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Protein

E3 SUMO-protein ligase CBX4

Gene

Cbx4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

E3 SUMO-protein ligase which facilitates SUMO1 conjugation by UBE2I. Involved in the sumoylation of HNRNPK, a p53/TP53 transcriptional coactivator, hence indirectly regulates p53/TP53 transcriptional activation resulting in p21/CDKN1A expression.
Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility.

Pathwayi: protein sumoylation

This protein is involved in the pathway protein sumoylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein sumoylation and in Protein modification.

GO - Molecular functioni

  • chromatin binding Source: MGI
  • enzyme binding Source: MGI
  • ligase activity Source: UniProtKB-KW
  • methylated histone binding Source: UniProtKB
  • phosphoprotein binding Source: MGI
  • single-stranded RNA binding Source: UniProtKB
  • SUMO binding Source: MGI
  • SUMO transferase activity Source: MGI
  • transcription regulatory region DNA binding Source: MGI

GO - Biological processi

  • chromatin modification Source: UniProtKB-KW
  • negative regulation of transcription, DNA-templated Source: MGI
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • protein sumoylation Source: MGI
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Ligase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-MMU-2559580. Oxidative Stress Induced Senescence.
R-MMU-3108214. SUMOylation of DNA damage response and repair proteins.
R-MMU-4570464. SUMOylation of RNA binding proteins.
UniPathwayiUPA00886.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 SUMO-protein ligase CBX4 (EC:6.3.2.-)
Alternative name(s):
Chromobox protein homolog 4
Polycomb 2 homolog
Short name:
Pc2
Short name:
mPc2
Gene namesi
Name:Cbx4
Synonyms:Pc2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1195985. Cbx4.

Subcellular locationi

  • Nucleus By similarity
  • Nucleus speckle By similarity

GO - Cellular componenti

  • nuclear body Source: MGI
  • nuclear speck Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB
  • PcG protein complex Source: UniProtKB
  • PRC1 complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 551551E3 SUMO-protein ligase CBX4PRO_0000080207Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki106 – 106Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki114 – 114Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei149 – 1491N6-acetyllysine; alternateBy similarity
Cross-linki149 – 149Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki205 – 205Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki212 – 212Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki280 – 280Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei463 – 4631PhosphoserineBy similarity
Cross-linki490 – 490Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO55187.
MaxQBiO55187.
PaxDbiO55187.
PRIDEiO55187.

PTM databases

iPTMnetiO55187.
PhosphoSiteiO55187.

Expressioni

Gene expression databases

BgeeiO55187.
CleanExiMM_CBX4.
GenevisibleiO55187. MM.

Interactioni

Subunit structurei

Interacts with SUV39H1 and HIPK2. Interacts with CSNK2B (By similarity). Component of a PRC1-like complex. Interacts with histone H3-K9Me3. Interacts with CHTOP.By similarity2 Publications

GO - Molecular functioni

  • enzyme binding Source: MGI
  • methylated histone binding Source: UniProtKB
  • phosphoprotein binding Source: MGI
  • SUMO binding Source: MGI

Protein-protein interaction databases

BioGridi198537. 23 interactions.
IntActiO55187. 20 interactions.
STRINGi10090.ENSMUSP00000026665.

Structurei

3D structure databases

ProteinModelPortaliO55187.
SMRiO55187. Positions 11-60.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 6959ChromoPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi383 – 39513Poly-HisAdd
BLAST

Domaini

The polyhistidine repeat may act as a targeting signal to nuclear speckles.By similarity

Sequence similaritiesi

Contains 1 chromo domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IPQ6. Eukaryota.
ENOG410ZQCR. LUCA.
GeneTreeiENSGT00530000063056.
HOGENOMiHOG000231219.
HOVERGENiHBG005257.
InParanoidiO55187.
KOiK11452.
OMAiHHHHAVD.
OrthoDBiEOG7PCJGP.
TreeFamiTF106456.

Family and domain databases

InterProiIPR000953. Chromo/shadow_dom.
IPR017984. Chromo_dom_subgr.
IPR023780. Chromo_domain.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
[Graphical view]
PfamiPF00385. Chromo. 1 hit.
[Graphical view]
PRINTSiPR00504. CHROMODOMAIN.
SMARTiSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
PROSITEiPS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O55187-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MELPAVGEHV FAVESIEKKR IRKGRVEYLV KWRGWSPKYN TWEPEENILD
60 70 80 90 100
PRLLIAFQNR ERQEQLMGYR KRGPKPKPLV VQVPTFARRS NVLTGLQDSS
110 120 130 140 150
ADNRAKLELG TQGKGQGHQY ELNSKKHHQY QPHSKERSGK PPPPGKSGKY
160 170 180 190 200
YYQLNSKKHH PYQPDPKMYD LQYQGGHKEA PSPTCPDLGT KSHPPDKWAH
210 220 230 240 250
GAAAKGYLGA VKPLGGGAGA PGKGSEKGPP NGMTPAPKEA VTGNGIGGKM
260 270 280 290 300
KIVKNKNKNG RIVIVMSKYM ENGMQAVKIK SGEAAEGEAR SPSHKKRAAE
310 320 330 340 350
ERHPQGDRTF KKAAGASEEK KAEVPCKRRE EEALVSGDAQ PQDLGSRKLS
360 370 380 390 400
PTKEAFGEQP LQLTTKPDLL AWDPARSSHP PAHHHHHHHH HHHHHTVGLN
410 420 430 440 450
LSHARKRCLS ETHGEREPCK KRLTARSIST PTCLGGSPVS EHPANVSPTA
460 470 480 490 500
ASLPQPEVIL LDSDLDEPID LRCVKMRSDA GEPPSTLQVK PEAPAVAAVV
510 520 530 540 550
APAPASEKPP AEAQEEPVEP LSEFKPFFGN IIITDVTANC LTVTFKEYVT

V
Length:551
Mass (Da):60,523
Last modified:December 12, 2006 - v2
Checksum:i382F8305FD803CF3
GO
Isoform 2 (identifier: O55187-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-66: Missing.

Note: No experimental confirmation available.
Show »
Length:485
Mass (Da):52,532
Checksum:iEAA3057099C0C58C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti77 – 771K → N in AAB96874 (PubMed:9367786).Curated
Sequence conflicti144 – 1452PG → AR in AAB96874 (PubMed:9367786).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6666Missing in isoform 2. 1 PublicationVSP_022009Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U63387 mRNA. Translation: AAB96874.1.
BC117801 mRNA. Translation: AAI17802.1.
BC117802 mRNA. Translation: AAI17803.1.
CCDSiCCDS25710.1. [O55187-1]
RefSeqiNP_031651.2. NM_007625.2. [O55187-1]
UniGeneiMm.268070.
Mm.471550.

Genome annotation databases

EnsembliENSMUST00000026665; ENSMUSP00000026665; ENSMUSG00000039989. [O55187-1]
GeneIDi12418.
KEGGimmu:12418.
UCSCiuc007mpv.2. mouse. [O55187-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U63387 mRNA. Translation: AAB96874.1.
BC117801 mRNA. Translation: AAI17802.1.
BC117802 mRNA. Translation: AAI17803.1.
CCDSiCCDS25710.1. [O55187-1]
RefSeqiNP_031651.2. NM_007625.2. [O55187-1]
UniGeneiMm.268070.
Mm.471550.

3D structure databases

ProteinModelPortaliO55187.
SMRiO55187. Positions 11-60.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198537. 23 interactions.
IntActiO55187. 20 interactions.
STRINGi10090.ENSMUSP00000026665.

PTM databases

iPTMnetiO55187.
PhosphoSiteiO55187.

Proteomic databases

EPDiO55187.
MaxQBiO55187.
PaxDbiO55187.
PRIDEiO55187.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026665; ENSMUSP00000026665; ENSMUSG00000039989. [O55187-1]
GeneIDi12418.
KEGGimmu:12418.
UCSCiuc007mpv.2. mouse. [O55187-1]

Organism-specific databases

CTDi8535.
MGIiMGI:1195985. Cbx4.

Phylogenomic databases

eggNOGiENOG410IPQ6. Eukaryota.
ENOG410ZQCR. LUCA.
GeneTreeiENSGT00530000063056.
HOGENOMiHOG000231219.
HOVERGENiHBG005257.
InParanoidiO55187.
KOiK11452.
OMAiHHHHAVD.
OrthoDBiEOG7PCJGP.
TreeFamiTF106456.

Enzyme and pathway databases

UniPathwayiUPA00886.
ReactomeiR-MMU-2559580. Oxidative Stress Induced Senescence.
R-MMU-3108214. SUMOylation of DNA damage response and repair proteins.
R-MMU-4570464. SUMOylation of RNA binding proteins.

Miscellaneous databases

PROiO55187.
SOURCEiSearch...

Gene expression databases

BgeeiO55187.
CleanExiMM_CBX4.
GenevisibleiO55187. MM.

Family and domain databases

InterProiIPR000953. Chromo/shadow_dom.
IPR017984. Chromo_dom_subgr.
IPR023780. Chromo_domain.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
[Graphical view]
PfamiPF00385. Chromo. 1 hit.
[Graphical view]
PRINTSiPR00504. CHROMODOMAIN.
SMARTiSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
PROSITEiPS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "MPc2, a new murine homolog of the Drosophila polycomb protein is a member of the mouse polycomb transcriptional repressor complex."
    Alkema M.J., Jacobs J., Voncken J.W., Jenkins N.A., Copeland N.G., Satijn D.P.E., Otte A.P., Berns A., van Lohuizen M.
    J. Mol. Biol. 273:993-1003(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
  3. "Mouse polycomb proteins bind differentially to methylated histone H3 and RNA and are enriched in facultative heterochromatin."
    Bernstein E., Duncan E.M., Masui O., Gil J., Heard E., Allis C.D.
    Mol. Cell. Biol. 26:2560-2569(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH H3-K9ME3.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen.
  5. "Five friends of methylated chromatin target of protein-arginine-methyltransferase[prmt]-1 (chtop), a complex linking arginine methylation to desumoylation."
    Fanis P., Gillemans N., Aghajanirefah A., Pourfarzad F., Demmers J., Esteghamat F., Vadlamudi R.K., Grosveld F., Philipsen S., van Dijk T.B.
    Mol. Cell. Proteomics 11:1263-1273(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CHTOP.

Entry informationi

Entry nameiCBX4_MOUSE
AccessioniPrimary (citable) accession number: O55187
Secondary accession number(s): Q149G5, Q149G6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: December 12, 2006
Last modified: June 8, 2016
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.