E3 SUMO-protein ligase CBX4 - Homo sapiens (Human)

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General annotation (Comments)

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Reviewed, UniProtKB/Swiss-Prot O00257 (CBX4_HUMAN)

Last modified June 16, 2009. Version 85. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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

Name:

CBX4

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Sequence length	558 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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	Protein modification; protein sumoylation.
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	Nucleus. Ref.6 Ref.10
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.

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Keywords
Biological process	Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Molecular function	Chromatin regulator Repressor
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	anti-apoptosis Ref.1 Traceable author statement. Source: ProtInc chromatin assembly or disassembly Inferred from electronic annotation. Source: InterPro chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chromatin Inferred from electronic annotation. Source: InterPro nucleus Ref.1 Inferred from direct assay. Source: MGI
Molecular function	chromatin binding Inferred from electronic annotation. Source: InterPro transcription corepressor activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

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Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Chain

1 – 558

558

E3 SUMO-protein ligase CBX4

PRO_0000080206

Domain

16 – 69

Chromo

Compositional bias

383 – 398

Poly-His

Compositional bias

499 – 508

Poly-Ala

Modified residue

413

Phosphoserine Ref.9

Modified residue

495

Phosphothreonine Ref.10

Cross-link

492

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.7

Alternative sequence

127 – 394

268

Missing in isoform 2.

VSP_001078

Sequence conflict

456

R → P in AAH14967. Ref.2

Sequence conflict

475

S → C in AAH14967. Ref.2

Sequence conflict

478

S → T in AAH14967. Ref.2

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Sequence		Length	Mass (Da)
Isoform 1 [UniParc]. Last modified May 1, 1999. Version 2. Checksum: 7158526991D33463 Show »	FASTA	558	61,228
10 20 30 40 50 60 MELPAVGEHV FAVESIEKKR IRKGRVEYLV KWRGWSPKYN TWEPEENILD PRLLIAFQNR 70 80 90 100 110 120 ERQEQLMGYR KRGPKPKPLV VQVPTFARRS NVLTGLQDSS TDNRAKLDLG AQGKGQGHQY 130 140 150 160 170 180 ELNSKKHHQY QPHSKEGKPR PPGKSGKYYY QLNSKKHHPY QPDPKMYDLQ YQGGHKEAPS 190 200 210 220 230 240 PTCPDLGAKS HPPDKWAQGA GAKGYLGAVK PLAGAAGAPG KGSEKGPPNG MMPAPKEAVT 250 260 270 280 290 300 GNGIGGKMKI VKNKNKNGRI VIVMSKYMEN GMQAVKIKSG EVAEGEARSP SHKKRAADER 310 320 330 340 350 360 HPPADRTFKK AAGAEEKKVE APPKRREEEV SGVSDPQPQD AGSRKLSPTK EAFGEQPLQL 370 380 390 400 410 420 TTKPDLLAWD PARNTHPPSH HPHPHPHHHH HHHHHHHHAV GLNLSHVRKR CLSETHGERE 430 440 450 460 470 480 PCKKRLTARS ISTPTCLGGS PAAERPADLP PAAALRQPEV ILLDSDLDEP IDLRSVKSRS 490 500 510 520 530 540 EAGEPPSSLQ VKPETPASAA VAVAAAAAPT TTAEKPPAEA QDEPAESLSE FKPFFGNIII 550 TDVTANCLTV TFKEYVTV « Hide
Isoform 2. Checksum: 1D50C7312D6AF905 Show »	FASTA	290	32,016
10 20 30 40 50 60 MELPAVGEHV FAVESIEKKR IRKGRVEYLV KWRGWSPKYN TWEPEENILD PRLLIAFQNR 70 80 90 100 110 120 ERQEQLMGYR KRGPKPKPLV VQVPTFARRS NVLTGLQDSS TDNRAKLDLG AQGKGQGHQY 130 140 150 160 170 180 ELNSKKHHHH AVGLNLSHVR KRCLSETHGE REPCKKRLTA RSISTPTCLG GSPAAERPAD 190 200 210 220 230 240 LPPAAALRQP EVILLDSDLD EPIDLRSVKS RSEAGEPPSS LQVKPETPAS AAVAVAAAAA 250 260 270 280 290 PTTTAEKPPA EAQDEPAESL SEFKPFFGNI IITDVTANCL TVTFKEYVTV « Hide

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	« Hide 'large scale' referencesShow '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.

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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

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2K28	NMR	-	A	8-65	[»]

ModBase

Search...

IntAct

O00257. 1 interaction.

PhosphoSite

O00257.

PRIDE

O00257.

Ensembl

ENSG00000141582. Homo sapiens. [Contig view]

GeneID

8535.

KEGG

hsa:8535.

GeneCards

GC17M075422.

H-InvDB

HIX0014237.

HGNC

HGNC:1554. CBX4.

HPA

HPA008228.

MIM

603079. gene.

PharmGKB

PA26129.

GenAtlas

Search...

HOGENOM

O00257.

HOVERGEN

O00257.

ArrayExpress

O00257.

Bgee

O00257.

CleanEx

HS_CBX4.

GermOnline

ENSG00000141582. Homo sapiens.

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...

NextBio

31968.

SOURCE

Search...

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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.

Entry name

CBX4_HUMAN

Accession

Primary (citable) accession number: O00257
Secondary accession number(s): Q96C04

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	May 1, 1999
Last modified:	June 16, 2009
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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