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Protein

Chromobox protein homolog 5

Gene

Cbx5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of heterochromatin that recognizes and binds histone H3 tails methylated at 'Lys-9' (H3K9me), leading to epigenetic repression. In contrast, it is excluded from chromatin when 'Tyr-41' of histone H3 is phosphorylated (H3Y41ph). Can interact with lamin-B receptor (LBR). This interaction can contribute to the association of the heterochromatin with the inner nuclear membrane. Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins (By similarity).By similarity

GO - Molecular functioni

  • chromatin binding Source: MGI
  • histone deacetylase binding Source: BHF-UCL
  • methylated histone binding Source: UniProtKB
  • protein binding, bridging Source: BHF-UCL
  • protein homodimerization activity Source: MGI
  • repressing transcription factor binding Source: BHF-UCL

GO - Biological processi

  • negative regulation of transcription, DNA-templated Source: MGI
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-983231. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
Chromobox protein homolog 5
Alternative name(s):
Heterochromatin protein 1 homolog alpha
Short name:
HP1 alpha
Gene namesi
Name:Cbx5
Synonyms:Hp1a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:109372. Cbx5.

Subcellular locationi

  • Nucleus
  • Chromosome
  • Chromosomecentromere

  • Note: Component of centromeric and pericentromeric heterochromatin. Associates with chromosomes during mitosis. Associates specifically with chromatin during metaphase and anaphase.

GO - Cellular componenti

  • chromocenter Source: MGI
  • heterochromatin Source: MGI
  • histone deacetylase complex Source: BHF-UCL
  • histone methyltransferase complex Source: BHF-UCL
  • kinetochore Source: MGI
  • nuclear chromosome, telomeric region Source: BHF-UCL
  • nuclear heterochromatin Source: MGI
  • nucleolus Source: MGI
  • nucleus Source: UniProtKB
  • pericentric heterochromatin Source: BHF-UCL
  • PML body Source: Ensembl
  • transcriptional repressor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 191191Chromobox protein homolog 5PRO_0000080209Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei11 – 111PhosphoserineBy similarity
Modified residuei12 – 121PhosphoserineBy similarity
Modified residuei13 – 131PhosphoserineBy similarity
Modified residuei14 – 141PhosphoserineCombined sources
Cross-linki32 – 32Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei92 – 921PhosphoserineCombined sources
Modified residuei93 – 931PhosphoserineCombined sources
Modified residuei95 – 951PhosphoserineBy similarity
Modified residuei97 – 971PhosphoserineBy similarity
Cross-linki102 – 102Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

Post-translational modificationi

Phosphorylation of HP1 and LBR may be responsible for some of the alterations in chromatin organization and nuclear structure which occur at various times during the cell cycle. Phosphorylated during interphase and possibly hyper-phosphorylated during mitosis (By similarity).By similarity
Ubiquitinated.By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ61686.
MaxQBiQ61686.
PaxDbiQ61686.
PeptideAtlasiQ61686.
PRIDEiQ61686.

PTM databases

iPTMnetiQ61686.
PhosphoSiteiQ61686.

Expressioni

Gene expression databases

BgeeiQ61686.
CleanExiMM_CBX5.
ExpressionAtlasiQ61686. baseline and differential.
GenevisibleiQ61686. MM.

Interactioni

Subunit structurei

Interacts directly with ATRX, CHAF1A, LBR, NIPBL, SP100 and STAM2 via the chromoshadow domain. Can interact directly with CBX3 via the chromoshadow domain. Interacts with histone H3 methylated at 'Lys-9'. Interacts with BAHD1, SETDB1, MIS12 and DSN1. Interacts with POGZ; POGZ and PXVXL motif-containing proteins such as INCENP and TRIM28 compete for interaction with CBX5. Interacts with INCENP. Interacts with CHAMP1 (By similarity). Interacts directly with TRIM28 via the chromoshadow domain. Interacts with KMT5B and KMT5C. Interacts with HP1BP3 and TRIM24. May form homodimers. Interacts with ASXL1 (By similarity).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Trim24Q641274EBI-307973,EBI-307947

GO - Molecular functioni

  • histone deacetylase binding Source: BHF-UCL
  • methylated histone binding Source: UniProtKB
  • protein binding, bridging Source: BHF-UCL
  • protein homodimerization activity Source: MGI
  • repressing transcription factor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi198538. 21 interactions.
DIPiDIP-28137N.
IntActiQ61686. 8 interactions.
MINTiMINT-191222.
STRINGi10090.ENSMUSP00000104441.

Structurei

Secondary structure

1
191
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 143Combined sources
Beta strandi22 – 3110Combined sources
Beta strandi34 – 418Combined sources
Helixi46 – 483Combined sources
Beta strandi51 – 533Combined sources
Turni54 – 563Combined sources
Helixi60 – 7314Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RVLNMR-A1-80[»]
2RVMNMR-A1-80[»]
2RVNNMR-A1-80[»]
ProteinModelPortaliQ61686.
SMRiQ61686. Positions 18-68, 112-170.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 7859Chromo 1PROSITE-ProRule annotationAdd
BLAST
Domaini121 – 17959Chromo 2; shadow subtypePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi11 – 144Poly-Ser

Sequence similaritiesi

Contains 2 chromo domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410KDV4. Eukaryota.
ENOG4111I3N. LUCA.
GeneTreeiENSGT00510000046310.
HOGENOMiHOG000220852.
HOVERGENiHBG000400.
InParanoidiQ61686.
KOiK11587.
OMAiWHAYPEE.
OrthoDBiEOG7QRQWW.
PhylomeDBiQ61686.
TreeFamiTF350503.

Family and domain databases

InterProiIPR000953. Chromo/shadow_dom.
IPR017984. Chromo_dom_subgr.
IPR023780. Chromo_domain.
IPR008251. Chromo_shadow_dom.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
[Graphical view]
PfamiPF00385. Chromo. 1 hit.
PF01393. Chromo_shadow. 1 hit.
[Graphical view]
PRINTSiPR00504. CHROMODOMAIN.
SMARTiSM00298. CHROMO. 2 hits.
SM00300. ChSh. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 2 hits.
PROSITEiPS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q61686-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKKTKRTAD SSSSEDEEEY VVEKVLDRRM VKGQVEYLLK WKGFSEEHNT
60 70 80 90 100
WEPEKNLDCP ELISEFMKKY KKMKEGENNK PREKSEGNKR KSSFSNSADD
110 120 130 140 150
IKSKKKREQS NDIARGFERG LEPEKIIGAT DSCGDLMFLM KWKDTDEADL
160 170 180 190
VLAKEANVKC PQIVIAFYEE RLTWHAYPED AENKEKESAK S
Length:191
Mass (Da):22,186
Last modified:November 1, 1997 - v1
Checksum:i8AB87E2F00DB8C40
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 681K → R in BAB31173 (PubMed:16141072).Curated
Sequence conflicti165 – 1651I → M in BAB31596 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99641 mRNA. Translation: CAA67960.1.
AF216290 mRNA. Translation: AAF80993.1.
AK008792 mRNA. Translation: BAB25897.1.
AK018349 mRNA. Translation: BAB31173.1.
AK030366 mRNA. Translation: BAC26923.1.
AK030442 mRNA. Translation: BAC26966.1.
AK032975 mRNA. Translation: BAC28107.1.
AK019198 mRNA. Translation: BAB31596.1.
BC004707 mRNA. Translation: AAH04707.1.
CCDSiCCDS37231.1.
RefSeqiNP_001070257.1. NM_001076789.1.
NP_001103686.1. NM_001110216.1.
NP_031652.1. NM_007626.3.
XP_006520435.1. XM_006520372.2.
XP_006520437.1. XM_006520374.2.
XP_006520438.1. XM_006520375.2.
XP_006520439.1. XM_006520376.2.
UniGeneiMm.262059.

Genome annotation databases

EnsembliENSMUST00000108813; ENSMUSP00000104441; ENSMUSG00000009575.
ENSMUST00000118152; ENSMUSP00000113157; ENSMUSG00000009575.
ENSMUST00000122182; ENSMUSP00000113158; ENSMUSG00000009575.
GeneIDi12419.
KEGGimmu:12419.
UCSCiuc007xxl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99641 mRNA. Translation: CAA67960.1.
AF216290 mRNA. Translation: AAF80993.1.
AK008792 mRNA. Translation: BAB25897.1.
AK018349 mRNA. Translation: BAB31173.1.
AK030366 mRNA. Translation: BAC26923.1.
AK030442 mRNA. Translation: BAC26966.1.
AK032975 mRNA. Translation: BAC28107.1.
AK019198 mRNA. Translation: BAB31596.1.
BC004707 mRNA. Translation: AAH04707.1.
CCDSiCCDS37231.1.
RefSeqiNP_001070257.1. NM_001076789.1.
NP_001103686.1. NM_001110216.1.
NP_031652.1. NM_007626.3.
XP_006520435.1. XM_006520372.2.
XP_006520437.1. XM_006520374.2.
XP_006520438.1. XM_006520375.2.
XP_006520439.1. XM_006520376.2.
UniGeneiMm.262059.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RVLNMR-A1-80[»]
2RVMNMR-A1-80[»]
2RVNNMR-A1-80[»]
ProteinModelPortaliQ61686.
SMRiQ61686. Positions 18-68, 112-170.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198538. 21 interactions.
DIPiDIP-28137N.
IntActiQ61686. 8 interactions.
MINTiMINT-191222.
STRINGi10090.ENSMUSP00000104441.

PTM databases

iPTMnetiQ61686.
PhosphoSiteiQ61686.

Proteomic databases

EPDiQ61686.
MaxQBiQ61686.
PaxDbiQ61686.
PeptideAtlasiQ61686.
PRIDEiQ61686.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000108813; ENSMUSP00000104441; ENSMUSG00000009575.
ENSMUST00000118152; ENSMUSP00000113157; ENSMUSG00000009575.
ENSMUST00000122182; ENSMUSP00000113158; ENSMUSG00000009575.
GeneIDi12419.
KEGGimmu:12419.
UCSCiuc007xxl.1. mouse.

Organism-specific databases

CTDi23468.
MGIiMGI:109372. Cbx5.

Phylogenomic databases

eggNOGiENOG410KDV4. Eukaryota.
ENOG4111I3N. LUCA.
GeneTreeiENSGT00510000046310.
HOGENOMiHOG000220852.
HOVERGENiHBG000400.
InParanoidiQ61686.
KOiK11587.
OMAiWHAYPEE.
OrthoDBiEOG7QRQWW.
PhylomeDBiQ61686.
TreeFamiTF350503.

Enzyme and pathway databases

ReactomeiR-MMU-983231. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

PROiQ61686.
SOURCEiSearch...

Gene expression databases

BgeeiQ61686.
CleanExiMM_CBX5.
ExpressionAtlasiQ61686. baseline and differential.
GenevisibleiQ61686. MM.

Family and domain databases

InterProiIPR000953. Chromo/shadow_dom.
IPR017984. Chromo_dom_subgr.
IPR023780. Chromo_domain.
IPR008251. Chromo_shadow_dom.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
[Graphical view]
PfamiPF00385. Chromo. 1 hit.
PF01393. Chromo_shadow. 1 hit.
[Graphical view]
PRINTSiPR00504. CHROMODOMAIN.
SMARTiSM00298. CHROMO. 2 hits.
SM00300. ChSh. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 2 hits.
PROSITEiPS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic control of transcription by nuclear receptors."
    le Douarin B., Nielsen A.L., Garnier J.-M., Ichinose H., Jeanmougin F., Losson R., Chambon P.
    EMBO J. 15:6701-6715(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, INTERACTION WITH HP1BP3; TRIM24 AND TRIM28.
  2. "Contiguous arrangement of p45 NFE2, HnRNP A1, and HP1 alpha on mouse chromosome 15 and human chromosome 12: evidence for suppression of these genes due to retroviral integration within the Fli-2 locus."
    Li Y.-J., Pak B.J., Higgins R.R., Lu S.-J., Ben-David Y.
    Genes Chromosomes Cancer 30:91-95(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo, Ovary and Pituitary.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "Interaction with members of the heterochromatin protein 1 (HP1) family and histone deacetylation are differentially involved in transcriptional silencing by members of the TIF1 family."
    Nielsen A.L., Ortiz J.A., You J., Oulad-Abdelghani M., Khechumian R., Gansmuller A., Chambon P., Losson R.
    EMBO J. 18:6385-6395(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRIM28.
  6. "A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin."
    Schotta G., Lachner M., Sarma K., Ebert A., Sengupta R., Reuter G., Reinberg D., Jenuwein T.
    Genes Dev. 18:1251-1262(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KMT5B AND KMT5C.
  7. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  8. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-92 AND SER-93, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiCBX5_MOUSE
AccessioniPrimary (citable) accession number: Q61686
Secondary accession number(s): Q9CS35, Q9CXD1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 6, 2016
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.