RING1_MOUSE - dbPTM
RING1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RING1_MOUSE
UniProt AC O35730
Protein Name E3 ubiquitin-protein ligase RING1
Gene Name Ring1
Organism Mus musculus (Mouse).
Sequence Length 406
Subcellular Localization Nucleus speckle.
Protein Description Constitutes one of the E3 ubiquitin-protein ligases that mediate monoubiquitination of 'Lys-119' of histone H2A, thereby playing a central role in histone code and gene regulation. H2A 'Lys-119' ubiquitination gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. Essential 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, rendering chromatin heritably changed in its expressibility. Compared to RNF2/RING2, it does not have the main E3 ubiquitin ligase activity on histone H2A, and it may rather act as a modulator of RNF2/RING2 activity (By similarity)..
Protein Sequence MTTPANAQNASKTWELSLYELHRTPQEAIMDGTEIAVSPRSLHSELMCPICLDMLKNTMTTKECLHRFCSDCIVTALRSGNKECPTCRKKLVSKRSLRPDPNFDALISKIYPSREEYEAHQDRVLIRLSRLHNQQALSSSIEEGLRMQAMHRAQRVRRPMPGSDQTATMSGGEGEPGEGEGDGEDVSSDSAPDSAPGPAPKRPRGAGAGASSVGTGGGAAGGACGGAGSEDSGDRGGTLGGGTLGPPSPPGAPSPPEPGGEIELVFRPHPLLVEKGEYCQTRYVKTTGNATVDHLSKYLALRIALERRQQQETTEPGGPGGGASDTGGPDGGGGERGVAGGGEGPEEPALPSLEGVSEKQYTIYIAPGGGAFTTLNGSLTLELVNEKFWKVSRPLELCYAPTKDPK
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
24PhosphorylationSLYELHRTPQEAIMD
EEEECCCCHHHHHHC		20.6925619855
33PhosphorylationQEAIMDGTEIAVSPR
HHHHHCCCEEEECCH		21.6925619855
38PhosphorylationDGTEIAVSPRSLHSE
CCCEEEECCHHHCHH		12.9423527152
139PhosphorylationHNQQALSSSIEEGLR
HCHHHHHHHHHHHHH		35.8629899451
140PhosphorylationNQQALSSSIEEGLRM
CHHHHHHHHHHHHHH		30.5525266776
170PhosphorylationSDQTATMSGGEGEPG
CCCCEEECCCCCCCC		39.0128285833
187PhosphorylationEGDGEDVSSDSAPDS
CCCCCCCCCCCCCCC		40.52-
190PhosphorylationGEDVSSDSAPDSAPG
CCCCCCCCCCCCCCC		43.58-
211PhosphorylationRGAGAGASSVGTGGG
CCCCCCCCCCCCCCC		25.3330635358
212PhosphorylationGAGAGASSVGTGGGA
CCCCCCCCCCCCCCC		24.8330635358
215PhosphorylationAGASSVGTGGGAAGG
CCCCCCCCCCCCCCC		30.4230635358
229PhosphorylationGACGGAGSEDSGDRG
CCCCCCCCCCCCCCC		37.3826370283
232PhosphorylationGGAGSEDSGDRGGTL
CCCCCCCCCCCCCCC		38.2428973931
238PhosphorylationDSGDRGGTLGGGTLG
CCCCCCCCCCCCCCC		25.6726643407
243PhosphorylationGGTLGGGTLGPPSPP
CCCCCCCCCCCCCCC		31.6426643407
248PhosphorylationGGTLGPPSPPGAPSP
CCCCCCCCCCCCCCC		47.0326824392
254PhosphorylationPSPPGAPSPPEPGGE
CCCCCCCCCCCCCCE		53.1826643407
285UbiquitinationYCQTRYVKTTGNATV
EEEEEEEEECCCCCH		31.2822790023
324PhosphorylationGGPGGGASDTGGPDG
CCCCCCCCCCCCCCC		38.6926643407
326PhosphorylationPGGGASDTGGPDGGG
CCCCCCCCCCCCCCC		41.3626643407
361PhosphorylationEGVSEKQYTIYIAPG
CCCCCCCEEEEEECC		13.2321930439
362PhosphorylationGVSEKQYTIYIAPGG
CCCCCCEEEEEECCC		12.5721930439
364PhosphorylationSEKQYTIYIAPGGGA
CCCCEEEEEECCCCC		5.3521930439
374PhosphorylationPGGGAFTTLNGSLTL
CCCCCEEEECCEEEE		16.2721930439
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 RING1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RING1_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 RING1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
H2A2C_HUMANHIST2H2ACphysical
16710298
EED_MOUSEEedphysical
24457600
RING2_MOUSERnf2physical
24457600
BMI1_HUMANBMI1physical
26496610
PHC1_HUMANPHC1physical
26496610
PHC2_HUMANPHC2physical
26496610
TRI27_HUMANTRIM27physical
26496610
RING2_HUMANRNF2physical
26496610
SPG7_HUMANSPG7physical
26496610
BRPF1_HUMANBRPF1physical
26496610
UBP7_HUMANUSP7physical
26496610
CBX4_HUMANCBX4physical
26496610
YAF2_HUMANYAF2physical
26496610
SCML2_HUMANSCML2physical
26496610
WDR5_HUMANWDR5physical
26496610
MGAP_HUMANMGAphysical
26496610
RYBP_HUMANRYBPphysical
26496610
CHM2A_HUMANCHMP2Aphysical
26496610
BCOR_HUMANBCORphysical
26496610
CBX8_HUMANCBX8physical
26496610
FBRS_HUMANFBRSphysical
26496610
PHC3_HUMANPHC3physical
26496610
LMBL2_HUMANL3MBTL2physical
26496610
PCGF6_HUMANPCGF6physical
26496610
PCGF1_HUMANPCGF1physical
26496610
PHLB2_HUMANPHLDB2physical
26496610
C1QT6_HUMANC1QTNF6physical
26496610
CENPX_HUMANSTRA13physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RING1_MOUSE

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Related Literatures of Post-Translational Modification

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