CCDB1_HUMAN
ID CCDB1_HUMAN Reviewed; 360 AA.
AC O95273; A8K3Q0; A8K3U2; Q6ZQN9; Q7Z519; Q8NBS7; Q8NBY2; Q9NS19; Q9NYH3;
AC Q9UHX9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 145.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CCND1, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND 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., Weinstein I.B.;
RT "Cloning and characterization of DIP1, a novel protein that is related to
RT 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 TISSUE
RP 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 protein
RT associated with liver-specific gene expression.";
RL Hepatology 32:357-366(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CCND1
RP 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 E2F-
RT 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 murine
RT 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., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT 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 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., 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 [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-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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., Chang M.-C.;
RT "Ribosomal phosphoprotein P0 interacts with GCIP and overexpression of P0
RT is associated with cellular proliferation in breast and liver carcinoma
RT cells.";
RL Oncogene 27:332-338(2008).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: May negatively regulate cell cycle progression. May act at
CC least in part via inhibition of the cyclin-D1/CDK4 complex, thereby
CC preventing phosphorylation of RB1 and blocking E2F-dependent
CC transcription. {ECO:0000269|PubMed:10801854}.
CC -!- SUBUNIT: Interacts with CCND1 and GRAP2. May also interact with COPS5,
CC RPLP0, SIRT6, SYF2 and TCF3. {ECO:0000269|PubMed:10801854,
CC ECO:0000269|PubMed:10854051, ECO:0000269|PubMed:10915743,
CC ECO:0000269|PubMed:11118353, ECO:0000269|PubMed:15887118,
CC ECO:0000269|PubMed:17131381, ECO:0000269|PubMed:17621266}.
CC -!- INTERACTION:
CC O95273; Q96PE1-2: ADGRA2; NbExp=3; IntAct=EBI-748961, EBI-12227349;
CC O95273; Q01433: AMPD2; NbExp=4; IntAct=EBI-748961, EBI-8796759;
CC O95273; P29972: AQP1; NbExp=3; IntAct=EBI-748961, EBI-745213;
CC O95273; Q7Z5H3: ARHGAP22; NbExp=3; IntAct=EBI-748961, EBI-3866859;
CC O95273; P51164: ATP4B; NbExp=3; IntAct=EBI-748961, EBI-3904463;
CC O95273; Q9BZE7: C22orf23; NbExp=5; IntAct=EBI-748961, EBI-10303102;
CC O95273; Q5I0X4: C6orf226; NbExp=4; IntAct=EBI-748961, EBI-10244057;
CC O95273; Q8IYE0: CCDC146; NbExp=3; IntAct=EBI-748961, EBI-10749669;
CC O95273; Q8IYE0-2: CCDC146; NbExp=3; IntAct=EBI-748961, EBI-10247802;
CC O95273; Q07002: CDK18; NbExp=3; IntAct=EBI-748961, EBI-746238;
CC O95273; Q6ZU64-3: CFAP65; NbExp=3; IntAct=EBI-748961, EBI-10255250;
CC O95273; Q8NE01: CNNM3; NbExp=3; IntAct=EBI-748961, EBI-741032;
CC O95273; Q92905: COPS5; NbExp=5; IntAct=EBI-748961, EBI-594661;
CC O95273; Q93034: CUL5; NbExp=4; IntAct=EBI-748961, EBI-1057139;
CC O95273; Q9NQL9: DMRT3; NbExp=3; IntAct=EBI-748961, EBI-9679045;
CC O95273; Q92608: DOCK2; NbExp=3; IntAct=EBI-748961, EBI-448771;
CC O95273; Q92731-3: ESR2; NbExp=3; IntAct=EBI-748961, EBI-12259414;
CC O95273; Q9BQ89: FAM110A; NbExp=3; IntAct=EBI-748961, EBI-1752811;
CC O95273; A0A0S2Z6M9: FAM126A; NbExp=3; IntAct=EBI-748961, EBI-16428876;
CC O95273; Q9BYI3: FAM126A; NbExp=3; IntAct=EBI-748961, EBI-11065686;
CC O95273; Q3B820: FAM161A; NbExp=5; IntAct=EBI-748961, EBI-719941;
CC O95273; Q5TZK3: FAM74A6; NbExp=3; IntAct=EBI-748961, EBI-10247271;
CC O95273; A0A0S2Z408: FH; NbExp=3; IntAct=EBI-748961, EBI-16428900;
CC O95273; Q9ULW2: FZD10; NbExp=3; IntAct=EBI-748961, EBI-8803802;
CC O95273; Q8NHY3: GAS2L2; NbExp=3; IntAct=EBI-748961, EBI-7960826;
CC O95273; Q9Y2Q3: GSTK1; NbExp=3; IntAct=EBI-748961, EBI-1053767;
CC O95273; P02008: HBZ; NbExp=3; IntAct=EBI-748961, EBI-719843;
CC O95273; P56524-2: HDAC4; NbExp=3; IntAct=EBI-748961, EBI-11953488;
CC O95273; P09429: HMGB1; NbExp=3; IntAct=EBI-748961, EBI-389432;
CC O95273; Q02363: ID2; NbExp=4; IntAct=EBI-748961, EBI-713450;
CC O95273; Q9NV31: IMP3; NbExp=6; IntAct=EBI-748961, EBI-747481;
CC O95273; Q6NXR0: IRGC; NbExp=3; IntAct=EBI-748961, EBI-12021374;
CC O95273; Q96GY3: LIN37; NbExp=3; IntAct=EBI-748961, EBI-748884;
CC O95273; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-748961, EBI-739832;
CC O95273; P36507: MAP2K2; NbExp=3; IntAct=EBI-748961, EBI-1056930;
CC O95273; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-748961, EBI-14086479;
CC O95273; P00540: MOS; NbExp=3; IntAct=EBI-748961, EBI-1757866;
CC O95273; Q9P015: MRPL15; NbExp=7; IntAct=EBI-748961, EBI-2371967;
CC O95273; Q69YI7: NAIF1; NbExp=3; IntAct=EBI-748961, EBI-10249231;
CC O95273; P60321: NANOS2; NbExp=5; IntAct=EBI-748961, EBI-10216569;
CC O95273; Q9UMY1: NOL7; NbExp=3; IntAct=EBI-748961, EBI-2862609;
CC O95273; Q6X4W1-2: NSMF; NbExp=3; IntAct=EBI-748961, EBI-12028784;
CC O95273; O75928: PIAS2; NbExp=4; IntAct=EBI-748961, EBI-348555;
CC O95273; Q9BSJ6: PIMREG; NbExp=6; IntAct=EBI-748961, EBI-2568609;
CC O95273; Q6IQ23-2: PLEKHA7; NbExp=3; IntAct=EBI-748961, EBI-12069346;
CC O95273; P02689: PMP2; NbExp=4; IntAct=EBI-748961, EBI-10193858;
CC O95273; Q8WUT1: POLDIP3; NbExp=3; IntAct=EBI-748961, EBI-10276663;
CC O95273; Q9UGP5-2: POLL; NbExp=3; IntAct=EBI-748961, EBI-10320765;
CC O95273; Q8WWY3: PRPF31; NbExp=5; IntAct=EBI-748961, EBI-1567797;
CC O95273; P40306: PSMB10; NbExp=5; IntAct=EBI-748961, EBI-603329;
CC O95273; P10276: RARA; NbExp=3; IntAct=EBI-748961, EBI-413374;
CC O95273; P10826-2: RARB; NbExp=3; IntAct=EBI-748961, EBI-8583223;
CC O95273; P82980: RBP5; NbExp=3; IntAct=EBI-748961, EBI-3941274;
CC O95273; P46779: RPL28; NbExp=7; IntAct=EBI-748961, EBI-366357;
CC O95273; Q96EH5: RPL39L; NbExp=4; IntAct=EBI-748961, EBI-6658607;
CC O95273; Q6DKI1: RPL7L1; NbExp=3; IntAct=EBI-748961, EBI-1052408;
CC O95273; P05388: RPLP0; NbExp=4; IntAct=EBI-748961, EBI-354101;
CC O95273; P62857: RPS28; NbExp=3; IntAct=EBI-748961, EBI-353027;
CC O95273; P55042: RRAD; NbExp=5; IntAct=EBI-748961, EBI-3911502;
CC O95273; Q9NUL5-4: SHFL; NbExp=3; IntAct=EBI-748961, EBI-11955083;
CC O95273; Q7RTY0: SLC16A13; NbExp=3; IntAct=EBI-748961, EBI-12243266;
CC O95273; Q9UQ90: SPG7; NbExp=3; IntAct=EBI-748961, EBI-717201;
CC O95273; O00506: STK25; NbExp=3; IntAct=EBI-748961, EBI-618295;
CC O95273; O95926: SYF2; NbExp=3; IntAct=EBI-748961, EBI-2557644;
CC O95273; Q15170: TCEAL1; NbExp=3; IntAct=EBI-748961, EBI-2511314;
CC O95273; P15923-1: TCF3; NbExp=3; IntAct=EBI-748961, EBI-769645;
CC O95273; D3DUQ6: TEAD4; NbExp=3; IntAct=EBI-748961, EBI-10176734;
CC O95273; A0A024R4Q5: TFPT; NbExp=3; IntAct=EBI-748961, EBI-11527449;
CC O95273; Q9P2Z0: THAP10; NbExp=5; IntAct=EBI-748961, EBI-745404;
CC O95273; Q9BT49: THAP7; NbExp=4; IntAct=EBI-748961, EBI-741350;
CC O95273; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-748961, EBI-10171534;
CC O95273; Q8IUR0: TRAPPC5; NbExp=8; IntAct=EBI-748961, EBI-3246160;
CC O95273; Q5W5X9: TTC23; NbExp=3; IntAct=EBI-748961, EBI-6447954;
CC O95273; Q8TAI1: TYMSOS; NbExp=3; IntAct=EBI-748961, EBI-742060;
CC O95273; O96014: WNT11; NbExp=3; IntAct=EBI-748961, EBI-8058160;
CC O95273; O43167: ZBTB24; NbExp=3; IntAct=EBI-748961, EBI-744471;
CC O95273; Q8N5A5: ZGPAT; NbExp=4; IntAct=EBI-748961, EBI-3439227;
CC O95273; Q15973: ZNF124; NbExp=3; IntAct=EBI-748961, EBI-2555767;
CC O95273; P52737: ZNF136; NbExp=5; IntAct=EBI-748961, EBI-749129;
CC O95273; Q12901: ZNF155; NbExp=3; IntAct=EBI-748961, EBI-10747670;
CC O95273; Q14929: ZNF169; NbExp=3; IntAct=EBI-748961, EBI-10234472;
CC O95273; P17024: ZNF20; NbExp=6; IntAct=EBI-748961, EBI-717634;
CC O95273; Q9UK11: ZNF223; NbExp=3; IntAct=EBI-748961, EBI-10322867;
CC O95273; Q9UIE0: ZNF230; NbExp=3; IntAct=EBI-748961, EBI-1105361;
CC O95273; Q9HCZ1: ZNF334; NbExp=4; IntAct=EBI-748961, EBI-748965;
CC O95273; Q53GI3: ZNF394; NbExp=3; IntAct=EBI-748961, EBI-10211248;
CC O95273; Q8TAU3: ZNF417; NbExp=4; IntAct=EBI-748961, EBI-740727;
CC O95273; Q8NDP4: ZNF439; NbExp=3; IntAct=EBI-748961, EBI-747580;
CC O95273; Q8WV37: ZNF480; NbExp=3; IntAct=EBI-748961, EBI-8490675;
CC O95273; Q9ULM2: ZNF490; NbExp=3; IntAct=EBI-748961, EBI-1105370;
CC O95273; Q9H707: ZNF552; NbExp=3; IntAct=EBI-748961, EBI-2555731;
CC O95273; Q8NEP9: ZNF555; NbExp=4; IntAct=EBI-748961, EBI-10270752;
CC O95273; Q8N988-2: ZNF557; NbExp=3; IntAct=EBI-748961, EBI-10699005;
CC O95273; Q8TBZ8: ZNF564; NbExp=3; IntAct=EBI-748961, EBI-10273713;
CC O95273; Q96N58: ZNF578; NbExp=3; IntAct=EBI-748961, EBI-11955189;
CC O95273; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-748961, EBI-745520;
CC O95273; Q7L945: ZNF627; NbExp=4; IntAct=EBI-748961, EBI-2797561;
CC O95273; Q9BS34: ZNF670; NbExp=6; IntAct=EBI-748961, EBI-745276;
CC O95273; Q9H7X3: ZNF696; NbExp=3; IntAct=EBI-748961, EBI-11090299;
CC O95273; Q8N508: ZNF697; NbExp=3; IntAct=EBI-748961, EBI-10265733;
CC O95273; Q96C28: ZNF707; NbExp=7; IntAct=EBI-748961, EBI-748111;
CC O95273; A8K8V0: ZNF785; NbExp=3; IntAct=EBI-748961, EBI-3925400;
CC O95273; Q8N393: ZNF786; NbExp=3; IntAct=EBI-748961, EBI-10265203;
CC O95273; Q9Y2P0: ZNF835; NbExp=3; IntAct=EBI-748961, EBI-5667516;
CC O95273; Q96EG3: ZNF837; NbExp=3; IntAct=EBI-748961, EBI-11962574;
CC O95273; Q16670: ZSCAN26; NbExp=3; IntAct=EBI-748961, EBI-3920053;
CC O95273; B0FTY2; NbExp=3; IntAct=EBI-748961, EBI-10175366;
CC O95273; B2R4U6; NbExp=3; IntAct=EBI-748961, EBI-10175477;
CC O95273; F4ZW62; NbExp=3; IntAct=EBI-748961, EBI-10177680;
CC O95273; Q5XG85; NbExp=3; IntAct=EBI-748961, EBI-10248413;
CC O95273; Q8N9J2; NbExp=3; IntAct=EBI-748961, EBI-10268244;
CC O95273; Q96BA2; NbExp=3; IntAct=EBI-748961, EBI-10282278;
CC O95273; Q60867: Neurod1; Xeno; NbExp=4; IntAct=EBI-748961, EBI-309315;
CC O95273; PRO_0000449633 [P0DTD1]: rep; Xeno; NbExp=5; IntAct=EBI-748961, EBI-25492395;
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 Name=3;
CC IsoId=O95273-3; Sequence=VSP_032012;
CC Name=4;
CC IsoId=O95273-4; Sequence=VSP_032012, VSP_032013, VSP_032016;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expression is down-
CC regulated in a variety of tumor types including breast, colon, prostate
CC and rectal tumors, and is up-regulated in certain hepatic carcinomas.
CC {ECO:0000269|PubMed:10801854, ECO:0000269|PubMed:10854051,
CC ECO:0000269|PubMed:10915743, ECO:0000269|PubMed:15887118,
CC ECO:0000269|PubMed:17131381}.
CC -!- DEVELOPMENTAL STAGE: Expression may increase during differentiation.
CC {ECO:0000269|PubMed:10854051}.
CC -!- INDUCTION: Expression is induced by sodium butyrate, an inhibitor of
CC colon cancer cell proliferation. {ECO:0000269|PubMed:17131381}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:10854051}.
CC -!- SIMILARITY: Belongs to the CCNDBP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD11777.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAP97163.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 CCDS; CCDS10092.1; -. [O95273-1]
DR RefSeq; NP_036274.3; NM_012142.4. [O95273-1]
DR PDB; 3AY5; X-ray; 2.50 A; A=1-360.
DR PDBsum; 3AY5; -.
DR AlphaFoldDB; O95273; -.
DR SMR; O95273; -.
DR BioGRID; 117117; 149.
DR IntAct; O95273; 145.
DR MINT; O95273; -.
DR STRING; 9606.ENSP00000300213; -.
DR iPTMnet; O95273; -.
DR MetOSite; O95273; -.
DR PhosphoSitePlus; O95273; -.
DR BioMuta; CCNDBP1; -.
DR EPD; O95273; -.
DR jPOST; O95273; -.
DR MassIVE; O95273; -.
DR MaxQB; O95273; -.
DR PaxDb; O95273; -.
DR PeptideAtlas; O95273; -.
DR PRIDE; O95273; -.
DR ProteomicsDB; 50774; -. [O95273-1]
DR ProteomicsDB; 50775; -. [O95273-2]
DR ProteomicsDB; 50776; -. [O95273-3]
DR ProteomicsDB; 50777; -. [O95273-4]
DR Antibodypedia; 23815; 249 antibodies from 30 providers.
DR DNASU; 23582; -.
DR Ensembl; ENST00000300213.9; ENSP00000300213.4; ENSG00000166946.14. [O95273-1]
DR Ensembl; ENST00000565296.5; ENSP00000455419.1; ENSG00000166946.14. [O95273-2]
DR Ensembl; ENST00000566515.5; ENSP00000456797.1; ENSG00000166946.14. [O95273-2]
DR GeneID; 23582; -.
DR KEGG; hsa:23582; -.
DR MANE-Select; ENST00000300213.9; ENSP00000300213.4; NM_012142.5; NP_036274.3.
DR UCSC; uc001zqv.4; human. [O95273-1]
DR CTD; 23582; -.
DR DisGeNET; 23582; -.
DR GeneCards; CCNDBP1; -.
DR HGNC; HGNC:1587; CCNDBP1.
DR HPA; ENSG00000166946; Tissue enriched (bone).
DR MIM; 607089; gene.
DR neXtProt; NX_O95273; -.
DR OpenTargets; ENSG00000166946; -.
DR PharmGKB; PA26154; -.
DR VEuPathDB; HostDB:ENSG00000166946; -.
DR eggNOG; ENOG502SGCW; Eukaryota.
DR GeneTree; ENSGT00390000018016; -.
DR HOGENOM; CLU_067580_0_0_1; -.
DR InParanoid; O95273; -.
DR OMA; KAHGKAD; -.
DR OrthoDB; 1249310at2759; -.
DR PhylomeDB; O95273; -.
DR TreeFam; TF336444; -.
DR PathwayCommons; O95273; -.
DR SignaLink; O95273; -.
DR BioGRID-ORCS; 23582; 22 hits in 1082 CRISPR screens.
DR ChiTaRS; CCNDBP1; human.
DR GeneWiki; CCNDBP1; -.
DR GenomeRNAi; 23582; -.
DR Pharos; O95273; Tbio.
DR PRO; PR:O95273; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; O95273; protein.
DR Bgee; ENSG00000166946; Expressed in trabecular bone tissue and 185 other tissues.
DR ExpressionAtlas; O95273; baseline and differential.
DR Genevisible; O95273; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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; PTHR15492; PTHR15492; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cytoplasm;
KW Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..360
FT /note="Cyclin-D1-binding protein 1"
FT /id="PRO_0000323372"
FT REGION 2..208
FT /note="Required for interaction with CCND1"
FT REGION 2..190
FT /note="Interaction with RPLP0"
FT /evidence="ECO:0000269|PubMed:17621266"
FT REGION 2..184
FT /note="Interaction with TCF3"
FT /evidence="ECO:0000269|PubMed:10915743"
FT REGION 150..360
FT /note="Interaction with TCF3"
FT /evidence="ECO:0000269|PubMed:10915743"
FT REGION 240..360
FT /note="Interaction with RPLP0"
FT /evidence="ECO:0000269|PubMed:17621266"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VAR_SEQ 1..128
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10931946,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_032012"
FT VAR_SEQ 308..333
FT /note="SAKLVSVLKKALEITKASHVTPQPED -> VSTGFEGIATEQMGRISLITSI
FT SCK (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032013"
FT VAR_SEQ 308..309
FT /note="SA -> EP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16303743"
FT /id="VSP_032014"
FT VAR_SEQ 310..360
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16303743"
FT /id="VSP_032015"
FT VAR_SEQ 334..360
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032016"
FT CONFLICT 40
FT /note="A -> D (in Ref. 1; AAD11777)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="Q -> R (in Ref. 4; AAP97163)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="F -> S (in Ref. 8; BAC11433)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="N -> S (in Ref. 8; BAC11433)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="E -> G (in Ref. 7; BAF83396)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="K -> R (in Ref. 7; BAC87645)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="L -> M (in Ref. 1; AAD11777 and 3; AAF67182)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="K -> R (in Ref. 7; BAC11530)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="S -> I (in Ref. 7; BAF83354)"
FT /evidence="ECO:0000305"
FT HELIX 17..29
FT /evidence="ECO:0007829|PDB:3AY5"
FT HELIX 31..36
FT /evidence="ECO:0007829|PDB:3AY5"
FT HELIX 49..73
FT /evidence="ECO:0007829|PDB:3AY5"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:3AY5"
FT HELIX 82..103
FT /evidence="ECO:0007829|PDB:3AY5"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:3AY5"
FT HELIX 112..137
FT /evidence="ECO:0007829|PDB:3AY5"
FT HELIX 154..160
FT /evidence="ECO:0007829|PDB:3AY5"
FT TURN 161..164
FT /evidence="ECO:0007829|PDB:3AY5"
FT HELIX 169..197
FT /evidence="ECO:0007829|PDB:3AY5"
FT HELIX 235..265
FT /evidence="ECO:0007829|PDB:3AY5"
FT HELIX 271..295
FT /evidence="ECO:0007829|PDB:3AY5"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:3AY5"
FT HELIX 301..324
FT /evidence="ECO:0007829|PDB:3AY5"
FT HELIX 335..352
FT /evidence="ECO:0007829|PDB:3AY5"
FT HELIX 353..358
FT /evidence="ECO:0007829|PDB:3AY5"
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
