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Reviewed, UniProtKB/Swiss-Prot P45973 (CBX5_HUMAN)

Last modified July 7, 2009. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

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

Protein attributes

Sequence length191 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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. 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 191191Chromobox protein homolog 5
PRO_0000080208

Regions

Domain20 – 7859Chromo 1
Domain121 – 17959Chromo 2; shadow subtype
Compositional bias11 – 144Poly-Ser

Amino acid modifications

Modified residue81Phosphothreonine Ref.13
Modified residue111Phosphoserine Ref.13 Ref.11 Ref.15
Modified residue121Phosphoserine Ref.11 Ref.15
Modified residue131Phosphoserine Ref.13 Ref.11 Ref.15
Modified residue141Phosphoserine Ref.13 Ref.11 Ref.15
Modified residue921Phosphoserine Ref.13 Ref.15 Ref.12 Ref.14
Modified residue1101Phosphoserine Ref.13

Sequences

Sequence LengthMass (Da)Tools
P45973-1 [UniParc].

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

FASTA19122,225
        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 

« Hide

References

« Hide '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.

Cross-references

Sequence databases

S62077 mRNA. Translation: AAB26994.1.
L07515 mRNA. Translation: AAA72327.1.
BC006821 mRNA. Translation: AAH06821.1.
U26311 mRNA. Translation: AAC50553.1.
IPIIPI00024662.
PIRG01808.
RefSeqNP_001120793.1.
NP_001120794.1.
NP_036249.1.
UniGeneHs.349283

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
3FDTX-ray2.00A18-75[»]
SMRP45973. Positions 115-178.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:5986N.
IntActP45973. 8 interactions.

PTM databases

PhosphoSiteP45973.

Proteomic databases

PeptideAtlasP45973.
PRIDEP45973.

Genome annotation databases

EnsemblENSG00000094916. Homo sapiens. [Contig view]
GeneID23468.
KEGGhsa:23468.
UCSCuc001sfh.2. human.

Organism-specific databases

GeneCardsGC12M052921.
H-InvDBHIX0010692.
HGNCHGNC:1555. CBX5.
HPACAB017548.
HPA016699.
MIM604478. gene.
PharmGKBPA26130.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP45973.
HOVERGENP45973.
OMAP45973. PREKSET.

Enzyme and pathway databases

Pathway_Interaction_DBaurora_b_pathway. Aurora B signaling.

Gene expression databases

ArrayExpressP45973.
BgeeP45973.
CleanExHS_CBX5.
GermOnlineENSG00000094916. Homo sapiens.

Family and domain databases

InterProIPR017984. Chromo_dom_subgr.
IPR008251. Chromo_shadow.
IPR018125. Chromo_shadow_sbgrp.
IPR000953. Chromodomain.
[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]
PROSITEPS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio45793.
SOURCESearch...

Entry information

Entry nameCBX5_HUMAN
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents