ID CUX1_RAT Reviewed; 1504 AA.
AC P53565; F1LRC5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 2.
DT 24-JAN-2024, entry version 165.
DE RecName: Full=Homeobox protein cut-like 1 {ECO:0000305};
DE AltName: Full=CCAAT displacement protein;
DE Short=CDP;
DE AltName: Full=CDP2;
DE AltName: Full=Homeobox protein cux-1;
DE Contains:
DE RecName: Full=CDP/Cux p110 {ECO:0000250|UniProtKB:P39880};
GN Name=Cux1 {ECO:0000312|RGD:620618}; Synonyms=Cdpl1, Cutl1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 643-1504, FUNCTION, AND PHOSPHORYLATION BY
RP PKA.
RC STRAIN=New England Deaconess Hospital; TISSUE=Adrenal medulla;
RX PubMed=7913462; DOI=10.1016/s0021-9258(17)32330-x;
RA Yoon S.O., Chikaraishi D.M.;
RT "Isolation of two E-box binding factors that interact with the rat tyrosine
RT hydroxylase enhancer.";
RL J. Biol. Chem. 269:18453-18462(1994).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438; SER-893; SER-1053 AND
RP SER-1495, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 ECO:0000269|PubMed:7913462}.
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. 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:0000250|UniProtKB:P53564}.
CC -!- PTM: Phosphorylated by PKA. {ECO:0000269|PubMed:7913462}.
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 -!- SIMILARITY: Belongs to the CUT homeobox family. {ECO:0000305}.
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DR EMBL; AABR06071155; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U09229; AAA21123.1; -; mRNA.
DR PIR; B53689; B53689.
DR RefSeq; XP_008758482.1; XM_008760260.2.
DR RefSeq; XP_008767387.1; XM_008769165.2.
DR AlphaFoldDB; P53565; -.
DR SMR; P53565; -.
DR IntAct; P53565; 1.
DR MINT; P53565; -.
DR STRING; 10116.ENSRNOP00000056243; -.
DR iPTMnet; P53565; -.
DR PhosphoSitePlus; P53565; -.
DR jPOST; P53565; -.
DR PaxDb; 10116-ENSRNOP00000001928; -.
DR PeptideAtlas; P53565; -.
DR Ensembl; ENSRNOT00000059486.6; ENSRNOP00000056243.3; ENSRNOG00000001424.9.
DR Ensembl; ENSRNOT00055000459; ENSRNOP00055000322; ENSRNOG00055000274.
DR Ensembl; ENSRNOT00060020018; ENSRNOP00060015701; ENSRNOG00060011805.
DR UCSC; RGD:620618; rat.
DR AGR; RGD:620618; -.
DR RGD; 620618; Cux1.
DR eggNOG; KOG0963; Eukaryota.
DR eggNOG; KOG2252; Eukaryota.
DR GeneTree; ENSGT00940000159751; -.
DR HOGENOM; CLU_005104_2_0_1; -.
DR InParanoid; P53565; -.
DR OrthoDB; 74668at2759; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001424; Expressed in testis and 19 other cell types or tissues.
DR Genevisible; P53565; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0042491; P:inner ear auditory receptor cell differentiation; ISO:RGD.
DR GO; GO:0001822; P:kidney development; ISO:RGD.
DR GO; GO:0030324; P:lung development; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0000301; P:retrograde transport, vesicle recycling within Golgi; IMP:RGD.
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 Coiled coil; Developmental protein; DNA-binding; Homeobox; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..1504
FT /note="Homeobox protein cut-like 1"
FT /id="PRO_0000202395"
FT CHAIN 743..1504
FT /note="CDP/Cux p110"
FT /evidence="ECO:0000250|UniProtKB:P39880"
FT /id="PRO_0000450799"
FT DNA_BIND 551..638
FT /note="CUT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00374"
FT DNA_BIND 918..1005
FT /note="CUT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00374"
FT DNA_BIND 1101..1188
FT /note="CUT 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00374"
FT DNA_BIND 1228..1287
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 404..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1196..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1296..1476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 67..359
FT /evidence="ECO:0000255"
FT COMPBIAS 444..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..836
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..894
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..912
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1066
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1296..1317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1438..1456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 734..742
FT /note="Cleavage; by CTSL"
FT /evidence="ECO:0000250|UniProtKB:P39880"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 750
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39880"
FT MOD_RES 893
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1043
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39880"
FT MOD_RES 1053
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39880"
FT MOD_RES 1321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53564"
FT MOD_RES 1457
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39880"
FT MOD_RES 1485
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39880"
FT MOD_RES 1495
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CROSSLNK 772
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P39880"
FT CROSSLNK 798
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P39880"
FT CROSSLNK 829
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P39880"
FT CROSSLNK 1268
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P39880"
SQ SEQUENCE 1504 AA; 164541 MW; C1E3CBC4F6829D63 CRC64;
MAANVGSMFQ YWKRFDLQQL QRELDATATV LANRQDESEQ SRKRLIEQSR EFKKNTPEDL
RKQVAPLLKS FQGEIDALSK RSKEAEAAFL TVYKRLIDVP DPVPALDLGQ QLEIKVQRLH
DIETENQKLR ETLEEYNKEF AEVKNQEVTI KALKEKIREY EQTLKSQAET IALEKEQKLQ
NDFAEKERKL QETQMSTTSK LEEAEHKLQT LQTALEKTRT ELFDLKTKYD EETTAKADEI
EMIMTDLERA NQRAEVAQRE AETLREQLSS ANHSLQLASQ IQKAPDVAIE VLTRSSLEVE
LAAKEREIAQ LVEDVQRLQA SLTKLRENSA SQISQLEQQL NAKNSTLKQL EEKLKGQADY
EDVKKELTTL KSMEFAPSEG AGTQDSTKPL EVLLLEKNRS LQSENATLRI SNSDLSGSAR
RKGRDQPESR RPGPLPASPP PQLPRNTGEQ VSNTNGTHHF SPAGLSQDFF SSNLASPSLP
LASTGKFALN SLLQRQLMQS FYSKAMQEAG STSTIFSTGP YSTNSISSPS PLQQSPDVNG
MAPSPSQSES AGSISEGEEI DTAEIARQVK EQLIKHNIGQ RIFGHYVLGL SQGSVSEILA
RPKPWNKLTV RGKEPFHKMK QFLSDEQNIL ALRSIQGRQR GNITTRIRAS ETGSDEAIKS
ILEQAKRELQ VQKTAEPVQA SSTASSGNSD DAIRSILQQA RREMEAQQAA LDPALKPAPL
SQPDLTILNP KLLSASPMST VSTYPPLAIS LKKTPAAPEA STSALPSAPA LKKEAQDAPT
LDPPGSADAT PGVLRPVKNE LVRGSTWKDP WWNPVQPERR NLTTSEETKA DETNASGKEK
TGSSQPRAER SQLQGPSATA EYWKEWPNAE SPYSQSSELS LTGASRSETP QNSPLPSSPI
VPMAKPAKPS VPPLTPEQYE VYMYQEVDTI ELTRQVKEKL AKNGICQRIF GEKVLGLSQG
SVSDMLSRPK PWSKLTQKGR EPFIRMQLWL NGELGQGVLP VQGQQQGPVL HSVTSLQDPL
QQGCVSSEST PKTSASCSPA PESPMSSSES VKSLTELVQQ PCPTIETSKE GKPPEPSDPP
TSDSQPTTPL PLSGHSALSI QELVAMSPEL DTYGITKRVK EVLTDNNLGQ RLFGETILGL
TQGSVSDLLA RPKPWHKLSL KGREPFVRMQ LWLNDPNNVE KLMDMKRMEK KAYMKRRHSS
VSDSQPCEPP SVGIDYSQGA SPQPQHQLKK PRVVLAPEEK EALKRAYQQK PYPSPKTIEE
LATQLNLKTS TVINWFHNYR SRIRRELFIE EIQAGSQGQA GASDSPSARS SRAAPSSEGD
SCDGVEAADT EEPGGNIVAT KSQGGPAEVT AAPADREEAT QPAEKAKAQP LSSGTPGQDD
GEDAGRSRPP PEGLADAPAP VPNLAAPAAG EDAATSATAP AMATEAPGAA RAGPAERSSA
LPSTSAPANA PARRPSSLQS LFGLPEAAGA RDNPVRKKKA ANLNSIIHRL EKAASREEPI
EWEF
//
