CDN2D_MOUSE
ID CDN2D_MOUSE Reviewed; 166 AA.
AC Q60773; Q60794; Q91YV3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Cyclin-dependent kinase 4 inhibitor D;
DE AltName: Full=p19-INK4d;
GN Name=Cdkn2d;
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], AND FUNCTION.
RC STRAIN=C57BL/Kaplan;
RX PubMed=7739547; DOI=10.1128/mcb.15.5.2672;
RA Hirai H., Roussel M.F., Kato J.-Y., Ashmun R.A., Sherr C.J.;
RT "Novel INK4 proteins, p19 and p18, are specific inhibitors of the cyclin D-
RT dependent kinases CDK4 and CDK6.";
RL Mol. Cell. Biol. 15:2672-2681(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=7739548; DOI=10.1128/mcb.15.5.2682;
RA Chan F.K.M., Zhang J., Cheng L., Shapiro D.N., Winoto A.;
RT "Identification of human and mouse p19, a novel CDK4 and CDK6 inhibitor
RT with homology to p16ink4.";
RL Mol. Cell. Biol. 15:2682-2688(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
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).
RN [8]
RP STRUCTURE BY NMR.
RX PubMed=9353127; DOI=10.1038/40202;
RA Luh F.Y., Archer S.J., Domaille P.J., Smith B.O., Owen D., Brotherton D.H.,
RA Raine A.R., Xu X., Brizuela L., Brenner S.L., Laue E.D.;
RT "Structure of the cyclin-dependent kinase inhibitor p19Ink4d.";
RL Nature 389:999-1003(1997).
CC -!- FUNCTION: Interacts strongly with CDK4 and CDK6 and inhibits them.
CC {ECO:0000269|PubMed:7739547, ECO:0000269|PubMed:7739548}.
CC -!- SUBUNIT: Interacts with CDK6. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CDKN2 cyclin-dependent kinase inhibitor
CC family. {ECO:0000305}.
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DR EMBL; U19597; AAC52194.1; -; mRNA.
DR EMBL; U20497; AAA85437.1; -; mRNA.
DR EMBL; AK132906; BAE21414.1; -; mRNA.
DR EMBL; AC122525; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466522; EDL25176.1; -; Genomic_DNA.
DR EMBL; BC013898; AAH13898.1; -; mRNA.
DR CCDS; CCDS22901.1; -.
DR PIR; A57379; A57379.
DR PIR; B57378; B57378.
DR RefSeq; NP_034008.2; NM_009878.3.
DR RefSeq; XP_006510031.1; XM_006509968.1.
DR PDB; 1AP7; NMR; -; A=1-166.
DR PDB; 1BLX; X-ray; 1.90 A; B=1-166.
DR PDBsum; 1AP7; -.
DR PDBsum; 1BLX; -.
DR AlphaFoldDB; Q60773; -.
DR SMR; Q60773; -.
DR CORUM; Q60773; -.
DR IntAct; Q60773; 1.
DR STRING; 10090.ENSMUSP00000083561; -.
DR iPTMnet; Q60773; -.
DR PhosphoSitePlus; Q60773; -.
DR EPD; Q60773; -.
DR PaxDb; Q60773; -.
DR PRIDE; Q60773; -.
DR ProteomicsDB; 283868; -.
DR Antibodypedia; 4404; 301 antibodies from 34 providers.
DR DNASU; 12581; -.
DR Ensembl; ENSMUST00000215619; ENSMUSP00000150701; ENSMUSG00000096472.
DR GeneID; 12581; -.
DR KEGG; mmu:12581; -.
DR UCSC; uc009okw.1; mouse.
DR CTD; 1032; -.
DR MGI; MGI:105387; Cdkn2d.
DR VEuPathDB; HostDB:ENSMUSG00000096472; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000159801; -.
DR HOGENOM; CLU_000134_37_0_1; -.
DR InParanoid; Q60773; -.
DR OMA; LHQEFVH; -.
DR OrthoDB; 1453965at2759; -.
DR PhylomeDB; Q60773; -.
DR TreeFam; TF333311; -.
DR BioGRID-ORCS; 12581; 1 hit in 113 CRISPR screens.
DR EvolutionaryTrace; Q60773; -.
DR PRO; PR:Q60773; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q60773; protein.
DR Bgee; ENSMUSG00000096472; Expressed in granulocyte and 258 other tissues.
DR ExpressionAtlas; Q60773; baseline and differential.
DR Genevisible; Q60773; MM.
DR GO; GO:0097129; C:cyclin D2-CDK4 complex; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; IPI:MGI.
DR GO; GO:0048102; P:autophagic cell death; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000731; P:DNA synthesis involved in DNA repair; ISO:MGI.
DR GO; GO:1902807; P:negative regulation of cell cycle G1/S phase transition; IDA:MGI.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; ISO:MGI.
DR GO; GO:0042326; P:negative regulation of phosphorylation; ISO:MGI.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0032526; P:response to retinoic acid; ISO:MGI.
DR GO; GO:0009411; P:response to UV; ISO:MGI.
DR GO; GO:0033280; P:response to vitamin D; ISO:MGI.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR Pfam; PF13857; Ank_5; 1.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ANK repeat; Cell cycle; Cytoplasm; Nucleus;
KW Reference proteome; Repeat; Tumor suppressor.
FT CHAIN 1..166
FT /note="Cyclin-dependent kinase 4 inhibitor D"
FT /id="PRO_0000144189"
FT REPEAT 41..69
FT /note="ANK 1"
FT REPEAT 73..102
FT /note="ANK 2"
FT REPEAT 106..135
FT /note="ANK 3"
FT REPEAT 138..165
FT /note="ANK 4"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P55273"
FT CONFLICT 16
FT /note="A -> R (in Ref. 1; AAC52194)"
FT /evidence="ECO:0000305"
FT CONFLICT 17
FT /note="A -> P (in Ref. 2; AAA85437)"
FT /evidence="ECO:0000305"
FT HELIX 7..17
FT /evidence="ECO:0007829|PDB:1BLX"
FT HELIX 21..29
FT /evidence="ECO:0007829|PDB:1BLX"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:1BLX"
FT HELIX 54..62
FT /evidence="ECO:0007829|PDB:1BLX"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:1AP7"
FT HELIX 77..84
FT /evidence="ECO:0007829|PDB:1BLX"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:1BLX"
FT HELIX 110..117
FT /evidence="ECO:0007829|PDB:1BLX"
FT HELIX 120..126
FT /evidence="ECO:0007829|PDB:1BLX"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:1BLX"
FT HELIX 142..148
FT /evidence="ECO:0007829|PDB:1BLX"
FT HELIX 152..160
FT /evidence="ECO:0007829|PDB:1BLX"
SQ SEQUENCE 166 AA; 17809 MW; 7B95D6C2294F9259 CRC64;
MLLEEVCVGD RLSGAAARGD VQEVRRLLHR ELVHPDALNR FGKTALQVMM FGSPAVALEL
LKQGASPNVQ DASGTSPVHD AARTGFLDTL KVLVEHGADV NALDSTGSLP IHLAIREGHS
SVVSFLAPES DLHHRDASGL TPLELARQRG AQNLMDILQG HMMIPM
