Reviewed,
UniProtKB/Swiss-Prot O00257 (CBX4_HUMAN)
Last modified
June 16, 2009.
Version 85.
History...
Clusters with 100%,
90%,
50% identity |
Documents (5) |
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Names and origin
| Protein names | Recommended name: E3 SUMO-protein ligase CBX4 Alternative name(s): Chromobox protein homolog 4 Polycomb 2 homolog Short name=Pc2 Short name=hPc2 | ||
| Gene names |
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| Organism | Homo sapiens (Human) | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 558 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | E3 SUMO-protein ligase which facilitates SUMO1 conjugation by UBE2I. Component of the Polycomb group (PcG) multiprotein PRC1 complex, a complex 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. Ref.6 Ref.8 Ref.10 |
| Pathway | |
| Subunit structure | Interacts with histone H3-K9Me3 By similarity. Component of chromatin-associated class II PcG repressive complex 1 (PRC1/hPRC-H) at least composed of PCGF2/RNF110, BMI1/PCGF4, CBX2/M33, CBX4/PC2, CBX8/PC3, PHC1, PHC2, PHC3, SCMH1, RING1 and RNF2/RING2. Interacts with SUV39H1 and HIPK2. |
| Subcellular location | |
| Tissue specificity | Ubiquitous. |
| Post-translational modification | Phosphorylated on Thr-495 by HIPK2 upon DNA damage; which enhances E3 SUMO-protein ligase activity and promotes sumoylation on Lys-492. Ref.10 Ref.9 |
| Sequence similarities | Contains 1 chromo domain. |
Ontologies
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: O00257-1) 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. | ||||||
| Isoform 2 (identifier: O00257-2) The sequence of this isoform differs from the canonical sequence as follows: 127-394: Missing. | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 558 | 558 | E3 SUMO-protein ligase CBX4 | PRO_0000080206 | |||||
Regions | |||||||||
| Domain | 16 – 69 | 54 | Chromo | ||||||
| Compositional bias | 383 – 398 | 16 | Poly-His | ||||||
| Compositional bias | 499 – 508 | 10 | Poly-Ala | ||||||
Amino acid modifications | |||||||||
| Modified residue | 413 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 495 | 1 | Phosphothreonine Ref.10 | ||||||
| Cross-link | 492 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.7 | |||||||
Natural variations | |||||||||
| Alternative sequence | 127 – 394 | 268 | Missing in isoform 2. | VSP_001078 | |||||
Experimental info | |||||||||
| Sequence conflict | 456 | 1 | R → P in AAH14967. Ref.2 | ||||||
| Sequence conflict | 475 | 1 | S → C in AAH14967. Ref.2 | ||||||
| Sequence conflict | 478 | 1 | S → T in AAH14967. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [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: 9315667] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Fetal brain. |
| [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] (ISOFORM 2). Tissue: Colon. |
| [3] | "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: 9199346] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 455-558. |
| [4] | "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: 12101246] [Abstract] Cited for: INTERACTION WITH SUV39H1. |
| [5] | "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: 12167701] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE PRC1 COMPLEX WITH PCGF2; BMI1; CBX2; CBX8; PHC1; PHC2; PHC3; SCMH1; RING1 AND RNF2. |
| [6] | "The polycomb protein Pc2 is a SUMO E3." Kagey M.H., Melhuish T.A., Wotton D. Cell 113:127-137(2003) [PubMed: 12679040] [Abstract] Cited for: FUNCTION, SUMOYLATION, SUBCELLULAR LOCATION. |
| [7] | "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: 15592428] [Abstract] Cited for: SUMOYLATION AT LYS-492. |
| [8] | "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: 16061479] [Abstract] Cited for: FUNCTION. |
| [9] | "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-413, MASS SPECTROMETRY. Tissue: Epithelium. |
| [10] | "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: 17018294] [Abstract] Cited for: FUNCTION, INTERACTION WITH HIPK2, SUMOYLATION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-495. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| AF013956 mRNA. Translation: AAB80718.1. BC014967 mRNA. Translation: AAH14967.1. U94344 mRNA. Translation: AAB62734.1. | |||||||||||||
| IPI | IPI00010872. IPI00877924. | ||||||||||||
| RefSeq | NP_003646.2. | ||||||||||||
| UniGene | Hs.714363 | ||||||||||||
3D structure databases | |||||||||||||
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| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | O00257. 1 interaction. | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | O00257. | ||||||||||||
Proteomic databases | |||||||||||||
| PRIDE | O00257. | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENSG00000141582. Homo sapiens. [Contig view] | ||||||||||||
| GeneID | 8535. | ||||||||||||
| KEGG | hsa:8535. | ||||||||||||
Organism-specific databases | |||||||||||||
| GeneCards | GC17M075422. | ||||||||||||
| H-InvDB | HIX0014237. | ||||||||||||
| HGNC | HGNC:1554. CBX4. | ||||||||||||
| HPA | HPA008228. | ||||||||||||
| MIM | 603079. gene. | ||||||||||||
| PharmGKB | PA26129. | ||||||||||||
| GenAtlas | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | O00257. | ||||||||||||
| HOVERGEN | O00257. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | O00257. | ||||||||||||
| Bgee | O00257. | ||||||||||||
| CleanEx | HS_CBX4. | ||||||||||||
| GermOnline | ENSG00000141582. Homo sapiens. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR017984. Chromo_dom_subgr. IPR000953. Chromodomain. [Graphical view] | ||||||||||||
| Pfam | PF00385. Chromo. 1 hit. [Graphical view] | ||||||||||||
| PRINTS | PR00504. CHROMODOMAIN. | ||||||||||||
| SMART | SM00298. CHROMO. 1 hit. [Graphical view] | ||||||||||||
| PROSITE | PS00598. CHROMO_1. 1 hit. PS50013. CHROMO_2. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other Resources | |||||||||||||
| NextBio | 31968. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | CBX4_HUMAN | ||||||||
| Accession | Primary (citable) accession number: O00257 Secondary accession number(s): Q96C04 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 17 Human chromosome 17: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


