TRPS1_HUMAN
ID TRPS1_HUMAN Reviewed; 1281 AA.
AC Q9UHF7; B4E1Z5; Q08AU2; Q9NWE1; Q9UHH6;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Zinc finger transcription factor Trps1;
DE AltName: Full=Tricho-rhino-phalangeal syndrome type I protein;
DE AltName: Full=Zinc finger protein GC79;
GN Name=TRPS1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=10615131; DOI=10.1038/71717;
RA Momeni P., Gloeckner G., Schmidt O., von Holtum D., Albrecht B.,
RA Gillessen-Kaesbach G., Hennekam R.C.M., Meinecke P., Zabel B.,
RA Rosenthal A., Horsthemke B., Luedecke H.-J.;
RT "Mutations in a new gene, encoding a zinc-finger protein, cause tricho-
RT rhino-phalangeal syndrome type I.";
RL Nat. Genet. 24:71-74(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Prostate;
RX PubMed=10974077; DOI=10.1093/jnci/92.17.1414;
RA Chang G.T.G., Steenbeek M., Schippers E., Blok L.J., van Weerden W.M.,
RA van Alewijk D.C.J.G., Eussen B.H.J., van Steenbrugge G.J., Brinkmann A.O.;
RT "Characterization of a zinc-finger protein and its association with
RT apoptosis in prostate cancer cells.";
RL J. Natl. Cancer Inst. 92:1414-1421(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 495-1281 (ISOFORM 1).
RC TISSUE=Embryo, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 FUNCTION, INTERACTION WITH RNF4, AND SUBCELLULAR LOCATION.
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1085, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP SUMOYLATION AT LYS-1192 AND LYS-1201, FUNCTION, AND MUTAGENESIS OF LYS-1192
RP AND LYS-1201.
RX PubMed=17391059; DOI=10.1515/bc.2007.051;
RA Kaiser F.J., Ludecke H.J., Weger S.;
RT "SUMOylation modulates transcriptional repression by TRPS1.";
RL Biol. Chem. 388:381-390(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-751; SER-1041 AND SER-1085,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
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., Buerckstuemmer T.,
RA 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-127; SER-178;
RP THR-751; SER-978; SER-1066 AND SER-1085, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-766; LYS-850 AND LYS-1201, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-766 AND LYS-1201, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-766; LYS-1003 AND LYS-1201, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-766 AND LYS-1201, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-29; LYS-76; LYS-263; LYS-418;
RP LYS-457; LYS-474; LYS-488; LYS-645; LYS-737; LYS-755; LYS-766; LYS-825;
RP LYS-850; LYS-877; LYS-879; LYS-925; LYS-937; LYS-965; LYS-1003; LYS-1012;
RP LYS-1030; LYS-1040; LYS-1070; LYS-1192 AND LYS-1201, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [19]
RP VARIANTS TRPS3 ASP-894; PRO-901; GLN-908; PRO-908 AND THR-919.
RX PubMed=11112658; DOI=10.1086/316926;
RA Luedecke H.-J., Schaper J., Meinecke P., Momeni P., Gross S.,
RA von Holtum D., Hirche H., Abramowicz M.J., Albrecht B., Apacik C.,
RA Christen H.-J., Claussen U., Devriendt K., Fastnacht E., Forderer A.,
RA Friedrich U., Goodship T.H.J., Greiwe M., Hamm H., Hennekam R.C.M.,
RA Hinkel G.K., Hoeltzenbein M., Kayserili H., Majewski F., Mathieu M.,
RA McLeod R., Midro A.T., Moog U., Nagai T., Niikawa N., Oerstavik K.H.,
RA Ploechl E., Seitz C., Schmidtke J., Tranebjaerg L., Tsukahara M.,
RA Wittwer B., Zabel B., Gillessen-Kaesbach G., Horsthemke B.;
RT "Genotypic and phenotypic spectrum in tricho-rhino-phalangeal syndrome
RT types I and III.";
RL Am. J. Hum. Genet. 68:81-91(2001).
RN [20]
RP VARIANT TRPS3 GLN-908.
RX PubMed=11807863; DOI=10.1002/ajmg.10081;
RA Kobayashi H., Hino M., Shimodahira M., Iwakura T., Ishihara T., Ikekubo K.,
RA Ogawa Y., Nakao K., Kurahachi H.;
RT "Missense mutation of TRPS1 in a family of tricho-rhino-phalangeal syndrome
RT type III.";
RL Am. J. Med. Genet. 107:26-29(2002).
RN [21]
RP VARIANTS TRPS1 CYS-952 AND HIS-952, AND CHARACTERIZATION OF VARIANTS TRPS1
RP CYS-952 AND HIS-952.
RX PubMed=14560312; DOI=10.1038/sj.ejhg.5201094;
RA Kaiser F.J., Brega P., Raff M.L., Byers P.H., Gallati S., Kay T.T.,
RA de Almeida S., Horsthemke B., Luedecke H.-J.;
RT "Novel missense mutations in the TRPS1 transcription factor define the
RT nuclear localization signal.";
RL Eur. J. Hum. Genet. 12:121-126(2004).
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:12885770, ECO:0000269|PubMed:17391059}.
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 -!- INTERACTION:
CC Q9UHF7; P78317: RNF4; NbExp=2; IntAct=EBI-2556151, EBI-2340927;
CC Q9UHF7; Q9Q2G4: ORF; Xeno; NbExp=3; IntAct=EBI-2556151, EBI-6248094;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12885770}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UHF7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UHF7-2; Sequence=VSP_037549;
CC Name=3;
CC IsoId=Q9UHF7-3; Sequence=VSP_037550;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in the adult. Found in fetal
CC brain, lung, kidney, liver, spleen and thymus. More highly expressed in
CC androgen-dependent than in androgen-independent prostate cancer cells.
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.
CC {ECO:0000269|PubMed:17391059}.
CC -!- DISEASE: Tricho-rhino-phalangeal syndrome 1 (TRPS1) [MIM:190350]:
CC Autosomal dominant disorder characterized by craniofacial and skeletal
CC abnormalities. It is allelic with tricho-rhino-phalangeal type 3.
CC Typical features include sparse scalp hair, a bulbous tip of the nose,
CC protruding ears, a long flat philtrum and a thin upper vermilion
CC border. Skeletal defects include cone-shaped epiphyses at the
CC phalanges, hip malformations and short stature.
CC {ECO:0000269|PubMed:14560312}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Tricho-rhino-phalangeal syndrome 2 (TRPS2) [MIM:150230]: A
CC syndrome that combines the clinical features of tricho-rhino-phalangeal
CC syndrome type 1 and multiple exostoses type 1. Affected individuals
CC manifest multiple dysmorphic facial features including large, laterally
CC protruding ears, a bulbous nose, an elongated upper lip, as well as
CC sparse scalp hair, winged scapulae, multiple cartilaginous exostoses,
CC redundant skin, and intellectual disability. Note=The gene represented
CC in this entry is involved in disease pathogenesis. A chromosomal
CC aberration resulting in the loss of functional copies of TRPS1 and EXT1
CC has been found in TRPS2 patients.
CC -!- DISEASE: Tricho-rhino-phalangeal syndrome 3 (TRPS3) [MIM:190351]:
CC Autosomal dominant disorder characterized by craniofacial and skeletal
CC abnormalities. It is allelic with tricho-rhino-phalangeal type 1. In
CC TRPS3 a more severe brachydactyly and growth retardation are observed.
CC {ECO:0000269|PubMed:11112658, ECO:0000269|PubMed:11807863}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI25021.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA91441.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF183810; AAF23614.1; -; mRNA.
DR EMBL; AF264784; AAG21134.1; -; mRNA.
DR EMBL; AK000948; BAA91441.1; ALT_FRAME; mRNA.
DR EMBL; AK304046; BAG64957.1; -; mRNA.
DR EMBL; AF178030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC125020; AAI25021.1; ALT_SEQ; mRNA.
DR CCDS; CCDS6318.2; -. [Q9UHF7-2]
DR CCDS; CCDS64957.1; -. [Q9UHF7-3]
DR CCDS; CCDS83316.1; -. [Q9UHF7-1]
DR RefSeq; NP_001269831.1; NM_001282902.2. [Q9UHF7-3]
DR RefSeq; NP_001269832.1; NM_001282903.2.
DR RefSeq; NP_001317528.1; NM_001330599.1. [Q9UHF7-1]
DR RefSeq; NP_054831.2; NM_014112.4. [Q9UHF7-2]
DR RefSeq; XP_006716688.1; XM_006716625.1.
DR RefSeq; XP_011515566.1; XM_011517264.1.
DR RefSeq; XP_011515568.1; XM_011517266.2.
DR RefSeq; XP_011515570.1; XM_011517268.1.
DR AlphaFoldDB; Q9UHF7; -.
DR BioGRID; 113078; 116.
DR ELM; Q9UHF7; -.
DR IntAct; Q9UHF7; 85.
DR MINT; Q9UHF7; -.
DR STRING; 9606.ENSP00000379065; -.
DR iPTMnet; Q9UHF7; -.
DR PhosphoSitePlus; Q9UHF7; -.
DR BioMuta; TRPS1; -.
DR DMDM; 20140909; -.
DR EPD; Q9UHF7; -.
DR jPOST; Q9UHF7; -.
DR MassIVE; Q9UHF7; -.
DR MaxQB; Q9UHF7; -.
DR PaxDb; Q9UHF7; -.
DR PeptideAtlas; Q9UHF7; -.
DR PRIDE; Q9UHF7; -.
DR ProteomicsDB; 84344; -. [Q9UHF7-1]
DR ProteomicsDB; 84345; -. [Q9UHF7-2]
DR ProteomicsDB; 84346; -. [Q9UHF7-3]
DR Antibodypedia; 42950; 143 antibodies from 26 providers.
DR DNASU; 7227; -.
DR Ensembl; ENST00000220888.9; ENSP00000220888.5; ENSG00000104447.13. [Q9UHF7-1]
DR Ensembl; ENST00000395715.8; ENSP00000379065.3; ENSG00000104447.13. [Q9UHF7-2]
DR Ensembl; ENST00000520276.5; ENSP00000428680.1; ENSG00000104447.13. [Q9UHF7-3]
DR Ensembl; ENST00000640765.1; ENSP00000492037.1; ENSG00000104447.13. [Q9UHF7-1]
DR GeneID; 7227; -.
DR KEGG; hsa:7227; -.
DR MANE-Select; ENST00000395715.8; ENSP00000379065.3; NM_014112.5; NP_054831.2. [Q9UHF7-2]
DR UCSC; uc003yny.5; human. [Q9UHF7-1]
DR CTD; 7227; -.
DR DisGeNET; 7227; -.
DR GeneCards; TRPS1; -.
DR GeneReviews; TRPS1; -.
DR HGNC; HGNC:12340; TRPS1.
DR HPA; ENSG00000104447; Tissue enhanced (brain, breast).
DR MalaCards; TRPS1; -.
DR MIM; 150230; phenotype.
DR MIM; 190350; phenotype.
DR MIM; 190351; phenotype.
DR MIM; 604386; gene.
DR neXtProt; NX_Q9UHF7; -.
DR OpenTargets; ENSG00000104447; -.
DR Orphanet; 77258; Trichorhinophalangeal syndrome type 1 and 3.
DR Orphanet; 502; Trichorhinophalangeal syndrome type 2.
DR PharmGKB; PA37013; -.
DR VEuPathDB; HostDB:ENSG00000104447; -.
DR eggNOG; KOG1601; Eukaryota.
DR GeneTree; ENSGT00940000157893; -.
DR InParanoid; Q9UHF7; -.
DR OMA; CEWSEGS; -.
DR OrthoDB; 120630at2759; -.
DR PhylomeDB; Q9UHF7; -.
DR TreeFam; TF350812; -.
DR PathwayCommons; Q9UHF7; -.
DR SignaLink; Q9UHF7; -.
DR SIGNOR; Q9UHF7; -.
DR BioGRID-ORCS; 7227; 30 hits in 1100 CRISPR screens.
DR ChiTaRS; TRPS1; human.
DR GeneWiki; Tricho-rhino-phalangeal_syndrome_Type_1; -.
DR GenomeRNAi; 7227; -.
DR Pharos; Q9UHF7; Tbio.
DR PRO; PR:Q9UHF7; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9UHF7; protein.
DR Bgee; ENSG00000104447; Expressed in mammary duct and 202 other tissues.
DR ExpressionAtlas; Q9UHF7; baseline and differential.
DR Genevisible; Q9UHF7; HS.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0032330; P:regulation of chondrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0001501; P:skeletal system development; IMP:UniProtKB.
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 Alternative splicing; Disease variant; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1281
FT /note="Zinc finger transcription factor Trps1"
FT /id="PRO_0000083508"
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..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..819
FT /note="Mediates interaction with GLI3"
FT /evidence="ECO:0000269|PubMed:19389374"
FT REGION 856..887
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:0000250"
FT REGION 1039..1080
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 1168..1196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..977
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 1039..1061
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q925H1"
FT MOD_RES 751
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 978
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1041
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1066
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1085
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT CROSSLNK 29
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 76
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 263
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 418
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 457
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 474
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 488
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 645
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 737
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 755
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 766
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 766
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 825
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 850
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 877
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 879
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 925
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 937
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 965
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1003
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 1012
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1030
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1040
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1070
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1192
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000269|PubMed:17391059"
FT CROSSLNK 1192
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1201
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT CROSSLNK 1201
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 1201
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1
FT /note="M -> MPYEVNAGYDFTNM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10615131"
FT /id="VSP_037549"
FT VAR_SEQ 1
FT /note="M -> MQSNM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037550"
FT VARIANT 654
FT /note="S -> L (in dbSNP:rs7002384)"
FT /id="VAR_038197"
FT VARIANT 894
FT /note="V -> D (in TRPS3; in heterozygous status has a
FT milder effect causing TRPS1)"
FT /evidence="ECO:0000269|PubMed:11112658"
FT /id="VAR_012807"
FT VARIANT 901
FT /note="T -> P (in TRPS3; severe; dbSNP:rs121908433)"
FT /evidence="ECO:0000269|PubMed:11112658"
FT /id="VAR_012808"
FT VARIANT 908
FT /note="R -> P (in TRPS3; severe)"
FT /evidence="ECO:0000269|PubMed:11112658"
FT /id="VAR_012809"
FT VARIANT 908
FT /note="R -> Q (in TRPS3; dbSNP:rs121908435)"
FT /evidence="ECO:0000269|PubMed:11112658,
FT ECO:0000269|PubMed:11807863"
FT /id="VAR_012810"
FT VARIANT 919
FT /note="A -> T (in TRPS3; dbSNP:rs1057518972)"
FT /evidence="ECO:0000269|PubMed:11112658"
FT /id="VAR_012811"
FT VARIANT 952
FT /note="R -> C (in TRPS1; prevents the transport into the
FT nucleus and thus reduces the nuclear TRPS1 concentration
FT consistent with haploinsufficiency; dbSNP:rs28939069)"
FT /evidence="ECO:0000269|PubMed:14560312"
FT /id="VAR_038198"
FT VARIANT 952
FT /note="R -> H (in TRPS1; prevents the transport into the
FT nucleus and thus reduces the nuclear TRPS1 concentration
FT consistent with haploinsufficiency; dbSNP:rs28939070)"
FT /evidence="ECO:0000269|PubMed:14560312"
FT /id="VAR_038199"
FT MUTAGEN 1192
FT /note="K->R: Very little change in sumoylation and 30%
FT reduction in repression activity. Almost complete loss of
FT sumoylation and 70% reduction in repression activity; when
FT associated with R-1201."
FT /evidence="ECO:0000269|PubMed:17391059"
FT MUTAGEN 1201
FT /note="K->R: Great loss of sumoylation and 30% reduction in
FT repression activity. Almost complete loss of sumoylation
FT and 70% reduction in repression activity; when associated
FT with R-1192."
FT /evidence="ECO:0000269|PubMed:17391059"
FT CONFLICT 115
FT /note="S -> F (in Ref. 1; AAF23614)"
FT /evidence="ECO:0000305"
FT CONFLICT 582
FT /note="T -> A (in Ref. 3; BAG64957)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1281 AA; 141521 MW; 2157B04F5BEB71CC CRC64;
MVRKKNPPLR NVASEGEGQI LEPIGTESKV SGKNKEFSAD QMSENTDQSD AAELNHKEEH
SLHVQDPSSS SKKDLKSAVL SEKAGFNYES PSKGGNFPSF PHDEVTDRNM LAFSSPAAGG
VCEPLKSPQR AEADDPQDMA CTPSGDSLET KEDQKMSPKA TEETGQAQSG QANCQGLSPV
SVASKNPQVP SDGGVRLNKS KTDLLVNDNP DPAPLSPELQ DFKCNICGYG YYGNDPTDLI
KHFRKYHLGL HNRTRQDAEL DSKILALHNM VQFSHSKDFQ KVNRSVFSGV LQDINSSRPV
LLNGTYDVQV TSGGTFIGIG RKTPDCQGNT KYFRCKFCNF TYMGNSSTEL EQHFLQTHPN
KIKASLPSSE VAKPSEKNSN KSIPALQSSD SGDLGKWQDK ITVKAGDDTP VGYSVPIKPL
DSSRQNGTEA TSYYWCKFCS FSCESSSSLK LLEHYGKQHG AVQSGGLNPE LNDKLSRGSV
INQNDLAKSS EGETMTKTDK SSSGAKKKDF SSKGAEDNMV TSYNCQFCDF RYSKSHGPDV
IVVGPLLRHY QQLHNIHKCT IKHCPFCPRG LCSPEKHLGE ITYPFACRKS NCSHCALLLL
HLSPGAAGSS RVKHQCHQCS FTTPDVDVLL FHYESVHESQ ASDVKQEANH LQGSDGQQSV
KESKEHSCTK CDFITQVEEE ISRHYRRAHS CYKCRQCSFT AADTQSLLEH FNTVHCQEQD
ITTANGEEDG HAISTIKEEP KIDFRVYNLL TPDSKMGEPV SESVVKREKL EEKDGLKEKV
WTESSSDDLR NVTWRGADIL RGSPSYTQAS LGLLTPVSGT QEQTKTLRDS PNVEAAHLAR
PIYGLAVETK GFLQGAPAGG EKSGALPQQY PASGENKSKD ESQSLLRRRR GSGVFCANCL
TTKTSLWRKN ANGGYVCNAC GLYQKLHSTP RPLNIIKQNN GEQIIRRRTR KRLNPEALQA
EQLNKQQRGS NEEQVNGSPL ERRSEDHLTE SHQREIPLPS LSKYEAQGSL TKSHSAQQPV
LVSQTLDIHK RMQPLHIQIK SPQESTGDPG NSSSVSEGKG SSERGSPIEK YMRPAKHPNY
SPPGSPIEKY QYPLFGLPFV HNDFQSEADW LRFWSKYKLS VPGNPHYLSH VPGLPNPCQN
YVPYPTFNLP PHFSAVGSDN DIPLDLAIKH SRPGPTANGA SKEKTKAPPN VKNEGPLNVV
KTEKVDRSTQ DELSTKCVHC GIVFLDEVMY ALHMSCHGDS GPFQCSICQH LCTDKYDFTT
HIQRGLHRNN AQVEKNGKPK E
