dbPTM

CBX4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CBX4_HUMAN
UniProt AC	O00257
Protein Name	E3 SUMO-protein ligase CBX4
Gene Name	CBX4
Organism	Homo sapiens (Human).
Sequence Length	560
Subcellular Localization	Nucleus . Nucleus speckle . Localization to nuclear polycomb bodies is required for ZNF131 sumoylation (PubMed:22467880). Localized in distinct foci on chromatin (PubMed:18927235).
Protein Description	E3 SUMO-protein ligase which facilitates SUMO1 conjugation by UBE2I. [PubMed: 12679040 Involved in the sumoylation of HNRNPK, a p53/TP53 transcriptional coactivator, hence indirectly regulates p53/TP53 transcriptional activation resulting in p21/CDKN1A expression. Monosumoylates ZNF131]
Protein Sequence	MELPAVGEHVFAVESIEKKRIRKGRVEYLVKWRGWSPKYNTWEPEENILDPRLLIAFQNRERQEQLMGYRKRGPKPKPLVVQVPTFARRSNVLTGLQDSSTDNRAKLDLGAQGKGQGHQYELNSKKHHQYQPHSKERAGKPPPPGKSGKYYYQLNSKKHHPYQPDPKMYDLQYQGGHKEAPSPTCPDLGAKSHPPDKWAQGAGAKGYLGAVKPLAGAAGAPGKGSEKGPPNGMMPAPKEAVTGNGIGGKMKIVKNKNKNGRIVIVMSKYMENGMQAVKIKSGEVAEGEARSPSHKKRAADERHPPADRTFKKAAGAEEKKVEAPPKRREEEVSGVSDPQPQDAGSRKLSPTKEAFGEQPLQLTTKPDLLAWDPARNTHPPSHHPHPHPHHHHHHHHHHHHAVGLNLSHVRKRCLSETHGEREPCKKRLTARSISTPTCLGGSPAAERPADLPPAAALPQPEVILLDSDLDEPIDLRCVKTRSEAGEPPSSLQVKPETPASAAVAVAAAAAPTTTAEKPPAEAQDEPAESLSEFKPFFGNIIITDVTANCLTVTFKEYVTV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
28	Phosphorylation	IRKGRVEYLVKWRGW CCCCCCEEEEEECCC	17.59	-
36	Phosphorylation	LVKWRGWSPKYNTWE EEEECCCCCCCCCCC	17.84	24719451
38	Ubiquitination	KWRGWSPKYNTWEPE EECCCCCCCCCCCCH	45.69	-
77	Sumoylation	RKRGPKPKPLVVQVP HHCCCCCCCEEEECC	58.05	28112733
90	Phosphorylation	VPTFARRSNVLTGLQ CCCCCHHCCCCCCCC	26.24	28985074
94	Phosphorylation	ARRSNVLTGLQDSST CHHCCCCCCCCCCCC	31.40	29978859
99	Phosphorylation	VLTGLQDSSTDNRAK CCCCCCCCCCCCCEE	23.37	29978859
100	Phosphorylation	LTGLQDSSTDNRAKL CCCCCCCCCCCCEEE	48.33	29978859
101	Phosphorylation	TGLQDSSTDNRAKLD CCCCCCCCCCCEEEE	41.04	29978859
106	Sumoylation	SSTDNRAKLDLGAQG CCCCCCEEEECCCCC	39.02	28112733
106	Acetylation	SSTDNRAKLDLGAQG CCCCCCEEEECCCCC	39.02	25953088
106	Ubiquitination	SSTDNRAKLDLGAQG CCCCCCEEEECCCCC	39.02	-
106	Sumoylation	SSTDNRAKLDLGAQG CCCCCCEEEECCCCC	39.02	-
114	Sumoylation	LDLGAQGKGQGHQYE EECCCCCCCCCCEEE	35.66	28112733
114	Sumoylation	LDLGAQGKGQGHQYE EECCCCCCCCCCEEE	35.66	-
114	Ubiquitination	LDLGAQGKGQGHQYE EECCCCCCCCCCEEE	35.66	-
120	Phosphorylation	GKGQGHQYELNSKKH CCCCCCEEECCCCCC	19.40	27642862
125	Ubiquitination	HQYELNSKKHHQYQP CEEECCCCCCCCCCC	55.86	-
125	Acetylation	HQYELNSKKHHQYQP CEEECCCCCCCCCCC	55.86	25953088
125	Sumoylation	HQYELNSKKHHQYQP CEEECCCCCCCCCCC	55.86	28112733
137	Methylation	YQPHSKERAGKPPPP CCCCCCCCCCCCCCC	52.99	-
147	Phosphorylation	KPPPPGKSGKYYYQL CCCCCCCCCCEEEEE	46.57	25072903
149	Ubiquitination	PPPGKSGKYYYQLNS CCCCCCCCEEEEECC	36.85	19608861
149	Acetylation	PPPGKSGKYYYQLNS CCCCCCCCEEEEECC	36.85	19608861
149	Sumoylation	PPPGKSGKYYYQLNS CCCCCCCCEEEEECC	36.85	-
149	Sumoylation	PPPGKSGKYYYQLNS CCCCCCCCEEEEECC	36.85	28112733
150	Phosphorylation	PPGKSGKYYYQLNSK CCCCCCCEEEEECCC	15.78	25072903
151	Phosphorylation	PGKSGKYYYQLNSKK CCCCCCEEEEECCCC	6.55	25072903
152	Phosphorylation	GKSGKYYYQLNSKKH CCCCCEEEEECCCCC	11.93	25072903
157	Acetylation	YYYQLNSKKHHPYQP EEEEECCCCCCCCCC	55.86	25953088
157	Sumoylation	YYYQLNSKKHHPYQP EEEEECCCCCCCCCC	55.86	28112733
158	Ubiquitination	YYQLNSKKHHPYQPD EEEECCCCCCCCCCC	47.14	-
167	Sumoylation	HPYQPDPKMYDLQYQ CCCCCCCCCCCCCCC	58.43	28112733
167	Ubiquitination	HPYQPDPKMYDLQYQ CCCCCCCCCCCCCCC	58.43	-
169	Phosphorylation	YQPDPKMYDLQYQGG CCCCCCCCCCCCCCC	21.45	26552605
173	Phosphorylation	PKMYDLQYQGGHKEA CCCCCCCCCCCCCCC	19.20	29214152
178	Ubiquitination	LQYQGGHKEAPSPTC CCCCCCCCCCCCCCC	59.87	-
178	Sumoylation	LQYQGGHKEAPSPTC CCCCCCCCCCCCCCC	59.87	28112733
182	Phosphorylation	GGHKEAPSPTCPDLG CCCCCCCCCCCCCCC	39.63	30266825
184	Phosphorylation	HKEAPSPTCPDLGAK CCCCCCCCCCCCCCC	40.79	30266825
191	Sumoylation	TCPDLGAKSHPPDKW CCCCCCCCCCCCCHH	47.72	28112733
197	Acetylation	AKSHPPDKWAQGAGA CCCCCCCHHHCCCCC	50.64	25953088
197	Ubiquitination	AKSHPPDKWAQGAGA CCCCCCCHHHCCCCC	50.64	-
205	Sumoylation	WAQGAGAKGYLGAVK HHCCCCCCCCHHCHH	47.36	-
205	Ubiquitination	WAQGAGAKGYLGAVK HHCCCCCCCCHHCHH	47.36	-
205	Sumoylation	WAQGAGAKGYLGAVK HHCCCCCCCCHHCHH	47.36	28112733
207	Phosphorylation	QGAGAKGYLGAVKPL CCCCCCCCHHCHHCC	10.97	18083107
212	Ubiquitination	KGYLGAVKPLAGAAG CCCHHCHHCCCCCCC	33.51	-
212	Acetylation	KGYLGAVKPLAGAAG CCCHHCHHCCCCCCC	33.51	25953088
212	Sumoylation	KGYLGAVKPLAGAAG CCCHHCHHCCCCCCC	33.51	-
212	Sumoylation	KGYLGAVKPLAGAAG CCCHHCHHCCCCCCC	33.51	28112733
223	Sumoylation	GAAGAPGKGSEKGPP CCCCCCCCCCCCCCC	59.20	28112733
223	Sumoylation	GAAGAPGKGSEKGPP CCCCCCCCCCCCCCC	59.20	-
223	Ubiquitination	GAAGAPGKGSEKGPP CCCCCCCCCCCCCCC	59.20	-
249	Sumoylation	TGNGIGGKMKIVKNK CCCCCCCCEEEEECC	31.63	28112733
249	Sumoylation	TGNGIGGKMKIVKNK CCCCCCCCEEEEECC	31.63	-
249	Ubiquitination	TGNGIGGKMKIVKNK CCCCCCCCEEEEECC	31.63	-
249	Methylation	TGNGIGGKMKIVKNK CCCCCCCCEEEEECC	31.63	-
249	Acetylation	TGNGIGGKMKIVKNK CCCCCCCCEEEEECC	31.63	25953088
267	Phosphorylation	GRIVIVMSKYMENGM CCEEEEECHHHHCCE	15.11	20068231
268	Sumoylation	RIVIVMSKYMENGMQ CEEEEECHHHHCCEE	30.44	28112733
269	Phosphorylation	IVIVMSKYMENGMQA EEEEECHHHHCCEEE	11.45	20068231
278	Ubiquitination	ENGMQAVKIKSGEVA HCCEEEEEEECCCCC	47.64	-
278	Sumoylation	ENGMQAVKIKSGEVA HCCEEEEEEECCCCC	47.64	-
278	Sumoylation	ENGMQAVKIKSGEVA HCCEEEEEEECCCCC	47.64	28112733
280	Ubiquitination	GMQAVKIKSGEVAEG CEEEEEEECCCCCCC	46.84	-
280	Sumoylation	GMQAVKIKSGEVAEG CEEEEEEECCCCCCC	46.84	28112733
280	Sumoylation	GMQAVKIKSGEVAEG CEEEEEEECCCCCCC	46.84	-
281	Phosphorylation	MQAVKIKSGEVAEGE EEEEEEECCCCCCCC	43.59	29396449
291	Phosphorylation	VAEGEARSPSHKKRA CCCCCCCCHHHHHHH	37.49	23401153
293	Phosphorylation	EGEARSPSHKKRAAD CCCCCCHHHHHHHHH	49.54	21955146
320	Sumoylation	AAGAEEKKVEAPPKR HCCCHHHCCCCCCCC	48.89	28112733
333	Phosphorylation	KRREEEVSGVSDPQP CCCHHHHCCCCCCCC	36.44	26074081
336	Phosphorylation	EEEVSGVSDPQPQDA HHHHCCCCCCCCCCC	47.28	20044836
345	Phosphorylation	PQPQDAGSRKLSPTK CCCCCCCCCCCCCCH	28.14	28985074
349	Phosphorylation	DAGSRKLSPTKEAFG CCCCCCCCCCHHHHC	33.29	23927012
351	Phosphorylation	GSRKLSPTKEAFGEQ CCCCCCCCHHHHCCC	37.83	23927012
352	Sumoylation	SRKLSPTKEAFGEQP CCCCCCCHHHHCCCC	50.89	28112733
363	Phosphorylation	GEQPLQLTTKPDLLA CCCCCCCCCCCCCEE	21.58	23927012
364	Phosphorylation	EQPLQLTTKPDLLAW CCCCCCCCCCCCEEC	49.53	23927012
365	Sumoylation	QPLQLTTKPDLLAWD CCCCCCCCCCCEECC	31.16	28112733
365 (in isoform 1)	Ubiquitination	-	31.16	21906983
365	Sumoylation	QPLQLTTKPDLLAWD CCCCCCCCCCCEECC	31.16	-
365	Ubiquitination	QPLQLTTKPDLLAWD CCCCCCCCCCCEECC	31.16	2190698
415	Phosphorylation	HVRKRCLSETHGERE HHHHHHHHHCCCCCC	44.04	29255136
417	Phosphorylation	RKRCLSETHGEREPC HHHHHHHCCCCCCCC	31.63	19276368
429	Phosphorylation	EPCKKRLTARSISTP CCCHHHHCCCCCCCC	24.86	26074081
432	Phosphorylation	KKRLTARSISTPTCL HHHHCCCCCCCCCCC	20.58	29255136
434	Phosphorylation	RLTARSISTPTCLGG HHCCCCCCCCCCCCC	29.58	29255136
435	Phosphorylation	LTARSISTPTCLGGS HCCCCCCCCCCCCCC	22.43	23663014
437	Phosphorylation	ARSISTPTCLGGSPA CCCCCCCCCCCCCCC	22.05	29255136
442	Phosphorylation	TPTCLGGSPAAERPA CCCCCCCCCCCCCCC	15.01	28387310
467	Phosphorylation	PEVILLDSDLDEPID CCEEEECCCCCCCEE	39.79	27499020
480	Phosphorylation	IDLRCVKTRSEAGEP EEEEEEECCCCCCCC	21.01	26074081
482	Phosphorylation	LRCVKTRSEAGEPPS EEEEECCCCCCCCCC	36.71	26074081
494	Sumoylation	PPSSLQVKPETPASA CCCCCCCCCCCCHHH	24.95	-
494	Sumoylation	PPSSLQVKPETPASA CCCCCCCCCCCCHHH	24.95	15592428
495	Phosphorylation	PSSLQVKPETPASAA CCCCCCCCCCCHHHH	52.41	17018294
497	Phosphorylation	SLQVKPETPASAAVA CCCCCCCCCHHHHHH	32.45	28112733

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
495	T	Phosphorylation	Kinase	HIPK2	Q9H2X6	PhosphoELM
497	T	Phosphorylation	Kinase	HIPK2	Q9H2X6	Uniprot
497	T	Phosphorylation	Kinase	P38A	Q16539	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
494	K	Phosphorylation	15592428
This phosphorylation stimulates E3 SUMO-protein ligase activity and promotes sumoylation on Lys-494, as well as sumoylation of other target proteins, such as HNRNPK.
494	K	Sumoylation	15592428
This phosphorylation stimulates E3 SUMO-protein ligase activity and promotes sumoylation on Lys-494, as well as sumoylation of other target proteins, such as HNRNPK.
497	T	Phosphorylation	17018294
Phosphorylated on Thr-497 by HIPK2 upon DNA damage.

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 CBX4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KMT2A_HUMAN	KMT2A	physical	12829790
CTBP1_HUMAN	CTBP1	physical	12829790
BMI1_HUMAN	BMI1	physical	12829790
CTBP1_HUMAN	CTBP1	physical	12679040
RING1_HUMAN	RING1	physical	9199346
BMI1_HUMAN	BMI1	physical	9199346
PHC1_HUMAN	PHC1	physical	9199346
RB_HUMAN	RB1	genetic	11583618
CTBP1_HUMAN	CTBP1	physical	9858600
CTBP2_HUMAN	CTBP2	physical	9858600
KDM5B_HUMAN	KDM5B	physical	19336002
SUV91_HUMAN	SUV39H1	physical	12101246
DNM3A_HUMAN	DNMT3A	physical	17439403
H31T_HUMAN	HIST3H3	physical	12700765
SYUA_HUMAN	SNCA	physical	21256122
RING2_HUMAN	RNF2	physical	22325352
PCGF2_HUMAN	PCGF2	physical	22325352
BMI1_HUMAN	BMI1	physical	22325352
RING1_HUMAN	RING1	physical	22325352
PHC1_HUMAN	PHC1	physical	22325352
PHC2_HUMAN	PHC2	physical	22325352
PHC3_HUMAN	PHC3	physical	22325352
CBX8_HUMAN	CBX8	physical	22325352
SCMH1_HUMAN	SCMH1	physical	22325352
MGAP_HUMAN	MGA	physical	22325352
ZEB2_HUMAN	ZEB2	physical	16061479
HNRPK_HUMAN	HNRNPK	physical	22825850
ZN131_HUMAN	ZNF131	physical	22467880
ANR26_HUMAN	ANKRD26	physical	21282530
BMI1_HUMAN	BMI1	physical	21282530
CBX2_HUMAN	CBX2	physical	21282530
CENPE_HUMAN	CENPE	physical	21282530
CSK21_HUMAN	CSNK2A1	physical	21282530
CSK22_HUMAN	CSNK2A2	physical	21282530
CSK2B_HUMAN	CSNK2B	physical	21282530
DI3L2_HUMAN	DIS3L2	physical	21282530
GTF2I_HUMAN	GTF2I	physical	21282530
H2B1B_HUMAN	HIST1H2BB	physical	21282530
1433B_HUMAN	YWHAB	physical	21282530
DCAF6_HUMAN	DCAF6	physical	21282530
KDM3A_HUMAN	KDM3A	physical	21282530
TRNK1_HUMAN	TRANK1	physical	21282530
MYCB2_HUMAN	MYCBP2	physical	21282530
NPM_HUMAN	NPM1	physical	21282530
PAR12_HUMAN	PARP12	physical	21282530
PARP1_HUMAN	PARP1	physical	21282530
PHC2_HUMAN	PHC2	physical	21282530
PSME3_HUMAN	PSME3	physical	21282530
RING2_HUMAN	RNF2	physical	21282530
RN213_HUMAN	RNF213	physical	21282530
CD158_HUMAN	CCDC158	physical	21282530
ZKSC7_HUMAN	ZKSCAN7	physical	21282530
CBX4_HUMAN	CBX4	physical	21282530
1433E_HUMAN	YWHAE	physical	21282530
1433Z_HUMAN	YWHAZ	physical	21282530
BMI1_HUMAN	BMI1	physical	26496610
PHC1_HUMAN	PHC1	physical	26496610
PHC2_HUMAN	PHC2	physical	26496610
H33_HUMAN	H3F3A	physical	26496610
HELLS_HUMAN	HELLS	physical	26496610
MYL6_HUMAN	MYL6	physical	26496610
RAD51_HUMAN	RAD51	physical	26496610
RING1_HUMAN	RING1	physical	26496610
RING2_HUMAN	RNF2	physical	26496610
SDC2_HUMAN	SDC2	physical	26496610
TXTP_HUMAN	SLC25A1	physical	26496610
TTC1_HUMAN	TTC1	physical	26496610
1433T_HUMAN	YWHAQ	physical	26496610
KDM2A_HUMAN	KDM2A	physical	26496610
S18L2_HUMAN	SS18L2	physical	26496610
TMA16_HUMAN	TMA16	physical	26496610
IMPCT_HUMAN	IMPACT	physical	26496610
CBX8_HUMAN	CBX8	physical	26496610
WIZ_HUMAN	WIZ	physical	26496610
PHC3_HUMAN	PHC3	physical	26496610
USMG5_HUMAN	USMG5	physical	26496610
RM55_HUMAN	MRPL55	physical	26496610
LAMA1_HUMAN	LAMA1	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 CBX4_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-149, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
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-90, AND MASSSPECTROMETRY.	19007248 [Abstract]
Sumoylation
Reference	PubMed
"Multiple activities contribute to Pc2 E3 function."; Kagey M.H., Melhuish T.A., Powers S.E., Wotton D.; EMBO J. 24:108-119(2005). Cited for: SUMOYLATION AT LYS-494.	15592428 [Abstract]

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