dbPTM

CBX8_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CBX8_HUMAN
UniProt AC	Q9HC52
Protein Name	Chromobox protein homolog 8
Gene Name	CBX8
Organism	Homo sapiens (Human).
Sequence Length	389
Subcellular Localization	Nucleus .
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. 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	MELSAVGERVFAAEALLKRRIRKGRMEYLVKWKGWSQKYSTWEPEENILDARLLAAFEEREREMELYGPKKRGPKPKTFLLKAQAKAKAKTYEFRSDSARGIRIPYPGRSPQDLASTSRAREGLRNMGLSPPASSTSTSSTCRAEAPRDRDRDRDRDRERDRERERERERERERERERERGTSRVDDKPSSPGDSSKKRGPKPRKELPDPSQRPLGEPSAGLGEYLKGRKLDDTPSGAGKFPAGHSVIQLARRQDSDLVQCGVTSPSSAEATGKLAVDTFPARVIKHRAAFLEAKGQGALDPNGTRVRHGSGPPSSGGGLYRDMGAQGGRPSLIARIPVARILGDPEEESWSPSLTNLEKVVVTDVTSNFLTVTIKESNTDQGFFKEKR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MELSAVGE -------CCCCHHHH	12.03	-
4	Phosphorylation	----MELSAVGERVF ----CCCCHHHHHHH	13.96	19007248
28	Phosphorylation	IRKGRMEYLVKWKGW HHHCCHHHHEEECCC	13.88	20860994
33	Ubiquitination	MEYLVKWKGWSQKYS HHHHEEECCCCCCCC	44.80	29967540
67	Phosphorylation	REREMELYGPKKRGP HHHHHHHHCCCCCCC	20.34	29496907
70	Ubiquitination	EMELYGPKKRGPKPK HHHHHCCCCCCCCCC	51.22	29967540
92	Phosphorylation	AKAKAKTYEFRSDSA HHHHCCEEEECCCCC	16.62	29496907
96	Phosphorylation	AKTYEFRSDSARGIR CCEEEECCCCCCCCC	41.04	28555341
106	Phosphorylation	ARGIRIPYPGRSPQD CCCCCCCCCCCCHHH	18.89	28102081
110	Phosphorylation	RIPYPGRSPQDLAST CCCCCCCCHHHHHHH	32.59	29255136
116	Phosphorylation	RSPQDLASTSRAREG CCHHHHHHHHHHHHH	33.92	28102081
117	Phosphorylation	SPQDLASTSRAREGL CHHHHHHHHHHHHHH	19.34	24732914
118	Phosphorylation	PQDLASTSRAREGLR HHHHHHHHHHHHHHH	22.80	24732914
130	Phosphorylation	GLRNMGLSPPASSTS HHHHCCCCCCCCCCC	24.10	25159151
134	Phosphorylation	MGLSPPASSTSTSST CCCCCCCCCCCCCCC	39.66	30243723
135	Phosphorylation	GLSPPASSTSTSSTC CCCCCCCCCCCCCCC	28.60	24732914
136	Phosphorylation	LSPPASSTSTSSTCR CCCCCCCCCCCCCCC	33.26	24732914
137	Phosphorylation	SPPASSTSTSSTCRA CCCCCCCCCCCCCCC	28.39	24732914
138	Phosphorylation	PPASSTSTSSTCRAE CCCCCCCCCCCCCCC	27.13	24732914
139	Phosphorylation	PASSTSTSSTCRAEA CCCCCCCCCCCCCCC	24.34	29396449
140	Phosphorylation	ASSTSTSSTCRAEAP CCCCCCCCCCCCCCC	31.45	29396449
141	Phosphorylation	SSTSTSSTCRAEAPR CCCCCCCCCCCCCCC	13.04	29396449
188	Acetylation	GTSRVDDKPSSPGDS CCCCCCCCCCCCCCC	42.19	26051181
190	Phosphorylation	SRVDDKPSSPGDSSK CCCCCCCCCCCCCCC	55.71	29255136
191	Phosphorylation	RVDDKPSSPGDSSKK CCCCCCCCCCCCCCC	41.24	29255136
195	Phosphorylation	KPSSPGDSSKKRGPK CCCCCCCCCCCCCCC	50.39	22167270
196	Phosphorylation	PSSPGDSSKKRGPKP CCCCCCCCCCCCCCC	47.11	22167270
198	Ubiquitination	SPGDSSKKRGPKPRK CCCCCCCCCCCCCCC	65.62	24816145
205	Ubiquitination	KRGPKPRKELPDPSQ CCCCCCCCCCCCCCC	72.61	29967540
205	Acetylation	KRGPKPRKELPDPSQ CCCCCCCCCCCCCCC	72.61	26051181
227	Ubiquitination	AGLGEYLKGRKLDDT CCHHHHHCCCCCCCC	56.63	29967540
234	Phosphorylation	KGRKLDDTPSGAGKF CCCCCCCCCCCCCCC	21.01	25159151
236	Phosphorylation	RKLDDTPSGAGKFPA CCCCCCCCCCCCCCC	43.28	24732914
240	Acetylation	DTPSGAGKFPAGHSV CCCCCCCCCCCCCHH	47.87	23749302
246	Phosphorylation	GKFPAGHSVIQLARR CCCCCCCHHHHHHHH	21.72	24732914
256	Phosphorylation	QLARRQDSDLVQCGV HHHHHCCCCCEECCC	25.22	23927012
264	Phosphorylation	DLVQCGVTSPSSAEA CCEECCCCCCCHHHH	21.87	30266825
265	Phosphorylation	LVQCGVTSPSSAEAT CEECCCCCCCHHHHC	22.00	23927012
267	Phosphorylation	QCGVTSPSSAEATGK ECCCCCCCHHHHCCC	41.78	30266825
268	Phosphorylation	CGVTSPSSAEATGKL CCCCCCCHHHHCCCE	33.25	30278072
272	Phosphorylation	SPSSAEATGKLAVDT CCCHHHHCCCEEHHC	26.76	23927012
274	Acetylation	SSAEATGKLAVDTFP CHHHHCCCEEHHCCC	28.99	26051181
279	Phosphorylation	TGKLAVDTFPARVIK CCCEEHHCCCHHHHH	25.56	28555341
295	Ubiquitination	RAAFLEAKGQGALDP HHHHHHHCCCCCCCC	42.25	-
305	Phosphorylation	GALDPNGTRVRHGSG CCCCCCCCEEECCCC	32.41	-
311	Phosphorylation	GTRVRHGSGPPSSGG CCEEECCCCCCCCCC	41.84	23927012
315	Phosphorylation	RHGSGPPSSGGGLYR ECCCCCCCCCCCCCC	44.76	30266825
316	Phosphorylation	HGSGPPSSGGGLYRD CCCCCCCCCCCCCCC	47.43	23403867
321	Phosphorylation	PSSGGGLYRDMGAQG CCCCCCCCCCCCCCC	14.08	23403867
324	Sulfoxidation	GGGLYRDMGAQGGRP CCCCCCCCCCCCCCC	3.38	21406390
332	Phosphorylation	GAQGGRPSLIARIPV CCCCCCCHHEEECCC	30.92	25159151
350	Phosphorylation	LGDPEEESWSPSLTN HCCCCCCCCCCCCCC	35.81	20068231
352	Phosphorylation	DPEEESWSPSLTNLE CCCCCCCCCCCCCCE	17.56	25159151
354	Phosphorylation	EEESWSPSLTNLEKV CCCCCCCCCCCCEEE	42.16	28102081
356	Phosphorylation	ESWSPSLTNLEKVVV CCCCCCCCCCEEEEE	41.94	30576142
386	Ubiquitination	NTDQGFFKEKR---- CCCCCCCCCCC----	61.13	29967540

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 CBX8_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CBX8_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 CBX8_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HAP1_HUMAN	HAP1	physical	16169070
SETB1_HUMAN	SETDB1	physical	16169070
EF1G_HUMAN	EEF1G	physical	16169070
KAT5_HUMAN	KAT5	physical	16169070
KAT7_HUMAN	KAT7	physical	16169070
U119A_HUMAN	UNC119	physical	16169070
PCGF2_HUMAN	PCGF2	physical	19636380
BMI1_HUMAN	BMI1	physical	19636380
BMI1_HUMAN	BMI1	physical	20601937
UBP7_HUMAN	USP7	physical	20601937
UBP11_HUMAN	USP11	physical	20601937
CBX8_HUMAN	CBX8	physical	20601937
KMT2A_HUMAN	KMT2A	physical	22094252
KAT5_HUMAN	KAT5	physical	22094252
BCLF1_HUMAN	BCLAF1	physical	21282530
BMI1_HUMAN	BMI1	physical	21282530
CSK21_HUMAN	CSNK2A1	physical	21282530
CSK2B_HUMAN	CSNK2B	physical	21282530
YBOX3_HUMAN	YBX3	physical	21282530
DGKZ_HUMAN	DGKZ	physical	21282530
DIM1_HUMAN	DIMT1	physical	21282530
DNLI3_HUMAN	LIG3	physical	21282530
EP300_HUMAN	EP300	physical	21282530
ESCO2_HUMAN	ESCO2	physical	21282530
FBRL_HUMAN	FBL	physical	21282530
RACK1_HUMAN	GNB2L1	physical	21282530
H2B1A_HUMAN	HIST1H2BA	physical	21282530
IF2B1_HUMAN	IGF2BP1	physical	21282530
IF2B2_HUMAN	IGF2BP2	physical	21282530
IF2B3_HUMAN	IGF2BP3	physical	21282530
ILF2_HUMAN	ILF2	physical	21282530
ILF3_HUMAN	ILF3	physical	21282530
JIP4_HUMAN	SPAG9	physical	21282530
KRI1_HUMAN	KRI1	physical	21282530
KRR1_HUMAN	KRR1	physical	21282530
LTV1_HUMAN	LTV1	physical	21282530
MK67I_HUMAN	NIFK	physical	21282530
MOV10_HUMAN	MOV10	physical	21282530
KI20B_HUMAN	KIF20B	physical	21282530
NBN_HUMAN	NBN	physical	21282530
OGA_HUMAN	MGEA5	physical	21282530
NFIL3_HUMAN	NFIL3	physical	21282530
NOG1_HUMAN	GTPBP4	physical	21282530
NOP2_HUMAN	NOP2	physical	21282530
NPM_HUMAN	NPM1	physical	21282530
HMGN5_HUMAN	HMGN5	physical	21282530
NUCL_HUMAN	NCL	physical	21282530
PCGF1_HUMAN	PCGF1	physical	21282530
PCGF2_HUMAN	PCGF2	physical	21282530
PCGF3_HUMAN	PCGF3	physical	21282530
PCGF5_HUMAN	PCGF5	physical	21282530
PCGF6_HUMAN	PCGF6	physical	21282530
PHC2_HUMAN	PHC2	physical	21282530
RING1_HUMAN	RING1	physical	21282530
RING2_HUMAN	RNF2	physical	21282530
RRP5_HUMAN	PDCD11	physical	21282530
SETD2_HUMAN	SETD2	physical	21282530
SSF1_HUMAN	PPAN	physical	21282530
STAU1_HUMAN	STAU1	physical	21282530
THOC4_HUMAN	ALYREF	physical	21282530
TSR1_HUMAN	TSR1	physical	21282530
UBR1_HUMAN	UBR1	physical	21282530
YBOX1_HUMAN	YBX1	physical	21282530
YTDC2_HUMAN	YTHDC2	physical	21282530
ZCHC3_HUMAN	ZCCHC3	physical	21282530
ZFR_HUMAN	ZFR	physical	21282530
CHAP1_HUMAN	CHAMP1	physical	21282530
CC136_HUMAN	CCDC136	physical	25416956
HMBX1_HUMAN	HMBOX1	physical	25416956
TSG10_HUMAN	TSGA10	physical	25416956
LZTS2_HUMAN	LZTS2	physical	25416956
GASP2_HUMAN	GPRASP2	physical	25416956
FSD2_HUMAN	FSD2	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956
CCD57_HUMAN	CCDC57	physical	25416956
BMI1_HUMAN	BMI1	physical	26496610
CENPB_HUMAN	CENPB	physical	26496610
E2F6_HUMAN	E2F6	physical	26496610
PHC1_HUMAN	PHC1	physical	26496610
PHC2_HUMAN	PHC2	physical	26496610
H15_HUMAN	HIST1H1B	physical	26496610
NUMA1_HUMAN	NUMA1	physical	26496610
PSB7_HUMAN	PSMB7	physical	26496610
RING1_HUMAN	RING1	physical	26496610
RING2_HUMAN	RNF2	physical	26496610
RL10_HUMAN	RPL10	physical	26496610
RL18A_HUMAN	RPL18A	physical	26496610
RL22_HUMAN	RPL22	physical	26496610
RS3A_HUMAN	RPS3A	physical	26496610
RS6_HUMAN	RPS6	physical	26496610
RS8_HUMAN	RPS8	physical	26496610
RS12_HUMAN	RPS12	physical	26496610
RS14_HUMAN	RPS14	physical	26496610
RS20_HUMAN	RPS20	physical	26496610
CBX4_HUMAN	CBX4	physical	26496610
H1X_HUMAN	H1FX	physical	26496610
TF3C4_HUMAN	GTF3C4	physical	26496610
SCML2_HUMAN	SCML2	physical	26496610
BAZ2A_HUMAN	BAZ2A	physical	26496610
ICE1_HUMAN	ICE1	physical	26496610
LCOR_HUMAN	C10orf12	physical	26496610
RL1D1_HUMAN	RSL1D1	physical	26496610
EXOS4_HUMAN	EXOSC4	physical	26496610
CHSTC_HUMAN	CHST12	physical	26496610
ZCCHV_HUMAN	ZC3HAV1	physical	26496610
DDX54_HUMAN	DDX54	physical	26496610
PHC3_HUMAN	PHC3	physical	26496610
CMS1_HUMAN	CMSS1	physical	26496610
PCGF5_HUMAN	PCGF5	physical	26496610
ESCO1_HUMAN	ESCO1	physical	26496610
SPB1_HUMAN	FTSJ3	physical	26496610

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 CBX8_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 AND SER-110,ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.	19007248 [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-110; SER-256 ANDSER-311, AND MASS SPECTROMETRY.	19690332 [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-110; SER-130; SER-256;SER-265; SER-332 AND SER-352, AND MASS SPECTROMETRY.	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-110 AND SER-265, ANDMASS SPECTROMETRY.	18691976 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 AND SER-110,ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.	19007248 [Abstract]