Full text data of CCNDBP1
CCNDBP1
(DIP1, GCIP, HHM)
[Confidence: low (only semi-automatic identification from reviews)]
Cyclin-D1-binding protein 1 (Grap2 and cyclin-D-interacting protein; Human homolog of Maid)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Cyclin-D1-binding protein 1 (Grap2 and cyclin-D-interacting protein; Human homolog of Maid)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O95273
ID CCDB1_HUMAN Reviewed; 360 AA.
AC O95273; A8K3Q0; A8K3U2; Q6ZQN9; Q7Z519; Q8NBS7; Q8NBY2; Q9NS19;
read moreAC Q9NYH3; Q9UHX9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 22-JAN-2014, entry version 78.
DE RecName: Full=Cyclin-D1-binding protein 1;
DE AltName: Full=Grap2 and cyclin-D-interacting protein;
DE AltName: Full=Human homolog of Maid;
GN Name=CCNDBP1; Synonyms=DIP1, GCIP, HHM;
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 [MRNA] (ISOFORM 1), INTERACTION WITH CCND1,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP PHOSPHORYLATION.
RX PubMed=10854051; DOI=10.1006/excr.2000.4884;
RA Yao Y., Doki Y., Jiang W., Imoto M., Venkatraj V.S., Warburton D.,
RA Santella R.M., Lu B., Yan L., Sun X.-H., Su T., Luo J.,
RA Weinstein I.B.;
RT "Cloning and characterization of DIP1, a novel protein that is related
RT to the Id family of proteins.";
RL Exp. Cell Res. 257:22-32(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH TCF3, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=10915743; DOI=10.1053/jhep.2000.9092;
RA Terai S., Aoki H., Thorgeirsson S.S.;
RT "Human homologue of maid: a dominant inhibitory helix-loop-helix
RT protein associated with liver-specific gene expression.";
RL Hepatology 32:357-366(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH
RP CCND1 AND GRAP2, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=10801854; DOI=10.1074/jbc.M002598200;
RA Xia C., Bao Z., Tabassam F., Ma W., Qiu M., Hua S., Liu M.;
RT "GCIP, a novel human grap2 and cyclin D interacting protein, regulates
RT E2F-mediated transcriptional activity.";
RL J. Biol. Chem. 275:20942-20948(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Gao J., Yu L., Mao N.H., Wan Y.Z., Yang Y.M., Zhao S.Y.;
RT "Cloning and characterization of a novel human cDNA homologous to
RT murine Maid mRNA.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Hypothalamus;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Hair follicle dermal papilla, Lung, Retinoblastoma, and
RC Trachea;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-
RT length human cDNAs encoding secretion or membrane proteins from oligo-
RT capped cDNA libraries.";
RL DNA Res. 12:117-126(2005).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pancreas;
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 [11]
RP INTERACTION WITH SYF2.
RX PubMed=11118353; DOI=10.1006/bbrc.2000.3992;
RA Chang M.-S., Chang C.-L., Huang C.-J., Yang Y.-C.;
RT "p29, a novel GCIP-interacting protein, localizes in the nucleus.";
RL Biochem. Biophys. Res. Commun. 279:732-737(2000).
RN [12]
RP TISSUE SPECIFICITY, AND INTERACTION WITH COPS5.
RX PubMed=15887118; DOI=10.1053/j.gastro.2005.03.014;
RA Takami T., Terai S., Yokoyama Y., Tanimoto H., Tajima K., Uchida K.,
RA Yamasaki T., Sakaida I., Nishina H., Thorgeirsson S.S., Okita K.;
RT "Human homologue of maid is a useful marker protein in
RT hepatocarcinogenesis.";
RL Gastroenterology 128:1369-1380(2005).
RN [13]
RP INTERACTION WITH SIRT6, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=17131381; DOI=10.1002/jcb.21140;
RA Ma W., Stafford L.J., Li D., Luo J., Li X., Ning G., Liu M.;
RT "GCIP/CCNDBP1, a helix-loop-helix protein, suppresses tumorigenesis.";
RL J. Cell. Biochem. 100:1376-1386(2007).
RN [14]
RP INTERACTION WITH RPLP0, AND SUBCELLULAR LOCATION.
RX PubMed=17621266; DOI=10.1038/sj.onc.1210651;
RA Chang T.-W., Chen C.-C., Chen K.-Y., Su J.-H., Chang J.-H.,
RA Chang M.-C.;
RT "Ribosomal phosphoprotein P0 interacts with GCIP and overexpression of
RT P0 is associated with cellular proliferation in breast and liver
RT carcinoma cells.";
RL Oncogene 27:332-338(2008).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: May negatively regulate cell cycle progression. May act
CC at least in part via inhibition of the cyclin-D1/CDK4 complex,
CC thereby preventing phosphorylation of RB1 and blocking E2F-
CC dependent transcription.
CC -!- SUBUNIT: Interacts with CCND1 and GRAP2. May also interact with
CC COPS5, RPLP0, SIRT6, SYF2 and TCF3.
CC -!- INTERACTION:
CC Q92905:COPS5; NbExp=5; IntAct=EBI-748961, EBI-594661;
CC Q02363:ID2; NbExp=4; IntAct=EBI-748961, EBI-713450;
CC Q60867:Neurod1 (xeno); NbExp=4; IntAct=EBI-748961, EBI-309315;
CC P55042:RRAD; NbExp=5; IntAct=EBI-748961, EBI-3911502;
CC P15923-1:TCF3; NbExp=3; IntAct=EBI-748961, EBI-769645;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O95273-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95273-2; Sequence=VSP_032014, VSP_032015;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=O95273-3; Sequence=VSP_032012;
CC Name=4;
CC IsoId=O95273-4; Sequence=VSP_032012, VSP_032013, VSP_032016;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expression is down-
CC regulated in a variety of tumor types including breast, colon,
CC prostate and rectal tumors, and is up-regulated in certain hepatic
CC carcinomas.
CC -!- DEVELOPMENTAL STAGE: Expression may increase during
CC differentiation.
CC -!- INDUCTION: Expression is induced by sodium butyrate, an inhibitor
CC of colon cancer cell proliferation.
CC -!- PTM: Phosphorylated.
CC -!- SIMILARITY: Belongs to the CCNDBP1 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD11777.1; Type=Frameshift; Positions=8, 14, 18;
CC Sequence=AAP97163.1; Type=Frameshift; Positions=17, 40;
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DR EMBL; AF082569; AAD11777.1; ALT_FRAME; mRNA.
DR EMBL; AF132034; AAF77613.1; -; mRNA.
DR EMBL; AF246144; AAF67182.1; -; mRNA.
DR EMBL; AF087852; AAP97163.1; ALT_FRAME; mRNA.
DR EMBL; AF113535; AAF14872.1; -; mRNA.
DR EMBL; CR450331; CAG29327.1; -; mRNA.
DR EMBL; AK075296; BAC11530.1; -; mRNA.
DR EMBL; AK128849; BAC87645.1; -; mRNA.
DR EMBL; AK290665; BAF83354.1; -; mRNA.
DR EMBL; AK290707; BAF83396.1; -; mRNA.
DR EMBL; AK075146; BAC11433.1; -; mRNA.
DR EMBL; CH471125; EAW92588.1; -; Genomic_DNA.
DR EMBL; CH471125; EAW92590.1; -; Genomic_DNA.
DR EMBL; BC009689; AAH09689.1; -; mRNA.
DR RefSeq; NP_036274.3; NM_012142.4.
DR UniGene; Hs.36794; -.
DR PDB; 3AY5; X-ray; 2.50 A; A=1-360.
DR PDBsum; 3AY5; -.
DR ProteinModelPortal; O95273; -.
DR SMR; O95273; 14-360.
DR IntAct; O95273; 21.
DR MINT; MINT-1411177; -.
DR PhosphoSite; O95273; -.
DR PaxDb; O95273; -.
DR PRIDE; O95273; -.
DR DNASU; 23582; -.
DR Ensembl; ENST00000300213; ENSP00000300213; ENSG00000166946.
DR Ensembl; ENST00000565296; ENSP00000455419; ENSG00000166946.
DR Ensembl; ENST00000566515; ENSP00000456797; ENSG00000166946.
DR GeneID; 23582; -.
DR KEGG; hsa:23582; -.
DR UCSC; uc001zqv.3; human.
DR CTD; 23582; -.
DR GeneCards; GC15P043477; -.
DR HGNC; HGNC:1587; CCNDBP1.
DR HPA; CAB020664; -.
DR MIM; 607089; gene.
DR neXtProt; NX_O95273; -.
DR PharmGKB; PA26154; -.
DR eggNOG; NOG19167; -.
DR HOVERGEN; HBG107623; -.
DR InParanoid; O95273; -.
DR OMA; CMNRIKE; -.
DR OrthoDB; EOG70S75V; -.
DR PhylomeDB; O95273; -.
DR ChiTaRS; CCNDBP1; human.
DR GeneWiki; CCNDBP1; -.
DR GenomeRNAi; 23582; -.
DR NextBio; 46190; -.
DR PRO; PR:O95273; -.
DR ArrayExpress; O95273; -.
DR Bgee; O95273; -.
DR Genevestigator; O95273; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
DR InterPro; IPR026907; CCNDBP1.
DR PANTHER; PTHR32435; PTHR32435; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell cycle;
KW Complete proteome; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 360 Cyclin-D1-binding protein 1.
FT /FTId=PRO_0000323372.
FT REGION 2 208 Required for interaction with CCND1.
FT REGION 2 190 Interaction with RPLP0.
FT REGION 2 184 Interaction with TCF3.
FT REGION 150 360 Interaction with TCF3.
FT REGION 240 360 Interaction with RPLP0.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 1 128 Missing (in isoform 3 and isoform 4).
FT /FTId=VSP_032012.
FT VAR_SEQ 308 333 SAKLVSVLKKALEITKASHVTPQPED -> VSTGFEGIATE
FT QMGRISLITSISCK (in isoform 4).
FT /FTId=VSP_032013.
FT VAR_SEQ 308 309 SA -> EP (in isoform 2).
FT /FTId=VSP_032014.
FT VAR_SEQ 310 360 Missing (in isoform 2).
FT /FTId=VSP_032015.
FT VAR_SEQ 334 360 Missing (in isoform 4).
FT /FTId=VSP_032016.
FT CONFLICT 40 40 A -> D (in Ref. 1; AAD11777).
FT CONFLICT 41 41 Q -> R (in Ref. 4; AAP97163).
FT CONFLICT 74 74 F -> S (in Ref. 8; BAC11433).
FT CONFLICT 211 211 N -> S (in Ref. 8; BAC11433).
FT CONFLICT 235 235 E -> G (in Ref. 7; BAF83396).
FT CONFLICT 267 267 K -> R (in Ref. 7; BAC87645).
FT CONFLICT 274 274 L -> M (in Ref. 1; AAD11777 and 3;
FT AAF67182).
FT CONFLICT 310 310 K -> R (in Ref. 7; BAC11530).
FT CONFLICT 334 334 S -> I (in Ref. 7; BAF83354).
FT HELIX 17 29
FT HELIX 31 36
FT HELIX 49 73
FT STRAND 76 78
FT HELIX 82 103
FT HELIX 108 110
FT HELIX 112 137
FT HELIX 154 160
FT TURN 161 164
FT HELIX 169 197
FT HELIX 235 265
FT HELIX 271 295
FT STRAND 296 298
FT HELIX 301 324
FT HELIX 335 352
FT HELIX 353 358
SQ SEQUENCE 360 AA; 40262 MW; 40C7C3686632F6A7 CRC64;
MASATAPAAA VPTLASPLEQ LRHLAEELRL LLPRVRVGEA QETTEEFNRE MFWRRLNEAA
VTVSREATTL TIVFSQLPLP SPQETQKFCE QVHAAIKAFI AVYYLLPKDQ GITLRKLVRG
ATLDIVDGMA QLMEVLSVTP TQSPENNDLI SYNSVWVACQ QMPQIPRDNK AAALLMLTKN
VDFVKDAHEE MEQAVEECDP YSGLLNDTEE NNSDNHNHED DVLGFPSNQD LYWSEDDQEL
IIPCLALVRA SKACLKKIRM LVAENGKKDQ VAQLDDIVDI SDEISPSVDD LALSIYPPMC
HLTVRINSAK LVSVLKKALE ITKASHVTPQ PEDSWIPLLI NAIDHCMNRI KELTQSELEL
//
ID CCDB1_HUMAN Reviewed; 360 AA.
AC O95273; A8K3Q0; A8K3U2; Q6ZQN9; Q7Z519; Q8NBS7; Q8NBY2; Q9NS19;
read moreAC Q9NYH3; Q9UHX9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 22-JAN-2014, entry version 78.
DE RecName: Full=Cyclin-D1-binding protein 1;
DE AltName: Full=Grap2 and cyclin-D-interacting protein;
DE AltName: Full=Human homolog of Maid;
GN Name=CCNDBP1; Synonyms=DIP1, GCIP, HHM;
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 [MRNA] (ISOFORM 1), INTERACTION WITH CCND1,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP PHOSPHORYLATION.
RX PubMed=10854051; DOI=10.1006/excr.2000.4884;
RA Yao Y., Doki Y., Jiang W., Imoto M., Venkatraj V.S., Warburton D.,
RA Santella R.M., Lu B., Yan L., Sun X.-H., Su T., Luo J.,
RA Weinstein I.B.;
RT "Cloning and characterization of DIP1, a novel protein that is related
RT to the Id family of proteins.";
RL Exp. Cell Res. 257:22-32(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH TCF3, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=10915743; DOI=10.1053/jhep.2000.9092;
RA Terai S., Aoki H., Thorgeirsson S.S.;
RT "Human homologue of maid: a dominant inhibitory helix-loop-helix
RT protein associated with liver-specific gene expression.";
RL Hepatology 32:357-366(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH
RP CCND1 AND GRAP2, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=10801854; DOI=10.1074/jbc.M002598200;
RA Xia C., Bao Z., Tabassam F., Ma W., Qiu M., Hua S., Liu M.;
RT "GCIP, a novel human grap2 and cyclin D interacting protein, regulates
RT E2F-mediated transcriptional activity.";
RL J. Biol. Chem. 275:20942-20948(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Gao J., Yu L., Mao N.H., Wan Y.Z., Yang Y.M., Zhao S.Y.;
RT "Cloning and characterization of a novel human cDNA homologous to
RT murine Maid mRNA.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Hypothalamus;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Hair follicle dermal papilla, Lung, Retinoblastoma, and
RC Trachea;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-
RT length human cDNAs encoding secretion or membrane proteins from oligo-
RT capped cDNA libraries.";
RL DNA Res. 12:117-126(2005).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pancreas;
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 [11]
RP INTERACTION WITH SYF2.
RX PubMed=11118353; DOI=10.1006/bbrc.2000.3992;
RA Chang M.-S., Chang C.-L., Huang C.-J., Yang Y.-C.;
RT "p29, a novel GCIP-interacting protein, localizes in the nucleus.";
RL Biochem. Biophys. Res. Commun. 279:732-737(2000).
RN [12]
RP TISSUE SPECIFICITY, AND INTERACTION WITH COPS5.
RX PubMed=15887118; DOI=10.1053/j.gastro.2005.03.014;
RA Takami T., Terai S., Yokoyama Y., Tanimoto H., Tajima K., Uchida K.,
RA Yamasaki T., Sakaida I., Nishina H., Thorgeirsson S.S., Okita K.;
RT "Human homologue of maid is a useful marker protein in
RT hepatocarcinogenesis.";
RL Gastroenterology 128:1369-1380(2005).
RN [13]
RP INTERACTION WITH SIRT6, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=17131381; DOI=10.1002/jcb.21140;
RA Ma W., Stafford L.J., Li D., Luo J., Li X., Ning G., Liu M.;
RT "GCIP/CCNDBP1, a helix-loop-helix protein, suppresses tumorigenesis.";
RL J. Cell. Biochem. 100:1376-1386(2007).
RN [14]
RP INTERACTION WITH RPLP0, AND SUBCELLULAR LOCATION.
RX PubMed=17621266; DOI=10.1038/sj.onc.1210651;
RA Chang T.-W., Chen C.-C., Chen K.-Y., Su J.-H., Chang J.-H.,
RA Chang M.-C.;
RT "Ribosomal phosphoprotein P0 interacts with GCIP and overexpression of
RT P0 is associated with cellular proliferation in breast and liver
RT carcinoma cells.";
RL Oncogene 27:332-338(2008).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: May negatively regulate cell cycle progression. May act
CC at least in part via inhibition of the cyclin-D1/CDK4 complex,
CC thereby preventing phosphorylation of RB1 and blocking E2F-
CC dependent transcription.
CC -!- SUBUNIT: Interacts with CCND1 and GRAP2. May also interact with
CC COPS5, RPLP0, SIRT6, SYF2 and TCF3.
CC -!- INTERACTION:
CC Q92905:COPS5; NbExp=5; IntAct=EBI-748961, EBI-594661;
CC Q02363:ID2; NbExp=4; IntAct=EBI-748961, EBI-713450;
CC Q60867:Neurod1 (xeno); NbExp=4; IntAct=EBI-748961, EBI-309315;
CC P55042:RRAD; NbExp=5; IntAct=EBI-748961, EBI-3911502;
CC P15923-1:TCF3; NbExp=3; IntAct=EBI-748961, EBI-769645;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O95273-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95273-2; Sequence=VSP_032014, VSP_032015;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=O95273-3; Sequence=VSP_032012;
CC Name=4;
CC IsoId=O95273-4; Sequence=VSP_032012, VSP_032013, VSP_032016;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expression is down-
CC regulated in a variety of tumor types including breast, colon,
CC prostate and rectal tumors, and is up-regulated in certain hepatic
CC carcinomas.
CC -!- DEVELOPMENTAL STAGE: Expression may increase during
CC differentiation.
CC -!- INDUCTION: Expression is induced by sodium butyrate, an inhibitor
CC of colon cancer cell proliferation.
CC -!- PTM: Phosphorylated.
CC -!- SIMILARITY: Belongs to the CCNDBP1 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD11777.1; Type=Frameshift; Positions=8, 14, 18;
CC Sequence=AAP97163.1; Type=Frameshift; Positions=17, 40;
CC -----------------------------------------------------------------------
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DR EMBL; AF082569; AAD11777.1; ALT_FRAME; mRNA.
DR EMBL; AF132034; AAF77613.1; -; mRNA.
DR EMBL; AF246144; AAF67182.1; -; mRNA.
DR EMBL; AF087852; AAP97163.1; ALT_FRAME; mRNA.
DR EMBL; AF113535; AAF14872.1; -; mRNA.
DR EMBL; CR450331; CAG29327.1; -; mRNA.
DR EMBL; AK075296; BAC11530.1; -; mRNA.
DR EMBL; AK128849; BAC87645.1; -; mRNA.
DR EMBL; AK290665; BAF83354.1; -; mRNA.
DR EMBL; AK290707; BAF83396.1; -; mRNA.
DR EMBL; AK075146; BAC11433.1; -; mRNA.
DR EMBL; CH471125; EAW92588.1; -; Genomic_DNA.
DR EMBL; CH471125; EAW92590.1; -; Genomic_DNA.
DR EMBL; BC009689; AAH09689.1; -; mRNA.
DR RefSeq; NP_036274.3; NM_012142.4.
DR UniGene; Hs.36794; -.
DR PDB; 3AY5; X-ray; 2.50 A; A=1-360.
DR PDBsum; 3AY5; -.
DR ProteinModelPortal; O95273; -.
DR SMR; O95273; 14-360.
DR IntAct; O95273; 21.
DR MINT; MINT-1411177; -.
DR PhosphoSite; O95273; -.
DR PaxDb; O95273; -.
DR PRIDE; O95273; -.
DR DNASU; 23582; -.
DR Ensembl; ENST00000300213; ENSP00000300213; ENSG00000166946.
DR Ensembl; ENST00000565296; ENSP00000455419; ENSG00000166946.
DR Ensembl; ENST00000566515; ENSP00000456797; ENSG00000166946.
DR GeneID; 23582; -.
DR KEGG; hsa:23582; -.
DR UCSC; uc001zqv.3; human.
DR CTD; 23582; -.
DR GeneCards; GC15P043477; -.
DR HGNC; HGNC:1587; CCNDBP1.
DR HPA; CAB020664; -.
DR MIM; 607089; gene.
DR neXtProt; NX_O95273; -.
DR PharmGKB; PA26154; -.
DR eggNOG; NOG19167; -.
DR HOVERGEN; HBG107623; -.
DR InParanoid; O95273; -.
DR OMA; CMNRIKE; -.
DR OrthoDB; EOG70S75V; -.
DR PhylomeDB; O95273; -.
DR ChiTaRS; CCNDBP1; human.
DR GeneWiki; CCNDBP1; -.
DR GenomeRNAi; 23582; -.
DR NextBio; 46190; -.
DR PRO; PR:O95273; -.
DR ArrayExpress; O95273; -.
DR Bgee; O95273; -.
DR Genevestigator; O95273; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
DR InterPro; IPR026907; CCNDBP1.
DR PANTHER; PTHR32435; PTHR32435; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell cycle;
KW Complete proteome; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 360 Cyclin-D1-binding protein 1.
FT /FTId=PRO_0000323372.
FT REGION 2 208 Required for interaction with CCND1.
FT REGION 2 190 Interaction with RPLP0.
FT REGION 2 184 Interaction with TCF3.
FT REGION 150 360 Interaction with TCF3.
FT REGION 240 360 Interaction with RPLP0.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 1 128 Missing (in isoform 3 and isoform 4).
FT /FTId=VSP_032012.
FT VAR_SEQ 308 333 SAKLVSVLKKALEITKASHVTPQPED -> VSTGFEGIATE
FT QMGRISLITSISCK (in isoform 4).
FT /FTId=VSP_032013.
FT VAR_SEQ 308 309 SA -> EP (in isoform 2).
FT /FTId=VSP_032014.
FT VAR_SEQ 310 360 Missing (in isoform 2).
FT /FTId=VSP_032015.
FT VAR_SEQ 334 360 Missing (in isoform 4).
FT /FTId=VSP_032016.
FT CONFLICT 40 40 A -> D (in Ref. 1; AAD11777).
FT CONFLICT 41 41 Q -> R (in Ref. 4; AAP97163).
FT CONFLICT 74 74 F -> S (in Ref. 8; BAC11433).
FT CONFLICT 211 211 N -> S (in Ref. 8; BAC11433).
FT CONFLICT 235 235 E -> G (in Ref. 7; BAF83396).
FT CONFLICT 267 267 K -> R (in Ref. 7; BAC87645).
FT CONFLICT 274 274 L -> M (in Ref. 1; AAD11777 and 3;
FT AAF67182).
FT CONFLICT 310 310 K -> R (in Ref. 7; BAC11530).
FT CONFLICT 334 334 S -> I (in Ref. 7; BAF83354).
FT HELIX 17 29
FT HELIX 31 36
FT HELIX 49 73
FT STRAND 76 78
FT HELIX 82 103
FT HELIX 108 110
FT HELIX 112 137
FT HELIX 154 160
FT TURN 161 164
FT HELIX 169 197
FT HELIX 235 265
FT HELIX 271 295
FT STRAND 296 298
FT HELIX 301 324
FT HELIX 335 352
FT HELIX 353 358
SQ SEQUENCE 360 AA; 40262 MW; 40C7C3686632F6A7 CRC64;
MASATAPAAA VPTLASPLEQ LRHLAEELRL LLPRVRVGEA QETTEEFNRE MFWRRLNEAA
VTVSREATTL TIVFSQLPLP SPQETQKFCE QVHAAIKAFI AVYYLLPKDQ GITLRKLVRG
ATLDIVDGMA QLMEVLSVTP TQSPENNDLI SYNSVWVACQ QMPQIPRDNK AAALLMLTKN
VDFVKDAHEE MEQAVEECDP YSGLLNDTEE NNSDNHNHED DVLGFPSNQD LYWSEDDQEL
IIPCLALVRA SKACLKKIRM LVAENGKKDQ VAQLDDIVDI SDEISPSVDD LALSIYPPMC
HLTVRINSAK LVSVLKKALE ITKASHVTPQ PEDSWIPLLI NAIDHCMNRI KELTQSELEL
//
MIM
607089
*RECORD*
*FIELD* NO
607089
*FIELD* TI
*607089 CYCLIN D-TYPE-BINDING PROTEIN 1; CCNDBP1
;;GRAP2 CYCLIN-D-INTERACTING PROTEIN; GCIP
read more*FIELD* TX
CLONING
In a yeast 2-hybrid screen with the C-terminal glu/pro-rich domain and
the SH3 domain (QC domain) of GRAP2 (604518) as bait, Xia et al. (2000)
cloned CCNDBP1, which they called GCIP, from a pretransformed human bone
marrow cDNA library. CCNDBP1 encodes a deduced 360-amino acid protein
with a calculated molecular mass of 40 kD. It is predicted to contain a
helix-loop-helix region without the basic DNA-binding domain, a central
acidic domain, and a leucine zipper motif. Northern blot analysis
detected a 1.3-kb transcript in all tissues examined, with highest
expression in heart, muscle, peripheral leukocytes, kidney, and brain.
RT-PCR revealed expression in all immune tissues, with relatively low
expression in bone marrow.
GENE FUNCTION
Xia et al. (2000) verified interaction between GCIP and the QC domain of
GRAP2 in yeast 2 hybrid assays, in in vitro binding assays, and by
Western blot analysis of immunoprecipitates of cotransfected COS-7
cells. GST pull-down assays of cell lysates from several cell lines and
coimmunoprecipitation of cyclin D with GCIP from GCIP-transfected cells
showed that GCIP also associates with cyclin D (CCND1; 168461).
Overexpression of GCIP in COS-7 cells reduced the phosphorylation of the
retinoblastoma protein (RB1; 614041) by immunopurified cyclin D/CDK4
(123829) complexes. GCIP expression also reduced the transcriptional
activity of a cotransfected E2F1 (189971) reporter plasmid.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the CCNDBP1
gene to chromosome 15 (TMAP WI16359).
*FIELD* RF
1. Xia, C.; Bao, Z.; Tabassam, F.; Ma, W.; Qiu, M.; Hua, S.; Liu,
M.: GCIP, a novel human Grap2 and cyclin D interacting protein, regulates
E2F-mediated transcriptional activity. J. Biol. Chem. 275: 20942-20948,
2000.
*FIELD* CD
Patricia A. Hartz: 7/2/2002
*FIELD* ED
alopez: 06/17/2011
carol: 7/2/2002
*RECORD*
*FIELD* NO
607089
*FIELD* TI
*607089 CYCLIN D-TYPE-BINDING PROTEIN 1; CCNDBP1
;;GRAP2 CYCLIN-D-INTERACTING PROTEIN; GCIP
read more*FIELD* TX
CLONING
In a yeast 2-hybrid screen with the C-terminal glu/pro-rich domain and
the SH3 domain (QC domain) of GRAP2 (604518) as bait, Xia et al. (2000)
cloned CCNDBP1, which they called GCIP, from a pretransformed human bone
marrow cDNA library. CCNDBP1 encodes a deduced 360-amino acid protein
with a calculated molecular mass of 40 kD. It is predicted to contain a
helix-loop-helix region without the basic DNA-binding domain, a central
acidic domain, and a leucine zipper motif. Northern blot analysis
detected a 1.3-kb transcript in all tissues examined, with highest
expression in heart, muscle, peripheral leukocytes, kidney, and brain.
RT-PCR revealed expression in all immune tissues, with relatively low
expression in bone marrow.
GENE FUNCTION
Xia et al. (2000) verified interaction between GCIP and the QC domain of
GRAP2 in yeast 2 hybrid assays, in in vitro binding assays, and by
Western blot analysis of immunoprecipitates of cotransfected COS-7
cells. GST pull-down assays of cell lysates from several cell lines and
coimmunoprecipitation of cyclin D with GCIP from GCIP-transfected cells
showed that GCIP also associates with cyclin D (CCND1; 168461).
Overexpression of GCIP in COS-7 cells reduced the phosphorylation of the
retinoblastoma protein (RB1; 614041) by immunopurified cyclin D/CDK4
(123829) complexes. GCIP expression also reduced the transcriptional
activity of a cotransfected E2F1 (189971) reporter plasmid.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the CCNDBP1
gene to chromosome 15 (TMAP WI16359).
*FIELD* RF
1. Xia, C.; Bao, Z.; Tabassam, F.; Ma, W.; Qiu, M.; Hua, S.; Liu,
M.: GCIP, a novel human Grap2 and cyclin D interacting protein, regulates
E2F-mediated transcriptional activity. J. Biol. Chem. 275: 20942-20948,
2000.
*FIELD* CD
Patricia A. Hartz: 7/2/2002
*FIELD* ED
alopez: 06/17/2011
carol: 7/2/2002