CBX6_HUMAN - dbPTM
CBX6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CBX6_HUMAN
UniProt AC O95503
Protein Name Chromobox protein homolog 6
Gene Name CBX6
Organism Homo sapiens (Human).
Sequence Length 412
Subcellular Localization Nucleus . Chromosome . Uniformely distributed in the nucleoplasm (PubMed:18927235). Localizes to the inactivated X chromosome in females (By similarity).
Protein Description 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. [PubMed: 21282530 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. Possibly contributes to the target selectivity of the PRC1 complex by binding specific regions of chromatin]
Protein Sequence MELSAVGERVFAAESIIKRRIRKGRIEYLVKWKGWAIKYSTWEPEENILDSRLIAAFEQKERERELYGPKKRGPKPKTFLLKARAQAEALRISDVHFSVKPSASASSPKLHSSAAVHRLKKDIRRCHRMSRRPLPRPDPQGGSPGLRPPISPFSETVRIINRKVKPREPKRNRIILNLKVIDKGAGGGGAGQGAGALARPKVPSRNRVIGKSKKFSESVLRTQIRHMKFGAFALYKPPPAPLVAPSPGKAEASAPGPGLLLAAPAAPYDARSSGSSGCPSPTPQSSDPDDTPPKLLPETVSPSAPSWREPEVLDLSLPPESAATSKRAPPEVTAAAGPAPPTAPEPAGASSEPEAGDWRPEMSPCSNVVVTDVTSNLLTVTIKEFCNPEDFEKVAAGVAGAAGGGGSIGASK
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
4Phosphorylation----MELSAVGERVF
----CCCCCHHHHHH		13.9619007248
15PhosphorylationERVFAAESIIKRRIR
HHHHHHHHHHHHHHH		25.5324719451
18UbiquitinationFAAESIIKRRIRKGR
HHHHHHHHHHHHCCC		33.6721890473
33UbiquitinationIEYLVKWKGWAIKYS
CEEEEEECCEEEEEC		38.5721890473
38UbiquitinationKWKGWAIKYSTWEPE
EECCEEEEECCCCCC		25.9621890473
39PhosphorylationWKGWAIKYSTWEPEE
ECCEEEEECCCCCCH		12.7620068231
40PhosphorylationKGWAIKYSTWEPEEN
CCEEEEECCCCCCHH		23.2620068231
41PhosphorylationGWAIKYSTWEPEENI
CEEEEECCCCCCHHC		30.6620068231
51PhosphorylationPEENILDSRLIAAFE
CCHHCCCHHHHHHHH		26.0720068231
60UbiquitinationLIAAFEQKERERELY
HHHHHHHHHHHHHHH		52.09-
82UbiquitinationKPKTFLLKARAQAEA
CCCCCHHHHHHHHHH		37.6621890473
93PhosphorylationQAEALRISDVHFSVK
HHHHHEECEEEEECC		27.4423186163
98PhosphorylationRISDVHFSVKPSASA
EECEEEEECCCCCCC		17.8523186163
100UbiquitinationSDVHFSVKPSASASS
CEEEEECCCCCCCCC		31.8621890473
100AcetylationSDVHFSVKPSASASS
CEEEEECCCCCCCCC		31.8612656479
102PhosphorylationVHFSVKPSASASSPK
EEEECCCCCCCCCCC		29.1923403867
104PhosphorylationFSVKPSASASSPKLH
EECCCCCCCCCCCCC		32.7821712546
106PhosphorylationVKPSASASSPKLHSS
CCCCCCCCCCCCCCH		44.6822617229
107PhosphorylationKPSASASSPKLHSSA
CCCCCCCCCCCCCHH		26.2723911959
112PhosphorylationASSPKLHSSAAVHRL
CCCCCCCCHHHHHHH		31.9123312004
113PhosphorylationSSPKLHSSAAVHRLK
CCCCCCCHHHHHHHH		14.9723403867
130PhosphorylationIRRCHRMSRRPLPRP
HHHHHHHHCCCCCCC		25.7027251275
143PhosphorylationRPDPQGGSPGLRPPI
CCCCCCCCCCCCCCC		23.7128985074
151PhosphorylationPGLRPPISPFSETVR
CCCCCCCCCCHHHHH		26.1821712546
154PhosphorylationRPPISPFSETVRIIN
CCCCCCCHHHHHHHC		35.4223312004
156PhosphorylationPISPFSETVRIINRK
CCCCCHHHHHHHCCC		17.5623312004
179UbiquitinationNRIILNLKVIDKGAG
CCEEEEEEEEECCCC		35.75-
183UbiquitinationLNLKVIDKGAGGGGA
EEEEEEECCCCCCCC		39.27-
204PhosphorylationLARPKVPSRNRVIGK
CCCCCCCCCCCCCCC		45.2120068231
214UbiquitinationRVIGKSKKFSESVLR
CCCCCCHHCCHHHHH		62.30-
236UbiquitinationFGAFALYKPPPAPLV
CCEEEEECCCCCCEE		52.47-
246PhosphorylationPAPLVAPSPGKAEAS
CCCEECCCCCCCCCC		36.2322617229
253PhosphorylationSPGKAEASAPGPGLL
CCCCCCCCCCCCCEE		26.8822210691
272PhosphorylationAAPYDARSSGSSGCP
CCCCCCCCCCCCCCC		40.5528450419
273PhosphorylationAPYDARSSGSSGCPS
CCCCCCCCCCCCCCC		36.8221815630
275PhosphorylationYDARSSGSSGCPSPT
CCCCCCCCCCCCCCC		26.0428450419
276PhosphorylationDARSSGSSGCPSPTP
CCCCCCCCCCCCCCC		48.1921815630
280PhosphorylationSGSSGCPSPTPQSSD
CCCCCCCCCCCCCCC		45.5425159151
282PhosphorylationSSGCPSPTPQSSDPD
CCCCCCCCCCCCCCC		37.9925159151
285PhosphorylationCPSPTPQSSDPDDTP
CCCCCCCCCCCCCCC		37.6028450419
286PhosphorylationPSPTPQSSDPDDTPP
CCCCCCCCCCCCCCC		48.1730108239
291PhosphorylationQSSDPDDTPPKLLPE
CCCCCCCCCCCCCCC		49.2025002506
299PhosphorylationPPKLLPETVSPSAPS
CCCCCCCCCCCCCCC		25.0930266825
301PhosphorylationKLLPETVSPSAPSWR
CCCCCCCCCCCCCCC		22.1330266825
303PhosphorylationLPETVSPSAPSWREP
CCCCCCCCCCCCCCC		45.3530266825
306PhosphorylationTVSPSAPSWREPEVL
CCCCCCCCCCCCCCC		38.1830108239
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of CBX6_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CBX6_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CBX6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RING2_HUMANRNF2physical
22325352
BMI1_HUMANBMI1physical
22325352
RING1_HUMANRING1physical
22325352
PHC1_HUMANPHC1physical
22325352
PHC2_HUMANPHC2physical
22325352
PHC3_HUMANPHC3physical
22325352
CBX4_HUMANCBX4physical
22325352
AHDC1_HUMANAHDC1physical
21282530
BPTF_HUMANBPTFphysical
21282530
CAF1B_HUMANCHAF1Bphysical
21282530
CE350_HUMANCEP350physical
21282530
CP135_HUMANCEP135physical
21282530
DACT1_HUMANDACT1physical
21282530
DNMT1_HUMANDNMT1physical
21282530
ELP4_HUMANELP4physical
21282530
H11_HUMANHIST1H1Aphysical
21282530
H15_HUMANHIST1H1Bphysical
21282530
H2B2E_HUMANHIST2H2BEphysical
21282530
H31T_HUMANHIST3H3physical
21282530
IF2B1_HUMANIGF2BP1physical
21282530
IF2B2_HUMANIGF2BP2physical
21282530
IF2B3_HUMANIGF2BP3physical
21282530
ILF2_HUMANILF2physical
21282530
FOXK2_HUMANFOXK2physical
21282530
KHDR1_HUMANKHDRBS1physical
21282530
KRI1_HUMANKRI1physical
21282530
LA_HUMANSSBphysical
21282530
LAS1L_HUMANLAS1Lphysical
21282530
MOV10_HUMANMOV10physical
21282530
NCOR2_HUMANNCOR2physical
21282530
NUCL_HUMANNCLphysical
21282530
NUMA1_HUMANNUMA1physical
21282530
PAIP1_HUMANPAIP1physical
21282530
PHC2_HUMANPHC2physical
21282530
RAD17_HUMANRAD17physical
21282530
ERCC6_HUMANERCC6physical
21282530
RTL9_HUMANRGAG1physical
21282530
RING1_HUMANRING1physical
21282530
RING2_HUMANRNF2physical
21282530
ULK2_HUMANULK2physical
21282530
YBOX1_HUMANYBX1physical
21282530
TOPZ1_HUMANTOPAZ1physical
21282530
ZMYM4_HUMANZMYM4physical
21282530
ZN33A_HUMANZNF33Aphysical
21282530
BMI1_HUMANBMI1physical
21282530
RN213_HUMANRNF213physical
21282530
CD158_HUMANCCDC158physical
21282530
ZKSC7_HUMANZKSCAN7physical
21282530
PCGF3_HUMANPCGF3physical
21282530
PCGF1_HUMANPCGF1physical
21282530
PCGF2_HUMANPCGF2physical
21282530
PCGF5_HUMANPCGF5physical
21282530
PCGF6_HUMANPCGF6physical
21282530
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CBX6_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301 AND SER-303, ANDMASS SPECTROMETRY.

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