RING1_HUMAN - dbPTM
RING1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RING1_HUMAN
UniProt AC Q06587
Protein Name E3 ubiquitin-protein ligase RING1
Gene Name RING1
Organism Homo sapiens (Human).
Sequence Length 406
Subcellular Localization Nucleus . 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..
Protein Sequence MTTPANAQNASKTWELSLYELHRTPQEAIMDGTEIAVSPRSLHSELMCPICLDMLKNTMTTKECLHRFCSDCIVTALRSGNKECPTCRKKLVSKRSLRPDPNFDALISKIYPSREEYEAHQDRVLIRLSRLHNQQALSSSIEEGLRMQAMHRAQRVRRPIPGSDQTTTMSGGEGEPGEGEGDGEDVSSDSAPDSAPGPAPKRPRGGGAGGSSVGTGGGGTGGVGGGAGSEDSGDRGGTLGGGTLGPPSPPGAPSPPEPGGEIELVFRPHPLLVEKGEYCQTRYVKTTGNATVDHLSKYLALRIALERRQQQEAGEPGGPGGGASDTGGPDGCGGEGGGAGGGDGPEEPALPSLEGVSEKQYTIYIAPGGGAFTTLNGSLTLELVNEKFWKVSRPLELCYAPTKDPK
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
2Phosphorylation------MTTPANAQN
------CCCCCCCCC		41.3023401153
3Phosphorylation-----MTTPANAQNA
-----CCCCCCCCCH		21.0723401153
11PhosphorylationPANAQNASKTWELSL
CCCCCCHHHHEEEEE		37.8623401153
12UbiquitinationANAQNASKTWELSLY
CCCCCHHHHEEEEEE		56.0721890473
12UbiquitinationANAQNASKTWELSLY
CCCCCHHHHEEEEEE		56.0721890473
12 (in isoform 1)Ubiquitination-56.0721890473
13PhosphorylationNAQNASKTWELSLYE
CCCCHHHHEEEEEEE		22.9823401153
17PhosphorylationASKTWELSLYELHRT
HHHHEEEEEEECCCC		19.8628796482
19PhosphorylationKTWELSLYELHRTPQ
HHEEEEEEECCCCHH		17.0528796482
24PhosphorylationSLYELHRTPQEAIMD
EEEECCCCHHHHHHC		20.6926074081
33PhosphorylationQEAIMDGTEIAVSPR
HHHHHCCCEEEECCH		21.6930266825
38PhosphorylationDGTEIAVSPRSLHSE
CCCEEEECCHHHCHH		12.9425159151
41PhosphorylationEIAVSPRSLHSELMC
EEEECCHHHCHHHHH		33.5426074081
44PhosphorylationVSPRSLHSELMCPIC
ECCHHHCHHHHHHHH		37.4124719451
62AcetylationLKNTMTTKECLHRFC
HHHCCCHHHHHHHHH		36.9526822725
622-HydroxyisobutyrylationLKNTMTTKECLHRFC
HHHCCCHHHHHHHHH		36.95-
62UbiquitinationLKNTMTTKECLHRFC
HHHCCCHHHHHHHHH		36.95-
79PhosphorylationCIVTALRSGNKECPT
HHHHHHHHCCCCCCH		47.7928555341
82AcetylationTALRSGNKECPTCRK
HHHHHCCCCCCHHHH		65.3126051181
96PhosphorylationKKLVSKRSLRPDPNF
HHHHCCHHCCCCCCH		32.2520873877
117PhosphorylationIYPSREEYEAHQDRV
HCCCHHHHHHHHHHH		17.42-
129PhosphorylationDRVLIRLSRLHNQQA
HHHHHHHHHHHCHHH		23.9729496963
138PhosphorylationLHNQQALSSSIEEGL
HHCHHHHHHHHHHHH		25.6723403867
139PhosphorylationHNQQALSSSIEEGLR
HCHHHHHHHHHHHHH		35.8621712546
140PhosphorylationNQQALSSSIEEGLRM
CHHHHHHHHHHHHHH		30.5523401153
163PhosphorylationVRRPIPGSDQTTTMS
CCCCCCCCCCCCEEC		22.6117081983
166PhosphorylationPIPGSDQTTTMSGGE
CCCCCCCCCEECCCC		29.2617081983
167PhosphorylationIPGSDQTTTMSGGEG
CCCCCCCCEECCCCC		18.1830108239
168PhosphorylationPGSDQTTTMSGGEGE
CCCCCCCEECCCCCC		16.8430108239
170PhosphorylationSDQTTTMSGGEGEPG
CCCCCEECCCCCCCC		41.3721130716
187PhosphorylationEGDGEDVSSDSAPDS
CCCCCCCCCCCCCCC		40.5219276368
188PhosphorylationGDGEDVSSDSAPDSA
CCCCCCCCCCCCCCC		35.1219276368
190PhosphorylationGEDVSSDSAPDSAPG
CCCCCCCCCCCCCCC		43.5819276368
194PhosphorylationSSDSAPDSAPGPAPK
CCCCCCCCCCCCCCC		34.9930108239
202MethylationAPGPAPKRPRGGGAG
CCCCCCCCCCCCCCC		25.7024394741
211PhosphorylationRGGGAGGSSVGTGGG
CCCCCCCCCCCCCCC		22.4130266825
212PhosphorylationGGGAGGSSVGTGGGG
CCCCCCCCCCCCCCC		28.0430266825
215PhosphorylationAGGSSVGTGGGGTGG
CCCCCCCCCCCCCCC		30.4230266825
220PhosphorylationVGTGGGGTGGVGGGA
CCCCCCCCCCCCCCC		33.7530266825
229PhosphorylationGVGGGAGSEDSGDRG
CCCCCCCCCCCCCCC		37.3830266825
232PhosphorylationGGAGSEDSGDRGGTL
CCCCCCCCCCCCCCC		38.2430266825
238PhosphorylationDSGDRGGTLGGGTLG
CCCCCCCCCCCCCCC		25.6729255136
243PhosphorylationGGTLGGGTLGPPSPP
CCCCCCCCCCCCCCC		31.6429255136
246 (in isoform 2)Ubiquitination-29.3421890473
248PhosphorylationGGTLGPPSPPGAPSP
CCCCCCCCCCCCCCC		47.0329255136
254PhosphorylationPSPPGAPSPPEPGGE
CCCCCCCCCCCCCCE		53.1825159151
268 (in isoform 2)Ubiquitination-23.2221890473
275 (in isoform 1)Ubiquitination-49.9521890473
275UbiquitinationPHPLLVEKGEYCQTR
CCCEEEECCCEEEEE		49.9521890473
275UbiquitinationPHPLLVEKGEYCQTR
CCCEEEECCCEEEEE		49.9521890473
278PhosphorylationLLVEKGEYCQTRYVK
EEEECCCEEEEEEEE		9.8729978859
281PhosphorylationEKGEYCQTRYVKTTG
ECCCEEEEEEEEECC		22.0229978859
283PhosphorylationGEYCQTRYVKTTGNA
CCEEEEEEEEECCCC		15.0829978859
285UbiquitinationYCQTRYVKTTGNATV
EEEEEEEEECCCCCH		31.28-
297UbiquitinationATVDHLSKYLALRIA
CCHHHHHHHHHHHHH		51.1221890473
297AcetylationATVDHLSKYLALRIA
CCHHHHHHHHHHHHH		51.1223749302
297 (in isoform 1)Ubiquitination-51.1221890473
297UbiquitinationATVDHLSKYLALRIA
CCHHHHHHHHHHHHH		51.1221890473
324PhosphorylationGGPGGGASDTGGPDG
CCCCCCCCCCCCCCC		38.6928348404
326PhosphorylationPGGGASDTGGPDGCG
CCCCCCCCCCCCCCC		41.3628348404
398S-nitrosylationVSRPLELCYAPTKDP
CCCCEEEEECCCCCC		1.6719483679
398S-nitrosocysteineVSRPLELCYAPTKDP
CCCCEEEEECCCCCC		1.67-
402PhosphorylationLELCYAPTKDPK---
EEEEECCCCCCC---		39.6528348404
403UbiquitinationELCYAPTKDPK----
EEEECCCCCCC----		71.61-
403AcetylationELCYAPTKDPK----
EEEECCCCCCC----		71.6125953088
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RING1_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 RING1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CBX4_HUMANCBX4physical
9858531
RYBP_HUMANRYBPphysical
16189514
CBX4_HUMANCBX4physical
9199346
BMI1_HUMANBMI1physical
9199346
PHC1_HUMANPHC1physical
9199346
BMI1_HUMANBMI1physical
9858531
RING1_HUMANRING1physical
9858531
CBX8_HUMANCBX8physical
10825164
E2F6_HUMANE2F6physical
11171983
RB_HUMANRB1physical
11583618
E2F1_HUMANE2F1physical
11583618
RYBP_HUMANRYBPphysical
10369680
BMI1_HUMANBMI1physical
16359901
RING2_HUMANRNF2physical
16359901
RING2_HUMANRNF2physical
16943429
RING2_HUMANRNF2physical
15386022
BMI1_HUMANBMI1physical
15386022
PHC2_HUMANPHC2physical
15386022
RING2_HUMANRNF2physical
21596310
RING2_HUMANRNF2physical
22325352
BMI1_HUMANBMI1physical
22325352
PCGF1_HUMANPCGF1physical
22325352
RYBP_HUMANRYBPphysical
22325352
CBX2_HUMANCBX2physical
22325352
YAF2_HUMANYAF2physical
22325352
WDR5_HUMANWDR5physical
22325352
PCGF2_HUMANPCGF2physical
22325352
A4_HUMANAPPphysical
21832049
P53_HUMANTP53physical
22907436
TYY1_HUMANYY1physical
16624538
BMI1_HUMANBMI1physical
22493164
SNAI1_HUMANSNAI1physical
24903147
YAF2_HUMANYAF2physical
25416956
RYBP_HUMANRYBPphysical
25416956
CBX8_HUMANCBX8physical
25416956
RING1_HUMANRING1physical
19956605
UB2D1_HUMANUBE2D1physical
19956605
PCGF2_HUMANPCGF2physical
21516116
FIBA_HUMANFGAphysical
28514442
FIBG_HUMANFGGphysical
28514442
FIBB_HUMANFGBphysical
28514442
ACADS_HUMANACADSphysical
28514442
HDAC1_HUMANHDAC1physical
28514442
BASI_HUMANBSGphysical
28832687
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 RING1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-38 AND THR-220, AND MASSSPECTROMETRY.
"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-38; SER-187; SER-188 ANDSER-190, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND MASSSPECTROMETRY.

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