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 27-MAR-2024, entry version 154. 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 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., 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; 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; Q9BYI3: HYCC1; NbExp=3; IntAct=EBI-748961, EBI-11065686; 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; 9606-ENSP00000300213; -. DR PeptideAtlas; O95273; -. DR ProteomicsDB; 50774; -. [O95273-1] DR ProteomicsDB; 50775; -. [O95273-2] DR ProteomicsDB; 50776; -. [O95273-3] DR ProteomicsDB; 50777; -. [O95273-4] DR Pumba; O95273; -. DR Antibodypedia; 23815; 265 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 AGR; HGNC:1587; -. DR CTD; 23582; -. DR DisGeNET; 23582; -. DR GeneCards; CCNDBP1; -. DR HGNC; HGNC:1587; CCNDBP1. DR HPA; ENSG00000166946; Group enriched (bone marrow, brain). 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; GCPNNQD; -. DR OrthoDB; 3022479at2759; -. DR PhylomeDB; O95273; -. DR TreeFam; TF336444; -. DR PathwayCommons; O95273; -. DR SignaLink; O95273; -. DR BioGRID-ORCS; 23582; 25 hits in 1160 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 187 other cell types or tissues. DR ExpressionAtlas; O95273; baseline and differential. 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 Gene3D; 1.20.1410.10; I/LWEQ domain; 1. DR Gene3D; 1.20.1420.10; Talin, central domain; 1. DR InterPro; IPR026907; GCIP-like. DR InterPro; IPR049317; GCIP-like_N. DR InterPro; IPR049318; GCIP_C. DR PANTHER; PTHR15492; CYCLIN D1-BINDING PROTEIN 1; 1. DR PANTHER; PTHR15492:SF4; CYCLIN-D1-BINDING PROTEIN 1; 1. DR Pfam; PF20936; GCIP_C; 1. DR Pfam; PF13324; GCIP_N; 1. DR Genevisible; O95273; HS. 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 //