P83916 (CBX1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chromobox protein homolog 1

Alternative name(s):
HP1Hsbeta
Heterochromatin protein 1 homolog beta
Short name=HP1 beta
Heterochromatin protein p25
M31
Modifier 1 protein
p25beta

Gene names

Name:	CBX1
Synonyms:	CBX

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

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 and SETDB1, SUV420H1 and SUV420H2. Interacts with PRDM6. Interacts with POGZ. Interacts with CHAMP1. Interacts with ASXL1. Ref.5 Ref.6 Ref.8 Ref.10 Ref.11 Ref.12
Subcellular location	Nucleus. Note: Unassociated with chromosomes during mitosis. Ref.1 Ref.4
Tissue specificity	Expressed in all adult and embryonic tissues.
Post-translational modification	Not phosphorylated. Ref.4 Ubiquitinated. Ref.13
Sequence similarities	Contains 2 chromo domains.

Ontologies

Keywords
Cellular component	Nucleus
Domain	Repeat
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara
Cellular_component	centromeric heterochromatin Inferred from electronic annotation. Source: Compara chromocenter Inferred from electronic annotation. Source: Compara chromosome, centromeric region Inferred from direct assay PubMed 8287692. Source: UniProtKB female pronucleus Inferred from electronic annotation. Source: Compara male pronucleus Inferred from electronic annotation. Source: Compara nuclear heterochromatin Traceable author statement Ref.1. Source: ProtInc nucleoplasm Traceable author statement Ref.1. Source: ProtInc spindle Inferred from direct assay PubMed 11101528. Source: UniProtKB
Molecular_function	chromatin binding Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ADNP	Q9H2P0	2	EBI-78129,EBI-1764854
ADNP2	Q6IQ32	2	EBI-78129,EBI-2838654
NR2F6	P10588	2	EBI-78129,EBI-2681496

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 185

185

Chromobox protein homolog 1

PRO_0000080199

Regions

Domain

21 – 79

59

Chromo 1

Domain

117 – 175

59

Chromo 2; shadow subtype

Sites

Binding site

21

1

Histone H3K9me2 By similarity

Binding site

23

1

Histone H3A7 By similarity

Binding site

40

1

Histone H3A7 By similarity

Binding site

42

1

Histone H3A7 By similarity

Binding site

42

1

Histone H3K9me2 By similarity

Binding site

45

1

Histone H3K9me2 By similarity

Binding site

58

1

Histone H3A7 By similarity

Binding site

60

1

Histone H3A7 By similarity

Binding site

125

1

PxVxL motif By similarity

Binding site

126

1

PxVxL motif By similarity

Binding site

135

1

PxVxL motif By similarity

Binding site

146

1

PxVxL motif By similarity

Binding site

163

1

PxVxL motif By similarity

Binding site

167

1

PxVxL motif By similarity

Binding site

168

1

PxVxL motif By similarity

Binding site

170

1

PxVxL motif By similarity

Amino acid modifications

Modified residue

89

1

Phosphoserine Ref.14 Ref.16

Modified residue

91

1

Phosphoserine Ref.16

Modified residue

175

1

Phosphoserine Ref.16

Experimental info

Mutagenesis

161

1

I → E: Abolishes homodimer formation and binding to EMSY. Ref.7

Secondary structure

1

.

.

.

.

.

.

.

.

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.

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.

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.

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.

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185

Helix Strand Turn

Details...

Beta strand

23 – 32

10

Beta strand

35 – 42

8

Helix

47 – 49

3

Beta strand

51 – 54

4

Helix

55 – 57

3

Helix

61 – 68

8

Helix

112 – 115

4

Beta strand

119 – 128

10

Beta strand

131 – 138

8

Beta strand

145 – 148

4

Helix

149 – 155

7

Helix

157 – 165

9

Beta strand

168 – 172

5

Sequences

	Sequence		Length	Mass (Da)
	P83916 [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]	"Heterochromatin protein HP1Hsbeta (p25beta) and its localization with centromeres in mitosis." Furuta K., Chan E.K.L., Kiyosawa K., Reimer G., Luderschmidt C., Tan E.M. Chromosoma 106:11-19(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION. Tissue: Liver tumor.
[2]	"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]. Tissue: Brain and Ovary.
[3]	Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 8-25; 122-137; 140-150 AND 156-167, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[4]	"Localization and phosphorylation of HP1 proteins during the cell cycle in mammalian cells." Minc E., Allory Y., Worman H.J., Courvalin J.-C., Buendia B. Chromosoma 108:220-234(1999) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, LACK OF PHOSPHORYLATION.
[5]	"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.
[6]	"EMSY links the BRCA2 pathway to sporadic breast and ovarian cancer." Hughes-Davies L., Huntsman D., Ruas M., Fuks F., Bye J., Chin S.-F., Milner J., Brown L.A., Hsu F., Gilks B., Nielsen T., Schulzer M., Chia S., Ragaz J., Cahn A., Linger L., Ozdag H., Cattaneo E. , Jordanova E.S., Schuuring E., Yu D.S., Venkitaraman A., Ponder B., Doherty A., Aparicio S., Bentley D., Theillet C., Ponting C.P., Caldas C., Kouzarides T. Cell 115:523-535(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EMSY.
[7]	"Binding of EMSY to HP1beta: implications for recruitment of HP1beta and BS69." Ekblad C.M.S., Chavali G.B., Basu B.P., Freund S.M.V., Veprintsev D., Hughes-Davies L., Kouzarides T., Doherty A.J., Itzhaki L.S. EMBO Rep. 6:675-680(2005) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF ILE-161.
[8]	"In vivo HP1 targeting causes large-scale chromatin condensation and enhanced histone lysine methylation." Verschure P.J., van der Kraan I., de Leeuw W., van der Vlag J., Carpenter A.E., Belmont A.S., van Driel R. Mol. Cell. Biol. 25:4552-4564(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SETDB1.
[9]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Liver.
[10]	"Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers." Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S., Butter F., Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G., Mann M. Cell 142:967-980(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CHAMP1 AND POGZ.
[11]	"ASXL1 represses retinoic acid receptor-mediated transcription through associating with HP1 and LSD1." Lee S.W., Cho Y.S., Na J.M., Park U.H., Kang M., Kim E.J., Um S.J. J. Biol. Chem. 285:18-29(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ASXL1.
[12]	"Human POGZ modulates dissociation of HP1alpha from mitotic chromosome arms through Aurora B activation." Nozawa R.S., Nagao K., Masuda H.T., Iwasaki O., Hirota T., Nozaki N., Kimura H., Obuse C. Nat. Cell Biol. 12:719-727(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH POGZ.
[13]	"Lamin A rod domain mutants target heterochromatin protein 1alpha and beta for proteasomal degradation by activation of F-box protein, FBXW10." Chaturvedi P., Parnaik V.K. PLoS ONE 5:E10620-E10620(2010) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION.
[14]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89; SER-91 AND SER-175, MASS SPECTROMETRY.
[17]	"Crystal structure of the HP1-EMSY complex reveals an unusual mode of HP1 binding." Huang Y., Myers M.P., Xu R.-M. Structure 14:703-712(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 104-175 IN COMPLEX WITH EMSY.
+	Additional computationally mapped references.

Web resources

Wikipedia

Heterochromatin protein 1 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U35451 mRNA. Translation: AAB81548.1.
BC002609 mRNA. Translation: AAH02609.1.
BC021302 mRNA. Translation: AAH21302.1.

IPI

IPI00878669.

PIR

G02080.

RefSeq

NP_001120700.1. NM_001127228.1.
NP_006798.1. NM_006807.4.

UniGene

Hs.77254.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FMM	X-ray	1.80	A/B/C/D	104-175	[»]
3F2U	X-ray	1.80	A	20-73	[»]
3Q6S	X-ray	1.93	A/B/C/D	108-185	[»]

ProteinModelPortal

P83916.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-28135N.
DIP-5982N.

IntAct

P83916. 52 interactions.

MINT

MINT-1378005.

STRING

9606.ENSP00000225603.

PTM databases

PhosphoSite

P83916.

Polymorphism databases

DMDM

48428808.

Proteomic databases

PaxDb

P83916.

PeptideAtlas

P83916.

PRIDE

P83916.

Protocols and materials databases

DNASU

10951.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000225603; ENSP00000225603; ENSG00000108468.
ENST00000393408; ENSP00000377060; ENSG00000108468.

GeneID

10951.

KEGG

hsa:10951.

UCSC

uc002ind.4. human.

Organism-specific databases

CTD

10951.

GeneCards

GC17M046147.

HGNC

HGNC:1551. CBX1.

HPA

CAB012265.

MIM

604511. gene.

neXtProt

NX_P83916.

PharmGKB

PA26126.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG264487.

HOGENOM

HOG000220852.

HOVERGEN

HBG000400.

InParanoid

P83916.

KO

K11585.

OMA

KSAQEGK.

OrthoDB

EOG4DBTG1.

PhylomeDB

P83916.

Gene expression databases

ArrayExpress

P83916.

Bgee

P83916.

CleanEx

HS_CBX1.

Genevestigator

P83916.

GermOnline

ENSG00000108468. Homo sapiens.

Family and domain databases

InterPro

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

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

ChEMBL

CHEMBL1741193.

ChiTaRS

CBX1. human.

EvolutionaryTrace

P83916.

GenomeRNAi

10951.

NextBio

41609.

SOURCE

Search...

Entry information

Entry name

CBX1_HUMAN

Accession

Primary (citable) accession number: P83916
Secondary accession number(s): P23197

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2004
Last sequence update:	June 7, 2004
Last modified:	May 1, 2013
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.