CBX2_HUMAN - dbPTM
CBX2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CBX2_HUMAN
UniProt AC Q14781
Protein Name Chromobox protein homolog 2
Gene Name CBX2
Organism Homo sapiens (Human).
Sequence Length 532
Subcellular Localization Nucleus . Chromosome . Localized in distinct foci on chromatin and in chromocenters. Localizes to the inactive X chromosome. Seems to be recruited to H3K27me3, H3K9ac and H3K3me2 sites on chromatin.
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]
Protein Sequence MEELSSVGEQVFAAECILSKRLRKGKLEYLVKWRGWSSKHNSWEPEENILDPRLLLAFQKKEHEKEVQNRKRGKRPRGRPRKLTAMSSCSRRSKLKEPDAPSKSKSSSSSSSSTSSSSSSDEEDDSDLDAKRGPRGRETHPVPQKKAQILVAKPELKDPIRKKRGRKPLPPEQKATRRPVSLAKVLKTARKDLGAPASKLPPPLSAPVAGLAALKAHAKEACGGPSAMATPENLASLMKGMASSPGRGGISWQSSIVHYMNRMTQSQAQAASRLALKAQATNKCGLGLDLKVRTQKGELGMSPPGSKIPKAPSGGAVEQKVGNTGGPPHTHGASRVPAGCPGPQPAPTQELSLQVLDLQSVKNGMPGVGLLARHATATKGVPATNPAPGKGTGSGLIGASGATMPTDTSKSEKLASRAVAPPTPASKRDCVKGSATPSGQESRTAPGEARKAATLPEMSAGEESSSSDSDPDSASPPSTGQNPSVSVQTSQDWKPTRSLIEHVFVTDVTANLITVTVKESPTSVGFFNLRHY
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
5Phosphorylation---MEELSSVGEQVF
---CHHHHHHHHHHH		26.6828348404
6Phosphorylation--MEELSSVGEQVFA
--CHHHHHHHHHHHH		46.9228348404
61UbiquitinationLLLAFQKKEHEKEVQ
HHHHHHHHHHHHHHH		54.22-
84PhosphorylationRGRPRKLTAMSSCSR
CCCCCHHHHHHHHCC		24.29-
87PhosphorylationPRKLTAMSSCSRRSK
CCHHHHHHHHCCHHC		26.2327732954
88PhosphorylationRKLTAMSSCSRRSKL
CHHHHHHHHCCHHCC		11.7427732954
90PhosphorylationLTAMSSCSRRSKLKE
HHHHHHHCCHHCCCC		32.4527732954
96UbiquitinationCSRRSKLKEPDAPSK
HCCHHCCCCCCCCCC		71.57-
102PhosphorylationLKEPDAPSKSKSSSS
CCCCCCCCCCCCCCC		51.8128348404
104PhosphorylationEPDAPSKSKSSSSSS
CCCCCCCCCCCCCCC		41.95-
107PhosphorylationAPSKSKSSSSSSSST
CCCCCCCCCCCCCCC		37.67-
120PhosphorylationSTSSSSSSDEEDDSD
CCCCCCCCCCCCCCC		51.49-
126PhosphorylationSSDEEDDSDLDAKRG
CCCCCCCCCCCCCCC		53.01-
146SumoylationTHPVPQKKAQILVAK
CCCCCHHHHEEEEEC		40.0328112733
146SumoylationTHPVPQKKAQILVAK
CCCCCHHHHEEEEEC		40.03-
153SumoylationKAQILVAKPELKDPI
HHEEEEECHHHCCHH		31.3928112733
153SumoylationKAQILVAKPELKDPI
HHEEEEECHHHCCHH		31.39-
181PhosphorylationKATRRPVSLAKVLKT
HHCCCCCHHHHHHHH		25.87-
184UbiquitinationRRPVSLAKVLKTARK
CCCCHHHHHHHHHHH		54.0929967540
191UbiquitinationKVLKTARKDLGAPAS
HHHHHHHHHHCCCHH		55.6429967540
198PhosphorylationKDLGAPASKLPPPLS
HHHCCCHHHCCCCCC		33.4021964256
199AcetylationDLGAPASKLPPPLSA
HHCCCHHHCCCCCCC		68.0930587479
205PhosphorylationSKLPPPLSAPVAGLA
HHCCCCCCCCHHHHH		35.98-
215UbiquitinationVAGLAALKAHAKEAC
HHHHHHHHHHHHHHH		33.1429967540
219UbiquitinationAALKAHAKEACGGPS
HHHHHHHHHHHCCCC		35.6629967540
230PhosphorylationGGPSAMATPENLASL
CCCCCCCCHHHHHHH		20.3221815630
243PhosphorylationSLMKGMASSPGRGGI
HHHHHHHCCCCCCCC		28.3322210691
244PhosphorylationLMKGMASSPGRGGIS
HHHHHHCCCCCCCCC		23.1022210691
247MethylationGMASSPGRGGISWQS
HHHCCCCCCCCCHHH		43.4824129315
247Asymmetric dimethylarginineGMASSPGRGGISWQS
HHHCCCCCCCCCHHH		43.48-
251PhosphorylationSPGRGGISWQSSIVH
CCCCCCCCHHHHHHH		23.4922210691
254PhosphorylationRGGISWQSSIVHYMN
CCCCCHHHHHHHHHH		18.7727251275
255PhosphorylationGGISWQSSIVHYMNR
CCCCHHHHHHHHHHH		17.3327251275
259PhosphorylationWQSSIVHYMNRMTQS
HHHHHHHHHHHCCHH		5.7922210691
272PhosphorylationQSQAQAASRLALKAQ
HHHHHHHHHHHHHHH		30.7320860994
277MethylationAASRLALKAQATNKC
HHHHHHHHHHHCCCC		32.61-
277UbiquitinationAASRLALKAQATNKC
HHHHHHHHHHHCCCC		32.6132142685
281PhosphorylationLALKAQATNKCGLGL
HHHHHHHCCCCCCCC		24.11-
283MethylationLKAQATNKCGLGLDL
HHHHHCCCCCCCCEE		25.89-
283UbiquitinationLKAQATNKCGLGLDL
HHHHHCCCCCCCCEE		25.8929967540
291UbiquitinationCGLGLDLKVRTQKGE
CCCCCEEEEEECCCC		29.36-
294PhosphorylationGLDLKVRTQKGELGM
CCEEEEEECCCCCCC		37.3120068231
302PhosphorylationQKGELGMSPPGSKIP
CCCCCCCCCCCCCCC		26.5830266825
306PhosphorylationLGMSPPGSKIPKAPS
CCCCCCCCCCCCCCC		32.9330266825
310UbiquitinationPPGSKIPKAPSGGAV
CCCCCCCCCCCCCCC		76.1329967540
320UbiquitinationSGGAVEQKVGNTGGP
CCCCCCCCCCCCCCC		38.3129967540
320SumoylationSGGAVEQKVGNTGGP
CCCCCCCCCCCCCCC		38.31-
320SumoylationSGGAVEQKVGNTGGP
CCCCCCCCCCCCCCC		38.31-
340GlutathionylationASRVPAGCPGPQPAP
CCCCCCCCCCCCCCC		3.7022555962
379UbiquitinationARHATATKGVPATNP
HHHCCCCCCCCCCCC		56.2829967540
390UbiquitinationATNPAPGKGTGSGLI
CCCCCCCCCCCCCCC		52.84-
423PhosphorylationSRAVAPPTPASKRDC
HHCCCCCCCCHHCHH		30.3530266825
426PhosphorylationVAPPTPASKRDCVKG
CCCCCCCHHCHHCCC		29.4427251275
427AcetylationAPPTPASKRDCVKGS
CCCCCCHHCHHCCCC		55.1325953088
427UbiquitinationAPPTPASKRDCVKGS
CCCCCCHHCHHCCCC		55.1329967540
432UbiquitinationASKRDCVKGSATPSG
CHHCHHCCCCCCCCC		54.18-
434PhosphorylationKRDCVKGSATPSGQE
HCHHCCCCCCCCCCC		24.2128102081
436PhosphorylationDCVKGSATPSGQESR
HHCCCCCCCCCCCCC		21.4928102081
438PhosphorylationVKGSATPSGQESRTA
CCCCCCCCCCCCCCC		49.0728102081
520PhosphorylationITVTVKESPTSVGFF
EEEEECCCCCEEECE		27.9721815630
522PhosphorylationVTVKESPTSVGFFNL
EEECCCCCEEECEEC		45.3725850435
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 CBX2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CBX2_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 CBX2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RING1_HUMANRING1physical
10369680
RING2_HUMANRNF2physical
22325352
BMI1_HUMANBMI1physical
22325352
RING1_HUMANRING1physical
22325352
PHC1_HUMANPHC1physical
22325352
PHC2_HUMANPHC2physical
22325352
PHC3_HUMANPHC3physical
22325352
CBX4_HUMANCBX4physical
22325352
SCML1_HUMANSCML1physical
22325352
MGAP_HUMANMGAphysical
22325352
MDFI_HUMANMDFIphysical
19060904
ANR26_HUMANANKRD26physical
21282530
BMI1_HUMANBMI1physical
21282530
CENPE_HUMANCENPEphysical
21282530
CSK21_HUMANCSNK2A1physical
21282530
CSK22_HUMANCSNK2A2physical
21282530
CSK2B_HUMANCSNK2Bphysical
21282530
DI3L2_HUMANDIS3L2physical
21282530
GTF2I_HUMANGTF2Iphysical
21282530
H2B1B_HUMANHIST1H2BBphysical
21282530
DCAF6_HUMANDCAF6physical
21282530
KDM3A_HUMANKDM3Aphysical
21282530
TRNK1_HUMANTRANK1physical
21282530
MYCB2_HUMANMYCBP2physical
21282530
NPM_HUMANNPM1physical
21282530
PAR12_HUMANPARP12physical
21282530
PARP1_HUMANPARP1physical
21282530
PHC2_HUMANPHC2physical
21282530
PSME3_HUMANPSME3physical
21282530
RING2_HUMANRNF2physical
21282530
RN213_HUMANRNF213physical
21282530
CD158_HUMANCCDC158physical
21282530
ZKSC7_HUMANZKSCAN7physical
21282530
KRA23_HUMANKRTAP2-4physical
25416956
KRA24_HUMANKRTAP2-4physical
25416956
DHX57_HUMANDHX57physical
25416956
RBY1F_HUMANRBMY1Fphysical
25416956
KR107_HUMANKRTAP10-7physical
25416956
KR109_HUMANKRTAP10-9physical
25416956
KR101_HUMANKRTAP10-1physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
61308046,XY sex reversal 5 (SRXY5)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CBX2_HUMAN

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Related Literatures of Post-Translational Modification

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