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P83916

- CBX1_HUMAN

UniProt

P83916 - CBX1_HUMAN

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Protein

Chromobox protein homolog 1

Gene
CBX1, CBX
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei21 – 211Histone H3K9me2 By similarity
Binding sitei23 – 231Histone H3A7 By similarity
Binding sitei40 – 401Histone H3A7 By similarity
Binding sitei42 – 421Histone H3A7 By similarity
Binding sitei42 – 421Histone H3K9me2 By similarity
Binding sitei45 – 451Histone H3K9me2 By similarity
Binding sitei58 – 581Histone H3A7 By similarity
Binding sitei60 – 601Histone H3A7 By similarity
Binding sitei125 – 1251PxVxL motif By similarity
Binding sitei126 – 1261PxVxL motif By similarity
Binding sitei135 – 1351PxVxL motif By similarity
Binding sitei146 – 1461PxVxL motif By similarity
Binding sitei163 – 1631PxVxL motif By similarity
Binding sitei167 – 1671PxVxL motif By similarity
Binding sitei168 – 1681PxVxL motif By similarity
Binding sitei170 – 1701PxVxL motif By similarity

GO - Molecular functioni

  1. chromatin binding Source: ProtInc
  2. enzyme binding Source: UniProtKB
  3. histone methyltransferase binding Source: BHF-UCL
  4. protein binding Source: UniProtKB

GO - Biological processi

  1. negative regulation of transcription, DNA-templated Source: Ensembl
Complete GO annotation...

Names & Taxonomyi

Protein namesi
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 namesi
Name:CBX1
Synonyms:CBX
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:1551. CBX1.

Subcellular locationi

Nucleus
Note: Unassociated with chromosomes during mitosis.2 Publications

GO - Cellular componenti

  1. centromeric heterochromatin Source: Ensembl
  2. chromatin Source: UniProtKB
  3. chromocenter Source: Ensembl
  4. chromosome, centromeric region Source: UniProtKB
  5. female pronucleus Source: Ensembl
  6. male pronucleus Source: Ensembl
  7. nuclear heterochromatin Source: ProtInc
  8. nucleoplasm Source: ProtInc
  9. spindle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi161 – 1611I → E: Abolishes homodimer formation and binding to EMSY. 1 Publication

Organism-specific databases

PharmGKBiPA26126.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 185185Chromobox protein homolog 1PRO_0000080199Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei89 – 891Phosphoserine2 Publications
Modified residuei91 – 911Phosphoserine1 Publication
Modified residuei175 – 1751Phosphoserine1 Publication

Post-translational modificationi

Not phosphorylated.1 Publication
Ubiquitinated.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP83916.
PaxDbiP83916.
PeptideAtlasiP83916.
PRIDEiP83916.

PTM databases

PhosphoSiteiP83916.

Expressioni

Tissue specificityi

Expressed in all adult and embryonic tissues.

Gene expression databases

ArrayExpressiP83916.
BgeeiP83916.
CleanExiHS_CBX1.
GenevestigatoriP83916.

Organism-specific databases

HPAiCAB012265.

Interactioni

Subunit structurei

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 ASXL1.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ADNPQ9H2P02EBI-78129,EBI-1764854
ADNP2Q6IQ322EBI-78129,EBI-2838654
HIST1H3DP684319EBI-78129,EBI-79722
NR2F6P105882EBI-78129,EBI-2681496

Protein-protein interaction databases

BioGridi116151. 54 interactions.
DIPiDIP-28135N.
IntActiP83916. 54 interactions.
MINTiMINT-1378005.
STRINGi9606.ENSP00000225603.

Structurei

Secondary structure

1
185
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 3210
Beta strandi35 – 428
Helixi47 – 493
Beta strandi51 – 544
Helixi55 – 573
Helixi61 – 688
Helixi112 – 1154
Beta strandi119 – 12810
Beta strandi131 – 1388
Beta strandi145 – 1484
Helixi149 – 1557
Helixi157 – 1659
Beta strandi168 – 1725

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FMMX-ray1.80A/B/C/D104-175[»]
3F2UX-ray1.80A20-73[»]
3Q6SX-ray1.93A/B/C/D108-185[»]
ProteinModelPortaliP83916.
SMRiP83916. Positions 27-80, 110-175.

Miscellaneous databases

EvolutionaryTraceiP83916.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 7959Chromo 1Add
BLAST
Domaini117 – 17559Chromo 2; shadow subtypeAdd
BLAST

Sequence similaritiesi

Contains 2 chromo domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG264487.
HOGENOMiHOG000220852.
HOVERGENiHBG000400.
InParanoidiP83916.
KOiK11585.
OMAiVHEKSAT.
OrthoDBiEOG7QRQWW.
PhylomeDBiP83916.
TreeFamiTF350503.

Family and domain databases

InterProiIPR017984. Chromo_dom_subgr.
IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
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.

P83916-1 [UniParc]FASTAAdd to Basket

« Hide

MGKKQNKKKV EEVLEEEEEE YVVEKVLDRR VVKGKVEYLL KWKGFSDEDN    50
TWEPEENLDC PDLIAEFLQS QKTAHETDKS EGGKRKADSD SEDKGEESKP 100
KKKKEESEKP RGFARGLEPE RIIGATDSSG ELMFLMKWKN SDEADLVPAK 150
EANVKCPQVV ISFYEERLTW HSYPSEDDDK KDDKN 185
Length:185
Mass (Da):21,418
Last modified:June 7, 2004 - v1
Checksum:iBE687AF9C66E48E3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U35451 mRNA. Translation: AAB81548.1.
BC002609 mRNA. Translation: AAH02609.1.
BC021302 mRNA. Translation: AAH21302.1.
CCDSiCCDS11525.1.
PIRiG02080.
RefSeqiNP_001120700.1. NM_001127228.1.
NP_006798.1. NM_006807.4.
UniGeneiHs.77254.

Genome annotation databases

EnsembliENST00000225603; ENSP00000225603; ENSG00000108468.
ENST00000393408; ENSP00000377060; ENSG00000108468.
GeneIDi10951.
KEGGihsa:10951.
UCSCiuc002ind.4. human.

Polymorphism databases

DMDMi48428808.

Cross-referencesi

Web resourcesi

Wikipedia

Heterochromatin protein 1 entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U35451 mRNA. Translation: AAB81548.1 .
BC002609 mRNA. Translation: AAH02609.1 .
BC021302 mRNA. Translation: AAH21302.1 .
CCDSi CCDS11525.1.
PIRi G02080.
RefSeqi NP_001120700.1. NM_001127228.1.
NP_006798.1. NM_006807.4.
UniGenei Hs.77254.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P83916.
SMRi P83916. Positions 27-80, 110-175.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116151. 54 interactions.
DIPi DIP-28135N.
IntActi P83916. 54 interactions.
MINTi MINT-1378005.
STRINGi 9606.ENSP00000225603.

Chemistry

ChEMBLi CHEMBL1741193.

PTM databases

PhosphoSitei P83916.

Polymorphism databases

DMDMi 48428808.

Proteomic databases

MaxQBi P83916.
PaxDbi P83916.
PeptideAtlasi P83916.
PRIDEi P83916.

Protocols and materials databases

DNASUi 10951.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000225603 ; ENSP00000225603 ; ENSG00000108468 .
ENST00000393408 ; ENSP00000377060 ; ENSG00000108468 .
GeneIDi 10951.
KEGGi hsa:10951.
UCSCi uc002ind.4. human.

Organism-specific databases

CTDi 10951.
GeneCardsi GC17M046147.
HGNCi HGNC:1551. CBX1.
HPAi CAB012265.
MIMi 604511. gene.
neXtProti NX_P83916.
PharmGKBi PA26126.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG264487.
HOGENOMi HOG000220852.
HOVERGENi HBG000400.
InParanoidi P83916.
KOi K11585.
OMAi VHEKSAT.
OrthoDBi EOG7QRQWW.
PhylomeDBi P83916.
TreeFami TF350503.

Miscellaneous databases

ChiTaRSi CBX1. human.
EvolutionaryTracei P83916.
GeneWikii CBX1.
GenomeRNAii 10951.
NextBioi 41609.
PROi P83916.
SOURCEi Search...

Gene expression databases

ArrayExpressi P83916.
Bgeei P83916.
CleanExi HS_CBX1.
Genevestigatori P83916.

Family and domain databases

InterProi IPR017984. Chromo_dom_subgr.
IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR008251. Chromo_shadow_dom.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
[Graphical view ]
Pfami PF00385. Chromo. 1 hit.
PF01393. Chromo_shadow. 1 hit.
[Graphical view ]
PRINTSi PR00504. CHROMODOMAIN.
SMARTi SM00298. CHROMO. 2 hits.
SM00300. ChSh. 1 hit.
[Graphical view ]
SUPFAMi SSF54160. SSF54160. 2 hits.
PROSITEi PS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: INTERACTION WITH EMSY.
  7. 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. 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.

Entry informationi

Entry nameiCBX1_HUMAN
AccessioniPrimary (citable) accession number: P83916
Secondary accession number(s): P23197
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: September 3, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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