Ambox notice.png

GONUTS is under stress! The website is currently experiencing long-wait times and frequent time-outs due to the record number of students, groups, and annotations related to CACAO this semester. We are currently working on increasing performance -- please accept our apologies for the technical difficulties.

You can help reduce stress on the server by:

  1. not reloading pages frequently - this just adds
  2. opening links in new windows (so you can read the old page)

HUMAN:CBX5

From GONUTS
Jump to: navigation, search

Contents

Species (Taxon ID) Homo sapiens (Human). (taxon:9606)
Gene Name(s) CBX5 ( synonyms: HP1A )
Protein Name(s)
  • Chromobox protein homolog 5
  • Antigen p25
  • Heterochromatin protein 1 homolog alpha
  • HP1 alpha
External Links
UniProt Identifier CBX5_HUMAN
UniProt Accessions P45973, B2R8T9,
EMBL S62077, L07515, AK313506, CH471054, BC006821, U26311,
PIR G01808,
RefSeq NP_001120793.1, NP_001120794.1, NP_036249.1,
PDB 3FDT, 3I3C,
IntAct P45973,
Ensembl ENST00000209875, ENST00000439541, ENST00000454593,
Pfam PF00385, PF01393,

Annotations

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0000118

histone deacetylase complex

ISS: Inferred from Sequence or Structural Similarity

C

Source: BHF-UCL

GO:0035097

histone methyltransferase complex

ISS: Inferred from Sequence or Structural Similarity

C

Source: BHF-UCL

GO:0031618

nuclear centromeric heterochromatin

NAS: Non-traceable Author Statement

C

Source: BHF-UCL

GO:0005635

nuclear envelope

TAS: Traceable Author Statement

C

Source: ProtInc

GO:0005730

nucleolus

IDA: Inferred from Direct Assay

C

Source: BHF-UCL

GO:0017053

transcriptional repressor complex

ISS: Inferred from Sequence or Structural Similarity

C

Source: BHF-UCL

GO:0016565

general transcriptional repressor activity

IMP: Inferred from Mutant Phenotype

F

Source: BHF-UCL

GO:0035064

methylated histone residue binding

IDA: Inferred from Direct Assay

F

Source: UniProtKB

GO:0030674

protein binding, bridging

ISS: Inferred from Sequence or Structural Similarity

F

Source: BHF-UCL

GO:0070491

transcription repressor binding

ISS: Inferred from Sequence or Structural Similarity

F

Source: BHF-UCL

GO:0006333

chromatin assembly or disassembly

IEA: Inferred from Electronic Annotation

P

Source: InterPro

GO:0000118

histone deacetylase complex

GO_REF:0000019

IEA: Inferred from Electronic Annotation

Ensembl:ENSMUSP00000113157

C

GO:0000118

histone deacetylase complex

GO_REF:0000024

ISS: Inferred from Sequence or Structural Similarity

UniProtKB:Q61686

C

GO:0000775

chromosome, centromeric region

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0137

C

GO:0000775

chromosome, centromeric region

GO_REF:0000023

IEA: Inferred from Electronic Annotation

SP_SL:SL-0047

C

GO:0000776

kinetochore

GO_REF:0000019

IEA: Inferred from Electronic Annotation

Ensembl:ENSMUSP00000113157

C

GO:0000792

heterochromatin

GO_REF:0000019

IEA: Inferred from Electronic Annotation

Ensembl:ENSMUSP00000113157

C

GO:0003682

chromatin binding

GO_REF:0000019

IEA: Inferred from Electronic Annotation

Ensembl:ENSMUSP00000113157

F

GO:0005515

protein binding

PMID:10330177[1]

IPI: Inferred from Physical Interaction

UniProtKB:Q13263

F

GO:0005515

protein binding

PMID:12711603[2]

IPI: Inferred from Physical Interaction

UniProtKB:O43463

F

GO:0005515

protein binding

PMID:12711603[2]

IPI: Inferred from Physical Interaction

UniProtKB:Q9UIS9

F

GO:0005515

protein binding

PMID:15502821[3]

IPI: Inferred from Physical Interaction

UniProtKB:Q9H081

F

GO:0005515

protein binding

PMID:15882967[4]

IPI: Inferred from Physical Interaction

UniProtKB:P23497

F

GO:0005515

protein binding

PMID:15882967[4]

IPI: Inferred from Physical Interaction

UniProtKB:P46100

F

GO:0005515

protein binding

PMID:15882967[4]

IPI: Inferred from Physical Interaction

UniProtKB:Q13111

F

GO:0005515

protein binding

PMID:15882967[4]

IPI: Inferred from Physical Interaction

UniProtKB:Q13263

F

GO:0005515

protein binding

PMID:15882967[4]

IPI: Inferred from Physical Interaction

UniProtKB:Q14739

F

GO:0005515

protein binding

PMID:15882967[4]

IPI: Inferred from Physical Interaction

UniProtKB:Q6KC79

F

GO:0005515

protein binding

PMID:19666599[5]

IPI: Inferred from Physical Interaction

UniProtKB:Q8TBE0

F

GO:0005515

protein binding

PMID:20850016[6]

IPI: Inferred from Physical Interaction

UniProtKB:Q7Z3K3

F

GO:0005515

protein binding

PMID:20850016[6]

IPI: Inferred from Physical Interaction

UniProtKB:Q96JM3

F

GO:0005515

protein binding

PMID:8663349[7]

IPI: Inferred from Physical Interaction

UniProtKB:Q14739

F

GO:0005515

protein binding

PMID:9636146[8]

IPI: Inferred from Physical Interaction

UniProtKB:O35892

F

GO:0005515

protein binding

PMID:9636146[8]

IPI: Inferred from Physical Interaction

UniProtKB:P23497-1

F

GO:0005515

protein binding

PMID:9636146[8]

IPI: Inferred from Physical Interaction

UniProtKB:P23497-2

F

GO:0005515

protein binding

PMID:9636147[9]

IPI: Inferred from Physical Interaction

UniProtKB:P23497

F

GO:0005515

protein binding

PMID:9636147[9]

IPI: Inferred from Physical Interaction

UniProtKB:P23497-3

F

GO:0005515

protein binding

PMID:9864353[10]

IPI: Inferred from Physical Interaction

UniProtKB:Q9NQS7

F

GO:0005515

protein binding

PMID:9864353[10]

IPI: Inferred from Physical Interaction

UniProtKB:Q9NQS7

F

GO:0005634

nucleus

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000953

C

GO:0005634

nucleus

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR008251

C

GO:0005634

nucleus

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0539

C

GO:0005634

nucleus

GO_REF:0000019

IEA: Inferred from Electronic Annotation

Ensembl:ENSMUSP00000113157

C

GO:0005634

nucleus

GO_REF:0000023

IEA: Inferred from Electronic Annotation

SP_SL:SL-0191

C

GO:0005634

nucleus

PMID:18029348[11]

IDA: Inferred from Direct Assay

C

GO:0005634

nucleus

PMID:19783980[12]

IDA: Inferred from Direct Assay

C

GO:0005634

nucleus

PMID:9636146[8]

IDA: Inferred from Direct Assay

C

GO:0005635

nuclear envelope

PMID:8663349[7]

TAS: Traceable Author Statement

C

GO:0005654

nucleoplasm

Reactome:REACT_25059

TAS: Traceable Author Statement

C

GO:0005694

chromosome

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0158

C

GO:0005694

chromosome

GO_REF:0000023

IEA: Inferred from Electronic Annotation

SP_SL:SL-0468

C

GO:0005720

nuclear heterochromatin

GO_REF:0000019

IEA: Inferred from Electronic Annotation

Ensembl:ENSMUSP00000113157

C

GO:0005720

nuclear heterochromatin

PMID:8663349[7]

TAS: Traceable Author Statement

C

GO:0005730

nucleolus

GO_REF:0000019

IEA: Inferred from Electronic Annotation

Ensembl:ENSMUSP00000113157

C

GO:0005730

nucleolus

PMID:9636146[8]

IDA: Inferred from Direct Assay

C

GO:0005737

cytoplasm

PMID:18029348[11]

IDA: Inferred from Direct Assay

C

GO:0007596

blood coagulation

Reactome:REACT_604

TAS: Traceable Author Statement

P

GO:0010369

chromocenter

GO_REF:0000019

IEA: Inferred from Electronic Annotation

Ensembl:ENSMUSP00000113157

C

GO:0017053

transcriptional repressor complex

GO_REF:0000019

IEA: Inferred from Electronic Annotation

Ensembl:ENSMUSP00000113157

C

GO:0017053

transcriptional repressor complex

GO_REF:0000024

ISS: Inferred from Sequence or Structural Similarity

UniProtKB:Q61686

C

GO:0019899

enzyme binding

PMID:19486527[13]

IPI: Inferred from Physical Interaction

UniProtKB:Q86Y97

F

GO:0030674

protein binding, bridging

GO_REF:0000019

IEA: Inferred from Electronic Annotation

Ensembl:ENSMUSP00000113157

F

GO:0030674

protein binding, bridging

GO_REF:0000024

ISS: Inferred from Sequence or Structural Similarity

UniProtKB:Q61686

F

GO:0031618

nuclear centromeric heterochromatin

PMID:16177824[14]

NAS: Non-traceable Author Statement

C

GO:0035064

methylated histone residue binding

PMID:19783980[12]

IDA: Inferred from Direct Assay

F

GO:0035064

methylated histone residue binding

PMID:21029866[15]

IDA: Inferred from Direct Assay

F

GO:0035097

histone methyltransferase complex

GO_REF:0000019

IEA: Inferred from Electronic Annotation

Ensembl:ENSMUSP00000113157

C

GO:0035097

histone methyltransferase complex

GO_REF:0000024

ISS: Inferred from Sequence or Structural Similarity

UniProtKB:Q61686

C

GO:0042826

histone deacetylase binding

GO_REF:0000019

IEA: Inferred from Electronic Annotation

Ensembl:ENSMUSP00000113157

F

GO:0044419

interspecies interaction between organisms

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0945

P

GO:0045892

negative regulation of transcription, DNA-dependent

GO_REF:0000019

IEA: Inferred from Electronic Annotation

Ensembl:ENSMUSP00000113157

P

GO:0045892

negative regulation of transcription, DNA-dependent

PMID:9636146[8]

IMP: Inferred from Mutant Phenotype

P

GO:0045892

negative regulation of transcription, DNA-dependent

PMID:9636147[9]

IDA: Inferred from Direct Assay

P

GO:0045892

negative regulation of transcription, DNA-dependent

PMID:9636147[9]

IMP: Inferred from Mutant Phenotype

P

GO:0070491

repressing transcription factor binding

GO_REF:0000019

IEA: Inferred from Electronic Annotation

Ensembl:ENSMUSP00000113157

F

GO:0070491

repressing transcription factor binding

GO_REF:0000024

ISS: Inferred from Sequence or Structural Similarity

UniProtKB:Q61686

F

colocalizes_with

GO:0016605

PML body

PMID:9636146[8]

IMP: Inferred from Mutant Phenotype

C


Notes

References

See Help:References for how to manage references in GONUTS.

  1. Ryan RF et al. (1999) KAP-1 corepressor protein interacts and colocalizes with heterochromatic and euchromatic HP1 proteins: a potential role for Krüppel-associated box-zinc finger proteins in heterochromatin-mediated gene silencing. Mol Cell Biol 19: 4366-78 PubMed GONUTS page
  2. 2.0 2.1 Fujita N et al. (2003) Methyl-CpG binding domain 1 (MBD1) interacts with the Suv39h1-HP1 heterochromatic complex for DNA methylation-based transcriptional repression. J Biol Chem 278: 24132-8 PubMed GONUTS page
  3. Obuse C et al. (2004) A conserved Mis12 centromere complex is linked to heterochromatic HP1 and outer kinetochore protein Zwint-1. Nat Cell Biol 6: 1135-41 PubMed GONUTS page
  4. 4.0 4.1 4.2 4.3 4.4 4.5 Lechner MS et al. (2005) The mammalian heterochromatin protein 1 binds diverse nuclear proteins through a common motif that targets the chromoshadow domain. Biochem Biophys Res Commun 331: 929-37 PubMed GONUTS page
  5. Bierne H et al. (2009) Human BAHD1 promotes heterochromatic gene silencing. Proc Natl Acad Sci U S A 106: 13826-31 PubMed GONUTS page
  6. 6.0 6.1 Vermeulen M et al. (2010) Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers. Cell 142: 967-80 PubMed GONUTS page
  7. 7.0 7.1 7.2 Ye Q & Worman HJ (1996) Interaction between an integral protein of the nuclear envelope inner membrane and human chromodomain proteins homologous to Drosophila HP1. J Biol Chem 271: 14653-6 PubMed GONUTS page
  8. 8.0 8.1 8.2 8.3 8.4 8.5 8.6 Seeler JS et al. (1998) Interaction of SP100 with HP1 proteins: a link between the promyelocytic leukemia-associated nuclear bodies and the chromatin compartment. Proc Natl Acad Sci U S A 95: 7316-21 PubMed GONUTS page
  9. 9.0 9.1 9.2 9.3 Lehming N et al. (1998) Chromatin components as part of a putative transcriptional repressing complex. Proc Natl Acad Sci U S A 95: 7322-6 PubMed GONUTS page
  10. 10.0 10.1 Ainsztein AM et al. (1998) INCENP centromere and spindle targeting: identification of essential conserved motifs and involvement of heterochromatin protein HP1. J Cell Biol 143: 1763-74 PubMed GONUTS page
  11. 11.0 11.1 Barbe L et al. (2008) Toward a confocal subcellular atlas of the human proteome. Mol Cell Proteomics 7: 499-508 PubMed GONUTS page
  12. 12.0 12.1 Dawson MA et al. (2009) JAK2 phosphorylates histone H3Y41 and excludes HP1alpha from chromatin. Nature 461: 819-22 PubMed GONUTS page
  13. Souza PP et al. (2009) The histone methyltransferase SUV420H2 and Heterochromatin Proteins HP1 interact but show different dynamic behaviours. BMC Cell Biol 10: 41 PubMed GONUTS page
  14. Ling PD et al. (2005) Mediation of Epstein-Barr virus EBNA-LP transcriptional coactivation by Sp100. EMBO J 24: 3565-75 PubMed GONUTS page
  15. Bartke T et al. (2010) Nucleosome-interacting proteins regulated by DNA and histone methylation. Cell 143: 470-84 PubMed GONUTS page
Personal tools
Namespaces
Variants
Actions
Navigation
Cacao
Journal Clubs
page contributors
Toolbox