TRPS1_MOUSE
ID TRPS1_MOUSE Reviewed; 1281 AA.
AC Q925H1;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=Zinc finger transcription factor Trps1;
GN Name=Trps1;
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], FUNCTION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Fetal intestine;
RX PubMed=11285235; DOI=10.1093/emboj/20.7.1715;
RA Malik T.H., Shoichet S.A., Latham P., Kroll T.G., Peters L.L.,
RA Shivdasani R.A.;
RT "Transcriptional repression and developmental functions of the atypical
RT vertebrate GATA protein TRPS1.";
RL EMBO J. 20:1715-1725(2001).
RN [2]
RP INTERACTION WITH RNF4.
RX PubMed=12885770; DOI=10.1074/jbc.m306259200;
RA Kaiser F.J., Moeroey T., Chang G.T., Horsthemke B., Luedecke H.J.;
RT "The RING finger protein RNF4, a co-regulator of transcription, interacts
RT with the TRPS1 transcription factor.";
RL J. Biol. Chem. 278:38780-38785(2003).
RN [3]
RP FUNCTION, AND INTERACTION WITH GLI3.
RX PubMed=19389374; DOI=10.1016/j.ydbio.2009.01.012;
RA Wuelling M., Kaiser F.J., Buelens L.A., Braunholz D., Shivdasani R.A.,
RA Depping R., Vortkamp A.;
RT "Trps1, a regulator of chondrocyte proliferation and differentiation,
RT interacts with the activator form of Gli3.";
RL Dev. Biol. 328:40-53(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 AND SER-216, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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. Binds specifically to GATA
CC sequences and represses expression of GATA-regulated genes at selected
CC sites and stages in vertebrate development. Regulates chondrocyte
CC proliferation and differentiation. Executes multiple functions in
CC proliferating chondrocytes, expanding the region of distal
CC chondrocytes, activating proliferation in columnar cells and supporting
CC the differentiation of columnar into hypertrophic chondrocytes.
CC {ECO:0000269|PubMed:11285235, ECO:0000269|PubMed:19389374}.
CC -!- SUBUNIT: Interacts with RNF4; regulates TRPS1 repressor activity.
CC Interacts specifically with the activator form of GLI3 (GLI3A) but not
CC with the repressor form (GLI3R). {ECO:0000269|PubMed:12885770,
CC ECO:0000269|PubMed:19389374}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: In the embryo, expression is detected in both
CC visceral and skeletal tissues. Found in the maxilla, mandible, snout,
CC prospective phalanges and in the femoral head within the developing
CC hip. Also expressed in the hair follicles.
CC -!- DEVELOPMENTAL STAGE: Detected prior to 7.5 dpc, with peak levels at
CC around 11.5 dpc. In the developing limbs and face, levels are highest
CC at 13.5 dpc and decline dramatically thereafter.
CC {ECO:0000269|PubMed:11285235}.
CC -!- PTM: Sumoylated. Sumoylation in the repressor domain inhibits the
CC transcription repression activity. Sumoylation on Lys-1201 is the major
CC site. Appears to be sumoylated on multiple sites (By similarity).
CC {ECO:0000250}.
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DR EMBL; AF346836; AAK39508.1; -; mRNA.
DR CCDS; CCDS27460.1; -.
DR AlphaFoldDB; Q925H1; -.
DR IntAct; Q925H1; 2.
DR MINT; Q925H1; -.
DR STRING; 10090.ENSMUSP00000129779; -.
DR iPTMnet; Q925H1; -.
DR PhosphoSitePlus; Q925H1; -.
DR MaxQB; Q925H1; -.
DR PaxDb; Q925H1; -.
DR PRIDE; Q925H1; -.
DR ProteomicsDB; 298139; -.
DR MGI; MGI:1927616; Trps1.
DR eggNOG; KOG1601; Eukaryota.
DR InParanoid; Q925H1; -.
DR PhylomeDB; Q925H1; -.
DR ChiTaRS; Trps1; mouse.
DR PRO; PR:Q925H1; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q925H1; protein.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0002062; P:chondrocyte differentiation; IGI:MGI.
DR GO; GO:0001942; P:hair follicle development; IMP:CACAO.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:CACAO.
DR GO; GO:1902043; P:positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; IGI:MGI.
DR GO; GO:0032330; P:regulation of chondrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0001501; P:skeletal system development; ISO:MGI.
DR GO; GO:0007178; P:transmembrane receptor protein serine/threonine kinase signaling pathway; IGI:MGI.
DR CDD; cd00202; ZnF_GATA; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR028440; TRPS1.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR000679; Znf_GATA.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR PANTHER; PTHR47034; PTHR47034; 1.
DR Pfam; PF00320; GATA; 1.
DR PRINTS; PR00619; GATAZNFINGER.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SMART; SM00401; ZnF_GATA; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00344; GATA_ZN_FINGER_1; 1.
DR PROSITE; PS50114; GATA_ZN_FINGER_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1281
FT /note="Zinc finger transcription factor Trps1"
FT /id="PRO_0000083509"
FT ZN_FING 222..247
FT /note="C2H2-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 333..358
FT /note="C2H2-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 614..637
FT /note="C2H2-type 3; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 666..689
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 692..715
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 896..920
FT /note="GATA-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT ZN_FING 1215..1237
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1243..1267
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..819
FT /note="Mediates interaction with GLI3"
FT /evidence="ECO:0000250"
FT REGION 856..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 961..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 985..1184
FT /note="Mediates interaction with RNF4"
FT /evidence="ECO:0000269|PubMed:12885770"
FT REGION 1040..1078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1281
FT /note="Transcriptional repressor domain"
FT /evidence="ECO:0000250"
FT REGION 1169..1195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..879
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..993
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1061
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHF7"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHF7"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 978
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHF7"
FT MOD_RES 1041
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHF7"
FT MOD_RES 1066
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHF7"
FT MOD_RES 1085
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHF7"
FT CROSSLNK 29
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHF7"
FT CROSSLNK 263
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHF7"
FT CROSSLNK 418
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHF7"
FT CROSSLNK 457
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHF7"
FT CROSSLNK 474
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHF7"
FT CROSSLNK 488
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHF7"
FT CROSSLNK 645
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHF7"
FT CROSSLNK 737
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHF7"
FT CROSSLNK 755
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHF7"
FT CROSSLNK 766
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UHF7"
FT CROSSLNK 766
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UHF7"
FT CROSSLNK 825
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHF7"
FT CROSSLNK 850
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHF7"
FT CROSSLNK 877
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHF7"
FT CROSSLNK 879
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHF7"
FT CROSSLNK 925
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHF7"
FT CROSSLNK 937
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHF7"
FT CROSSLNK 965
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHF7"
FT CROSSLNK 1003
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHF7"
FT CROSSLNK 1012
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHF7"
FT CROSSLNK 1030
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHF7"
FT CROSSLNK 1040
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHF7"
FT CROSSLNK 1070
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHF7"
FT CROSSLNK 1192
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 1192
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UHF7"
FT CROSSLNK 1201
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 1201
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UHF7"
FT CROSSLNK 1201
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UHF7"
SQ SEQUENCE 1281 AA; 141035 MW; F0A71900C2357898 CRC64;
MVRKKHPPLR NVASEGEGQT LEPTATESKV SGKNKELSAD QMSENTDQSD VAELNSKEEH
STHGQEPSSS GKKDLQISGL SEKAGFNYES PSKGGSLVSF PHDEVTDRNM LAFSSPAAGG
VCEPLKSPQR AEADDPQDMA CTPSGDSLET KEEHKMSPKA TEETGPVQSG QANCQGLSPV
SVASKNPQVP SDGGVRLSKP KGDLLVNDNP DPAPLSPELQ DFKCNICGYG YYGNDPTDLI
KHFRKYHLGL HNRTRQDAEL DSKILALHNM VQFSHSKDFQ KVNRSVLSGV LQDISSSRPA
LLNGTYDVQV TSGGTFIGIG RKTPDCQGNT KYFRCKFCNF TYMGNSSTEL EQHFLQTHPN
KIKVSLPSSE GVKPSEKNSN KSIPALRASD SGDVGKWQDK MTVKAGDDTP VGYSVPIKPL
DSSRQNGTEA TSYYWCKFCS FSCESSSSLK LLEHYGKQHG AVQSGGLNPE LNDKLPRGSV
INQNDLAKSV EGEPLTKPEK GLSGAKKKDF PSKGAEDNMV TSYNCQFCDF RYSKSHGPDV
IVVGPLLRHY QQLHNIHKCT IKHCPFCPRG LCSPEKHLGE ITYPFACRKS NCSHCALLLL
HLSPGVAGSS RVKHQCHQCS FSTPDVDVLL FHYETVHESQ ASDVKQEANH LLGSDGQQAV
RDSKEHSCTK CDFITQVEEE ISRHYRRAHS CYKCRQCSFT AADTQSLLEH FNTVHCQEQE
ITTANGEEGG HAIPTIKEEP KIDLKVYSLL NPDSKMGETV PESIVKREKL DDKEGLKDKI
WTESSTDDLR GVAWRGADIL RGSPSYTQAS LGLLTPVSSS QEQTKTLRDS PNVEAAHLAR
PMYGLAVDTK GFLQGAPAGS EKSASLTQQY PASGESKTKD ESQSLLRRRR GSGVFCANCL
TTKTSLWRKN ANGGYVCNAC GLYQKLHSTP RPLNIIKQNN GEQIIRRRTR KRLNPEALQA
EQLNKQQRGS GEEQVNGSPL ERRSEDHLSE SHPREIPLPS LSKYEAQGSL TKSHSAQQPV
LVSQALDIHK RMQPLHIQIK SPQESTGDPG NSSSVSDGKG SSERGSPIEK YMRPAKHPNY
SPPGSPIEKY QYPLFGVPFV HNDFQSEADW LRFWSKYKLS VPGNPHYLSH VPGLPNPCQN
YVPYPTFNLP PHFSAVGSDN DIPLDLAIKH SRPGPTANGA SKEKTKAPPT VKNEDPLNVV
KTEKVDRSTQ DELSTKCVHC GIVFLDEVMY ALHMSCHGDS GPFQCSICQH LCTDKYDFTT
HIQRGLHRNN AQAEKNGKPK E
