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P83916 (CBX1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 185185Chromobox protein homolog 1
PRO_0000080199

Regions

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

Sites

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

Amino acid modifications

Modified residue891Phosphoserine Ref.14 Ref.16
Modified residue911Phosphoserine Ref.16
Modified residue1751Phosphoserine Ref.16

Experimental info

Mutagenesis1611I → E: Abolishes homodimer formation and binding to EMSY. Ref.7

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P83916 [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]"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, IDENTIFICATION BY 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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.
PIRG02080.
RefSeqNP_001120700.1. NM_001127228.1.
NP_006798.1. NM_006807.4.
UniGeneHs.77254.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2FMMX-ray1.80A/B/C/D104-175[»]
3F2UX-ray1.80A20-73[»]
3Q6SX-ray1.93A/B/C/D108-185[»]
ProteinModelPortalP83916.
SMRP83916. Positions 27-80, 110-175.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116151. 52 interactions.
DIPDIP-28135N.
IntActP83916. 54 interactions.
MINTMINT-1378005.
STRING9606.ENSP00000225603.

Chemistry

ChEMBLCHEMBL1741193.

PTM databases

PhosphoSiteP83916.

Polymorphism databases

DMDM48428808.

Proteomic databases

PaxDbP83916.
PeptideAtlasP83916.
PRIDEP83916.

Protocols and materials databases

DNASU10951.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000225603; ENSP00000225603; ENSG00000108468.
ENST00000393408; ENSP00000377060; ENSG00000108468.
GeneID10951.
KEGGhsa:10951.
UCSCuc002ind.4. human.

Organism-specific databases

CTD10951.
GeneCardsGC17M046147.
HGNCHGNC:1551. CBX1.
HPACAB012265.
MIM604511. gene.
neXtProtNX_P83916.
PharmGKBPA26126.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG264487.
HOGENOMHOG000220852.
HOVERGENHBG000400.
InParanoidP83916.
KOK11585.
OMAQSQKSAH.
OrthoDBEOG7QRQWW.
PhylomeDBP83916.
TreeFamTF350503.

Gene expression databases

ArrayExpressP83916.
BgeeP83916.
CleanExHS_CBX1.
GenevestigatorP83916.

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. human.
EvolutionaryTraceP83916.
GeneWikiCBX1.
GenomeRNAi10951.
NextBio41609.
PROP83916.
SOURCESearch...

Entry information

Entry nameCBX1_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM