dbPTM

RYBP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RYBP_HUMAN
UniProt AC	Q8N488
Protein Name	RING1 and YY1-binding protein
Gene Name	RYBP
Organism	Homo sapiens (Human).
Sequence Length	228
Subcellular Localization	Nucleus . Cytoplasm . Nucleus, nucleoplasm . Primarily found in the nucleus. Detected in a punctate pattern likely to represent Polycomb group (PcG) bodies (By similarity).
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-like complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. [PubMed: 25519132 Component of a PRC1-like complex that mediates monoubiquitination of histone H2A 'Lys-119' on the X chromosome and is required for normal silencing of one copy of the X chromosome in XX females. May stimulate ubiquitination of histone H2A 'Lys-119' by recruiting the complex to target sites (By similarity Inhibits ubiquitination and subsequent degradation of TP53, and thereby plays a role in regulating transcription of TP53 target genes]
Protein Sequence	MTMGDKKSPTRPKRQAKPAADEGFWDCSVCTFRNSAEAFKCSICDVRKGTSTRKPRINSQLVAQQVAQQYATPPPPKKEKKEKVEKQDKEKPEKDKEISPSVTKKNTNKKTKPKSDILKDPPSEANSIQSANATTKTSETNHTSRPRLKNVDRSTAQQLAVTVGNVTVIITDFKEKTRSSSTSSSTVTSSAGSEQQNQSSSGSESTDKGSSRSSTPKGDMSAVNDESF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Phosphorylation	MTMGDKKSPTRPKRQ CCCCCCCCCCCCCCC	36.93	17081983
10	Phosphorylation	MGDKKSPTRPKRQAK CCCCCCCCCCCCCCC	67.69	20068231
17	Ubiquitination	TRPKRQAKPAADEGF CCCCCCCCCCCCCCC	27.18	32015554
40	Methylation	RNSAEAFKCSICDVR ECCCHHHCCEECCCC	33.83	115977433
40	Ubiquitination	RNSAEAFKCSICDVR ECCCHHHCCEECCCC	33.83	33845483
59	Phosphorylation	TRKPRINSQLVAQQV CCCCCCCHHHHHHHH	23.63	26055452
70	Phosphorylation	AQQVAQQYATPPPPK HHHHHHHHCCCCCCC	10.60	28796482
72	Phosphorylation	QVAQQYATPPPPKKE HHHHHHCCCCCCCHH	31.24	25159151
77	Sumoylation	YATPPPPKKEKKEKV HCCCCCCCHHHHHHH	78.37	28112733
99	Phosphorylation	PEKDKEISPSVTKKN CCCCCCCCCCCCCCC	16.53	29255136
101	Phosphorylation	KDKEISPSVTKKNTN CCCCCCCCCCCCCCC	35.31	30266825
103	Phosphorylation	KEISPSVTKKNTNKK CCCCCCCCCCCCCCC	40.41	22167270
104	Acetylation	EISPSVTKKNTNKKT CCCCCCCCCCCCCCC	41.70	25953088
104	Ubiquitination	EISPSVTKKNTNKKT CCCCCCCCCCCCCCC	41.70	32015554
107	Phosphorylation	PSVTKKNTNKKTKPK CCCCCCCCCCCCCCH	58.24	-
114	Ubiquitination	TNKKTKPKSDILKDP CCCCCCCHHHHHCCC	63.42	23000965
115	Phosphorylation	NKKTKPKSDILKDPP CCCCCCHHHHHCCCH	38.11	25159151
119	Ubiquitination	KPKSDILKDPPSEAN CCHHHHHCCCHHHHH	69.40	23000965
123	Phosphorylation	DILKDPPSEANSIQS HHHCCCHHHHHHHHH	55.52	30266825
127	Phosphorylation	DPPSEANSIQSANAT CCHHHHHHHHHCCCC	29.11	23401153
130	Phosphorylation	SEANSIQSANATTKT HHHHHHHHCCCCCCC	23.09	23401153
134	Phosphorylation	SIQSANATTKTSETN HHHHCCCCCCCCCCC	28.74	22199227
135	Phosphorylation	IQSANATTKTSETNH HHHCCCCCCCCCCCC	29.89	22199227
136	Ubiquitination	QSANATTKTSETNHT HHCCCCCCCCCCCCC	45.78	21906983
154	Phosphorylation	RLKNVDRSTAQQLAV CCCCCCHHHHHHHHH	24.51	20068231
155	Phosphorylation	LKNVDRSTAQQLAVT CCCCCHHHHHHHHHE	29.40	20068231
162	Phosphorylation	TAQQLAVTVGNVTVI HHHHHHHEECCEEEE	19.65	20068231
167	Phosphorylation	AVTVGNVTVIITDFK HHEECCEEEEEECCC	15.24	20068231
171	Phosphorylation	GNVTVIITDFKEKTR CCEEEEEECCCHHHC	25.02	20068231
177	Phosphorylation	ITDFKEKTRSSSTSS EECCCHHHCCCCCCC	36.55	28450419
179	Phosphorylation	DFKEKTRSSSTSSST CCCHHHCCCCCCCCE	33.59	25159151
180	Phosphorylation	FKEKTRSSSTSSSTV CCHHHCCCCCCCCEE	34.05	28450419
181	Phosphorylation	KEKTRSSSTSSSTVT CHHHCCCCCCCCEEE	33.29	30206219
182	Phosphorylation	EKTRSSSTSSSTVTS HHHCCCCCCCCEEEC	34.28	28450419
183	Phosphorylation	KTRSSSTSSSTVTSS HHCCCCCCCCEEECC	25.00	30206219
184	Phosphorylation	TRSSSTSSSTVTSSA HCCCCCCCCEEECCC	30.07	28450419
185	Phosphorylation	RSSSTSSSTVTSSAG CCCCCCCCEEECCCC	27.02	28450419
186	Phosphorylation	SSSTSSSTVTSSAGS CCCCCCCEEECCCCC	29.74	25262027
188	Phosphorylation	STSSSTVTSSAGSEQ CCCCCEEECCCCCCC	19.63	30206219
189	Phosphorylation	TSSSTVTSSAGSEQQ CCCCEEECCCCCCCC	17.54	28450419
190	Phosphorylation	SSSTVTSSAGSEQQN CCCEEECCCCCCCCC	27.55	28450419
193	Phosphorylation	TVTSSAGSEQQNQSS EEECCCCCCCCCCCC	31.76	28450419
199	Phosphorylation	GSEQQNQSSSGSEST CCCCCCCCCCCCCCC	33.74	25159151
200	Phosphorylation	SEQQNQSSSGSESTD CCCCCCCCCCCCCCC	29.02	25262027
201	Phosphorylation	EQQNQSSSGSESTDK CCCCCCCCCCCCCCC	52.14	25262027
203	Phosphorylation	QNQSSSGSESTDKGS CCCCCCCCCCCCCCC	30.26	28450419
205	Phosphorylation	QSSSGSESTDKGSSR CCCCCCCCCCCCCCC	43.53	28450419
206	Phosphorylation	SSSGSESTDKGSSRS CCCCCCCCCCCCCCC	37.36	28450419
208	Ubiquitination	SGSESTDKGSSRSST CCCCCCCCCCCCCCC	61.86	-
210	Phosphorylation	SESTDKGSSRSSTPK CCCCCCCCCCCCCCC	28.46	28102081
211	Phosphorylation	ESTDKGSSRSSTPKG CCCCCCCCCCCCCCC	44.87	28102081
213	Phosphorylation	TDKGSSRSSTPKGDM CCCCCCCCCCCCCCC	40.28	22617229
214	Phosphorylation	DKGSSRSSTPKGDMS CCCCCCCCCCCCCCC	47.85	25159151
215	Phosphorylation	KGSSRSSTPKGDMSA CCCCCCCCCCCCCCC	30.21	25159151
221	Phosphorylation	STPKGDMSAVNDESF CCCCCCCCCCCCCCC	33.53	22115753
227	Phosphorylation	MSAVNDESF------ CCCCCCCCC------	38.84	25159151

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
-	K	Ubiquitination	E3 ubiquitin ligase	RNF2	Q99496	PMID:17070805

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
E2F6_HUMAN	E2F6	physical	11171983
RING1_HUMAN	RING1	physical	10369680
CBX2_HUMAN	CBX2	physical	10369680
TYY1_HUMAN	YY1	physical	10369680
CASPA_HUMAN	CASP10	physical	11395500
FADD_HUMAN	FADD	physical	11395500
ABL1_HUMAN	ABL1	physical	8943360
MDM2_HUMAN	MDM2	physical	19098711
P53_HUMAN	TP53	physical	19098711
RING1_HUMAN	RING1	physical	16943429
RING2_HUMAN	RNF2	physical	16943429
RING2_HUMAN	RNF2	physical	22325352
PCGF1_HUMAN	PCGF1	physical	22325352
PCGF2_HUMAN	PCGF2	physical	22325352
PCGF3_HUMAN	PCGF3	physical	22325352
BMI1_HUMAN	BMI1	physical	22325352
PCGF5_HUMAN	PCGF5	physical	22325352
PCGF6_HUMAN	PCGF6	physical	22325352
RING1_HUMAN	RING1	physical	22325352
LMBL2_HUMAN	L3MBTL2	physical	22325352
CBX3_HUMAN	CBX3	physical	22325352
E2F6_HUMAN	E2F6	physical	22325352
TFDP1_HUMAN	TFDP1	physical	22325352
WDR5_HUMAN	WDR5	physical	22325352
MGAP_HUMAN	MGA	physical	22325352
SKP1_HUMAN	SKP1	physical	22325352
BCOR_HUMAN	BCOR	physical	22325352
BCORL_HUMAN	BCORL1	physical	22325352
KDM2B_HUMAN	KDM2B	physical	22325352
UBP7_HUMAN	USP7	physical	22325352
FBRS_HUMAN	FBRS	physical	22325352
FBSL_HUMAN	FBRSL1	physical	22325352
CSK21_HUMAN	CSNK2A1	physical	22325352
CSK22_HUMAN	CSNK2A2	physical	22325352
CSK2B_HUMAN	CSNK2B	physical	22325352
TYY1_HUMAN	YY1	physical	11953439
GABP1_HUMAN	GABPB1	physical	11953439
PCGF3_HUMAN	PCGF3	physical	26186194
UBP7_HUMAN	USP7	physical	26186194
BCOR_HUMAN	BCOR	physical	26186194
BCORL_HUMAN	BCORL1	physical	26186194
MORC4_HUMAN	MORC4	physical	26186194
TFDP1_HUMAN	TFDP1	physical	26186194
KDM2B_HUMAN	KDM2B	physical	26186194
MCAF1_HUMAN	ATF7IP	physical	26186194
FBRS_HUMAN	FBRS	physical	26186194
MGAP_HUMAN	MGA	physical	26186194
HERC2_HUMAN	HERC2	physical	26186194
CSK21_HUMAN	CSNK2A1	physical	26186194
AUTS2_HUMAN	AUTS2	physical	26186194
CSK2B_HUMAN	CSNK2B	physical	26186194
RING2_HUMAN	RNF2	physical	26186194
RING1_HUMAN	RING1	physical	26186194
LMBL2_HUMAN	L3MBTL2	physical	26186194
PCGF1_HUMAN	PCGF1	physical	26186194
PCGF6_HUMAN	PCGF6	physical	26186194
FBSL_HUMAN	FBRSL1	physical	26186194
PCGF2_HUMAN	PCGF2	physical	26186194
BMI1_HUMAN	BMI1	physical	26186194
FANK1_HUMAN	FANK1	physical	27060496
CASP8_HUMAN	CASP8	physical	27989698
PCGF1_HUMAN	PCGF1	physical	28514442
PCGF3_HUMAN	PCGF3	physical	28514442
LMBL2_HUMAN	L3MBTL2	physical	28514442
KDM2B_HUMAN	KDM2B	physical	28514442
BMI1_HUMAN	BMI1	physical	28514442
MORC4_HUMAN	MORC4	physical	28514442
FBRS_HUMAN	FBRS	physical	28514442
AUTS2_HUMAN	AUTS2	physical	28514442
BCOR_HUMAN	BCOR	physical	28514442
RING2_HUMAN	RNF2	physical	28514442
BCORL_HUMAN	BCORL1	physical	28514442
FBSL_HUMAN	FBRSL1	physical	28514442
TFDP1_HUMAN	TFDP1	physical	28514442
MGAP_HUMAN	MGA	physical	28514442
CSK21_HUMAN	CSNK2A1	physical	28514442
MCAF1_HUMAN	ATF7IP	physical	28514442
RING1_HUMAN	RING1	physical	28514442
ENL_HUMAN	MLLT1	physical	28514442
TFDP2_HUMAN	TFDP2	physical	28514442
UBP7_HUMAN	USP7	physical	28514442
CSK2B_HUMAN	CSNK2B	physical	28514442
HDAC1_HUMAN	HDAC1	physical	28514442

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 RYBP_HUMAN

Related Literatures of Post-Translational Modification

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-127; SER-130 ANDSER-227, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99 AND SER-127, AND MASSSPECTROMETRY.	19413330 [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-127 AND SER-130, ANDMASS SPECTROMETRY.	18669648 [Abstract]