ID TRIP4_HUMAN Reviewed; 581 AA. AC Q15650; B2RAS0; Q96ED7; Q9UKH0; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 4. DT 28-JAN-2026, entry version 201. DE RecName: Full=Activating signal cointegrator 1 {ECO:0000303|PubMed:10454579}; DE Short=ASC-1 {ECO:0000303|PubMed:10454579}; DE AltName: Full=Thyroid receptor-interacting protein 4 {ECO:0000303|PubMed:7776974}; DE Short=TR-interacting protein 4 {ECO:0000303|PubMed:7776974}; DE Short=TRIP-4 {ECO:0000303|PubMed:7776974}; GN Name=TRIP4 {ECO:0000312|EMBL:AAC41738.1, ECO:0000312|HGNC:HGNC:12310}; GN Synonyms=RQT4 {ECO:0000303|PubMed:32099016}; 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], FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND RP DOMAIN. RX PubMed=10454579; DOI=10.1128/mcb.19.9.6323; RA Kim H.J., Yi J.Y., Sung H.S., Moore D.D., Jhun B.H., Lee Y.C., Lee J.W.; RT "Activating signal cointegrator 1, a novel transcription coactivator of RT nuclear receptors, and its cytosolic localization under conditions of serum RT deprivation."; RL Mol. Cell. Biol. 19:6323-6332(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 125-491. RX PubMed=7776974; DOI=10.1210/mend.9.2.7776974; RA Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.; RT "Two classes of proteins dependent on either the presence or absence of RT thyroid hormone for interaction with the thyroid hormone receptor."; RL Mol. Endocrinol. 9:243-254(1995). RN [6] RP SUBUNIT, AND DOMAIN. RX PubMed=12390891; DOI=10.1095/biolreprod.102.006155; RA Lee Y.S., Kim H.-J., Lee H.J., Lee J.W., Chun S.-Y., Ko S.-K., Lee K.; RT "Activating signal cointegrator 1 is highly expressed in murine testicular RT Leydig cells and enhances the ligand-dependent transactivation of androgen RT receptor."; RL Biol. Reprod. 67:1580-1587(2002). RN [7] RP FUNCTION, IDENTIFICATION OF THE ASC-1 COMPLEX, AND SUBCELLULAR LOCATION. RX PubMed=12077347; DOI=10.1128/mcb.22.14.5203-5211.2002; RA Jung D.-J., Sung H.-S., Goo Y.-W., Lee H.M., Park O.K., Jung S.-Y., Lim J., RA Kim H.-J., Lee S.-K., Kim T.S., Lee J.W., Lee Y.C.; RT "Novel transcription coactivator complex containing activating signal RT cointegrator 1."; RL Mol. Cell. Biol. 22:5203-5211(2002). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [11] RP SUBCELLULAR LOCATION, INTERACTION WITH NEK6, AND PHOSPHORYLATION BY NEK6. RX PubMed=20873783; DOI=10.1021/pr100562w; RA Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C., Santana Bernachi J., RA Paes Leme A.F., Kobarg J.; RT "Characterization of hNek6 interactome reveals an important role for its RT short N-terminal domain and colocalization with proteins at the RT centrosome."; RL J. Proteome Res. 9:6298-6316(2010). RN [12] RP 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 [13] 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276 AND SER-341, AND RP IDENTIFICATION BY MASS 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 [15] RP FUNCTION, INTERACTION WITH CSRP1, SUBCELLULAR LOCATION, AND INVOLVEMENT IN RP SMABF1. RX PubMed=26924529; DOI=10.1016/j.ajhg.2016.01.006; RA Knierim E., Hirata H., Wolf N.I., Morales-Gonzalez S., Schottmann G., RA Tanaka Y., Rudnik-Schoeneborn S., Orgeur M., Zerres K., Vogt S., RA van Riesen A., Gill E., Seifert F., Zwirner A., Kirschner J., Goebel H.H., RA Huebner C., Stricker S., Meierhofer D., Stenzel W., Schuelke M.; RT "Mutations in subunits of the activating signal cointegrator 1 complex are RT associated with prenatal spinal muscular atrophy and congenital bone RT fractures."; RL Am. J. Hum. Genet. 98:473-489(2016). RN [16] RP FUNCTION, INTERACTION WITH DDRGK1; EP300; ESR1; NCOA1; UFL1 AND UFSP2, RP SUBCELLULAR LOCATION, REGION, UFMYLATION AT LYS-324; LYS-325; LYS-334 AND RP LYS-367 BY UFL1, AND DEUFMYLATION BY UFSP2. RX PubMed=25219498; DOI=10.1016/j.molcel.2014.08.007; RA Yoo H.M., Kang S.H., Kim J.Y., Lee J.E., Seong M.W., Lee S.W., Ka S.H., RA Sou Y.S., Komatsu M., Tanaka K., Lee S.T., Noh D.Y., Baek S.H., Jeon Y.J., RA Chung C.H.; RT "Modification of ASC1 by UFM1 is crucial for ERalpha transactivation and RT breast cancer development."; RL Mol. Cell 56:261-274(2014). RN [17] RP INVOLVEMENT IN MDCDC. RX PubMed=27008887; DOI=10.1093/hmg/ddw033; RA Davignon L., Chauveau C., Julien C., Dill C., Duband-Goulet I., Cabet E., RA Buendia B., Lilienbaum A., Rendu J., Minot M.C., Guichet A., Allamand V., RA Vadrot N., Faure J., Odent S., Lazaro L., Leroy J.P., Marcorelles P., RA Dubourg O., Ferreiro A.; RT "The transcription coactivator ASC-1 is a regulator of skeletal myogenesis, RT and its deficiency causes a novel form of congenital muscle disease."; RL Hum. Mol. Genet. 25:1559-1573(2016). RN [18] RP INTERACTION WITH ZCCHC4. RX PubMed=31799605; DOI=10.1093/nar/gkz1147; RA Pinto R., Vaagboe C.B., Jakobsson M.E., Kim Y., Baltissen M.P., RA O'Donohue M.F., Guzman U.H., Malecki J.M., Wu J., Kirpekar F., Olsen J.V., RA Gleizes P.E., Vermeulen M., Leidel S.A., Slupphaug G., Falnes P.O.; RT "The human methyltransferase ZCCHC4 catalyses N6-methyladenosine RT modification of 28S ribosomal RNA."; RL Nucleic Acids Res. 48:830-846(2020). RN [19] RP FUNCTION, AND IDENTIFICATION IN THE RQT COMPLEX. RX PubMed=32579943; DOI=10.1016/j.molcel.2020.06.006; RA Juszkiewicz S., Speldewinde S.H., Wan L., Svejstrup J.Q., Hegde R.S.; RT "The ASC-1 complex disassembles collided ribosomes."; RL Mol. Cell 79:603-614(2020). RN [20] RP FUNCTION, AND IDENTIFICATION IN THE RQT COMPLEX. RX PubMed=32099016; DOI=10.1038/s41598-020-60241-w; RA Hashimoto S., Sugiyama T., Yamazaki R., Nobuta R., Inada T.; RT "Identification of a novel trigger complex that facilitates ribosome- RT associated quality control in mammalian cells."; RL Sci. Rep. 10:3422-3422(2020). RN [21] RP STRUCTURE BY NMR OF 435-581. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the TRIP_4C domain of target of activating signal RT cointegrator 1."; RL Submitted (DEC-2006) to the PDB data bank. RN [22] RP FUNCTION, AND IDENTIFICATION IN THE RQT COMPLEX. RX PubMed=36302773; DOI=10.1038/s41467-022-34097-9; RA Narita M., Denk T., Matsuo Y., Sugiyama T., Kikuguchi C., Ito S., Sato N., RA Suzuki T., Hashimoto S., Machova I., Tesina P., Beckmann R., Inada T.; RT "A distinct mammalian disome collision interface harbors K63-linked RT polyubiquitination of uS10 to trigger hRQT-mediated subunit dissociation."; RL Nat. Commun. 13:6411-6411(2022). CC -!- FUNCTION: Transcription coactivator which associates with nuclear CC receptors, transcriptional coactivators including EP300, CREBBP and CC NCOA1, and basal transcription factors like TBP and TFIIA to facilitate CC nuclear receptors-mediated transcription (PubMed:10454579, CC PubMed:25219498). May thereby play an important role in establishing CC distinct coactivator complexes under different cellular conditions CC (PubMed:10454579, PubMed:25219498). Plays a role in thyroid hormone CC receptor and estrogen receptor transactivation (PubMed:10454579, CC PubMed:25219498). Also involved in androgen receptor transactivation CC (By similarity). Plays a pivotal role in the transactivation of NF- CC kappa-B, SRF and AP1 (PubMed:12077347). Acts as a mediator of CC transrepression between nuclear receptor and either AP1 or NF-kappa-B CC (PubMed:12077347). May play a role in the development of neuromuscular CC junction (PubMed:26924529). May play a role in late myogenic CC differentiation (By similarity). Also functions as part of the RQC CC trigger (RQT) complex that activates the ribosome quality control (RQC) CC pathway, a pathway that degrades nascent peptide chains during CC problematic translation (PubMed:32099016, PubMed:32579943, CC PubMed:36302773). {ECO:0000250|UniProtKB:Q9QXN3, CC ECO:0000269|PubMed:10454579, ECO:0000269|PubMed:12077347, CC ECO:0000269|PubMed:25219498, ECO:0000269|PubMed:26924529, CC ECO:0000269|PubMed:32099016, ECO:0000269|PubMed:32579943, CC ECO:0000269|PubMed:36302773}. CC -!- SUBUNIT: Interacts with the thyroid hormone receptor/TR (via the CC ligand-binding domain); this interaction requires the presence of CC thyroid hormone (PubMed:10454579). Interacts with the androgen CC receptor/AR; in an androgen, testosterone and dihydrotestosterone- CC dependent manner (PubMed:12390891). Interacts with ESR1 (estrogen CC ligand-bound); competes with UFSP2 (PubMed:10454579, PubMed:25219498). CC Interacts with UFSP2; competes with ligand-bound ESR1 CC (PubMed:25219498). Interacts with DDRGK1 and UFL1; the interaction with CC DDRGK1 is direct (PubMed:25219498). Interacts with NCOA1 CC (PubMed:25219498). Interacts with EP300 (PubMed:25219498). Part of the CC ASC-1 complex, that contains TRIP4, ASCC1, ASCC2 and ASCC3 CC (PubMed:12077347). Identified in the RQT (ribosome quality control CC trigger) complex, that contains ASCC2, ASCC3 and TRIP4 CC (PubMed:32099016, PubMed:32579943, PubMed:36302773). Interacts with CC NEK6 (PubMed:20873783). Interacts with CSRP1 (PubMed:26924529). CC Interacts with ZCCHC4 (PubMed:31799605). {ECO:0000269|PubMed:10454579, CC ECO:0000269|PubMed:12077347, ECO:0000269|PubMed:12390891, CC ECO:0000269|PubMed:20873783, ECO:0000269|PubMed:25219498, CC ECO:0000269|PubMed:26924529, ECO:0000269|PubMed:31799605, CC ECO:0000269|PubMed:32099016, ECO:0000269|PubMed:32579943, CC ECO:0000269|PubMed:36302773}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10454579, CC ECO:0000269|PubMed:12077347, ECO:0000269|PubMed:20873783, CC ECO:0000269|PubMed:26924529}. Cytoplasm, cytosol CC {ECO:0000269|PubMed:10454579, ECO:0000269|PubMed:20873783}. Cytoplasm, CC cytoskeleton, microtubule organizing center, centrosome CC {ECO:0000269|PubMed:20873783}. Note=Cytoplasmic under conditions of CC serum deprivation (PubMed:10454579). Colocalizes with NEK6 in the CC centrosome (PubMed:20873783). {ECO:0000269|PubMed:10454579, CC ECO:0000269|PubMed:20873783}. CC -!- DOMAIN: The C4-type zinc finger mediates a competitive interaction with CC UFSP2 and ligand-bound nuclear receptors. It also mediates interaction CC with the transcriptional coactivators and the basal transcription CC machinery. {ECO:0000269|PubMed:10454579, ECO:0000269|PubMed:12390891, CC ECO:0000269|PubMed:25219498}. CC -!- PTM: Phosphorylated by NEK6. {ECO:0000269|PubMed:20873783}. CC -!- PTM: Polyufmylated by the UFM1-conjugating system composed of the CC enzymes UBA5, UFC1 and UFL1. Deufmylated by the protease UFSP2. CC Ufmylation of TRIP4 is promoted by ligand-bound nuclear receptors that CC compete with UFSP2 for interaction with TRIP4. Nuclear receptors- CC induced ufmylation promotes the recruitment of additional CC transcriptional coactivators like EP300 and NCOA1 and therefore the CC assembly of a coactivator complex facilitating nuclear receptor- CC mediated transcription. {ECO:0000269|PubMed:25219498}. CC -!- DISEASE: Spinal muscular atrophy with congenital bone fractures 1 CC (SMABF1) [MIM:616866]: An autosomal recessive neuromuscular disorder CC characterized by prenatal-onset spinal muscular atrophy, multiple CC congenital contractures consistent with arthrogryposis multiplex CC congenita, respiratory distress, and congenital bone fractures. CC {ECO:0000269|PubMed:26924529}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Muscular dystrophy, congenital, Davignon-Chauveau type (MDCDC) CC [MIM:617066]: An autosomal recessive, severe congenital muscular CC dystrophy characterized by neonatal onset of muscle weakness CC predominantly involving axial muscles, life-threatening respiratory CC failure, skin abnormalities and joint hyperlaxity without contractures. CC Muscle biopsies show multi-minicores, caps and dystrophic lesions. CC {ECO:0000269|PubMed:27008887}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SEQUENCE CAUTION: CC Sequence=AAC41738.1; 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; AF168418; AAF01278.1; -; mRNA. DR EMBL; AK314319; BAG36967.1; -; mRNA. DR EMBL; CH471082; EAW77685.1; -; Genomic_DNA. DR EMBL; BC012448; AAH12448.1; -; mRNA. DR EMBL; L40371; AAC41738.1; ALT_FRAME; mRNA. DR CCDS; CCDS10194.1; -. DR RefSeq; NP_001308853.1; NM_001321924.1. DR RefSeq; NP_057297.2; NM_016213.4. DR PDB; 2E5O; NMR; -; A=435-581. DR PDB; 8ALZ; EM; 3.40 A; A=1-581. DR PDB; 8YEW; X-ray; 1.90 A; A=435-581. DR PDB; 8YEY; X-ray; 2.00 A; A/C=435-581. DR PDB; 8YFI; X-ray; 2.02 A; A=435-581. DR PDB; 8YFJ; X-ray; 1.84 A; A=435-581. DR PDB; 8YXW; X-ray; 2.10 A; A/C=435-575. DR PDB; 8YXX; X-ray; 2.65 A; A/C=435-575. DR PDB; 9KYK; X-ray; 1.02 A; A=410-581. DR PDB; 9KYL; X-ray; 2.15 A; A/B=410-581. DR PDBsum; 2E5O; -. DR PDBsum; 8ALZ; -. DR PDBsum; 8YEW; -. DR PDBsum; 8YEY; -. DR PDBsum; 8YFI; -. DR PDBsum; 8YFJ; -. DR PDBsum; 8YXW; -. DR PDBsum; 8YXX; -. DR PDBsum; 9KYK; -. DR PDBsum; 9KYL; -. DR AlphaFoldDB; Q15650; -. DR EMDB; EMD-15521; -. DR SMR; Q15650; -. DR BioGRID; 114735; 213. DR ComplexPortal; CPX-6642; RQT ribosome-associated quality control trigger complex. DR CORUM; Q15650; -. DR FunCoup; Q15650; 2065. DR IntAct; Q15650; 49. DR STRING; 9606.ENSP00000261884; -. DR iPTMnet; Q15650; -. DR PhosphoSitePlus; Q15650; -. DR SwissPalm; Q15650; -. DR BioMuta; TRIP4; -. DR DMDM; 116242828; -. DR jPOST; Q15650; -. DR MassIVE; Q15650; -. DR PaxDb; 9606-ENSP00000261884; -. DR PeptideAtlas; Q15650; -. DR ProteomicsDB; 60688; -. DR Pumba; Q15650; -. DR Antibodypedia; 1761; 279 antibodies from 33 providers. DR DNASU; 9325; -. DR Ensembl; ENST00000261884.8; ENSP00000261884.3; ENSG00000103671.11. DR GeneID; 9325; -. DR KEGG; hsa:9325; -. DR MANE-Select; ENST00000261884.8; ENSP00000261884.3; NM_016213.5; NP_057297.2. DR UCSC; uc002anm.3; human. DR AGR; HGNC:12310; -. DR ClinPGx; PA36988; -. DR CTD; 9325; -. DR DisGeNET; 9325; -. DR GeneCards; TRIP4; -. DR HGNC; HGNC:12310; TRIP4. DR HPA; ENSG00000103671; Low tissue specificity. DR MalaCards; TRIP4; -. DR MIM; 604501; gene. DR MIM; 616866; phenotype. DR MIM; 617066; phenotype. DR OpenTargets; ENSG00000103671; -. DR Orphanet; 486815; Congenital muscular dystrophy-respiratory failure-skin abnormalities-joint hyperlaxity syndrome. DR Orphanet; 486811; Prenatal-onset spinal muscular atrophy with congenital bone fractures. DR VEuPathDB; HostDB:ENSG00000103671; -. DR eggNOG; KOG2845; Eukaryota. DR GeneTree; ENSGT00390000005300; -. DR HOGENOM; CLU_025737_1_0_1; -. DR InParanoid; Q15650; -. DR OMA; EFNSYRH; -. DR OrthoDB; 338816at2759; -. DR PAN-GO; Q15650; 3 GO annotations based on evolutionary models. DR PhylomeDB; Q15650; -. DR PathwayCommons; Q15650; -. DR SignaLink; Q15650; -. DR Agora; ENSG00000103671; -. DR BioGRID-ORCS; 9325; 16 hits in 1159 CRISPR screens. DR ChiTaRS; TRIP4; human. DR EvolutionaryTrace; Q15650; -. DR GeneWiki; TRIP4; -. DR GenomeRNAi; 9325; -. DR Pharos; Q15650; Tbio. DR PRO; PR:Q15650; -. DR Proteomes; UP000005640; Chromosome 15. DR RNAct; Q15650; protein. DR Bgee; ENSG00000103671; Expressed in sural nerve and 193 other cell types or tissues. DR ExpressionAtlas; Q15650; baseline and differential. DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0031594; C:neuromuscular junction; IMP:UniProtKB. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0180022; C:RQC-trigger complex; IDA:UniProtKB. DR GO; GO:0035035; F:histone acetyltransferase binding; IPI:UniProtKB. DR GO; GO:0030331; F:nuclear estrogen receptor binding; IPI:UniProtKB. DR GO; GO:0016922; F:nuclear receptor binding; IDA:UniProtKB. DR GO; GO:0002020; F:protease binding; IPI:UniProtKB. DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB. DR GO; GO:0003713; F:transcription coactivator activity; IMP:UniProtKB. DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; IPI:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0030520; P:estrogen receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IMP:UniProtKB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0045661; P:regulation of myoblast differentiation; ISS:UniProtKB. DR GO; GO:0072344; P:rescue of stalled ribosome; IDA:UniProtKB. DR GO; GO:0032790; P:ribosome disassembly; IDA:UniProtKB. DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; IMP:UniProtKB. DR CDD; cd06554; ASCH_ASC-1_like; 1. DR FunFam; 2.30.130.30:FF:000004; Activating signal cointegrator 1; 1. DR Gene3D; 2.30.130.30; Hypothetical protein; 1. DR InterPro; IPR007374; ASCH_domain. DR InterPro; IPR015947; PUA-like_sf. DR InterPro; IPR056994; TRI4_N. DR InterPro; IPR039128; TRIP4-like. DR InterPro; IPR009349; TRIP4/RQT4_C2HC5_Znf. DR InterPro; IPR056993; TRIP4_3rd_dom. DR PANTHER; PTHR12963:SF4; ACTIVATING SIGNAL COINTEGRATOR 1; 1. DR PANTHER; PTHR12963; THYROID RECEPTOR INTERACTING PROTEIN RELATED; 1. DR Pfam; PF04266; ASCH; 1. DR Pfam; PF23135; TRI4_N; 1. DR Pfam; PF23134; TRIP4_3rd; 1. DR Pfam; PF06221; zf-C2HC5; 1. DR SMART; SM01022; ASCH; 1. DR SUPFAM; SSF88697; PUA domain-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Congenital muscular dystrophy; Cytoplasm; KW Cytoskeleton; Isopeptide bond; Metal-binding; Neurodegeneration; Nucleus; KW Phosphoprotein; Proteomics identification; Reference proteome; KW Transcription; Transcription regulation; Ubl conjugation; Zinc; KW Zinc-finger. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330" FT CHAIN 2..581 FT /note="Activating signal cointegrator 1" FT /id="PRO_0000065631" FT DOMAIN 437..531 FT /note="ASCH" FT /evidence="ECO:0000255" FT ZN_FING 171..187 FT /note="C4-type" FT REGION 97..118 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 200..300 FT /note="Mediates interaction with DDRGK1" FT /evidence="ECO:0000269|PubMed:25219498" FT REGION 300..400 FT /note="Mediates interaction with UFL1" FT /evidence="ECO:0000269|PubMed:25219498" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330" FT MOD_RES 276 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 289 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q9QXN3" FT MOD_RES 341 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 324 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in UFM1)" FT /evidence="ECO:0000305|PubMed:25219498" FT CROSSLNK 325 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in UFM1)" FT /evidence="ECO:0000305|PubMed:25219498" FT CROSSLNK 334 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in UFM1)" FT /evidence="ECO:0000305|PubMed:25219498" FT CROSSLNK 367 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in UFM1)" FT /evidence="ECO:0000305|PubMed:25219498" FT CONFLICT 157 FT /note="G -> R (in Ref. 1; AAF01278 and 5; AAC41738)" FT /evidence="ECO:0000305" FT CONFLICT 164 FT /note="L -> A (in Ref. 1; AAF01278)" FT /evidence="ECO:0000305" FT CONFLICT 475 FT /note="K -> N (in Ref. 5; AAC41738)" FT /evidence="ECO:0000305" FT STRAND 176..178 FT /evidence="ECO:0007829|PDB:8ALZ" FT TURN 185..187 FT /evidence="ECO:0007829|PDB:8ALZ" FT STRAND 197..199 FT /evidence="ECO:0007829|PDB:8ALZ" FT TURN 201..203 FT /evidence="ECO:0007829|PDB:8ALZ" FT HELIX 210..218 FT /evidence="ECO:0007829|PDB:8ALZ" FT HELIX 396..404 FT /evidence="ECO:0007829|PDB:8ALZ" FT HELIX 425..428 FT /evidence="ECO:0007829|PDB:8ALZ" FT STRAND 435..439 FT /evidence="ECO:0007829|PDB:8YFJ" FT HELIX 443..448 FT /evidence="ECO:0007829|PDB:8YFJ" FT STRAND 454..459 FT /evidence="ECO:0007829|PDB:8YFJ" FT STRAND 465..471 FT /evidence="ECO:0007829|PDB:8YFJ" FT HELIX 478..492 FT /evidence="ECO:0007829|PDB:8YFJ" FT STRAND 504..518 FT /evidence="ECO:0007829|PDB:8YFJ" FT HELIX 519..525 FT /evidence="ECO:0007829|PDB:8YFJ" FT TURN 527..529 FT /evidence="ECO:0007829|PDB:8YFJ" FT HELIX 530..532 FT /evidence="ECO:0007829|PDB:8YFJ" FT STRAND 535..552 FT /evidence="ECO:0007829|PDB:8YFJ" FT STRAND 557..561 FT /evidence="ECO:0007829|PDB:8YFJ" FT HELIX 564..574 FT /evidence="ECO:0007829|PDB:8YFJ" FT HELIX 576..578 FT /evidence="ECO:0007829|PDB:8YEW" SQ SEQUENCE 581 AA; 66146 MW; DADD3994533A808E CRC64; MAVAGAVSGE PLVHWCTQQL RKTFGLDVSE EIIQYVLSIE SAEEIREYVT DLLQGNEGKK GQFIEELITK WQKNDQELIS DPLQQCFKKD EILDGQKSGD HLKRGRKKGR NRQEVPAFTE PDTTAEVKTP FDLAKAQENS NSVKKKTKFV NLYTREGQDR LAVLLPGRHP CDCLGQKHKL INNCLICGRI VCEQEGSGPC LFCGTLVCTH EEQDILQRDS NKSQKLLKKL MSGVENSGKV DISTKDLLPH QELRIKSGLE KAIKHKDKLL EFDRTSIRRT QVIDDESDYF ASDSNQWLSK LERETLQKRE EELRELRHAS RLSKKVTIDF AGRKILEEEN SLAEYHSRLD ETIQAIANGT LNQPLTKLDR SSEEPLGVLV NPNMYQSPPQ WVDHTGAASQ KKAFRSSGFG LEFNSFQHQL RIQDQEFQEG FDGGWCLSVH QPWASLLVRG IKRVEGRSWY TPHRGRLWIA ATAKKPSPQE VSELQATYRL LRGKDVEFPN DYPSGCLLGC VDLIDCLSQK QFKEQFPDIS QESDSPFVFI CKNPQEMVVK FPIKGNPKIW KLDSKIHQGA KKGLMKQNKA V //