CCDB1_MOUSE
ID CCDB1_MOUSE Reviewed; 356 AA.
AC Q3TVC7; Q3UMI3; Q61162; Q99JA7; Q99KG4;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Cyclin-D1-binding protein 1;
DE AltName: Full=Grap2 and cyclin-D-interacting protein;
DE AltName: Full=Maternal Id-like protein;
DE AltName: Full=Stage specific embryonic cDNA-8 protein;
DE Short=SSEC-8;
GN Name=Ccndbp1; Synonyms=Dip1, Gcip, Maid;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6 X DBA/2;
RX PubMed=9186056;
RX DOI=10.1002/(sici)1097-0177(199706)209:2<217::aid-aja7>3.0.co;2-l;
RA Hwang S.-Y., Oh B., Fuechtbauer A., Fuechtbauer E.-M., Johnson K.R.,
RA Solter D., Knowles B.B.;
RT "Maid: a maternally transcribed novel gene encoding a potential negative
RT regulator of bHLH proteins in the mouse egg and zygote.";
RL Dev. Dyn. 209:217-226(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Cerebellum, Dendritic cell, Embryo, Lung, and Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [5]
RP FUNCTION, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=17256742; DOI=10.1002/hep.21461;
RA Sonnenberg-Riethmacher E., Wuestefeld T., Miehe M., Trautwein C.,
RA Riethmacher D.;
RT "Maid (GCIP) is involved in cell cycle control of hepatocytes.";
RL Hepatology 45:404-411(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). May be required for hepatocyte
CC proliferation. {ECO:0000250, ECO:0000269|PubMed:17256742}.
CC -!- SUBUNIT: Interacts with CCND1 and GRAP2. May also interact with COPS5,
CC RPLP0, SIRT6, SYF2 and TCF3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3TVC7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3TVC7-2; Sequence=VSP_032017;
CC Name=3;
CC IsoId=Q3TVC7-3; Sequence=VSP_032018;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in brain, intestine,
CC muscle and ovary and at lower levels in heart, kidney, liver, lung,
CC spleen and testis. {ECO:0000269|PubMed:9186056}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in the unfertilized egg.
CC Expression is reduced at the two cell and blastocyst stages. Expressed
CC in the liver, CNS and dorsal root ganglia throughout organogenesis.
CC Also expressed in the intestine, kidney, lung, nasal cavities and
CC thymus from 13 dpc. {ECO:0000269|PubMed:17256742,
CC ECO:0000269|PubMed:9186056}.
CC -!- INDUCTION: Expression is induced by partial hepatectomy.
CC {ECO:0000269|PubMed:17256742}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CCNDBP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB58118.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U50734; AAB58118.1; ALT_FRAME; mRNA.
DR EMBL; AK144883; BAE26115.1; -; mRNA.
DR EMBL; AK154285; BAE32489.1; -; mRNA.
DR EMBL; AK160205; BAE35692.1; -; mRNA.
DR EMBL; AK163150; BAE37214.1; -; mRNA.
DR EMBL; AK167345; BAE39444.1; -; mRNA.
DR EMBL; AL844548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001984; AAH01984.2; -; mRNA.
DR EMBL; BC004673; AAH04673.1; -; mRNA.
DR EMBL; BC005802; AAH05802.1; -; mRNA.
DR CCDS; CCDS38213.1; -. [Q3TVC7-1]
DR RefSeq; NP_034891.2; NM_010761.2. [Q3TVC7-1]
DR AlphaFoldDB; Q3TVC7; -.
DR SMR; Q3TVC7; -.
DR IntAct; Q3TVC7; 2.
DR MINT; Q3TVC7; -.
DR STRING; 10090.ENSMUSP00000062496; -.
DR PhosphoSitePlus; Q3TVC7; -.
DR EPD; Q3TVC7; -.
DR MaxQB; Q3TVC7; -.
DR PaxDb; Q3TVC7; -.
DR PeptideAtlas; Q3TVC7; -.
DR PRIDE; Q3TVC7; -.
DR ProteomicsDB; 281322; -. [Q3TVC7-1]
DR ProteomicsDB; 281323; -. [Q3TVC7-2]
DR ProteomicsDB; 281324; -. [Q3TVC7-3]
DR Antibodypedia; 23815; 249 antibodies from 30 providers.
DR DNASU; 17151; -.
DR Ensembl; ENSMUST00000060455; ENSMUSP00000062496; ENSMUSG00000023572. [Q3TVC7-1]
DR Ensembl; ENSMUST00000099489; ENSMUSP00000097088; ENSMUSG00000023572. [Q3TVC7-2]
DR Ensembl; ENSMUST00000171260; ENSMUSP00000125961; ENSMUSG00000023572. [Q3TVC7-3]
DR GeneID; 17151; -.
DR KEGG; mmu:17151; -.
DR UCSC; uc008lxg.1; mouse. [Q3TVC7-1]
DR CTD; 23582; -.
DR MGI; MGI:109595; Ccndbp1.
DR VEuPathDB; HostDB:ENSMUSG00000023572; -.
DR eggNOG; ENOG502SGCW; Eukaryota.
DR GeneTree; ENSGT00390000018016; -.
DR HOGENOM; CLU_067580_0_0_1; -.
DR InParanoid; Q3TVC7; -.
DR OMA; KAHGKAD; -.
DR OrthoDB; 1249310at2759; -.
DR PhylomeDB; Q3TVC7; -.
DR TreeFam; TF336444; -.
DR BioGRID-ORCS; 17151; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q3TVC7; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q3TVC7; protein.
DR Bgee; ENSMUSG00000023572; Expressed in blood and 253 other tissues.
DR ExpressionAtlas; Q3TVC7; baseline and differential.
DR Genevisible; Q3TVC7; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO: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 Acetylation; Alternative splicing; Cell cycle; Cytoplasm; Nucleus;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O95273"
FT CHAIN 2..356
FT /note="Cyclin-D1-binding protein 1"
FT /id="PRO_0000323374"
FT REGION 2..205
FT /note="Required for interaction with CCND1"
FT /evidence="ECO:0000250"
FT REGION 2..187
FT /note="Interaction with RPLP0"
FT /evidence="ECO:0000250"
FT REGION 2..181
FT /note="Interaction with TCF3"
FT /evidence="ECO:0000250"
FT REGION 147..356
FT /note="Interaction with TCF3"
FT /evidence="ECO:0000250"
FT REGION 198..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..356
FT /note="Interaction with RPLP0"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O95273"
FT VAR_SEQ 1..47
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9186056"
FT /id="VSP_032017"
FT VAR_SEQ 304..349
FT /note="SAKLVSVLIKALEITKASHVSPHPGDSWIPLLINAVDHCMNRIKAL -> VN
FT VWTLRGSVTLPDYPETVHSLNLELVWQQASPAIALPLCPQRWSNRYTHGHTSFFYVCLG
FT LNSCPYACKHS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032018"
SQ SEQUENCE 356 AA; 39356 MW; E112C12AB12B7568 CRC64;
MASSTAAVPF LAPPLEQLRH LAEELRSLLP RVRVGEAQET AEEFNREMFW RRLNEAAVKV
NGEATVLTTH FSKLPWPSPQ ETQRICEQVR IAIEEIIIVY YSLPKDQGIT LRKLVRNAAL
DIVDGMAQLL EVLLTAPSQS TENGDLISCN SVSVACQQVP EIPKDNKAAA LLMLTKSVDF
VKDAHEEMEQ AVEECDPYSG LLNDSEDNSD SHSDEDGVLG LPSNRDSYWS EEDQELIIPC
LALVRASRAS LKKIRILVAE NGKKDEVAQL DDIVDISDEI SPSVDDLVLS IYPPVCHLTV
RISSAKLVSV LIKALEITKA SHVSPHPGDS WIPLLINAVD HCMNRIKALT QRAAEL
