CBX5_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CBX5_MOUSE
• UniProt AC: Q61686
• Protein Name: Chromobox protein homolog 5
• Gene Name: Cbx5
• Organism: Mus musculus (Mouse).
• Sequence Length: 191
• Subcellular Localization: Nucleus . Chromosome. Chromosome, centromere. Colocalizes with HNRNPU in the nucleus (By similarity). Component of centromeric and pericentromeric heterochromatin. Associates with chromosomes during mitosis. Associates specifically with chromatin dur
• Protein Description: Component of heterochromatin that recognizes and binds histone H3 tails methylated at 'Lys-9' (H3K9me), leading to epigenetic repression. In contrast, it is excluded from chromatin when 'Tyr-41' of histone H3 is phosphorylated (H3Y41ph). Can interact with lamin-B receptor (LBR). This interaction can contribute to the association of the heterochromatin with the inner nuclear membrane. Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins (By similarity)..
• Protein Sequence: MGKKTKRTADSSSSEDEEEYVVEKVLDRRMVKGQVEYLLKWKGFSEEHNTWEPEKNLDCPELISEFMKKYKKMKEGENNKPREKSEGNKRKSSFSNSADDIKSKKKREQSNDIARGFERGLEPEKIIGATDSCGDLMFLMKWKDTDEADLVLAKEANVKCPQIVIAFYEERLTWHAYPEDAENKEKESAKS

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
8	Phosphorylation	MGKKTKRTADSSSSE CCCCCCCCCCCCCCC	36.05	27087446
11	Phosphorylation	KTKRTADSSSSEDEE CCCCCCCCCCCCCHH	29.65	27087446
12	Phosphorylation	TKRTADSSSSEDEEE CCCCCCCCCCCCHHH	38.13	27087446
13	Phosphorylation	KRTADSSSSEDEEEY CCCCCCCCCCCHHHH	41.52	27087446
14	Phosphorylation	RTADSSSSEDEEEYV CCCCCCCCCCHHHHH	51.52	27087446
20	Phosphorylation	SSEDEEEYVVEKVLD CCCCHHHHHHHHHHH	17.05	25619855
32	Ubiquitination	VLDRRMVKGQVEYLL HHHHHHHHHHHHHHH	33.99	-
40	Acetylation	GQVEYLLKWKGFSEE HHHHHHHHCCCCCCH	44.24	-
45	Phosphorylation	LLKWKGFSEEHNTWE HHHCCCCCCHHCCCC	51.23	29514104
59	Glutathionylation	EPEKNLDCPELISEF CCCCCCCHHHHHHHH	2.96	24333276
68	Acetylation	ELISEFMKKYKKMKE HHHHHHHHHHHHHHC	59.27	23806337
68	Ubiquitination	ELISEFMKKYKKMKE HHHHHHHHHHHHHHC	59.27	22790023
84	Sumoylation	ENNKPREKSEGNKRK CCCCCCCCCCCCCCC	55.90	-
85	Phosphorylation	NNKPREKSEGNKRKS CCCCCCCCCCCCCCH	46.08	19854140
91	Ubiquitination	KSEGNKRKSSFSNSA CCCCCCCCHHCCCCH	52.65	-
92	Phosphorylation	SEGNKRKSSFSNSAD CCCCCCCHHCCCCHH	40.42	27087446
93	Phosphorylation	EGNKRKSSFSNSADD CCCCCCHHCCCCHHH	35.41	27087446
95	Phosphorylation	NKRKSSFSNSADDIK CCCCHHCCCCHHHHH	31.64	25521595
97	Phosphorylation	RKSSFSNSADDIKSK CCHHCCCCHHHHHHH	31.70	23684622
102	Acetylation	SNSADDIKSKKKREQ CCCHHHHHHHHHHHH	64.32	23806337
102	Ubiquitination	SNSADDIKSKKKREQ CCCHHHHHHHHHHHH	64.32	22790023
110	Phosphorylation	SKKKREQSNDIARGF HHHHHHHHHHHHHHH	31.55	26824392
125	Ubiquitination	ERGLEPEKIIGATDS HHCCCHHHEEEECCC	50.79	22790023
130	Phosphorylation	PEKIIGATDSCGDLM HHHEEEECCCCCCEE	24.19	28066266
132	Phosphorylation	KIIGATDSCGDLMFL HEEEECCCCCCEEEE	18.69	24719451
143	Ubiquitination	LMFLMKWKDTDEADL EEEEEECCCCCHHHE	45.27	22790023
154	Ubiquitination	EADLVLAKEANVKCP HHHEEEEHHHCCCCC	53.88	22790023
159	Ubiquitination	LAKEANVKCPQIVIA EEHHHCCCCCEEEEE	39.75	22790023
160	S-nitrosocysteine	AKEANVKCPQIVIAF EHHHCCCCCEEEEEE	2.33	-
160	S-nitrosylation	AKEANVKCPQIVIAF EHHHCCCCCEEEEEE	2.33	20925432
184	Ubiquitination	YPEDAENKEKESAKS CHHHHHHHHHHHHCC	62.76	-

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
11	S	Phosphorylation	Kinase	CSNK2A1	Q60737	GPS
12	S	Phosphorylation	Kinase	CSNK2A1	Q60737	GPS
13	S	Phosphorylation	Kinase	CSNK2A1	Q60737	GPS
14	S	Phosphorylation	Kinase	CSNK2A1	Q60737	GPS
97	S	Phosphorylation	Kinase	CSNK2A1	Q60737	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CBX5_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CBX5_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CBX5_MOUSE	Cbx5	physical	12565857
H33_BOVIN	H3F3A	physical	17135209
LBR_MOUSE	Lbr	physical	11571267
H33_MOUSE	H3f3a	physical	11571267
TRI66_MOUSE	Trim66	physical	15322135
CAF1A_MOUSE	Chaf1a	physical	15306854
CAF1B_MOUSE	Chaf1b	physical	15306854
TIF1B_MOUSE	Trim28	physical	10562550
H14_MOUSE	Hist1h1e	physical	16127177
TIF1A_MOUSE	Trim24	physical	8978696
TIF1A_MOUSE	Trim24	physical	10562550
HDAC4_HUMAN	HDAC4	physical	12242305
HDAC5_HUMAN	HDAC5	physical	12242305
HDAC9_MOUSE	Hdac9	physical	12242305
SUV91_HUMAN	SUV39H1	physical	12242305
HDAC9_MOUSE	Hdac9	genetic	12242305
KI67_HUMAN	MKI67	physical	11793364
SUV91_MOUSE	Suv39h1	physical	28059589

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93, AND MASSSPECTROMETRY.
PubMed: 19367708

"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-12; SER-13 ANDSER-14, AND MASS SPECTROMETRY.
PubMed: 17622165

"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line.";
Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
Mol. Cell. Proteomics 3:279-286(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-93, AND MASSSPECTROMETRY.
PubMed: 14729942