RYBP_MOUSE - dbPTM
RYBP_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RYBP_MOUSE
UniProt AC Q8CCI5
Protein Name RING1 and YY1-binding protein
Gene Name Rybp
Organism Mus musculus (Mouse).
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.
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: 22325148]
Protein Sequence MTMGDKKSPTRPKRQAKPAADEGFWDCSVCTFRNSAEAFKCSICDVRKGTSTRKPRINSQLVAQQVAQQYATPPPPKKEKKEKVEKPDKEKPEKDKDISPSVTKKNTNKKTKPKSDILKDPPSEANSIQSANATTKTSETNHTSRPRLKNVDRSTAQQLAVTVGNVTVIITDFKEKTRSSSTSSSTVTSSAGSEQQNQSSSGSESTDKGSSRSSTPKGDMSAVNDESF
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 Orthologous
Protein Cluster
8PhosphorylationMTMGDKKSPTRPKRQ
CCCCCCCCCCCCCCC		36.9329895711
10PhosphorylationMGDKKSPTRPKRQAK
CCCCCCCCCCCCCCC		67.6928066266
59PhosphorylationTRKPRINSQLVAQQV
CCCCCCCHHHHHHHH		23.6325338131
70PhosphorylationAQQVAQQYATPPPPK
HHHHHHHHCCCCCCC		10.6026643407
72PhosphorylationQVAQQYATPPPPKKE
HHHHHHCCCCCCCHH		31.2426643407
99PhosphorylationPEKDKDISPSVTKKN
CCCCCCCCHHHCCCC		22.6626824392
101PhosphorylationKDKDISPSVTKKNTN
CCCCCCHHHCCCCCC		35.3126824392
103PhosphorylationKDISPSVTKKNTNKK
CCCCHHHCCCCCCCC		40.4125619855
115PhosphorylationNKKTKPKSDILKDPP
CCCCCCHHHHHCCCH		38.1129472430
119UbiquitinationKPKSDILKDPPSEAN
CCHHHHHCCCHHHHH		69.40-
123PhosphorylationDILKDPPSEANSIQS
HHHCCCHHHHHHHHH		55.5222802335
127PhosphorylationDPPSEANSIQSANAT
CCHHHHHHHHHCCCC		29.1121082442
130PhosphorylationSEANSIQSANATTKT
HHHHHHHHCCCCCCC		23.0921082442
134PhosphorylationSIQSANATTKTSETN
HHHHCCCCCCCCCCC		28.7429472430
135PhosphorylationIQSANATTKTSETNH
HHHCCCCCCCCCCCC		29.8929472430
136UbiquitinationQSANATTKTSETNHT
HHCCCCCCCCCCCCC		45.7822790023
177PhosphorylationITDFKEKTRSSSTSS
EECCCHHHCCCCCCC		36.5525338131
179PhosphorylationDFKEKTRSSSTSSST
CCCHHHCCCCCCCCE		33.5927087446
180PhosphorylationFKEKTRSSSTSSSTV
CCHHHCCCCCCCCEE		34.0529895711
181PhosphorylationKEKTRSSSTSSSTVT
CHHHCCCCCCCCEEE		33.2929895711
182PhosphorylationEKTRSSSTSSSTVTS
HHHCCCCCCCCEEEC		34.2826160508
183PhosphorylationKTRSSSTSSSTVTSS
HHCCCCCCCCEEECC		25.0026160508
184PhosphorylationTRSSSTSSSTVTSSA
HCCCCCCCCEEECCC		30.0729895711
185PhosphorylationRSSSTSSSTVTSSAG
CCCCCCCCEEECCCC		27.0226160508
186PhosphorylationSSSTSSSTVTSSAGS
CCCCCCCEEECCCCC		29.7426160508
188PhosphorylationSTSSSTVTSSAGSEQ
CCCCCEEECCCCCCC		19.6326160508
189PhosphorylationTSSSTVTSSAGSEQQ
CCCCEEECCCCCCCC		17.5425777480
190PhosphorylationSSSTVTSSAGSEQQN
CCCEEECCCCCCCCC		27.5529895711
193PhosphorylationTVTSSAGSEQQNQSS
EEECCCCCCCCCCCC		31.7627087446
199PhosphorylationGSEQQNQSSSGSEST
CCCCCCCCCCCCCCC		33.7429895711
200PhosphorylationSEQQNQSSSGSESTD
CCCCCCCCCCCCCCC		29.0226160508
201PhosphorylationEQQNQSSSGSESTDK
CCCCCCCCCCCCCCC		52.1427087446
203PhosphorylationQNQSSSGSESTDKGS
CCCCCCCCCCCCCCC		30.2626160508
205PhosphorylationQSSSGSESTDKGSSR
CCCCCCCCCCCCCCC		43.5326160508
206PhosphorylationSSSGSESTDKGSSRS
CCCCCCCCCCCCCCC		37.3622668510
210PhosphorylationSESTDKGSSRSSTPK
CCCCCCCCCCCCCCC		28.4626160508
211PhosphorylationESTDKGSSRSSTPKG
CCCCCCCCCCCCCCC		44.8726160508
213PhosphorylationTDKGSSRSSTPKGDM
CCCCCCCCCCCCCCC		40.2823684622
214PhosphorylationDKGSSRSSTPKGDMS
CCCCCCCCCCCCCCC		47.8525521595
215PhosphorylationKGSSRSSTPKGDMSA
CCCCCCCCCCCCCCC		30.2125521595
221PhosphorylationSTPKGDMSAVNDESF
CCCCCCCCCCCCCCC		33.5329895711
227PhosphorylationMSAVNDESF------
CCCCCCCCC------		38.8423375375
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
-KUbiquitinationE3 ubiquitin ligaseRnf2Q9CQJ4
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RYBP_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBC_HUMANUBCphysical
17070805
RING1_MOUSERing1physical
17070805
RING2_MOUSERnf2physical
17070805
RING1_MOUSERing1physical
22325148
PCGF6_MOUSEPcgf6physical
22325148
RING2_MOUSERnf2physical
22325148
PCGF1_MOUSEPcgf1physical
22325148
PCGF2_MOUSEPcgf2physical
22325148
RYBP_MOUSERybpphysical
22325148
RING2_MOUSERnf2physical
28111200
PO5F1_MOUSEPou5f1physical
28111200
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RYBP_MOUSE

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Related Literatures of Post-Translational Modification

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