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Q13185 (CBX3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 151. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chromobox protein homolog 3
Alternative name(s):
HECH
Heterochromatin protein 1 homolog gamma
Short name=HP1 gamma
Modifier 2 protein
Gene names
Name:CBX3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length183 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Seems to be involved in transcriptional silencing in heterochromatin-like complexes. Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. May contribute to the association of the heterochromatin with the inner nuclear membrane through its interaction with lamin B receptor (LBR). Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins.

Subunit structure

Binds directly to CHAF1A. Interacts with histone H3 methylated at 'Lys-9'. Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2, MBLR, L3MBTL2 and YAF2. Interacts with LBR, INCENP, TRIM28/TIF1B, SUV420H1, SUV420H2 and SP100. Interacts with TIF1A By similarity. Interacts with MIS12 and DSN1. Can interact directly with CBX5 via the chromoshadow domain. Interacts with POGZ. Interacts with CHAMP1. Interacts with ASXL1. Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.21 Ref.22 Ref.23

Subcellular location

Nucleus Potential. Note: Associates with euchromatin and is largely excluded from constitutive heterochromatin. May be associated with microtubules and mitotic poles during mitosis Potential. Ref.10

Post-translational modification

Phosphorylated by PIM1. Phosphorylated during interphase and possibly hyper-phosphorylated during mitosis. Ref.3 Ref.10

Sequence similarities

Contains 2 chromo domains.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainRepeat
   Molecular functionChromatin regulator
Repressor
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin remodeling

Non-traceable author statement Ref.1. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 9636147. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchromatin

Inferred from direct assay PubMed 11101528. Source: UniProtKB

condensed chromosome, centromeric region

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear centromeric heterochromatin

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear envelope

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear euchromatin

Inferred from direct assay PubMed 11124534. Source: UniProtKB

nuclear heterochromatin

Inferred from direct assay PubMed 11124534. Source: UniProtKB

nuclear inner membrane

Non-traceable author statement Ref.1. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 17540172. Source: UniProtKB

spindle

Inferred from direct assay PubMed 11101528. Source: UniProtKB

   Molecular_functionenzyme binding

Inferred from physical interaction PubMed 19486527. Source: UniProtKB

histone methyltransferase binding

Inferred from physical interaction PubMed 19486527. Source: BHF-UCL

identical protein binding

Inferred from physical interaction PubMed 19486527PubMed 21888893. Source: IntAct

protein domain specific binding

Inferred from physical interaction Ref.1PubMed 9636147. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 183182Chromobox protein homolog 3
PRO_0000080203

Regions

Domain30 – 8859Chromo 1
Domain121 – 17959Chromo 2; shadow subtype

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue51N6-acetyllysine By similarity
Modified residue101N6-acetyllysine Ref.20
Modified residue441N6-acetyllysine Ref.20
Modified residue501N6-acetyllysine Ref.20
Modified residue931Phosphoserine Ref.16 Ref.24 Ref.26
Modified residue951Phosphoserine Ref.18 Ref.24 Ref.26
Modified residue971Phosphoserine Ref.26
Modified residue991Phosphoserine Ref.26
Modified residue1761Phosphoserine Ref.18

Experimental info

Sequence conflict1111A → G in AAH14380. Ref.5
Sequence conflict1111A → V in AAF62370. Ref.4
Sequence conflict1301T → I in AAB48101. Ref.1
Sequence conflict1301T → I in BAA83340. Ref.3

Secondary structure

....................... 183
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q13185 [UniParc].

Last modified October 17, 2006. Version 4.
Checksum: 5928C63E0C93A76A

FASTA18320,811
        10         20         30         40         50         60 
MASNKTTLQK MGKKQNGKSK KVEEAEPEEF VVEKVLDRRV VNGKVEYFLK WKGFTDADNT 

        70         80         90        100        110        120 
WEPEENLDCP ELIEAFLNSQ KAGKEKDGTK RKSLSDSESD DSKSKKKRDA ADKPRGFARG 

       130        140        150        160        170        180 
LDPERIIGAT DSSGELMFLM KWKDSDEADL VLAKEANMKC PQIVIAFYEE RLTWHSCPED 


EAQ 

« Hide

References

« Hide 'large scale' references
[1]"Interaction between an integral protein of the nuclear envelope inner membrane and human chromodomain proteins homologous to Drosophila HP1."
Ye Q., Worman H.J.
J. Biol. Chem. 271:14653-14656(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-183.
[2]Ye Q., Worman H.J.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Identification of heterochromatin protein 1 (HP1) as a phosphorylation target by Pim-1 kinase and the effect of phosphorylation on the transcriptional repression function of HP1."
Koike N., Maita H., Taira T., Ariga H., Iguchi-Ariga S.M.M.
FEBS Lett. 467:17-21(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-183, PHOSPHORYLATION BY PIM1.
[4]Chen J.H., Luo W.Q., Hu S.N., Zhou H.J., Huang X.W., Zhou Y., Yuan J.G., Qiang B.Q.
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"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: Bone marrow and Placenta.
[6]Lubec G., Afjehi-Sadat L.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 160-171, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[7]"Domain-specific interactions of human HP1-type chromodomain proteins and inner nuclear membrane protein LBR."
Ye Q., Callebaut I., Pezhman A., Courvalin J.-C., Worman H.J.
J. Biol. Chem. 272:14983-14989(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LBR AND CBX5.
[8]"INCENP centromere and spindle targeting: identification of essential conserved motifs and involvement of heterochromatin protein HP1."
Ainsztein A.M., Kandels-Lewis S.E., Mackay A.M., Earnshaw W.C.
J. Cell Biol. 143:1763-1774(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH INCENP.
[9]"Interaction of SP100 with HP1 proteins: a link between the promyelocytic leukemia-associated nuclear bodies and the chromatin compartment."
Seeler J.-S., Marchio A., Sitterlin D., Transy C., Dejean A.
Proc. Natl. Acad. Sci. U.S.A. 95:7316-7321(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SP100.
[10]"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, PHOSPHORYLATION.
[11]"KAP-1 corepressor protein interacts and colocalizes with heterochromatic and euchromatic HP1 proteins: a potential role for Kruppel-associated box-zinc finger proteins in heterochromatin-mediated gene silencing."
Ryan R.F., Schultz D.C., Ayyanathan K., Singh P.B., Friedman J.R., Fredericks W.J., Rauscher F.J. III
Mol. Cell. Biol. 19:4366-4378(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRIM28.
[12]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HISTONE H3 LYS-9.
[13]"A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells."
Ogawa H., Ishiguro K., Gaubatz S., Livingston D.M., Nakatani Y.
Science 296:1132-1136(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN COMPLEX WITH E2F6; TFDP1; MAX; MGA; BAT8; EUHMTASE1; RING1; RNF2; MBLR; L3MBTL2 AND YAF2.
[14]"A conserved Mis12 centromere complex is linked to heterochromatic HP1 and outer kinetochore protein Zwint-1."
Obuse C., Iwasaki O., Kiyomitsu T., Goshima G., Toyoda Y., Yanagida M.
Nat. Cell Biol. 6:1135-1141(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MIS12 AND DSN1.
[15]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95 AND SER-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"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.
[20]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-10; LYS-44 AND LYS-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"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.
[22]"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.
[23]"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.
[24]"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-93 AND SER-95, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"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].
[26]"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-93; SER-95; SER-97 AND SER-99, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"Crystal structure of the complex of chromobox homolog 3 (CBX3) [Homo sapiens] and peptide."
Structural genomics consortium (SGC)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 29-86 IN COMPLEX WITH PEPTIDE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U26312 mRNA. Translation: AAB48101.1.
AB030905 mRNA. Translation: BAA83340.1.
AF136630 mRNA. Translation: AAF62370.1.
BC000954 mRNA. Translation: AAH00954.1.
BC014380 mRNA. Translation: AAH14380.1.
RefSeqNP_009207.2. NM_007276.4.
NP_057671.2. NM_016587.3.
XP_005249668.1. XM_005249611.1.
UniGeneHs.381189.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2L11NMR-A29-81[»]
3DM1X-ray2.40A/C/E/G29-86[»]
3KUPX-ray1.77A/B/C/D110-173[»]
3TZDX-ray1.81A29-81[»]
ProteinModelPortalQ13185.
SMRQ13185. Positions 29-81, 112-173.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116463. 89 interactions.
DIPDIP-5985N.
IntActQ13185. 50 interactions.
MINTMINT-5002782.
STRING9606.ENSP00000336687.

PTM databases

PhosphoSiteQ13185.

Polymorphism databases

DMDM116241284.

2D gel databases

SWISS-2DPAGEQ13185.

Proteomic databases

PaxDbQ13185.
PeptideAtlasQ13185.
PRIDEQ13185.

Protocols and materials databases

DNASU11335.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000337620; ENSP00000336687; ENSG00000122565.
ENST00000396386; ENSP00000379670; ENSG00000122565.
GeneID11335.
KEGGhsa:11335.
UCSCuc003sxt.3. human.

Organism-specific databases

CTD11335.
GeneCardsGC07P026207.
HGNCHGNC:1553. CBX3.
HPACAB001973.
HPA004902.
MIM604477. gene.
neXtProtNX_Q13185.
PharmGKBPA26128.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG264487.
HOGENOMHOG000220852.
HOVERGENHBG000400.
InParanoidQ13185.
KOK11586.
OMARESADKP.
OrthoDBEOG7QRQWW.
PhylomeDBQ13185.
TreeFamTF350503.

Gene expression databases

ArrayExpressQ13185.
BgeeQ13185.
CleanExHS_CBX3.
GenevestigatorQ13185.

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

ChiTaRSCBX3. human.
EvolutionaryTraceQ13185.
GeneWikiCBX3.
GenomeRNAi11335.
NextBio43065.
PROQ13185.
SOURCESearch...

Entry information

Entry nameCBX3_HUMAN
AccessionPrimary (citable) accession number: Q13185
Secondary accession number(s): Q96CD7 expand/collapse secondary AC list , Q99409, Q9BVS3, Q9P0Z6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 151 of the entry and version 4 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 7

Human chromosome 7: entries, gene names and cross-references to MIM