CUX1_CANLF
ID CUX1_CANLF Reviewed; 975 AA.
AC P39881;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Homeobox protein cut-like 1 {ECO:0000305};
DE AltName: Full=CCAAT displacement protein;
DE Short=CDP;
DE AltName: Full=Clox-1;
DE AltName: Full=Homeobox protein Clox;
DE AltName: Full=Homeobox protein cux-1;
DE Contains:
DE RecName: Full=CDP/Cux p110 {ECO:0000250|UniProtKB:P39880};
DE Flags: Fragment;
GN Name=CUX1; Synonyms=CLOX, CUTL1;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart ventricle;
RX PubMed=1363085; DOI=10.1242/dev.116.2.321;
RA Andres V., Nadal-Ginard B., Mahdavi V.;
RT "Clox, a mammalian homeobox gene related to Drosophila cut, encodes DNA-
RT binding regulatory proteins differentially expressed during development.";
RL Development 116:321-334(1992).
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:0000250|UniProtKB:P39880}.
CC -!- SUBUNIT: Interacts with BANP. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms may be produced.;
CC Name=1;
CC IsoId=P39881-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: A broad pattern of expression observed in tissues
CC of diverse origins, such as cartilage, liver, brain, lung, heart and
CC skeletal muscle. There are 2 distinct protein species: the larger one
CC (230-250 kDa) is found mainly in adult brain, lung and heart, and the
CC smaller one (180-190 kDa) predominates in early embryonic tissues.
CC -!- DEVELOPMENTAL STAGE: Differentially expressed during development. Small
CC protein species predominate in early embryos and are up-regulated in
CC committed myoblasts and chondrocytes, but down-regulated upon terminal
CC differentiation. Large species are detected mainly in adult tissues and
CC terminally differentiated cells.
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:0000250|UniProtKB:P39880}.
CC -!- PTM: Phosphorylated by PKA. {ECO:0000250|UniProtKB:P53565}.
CC -!- MISCELLANEOUS: Asn-730 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; X69017; CAA48782.1; -; mRNA.
DR PIR; S33121; S33121.
DR AlphaFoldDB; P39881; -.
DR SMR; P39881; -.
DR InParanoid; P39881; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00086; homeodomain; 1.
DR Gene3D; 1.10.260.40; -; 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 Pfam; PF02376; CUT; 3.
DR Pfam; PF00046; Homeodomain; 1.
DR SMART; SM01109; CUT; 3.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF47413; SSF47413; 3.
DR PROSITE; PS51042; CUT; 3.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Coiled coil; Developmental protein; DNA-binding;
KW Homeobox; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN <1..975
FT /note="Homeobox protein cut-like 1"
FT /id="PRO_0000202392"
FT CHAIN 200..975
FT /note="CDP/Cux p110"
FT /evidence="ECO:0000250|UniProtKB:P39880"
FT /id="PRO_0000450796"
FT DNA_BIND <1..73
FT /note="CUT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00374"
FT DNA_BIND 374..461
FT /note="CUT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00374"
FT DNA_BIND 557..644
FT /note="CUT 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00374"
FT DNA_BIND 684..743
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 90..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 113..169
FT /evidence="ECO:0000255"
FT COMPBIAS 94..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..369
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..542
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..832
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..888
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..922
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 87..88
FT /note="Cleavage; by CTSL"
FT /evidence="ECO:0000250|UniProtKB:P39880"
FT SITE 191..199
FT /note="Cleavage; by CTSL"
FT /evidence="ECO:0000250|UniProtKB:P39880"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39880"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53565"
FT MOD_RES 499
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39880"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53565"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39880"
FT MOD_RES 777
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53564"
FT MOD_RES 925
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39880"
FT MOD_RES 956
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39880"
FT MOD_RES 966
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53564"
FT CROSSLNK 229
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P39880"
FT CROSSLNK 255
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P39880"
FT CROSSLNK 286
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P39880"
FT CROSSLNK 724
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P39880"
FT NON_TER 1
SQ SEQUENCE 975 AA; 105429 MW; 724243B32C5BCFD9 CRC64;
SRQVKEQLIK HNIGQRIFGH YVLGLSQGSV SEILARPKPW NKLTVRGKEP FHKMKQFLSD
EQNILALRSI QGRQRENPGQ SLNRLFQEVP KRRNGSEGNI TTRIRASETG SDEAIKSILE
QAKRELQVQK TAEPAQPSST SSSGTSDDAI RSILQQARRE MEAQQAALDP ALKPAPLSQA
DLAILSPKLI PSSPMSSVSS YPPLALSLKK PPTAPDTSAS TLPNPPALKK ESQDAPGLDL
PGAAESAQGV LRHVKSELGR SGVWKDHWWS TVQPERKSAA PPEDAKSEEA GGTKEKGGGQ
GHGPIAASSR DPHHRRSTGR NGPALSPRTP QSSELSLTGA SRSETPQNSP LPSSPIVPMS
KPAKPSVPPL TPEQYEIYMY QEVDTIELTR QVKEKLAKNG ICQRIFGEKV LGLSQGSVSD
MLSRPKPWSK LTQKGREPFI RMQLWLNGEL GQGVLPVQGQ QQGPVLHSVT SLQDPLQQGC
VSSESTPKTS ASCSPAPESP MSSSESVKSL TELVQQPCPP IETSKDGKPP EPSDPPASDS
QPATPLPLSG HSALSIQELV AMSPELDTYG ITKRVKEVLT DNNLGQRLFG ETILGLTQGS
VSDLLSRPKP WHKLSLKGRE PFVRMQLWLN DPNNVEKLMD MKRMEKKAYM KRRHSSVSDS
QPCEPPSVGI DYSQGASPQP QHQLKKPRVV LAPEEKEALK RAYQQKPYPS PKTIEELATQ
LNLKTSTVIN WFHNYRSRIR RELFIEEIQA GSQGQAGARH SPSARSSGAA PSSEGDSCDG
VEAAEGPGAA DAEESAPAAA AKSQGGPAEA AVAPEEREEA PRPAEKRSRR PRGPGPGPGR
RGGGGPAPGA PAAPAAAARG PSRRPGARAK PRRRRRRRRR HARGGGRRYL SRPARGGPCR
ARDGAHRSSA LPSTSAPAAA RRPSSLQSLF GLPEAAGARD SRDNPLRKKK AANLNSIIHR
LEKAASREEP IEWEF
