TRIP4_HUMAN
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 03-AUG-2022, entry version 184.
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, IDENTIFICATION IN THE RQT COMPLEX, AND INTERACTION WITH ASCC2 AND
RP ASCC3.
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 [20]
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.
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. May thereby play an important
CC role in establishing distinct coactivator complexes under different
CC cellular conditions. Plays a role in thyroid hormone receptor and
CC estrogen receptor transactivation (PubMed:10454579, PubMed:25219498).
CC Also involved in androgen receptor transactivation (By similarity).
CC Plays a pivotal role in the transactivation of NF-kappa-B, SRF and AP1.
CC Acts as a mediator of transrepression between nuclear receptor and
CC either AP1 or NF-kappa-B (PubMed:12077347). May play a role in the
CC development of neuromuscular junction (PubMed:26924529). May play a
CC role in late myogenic differentiation (By similarity). Also functions
CC as part of the RQC trigger (RQT) complex that activates the ribosome
CC quality control (RQC) pathway, a pathway that degrades nascent peptide
CC chains during problematic translation (PubMed:32099016).
CC {ECO:0000250|UniProtKB:Q9QXN3, ECO:0000269|PubMed:10454579,
CC ECO:0000269|PubMed:12077347, ECO:0000269|PubMed:25219498,
CC ECO:0000269|PubMed:26924529, ECO:0000269|PubMed:32099016}.
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). Interacts with ASCC2 (PubMed:32099016). Interacts
CC with ASCC3 (PubMed:32099016). Interacts with NEK6 (PubMed:20873783).
CC Interacts with CSRP1 (PubMed:26924529). Interacts with ZCCHC4
CC (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}.
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 PDBsum; 2E5O; -.
DR AlphaFoldDB; Q15650; -.
DR SMR; Q15650; -.
DR BioGRID; 114735; 190.
DR ComplexPortal; CPX-6642; RQT ribosome-associated quality control trigger complex.
DR CORUM; Q15650; -.
DR IntAct; Q15650; 21.
DR STRING; 9606.ENSP00000261884; -.
DR iPTMnet; Q15650; -.
DR PhosphoSitePlus; Q15650; -.
DR SwissPalm; Q15650; -.
DR BioMuta; TRIP4; -.
DR DMDM; 116242828; -.
DR EPD; Q15650; -.
DR jPOST; Q15650; -.
DR MassIVE; Q15650; -.
DR MaxQB; Q15650; -.
DR PaxDb; Q15650; -.
DR PeptideAtlas; Q15650; -.
DR PRIDE; Q15650; -.
DR ProteomicsDB; 60688; -.
DR Antibodypedia; 1761; 296 antibodies from 32 providers.
DR DNASU; 9325; -.
DR Ensembl; ENST00000261884.8; ENSP00000261884.3; ENSG00000103671.10.
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 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 neXtProt; NX_Q15650; -.
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 PharmGKB; PA36988; -.
DR VEuPathDB; HostDB:ENSG00000103671; -.
DR eggNOG; KOG2845; Eukaryota.
DR GeneTree; ENSGT00390000005300; -.
DR HOGENOM; CLU_025737_1_0_1; -.
DR InParanoid; Q15650; -.
DR OMA; CVDVTDC; -.
DR OrthoDB; 1132270at2759; -.
DR PhylomeDB; Q15650; -.
DR TreeFam; TF314842; -.
DR PathwayCommons; Q15650; -.
DR SignaLink; Q15650; -.
DR BioGRID-ORCS; 9325; 15 hits in 1081 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 191 other tissues.
DR ExpressionAtlas; Q15650; baseline and differential.
DR Genevisible; Q15650; HS.
DR GO; GO:0099053; C:activating signal cointegrator 1 complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005815; C:microtubule organizing center; 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: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:InterPro.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0045661; P:regulation of myoblast differentiation; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0072344; P:rescue of stalled ribosome; IMP:UniProtKB.
DR GO; GO:0032790; P:ribosome disassembly; IC:ComplexPortal.
DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:1901998; P:toxin transport; IEA:Ensembl.
DR InterPro; IPR007374; ASCH_domain.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR039128; TRIP4-like.
DR InterPro; IPR009349; Znf_C2HC5.
DR PANTHER; PTHR12963; PTHR12963; 1.
DR Pfam; PF04266; ASCH; 1.
DR Pfam; PF06221; zf-C2HC5; 1.
DR SMART; SM01022; ASCH; 1.
DR SUPFAM; SSF88697; SSF88697; 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; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; 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 435..439
FT /evidence="ECO:0007829|PDB:2E5O"
FT HELIX 443..448
FT /evidence="ECO:0007829|PDB:2E5O"
FT STRAND 454..459
FT /evidence="ECO:0007829|PDB:2E5O"
FT STRAND 465..471
FT /evidence="ECO:0007829|PDB:2E5O"
FT HELIX 478..492
FT /evidence="ECO:0007829|PDB:2E5O"
FT STRAND 504..518
FT /evidence="ECO:0007829|PDB:2E5O"
FT HELIX 521..525
FT /evidence="ECO:0007829|PDB:2E5O"
FT TURN 530..532
FT /evidence="ECO:0007829|PDB:2E5O"
FT STRAND 535..546
FT /evidence="ECO:0007829|PDB:2E5O"
FT STRAND 557..561
FT /evidence="ECO:0007829|PDB:2E5O"
FT HELIX 564..572
FT /evidence="ECO:0007829|PDB:2E5O"
FT HELIX 573..575
FT /evidence="ECO:0007829|PDB:2E5O"
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
