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Database: UniProt
Entry: O14529
LinkDB: O14529
Original site: O14529 
ID   CUX2_HUMAN              Reviewed;        1486 AA.
AC   O14529; A7E2Y4;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 4.
DT   26-NOV-2014, entry version 137.
DE   RecName: Full=Homeobox protein cut-like 2;
DE   AltName: Full=Homeobox protein cux-2;
GN   Name=CUX2; Synonyms=CUTL2, KIAA0293;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-1472.
RC   TISSUE=Brain;
RX   PubMed=9179496; DOI=10.1093/dnares/4.1.53;
RA   Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N.,
RA   Nomura N.;
RT   "Construction and characterization of human brain cDNA libraries
RT   suitable for analysis of cDNA clones encoding relatively large
RT   proteins.";
RL   DNA Res. 4:53-59(1997).
RN   [2]
RP   SEQUENCE REVISION.
RX   PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA   Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT   "Construction of expression-ready cDNA clones for KIAA genes: manual
RT   curation of 330 KIAA cDNA clones.";
RL   DNA Res. 9:99-106(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA   Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA   Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA   Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA   Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA   Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA   Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA   Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA   Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA   Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA   Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA   Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA   Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA   Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA   Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA   Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA   Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA   Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA   Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA   Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA   Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA   Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA   Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA   Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA   Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA   Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA   Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA   Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA   Kucherlapati R., Weinstock G., Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-1472.
RC   TISSUE=Brain;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, AND IDENTIFICATION
RP   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   [6]
RP   STRUCTURE BY NMR OF 544-631 AND 887-1125.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the first, second and third CUT domains of
RT   human homeobox protein CUX-2 (CUT-like 2).";
RL   Submitted (OCT-2005) to the PDB data bank.
CC   -!- FUNCTION: May be a transcription factor involved in neural
CC       specification. Binds to DNA in a sequence-specific manner (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
CC       ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00374}.
CC   -!- SIMILARITY: Belongs to the CUT homeobox family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 3 CUT DNA-binding domains.
CC       {ECO:0000255|PROSITE-ProRule:PRU00374}.
CC   -!- SIMILARITY: Contains 1 homeobox DNA-binding domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00108}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA22962.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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DR   EMBL; AB006631; BAA22962.2; ALT_INIT; mRNA.
DR   EMBL; AC005805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC002979; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC002352; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC002978; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC151245; AAI51246.1; -; mRNA.
DR   CCDS; CCDS41837.1; -.
DR   RefSeq; NP_056082.2; NM_015267.3.
DR   UniGene; Hs.124953; -.
DR   PDB; 1WH6; NMR; -; A=887-974.
DR   PDB; 1WH8; NMR; -; A=1028-1125.
DR   PDB; 1X2L; NMR; -; A=544-631.
DR   PDBsum; 1WH6; -.
DR   PDBsum; 1WH8; -.
DR   PDBsum; 1X2L; -.
DR   ProteinModelPortal; O14529; -.
DR   SMR; O14529; 549-631, 887-976, 1032-1220.
DR   STRING; 9606.ENSP00000261726; -.
DR   PhosphoSite; O14529; -.
DR   MaxQB; O14529; -.
DR   PaxDb; O14529; -.
DR   PRIDE; O14529; -.
DR   DNASU; 23316; -.
DR   Ensembl; ENST00000261726; ENSP00000261726; ENSG00000111249.
DR   GeneID; 23316; -.
DR   KEGG; hsa:23316; -.
DR   UCSC; uc001tsa.2; human.
DR   CTD; 23316; -.
DR   GeneCards; GC12P111471; -.
DR   HGNC; HGNC:19347; CUX2.
DR   HPA; HPA044772; -.
DR   MIM; 610648; gene.
DR   neXtProt; NX_O14529; -.
DR   PharmGKB; PA162382977; -.
DR   eggNOG; NOG325167; -.
DR   GeneTree; ENSGT00530000063019; -.
DR   HOGENOM; HOG000143386; -.
DR   HOVERGEN; HBG051268; -.
DR   InParanoid; O14529; -.
DR   KO; K09313; -.
DR   OMA; LVFPPAF; -.
DR   OrthoDB; EOG7VTDMF; -.
DR   PhylomeDB; O14529; -.
DR   TreeFam; TF318206; -.
DR   ChiTaRS; CUX2; human.
DR   EvolutionaryTrace; O14529; -.
DR   GenomeRNAi; 23316; -.
DR   NextBio; 45200; -.
DR   PRO; PR:O14529; -.
DR   Bgee; O14529; -.
DR   CleanEx; HS_CUX2; -.
DR   ExpressionAtlas; O14529; baseline and differential.
DR   Genevestigator; O14529; -.
DR   GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProt.
DR   GO; GO:0005634; C:nucleus; IDA:UniProt.
DR   GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; ISS:UniProt.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProt.
DR   GO; GO:0071310; P:cellular response to organic substance; IEA:Ensembl.
DR   GO; GO:0050890; P:cognition; IMP:UniProt.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProt.
DR   GO; GO:0050775; P:positive regulation of dendrite morphogenesis; ISS:UniProt.
DR   GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; ISS:UniProt.
DR   GO; GO:2000463; P:positive regulation of excitatory postsynaptic membrane potential; ISS:UniProt.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProt.
DR   GO; GO:0051965; P:positive regulation of synapse assembly; ISS:UniProt.
DR   GO; GO:0007614; P:short-term memory; ISS:UniProt.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.60; -; 1.
DR   Gene3D; 1.10.260.40; -; 3.
DR   InterPro; IPR003350; CUT_dom.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom.
DR   Pfam; PF02376; CUT; 3.
DR   Pfam; PF00046; Homeobox; 1.
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   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Complete proteome; DNA-binding; Homeobox;
KW   Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
KW   Transcription; Transcription regulation.
FT   CHAIN         1   1486       Homeobox protein cut-like 2.
FT                                /FTId=PRO_0000202396.
FT   DNA_BIND    544    631       CUT 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00374}.
FT   DNA_BIND    887    974       CUT 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00374}.
FT   DNA_BIND   1038   1125       CUT 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00374}.
FT   DNA_BIND   1168   1227       Homeobox. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00108}.
FT   COILED      195    374       {ECO:0000255}.
FT   COILED      690    717       {ECO:0000255}.
FT   COMPBIAS    440    535       Pro-rich.
FT   COMPBIAS    802    813       Poly-Ser.
FT   COMPBIAS   1327   1437       Pro-rich.
FT   MOD_RES     143    143       Phosphoserine.
FT                                {ECO:0000269|PubMed:18669648}.
FT   VARIANT    1472   1472       V -> L (in dbSNP:rs6490073).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:9179496}.
FT                                /FTId=VAR_065096.
FT   HELIX       555    568       {ECO:0000244|PDB:1X2L}.
FT   HELIX       573    579       {ECO:0000244|PDB:1X2L}.
FT   HELIX       585    593       {ECO:0000244|PDB:1X2L}.
FT   HELIX       598    600       {ECO:0000244|PDB:1X2L}.
FT   HELIX       603    616       {ECO:0000244|PDB:1X2L}.
FT   HELIX       620    630       {ECO:0000244|PDB:1X2L}.
FT   HELIX       889    893       {ECO:0000244|PDB:1WH6}.
FT   HELIX       898    910       {ECO:0000244|PDB:1WH6}.
FT   TURN        911    913       {ECO:0000244|PDB:1WH6}.
FT   HELIX       916    922       {ECO:0000244|PDB:1WH6}.
FT   HELIX       928    936       {ECO:0000244|PDB:1WH6}.
FT   TURN        941    943       {ECO:0000244|PDB:1WH6}.
FT   HELIX       946    961       {ECO:0000244|PDB:1WH6}.
FT   HELIX      1037   1043       {ECO:0000244|PDB:1WH8}.
FT   HELIX      1049   1062       {ECO:0000244|PDB:1WH8}.
FT   HELIX      1067   1073       {ECO:0000244|PDB:1WH8}.
FT   HELIX      1079   1087       {ECO:0000244|PDB:1WH8}.
FT   TURN       1092   1094       {ECO:0000244|PDB:1WH8}.
FT   HELIX      1097   1111       {ECO:0000244|PDB:1WH8}.
FT   HELIX      1115   1123       {ECO:0000244|PDB:1WH8}.
SQ   SEQUENCE   1486 AA;  161677 MW;  71782EF5214D0262 CRC64;
     MAANVGSMFQ YWKRFDLRRL QKELNSVASE LSARQEESEH SHKHLIELRR EFKKNVPEEI
     REMVAPVLKS FQAEVVALSK RSQEAEAAFL SVYKQLIEAP DPVPVFEAAR SLDDRLQPPS
     FDPSGQPRRD LHTSWKRNPE LLSPKEQREG TSPAGPTLTE GSRLPGIPGK ALLTETLLQR
     NEAEKQKGLQ EVQITLAARL GEAEEKIKVL HSALKATQAE LLELRRKYDE EAASKADEVG
     LIMTNLEKAN QRAEAAQREV ESLREQLASV NSSIRLACCS PQGPSGDKVN FTLCSGPRLE
     AALASKDREI LRLLKDVQHL QSSLQELEEA SANQIADLER QLTAKSEAIE KLEEKLQAQS
     DYEEIKTELS ILKAMKLASS TCSLPQGMAK PEDSLLIAKE AFFPTQKFLL EKPSLLASPE
     EDPSEDDSIK DSLGTEQSYP SPQQLPPPPG PEDPLSPSPG QPLLGPSLGP DGTRTFSLSP
     FPSLASGERL MMPPAAFKGE AGGLLVFPPA FYGAKPPTAP ATPAPGPEPL GGPEPADGGG
     GGAAGPGAEE EQLDTAEIAF QVKEQLLKHN IGQRVFGHYV LGLSQGSVSE ILARPKPWRK
     LTVKGKEPFI KMKQFLSDEQ NVLALRTIQV RQRGSITPRI RTPETGSDDA IKSILEQAKK
     EIESQKGGEP KTSVAPLSIA NGTTPASTSE DAIKSILEQA RREMQAQQQA LLEMEVAPRG
     RSVPPSPPER PSLATASQNG APALVKQEEG SGGPAQAPLP VLSPAAFVQS IIRKVKSEIG
     DAGYFDHHWA SDRGLLSRPY ASVSPSLSSS SSSGYSGQPN GRAWPRGDEA PVPPEDEAAA
     GAEDEPPRTG ELKAEGATAE AGARLPYYPA YVPRTLKPTV PPLTPEQYEL YMYREVDTLE
     LTRQVKEKLA KNGICQRIFG EKVLGLSQGS VSDMLSRPKP WSKLTQKGRE PFIRMQLWLS
     DQLGQAVGQQ PGASQASPTE PRSSPSPPPS PTEPEKSSQE PLSLSLESSK ENQQPEGRSS
     SSLSGKMYSG SQAPGGIQEI VAMSPELDTY SITKRVKEVL TDNNLGQRLF GESILGLTQG
     SVSDLLSRPK PWHKLSLKGR EPFVRMQLWL NDPHNVEKLR DMKKLEKKAY LKRRYGLIST
     GSDSESPATR SECPSPCLQP QDLSLLQIKK PRVVLAPEEK EALRKAYQLE PYPSQQTIEL
     LSFQLNLKTN TVINWFHNYR SRMRREMLVE GTQDEPDLDP SGGPGILPPG HSHPDPTPQS
     PDSETEDQKP TVKELELQEG PEENSTPLTT QDKAQVRIKQ EQMEEDAEEE AGSQPQDSGE
     LDKGQGPPKE EHPDPPGNDG LPKVAPGPLL PGGSTPDCPS LHPQQESEAG ERLHPDPLSF
     KSASESSRCS LEVSLNSPSA ASSPGLMMSV SPVPSSSAPI SPSPPGAPPA KVPSASPTAD
     MAGALHPSAK VNPNLQRRHE KMANLNNIIY RVERAANREE ALEWEF
//
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