dbPTM

CBX3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CBX3_HUMAN
UniProt AC	Q13185
Protein Name	Chromobox protein homolog 3
Gene Name	CBX3
Organism	Homo sapiens (Human).
Sequence Length	183
Subcellular Localization	Nucleus . Associates with euchromatin and is largely excluded from constitutive heterochromatin. May be associated with microtubules and mitotic poles during mitosis (Potential).
Protein Description	Seems to be involved in transcriptional silencing in heterochromatin-like complexes. Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. May contribute to the association of the heterochromatin with the inner nuclear membrane through its interaction with lamin B receptor (LBR). Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins. Contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation, mediates the recruitment of the methyltransferases SUV39H1 and/or SUV39H2 by the PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1. Mediates the recruitement of NIPBL to sites of DNA damage at double-strand breaks (DSBs). [PubMed: 28167679]
Protein Sequence	MASNKTTLQKMGKKQNGKSKKVEEAEPEEFVVEKVLDRRVVNGKVEYFLKWKGFTDADNTWEPEENLDCPELIEAFLNSQKAGKEKDGTKRKSLSDSESDDSKSKKKRDAADKPRGFARGLDPERIIGATDSSGELMFLMKWKDSDEADLVLAKEANMKCPQIVIAFYEERLTWHSCPEDEAQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASNKTTLQ ------CCCCHHHHH	23.08	-
3	Phosphorylation	-----MASNKTTLQK -----CCCCHHHHHH	37.25	24719451
5	Acetylation	---MASNKTTLQKMG ---CCCCHHHHHHHH	40.15	23749302
5	Sumoylation	---MASNKTTLQKMG ---CCCCHHHHHHHH	40.15	28112733
5	Ubiquitination	---MASNKTTLQKMG ---CCCCHHHHHHHH	40.15	-
5	Sumoylation	---MASNKTTLQKMG ---CCCCHHHHHHHH	40.15	-
7	Phosphorylation	-MASNKTTLQKMGKK -CCCCHHHHHHHHHH	28.88	21601212
10	Sumoylation	SNKTTLQKMGKKQNG CCHHHHHHHHHHCCC	53.37	-
10	Sumoylation	SNKTTLQKMGKKQNG CCHHHHHHHHHHCCC	53.37	28112733
10	Ubiquitination	SNKTTLQKMGKKQNG CCHHHHHHHHHHCCC	53.37	19608861
10	Acetylation	SNKTTLQKMGKKQNG CCHHHHHHHHHHCCC	53.37	19608861
20	Acetylation	KKQNGKSKKVEEAEP HHCCCCCCCCHHCCC	65.41	25953088
20	Ubiquitination	KKQNGKSKKVEEAEP HHCCCCCCCCHHCCC	65.41	-
21	Sumoylation	KQNGKSKKVEEAEPE HCCCCCCCCHHCCCH	63.07	-
21	Ubiquitination	KQNGKSKKVEEAEPE HCCCCCCCCHHCCCH	63.07	21906983
21	Sumoylation	KQNGKSKKVEEAEPE HCCCCCCCCHHCCCH	63.07	28112733
21	Acetylation	KQNGKSKKVEEAEPE HCCCCCCCCHHCCCH	63.07	23236377
21	Methylation	KQNGKSKKVEEAEPE HCCCCCCCCHHCCCH	63.07	-
34	Ubiquitination	PEEFVVEKVLDRRVV CHHHHEEEHHEECEE	36.17	21906983
34	Acetylation	PEEFVVEKVLDRRVV CHHHHEEEHHEECEE	36.17	26051181
44	Ubiquitination	DRRVVNGKVEYFLKW EECEECCEEEEEEEE	27.04	19608861
44	Succinylation	DRRVVNGKVEYFLKW EECEECCEEEEEEEE	27.04	23954790
44	Methylation	DRRVVNGKVEYFLKW EECEECCEEEEEEEE	27.04	19608861
44	Acetylation	DRRVVNGKVEYFLKW EECEECCEEEEEEEE	27.04	19608861
47	Phosphorylation	VVNGKVEYFLKWKGF EECCEEEEEEEECCC	19.73	28152594
50	Ubiquitination	GKVEYFLKWKGFTDA CEEEEEEEECCCCCC	36.64	21906983
50	Acetylation	GKVEYFLKWKGFTDA CEEEEEEEECCCCCC	36.64	19608861
52	Ubiquitination	VEYFLKWKGFTDADN EEEEEEECCCCCCCC	42.43	-
55	Phosphorylation	FLKWKGFTDADNTWE EEEECCCCCCCCCCC	38.66	24732914
60	Phosphorylation	GFTDADNTWEPEENL CCCCCCCCCCCHHCC	31.58	24732914
69	Glutathionylation	EPEENLDCPELIEAF CCHHCCCCHHHHHHH	2.96	22555962
79	Phosphorylation	LIEAFLNSQKAGKEK HHHHHHHHHHCCCCC	34.89	26074081
81	Acetylation	EAFLNSQKAGKEKDG HHHHHHHHCCCCCCC	59.95	26051181
81	Ubiquitination	EAFLNSQKAGKEKDG HHHHHHHHCCCCCCC	59.95	-
84	Acetylation	LNSQKAGKEKDGTKR HHHHHCCCCCCCCCC	67.46	129451
84	Ubiquitination	LNSQKAGKEKDGTKR HHHHHCCCCCCCCCC	67.46	-
86	Ubiquitination	SQKAGKEKDGTKRKS HHHCCCCCCCCCCCC	66.01	-
89	Phosphorylation	AGKEKDGTKRKSLSD CCCCCCCCCCCCCCC	37.50	26074081
92	Ubiquitination	EKDGTKRKSLSDSES CCCCCCCCCCCCCCC	58.25	21906983
93	Phosphorylation	KDGTKRKSLSDSESD CCCCCCCCCCCCCCC	36.82	29255136
95	Phosphorylation	GTKRKSLSDSESDDS CCCCCCCCCCCCCCC	46.30	29255136
97	Phosphorylation	KRKSLSDSESDDSKS CCCCCCCCCCCCCHH	35.31	29255136
99	Phosphorylation	KSLSDSESDDSKSKK CCCCCCCCCCCHHHH	51.15	29255136
102	Phosphorylation	SDSESDDSKSKKKRD CCCCCCCCHHHHHHH	43.76	29255136
103	Ubiquitination	DSESDDSKSKKKRDA CCCCCCCHHHHHHHH	73.60	21906983
103	Sumoylation	DSESDDSKSKKKRDA CCCCCCCHHHHHHHH	73.60	28112733
103	Acetylation	DSESDDSKSKKKRDA CCCCCCCHHHHHHHH	73.60	25953088
103	Sumoylation	DSESDDSKSKKKRDA CCCCCCCHHHHHHHH	73.60	-
104	Phosphorylation	SESDDSKSKKKRDAA CCCCCCHHHHHHHHH	54.37	24732914
105	Ubiquitination	ESDDSKSKKKRDAAD CCCCCHHHHHHHHHH	67.08	-
113	Ubiquitination	KKRDAADKPRGFARG HHHHHHHCCCCCCCC	31.71	21906983
113	Acetylation	KKRDAADKPRGFARG HHHHHHHCCCCCCCC	31.71	26051181
119	Methylation	DKPRGFARGLDPERI HCCCCCCCCCCHHHE	43.90	-
130	Phosphorylation	PERIIGATDSSGELM HHHEEEEECCCCCEE	31.07	25850435
132	Phosphorylation	RIIGATDSSGELMFL HEEEEECCCCCEEEE	35.57	21712546
133	Phosphorylation	IIGATDSSGELMFLM EEEEECCCCCEEEEE	38.81	22617229
141	Ubiquitination	GELMFLMKWKDSDEA CCEEEEEEECCCCHH	53.92	-
143	Methylation	LMFLMKWKDSDEADL EEEEEEECCCCHHHE	41.66	-
143	Ubiquitination	LMFLMKWKDSDEADL EEEEEEECCCCHHHE	41.66	21906983
143	Acetylation	LMFLMKWKDSDEADL EEEEEEECCCCHHHE	41.66	26051181
145	Phosphorylation	FLMKWKDSDEADLVL EEEEECCCCHHHEEE	33.35	28348404
154	Sumoylation	EADLVLAKEANMKCP HHHEEEHHHHCCCCC	53.88	28112733
154	Ubiquitination	EADLVLAKEANMKCP HHHEEEHHHHCCCCC	53.88	21906983
154	Acetylation	EADLVLAKEANMKCP HHHEEEHHHHCCCCC	53.88	26051181
159	Ubiquitination	LAKEANMKCPQIVIA EHHHHCCCCCEEEEE	42.44	-
160	Glutathionylation	AKEANMKCPQIVIAF HHHHCCCCCEEEEEE	1.77	22555962
168	Phosphorylation	PQIVIAFYEERLTWH CEEEEEEEHHHCCCC	14.09	28152594
173	Phosphorylation	AFYEERLTWHSCPED EEEHHHCCCCCCCHH	27.61	22167270
176	Phosphorylation	EERLTWHSCPEDEAQ HHHCCCCCCCHHHCC	23.95	19664994
177	Glutathionylation	ERLTWHSCPEDEAQ- HHCCCCCCCHHHCC-	2.50	22555962

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
55	T	Phosphorylation	Kinase	AKT1	P31749	PSP
89	T	Phosphorylation	Kinase	AKT1	P31749	PSP
93	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
93	S	Phosphorylation	Kinase	MSK1	O75582	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CBX3_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 CBX3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LBR_HUMAN	LBR	physical	8663349
SP100_HUMAN	SP100	physical	9636147
TIF1B_HUMAN	TRIM28	physical	11336697
CBX1_HUMAN	CBX1	physical	11336697
CBX3_HUMAN	CBX3	physical	11336697
CBX5_HUMAN	CBX5	physical	11336697
PIM1_HUMAN	PIM1	physical	10664448
RING1_HUMAN	RING1	physical	12004135
E2F6_HUMAN	E2F6	physical	12004135
YAF2_HUMAN	YAF2	physical	12004135
PCGF6_HUMAN	PCGF6	physical	12004135
H14_HUMAN	HIST1H1E	physical	19144645
TIF1B_HUMAN	TRIM28	physical	20936779
MGAP_HUMAN	MGA	physical	20936779
NSD3_HUMAN	WHSC1L1	physical	20936779
RELB_HUMAN	RELB	physical	19690169
PAX3_MOUSE	Pax3	physical	16945326
RPB1_HUMAN	POLR2A	physical	16061184
DNM3B_HUMAN	DNMT3B	physical	15120635
TIF1B_HUMAN	TRIM28	physical	10330177
TIF1B_HUMAN	TRIM28	physical	20675861
H31_HUMAN	HIST1H3A	physical	20011120
LMBL2_HUMAN	L3MBTL2	physical	21596310
CHD4_HUMAN	CHD4	physical	21888893
POGZ_HUMAN	POGZ	physical	21888893
ADNP_HUMAN	ADNP	physical	21888893
Z280D_HUMAN	ZNF280D	physical	21888893
TIF1B_HUMAN	TRIM28	physical	21888893
XRCC6_HUMAN	XRCC6	physical	21888893
ZNF8_HUMAN	ZNF8	physical	21888893
CBX3_HUMAN	CBX3	physical	21888893
CBX5_HUMAN	CBX5	physical	21888893
H2AB1_HUMAN	H2AFB1	physical	21888893
ADNP2_HUMAN	ADNP2	physical	21888893
RPB1_HUMAN	POLR2A	physical	22684280
H14_HUMAN	HIST1H1E	physical	22514736
EHMT2_HUMAN	EHMT2	physical	22514736
KLF11_HUMAN	KLF11	physical	22318730
TB182_HUMAN	TNKS1BP1	physical	22939629
H2AY_HUMAN	H2AFY	physical	22939629
PURA2_HUMAN	ADSS	physical	22863883
DCK_HUMAN	DCK	physical	22863883
CH10_HUMAN	HSPE1	physical	22863883
IDHC_HUMAN	IDH1	physical	22863883
SCOT1_HUMAN	OXCT1	physical	22863883
PTMS_HUMAN	PTMS	physical	22863883
TALDO_HUMAN	TALDO1	physical	22863883
THOP1_HUMAN	THOP1	physical	22863883
WDR1_HUMAN	WDR1	physical	22863883
H31_HUMAN	HIST1H3A	physical	24576085
ADNP_HUMAN	ADNP	physical	20850016
POGZ_HUMAN	POGZ	physical	20850016
CBX5_HUMAN	CBX5	physical	20850016
CAF1A_HUMAN	CHAF1A	physical	20850016
MGAP_HUMAN	MGA	physical	20850016
TIF1B_HUMAN	TRIM28	physical	20850016
CAF1B_HUMAN	CHAF1B	physical	20850016
NIPBL_HUMAN	NIPBL	physical	20850016
FAF1_HUMAN	FAF1	physical	26344197
SYAP1_HUMAN	SYAP1	physical	26344197
BARD1_HUMAN	BARD1	physical	25634209

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 CBX3_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-10; LYS-44 AND LYS-50, ANDMASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND MASSSPECTROMETRY.	19369195 [Abstract]
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND MASSSPECTROMETRY.	18318008 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95 AND SER-176, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97 AND SER-176, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93 AND SER-95, AND MASSSPECTROMETRY.	17287340 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93, AND MASSSPECTROMETRY.	16964243 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93 AND SER-95, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; Kim J.-E., Tannenbaum S.R., White F.M.; J. Proteome Res. 4:1339-1346(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93 AND SER-95, AND MASSSPECTROMETRY.	16083285 [Abstract]