P83917 (CBX1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	185 AA.
Sequence status	Complete.
Protein existence	Evidence 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 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.

Ontologies

Keywords
Cellular component	Nucleus
Domain	Repeat
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	negative regulation of transcription, DNA-dependent Inferred from direct assay Ref.5. Source: MGI
Cellular component	centromeric heterochromatin Inferred from direct assay. Source: MGI chromocenter Inferred from direct assay. Source: MGI female pronucleus Inferred from direct assay. Source: MGI male pronucleus Inferred from direct assay. Source: MGI
Molecular function	identical protein binding Inferred from physical interaction Ref.11. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-78119,EBI-78119
Chaf1a	Q9QWF0	3	EBI-78119,EBI-639217
Hist1h3a	P68433	6	EBI-78119,EBI-79743
Trim24	Q64127	4	EBI-78119,EBI-307947

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 185

185

Chromobox protein homolog 1

PRO_0000080200

Regions

Domain

21 – 79

59

Chromo 1

Domain

117 – 175

59

Chromo 2; shadow subtype

Sites

Binding site

21

1

Histone H3K9me2

Binding site

23

1

Histone H3A7

Binding site

40

1

Histone H3A7

Binding site

42

1

Histone H3A7

Binding site

42

1

Histone H3K9me2

Binding site

45

1

Histone H3K9me2

Binding site

58

1

Histone H3A7

Binding site

60

1

Histone H3A7

Binding site

125

1

PxVxL motif

Binding site

126

1

PxVxL motif

Binding site

135

1

PxVxL motif

Binding site

146

1

PxVxL motif

Binding site

163

1

PxVxL motif

Binding site

167

1

PxVxL motif

Binding site

168

1

PxVxL motif

Binding site

170

1

PxVxL motif

Amino acid modifications

Modified residue

89

1

Phosphoserine By similarity

Modified residue

175

1

Phosphoserine By similarity

Experimental info

Mutagenesis

23

1

V → M: Abolishes interaction with SUV39H1. Ref.7

Mutagenesis

26

1

V → R: Abolishes interaction with SUV39H1. Ref.7

Mutagenesis

161

1

I → E: Abolishes homodimer formation.

Mutagenesis

164

1

Y → E: Abolishes homodimer formation.

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

185

Helix Strand Turn

Details...

Beta strand

22 – 26

5

Beta strand

40 – 45

6

Turn

55 – 57

3

Helix

61 – 71

11

Beta strand

73 – 75

3

Helix

112 – 115

4

Beta strand

125 – 134

10

Beta strand

141 – 143

3

Helix

149 – 155

7

Helix

157 – 166

10

Sequences

	Sequence		Length	Mass (Da)
	P83917 [UniParc]. Last modified June 7, 2004. Version 1. Checksum: BE687AF9C66E48E3	FASTA	185	21,418
	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

References

	« Hide 'large scale' referencesShow '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: 1708124] [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. , 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: 16141072] [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: 8978696] [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: 10202156] [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: 10562550] [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: 11571267] [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: 11242053] [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: 15145825] [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: 16537907] [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: 9171360] [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: 10747027] [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: 11882902] [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: 14765118] [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.

IPI

IPI00129466.

PIR

S26847.

RefSeq

NP_031648.1. NM_007622.3.

UniGene

Mm.29055.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AP0	NMR	-	A	10-80	[»]
1DZ1	NMR	-	A/B	104-171	[»]
1GUW	NMR	-	A	10-80	[»]
1S4Z	NMR	-	A/B	104-175	[»]

ProteinModelPortal

P83917.

SMR

P83917. Positions 27-80, 110-175.

ModBase

Search...

Protein-protein interaction databases

IntAct

P83917. 37 interactions.

MINT

MINT-191134.

STRING

P83917.

PTM databases

PhosphoSite

P83917.

2D gel databases

REPRODUCTION-2DPAGE

IPI00129466.

Proteomic databases

PRIDE

P83917.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000093943; ENSMUSP00000091475; ENSMUSG00000018666.

GeneID

12412.

KEGG

mmu:12412.

Organism-specific databases

CTD

10951.

MGI

MGI:105369. Cbx1.

Phylogenomic databases

HOGENOM

HBG314523.

HOVERGEN

HBG000400.

InParanoid

P83917.

OMA

GEESRPK.

OrthoDB

EOG4DBTG1.

PhylomeDB

P83917.

Gene expression databases

ArrayExpress

P83917.

Bgee

P83917.

CleanEx

MM_CBX1.

Genevestigator

P83917.

GermOnline

ENSMUSG00000018666. Mus musculus.

Family and domain databases

InterPro

IPR017984. Chromo_dom_subgr.
IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR008251. Chromo_shadow.
IPR018125. Chromo_shadow_sbgrp.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
[Graphical view]

KO

K11585.

Pfam

PF00385. Chromo. 1 hit.
PF01393. Chromo_shadow. 1 hit.
[Graphical view]

PRINTS

PR00504. CHROMODOMAIN.

SMART

SM00298. CHROMO. 2 hits.
SM00300. ChSh. 1 hit.
[Graphical view]

SUPFAM

SSF54160. Chromodomain-like. 2 hits.

PROSITE

PS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

NextBio

460465.

SOURCE

Search...

Entry information

Entry name

CBX1_MOUSE

Accession

Primary (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:	January 25, 2012
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program