CBX2_MOUSE - dbPTM
CBX2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CBX2_MOUSE
UniProt AC P30658
Protein Name Chromobox protein homolog 2
Gene Name Cbx2
Organism Mus musculus (Mouse).
Sequence Length 519
Subcellular Localization Nucleus speckle . Chromosome . Localizes to the inactivated X chromosome in females.
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 (By similarity). 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 (By similarity). Binds to histone H3 trimethylated at 'Lys-9' (H3K9me3) or at 'Lys-27' (H3K27me3). [PubMed: 16537902 Plays a role in the lineage differentiation of the germ layers in embryonic development]
Protein Sequence MEELSSVGEQVFAAECILSKRLRKGKLEYLVKWRGWSSKHNSWEPEENILDPRLLLAFQKKEHEKEVQNRKRGKRPRGRPRKHTVTSSCSRRSKLKEPDAPSKSKSSSSSSSSTSSSSSSDEEEDDSDLDSKRGPRGRETHPVPQKKAQILVAKPELKDPIRKKRGRKPLPPEQKAARRPVSLAKVLKTTRKDLGTSAAKLPPPLSAPVAGLAALKAHTKEACGGPSTMATPENLASLMKGMAGSPSRGGIWQSSIVHYMNRMSQSQVQAASRLALKAQATNKCGLGLDLKVRTQKGGELGGSPAGGKVPKAPGGGAAEQQRGNHSGSPGAQLAPTQELSLQVLDLQSVKNGVPGVGLLARHAPAKAIPATNPATGKGPGSGPTGANMTNAPTDNNKGEKLTCKATALPAPSVKRDTVKSVAASGGQEGHTAPGEGRKPPALSELSTGEENSSSDSDPDSTSLPSAAQNLSVAIQTSQDWKPTRSLIEHVFVTDVTANLITVTVKESPTSVGFFNLRHY
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
87PhosphorylationPRKHTVTSSCSRRSK
CCCCCCCCHHCCCHH
25.6322871156
88PhosphorylationRKHTVTSSCSRRSKL
CCCCCCCHHCCCHHC
13.5222871156
167DimethylationPIRKKRGRKPLPPEQ
HHHHCCCCCCCCHHH
41.26-
245PhosphorylationLMKGMAGSPSRGGIW
HHHHHCCCCCCCCCC
15.3427717184
248Asymmetric dimethylarginineGMAGSPSRGGIWQSS
HHCCCCCCCCCCHHH
51.22-
248MethylationGMAGSPSRGGIWQSS
HHCCCCCCCCCCHHH
51.2224129315
303PhosphorylationKGGELGGSPAGGKVP
CCCCCCCCCCCCCCC
15.1326824392
326PhosphorylationEQQRGNHSGSPGAQL
HHCCCCCCCCCCCCC
44.9926745281
328PhosphorylationQRGNHSGSPGAQLAP
CCCCCCCCCCCCCCC
24.1523984901
336PhosphorylationPGAQLAPTQELSLQV
CCCCCCCCCCEEEEE
29.1223984901
340PhosphorylationLAPTQELSLQVLDLQ
CCCCCCEEEEEECHH
18.9226745281
507PhosphorylationITVTVKESPTSVGFF
EEEEECCCCCEEECE
27.9728066266
509PhosphorylationVTVKESPTSVGFFNL
EEECCCCCEEECEEC
45.3728066266

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_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CBX2_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PHC1_HUMANPHC1physical
12167701
BMI1_HUMANBMI1physical
12167701
RING1_HUMANRING1physical
12167701
CBX4_HUMANCBX4physical
12167701
PHC3_HUMANPHC3physical
12167701
SMCA5_HUMANSMARCA5physical
12167701
SCMH1_HUMANSCMH1physical
12167701
HSP74_HUMANHSPA4physical
12167701
PHC2_HUMANPHC2physical
12167701
BMI1_MOUSEBmi1physical
9571155
PHC1_MOUSEPhc1physical
9571155
RING1_MOUSERing1physical
9312051
H33_MOUSEH3f3aphysical
20493168
NRAM1_MOUSESlc11a1physical
17726103

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CBX2_MOUSE

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Related Literatures of Post-Translational Modification

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