Chromobox protein homolog 5 - Homo sapiens (Human)

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Names and origin

Protein names

Recommended name:
    Chromobox protein homolog 5
Alternative name(s):
    Heterochromatin protein 1 homolog alpha
      Short name=HP1 alpha
    Antigen p25

Gene names

Name:	CBX5
Synonyms:	HP1A

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	191 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Component of heterochromatin. Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. Can interact with lamin B receptor (LBR). This interaction can contribute to the association of the heterochromatin with the inner nuclear membrane. Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins.
Subunit structure	Interacts with SUV420H1 and SUV420H2 By similarity. Interacts directly with ATRX, CHAF1A, LBR, NIPBL, SP100, STAM2 and TRIM28 via the chromoshadow domain. Can interact directly with CBX3 via the chromoshadow domain. Interacts with histone H3 methylated at 'Lys-9'. Interacts with MIS12 and C20orf127. Interacts with HP1BP3 By similarity.
Subcellular location	Nucleus. Centromere. Note: Component of centromeric and pericentromeric heterochromatin. Associates with chromosomes during mitosis. Associates specifically with chromatin during metaphase and anaphase. Ref.6
Post-translational modification	Phosphorylation of HP1 and LBR may be responsible for some of the alterations in chromatin organization and nuclear structure which occur at various times during the cell cycle By similarity. Phosphorylated during interphase and possibly hyper-phosphorylated during mitosis.
Sequence similarities	Contains 2 chromo domains.

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Ontologies

Keywords
Cellular component	Centromere Nucleus
Domain	Repeat
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	chromatin assembly or disassembly Inferred from electronic annotation. Source: InterPro negative regulation of transcription Inferred from direct assay. Source: UniProtKB
Cellular component	nuclear centromeric heterochromatin Non-traceable author statement. Source: UniProtKB nuclear envelope Ref.3 Traceable author statement. Source: ProtInc nucleolus Inferred from direct assay. Source: UniProtKB
Molecular function	chromatin binding Inferred from electronic annotation. Source: InterPro general transcriptional repressor activity Inferred from mutant phenotype. Source: UniProtKB protein binding Ref.3 Ref.8 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
INCENP	Q9NQS7	1	EBI-78219,EBI-307907
LBR	Q14739	1	EBI-78219,EBI-1055147
MBD1	Q9UIS9	4	EBI-78219,EBI-867196
SUV39H1	O43463	1	EBI-78219,EBI-349968
TRIM28	Q13263	2	EBI-78219,EBI-78139

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 191

191

Chromobox protein homolog 5

PRO_0000080208

Regions

Domain

20 – 78

Chromo 1

Domain

121 – 179

Chromo 2; shadow subtype

Compositional bias

11 – 14

Poly-Ser

Amino acid modifications

Modified residue

Phosphothreonine Ref.13

Modified residue

Phosphoserine Ref.13 Ref.11 Ref.15

Modified residue

Phosphoserine Ref.11 Ref.15

Modified residue

Phosphoserine Ref.13 Ref.11 Ref.15

Modified residue

Phosphoserine Ref.13 Ref.11 Ref.15

Modified residue

Phosphoserine Ref.13 Ref.15 Ref.12 Ref.14

Modified residue

110

Phosphoserine Ref.13

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Sequences

Sequence

Length

Mass (Da)

Tools

P45973-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 16FFC476367093B1
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FASTA

191

22,225

        10         20         30         40         50         60 
MGKKTKRTAD SSSSEDEEEY VVEKVLDRRV VKGQVEYLLK WKGFSEEHNT WEPEKNLDCP 

        70         80         90        100        110        120 
ELISEFMKKY KKMKEGENNK PREKSESNKR KSNFSNSADD IKSKKKREQS NDIARGFERG 

       130        140        150        160        170        180 
LEPEKIIGAT DSCGDLMFLM KWKDTDEADL VLAKEANVKC PQIVIAFYEE RLTWHAYPED 

       190 
AENKEKETAK S

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of a human homologue of Drosophila heterochromatin protein HP1 using anti-centromere autoantibodies with anti-chromo specificity." Saunders W.S., Chue C., Goebl M., Craig C., Clark R.F., Powers J.A., Eissenberg J.C., Elgin S.C.R., Rothfield N.F., Earnshaw W.C. J. Cell Sci. 104:573-582(1993) [PubMed: 8505380] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[3]	"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: 8663349] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-191.
[4]	Lubec G., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 33-40; 56-68; 126-154 AND 160-184, MASS SPECTROMETRY. Tissue: Fetal brain cortex.
[5]	"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: 9169472] [Abstract] Cited for: INTERACTION WITH LBR AND CBX3.
[6]	"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: 10460410] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION.
[7]	"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: 11242053] [Abstract] Cited for: INTERACTION WITH HISTONE H3 LYS-9.
[8]	"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: 15502821] [Abstract] Cited for: INTERACTION WITH MIS12 AND C20ORF127.
[9]	"The mammalian heterochromatin protein 1 binds diverse nuclear proteins through a common motif that targets the chromoshadow domain." Lechner M.S., Schultz D.C., Negorev D., Maul G.G., Rauscher F.J. III Biochem. Biophys. Res. Commun. 331:929-937(2005) [PubMed: 15882967] [Abstract] Cited for: INTERACTION WITH ATRX; CHAF1A; LBR; NIPBL; SP100; STAM2 AND TRIM28.
[10]	"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: 15899859] [Abstract] Cited for: INTERACTION WITH SETDB1.
[11]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-12; SER-13 AND SER-14, MASS SPECTROMETRY. Tissue: Epithelium.
[12]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, MASS SPECTROMETRY. Tissue: Epithelium.
[13]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8; SER-11; SER-13; SER-14; SER-92 AND SER-110, MASS SPECTROMETRY.
[14]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, MASS SPECTROMETRY.
[15]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-12; SER-13; SER-14 AND SER-92, MASS SPECTROMETRY.
[16]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

S62077 mRNA. Translation: AAB26994.1.
L07515 mRNA. Translation: AAA72327.1.
BC006821 mRNA. Translation: AAH06821.1.
U26311 mRNA. Translation: AAC50553.1.

IPI

IPI00024662.

PIR

G01808.

RefSeq

NP_001120793.1.
NP_001120794.1.
NP_036249.1.

UniGene

Hs.349283

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3FDT	X-ray	2.00	A	18-75	[»]

SMR

P45973. Positions 115-178.

ModBase

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Protein-protein interaction databases

DIP

DIP:5986N.

IntAct

P45973. 8 interactions.

PTM databases

PhosphoSite

P45973.

Proteomic databases

PeptideAtlas

P45973.

PRIDE

P45973.

Genome annotation databases

Ensembl

ENSG00000094916. Homo sapiens. [Contig view]

GeneID

23468.

KEGG

hsa:23468.

UCSC

uc001sfh.2. human.

Organism-specific databases

GeneCards

GC12M052921.

H-InvDB

HIX0010692.

HGNC

HGNC:1555. CBX5.

HPA

CAB017548.
HPA016699.

MIM

604478. gene.

PharmGKB

PA26130.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P45973.

HOVERGEN

P45973.

OMA

P45973. PREKSET.

Enzyme and pathway databases

Pathway_Interaction_DB

aurora_b_pathway. Aurora B signaling.

Gene expression databases

ArrayExpress

P45973.

Bgee

P45973.

CleanEx

HS_CBX5.

GermOnline

ENSG00000094916. Homo sapiens.

Family and domain databases

InterPro

IPR017984. Chromo_dom_subgr.
IPR008251. Chromo_shadow.
IPR018125. Chromo_shadow_sbgrp.
IPR000953. Chromodomain.
[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]

PROSITE

PS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 2 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

45793.

SOURCE

Search...

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Entry information

Entry name

CBX5_HUMAN

Accession

Primary (citable) accession number: P45973

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	July 7, 2009
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents