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}.
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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 Genevisible; P39880; HS.
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.
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
//
