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P83917

- CBX1_MOUSE

UniProt

P83917 - CBX1_MOUSE

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Protein
Chromobox protein homolog 1
Gene
Cbx1, Cbx
Organism
Mus musculus (Mouse)
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
Binding sitei23 – 231Histone H3A7
Binding sitei40 – 401Histone H3A7
Binding sitei42 – 421Histone H3A7
Binding sitei42 – 421Histone H3K9me2
Binding sitei45 – 451Histone H3K9me2
Binding sitei58 – 581Histone H3A7
Binding sitei60 – 601Histone H3A7
Binding sitei125 – 1251PxVxL motif
Binding sitei126 – 1261PxVxL motif
Binding sitei135 – 1351PxVxL motif
Binding sitei146 – 1461PxVxL motif
Binding sitei163 – 1631PxVxL motif
Binding sitei167 – 1671PxVxL motif
Binding sitei168 – 1681PxVxL motif
Binding sitei170 – 1701PxVxL motif

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. protein binding Source: IntAct
  3. protein homodimerization activity Source: MGI

GO - Biological processi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Chromobox protein homolog 1
Alternative name(s):
Heterochromatin protein 1 homolog beta
Short name:
HP1 beta
Heterochromatin protein p25
M31
Modifier 1 protein
Gene namesi
Name:Cbx1
Synonyms:Cbx
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:105369. Cbx1.

Subcellular locationi

Nucleus By similarity
Note: Unassociated with chromosomes during mitosis By similarity.

GO - Cellular componenti

  1. centromeric heterochromatin Source: MGI
  2. chromatin Source: MGI
  3. chromocenter Source: MGI
  4. female pronucleus Source: MGI
  5. male pronucleus Source: MGI
  6. spindle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi23 – 231V → M: Abolishes interaction with SUV39H1. 1 Publication
Mutagenesisi26 – 261V → R: Abolishes interaction with SUV39H1. 1 Publication
Mutagenesisi161 – 1611I → E: Abolishes homodimer formation.
Mutagenesisi164 – 1641Y → E: Abolishes homodimer formation.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 185185Chromobox protein homolog 1
PRO_0000080200Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei89 – 891Phosphoserine By similarity
Modified residuei91 – 911Phosphoserine By similarity
Modified residuei175 – 1751Phosphoserine By similarity

Post-translational modificationi

Not phosphorylated By similarity.
Ubiquitinated.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP83917.
PaxDbiP83917.
PRIDEiP83917.

2D gel databases

REPRODUCTION-2DPAGEIPI00129466.

PTM databases

PhosphoSiteiP83917.

Expressioni

Tissue specificityi

In all adult and embryonic tissues.1 Publication

Gene expression databases

ArrayExpressiP83917.
BgeeiP83917.
CleanExiMM_CBX1.
GenevestigatoriP83917.

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, SETDB1, SUV420H1 and SUV420H2. Interacts with PRDM6. Interacts with POGZ. Interacts with CHAMP1. Interacts with ASXL1 By similarity.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-78119,EBI-78119
Chaf1aQ9QWF03EBI-78119,EBI-639217
Hist1h3iP684336EBI-78119,EBI-79743
Trim24Q641274EBI-78119,EBI-307947

Protein-protein interaction databases

BioGridi198534. 38 interactions.
DIPiDIP-30892N.
IntActiP83917. 37 interactions.
MINTiMINT-191134.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 133
Beta strandi22 – 3110
Beta strandi33 – 4715
Beta strandi51 – 544
Turni55 – 573
Helixi61 – 677
Turni68 – 725
Turni75 – 773
Beta strandi104 – 1074
Helixi112 – 1154
Beta strandi125 – 13410
Beta strandi141 – 1433
Beta strandi145 – 1484
Helixi149 – 1557
Helixi157 – 16610

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AP0NMR-A10-80[»]
1DZ1NMR-A/B104-171[»]
1GUWNMR-A10-80[»]
1S4ZNMR-A/B104-176[»]
ProteinModelPortaliP83917.
SMRiP83917. Positions 27-80, 110-175.

Miscellaneous databases

EvolutionaryTraceiP83917.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 2 chromo domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG264487.
GeneTreeiENSGT00510000046310.
HOGENOMiHOG000220852.
HOVERGENiHBG000400.
InParanoidiP83917.
KOiK11585.
OMAiCEVIRAC.
OrthoDBiEOG7QRQWW.
PhylomeDBiP83917.
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.

P83917-1 [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
X56690 mRNA. Translation: CAA40018.1.
AK014215 mRNA. Translation: BAB29211.1.
CCDSiCCDS25303.1.
PIRiS26847.
RefSeqiNP_031648.1. NM_007622.3.
XP_006532162.1. XM_006532099.1.
XP_006532163.1. XM_006532100.1.
UniGeneiMm.29055.

Genome annotation databases

EnsembliENSMUST00000093943; ENSMUSP00000091475; ENSMUSG00000018666.
GeneIDi12412.
KEGGimmu:12412.
UCSCiuc007lck.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X56690 mRNA. Translation: CAA40018.1 .
AK014215 mRNA. Translation: BAB29211.1 .
CCDSi CCDS25303.1.
PIRi S26847.
RefSeqi NP_031648.1. NM_007622.3.
XP_006532162.1. XM_006532099.1.
XP_006532163.1. XM_006532100.1.
UniGenei Mm.29055.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AP0 NMR - A 10-80 [» ]
1DZ1 NMR - A/B 104-171 [» ]
1GUW NMR - A 10-80 [» ]
1S4Z NMR - A/B 104-176 [» ]
ProteinModelPortali P83917.
SMRi P83917. Positions 27-80, 110-175.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198534. 38 interactions.
DIPi DIP-30892N.
IntActi P83917. 37 interactions.
MINTi MINT-191134.

PTM databases

PhosphoSitei P83917.

2D gel databases

REPRODUCTION-2DPAGE IPI00129466.

Proteomic databases

MaxQBi P83917.
PaxDbi P83917.
PRIDEi P83917.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000093943 ; ENSMUSP00000091475 ; ENSMUSG00000018666 .
GeneIDi 12412.
KEGGi mmu:12412.
UCSCi uc007lck.1. mouse.

Organism-specific databases

CTDi 10951.
MGIi MGI:105369. Cbx1.

Phylogenomic databases

eggNOGi NOG264487.
GeneTreei ENSGT00510000046310.
HOGENOMi HOG000220852.
HOVERGENi HBG000400.
InParanoidi P83917.
KOi K11585.
OMAi CEVIRAC.
OrthoDBi EOG7QRQWW.
PhylomeDBi P83917.
TreeFami TF350503.

Miscellaneous databases

ChiTaRSi CBX1. mouse.
EvolutionaryTracei P83917.
NextBioi 281200.
PROi P83917.
SOURCEi Search...

Gene expression databases

ArrayExpressi P83917.
Bgeei P83917.
CleanExi MM_CBX1.
Genevestigatori P83917.

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. "A sequence motif found in a Drosophila heterochromatin protein is conserved in animals and plants."
    Singh P.B., Miller J.R., Pearce J., Kothary R., Burton R.D., Paro R., James T.C., Gaunt S.J.
    Nucleic Acids Res. 19:789-794(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DOMAIN.
    Strain: C57BL/6.
    Tissue: Embryo.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Head.
  3. "A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic control of transcription by nuclear receptors."
    le Douarin B., Nielsen A.L., Garnier J.-M., Ichinose H., Jeanmougin F., Losson R., Chambon P.
    EMBO J. 15:6701-6715(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TIF1A.
  4. "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.
  5. "Interaction with members of the heterochromatin protein 1 (HP1) family and histone deacetylation are differentially involved in transcriptional silencing by members of the TIF1 family."
    Nielsen A.L., Ortiz J.A., You J., Oulad-Abdelghani M., Khechumian R., Gansmuller A., Chambon P., Losson R.
    EMBO J. 18:6385-6395(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRIM28.
  6. "Histones H3/H4 form a tight complex with the inner nuclear membrane protein LBR and heterochromatin protein 1."
    Polioudaki H., Kourmouli N., Drosou V., Bakou A., Theodoropoulos P.A., Singh P.B., Giannakouros T., Georgatos S.D.
    EMBO Rep. 2:920-925(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HISTONE H3 AND LBR.
  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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HISTONE H3 LYS-9, MUTAGENESIS OF VAL-23 AND VAL-26.
  8. "A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin."
    Schotta G., Lachner M., Sarma K., Ebert A., Sengupta R., Reuter G., Reinberg D., Jenuwein T.
    Genes Dev. 18:1251-1262(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SUV420H1 AND SUV420H2.
  9. "PRISM/PRDM6, a transcriptional repressor that promotes the proliferative gene program in smooth muscle cells."
    Davis C.A., Haberland M., Arnold M.A., Sutherland L.B., McDonald O.G., Richardson J.A., Childs G., Harris S., Owens G.K., Olson E.N.
    Mol. Cell. Biol. 26:2626-2636(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRDM6.
  10. "Structure of the chromatin binding (chromo) domain from mouse modifier protein 1."
    Ball L.J., Murzina N.V., Broadhurst R.W., Raine A.R., Archer S.J., Stott F.J., Murzin A.G., Singh P.B., Domaille P.J., Laue E.D.
    EMBO J. 16:2473-2481(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 10-80.
  11. "The structure of mouse HP1 suggests a unique mode of single peptide recognition by the shadow chromo domain dimer."
    Brasher S.V., Smith B.O., Fogh R.H., Nietlispach D., Thiru A., Nielsen P.R., Broadhurst R.W., Ball L.J., Murzina N.V., Laue E.D.
    EMBO J. 19:1587-1597(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 104-171, SUBUNIT, INTERACTION WITH CHAF1A AND TRIM28, MUTAGENESIS.
  12. "Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9."
    Nielsen P.R., Nietlispach D., Mott H.R., Callaghan J., Bannister A., Kouzarides T., Murzin A.G., Murzina N.V., Laue E.D.
    Nature 416:103-107(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 10-80.
  13. "Structural basis of HP1/PXVXL motif peptide interactions and HP1 localisation to heterochromatin."
    Thiru A., Nietlispach D., Mott H.R., Okuwaki M., Lyon D., Nielsen P.R., Hirshberg M., Verreault A., Murzina N.V., Laue E.D.
    EMBO J. 23:489-499(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 104-175, SUBUNIT, INTERACTION WITH CHAF1A.

Entry informationi

Entry nameiCBX1_MOUSE
AccessioniPrimary (citable) accession number: P83917
Secondary accession number(s): P23197
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: July 9, 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

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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