RN126_HUMAN - dbPTM
RN126_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RN126_HUMAN
UniProt AC Q9BV68
Protein Name E3 ubiquitin-protein ligase RNF126 {ECO:0000305}
Gene Name RNF126 {ECO:0000312|HGNC:HGNC:21151}
Organism Homo sapiens (Human).
Sequence Length 326
Subcellular Localization Cytoplasm . Nucleus .
Protein Description E3 ubiquitin-protein ligase that mediates ubiquitination oF target proteins. [PubMed: 23277564]
Protein Sequence MAEASPHPGRYFCHCCSVEIVPRLPDYICPRCESGFIEELPEETRSTENGSAPSTAPTDQSRPPLEHVDQHLFTLPQGYGQFAFGIFDDSFEIPTFPPGAQADDGRDPESRRERDHPSRHRYGARQPRARLTTRRATGRHEGVPTLEGIIQQLVNGIITPATIPSLGPWGVLHSNPMDYAWGANGLDAIITQLLNQFENTGPPPADKEKIQALPTVPVTEEHVGSGLECPVCKDDYALGERVRQLPCNHLFHDGCIVPWLEQHDSCPVCRKSLTGQNTATNPPGLTGVSFSSSSSSSSSSSPSNENATWSPLGRPQPPRPLSNLTL
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
2Acetylation------MAEASPHPG
------CCCCCCCCC		22.5120068231
5Phosphorylation---MAEASPHPGRYF
---CCCCCCCCCCEE		18.4223401153
17PhosphorylationRYFCHCCSVEIVPRL
CEECEEEEEEEECCC		28.3328857561
27PhosphorylationIVPRLPDYICPRCES
EECCCCCCCCCCCCC		11.5027642862
128DimethylationRYGARQPRARLTTRR
CCCCCCCCHHCCCCH		24.81-
128MethylationRYGARQPRARLTTRR
CCCCCCCCHHCCCCH		24.8154561745
130DimethylationGARQPRARLTTRRAT
CCCCCCHHCCCCHHC		33.57-
130MethylationGARQPRARLTTRRAT
CCCCCCHHCCCCHHC		33.5754558829
209UbiquitinationPPPADKEKIQALPTV
CCCCCHHHHCCCCCC		45.95-
233UbiquitinationGLECPVCKDDYALGE
CCCCCCCCCCHHHCH		54.60-
233AcetylationGLECPVCKDDYALGE
CCCCCCCCCCHHHCH		54.6026051181
278PhosphorylationKSLTGQNTATNPPGL
HHHCCCCCCCCCCCC		27.29-
286 (in isoform 2)Phosphorylation-41.2630177828
286PhosphorylationATNPPGLTGVSFSSS
CCCCCCCCEEEECCC		41.2625159151
289 (in isoform 2)Phosphorylation-22.2830177828
291 (in isoform 2)Phosphorylation-23.0828348404
292 (in isoform 2)Phosphorylation-32.0328348404
293PhosphorylationTGVSFSSSSSSSSSS
CEEEECCCCCCCCCC		32.80-
293 (in isoform 2)Phosphorylation-32.8028348404
294PhosphorylationGVSFSSSSSSSSSSS
EEEECCCCCCCCCCC		35.87-
294 (in isoform 2)Phosphorylation-35.8728348404
295PhosphorylationVSFSSSSSSSSSSSP
EEECCCCCCCCCCCC		35.87-
295 (in isoform 2)Phosphorylation-35.8728348404
296PhosphorylationSFSSSSSSSSSSSPS
EECCCCCCCCCCCCC		35.87-
296 (in isoform 2)Phosphorylation-35.8728348404
297 (in isoform 2)Phosphorylation-35.8728348404
298 (in isoform 2)Phosphorylation-35.8728348404
299 (in isoform 2)Phosphorylation-36.4628348404
300 (in isoform 2)Phosphorylation-48.4928348404
301 (in isoform 2)Phosphorylation-34.0018691976
301PhosphorylationSSSSSSSSPSNENAT
CCCCCCCCCCCCCCC		34.0018691976
303 (in isoform 2)Phosphorylation-59.7428348404
308 (in isoform 2)Phosphorylation-37.7530177828
309 (in isoform 2)Phosphorylation-8.7827251275
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 RN126_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RN126_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 RN126_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDN1A_HUMANCDKN1Aphysical
23026136
RN126_HUMANRNF126physical
23026136
UBC_HUMANUBCphysical
22992278
UB2D2_HUMANUBE2D2physical
22992278
UBE2K_MOUSEUbe2kphysical
22992278
RN126_HUMANRNF126physical
23418353
UB2D2_HUMANUBE2D2physical
23418353
UBE2N_HUMANUBE2Nphysical
23418353
EGFR_HUMANEGFRphysical
23418353
SCAM3_HUMANSCAMP3physical
23418353
AICDA_HUMANAICDAphysical
23277564
UB2D2_HUMANUBE2D2physical
23277564
UB2D3_HUMANUBE2D3physical
23277564
TRI11_HUMANTRIM11physical
22493164
TRI52_HUMANTRIM52physical
22493164
UBB_HUMANUBBphysical
26186194
BAG6_HUMANBAG6physical
26186194
GET4_HUMANGET4physical
26186194
MINY1_HUMANFAM63Aphysical
26186194
TAXB1_HUMANTAX1BP1physical
26186194
LRWD1_HUMANLRWD1physical
26186194
ABCB6_HUMANABCB6physical
26186194
CRYM_HUMANCRYMphysical
26186194
ASNA_HUMANASNA1physical
26186194
SKP2_HUMANSKP2physical
26186194
GDC_HUMANSLC25A16physical
26186194
PJA1_HUMANPJA1physical
26186194
WRP73_HUMANWRAP73physical
26186194
APOD_HUMANAPODphysical
26186194
K0100_HUMANKIAA0100physical
26186194
KLH42_HUMANKLHL42physical
26186194
CAN15_HUMANCAPN15physical
26186194
E2F1_HUMANE2F1physical
26234677
SMC3_HUMANSMC3physical
26508657
RAD50_HUMANRAD50physical
26508657
BRE1A_HUMANRNF20physical
26508657
SMC1A_HUMANSMC1Aphysical
26508657
PFKAP_HUMANPFKPphysical
26508657
SK2L2_HUMANSKIV2L2physical
26508657
DPOD1_HUMANPOLD1physical
26508657
RIR1_HUMANRRM1physical
26508657
ADT2_HUMANSLC25A5physical
26508657
XPOT_HUMANXPOTphysical
26508657
UBP7_HUMANUSP7physical
26508657
SART3_HUMANSART3physical
26508657
SYQ_HUMANQARSphysical
26508657
GDE_HUMANAGLphysical
26508657
AP2A2_HUMANAP2A2physical
26508657
AT2A2_HUMANATP2A2physical
26508657
BAG6_HUMANBAG6physical
26508657
COPA_HUMANCOPAphysical
26508657
COPB_HUMANCOPB1physical
26508657
COPB2_HUMANCOPB2physical
26508657
COPG1_HUMANCOPG1physical
26508657
RRP44_HUMANDIS3physical
26508657
EIF3A_HUMANEIF3Aphysical
26508657
IF4G2_HUMANEIF4G2physical
26508657
SYEP_HUMANEPRSphysical
26508657
GFPT1_HUMANGFPT1physical
26508657
SYIM_HUMANIARS2physical
26508657
MIC60_HUMANIMMTphysical
26508657
IRS4_HUMANIRS4physical
26508657
LARP4_HUMANLARP4physical
26508657
MCM2_HUMANMCM2physical
26508657
MYO6_HUMANMYO6physical
26508657
NAA15_HUMANNAA15physical
26508657
NUP93_HUMANNUP93physical
26508657
MSH6_HUMANMSH6physical
26508657
MSH2_HUMANMSH2physical
26508657
MCM4_HUMANMCM4physical
26508657
BAG6_HUMANBAG6physical
24981174
XRCC5_HUMANXRCC5physical
27895153
XRCC6_HUMANXRCC6physical
27895153
FRDA_HUMANFXNphysical
28228265
UBB_HUMANUBBphysical
28514442
MINY1_HUMANFAM63Aphysical
28514442
TAXB1_HUMANTAX1BP1physical
28514442
CAN15_HUMANCAPN15physical
28514442
CRYM_HUMANCRYMphysical
28514442
K0100_HUMANKIAA0100physical
28514442
BAG6_HUMANBAG6physical
28514442
GET4_HUMANGET4physical
28514442
SKP2_HUMANSKP2physical
28514442
LRWD1_HUMANLRWD1physical
28514442
KLH42_HUMANKLHL42physical
28514442
APOD_HUMANAPODphysical
28514442
GDC_HUMANSLC25A16physical
28514442
BBS1_HUMANBBS1physical
27173435
BAG6_HUMANBAG6physical
27193484
UBL4A_HUMANUBL4Aphysical
27193484
RN126_HUMANRNF126physical
29167269
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 RN126_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory