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P83917 (CBX1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chromobox protein homolog 1
Alternative name(s):
Heterochromatin protein 1 homolog beta
Short name=HP1 beta
Heterochromatin protein p25
M31
Modifier 1 protein
Gene names
Name:Cbx1
Synonyms:Cbx
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length185 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of heterochromatin. Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. Interaction with lamin B receptor (LBR) can contribute to the association of the heterochromatin with the inner nuclear membrane.

Subunit structure

Homodimer. Interacts directly with CHAF1A, EMSY, LBR, TIF1/TIF1A and TRIM28/TIF1B PXVXL motif via the chromoshadow domain. Interacts directly with histone H3 methylated at 'Lys-9' via the chromo domain. Interacts with SUV39H1, SETDB1, SUV420H1 and SUV420H2. Interacts with PRDM6. Interacts with POGZ. Interacts with CHAMP1. Interacts with ASXL1 By similarity. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.13

Subcellular location

Nucleus By similarity. Note: Unassociated with chromosomes during mitosis By similarity.

Tissue specificity

In all adult and embryonic tissues. Ref.1

Post-translational modification

Not phosphorylated By similarity.

Ubiquitinated.

Sequence similarities

Contains 2 chromo domains.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 185185Chromobox protein homolog 1
PRO_0000080200

Regions

Domain21 – 7959Chromo 1
Domain117 – 17559Chromo 2; shadow subtype

Sites

Binding site211Histone H3K9me2
Binding site231Histone H3A7
Binding site401Histone H3A7
Binding site421Histone H3A7
Binding site421Histone H3K9me2
Binding site451Histone H3K9me2
Binding site581Histone H3A7
Binding site601Histone H3A7
Binding site1251PxVxL motif
Binding site1261PxVxL motif
Binding site1351PxVxL motif
Binding site1461PxVxL motif
Binding site1631PxVxL motif
Binding site1671PxVxL motif
Binding site1681PxVxL motif
Binding site1701PxVxL motif

Amino acid modifications

Modified residue891Phosphoserine By similarity
Modified residue911Phosphoserine By similarity
Modified residue1751Phosphoserine By similarity

Experimental info

Mutagenesis231V → M: Abolishes interaction with SUV39H1. Ref.7
Mutagenesis261V → R: Abolishes interaction with SUV39H1. Ref.7
Mutagenesis1611I → E: Abolishes homodimer formation.
Mutagenesis1641Y → E: Abolishes homodimer formation.

Secondary structure

............................ 185
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P83917 [UniParc].

Last modified June 7, 2004. Version 1.
Checksum: BE687AF9C66E48E3

FASTA18521,418
        10         20         30         40         50         60 
MGKKQNKKKV EEVLEEEEEE YVVEKVLDRR VVKGKVEYLL KWKGFSDEDN TWEPEENLDC 

        70         80         90        100        110        120 
PDLIAEFLQS QKTAHETDKS EGGKRKADSD SEDKGEESKP KKKKEESEKP RGFARGLEPE 

       130        140        150        160        170        180 
RIIGATDSSG ELMFLMKWKN SDEADLVPAK EANVKCPQVV ISFYEERLTW HSYPSEDDDK 


KDDKN 

« Hide

References

« Hide 'large scale' references
[1]"A sequence motif found in a Drosophila heterochromatin protein is conserved in animals and plants."
Singh P.B., Miller J.R., Pearce J., Kothary R., Burton R.D., Paro R., James T.C., Gaunt S.J.
Nucleic Acids Res. 19:789-794(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DOMAIN.
Strain: C57BL/6.
Tissue: Embryo.
[2]"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. expand/collapse author list , 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: Head.
[3]"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: INTERACTION WITH TIF1A.
[4]"Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31."
Aagaard L., Laible G., Selenko P., Schmid M., Dorn R., Schotta G., Kuhfittig S., Wolf A., Lebersorger A., Singh P.B., Reuter G., Jenuwein T.
EMBO J. 18:1923-1938(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SUV39H1.
[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]"Histones H3/H4 form a tight complex with the inner nuclear membrane protein LBR and heterochromatin protein 1."
Polioudaki H., Kourmouli N., Drosou V., Bakou A., Theodoropoulos P.A., Singh P.B., Giannakouros T., Georgatos S.D.
EMBO Rep. 2:920-925(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HISTONE H3 AND LBR.
[7]"Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins."
Lachner M., O'Carroll D., Rea S., Mechtler K., Jenuwein T.
Nature 410:116-120(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HISTONE H3 LYS-9, MUTAGENESIS OF VAL-23 AND VAL-26.
[8]"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 SUV420H1 AND SUV420H2.
[9]"PRISM/PRDM6, a transcriptional repressor that promotes the proliferative gene program in smooth muscle cells."
Davis C.A., Haberland M., Arnold M.A., Sutherland L.B., McDonald O.G., Richardson J.A., Childs G., Harris S., Owens G.K., Olson E.N.
Mol. Cell. Biol. 26:2626-2636(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRDM6.
[10]"Structure of the chromatin binding (chromo) domain from mouse modifier protein 1."
Ball L.J., Murzina N.V., Broadhurst R.W., Raine A.R., Archer S.J., Stott F.J., Murzin A.G., Singh P.B., Domaille P.J., Laue E.D.
EMBO J. 16:2473-2481(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 10-80.
[11]"The structure of mouse HP1 suggests a unique mode of single peptide recognition by the shadow chromo domain dimer."
Brasher S.V., Smith B.O., Fogh R.H., Nietlispach D., Thiru A., Nielsen P.R., Broadhurst R.W., Ball L.J., Murzina N.V., Laue E.D.
EMBO J. 19:1587-1597(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 104-171, SUBUNIT, INTERACTION WITH CHAF1A AND TRIM28, MUTAGENESIS.
[12]"Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9."
Nielsen P.R., Nietlispach D., Mott H.R., Callaghan J., Bannister A., Kouzarides T., Murzin A.G., Murzina N.V., Laue E.D.
Nature 416:103-107(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 10-80.
[13]"Structural basis of HP1/PXVXL motif peptide interactions and HP1 localisation to heterochromatin."
Thiru A., Nietlispach D., Mott H.R., Okuwaki M., Lyon D., Nielsen P.R., Hirshberg M., Verreault A., Murzina N.V., Laue E.D.
EMBO J. 23:489-499(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 104-175, SUBUNIT, INTERACTION WITH CHAF1A.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X56690 mRNA. Translation: CAA40018.1.
AK014215 mRNA. Translation: BAB29211.1.
CCDSCCDS25303.1.
PIRS26847.
RefSeqNP_031648.1. NM_007622.3.
XP_006532162.1. XM_006532099.1.
XP_006532163.1. XM_006532100.1.
UniGeneMm.29055.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AP0NMR-A10-80[»]
1DZ1NMR-A/B104-171[»]
1GUWNMR-A10-80[»]
1S4ZNMR-A/B104-176[»]
ProteinModelPortalP83917.
SMRP83917. Positions 27-80, 110-175.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198534. 38 interactions.
DIPDIP-30892N.
IntActP83917. 37 interactions.
MINTMINT-191134.

PTM databases

PhosphoSiteP83917.

2D gel databases

REPRODUCTION-2DPAGEIPI00129466.

Proteomic databases

MaxQBP83917.
PaxDbP83917.
PRIDEP83917.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000093943; ENSMUSP00000091475; ENSMUSG00000018666.
GeneID12412.
KEGGmmu:12412.
UCSCuc007lck.1. mouse.

Organism-specific databases

CTD10951.
MGIMGI:105369. Cbx1.

Phylogenomic databases

eggNOGNOG264487.
GeneTreeENSGT00510000046310.
HOGENOMHOG000220852.
HOVERGENHBG000400.
InParanoidP83917.
KOK11585.
OMACEVIRAC.
OrthoDBEOG7QRQWW.
PhylomeDBP83917.
TreeFamTF350503.

Gene expression databases

ArrayExpressP83917.
BgeeP83917.
CleanExMM_CBX1.
GenevestigatorP83917.

Family and domain databases

InterProIPR017984. Chromo_dom_subgr.
IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR008251. Chromo_shadow_dom.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
[Graphical view]
PfamPF00385. Chromo. 1 hit.
PF01393. Chromo_shadow. 1 hit.
[Graphical view]
PRINTSPR00504. CHROMODOMAIN.
SMARTSM00298. CHROMO. 2 hits.
SM00300. ChSh. 1 hit.
[Graphical view]
SUPFAMSSF54160. SSF54160. 2 hits.
PROSITEPS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCBX1. mouse.
EvolutionaryTraceP83917.
NextBio281200.
PROP83917.
SOURCESearch...

Entry information

Entry nameCBX1_MOUSE
AccessionPrimary (citable) accession number: P83917
Secondary accession number(s): P23197
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: July 9, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot