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 27-MAR-2024, entry version 200. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 131. DR ELM; Q9UHF7; -. DR IntAct; Q9UHF7; 87. DR MINT; Q9UHF7; -. DR STRING; 9606.ENSP00000379065; -. DR GlyGen; Q9UHF7; 3 sites, 1 O-linked glycan (3 sites). 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; 9606-ENSP00000379065; -. DR PeptideAtlas; Q9UHF7; -. DR ProteomicsDB; 84344; -. [Q9UHF7-1] DR ProteomicsDB; 84345; -. [Q9UHF7-2] DR ProteomicsDB; 84346; -. [Q9UHF7-3] DR Pumba; Q9UHF7; -. DR Antibodypedia; 42950; 185 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 AGR; HGNC:12340; -. DR CTD; 7227; -. DR DisGeNET; 7227; -. DR GeneCards; TRPS1; -. DR GeneReviews; TRPS1; -. DR HGNC; HGNC:12340; TRPS1. DR HPA; ENSG00000104447; Tissue enriched (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. 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; SVINHND; -. DR OrthoDB; 2948149at2759; -. DR PhylomeDB; Q9UHF7; -. DR TreeFam; TF350812; -. DR PathwayCommons; Q9UHF7; -. DR SignaLink; Q9UHF7; -. DR SIGNOR; Q9UHF7; -. DR BioGRID-ORCS; 7227; 36 hits in 1182 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 204 other cell types or tissues. DR ExpressionAtlas; Q9UHF7; baseline and differential. 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; 3.30.160.60; Classic Zinc Finger; 2. DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 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; ZINC FINGER TRANSCRIPTION FACTOR TRPS1; 1. DR PANTHER; PTHR47034:SF1; ZINC FINGER TRANSCRIPTION FACTOR TRPS1; 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; beta-beta-alpha zinc fingers; 1. DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 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. DR Genevisible; Q9UHF7; HS. 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 //