ID CUX1_HUMAN Reviewed; 1505 AA. AC P39880; B3KV79; J3KQV9; Q6NYH4; Q75LE5; Q75MT2; Q75MT3; Q86UJ7; Q9UEV5; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 3. DT 27-MAR-2024, entry version 210. DE RecName: Full=Homeobox protein cut-like 1 {ECO:0000305}; DE AltName: Full=CCAAT displacement protein; DE Short=CDP; DE AltName: Full=CDP/Cux p200 {ECO:0000303|PubMed:15099520}; DE AltName: Full=Homeobox protein cux-1; DE Contains: DE RecName: Full=CDP/Cux p110 {ECO:0000303|PubMed:15099520}; GN Name=CUX1 {ECO:0000312|HGNC:HGNC:2557}; Synonyms=CUTL1; 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] (ISOFORMS 1 AND 2). RC TISSUE=Umbilical vein; RX PubMed=1301999; DOI=10.1038/ng0492-50; RA Neufeld E.J., Skalnik D.G., Lievens P.M.-J., Orkin S.H.; RT "Human CCAAT displacement protein is homologous to the Drosophila RT homeoprotein, cut."; RL Nat. Genet. 1:50-55(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 11). RC TISSUE=Brain; 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]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Duodenum; 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 [GENOMIC DNA] OF 48-224 (ISOFORMS 1/2/3). RX PubMed=9799793; DOI=10.1101/gr.8.10.1060; RA Gloeckner G., Scherer S., Schattevoy R., Boright A.P., Weber J., RA Tsui L.-C., Rosenthal A.; RT "Large-scale sequencing of two regions in human chromosome 7q22: analysis RT of 650 kb of genomic sequence around the EPO and CUTL1 loci reveals 17 RT genes."; RL Genome Res. 8:1060-1073(1998). RN [6] RP ALTERNATIVE SPLICING (ISOFORMS 5; 6 AND 7). RX PubMed=10607901; DOI=10.1016/s0378-1119(99)00465-5; RA Rong Zeng W., Soucie E., Sung Moon N., Martin-Soudant N., Berube G., RA Leduy L., Nepveu A.; RT "Exon/intron structure and alternative transcripts of the CUTL1 gene."; RL Gene 241:75-85(2000). RN [7] RP FUNCTION, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, AND DNA-BINDING. RX PubMed=15099520; DOI=10.1016/s1097-2765(04)00209-6; RA Goulet B., Baruch A., Moon N.S., Poirier M., Sansregret L.L., Erickson A., RA Bogyo M., Nepveu A.; RT "A cathepsin L isoform that is devoid of a signal peptide localizes to the RT nucleus in S phase and processes the CDP/Cux transcription factor."; RL Mol. Cell 14:207-219(2004). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). 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 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 [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-763, AND IDENTIFICATION BY RP 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-1059; SER-1270; SER-1455 AND RP SER-1486, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540 (ISOFORM 11), RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-811, AND IDENTIFICATION BY MASS RP 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 [16] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-785, AND IDENTIFICATION BY MASS RP 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 [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [18] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-785; LYS-811; LYS-842 AND RP LYS-1284, AND IDENTIFICATION BY 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 INVOLVEMENT IN GDDI, AND VARIANT GDDI 862-GLN--PHE-1505 DEL. RX PubMed=30014507; DOI=10.1002/ana.25278; RA Platzer K., Cogne B., Hague J., Marcelis C.L., Mitter D., Oberndorff K., RA Park S.M., Ploos van Amstel H.K., Simonic I., van der Smagt J.J., RA Stegmann A.P.A., Stevens S.J.C., Stumpel C.T.R.M., Vincent M., Lemke J.R., RA Jamra R.; RT "Haploinsufficiency of CUX1 causes nonsyndromic global developmental delay RT with possible catch-up development."; RL Ann. Neurol. 84:200-207(2018). CC -!- FUNCTION: Transcription factor involved in the control of neuronal CC differentiation in the brain. Regulates dendrite development and CC branching, and dendritic spine formation in cortical layers II-III. CC Also involved in the control of synaptogenesis. In addition, it has CC probably a broad role in mammalian development as a repressor of CC developmentally regulated gene expression. May act by preventing CC binding of positively-activing CCAAT factors to promoters. Component of CC nf-munr repressor; binds to the matrix attachment regions (MARs) (5' CC and 3') of the immunoglobulin heavy chain enhancer. Represses T-cell CC receptor (TCR) beta enhancer function by binding to MARbeta, an ATC- CC rich DNA sequence located upstream of the TCR beta enhancer. Binds to CC the TH enhancer; may require the basic helix-loop-helix protein TCF4 as CC a coactivator. {ECO:0000250|UniProtKB:P53564}. CC -!- FUNCTION: [CDP/Cux p110]: Plays a role in cell cycle progression, in CC particular at the G1/S transition. As cells progress into S phase, a CC fraction of CUX1 molecules is proteolytically processed into N- CC terminally truncated proteins of 110 kDa. While CUX1 only transiently CC binds to DNA and carries the CCAAT-displacement activity, CDP/Cux p110 CC makes a stable interaction with DNA and stimulates expression of genes CC such as POLA1. {ECO:0000269|PubMed:15099520}. CC -!- SUBUNIT: Interacts with BANP. Interacts with SATB1 (via DNA-binding CC domains); the interaction inhibits the attachment of both proteins to CC DNA (By similarity). {ECO:0000250|UniProtKB:P53564}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15099520}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=11; CC Comment=Additional isoforms seem to exist.; CC Name=1; CC IsoId=P39880-1; Sequence=Displayed; CC Name=2; CC IsoId=P39880-2; Sequence=VSP_002310; CC Name=3; CC IsoId=P39880-3; Sequence=VSP_015747; CC Name=5; CC IsoId=P39880-4; Sequence=VSP_017358; CC Name=6; CC IsoId=P39880-5; Sequence=VSP_017359; CC Name=7; CC IsoId=P39880-6; Sequence=VSP_017358, VSP_017359; CC Name=11; CC IsoId=P39880-9; Sequence=VSP_015747, VSP_045924, VSP_045925, CC VSP_045926; CC Name=4; Synonyms=CASP; CC IsoId=Q13948-1; Sequence=External; CC Name=8; CC IsoId=Q13948-2; Sequence=External; CC Name=9; CC IsoId=Q13948-9; Sequence=External; CC Name=10; CC IsoId=Q13948-10; Sequence=External; CC -!- PTM: Phosphorylated by PKA. {ECO:0000250|UniProtKB:P53565}. CC -!- PTM: As cells progress into S phase, a fraction of CUX1 molecules is CC proteolytically processed into N-terminally truncated proteins of 110 CC kDa by CTSL. Cell cycle-dependent processing of CUX1 serves to generate CC a CDP/Cux p110 with distinct DNA binding and transcriptional CC properties. {ECO:0000269|PubMed:15099520}. CC -!- DISEASE: Global developmental delay with or without impaired CC intellectual development (GDDI) [MIM:618330]: An autosomal dominant CC disorder characterized by global developmental delay associated with CC mild-to-moderate intellectual disability, hypotonia and short stature CC in some patients. {ECO:0000269|PubMed:30014507}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC -!- MISCELLANEOUS: Asn-1290 may participate in regulating DNA-binding CC activity by promoting homo- and heterodimerization. CC -!- SIMILARITY: Belongs to the CUT homeobox family. {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; M74099; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK122726; BAG53691.1; -; mRNA. DR EMBL; AC005072; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC005086; AAP22331.1; -; Genomic_DNA. DR EMBL; AC005088; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC005096; AAS07410.1; -; Genomic_DNA. DR EMBL; AC005103; AAS07388.1; -; Genomic_DNA. DR EMBL; AC092788; AAS07523.1; -; Genomic_DNA. DR EMBL; BC066592; AAH66592.1; -; mRNA. DR EMBL; AF047825; AAC78778.1; -; Genomic_DNA. DR CCDS; CCDS56498.1; -. [P39880-3] DR CCDS; CCDS56499.1; -. [P39880-9] DR CCDS; CCDS5721.1; -. [P39880-1] DR RefSeq; NP_001189472.1; NM_001202543.1. [P39880-3] DR RefSeq; NP_001189473.1; NM_001202544.2. DR RefSeq; NP_001189474.1; NM_001202545.2. [P39880-9] DR RefSeq; NP_852477.1; NM_181500.3. DR RefSeq; NP_853530.2; NM_181552.3. [P39880-1] DR AlphaFoldDB; P39880; -. DR SMR; P39880; -. DR BioGRID; 107903; 209. DR ELM; P39880; -. DR IntAct; P39880; 64. DR MINT; P39880; -. DR STRING; 9606.ENSP00000353401; -. DR GlyCosmos; P39880; 1 site, 1 glycan. DR GlyGen; P39880; 5 sites, 1 O-linked glycan (5 sites). DR iPTMnet; P39880; -. DR MetOSite; P39880; -. DR PhosphoSitePlus; P39880; -. DR BioMuta; CUX1; -. DR EPD; P39880; -. DR jPOST; P39880; -. DR MassIVE; P39880; -. DR PaxDb; 9606-ENSP00000353401; -. DR PeptideAtlas; P39880; -. DR ProteomicsDB; 55321; -. [P39880-1] DR ProteomicsDB; 55322; -. [P39880-2] DR ProteomicsDB; 55323; -. [P39880-3] DR ProteomicsDB; 55324; -. [P39880-4] DR ProteomicsDB; 55325; -. [P39880-5] DR ProteomicsDB; 55326; -. [P39880-6] DR Pumba; P39880; -. DR Antibodypedia; 48390; 504 antibodies from 35 providers. DR DNASU; 1523; -. DR Ensembl; ENST00000292535.12; ENSP00000292535.7; ENSG00000257923.12. [P39880-1] DR Ensembl; ENST00000360264.7; ENSP00000353401.3; ENSG00000257923.12. [P39880-3] DR Ensembl; ENST00000425244.6; ENSP00000409745.2; ENSG00000257923.12. [P39880-9] DR Ensembl; ENST00000546411.7; ENSP00000450125.3; ENSG00000257923.12. [P39880-1] DR Ensembl; ENST00000549414.6; ENSP00000446630.2; ENSG00000257923.12. [P39880-2] DR Ensembl; ENST00000550008.6; ENSP00000447373.2; ENSG00000257923.12. [P39880-5] DR Ensembl; ENST00000556210.1; ENSP00000451558.1; ENSG00000257923.12. [P39880-6] DR GeneID; 1523; -. DR MANE-Select; ENST00000292535.12; ENSP00000292535.7; NM_181552.4; NP_853530.2. DR UCSC; uc003uys.5; human. [P39880-1] DR AGR; HGNC:2557; -. DR CTD; 1523; -. DR DisGeNET; 1523; -. DR GeneCards; CUX1; -. DR HGNC; HGNC:2557; CUX1. DR HPA; ENSG00000257923; Low tissue specificity. DR MalaCards; CUX1; -. DR MIM; 116896; gene. DR MIM; 618330; phenotype. DR neXtProt; NX_P39880; -. DR OpenTargets; ENSG00000257923; -. DR Orphanet; 178469; Autosomal dominant non-syndromic intellectual disability. DR PharmGKB; PA162382924; -. DR VEuPathDB; HostDB:ENSG00000257923; -. DR eggNOG; KOG0963; Eukaryota. DR eggNOG; KOG2252; Eukaryota. DR GeneTree; ENSGT00940000159751; -. DR HOGENOM; CLU_016758_0_0_1; -. DR InParanoid; P39880; -. DR OMA; LESKPYH; -. DR OrthoDB; 74668at2759; -. DR PhylomeDB; P39880; -. DR TreeFam; TF318206; -. DR PathwayCommons; P39880; -. DR Reactome; R-HSA-1839117; Signaling by cytosolic FGFR1 fusion mutants. DR Reactome; R-HSA-5655302; Signaling by FGFR1 in disease. DR SignaLink; P39880; -. DR SIGNOR; P39880; -. DR BioGRID-ORCS; 1523; 26 hits in 1205 CRISPR screens. DR ChiTaRS; CUX1; human. DR GeneWiki; CUTL1; -. DR GenomeRNAi; 1523; -. DR Pharos; P39880; Tbio. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; P39880; Protein. DR Bgee; ENSG00000257923; Expressed in secondary oocyte and 208 other cell types or tissues. DR ExpressionAtlas; P39880; baseline and differential. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISS:CAFA. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:ProtInc. DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; ISS:CAFA. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd00086; homeodomain; 1. DR Gene3D; 1.10.10.60; Homeodomain-like; 1. DR Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 3. DR InterPro; IPR003350; CUT_dom. DR InterPro; IPR009057; Homeobox-like_sf. DR InterPro; IPR017970; Homeobox_CS. DR InterPro; IPR001356; Homeobox_dom. DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf. DR PANTHER; PTHR14043; CCAAT DISPLACEMENT PROTEIN-RELATED; 1. DR PANTHER; PTHR14043:SF4; HOMEOBOX PROTEIN CUT-LIKE 1; 1. DR Pfam; PF02376; CUT; 3. DR Pfam; PF00046; Homeodomain; 1. DR SMART; SM01109; CUT; 3. DR SMART; SM00389; HOX; 1. DR SUPFAM; SSF46689; Homeodomain-like; 1. DR SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 3. DR PROSITE; PS51042; CUT; 3. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR Genevisible; P39880; HS. PE 1: Evidence at protein level; KW Alternative splicing; Coiled coil; Developmental protein; Disease variant; KW DNA-binding; Homeobox; Intellectual disability; Isopeptide bond; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1..1505 FT /note="Homeobox protein cut-like 1" FT /id="PRO_0000202393" FT CHAIN 756..1505 FT /note="CDP/Cux p110" FT /evidence="ECO:0000303|PubMed:15099520" FT /id="PRO_0000450797" FT DNA_BIND 542..629 FT /note="CUT 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00374" FT DNA_BIND 934..1021 FT /note="CUT 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00374" FT DNA_BIND 1117..1204 FT /note="CUT 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00374" FT DNA_BIND 1244..1303 FT /note="Homeobox" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108" FT REGION 396..455 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 512..552 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 646..669 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 682..704 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 768..802 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 815..930 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1036..1110 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1210..1247 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1312..1480 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 56..407 FT /evidence="ECO:0000255" FT COMPBIAS 437..455 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 512..546 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 650..664 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 687..704 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 835..849 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 861..910 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 911..929 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1036..1073 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1083..1102 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1219..1241 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1312..1330 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1355..1370 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1440..1455 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 643..644 FT /note="Cleavage; by CTSL" FT /evidence="ECO:0000269|PubMed:15099520" FT SITE 747..755 FT /note="Cleavage; by CTSL" FT /evidence="ECO:0000269|PubMed:15099520" FT MOD_RES 763 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 909 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P53565" FT MOD_RES 1059 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1069 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P53565" FT MOD_RES 1270 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1337 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P53564" FT MOD_RES 1455 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1486 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1496 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P53564" FT CROSSLNK 785 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 811 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 842 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1284 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..10 FT /note="MLCVAGARLK -> MAANVGSMFQYWKRFDLQQLQ (in isoform 3 FT and isoform 11)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_015747" FT VAR_SEQ 90..135 FT /note="Missing (in isoform 11)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045924" FT VAR_SEQ 408..509 FT /note="Missing (in isoform 5 and isoform 7)" FT /evidence="ECO:0000305" FT /id="VSP_017358" FT VAR_SEQ 409..667 FT /note="SARRKGKDQPESRRPGSLPAPPPSQLPRNPGEQASNTNGTHQFSPAGLSQDF FT FSSSLASPSLPLASTGKFALNSLLQRQLMQSFYSKAMQEAGSTSMIFSTGPYSTNSISS FT QSPLQQSPDVNGMAPSPSQSESAGSVSEGEEMDTAEIARQVKEQLIKHNIGQRIFGHYV FT LGLSQGSVSEILARPKPWNKLTVRGKEPFHKMKQFLSDEQNILALRSIQGRQRENPGQS FT LNRLFQEVPKRRNGSEGNITTRIRASETGS -> RCAELQVRITEAVATATEQRELIAR FT LEQDLSIIQSIQRPDAEGAAEHRLEKIPEPIKEATALFYGPAAPASGALPEGQVDSLLS FT IISSQRERFRARNQELEAENRLAQHTLQALQSELDSLRADNIKLFEKIKFLQSYPGRGS FT GSDDTELRYSSQYEERLDPFSSFSKRERQRKYLSLSPWDKATLSMGRLVLSNKMARTIG FT FFYTLFLHCLVFLVLYKLAWSESMERDCATFCAKKFADHLHKFHENDNGAAAGDLWQ FT (in isoform 11)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045925" FT VAR_SEQ 632..687 FT /note="Missing (in isoform 6 and isoform 7)" FT /evidence="ECO:0000305" FT /id="VSP_017359" FT VAR_SEQ 632..653 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:1301999" FT /id="VSP_002310" FT VAR_SEQ 668..1505 FT /note="Missing (in isoform 11)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045926" FT VARIANT 862..1505 FT /note="Missing (in GDDI)" FT /evidence="ECO:0000269|PubMed:30014507" FT /id="VAR_081977" FT CONFLICT 5 FT /note="A -> R (in Ref. 1; M74099)" FT /evidence="ECO:0000305" FT CONFLICT 145 FT /note="K -> I (in Ref. 2; BAG53691)" FT /evidence="ECO:0000305" FT CONFLICT 260 FT /note="A -> V (in Ref. 2; BAG53691)" FT /evidence="ECO:0000305" FT CONFLICT 704..705 FT /note="DA -> EP (in Ref. 1; M74099)" FT /evidence="ECO:0000305" FT CONFLICT 844 FT /note="E -> R (in Ref. 1; M74099)" FT /evidence="ECO:0000305" FT CONFLICT 1436 FT /note="S -> T (in Ref. 1; M74099)" FT /evidence="ECO:0000305" FT MOD_RES P39880-9:540 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" SQ SEQUENCE 1505 AA; 164187 MW; 0F9027E5B8F08D95 CRC64; MLCVAGARLK RELDATATVL ANRQDESEQS RKRLIEQSRE FKKNTPEDLR KQVAPLLKSF QGEIDALSKR SKEAEAAFLN VYKRLIDVPD PVPALDLGQQ LQLKVQRLHD IETENQKLRE TLEEYNKEFA EVKNQEVTIK ALKEKIREYE QTLKNQAETI ALEKEQKLQN DFAEKERKLQ ETQMSTTSKL EEAEHKVQSL QTALEKTRTE LFDLKTKYDE ETTAKADEIE MIMTDLERAN QRAEVAQREA ETLREQLSSA NHSLQLASQI QKAPDVEQAI EVLTRSSLEV ELAAKEREIA QLVEDVQRLQ ASLTKLRENS ASQISQLEQQ LSAKNSTLKQ LEEKLKGQAD YEEVKKELNI LKSMEFAPSE GAGTQDAAKP LEVLLLEKNR SLQSENAALR ISNSDLSGSA RRKGKDQPES RRPGSLPAPP PSQLPRNPGE QASNTNGTHQ FSPAGLSQDF FSSSLASPSL PLASTGKFAL NSLLQRQLMQ SFYSKAMQEA GSTSMIFSTG PYSTNSISSQ SPLQQSPDVN GMAPSPSQSE SAGSVSEGEE MDTAEIARQV KEQLIKHNIG QRIFGHYVLG LSQGSVSEIL ARPKPWNKLT VRGKEPFHKM KQFLSDEQNI LALRSIQGRQ RENPGQSLNR LFQEVPKRRN GSEGNITTRI RASETGSDEA IKSILEQAKR ELQVQKTAEP AQPSSASGSG NSDDAIRSIL QQARREMEAQ QAALDPALKQ APLSQSDITI LTPKLLSTSP MPTVSSYPPL AISLKKPSAA PEAGASALPN PPALKKEAQD APGLDPQGAA DCAQGVLRQV KNEVGRSGAW KDHWWSAVQP ERRNAASSEE AKAEETGGGK EKGSGGSGGG SQPRAERSQL QGPSSSEYWK EWPSAESPYS QSSELSLTGA SRSETPQNSP LPSSPIVPMS KPTKPSVPPL TPEQYEVYMY QEVDTIELTR QVKEKLAKNG ICQRIFGEKV LGLSQGSVSD MLSRPKPWSK LTQKGREPFI RMQLWLNGEL GQGVLPVQGQ QQGPVLHSVT SLQDPLQQGC VSSESTPKTS ASCSPAPESP MSSSESVKSL TELVQQPCPP IEASKDSKPP EPSDPPASDS QPTTPLPLSG HSALSIQELV AMSPELDTYG ITKRVKEVLT DNNLGQRLFG ETILGLTQGS VSDLLARPKP WHKLSLKGRE PFVRMQLWLN DPNNVEKLMD MKRMEKKAYM KRRHSSVSDS QPCEPPSVGT EYSQGASPQP QHQLKKPRVV LAPEEKEALK RAYQQKPYPS PKTIEDLATQ LNLKTSTVIN WFHNYRSRIR RELFIEEIQA GSQGQAGASD SPSARSGRAA PSSEGDSCDG VEATEGPGSA DTEEPKSQGE AEREEVPRPA EQTEPPPSGT PGPDDARDDD HEGGPVEGPG PLPSPASATA TAAPAAPEDA ATSAAAAPGE GPAAPSSAPP PSNSSSSSAP RRPSSLQSLF GLPEAAGARD SRDNPLRKKK AANLNSIIHR LEKAASREEP IEWEF //