT "Analysis of TSHZ2 and TSHZ3 genes in congenital pelvi-ureteric junction
RT obstruction.";
RL Nephrol. Dial. Transplant. 25:54-60(2010).
CC -!- FUNCTION: Probable transcriptional regulator involved in developmental
CC processes. May act as a transcriptional repressor (Potential).
CC {ECO:0000305}.
CC -!- SUBUNIT: Interacts (via homeobox domain) with APBB1 (via PID domain 1).
CC {ECO:0000269|PubMed:19343227}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed in mesenchymal cells in proximal ureters
CC at 14 dpc, preceding the smooth muscle precursor cells differentiation
CC and the expression of contractile proteins from 15 dpc.
CC {ECO:0000269|PubMed:19745106}.
CC -!- PTM: Sumoylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the teashirt C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF64095.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD90333.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC079877; AAH79877.1; -; mRNA.
DR EMBL; BC079550; AAH79550.1; -; mRNA.
DR EMBL; AK220569; BAD90333.1; ALT_INIT; mRNA.
DR EMBL; AF207880; AAF64095.1; ALT_INIT; Genomic_DNA.
DR CCDS; CCDS50805.1; -.
DR RefSeq; NP_536703.2; NM_080455.2.
DR RefSeq; XP_011237817.1; XM_011239515.2.
DR RefSeq; XP_017173455.1; XM_017317966.1.
DR AlphaFoldDB; Q68FE9; -.
DR BioGRID; 230794; 1.
DR STRING; 10090.ENSMUSP00000104785; -.
DR iPTMnet; Q68FE9; -.
DR PhosphoSitePlus; Q68FE9; -.
DR MaxQB; Q68FE9; -.
DR PaxDb; Q68FE9; -.
DR PRIDE; Q68FE9; -.
DR ProteomicsDB; 297662; -.
DR Antibodypedia; 52541; 121 antibodies from 27 providers.
DR DNASU; 228911; -.
DR Ensembl; ENSMUST00000109157; ENSMUSP00000104785; ENSMUSG00000047907.
DR Ensembl; ENSMUST00000109159; ENSMUSP00000104787; ENSMUSG00000047907.
DR GeneID; 228911; -.
DR KEGG; mmu:228911; -.
DR UCSC; uc008obo.2; mouse.
DR CTD; 128553; -.
DR MGI; MGI:2153084; Tshz2.
DR VEuPathDB; HostDB:ENSMUSG00000047907; -.
DR eggNOG; ENOG502QV71; Eukaryota.
DR GeneTree; ENSGT00950000183051; -.
DR HOGENOM; CLU_010469_0_0_1; -.
DR InParanoid; Q68FE9; -.
DR OMA; TGHYQDN; -.
DR OrthoDB; 106971at2759; -.
DR PhylomeDB; Q68FE9; -.
DR TreeFam; TF328447; -.
DR BioGRID-ORCS; 228911; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Tshz2; mouse.
DR PRO; PR:Q68FE9; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q68FE9; protein.
DR Bgee; ENSMUSG00000047907; Expressed in olfactory epithelium and 209 other tissues.
DR ExpressionAtlas; Q68FE9; baseline and differential.
DR Genevisible; Q68FE9; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR027008; Teashirt_fam.
DR InterPro; IPR027010; Tshz2.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR12487; PTHR12487; 1.
DR PANTHER; PTHR12487:SF3; PTHR12487:SF3; 1.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW Coiled coil; Developmental protein; DNA-binding; Homeobox; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1030
FT /note="Teashirt homolog 2"
FT /id="PRO_0000047065"
FT ZN_FING 216..240
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 276..300
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 381..405
FT /note="C2H2-type 3; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT DNA_BIND 837..907
FT /note="Homeobox"
FT ZN_FING 922..944
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 990..1013
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1009..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 11..42
FT /evidence="ECO:0000255"
FT COMPBIAS 23..37
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..488
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..979
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1030
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 976
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 189
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NRE2"
FT CROSSLNK 307
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NRE2"
FT CROSSLNK 316
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NRE2"
FT CROSSLNK 418
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NRE2"
FT CROSSLNK 462
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NRE2"
FT CROSSLNK 480
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NRE2"
FT CROSSLNK 497
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NRE2"
FT CROSSLNK 601
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NRE2"
FT CROSSLNK 652
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NRE2"
FT CROSSLNK 796
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NRE2"
FT CROSSLNK 816
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NRE2"
FT CROSSLNK 962
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NRE2"
FT CONFLICT 159..227
FT /note="Missing (in Ref. 1; AAH79550)"
FT /evidence="ECO:0000305"
FT CONFLICT 607
FT /note="K -> R (in Ref. 3; AAF64095)"
FT /evidence="ECO:0000305"
FT CONFLICT 1012
FT /note="T -> A (in Ref. 3; AAF64095)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1030 AA; 114223 MW; 1F8075095AE4D60E CRC64;
MPRRKQQAPK RAAGYAQEEV LKEEEEIKEE EEEEEDSGSV AQHQSSNDTG TDEELETGPE
QKGYFSCQNS PGSHLSNQDA ENESLLSDAS DQVSDVKSVC GRDVSDKKAN THPKLPSEPH
NCMDKMTAVY ANILSDSYWS GLGLGFKLSN SERRNCDTRN SSGKNDFDWH QDALSKSLQQ
NLPSRSVSKP SLFSSVQLYR QSSKLCGSVF TGASRFRCRQ CSAAYDTLVE LTVHMNETGH
YQDDNRKKDK LRPTSYSKPR KRAFQDMDKE DAQKVLKCMF CGDSFDSLQD LSVHMIKTKH
YQKVPLKEPV PTISSKMVTP AKKRVFDVNR PCSPDSTTGS LADSFSSQKS ANLQLPSNSR
YGYQNGASYT WQFEACKSQI LKCMECGSSH DTLQQLTTHM MVTGHFLKVT SSASKKGKQL
VLDPLAVEKM QSLSETPNSE SLAPKPSSNS PSECTASTTE LKKESKKEKG EGIEDEQGVK
SEDYEDSLQK PLDPTIKYQY LREEDLEDGS KGGGDILKSL ENTVTTAINK AQNGAPSWSA
YPSIHAAYQL SEGTKPPMAM GSQILQIRPN LANKLRPIAP KWKGMPLGPV PTSLALYTQV
KKETEDKDEV VKQCGKESPH EEATSFSQPE GESFSKIEPP SESRKAEPCP LKEEEKPQKE
KPEPLEPVSS LTNGCAPANH TPALPSINPL SALQSVLNNH LGKATEPLRS PSCSSPNSST
SPVFHKSSLH VVDKPVISPT STRPAASVAR HYLFENTDQP IDLTKSKSKR AESSQAQSCT
SPPQKHALCD IADMVKVLPK ATTPKPAASS RVPPMKLEID VRRFEDVSSE VSTLHKRKGR
QSNWNPQHLL ILQAQFASSL FQTSEGKYLL SDLGPQERMQ ISKFTGLSMT TISHWLANVK
YQLRKTGGTK FLKNMDKGHP IFYCSDCASQ FRTPSTYISH LESHLGFQMK DMTRMAADQQ
SKVEQEISRV SSAQRSPETI AGEEDTDSKF KCKLCRRTFV SKHAVKLHLS KTHSKSPEHH
SQFVADVDEE
