CBX5_MOUSE
ID CBX5_MOUSE Reviewed; 191 AA.
AC Q61686; Q9CS35; Q9CXD1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Chromobox protein homolog 5;
DE AltName: Full=Heterochromatin protein 1 homolog alpha;
DE Short=HP1 alpha;
GN Name=Cbx5; Synonyms=Hp1a;
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], SUBUNIT, AND INTERACTION WITH HP1BP3; TRIM24
RP AND TRIM28.
RX PubMed=8978696;
RA le Douarin B., Nielsen A.L., Garnier J.-M., Ichinose H., Jeanmougin F.,
RA Losson R., Chambon P.;
RT "A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic
RT control of transcription by nuclear receptors.";
RL EMBO J. 15:6701-6715(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11107181;
RX DOI=10.1002/1098-2264(2000)9999:9999<::aid-gcc1058>3.0.co;2-a;
RA Li Y.-J., Pak B.J., Higgins R.R., Lu S.-J., Ben-David Y.;
RT "Contiguous arrangement of p45 NFE2, HnRNP A1, and HP1 alpha on mouse
RT chromosome 15 and human chromosome 12: evidence for suppression of these
RT genes due to retroviral integration within the Fli-2 locus.";
RL Genes Chromosomes Cancer 30:91-95(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Ovary, and Pituitary;
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 MRNA].
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 INTERACTION WITH TRIM28.
RX PubMed=10562550; DOI=10.1093/emboj/18.22.6385;
RA Nielsen A.L., Ortiz J.A., You J., Oulad-Abdelghani M., Khechumian R.,
RA Gansmuller A., Chambon P., Losson R.;
RT "Interaction with members of the heterochromatin protein 1 (HP1) family and
RT histone deacetylation are differentially involved in transcriptional
RT silencing by members of the TIF1 family.";
RL EMBO J. 18:6385-6395(1999).
RN [6]
RP INTERACTION WITH KMT5B AND KMT5C.
RX PubMed=15145825; DOI=10.1101/gad.300704;
RA Schotta G., Lachner M., Sarma K., Ebert A., Sengupta R., Reuter G.,
RA Reinberg D., Jenuwein T.;
RT "A silencing pathway to induce H3-K9 and H4-K20 trimethylation at
RT constitutive heterochromatin.";
RL Genes Dev. 18:1251-1262(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-92 AND SER-93, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [10]
RP INTERACTION WITH SMYD5.
RX PubMed=28250819; DOI=10.1186/s13072-017-0115-7;
RA Kidder B.L., Hu G., Cui K., Zhao K.;
RT "SMYD5 regulates H4K20me3-marked heterochromatin to safeguard ES cell self-
RT renewal and prevent spurious differentiation.";
RL Epigenetics Chromatin 10:8-8(2017).
CC -!- FUNCTION: Component of heterochromatin that recognizes and binds
CC histone H3 tails methylated at 'Lys-9' (H3K9me), leading to epigenetic
CC repression. In contrast, it is excluded from chromatin when 'Tyr-41' of
CC histone H3 is phosphorylated (H3Y41ph). Can interact with lamin-B
CC receptor (LBR). This interaction can contribute to the association of
CC the heterochromatin with the inner nuclear membrane. Involved in the
CC formation of functional kinetochore through interaction with MIS12
CC complex proteins (By similarity). {ECO:0000250|UniProtKB:P45973}.
CC -!- SUBUNIT: Interacts directly with ATRX, CHAF1A, LBR, NIPBL, SP100 and
CC STAM2 via the chromoshadow domain. Can interact directly with CBX3 via
CC the chromoshadow domain. Interacts with histone H3 methylated at 'Lys-
CC 9'. Interacts with BAHD1, SETDB1, MIS12 and DSN1. Interacts with POGZ;
CC POGZ and PXVXL motif-containing proteins such as INCENP and TRIM28
CC compete for interaction with CBX5. Interacts with INCENP. Interacts
CC with CHAMP1 (By similarity). Interacts directly with TRIM28 via the
CC chromoshadow domain (PubMed:8978696). Interacts with KMT5B and KMT5C
CC (PubMed:15145825). Interacts with HP1BP3 and TRIM24 (PubMed:8978696).
CC Interacts with PRR14 (via N-terminus) (By similarity). Interacts with
CC RRP1B (By similarity). Interacts with HNRNPU (via C-terminus); this
CC interaction is, at least in part, RNA-dependent (By similarity).
CC Interacts with LRIF1 (via PxVxL motif) (By similarity). Interacts with
CC ZNF263; recruited to the SIX3 promoter along with other proteins
CC involved in chromatin modification and transcriptional corepression
CC where it contributes to transcriptional repression (By similarity). May
CC form homodimers (PubMed:8978696). Interacts with SMYD5
CC (PubMed:28250819). {ECO:0000250|UniProtKB:P45973,
CC ECO:0000269|PubMed:15145825, ECO:0000269|PubMed:28250819,
CC ECO:0000269|PubMed:8978696}.
CC -!- INTERACTION:
CC Q61686; Q8BUH8: Senp7; NbExp=4; IntAct=EBI-307973, EBI-15972382;
CC Q61686; Q64127: Trim24; NbExp=4; IntAct=EBI-307973, EBI-307947;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P45973}.
CC Chromosome. Chromosome, centromere. Note=Colocalizes with HNRNPU in the
CC nucleus (By similarity). Component of centromeric and pericentromeric
CC heterochromatin. Associates with chromosomes during mitosis. Associates
CC specifically with chromatin during metaphase and anaphase.
CC {ECO:0000250|UniProtKB:P45973}.
CC -!- PTM: Phosphorylation of HP1 and LBR may be responsible for some of the
CC alterations in chromatin organization and nuclear structure which occur
CC at various times during the cell cycle. Phosphorylated during
CC interphase and possibly hyper-phosphorylated during mitosis.
CC {ECO:0000250|UniProtKB:P45973}.
CC -!- PTM: Ubiquitinated. {ECO:0000250|UniProtKB:P45973}.
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DR EMBL; X99641; CAA67960.1; -; mRNA.
DR EMBL; AF216290; AAF80993.1; -; mRNA.
DR EMBL; AK008792; BAB25897.1; -; mRNA.
DR EMBL; AK018349; BAB31173.1; -; mRNA.
DR EMBL; AK030366; BAC26923.1; -; mRNA.
DR EMBL; AK030442; BAC26966.1; -; mRNA.
DR EMBL; AK032975; BAC28107.1; -; mRNA.
DR EMBL; AK019198; BAB31596.1; -; mRNA.
DR EMBL; BC004707; AAH04707.1; -; mRNA.
DR CCDS; CCDS37231.1; -.
DR RefSeq; NP_001070257.1; NM_001076789.1.
DR RefSeq; NP_001103686.1; NM_001110216.1.
DR RefSeq; NP_031652.1; NM_007626.3.
DR RefSeq; XP_006520435.1; XM_006520372.3.
DR RefSeq; XP_006520437.1; XM_006520374.3.
DR RefSeq; XP_006520438.1; XM_006520375.3.
DR RefSeq; XP_006520439.1; XM_006520376.3.
DR PDB; 2RVL; NMR; -; A=1-80.
DR PDB; 2RVM; NMR; -; A=1-80.
DR PDB; 2RVN; NMR; -; A=1-80.
DR PDBsum; 2RVL; -.
DR PDBsum; 2RVM; -.
DR PDBsum; 2RVN; -.
DR AlphaFoldDB; Q61686; -.
DR BMRB; Q61686; -.
DR SMR; Q61686; -.
DR BioGRID; 198538; 75.
DR DIP; DIP-28137N; -.
DR IntAct; Q61686; 13.
DR MINT; Q61686; -.
DR STRING; 10090.ENSMUSP00000113157; -.
DR iPTMnet; Q61686; -.
DR PhosphoSitePlus; Q61686; -.
DR EPD; Q61686; -.
DR jPOST; Q61686; -.
DR MaxQB; Q61686; -.
DR PaxDb; Q61686; -.
DR PeptideAtlas; Q61686; -.
DR PRIDE; Q61686; -.
DR ProteomicsDB; 265572; -.
DR Antibodypedia; 4311; 941 antibodies from 45 providers.
DR DNASU; 12419; -.
DR Ensembl; ENSMUST00000108813; ENSMUSP00000104441; ENSMUSG00000009575.
DR Ensembl; ENSMUST00000118152; ENSMUSP00000113157; ENSMUSG00000009575.
DR Ensembl; ENSMUST00000122182; ENSMUSP00000113158; ENSMUSG00000009575.
DR GeneID; 12419; -.
DR KEGG; mmu:12419; -.
DR UCSC; uc007xxl.1; mouse.
DR CTD; 23468; -.
DR MGI; MGI:109372; Cbx5.
DR VEuPathDB; HostDB:ENSMUSG00000009575; -.
DR eggNOG; KOG1911; Eukaryota.
DR GeneTree; ENSGT00940000158801; -.
DR HOGENOM; CLU_045874_1_0_1; -.
DR InParanoid; Q61686; -.
DR OMA; KCPLKML; -.
DR OrthoDB; 1628171at2759; -.
DR PhylomeDB; Q61686; -.
DR TreeFam; TF350503; -.
DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR BioGRID-ORCS; 12419; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Cbx5; mouse.
DR PRO; PR:Q61686; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q61686; protein.
DR Bgee; ENSMUSG00000009575; Expressed in floor plate of midbrain and 281 other tissues.
DR ExpressionAtlas; Q61686; baseline and differential.
DR Genevisible; Q61686; MM.
DR GO; GO:0010369; C:chromocenter; IDA:MGI.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:BHF-UCL.
DR GO; GO:0000792; C:heterochromatin; IDA:MGI.
DR GO; GO:0000118; C:histone deacetylase complex; IDA:BHF-UCL.
DR GO; GO:0035097; C:histone methyltransferase complex; IDA:BHF-UCL.
DR GO; GO:0000776; C:kinetochore; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:BHF-UCL.
DR GO; GO:0016605; C:PML body; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0090734; C:site of DNA damage; ISS:UniProtKB.
DR GO; GO:0017053; C:transcription repressor complex; IDA:BHF-UCL.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0035064; F:methylated histone binding; IPI:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISS:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:BHF-UCL.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR017984; Chromo_dom_subgr.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR008251; Chromo_shadow_dom.
DR InterPro; IPR023779; Chromodomain_CS.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF01393; Chromo_shadow; 1.
DR PRINTS; PR00504; CHROMODOMAIN.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00300; ChSh; 1.
DR SUPFAM; SSF54160; SSF54160; 2.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Centromere; Chromosome; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..191
FT /note="Chromobox protein homolog 5"
FT /id="PRO_0000080209"
FT DOMAIN 20..78
FT /note="Chromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 121..179
FT /note="Chromo 2; shadow subtype"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P45973"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P45973"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P45973"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 40
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13185"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P45973"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P45973"
FT CROSSLNK 32
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P45973"
FT CROSSLNK 91
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P45973"
FT CROSSLNK 102
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P45973"
FT CROSSLNK 106
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P45973"
FT CROSSLNK 154
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P45973"
FT CROSSLNK 184
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P45973"
FT CONFLICT 68
FT /note="K -> R (in Ref. 3; BAB31173)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="I -> M (in Ref. 3; BAB31596)"
FT /evidence="ECO:0000305"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:2RVL"
FT STRAND 22..31
FT /evidence="ECO:0007829|PDB:2RVL"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:2RVL"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:2RVL"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:2RVL"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:2RVL"
FT HELIX 60..73
FT /evidence="ECO:0007829|PDB:2RVL"
SQ SEQUENCE 191 AA; 22186 MW; 8AB87E2F00DB8C40 CRC64;
MGKKTKRTAD SSSSEDEEEY VVEKVLDRRM VKGQVEYLLK WKGFSEEHNT WEPEKNLDCP
ELISEFMKKY KKMKEGENNK PREKSEGNKR KSSFSNSADD IKSKKKREQS NDIARGFERG
LEPEKIIGAT DSCGDLMFLM KWKDTDEADL VLAKEANVKC PQIVIAFYEE RLTWHAYPED
AENKEKESAK S
