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O00257

- CBX4_HUMAN

UniProt

O00257 - CBX4_HUMAN

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Protein

E3 SUMO-protein ligase CBX4

Gene

CBX4

Organism
Homo sapiens (Human)
Status
Reviewed - 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. Monosumoylates ZNF131.
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

GO - Molecular functioni

  1. chromatin binding Source: Ensembl
  2. enzyme binding Source: UniProtKB
  3. ligase activity Source: UniProtKB-KW
  4. single-stranded RNA binding Source: Ensembl
  5. SUMO binding Source: MGI
  6. transcription corepressor activity Source: ProtInc
  7. transcription regulatory region DNA binding Source: Ensembl

GO - Biological processi

  1. chromatin modification Source: UniProtKB-KW
  2. negative regulation of apoptotic process Source: ProtInc
  3. negative regulation of transcription, DNA-templated Source: UniProtKB
  4. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  5. protein sumoylation Source: UniProtKB-UniPathway
  6. 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

ReactomeiREACT_169436. Oxidative Stress Induced Senescence.
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:
hPc2
Gene namesi
Name:CBX4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:1554. CBX4.

Subcellular locationi

Nucleus. Nucleus speckle
Note: Localization to nuclear polycomb bodies is required for ZNF131 sumoylation.

GO - Cellular componenti

  1. nuclear body Source: Ensembl
  2. nucleoplasm Source: Reactome
  3. nucleus Source: UniProtKB
  4. PcG protein complex Source: UniProtKB
  5. PRC1 complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi434 – 4341S → A: Abolishes interaction with YWHAZ and YWHAE; impairs interaction with PCGF6 and BMI1; no effect on interaction with RNF2. 1 Publication
Mutagenesisi494 – 4941K → R: No effect on ZNF131 sumoylation. 1 Publication
Mutagenesisi497 – 4971T → A: Small decrease in ZNF131 sumoylation. 1 Publication

Organism-specific databases

PharmGKBiPA26129.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 560560E3 SUMO-protein ligase CBX4PRO_0000080206Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei149 – 1491N6-acetyllysine1 Publication
Cross-linki494 – 494Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei497 – 4971Phosphothreonine; by HIPK21 Publication

Post-translational modificationi

Phosphorylated on Thr-497 by HIPK2 upon DNA damage. This phosphorylation stimulates E3 SUMO-protein ligase activity and promotes sumoylation on Lys-494, as well as sumoylation of other target proteins, such as HNRNPK.3 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO00257.
PaxDbiO00257.
PRIDEiO00257.

PTM databases

PhosphoSiteiO00257.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiO00257.
CleanExiHS_CBX4.
ExpressionAtlasiO00257. baseline and differential.
GenevestigatoriO00257.

Organism-specific databases

HPAiHPA008228.

Interactioni

Subunit structurei

Interacts with histone H3-K9Me3. Interacts with CHTOP (By similarity). Component of a PRC1-like complex. Self-associates. Interacts with SUV39H1 and HIPK2. Interacts with CSNK2B.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BMI1P352264EBI-722425,EBI-2341576
CSNK2A1P684002EBI-4392727,EBI-347804
CSNK2BP678702EBI-4392727,EBI-348169
HIF1AQ1666515EBI-722425,EBI-447269
PCGF6Q9BYE72EBI-4392727,EBI-1048026
RNF2Q994962EBI-4392727,EBI-722416
YWHABP319462EBI-722425,EBI-359815
YWHAEP622582EBI-4392727,EBI-356498
YWHAZP631042EBI-4392727,EBI-347088

Protein-protein interaction databases

BioGridi114105. 76 interactions.
DIPiDIP-42042N.
IntActiO00257. 49 interactions.
MINTiMINT-1196265.
STRINGi9606.ENSP00000269397.

Structurei

Secondary structure

1
560
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi13 – 2210Combined sources
Beta strandi25 – 328Combined sources
Helixi37 – 393Combined sources
Beta strandi41 – 444Combined sources
Helixi45 – 484Combined sources
Helixi51 – 533Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K28NMR-A8-65[»]
3I8ZX-ray1.51A8-62[»]
ProteinModelPortaliO00257.
SMRiO00257. Positions 11-60.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO00257.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 539539Interaction with BMI1Add
BLAST
Regioni540 – 56021Interaction with RNF2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi378 – 40023His-richAdd
BLAST
Compositional biasi389 – 40012Poly-HisAdd
BLAST
Compositional biasi499 – 51012Poly-AlaAdd
BLAST

Domaini

The polyhistidine repeat may act as a targeting signal to nuclear speckles.1 Publication

Sequence similaritiesi

Contains 1 chromo domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG281109.
GeneTreeiENSGT00530000063056.
HOGENOMiHOG000206923.
HOVERGENiHBG005257.
InParanoidiO00257.
KOiK11452.
OMAiKWAHGAG.
OrthoDBiEOG7PCJGP.
PhylomeDBiO00257.
TreeFamiTF106456.

Family and domain databases

InterProiIPR017984. Chromo_dom_subgr.
IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
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. Align

Isoform 1 (identifier: O00257-1) [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
TDNRAKLDLG AQGKGQGHQY ELNSKKHHQY QPHSKERAGK PPPPGKSGKY
160 170 180 190 200
YYQLNSKKHH PYQPDPKMYD LQYQGGHKEA PSPTCPDLGA KSHPPDKWAQ
210 220 230 240 250
GAGAKGYLGA VKPLAGAAGA PGKGSEKGPP NGMMPAPKEA VTGNGIGGKM
260 270 280 290 300
KIVKNKNKNG RIVIVMSKYM ENGMQAVKIK SGEVAEGEAR SPSHKKRAAD
310 320 330 340 350
ERHPPADRTF KKAAGAEEKK VEAPPKRREE EVSGVSDPQP QDAGSRKLSP
360 370 380 390 400
TKEAFGEQPL QLTTKPDLLA WDPARNTHPP SHHPHPHPHH HHHHHHHHHH
410 420 430 440 450
AVGLNLSHVR KRCLSETHGE REPCKKRLTA RSISTPTCLG GSPAAERPAD
460 470 480 490 500
LPPAAALPQP EVILLDSDLD EPIDLRCVKT RSEAGEPPSS LQVKPETPAS
510 520 530 540 550
AAVAVAAAAA PTTTAEKPPA EAQDEPAESL SEFKPFFGNI IITDVTANCL
560
TVTFKEYVTV
Length:560
Mass (Da):61,368
Last modified:July 28, 2009 - v3
Checksum:iDF5C8C4C0CCB1F31
GO
Isoform 2 (identifier: O00257-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     127-396: Missing.

Show »
Length:290
Mass (Da):31,987
Checksum:iB1E71D5122A7B7FA
GO

Sequence cautioni

The sequence AAH14967.1 differs from that shown. Reason: Aberrant splicing.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti137 – 1382Missing in AAB80718. (PubMed:9315667)Curated
Sequence conflicti142 – 1421P → R in AAB80718. (PubMed:9315667)Curated
Sequence conflicti458 – 4581P → R in AAB80718. (PubMed:9315667)Curated
Sequence conflicti458 – 4581P → R in AAB62734. (PubMed:15489334)Curated
Sequence conflicti477 – 4771C → S in AAB80718. (PubMed:9315667)Curated
Sequence conflicti477 – 4771C → S in AAB62734. (PubMed:15489334)Curated
Sequence conflicti480 – 4801T → S in AAB80718. (PubMed:9315667)Curated
Sequence conflicti480 – 4801T → S in AAB62734. (PubMed:15489334)Curated
Sequence conflicti505 – 5051V → VAA in ACA49234. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei127 – 396270Missing in isoform 2. 1 PublicationVSP_041599Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF013956 mRNA. Translation: AAB80718.1.
EU439707 mRNA. Translation: ACA49234.1.
AY390430 mRNA. Translation: AAQ97596.1.
AC100791 Genomic DNA. No translation available.
BC014967 mRNA. Translation: AAH14967.1. Sequence problems.
U94344 mRNA. Translation: AAB62734.1.
CCDSiCCDS32758.1. [O00257-1]
RefSeqiNP_003646.2. NM_003655.2. [O00257-1]
UniGeneiHs.405046.

Genome annotation databases

EnsembliENST00000269397; ENSP00000269397; ENSG00000141582. [O00257-1]
GeneIDi8535.
KEGGihsa:8535.
UCSCiuc002jxe.3. human. [O00257-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF013956 mRNA. Translation: AAB80718.1 .
EU439707 mRNA. Translation: ACA49234.1 .
AY390430 mRNA. Translation: AAQ97596.1 .
AC100791 Genomic DNA. No translation available.
BC014967 mRNA. Translation: AAH14967.1 . Sequence problems.
U94344 mRNA. Translation: AAB62734.1 .
CCDSi CCDS32758.1. [O00257-1 ]
RefSeqi NP_003646.2. NM_003655.2. [O00257-1 ]
UniGenei Hs.405046.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2K28 NMR - A 8-65 [» ]
3I8Z X-ray 1.51 A 8-62 [» ]
ProteinModelPortali O00257.
SMRi O00257. Positions 11-60.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114105. 76 interactions.
DIPi DIP-42042N.
IntActi O00257. 49 interactions.
MINTi MINT-1196265.
STRINGi 9606.ENSP00000269397.

PTM databases

PhosphoSitei O00257.

Proteomic databases

MaxQBi O00257.
PaxDbi O00257.
PRIDEi O00257.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000269397 ; ENSP00000269397 ; ENSG00000141582 . [O00257-1 ]
GeneIDi 8535.
KEGGi hsa:8535.
UCSCi uc002jxe.3. human. [O00257-1 ]

Organism-specific databases

CTDi 8535.
GeneCardsi GC17M077806.
H-InvDB HIX0014237.
HGNCi HGNC:1554. CBX4.
HPAi HPA008228.
MIMi 603079. gene.
neXtProti NX_O00257.
PharmGKBi PA26129.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG281109.
GeneTreei ENSGT00530000063056.
HOGENOMi HOG000206923.
HOVERGENi HBG005257.
InParanoidi O00257.
KOi K11452.
OMAi KWAHGAG.
OrthoDBi EOG7PCJGP.
PhylomeDBi O00257.
TreeFami TF106456.

Enzyme and pathway databases

UniPathwayi UPA00886 .
Reactomei REACT_169436. Oxidative Stress Induced Senescence.

Miscellaneous databases

ChiTaRSi CBX4. human.
EvolutionaryTracei O00257.
GenomeRNAii 8535.
NextBioi 31968.
PROi O00257.
SOURCEi Search...

Gene expression databases

Bgeei O00257.
CleanExi HS_CBX4.
ExpressionAtlasi O00257. baseline and differential.
Genevestigatori O00257.

Family and domain databases

InterProi IPR017984. Chromo_dom_subgr.
IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
[Graphical view ]
Pfami PF00385. Chromo. 1 hit.
[Graphical view ]
PRINTSi PR00504. CHROMODOMAIN.
SMARTi SM00298. CHROMO. 1 hit.
[Graphical view ]
SUPFAMi SSF54160. SSF54160. 1 hit.
PROSITEi PS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Interference with the expression of a novel human polycomb protein, hPc2, results in cellular transformation and apoptosis."
    Satijn D.P.E., Olson D.J., van der Vlag J., Hamer K.M., Lambrechts C., Masselink H., Gunster M.J., Sewalt R.G.A.B., van Driel R., Otte A.P.
    Mol. Cell. Biol. 17:6076-6086(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Fetal brain.
  2. "Genome-wide analysis of histidine repeats reveals their role in the localization of human proteins to the nuclear speckles compartment."
    Salichs E., Ledda A., Mularoni L., Alba M.M., de la Luna S.
    PLoS Genet. 5:E1000397-E1000397(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
  3. "Cloning and identification of NS5ATP1-binding protein 16."
    Liu M., Cheng J., Wang L.
    Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  4. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORM 1).
    Tissue: Colon.
  6. "RING1 is associated with the polycomb group protein complex and acts as a transcriptional repressor."
    Satijn D.P.E., Gunster M.J., van der Vlag J., Hamer K.M., Schul W., Alkema M.J., Saurin A.J., Freemont P.S., van Driel R., Otte A.P.
    Mol. Cell. Biol. 17:4105-4113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 457-560 (ISOFORM 1).
  7. "Selective interactions between vertebrate polycomb homologs and the SUV39H1 histone lysine methyltransferase suggest that histone H3-K9 methylation contributes to chromosomal targeting of Polycomb group proteins."
    Sewalt R.G.A.B., Lachner M., Vargas M., Hamer K.M., den Blaauwen J.L., Hendrix T., Melcher M., Schweizer D., Jenuwein T., Otte A.P.
    Mol. Cell. Biol. 22:5539-5553(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SUV39H1.
  8. "The core of the polycomb repressive complex is compositionally and functionally conserved in flies and humans."
    Levine S.S., Weiss A., Erdjument-Bromage H., Shao Z., Tempst P., Kingston R.E.
    Mol. Cell. Biol. 22:6070-6078(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A PRC1-LIKE HPRC-H COMPLEX WITH BMI1; CBX2; CBX8; PHC1; PHC2; PHC3; RING1 AND RNF2.
  9. "The polycomb protein Pc2 is a SUMO E3."
    Kagey M.H., Melhuish T.A., Wotton D.
    Cell 113:127-137(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUMOYLATION, SUBCELLULAR LOCATION.
  10. "Multiple activities contribute to Pc2 E3 function."
    Kagey M.H., Melhuish T.A., Powers S.E., Wotton D.
    EMBO J. 24:108-119(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-494.
  11. "Pc2-mediated sumoylation of Smad-interacting protein 1 attenuates transcriptional repression of E-cadherin."
    Long J., Zuo D., Park M.
    J. Biol. Chem. 280:35477-35489(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Phosphorylation-dependent control of Pc2 SUMO E3 ligase activity by its substrate protein HIPK2."
    Roscic A., Moeller A., Calzado M.A., Renner F., Wimmer V.C., Gresko E., Luedi K.S., Schmitz M.L.
    Mol. Cell 24:77-89(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HIPK2, SUMOYLATION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-497.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Several distinct polycomb complexes regulate and co-localize on the INK4a tumor suppressor locus."
    Maertens G.N., El Messaoudi-Aubert S., Racek T., Stock J.K., Nicholls J., Rodriguez-Niedenfuhr M., Gil J., Peters G.
    PLoS ONE 4:E6380-E6380(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A PRC1-LIKE COMPLEX.
  15. "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-149, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Interaction proteomics analysis of polycomb proteins defines distinct PRC1 Complexes in mammalian cells."
    Vandamme J., Volkel P., Rosnoblet C., Le Faou P., Angrand P.O.
    Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY (ISOFORM 2), IDENTIFICATION IN A PRC1-LIKE COMPLEX, SELF-ASSOCIATION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-434.
  17. "Small ubiquitin-like modifier (SUMO) modification of zinc finger protein 131 potentiates its negative effect on estrogen signaling."
    Oh Y., Chung K.C.
    J. Biol. Chem. 287:17517-17529(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ZNF131 SUMOYLATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-494 AND THR-497.
  18. "DNA damage-induced heterogeneous nuclear ribonucleoprotein K SUMOylation regulates p53 transcriptional activation."
    Pelisch F., Pozzi B., Risso G., Munoz M.J., Srebrow A.
    J. Biol. Chem. 287:30789-30799(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  19. "Solution NMR structure of the chromo domain of the chromobox protein homolog 4."
    Structural genomics consortium (SGC)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 8-65.
  20. "Crystal structure of human chromobox homolog 4 (cbx4)."
    Structural genomics consortium (SGC)
    Submitted (SEP-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.51 ANGSTROMS) OF 8-62.

Entry informationi

Entry nameiCBX4_HUMAN
AccessioniPrimary (citable) accession number: O00257
Secondary accession number(s): B1PJR7, Q6TPI8, Q96C04
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: July 28, 2009
Last modified: October 29, 2014
This is version 142 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

The human orthologs of the Drosophila Polycomb group protein Pc are CBX2, CBX4, CBX6, CBX7 and CBX8. These show distinct nuclear localizations, contribute differently to transcriptional repression, and appear to be part of distinct PRC1-like protein complexes. The hPRC-H complex purified in PubMed:12167701 probably presents a mixture of different complexes containing different Polycomb group proteins.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3