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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)DescriptionActionsGraphical viewLength
ChainiPRO_00000802091 – 191Chromobox protein homolog 5Add BLAST191

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei11PhosphoserineBy similarity1
Modified residuei12PhosphoserineBy similarity1
Modified residuei13PhosphoserineBy similarity1
Modified residuei14PhosphoserineCombined sources1
Cross-linki32Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei92PhosphoserineCombined sources1
Modified residuei93PhosphoserineCombined sources1
Modified residuei95PhosphoserineBy similarity1
Modified residuei97PhosphoserineBy similarity1
Cross-linki102Glycyl 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.
PhosphoSitePlusiQ61686.

Expressioni

Gene expression databases

BgeeiENSMUSG00000009575.
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 interactors.
DIPiDIP-28137N.
IntActiQ61686. 8 interactors.
MINTiMINT-191222.
STRINGi10090.ENSMUSP00000104441.

Structurei

Secondary structure

1191
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi12 – 14Combined sources3
Beta strandi22 – 31Combined sources10
Beta strandi34 – 41Combined sources8
Helixi46 – 48Combined sources3
Beta strandi51 – 53Combined sources3
Turni54 – 56Combined sources3
Helixi60 – 73Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2RVLNMR-A1-80[»]
2RVMNMR-A1-80[»]
2RVNNMR-A1-80[»]
ProteinModelPortaliQ61686.
SMRiQ61686.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 78Chromo 1PROSITE-ProRule annotationAdd BLAST59
Domaini121 – 179Chromo 2; shadow subtypePROSITE-ProRule annotationAdd BLAST59

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi11 – 14Poly-Ser4

Sequence similaritiesi

Contains 2 chromo domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410KDV4. Eukaryota.
ENOG4111I3N. LUCA.
GeneTreeiENSGT00510000046310.
HOGENOMiHOG000220852.
HOVERGENiHBG000400.
InParanoidiQ61686.
KOiK11587.
OMAiWHAYPEE.
OrthoDBiEOG091G0RBS.
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)DescriptionActionsGraphical viewLength
Sequence conflicti68K → R in BAB31173 (PubMed:16141072).Curated1
Sequence conflicti165I → M in BAB31596 (PubMed:16141072).Curated1

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_006520372.3.
XP_006520437.1. XM_006520374.3.
XP_006520438.1. XM_006520375.3.
XP_006520439.1. XM_006520376.3.
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_006520372.3.
XP_006520437.1. XM_006520374.3.
XP_006520438.1. XM_006520375.3.
XP_006520439.1. XM_006520376.3.
UniGeneiMm.262059.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2RVLNMR-A1-80[»]
2RVMNMR-A1-80[»]
2RVNNMR-A1-80[»]
ProteinModelPortaliQ61686.
SMRiQ61686.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiQ61686.
PhosphoSitePlusiQ61686.

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.
OrthoDBiEOG091G0RBS.
PhylomeDBiQ61686.
TreeFamiTF350503.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ61686.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000009575.
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...

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: November 2, 2016
This is version 148 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.